id
int64 | text
string | metadata
dict | line_start_n_end_idx
dict | quality_signals
dict | eai_taxonomy
dict | fdc_level2_prefix
string | pid
string |
|---|---|---|---|---|---|---|---|
8,931,606,065,125,391,000
|
GO:0120227: acyl-CoA binding (Molecular function)
"Interacting selectively and non-covalently with an acyl-CoA, a thioester that results from the formal condensation of the thiol group of coenzyme A with the carboxy group of any carboxylic acid." [GOC:krc]
There are 309 sequences with this label.
Enriched clusters
Name Species % in cluster p-value corrected p-value action
Sequences (309) (download table)
Info: GO-associations disabled for items with more than 300 associated sequences !
InterPro Domains
Family Terms
|
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57
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cf5cd1df0ee2161e1684bdc019357275
|
4,302,764,628,778,546,000
|
ePrints@IIScePrints@IISc Home | About | Browse | Latest Additions | Advanced Search | Contact | Help
Browse by Author
Up a level
Export as [feed] Atom [feed] RSS 1.0 [feed] RSS 2.0
Group by: Item Type | No Grouping
Number of items: 2.
Journal Article
Gadgil, Madhav and Rao, Seshagiri PR and Utkarsh, G and Pramod, P and Chhatre, Ashwini (2000) New meanings for old knowledge: the people's biodiversity registers program. In: Ecological Applications, 10 (5). pp. 1307-1317.
Utkarsh, G and Joshi, NV and Gadgil, M (1998) On the patterns of tree diversity in the Western Ghats of India. In: Current Science, 75 (6). pp. 594-603.
This list was generated on Tue Mar 11 14:11:58 2014 IST.
|
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cf5cd1df0ee2161e1684bdc019357275
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-2,995,674,282,122,959,000
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STRINGSTRING
STRING protein interaction network
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
DR97_2859annotation not available (155 aa)
Predicted Functional Partners:
DR97_2860
UPF0391 membrane protein AO896_26960
0.932
DR97_4144
DUF3509 domain-containing protein
0.629
DR97_2563
annotation not available
0.627
DR97_1000
annotation not available
0.616
DR97_5175
Uncharacterized protein
0.611
DR97_1891
annotation not available
0.591
DR97_1522
Amidase
0.567
DR97_1947
Uncharacterized protein
0.549
algK
May be involved in the polymerization of mannuronate to alginate
0.526
DR97_4894
Putative membrane protein
0.517
Your Current Organism:
Pseudomonas aeruginosa
NCBI taxonomy Id: 287
Other names: ATCC 10145, ATCC 10145-U, Bacillus aeruginosus, Bacillus pyocyaneus, Bacterium aeruginosum, Bacterium pyocyaneum, CCEB 481, CCUG 28447, CCUG 29297, CCUG 551, CFBP 2466, CIP 100720, DSM 50071, IBCS 277, IFO 12689, JCM 5962, Micrococcus pyocyaneus, NBRC 12689, NCCB 76039, NCIB 8295, NCIMB 8295, NCTC 10332, NRRL B-771, P. aeruginosa, Pseudomonas polycolor, Pseudomonas pyocyanea, Pseudomonas sp. RV3, RH 815, VKM B-588, bacterium ASFP-37, bacterium ASFP-38, bacterium ASFP-45, bacterium ASFP-46, bacterium ASFP-48
Server load: low (13%) [HD]
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Strain Name:
B6.129P2(Cg)-Krt12tm1Wwk/J
Stock Number:
022813
Order this mouse
Availability:
Cryopreserved - Ready for recovery
These Ktr12-/- mice may be useful for studying the maintenance of the corneal epithelium.
Description
The genotypes of the animals provided may not reflect those discussed in the strain description or the mating scheme utilized by The Jackson Laboratory prior to cryopreservation. Please inquire for possible genotypes for this specific strain.
Strain Information
Type Congenic; Mutant Strain; Targeted Mutation;
Additional information on Genetically Engineered and Mutant Mice.
Visit our online Nomenclature tutorial.
Additional information on Congenic nomenclature.
Specieslaboratory mouse
Donating Investigator Winston W.Y. Kao, University of Cincinnati
Description
In this strain, a neo cassette replaces exons 3-7 and intron 7 of the keratin 12 (Krt12) gene with a neomycin resistance (neo) cassette, abolishing gene expression. Keratin 12 is a type I intermediate filament chain keratin, expressed in corneal epithelia. Keratin 12 also pairs with Keratin 3 and forms intermediate filaments in the cornea. Heterozygous mice appear phenotypically normal. Homozygotes are viable and fertile. The cornea of these Ktr12-/- mice are fragile, and contain fewer cellular layers and fewer intermediate filaments.
Development
A targeting vector was designed to replace exons 3-7 and intron 7 of the keratin 12 (Krt12) gene with a neomycin resistance (neo) cassette. The construct was electroporated into 129P2/OlaHsd-derived E14.1 embryonic stem (ES) cells. Correctly targeted ES cells were injected into C57BL/6 blastocysts and the resulting chimeric mice were bred to Black Swiss mice. These mice were backcrossed 20 generations to C57BL/6J mice. Upon arrival at The Jackson Laboratory, mice were bred to C57BL/6J (Stock No. 000664) for at least one generation to establish the colony.
Control Information
Control
000664 C57BL/6J (approximate)
Considerations for Choosing Controls
Related Strains
Strains carrying other alleles of Krt12
023055 B6.129(Cg)-Krt12tm3(cre)Wwk/J
View Strains carrying other alleles of Krt12 (1 strain)
Phenotype
Phenotype Information
View Related Disease (OMIM) Terms
Related Disease (OMIM) Terms provided by MGI
- Potential model based on gene homology relationships. Phenotypic similarity to the human disease has not been tested.
Corneal Dystrophy, Meesmann; MECD (KRT12)
View Mammalian Phenotype Terms
Mammalian Phenotype Terms provided by MGI
assigned by genotype
The following phenotype information is associated with a similar, but not exact match to this JAX® Mice strain.
Krt12tm1Wwk/Krt12tm1Wwk
involves: 129P2/OlaHsd * NIH Black Swiss
• vision/eye phenotype
• abnormal corneal epithelium morphology
• the corneal epithelium contains about 3 fewer cell layers and the layers present are not firmly attached to the underlying layers (MGI Ref ID J:38023)
• the superficial epithelial cells are swollen, easily removed with gentle brushing, and lack keratin intermediate filaments (MGI Ref ID J:38023)
View Research Applications
Research Applications
This mouse can be used to support research in many areas including:
Cell Biology Research
Defects in Extracellular Matrix Molecules
Developmental Biology Research
Defects in Extracellular Matrix Molecules
Eye Defects
Sensorineural Research
Eye Defects
Genes & Alleles
Gene & Allele Information provided by MGI
Allele Symbol Krt12tm1Wwk
Allele Name targeted mutation 1, Winston W Y Kao
Allele Type Targeted (Null/Knockout)
Strain of Origin129P2/OlaHsd
Gene Symbol and Name Krt12, keratin 12
Chromosome 11
Gene Common Name(s) AI835216; K12; Ka12; Krt1-12; expressed sequence AI835216; keratin complex 1, acidic, gene 12;
Molecular Note Exons 3-7 and intron 7 were replaced with a neomycin resistance gene. Immunohistochemistry, Western blot, Northern blot and in situ hybridization confirmed lack of gene expression. [MGI Ref ID J:38023]
Genotyping
Genotyping Information
Genotyping Protocols
Krt12tm1Wwkalternate1, Standard PCR
Helpful Links
Genotyping resources and troubleshooting
References
References provided by MGI
Additional References
Krt12tm1Wwk related
Hayashi Y; Call MK; Liu CY; Hayashi M; Babcock G; Ohashi Y; Kao WW. 2010. Monoallelic expression of Krt12 gene during corneal-type epithelium differentiation of limbal stem cells. Invest Ophthalmol Vis Sci 51(9):4562-8. [PubMed: 20393120] [MGI Ref ID J:164088]
Kao WW; Liu CY; Converse RL; Shiraishi A; Kao CW; Ishizaki M; Doetschman T; Duffy J. 1996. Keratin 12-deficient mice have fragile corneal epithelia. Invest Ophthalmol Vis Sci 37(13):2572-84. [PubMed: 8977471] [MGI Ref ID J:38023]
Health & husbandry
The genotypes of the animals provided may not reflect those discussed in the strain description or the mating scheme utilized by The Jackson Laboratory prior to cryopreservation. Please inquire for possible genotypes for this specific strain.
Health & Colony Maintenance Information
Animal Health Reports
Production of mice from cryopreserved embryos or sperm occurs in a maximum barrier room, G200.
Colony Maintenance
Breeding & HusbandryWhen maintaining a live colony, homozygous mice may be bred together.
Pricing and Purchasing
Pricing, Supply Level & Notes, Controls
Pricing for USA, Canada and Mexico shipping destinations View International Pricing
Cryopreserved
Cryopreserved Mice - Ready for Recovery
Price (US dollars $)
Cryorecovery* $2525.00
Animals Provided
At least two mice that carry the mutation (if it is a mutant strain) will be provided. Their genotypes may not reflect those discussed in the strain description. Please inquire for possible genotypes and see additional details below.
Standard Supply
Cryopreserved. Ready for recovery. Please refer to pricing and supply notes on the strain data sheet for further information.
Supply Notes
• Cryorecovery - Standard.
Progeny testing is not required.
The average number of mice provided from recovery of our cryopreserved strains is 10. The total number of animals provided, their gender and genotype will vary. We will fulfill your order by providing at least two pair of mice, at least one animal of each pair carrying the mutation of interest. Please inquire if larger numbers of animals with specific genotype and genders are needed. Animals typically ship between 10 and 14 weeks from the date of your order. If a second cryorecovery is needed in order to provide the minimum number of animals, animals will ship within 25 weeks. IMPORTANT NOTE: The genotypes of animals provided may not reflect the mating scheme utilized by The Jackson Laboratory prior to cryopreservation, or that discussed in the strain description. Please inquire about possible genotypes which will be recovered for this specific strain. The Jackson Laboratory cannot guarantee the reproductive success of mice shipped to your facility. If the mice are lost after the first three days (post-arrival) or do not produce progeny at your facility, a new order and fee will be necessary.
Cryorecovery to establish a Dedicated Supply for greater quantities of mice. Mice recovered can be used to establish a dedicated colony to contractually supply you mice according to your requirements. Price by quotation. For more information on Dedicated Supply, please contact JAX® Services, Tel: 1-800-422-6423 (from U.S.A., Canada or Puerto Rico only) or 1-207-288-5845 (from any location).
Pricing for International shipping destinations View USA Canada and Mexico Pricing
Cryopreserved
Cryopreserved Mice - Ready for Recovery
Price (US dollars $)
Cryorecovery* $3283.00
Animals Provided
At least two mice that carry the mutation (if it is a mutant strain) will be provided. Their genotypes may not reflect those discussed in the strain description. Please inquire for possible genotypes and see additional details below.
Standard Supply
Cryopreserved. Ready for recovery. Please refer to pricing and supply notes on the strain data sheet for further information.
Supply Notes
• Cryorecovery - Standard.
Progeny testing is not required.
The average number of mice provided from recovery of our cryopreserved strains is 10. The total number of animals provided, their gender and genotype will vary. We will fulfill your order by providing at least two pair of mice, at least one animal of each pair carrying the mutation of interest. Please inquire if larger numbers of animals with specific genotype and genders are needed. Animals typically ship between 10 and 14 weeks from the date of your order. If a second cryorecovery is needed in order to provide the minimum number of animals, animals will ship within 25 weeks. IMPORTANT NOTE: The genotypes of animals provided may not reflect the mating scheme utilized by The Jackson Laboratory prior to cryopreservation, or that discussed in the strain description. Please inquire about possible genotypes which will be recovered for this specific strain. The Jackson Laboratory cannot guarantee the reproductive success of mice shipped to your facility. If the mice are lost after the first three days (post-arrival) or do not produce progeny at your facility, a new order and fee will be necessary.
Cryorecovery to establish a Dedicated Supply for greater quantities of mice. Mice recovered can be used to establish a dedicated colony to contractually supply you mice according to your requirements. Price by quotation. For more information on Dedicated Supply, please contact JAX® Services, Tel: 1-800-422-6423 (from U.S.A., Canada or Puerto Rico only) or 1-207-288-5845 (from any location).
View USA Canada and Mexico Pricing View International Pricing
Standard Supply
Cryopreserved. Ready for recovery. Please refer to pricing and supply notes on the strain data sheet for further information.
Control Information
Control
000664 C57BL/6J (approximate)
Considerations for Choosing Controls
Control Pricing Information for Genetically Engineered Mutant Strains.
Payment Terms and Conditions
Terms are granted by individual review and stated on the customer invoice(s) and account statement. These transactions are payable in U.S. currency within the granted terms. Payment for services, products, shipping containers, and shipping costs that are rendered are expected within the payment terms indicated on the invoice or stated by contract. Invoices and account balances in arrears of stated terms may result in The Jackson Laboratory pursuing collection activities including but not limited to outside agencies and court filings.
See Terms of Use tab for General Terms and Conditions
The Jackson Laboratory's Genotype Promise
The Jackson Laboratory has rigorous genetic quality control and mutant gene genotyping programs to ensure the genetic background of JAX® Mice strains as well as the genotypes of strains with identified molecular mutations. JAX® Mice strains are only made available to researchers after meeting our standards. However, the phenotype of each strain may not be fully characterized and/or captured in the strain data sheets. Therefore, we cannot guarantee a strain's phenotype will meet all expectations. To ensure that JAX® Mice will meet the needs of individual research projects or when requesting a strain that is new to your research, we suggest ordering and performing tests on a small number of mice to determine suitability for your particular project.
Ordering Information
JAX® Mice
Surgical and Preconditioning Services
JAX® Services
Customer Services and Support
Tel: 1-800-422-6423 or 1-207-288-5845
Fax: 1-207-288-6150
Technical Support Email Form
Terms of Use
Terms of Use
General Terms and Conditions
Contact information
General inquiries regarding Terms of Use
Contracts Administration
phone:207-288-6470
JAX® Mice, Products & Services Conditions of Use
"MICE" means mouse strains, their progeny derived by inbreeding or crossbreeding, unmodified derivatives from mouse strains or their progeny supplied by The Jackson Laboratory ("JACKSON"). "PRODUCTS" means biological materials supplied by JACKSON, and their derivatives. "RECIPIENT" means each recipient of MICE, PRODUCTS, or services provided by JACKSON including each institution, its employees and other researchers under its control. MICE or PRODUCTS shall not be: (i) used for any purpose other than the internal research, (ii) sold or otherwise provided to any third party for any use, or (iii) provided to any agent or other third party to provide breeding or other services. Acceptance of MICE or PRODUCTS from JACKSON shall be deemed as agreement by RECIPIENT to these conditions, and departure from these conditions requires JACKSON's prior written authorization.
No Warranty
MICE, PRODUCTS AND SERVICES ARE PROVIDED “AS IS”. JACKSON EXTENDS NO WARRANTIES OF ANY KIND, EITHER EXPRESS, IMPLIED, OR STATUTORY, WITH RESPECT TO MICE, PRODUCTS OR SERVICES, INCLUDING ANY IMPLIED WARRANTY OF MERCHANTABILITY OR FITNESS FOR A PARTICULAR PURPOSE, OR ANY WARRANTY OF NON-INFRINGEMENT OF ANY PATENT, TRADEMARK, OR OTHER INTELLECTUAL PROPERTY RIGHTS.
In case of dissatisfaction for a valid reason and claimed in writing by a purchaser within ninety (90) days of receipt of mice, products or services, JACKSON will, at its option, provide credit or replacement for the mice or product received or the services provided.
No Liability
In no event shall JACKSON, its trustees, directors, officers, employees, and affiliates be liable for any causes of action or damages, including any direct, indirect, special, or consequential damages, arising out of the provision of MICE, PRODUCTS or services, including economic damage or injury to property and lost profits, and including any damage arising from acts or negligence on the part of JACKSON, its agents or employees. Unless prohibited by law, in purchasing or receiving MICE, PRODUCTS or services from JACKSON, purchaser or recipient, or any party claiming by or through them, expressly releases and discharges JACKSON from all such causes of action or damages, and further agrees to defend and indemnify JACKSON from any costs or damages arising out of any third party claims.
MICE and PRODUCTS are to be used in a safe manner and in accordance with all applicable governmental rules and regulations.
The foregoing represents the General Terms and Conditions applicable to JACKSON’s MICE, PRODUCTS or services. In addition, special terms and conditions of sale of certain MICE, PRODUCTS or services may be set forth separately in JACKSON web pages, catalogs, price lists, contracts, and/or other documents, and these special terms and conditions shall also govern the sale of these MICE, PRODUCTS and services by JACKSON, and by its licensees and distributors.
Acceptance of delivery of MICE, PRODUCTS or services shall be deemed agreement to these terms and conditions. No purchase order or other document transmitted by purchaser or recipient that may modify the terms and conditions hereof, shall be in any way binding on JACKSON, and instead the terms and conditions set forth herein, including any special terms and conditions set forth separately, shall govern the sale of MICE, PRODUCTS or services by JACKSON.
(6.8)
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InvisibleImorph
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Registered: 11/10/01
Posts: 146
old spore packaging materials?
#467186 - 11/23/01 02:44 AM (16 years, 1 month ago)
hello everybody does anybody know who use to use a small piece of plastic tubing bent into a circle and held togather by a plug of wire (about 10gauge) to ship spores to customers??? and if so is it possible to say what was the P. variety?... yes i even had a "pasterite compost machine " once upon time. itz been a while!
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InvisibleImorph
journeyman
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Registered: 11/10/01
Posts: 146
Re: old spore packaging materials? [Re: Imorph]
#467768 - 11/23/01 09:13 PM (16 years, 1 month ago)
No bodys been around to have seen this packaging from yesteryear? strain?
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Int. J. Mol. Sci. 2017, 18(2), 352; doi:10.3390/ijms18020352
Induction of Syndecan-4 by Organic–Inorganic Hybrid Molecules with a 1,10-Phenanthroline Structure in Cultured Vascular Endothelial Cells
1
Department of Environmental Health, Faculty of Pharmaceutical Sciences, Tokyo University of Science, Noda 278-8510, Japan
2
Department of Environmental Health, School of Pharmacy, Tokyo University of Pharmacy and Life Sciences, Hachioji 192-0392, Japan
3
Department of Environmental Health, Faculty of Pharmaceutical Sciences, Toho University, Funabashi 274-8510, Japan
4
Department of Chemistry, Faculty of Science, Tokyo University of Science, Shinjuku 162-8601, Japan
*
Author to whom correspondence should be addressed.
Academic Editors: Yasumitsu Ogra and Takafumi Hirata
Received: 12 December 2016 / Revised: 27 January 2017 / Accepted: 2 February 2017 / Published: 8 February 2017
View Full-Text | Download PDF [1668 KB, uploaded 8 February 2017] |
Abstract
Organic–inorganic hybrid molecules constitute analytical tools used in biological systems. Vascular endothelial cells synthesize and secrete proteoglycans, which are macromolecules consisting of a core protein and glycosaminoglycan side chains. Although the expression of endothelial proteoglycans is regulated by several cytokines/growth factors, there may be alternative pathways for proteoglycan synthesis aside from downstream pathways activated by these cytokines/growth factors. Here, we investigated organic–inorganic hybrid molecules to determine a variant capable of analyzing the expression of syndecan-4, a transmembrane heparan-sulfate proteoglycan, and identified 1,10-phenanthroline (o-Phen) with or without zinc (Zn-Phen) or rhodium (Rh-Phen). Bovine aortic endothelial cells in culture were treated with these compounds, and the expression of syndecan-4 mRNA and core proteins was determined by real-time reverse transcription polymerase chain reaction and Western blot analysis, respectively. Our findings indicated that o-Phen and Zn-Phen specifically and strongly induced syndecan-4 expression in cultured vascular endothelial cells through activation of the hypoxia-inducible factor-1α/β pathway via inhibition of prolyl hydroxylase-domain-containing protein 2. These results demonstrated an alternative pathway involved in mediating induction of endothelial syndecan-4 expression and revealed organic–inorganic hybrid molecules as effective tools for analyzing biological systems. View Full-Text
Keywords: endothelial cells; proteoglycan; 1,10-phenanthroline; syndecan-4; bioorganometallics endothelial cells; proteoglycan; 1,10-phenanthroline; syndecan-4; bioorganometallics
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Hara, T.; Kojima, T.; Matsuzaki, H.; Nakamura, T.; Yoshida, E.; Fujiwara, Y.; Yamamoto, C.; Saito, S.; Kaji, T. Induction of Syndecan-4 by Organic–Inorganic Hybrid Molecules with a 1,10-Phenanthroline Structure in Cultured Vascular Endothelial Cells. Int. J. Mol. Sci. 2017, 18, 352.
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57
|
cf5cd1df0ee2161e1684bdc019357275
|
5,161,853,917,916,012,000
|
Creative biogene
SHARE THIS
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Panoply™ Human SEBOX Knockdown Stable Cell Line
See other products for SEBOX
Cat.No.
CSC-DC013931
Description
Creative Biogene's Knockdown Cell Lines are target specific shRNA lentivirus transduced cells. The percent knockdown levels range from 75-99% depending on the gene, as evaluated by RT-PCR. Cells are rigorously qualified and mycoplasma free.
Gene
SEBOX
Gene Species
Human
Host Cell
HEK293 (Hela and other cell types are also available)
Growth Properties
Adherent
Morphology
Epithelial
Quality Control
Negative for bacteria, yeast, fungi and mycoplasma.
Size
2 × 10^6 cells / vial
Storage
Liquid Nitrogen
Ship
Dry Ice
Gene Information
Official Symbol
SEBOX
Synonyms
OG9; OG-9; OG9X
GeneID
mRNA Refseq
Protein Refseq
MIM
UniProt ID
Q9HB31
Chromosome Location
17q11.2
Function
molecular_function; sequence-specific DNA binding; sequence-specific DNA binding transcription factor activity;
Related Products
Cat#
Product Name
Host Cell
Gene Symbol
Species
Price
CSC-SC013931
HEK293 ,CHO, etc.
SEBOX
Human
Cat#
Product Name
Titer
Product Size
Species
Price
AD14368Z
>1x 10^9 vp/ml
1 x 0.2 ml
Human
Cat#
Product Name
Size/Form
Species
Price
CDCB176862
------
Danio rerio (zebrafish)
SHW015387
------
Danio rerio (zebrafish)
Related Services
Quick Inquiry
Please input "biogene" as verification code.
SEBOX Related Products
Contact us to order
USA
45-1 Ramsey Road, Shirley, NY 11967, USA
Tel: 1-631-626-9181
Fax: 1-631-614-7828
Email: [email protected]
Europe
Tel: 44-207-097-1828
Email: [email protected]
CBpromise
24x7 CUSTOMER SERVICE
CONTACT US TO ORDER
;
CONTACT CREATIVE BIOGENE
45-1 Ramsey Road, Shirley, NY 11967, USA
Tel: 1-631-626-9181
Fax: 1-631-614-7828
Email: [email protected]
Europe
Tel: 44-207-097-1828
Terms & Conditions | Privacy Policy | Sitemap | FAQ | © 2010-2018 Creative Biogene. All Rights Reserved.
|
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57
|
cf5cd1df0ee2161e1684bdc019357275
|
-8,339,463,563,756,465,000
|
• Publications
• Influence
Mitochondrial transcription factor A is necessary for mtDNA maintance and embryogenesis in mice
TLDR
The mouse gene for mitochondrial transcription factor A (Tfam), formerly known as m-mtTFA, is disrupted by gene targetting of loxP-sites followed by cre-mediated excision in vivo and is the first mammalian protein demonstrated to regulate mtDNA copy number in vivo. Expand
Replication of animal mitochondrial DNA
Sequence and gene organization of mouse mitochondrial DNA
TLDR
The mouse mitochondrial DNA genome is highly homologous in overall sequence and in gene organization to human mitochondrial DNA, with the descending order of conserved regions being tRNA genes; origin of light-strand replication; r RNA genes; knownprotein-coding genes; unidentified protein-c coding genes; displacement-loop region. Expand
Mitochondrial DNA maintenance in vertebrates.
TLDR
Because features of a transcription-primed mechanism appear to be conserved in vertebrates, a general model for initiation of vertebrate heavy-strand DNA synthesis is proposed. Expand
Replication and transcription of vertebrate mitochondrial DNA.
Dilated cardiomyopathy and atrioventricular conduction blocks induced by heart-specific inactivation of mitochondrial DNA gene expression
TLDR
This animal model reproduces biochemical, morphological and physiological features of the dilated cardiomyopathy of Kearns-Sayre syndrome and provides genetic evidence that the respiratory chain is critical for normal heart function. Expand
Elongation of displacement-loop strands in human and mouse mitochondrial DNA is arrested near specific template sequences.
TLDR
Direct sizing at the nucleotide level indicates that the 3' ends of D-loop strands of human and mouse mtDNA are discrete and map within three to five nucleotides on the complementary template strand. Expand
Similarity of human mitochondrial transcription factor 1 to high mobility group proteins.
TLDR
Human mitochondrial transcription factor 1 has been sequenced and is a nucleus-encoded DNA binding protein of 204 amino acids (24,400 daltons) with no similarities to any other DNA binding proteins except for the existence of two domains that are characteristic of high mobility group (HMG) proteins. Expand
Nuclear RNase MRP is required for correct processing of pre-5.8S rRNA in Saccharomyces cerevisiae.
TLDR
Results are consistent with RNase MRP playing a role in a late step of rRNA processing and indicate a requirement for having the smaller form of 5.8S rRNA, and they argue for processing at the B1 position being composed of two separate cleavage events catalyzed by two different activities. Expand
Purification and characterization of human mitochondrial transcription factor 1.
TLDR
Although mtTF1 is the only mitochondrial DNA-binding transcription factor to be purified and characterized, its properties, such as a high affinity for random DNA and a weak specificity for one of its target sequences, may typify this class of regulatory proteins. Expand
...
1
2
3
4
5
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cf5cd1df0ee2161e1684bdc019357275
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6,664,831,121,853,664,000
|
c424. pC 框架區間
Tags :
Accepted rate : 80人/112人 ( 71% ) [非即時]
評分方式：
Tolerant
最近更新 : 2017-12-06 23:56
Content
基因是含有特定遺傳信息的結構,用來決定生物的種性特徵。
生物學家發現,與特定功能相關的一群基因在基因序列上的位置通常十分靠近, 因此在基因序列中的連續片段被認為是有意義的。
一個包含 n 個基因的序列可以用 {1, 2, ..., n} 所組成的排列 S= (s1, s2, ..., sn) 來表示。
為了預測基因序列 S 上可能有意義的片段,一位生物學家遭遇了下列問題。
令 F(a, b) 代表在基因序列 S 上位置落在基因 a 和基因 b 之間的所有整數所構成的集合 (含 a 和 b)。
例如,令 S = (2, 7, 6, 4, 14, 13, 5, 8, 1, 9, 11, 10, 12, 3),
則 F(6, 8) = F(8, 6) = {6, 4, 14, 13, 5, 8}。
令 I(a, b) 代表數線上 a 和 b 這兩個整數間所有整數所構成的集合 (含 a 和 b)。
例如,I(6, 8) = I(8, 6) = {6, 7, 8}。在基因序列 S上如果兩個整數 a 和 b , 1 <= a < b <= n,
滿足 F(a, b) = I(a, b) 則稱 (a, b) 構成一個「框架區間」 (framed interval)。
舉例來說, 考慮基因序列 S = (2, 7, 6, 4, 14, 13, 5, 8, 1, 9,11, 10, 12, 3), 以 (a, b) = (9, 12) 為例,
因為 F(9, 12) = {9, 11, 10, 12} = {9, 10, 11, 12}= I(9, 12),所以 (9, 12) 是一個框架區間。
相同的 (6, 7)、(10, 11) 和 (13, 14) 也是框架區間。
這位生物學家想知道給定一個基因序列 S,有多少數對 (a, b) , 1 <= a < b <= n, 是一個框架區間?
例如,在基因序列 S = (2, 1, 5, 4, 3) 上,是框架區間的數對 (a, b) ,1 <= a < b <= 5,
有 (1, 2)、(3, 4)、(3, 5) 和 (4, 5), 共四個。
Input
第一行有一整數 T,代表有 T 組測試資料。
接下來每兩行用來描述一組基因序列,
第一行有一整數 n, 第二行有 n 個整數 s1, s2, ..., sn (數字之間以一個空白隔開),
代表基因序列 S = (s1, s2, ..., sn), 任兩個數字都不相同且1 <= s1, s2, ..., sn <= n。
Output
針對所輸入的基因序列 S,輸出一個數字,代表有多少數對 (a, b), 1 <= a < b <= n, 是一個框架區間?
Sample Input #1
輸入範例 1:
3
4
3 1 4 2
4
3 2 1 4
5
2 1 5 4 3
輸入範例 2:
2
14
2 7 6 4 14 13 5 8 1 9 11 10 12 3
11
3 10 4 5 6 8 7 9 11 2 1
Sample Output #1
輸出範例 1:
0
3
4
輸出範例 2:
4
9
測資資訊：
記憶體限制： 128 MB
不公開 測資點#0 (30%): 10.0s , <1M
不公開 測資點#1 (10%): 10.0s , <1M
不公開 測資點#2 (10%): 10.0s , <1M
不公開 測資點#3 (10%): 10.0s , <1M
不公開 測資點#4 (40%): 10.0s , <1M
Hint ：
本題共有三組測試資料。每組可有多個輸入檔案,全部答對該組才得分。
第一組 30 分,所有的測資 T <= 20、1 <= n <= 100。
第二組 30 分,所有的測資 T <= 6、1 <= n <= 3000。
第三組 40 分,所有的測資 T <= 20、1 <= n <= 5000。
Tags:
出處:
104學年度全國資訊學科能力競賽 [管理者： andy89923 (CTFang) ]
Status Forum 排行
ID User Problem Subject Hit Post Date
沒有發現任何「解題報告」
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Ocean acidification threatens Bering Sea crabs. But can they adapt? (audio)
An adult male red king crab in Bob Foy’s Kodiak laboratory. (Photo by Eric Keto / Alaska’s Energy Desk)
Ocean acidification could threaten some of Alaska’s most important fisheries. Researchers warn that populations of red king crab in the Bering Sea – made famous by the show The Deadliest Catch – could collapse by the end of the century.
But it’s possible the crabs might be able to evolve and adapt to the changing oceans. The big question is – will they have enough time?
Robert Foy directs the Alaska Fisheries Science Center’s Kodiak Laboratory. (Photo by Eric Keto / Alaska’s Energy Desk)
Biologist Robert Foy reaches into a tank in his Kodiak lab, as about twenty red king crabs move around on the bottom. They are giant. They are spiny. They are… kind of terrifying. But not to Foy. He scoops one out by the back leg.
“As long as you stay away from the first two, the pincers, you’re just fine,” he says.
Foy directs the Alaska Fisheries Science Center’s Kodiak Laboratory. His seawater lab is wall-to-wall crabs, in tanks and re-purposed containers: baby tanner crabs no bigger than a quarter and adult king crabs the size of my torso; crabs in tupperware, crabs in laundry baskets, crabs stacked in what Foy calls the “crab condominium.” A tangle of pipes and wires feed seawater into the different tanks, each one carefully calibrated by temperature and pH.
This lab offers a peek into the future. The tanks represent the oceans around Alaska decades from now. And Foy says that future is alarming.
“The expectation in change in pH over the next five decades in Alaska is fairly dramatic,” he says.
The change in pH is a measure of how acidic the ocean is becoming. In simple terms, the more carbon dioxide is dissolved in the water, the more acidic it becomes.
Ocean acidification is the less-well-understood fellow-traveler to climate change, the other impact of pumping CO2 into the atmosphere. And like climate change, it’s expected to happen faster at high latitudes — like the waters around Alaska — than in the rest of the world.
Eggs in a female red king crab. The laboratory studies the impacts of ocean acidification on crabs from the earliest life stages. (Photo by Eric Keto / Alaska’s Energy Desk)
Foy began this work about a decade ago, and his lab has been able to run long-term experiments, over years. It’s some of the first concrete evidence we have of what ocean acidification might mean for marine species.
And his first results are discouraging – at least for red king crabs. Under conditions similar to what researchers are eventually predicting for Alaska, pretty much all the young red king crabs died.
“If the results in the laboratory are accurate, and there’s no acclimation, you would see stock failure about 100 years from now,” Foy says.
That’s in part because it’s harder for many crabs to make and maintain shells in more acidic water: the chemistry isn’t right. But Foy’s team found that a bigger problem may be the sheer energy required for crabs to keep their internal pH right, when the external pH is wrong.
In very acidic water, most red king crabs didn’t make it past their early life stages.
But some did. And that’s giving researchers like Foy hope. Because if the survivors have some trait, something in their genetic make-up that helps them cope with more acidic waters, it’s possible they could pass that on to their offspring and the species could evolve.
But with oceans changing so fast – is there time for that?
“That’s the question,” Foy says. “Even if they could acclimate in a short period of time, or even adapt over a longer period of time, what kind of abilities will they have to do that physiologically if it happens over the scale of 50 years? That’s only a handful of generations for a crab species.”
Crabs are housed in tanks with varying pH and temperature, to mimic the conditions researchers predict will prevail in Alaska waters decades from now. (Photo by Eric Keto / Alaska’s Energy Desk)
This question is something crab fishermen are very aware of.
Edward Poulsen is a partner on two Bering Sea crab vessels. He grew up in the industry; he says his dad was one of its pioneers.
“It’s one of those things where you don’t want to think about it too much,” Poulsen says. “Because if you think about it too much, it’s pretty depressing.”
Poulsen knows the science. So do his fellow vessel-owners. He says everyone is concerned. But the potential problems are far enough in the future, and it’s not clear there’s anything fishermen can do about it.
“A lot of us, this is all we know, this is what we do,” Poulsen says. “And now the government’s telling us, ‘Your future might be at risk.’ I think it’s a little bit like you want to put your head in the sand and ignore what could be coming down the path.”
Poulsen says fishermen basically have two choices: they can try to diversify their business, and branch out into other fisheries.
Or they can hope the crabs adapt.
Rachel Waldholz, KTOO Public Media, 3 November 2017. Text and audio.
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• 1,147,041 hits
OA-ICC HIGHLIGHTS
Ocean acidification in the IPCC AR5 WG II
OUP book
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Cell Structure and Function-Plant Cell and Animal Cell (NEET (NTA)-National Eligibility cum Entrance Test (Medical) Biology): Questions 56 - 62 of 106
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Question number: 56
» Cell Structure and Function » Plant Cell and Animal Cell
Appeared in Year: 2005
MCQ▾
Question
Ectophloic siphonostele is found in: [AIPMT]
Choices
Choice (4) Response
a.
Osmunda and Equisetum
b.
Marsilea and Botrychium
c.
Dicksonia and Maiden hair fern
d.
Adiantum and Cucurbitaceae
Question number: 57
» Cell Structure and Function » Plant Cell and Animal Cell
MCQ▾
Question
Normal secondary growth takes place in-
Choices
Choice (4) Response
a.
Only in dicots
b.
Gymnosperms & Monocots
c.
Dicots & Gymnosperms
d.
Dicots & Monocots
Question number: 58
» Cell Structure and Function » Plant Cell and Animal Cell
Appeared in Year: 2001
MCQ▾
Question
Companion cells are associated with: [RPMT]
Choices
Choice (4) Response
a.
Vessels of Angiosperms
b.
Tracheids of Angiosperms
c.
Tracheids of Gymnosperms
d.
Sieve tubes of Angiosperms
Question number: 59
» Cell Structure and Function » Plant Cell and Animal Cell
Appeared in Year: 2003
MCQ▾
Question
Mesophyll is differentiated in spongy & palisade tissue is: - [RPMT]
Choices
Choice (4) Response
a.
Dorsiventral leaf
b.
Isobilateral leaf
c.
None
d.
Isobilateral root
Question number: 60
» Cell Structure and Function » Plant Cell and Animal Cell
Appeared in Year: 1998
MCQ▾
Question
Extra stellar secondary growth takes place by
Choices
Choice (4) Response
a.
Phellogen
b.
Phellem
c.
Vascular cambium
d.
Phelloderm
Question number: 61
» Cell Structure and Function » Plant Cell and Animal Cell
MCQ▾
Question
Living tissue in lenticel is called
Choices
Choice (4) Response
a.
Conjunctive tissue
b.
Connective tissue
c.
Phelloderm
d.
Complementary tissue
Question number: 62
» Cell Structure and Function » Plant Cell and Animal Cell
Appeared in Year: 2001
MCQ▾
Question
The resin duct of Gymnosperm is an example of [RPMT]
Choices
Choice (4) Response
a.
Schizogenous cavity
b.
Intracellular space
c.
Lysigenous cavity
d.
Vacuole containing stored material
f Page
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TY - JOUR UR - https://doi.org/10.7287/peerj.preprints.2305v1 DO - 10.7287/peerj.preprints.2305v1 TI - Computational characterization and epitope prediction for Bet-v1 like protein of Cannabis sativa AU - Basharat,Zarrin DA - 2016/07/20 PY - 2016 KW - allergen KW - epitope prediction KW - Structure modeling KW - phosphorylation KW - Cannabis sativa AB - Cannabis sativa encodes a Bet-v1 like protein is an allergen and a causuative agent of pollen allergy. Multiple sequence alignment of this protein revealed conserved residues in Betv1 domain. Identification of linear epitopes of this protein was done after preliminary bioinformatics characterization and structure prediction. Structure prediction was done using Modeller software and minimized using Swiss PDBViewer. Six linear epitopes were then, predicted using EMBOSS antigenic program. Phylogenetic analysis of Bet-v1 with other sequences demonstrated divergence patterns with allergens of other species but revealed conserved residues in allergenic epitopes. This study can serve as an informational aid in the development of hypoallergenic vaccine for Cannabis sativa allergy. VL - 4 SP - e2305v1 T2 - PeerJ Preprints JO - PeerJ Preprints J2 - PeerJ Preprints SN - 2167-9843 ER -
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-4,676,866,149,141,512,000
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WoRMS banner
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WoRMS taxon details
Checked: verified by a taxonomic editorHygrocrocis C.Agardh, 1824
AphiaID: 604954
Classification: Biota > Unreviewed: has not been verified by a taxonomic editorBacteria (Kingdom) > Unreviewed: has not been verified by a taxonomic editorBacteria incertae sedis (Phylum) > Checked: verified by a taxonomic editorHygrocrocis (Genus)
Status Unaccepted: synonym, or anything that is not accepted unaccepted
Rank Genus
Parent Unreviewed: has not been verified by a taxonomic editorBacteria incertae sedis
Source basis of record Guiry, M.D. & Guiry, G.M. (2017). AlgaeBase. World-wide electronic publication, National University of Ireland, Galway., available online at http://www.algaebase.org [details]
Direct child
taxa (1)
[show all]
Species Checked: verified by a taxonomic editorHygrocrocis olivacea C.Agardh, 1827
Link Unreviewed: has not been verified by a taxonomic editorPublished in AlgaeBase Logo AlgaeBase
LSID urn:lsid:marinespecies.org:taxname:604954
Taxonomic
Edit history
Date action by
2012-07-02 12:33:47Z created Guiry, Michael D.
[Taxonomic tree] [Occurrence map] [Google] [Google scholar] [Google images]
Citation: WoRMS (2015). Hygrocrocis C.Agardh, 1824. In: Guiry, M.D. & Guiry, G.M. (2015). AlgaeBase. World-wide electronic publication, National University of Ireland, Galway (taxonomic information republished from AlgaeBase with permission of M.D. Guiry). Accessed through: World Register of Marine Species at http://marinespecies.org/aphia.php/aphia.php?p=taxdetails&id=604954 on 2017-02-26
Creative Commons License The webpage text is licensed under a Creative Commons Attribution 4.0 License
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Web Access Research Portal
Research Output Details
Powell, S and Ferguson, SH and Bowman, JP and Snape, I, “Using Real-Time PCR to Assess Changes in the Hydrocarbon-Degrading Microbial Community in Antarctic Soil During Bioremediation”, Microbial Ecology, 52 (3) pp. 523-532. ISSN 0095-3628 (2006) [Refereed Article]
Data TypeValue
Type of ResearchApplied Research
Research DivisionBiological Sciences
Research GroupMicrobiology
Research FieldMicrobial Ecology
Research Objective DivisionEnvironment
Research Objective GroupEcosystem Assessment and Management
Research Objective FieldEcosystem Assessment and Management of Marine Environments
Visit Item on eCitehttp://ecite.utas.edu.au/31830
Digital Object Identifierdoi:10.1007/s00248-006-9131-z
Scopus Source URLView the full record on Scopus
Scopus Citing URLView the list of citing articles on Scopus
Web of Science® Source URLView the full record on Web of Science®
Web of Science® Citing URLView the list of citing articles on Web of Science®
Web of Science® Related URLView the list of related articles on Web of Science®
Number of Times Cited79
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Skip to main content Skip to accessibility
This website is not compatible with your web browser. You should install a newer browser. If you live in Jersey and need help upgrading call the States of Jersey web team on 440099.
Government of Jerseygov.je
Information and public services for the Island of Jersey
L'înformâtion et les sèrvices publyis pouor I'Île dé Jèrri
Jersey Biodiversity Partnership
What is the Jersey Biodiversity Partnership?
The Jersey Biodiversity Partnership is an informal partnership of more than 30 organisations and individuals committed to preserving and enhancing biodiversity in Jersey. Organisations within the partnership provide support in a variety of ways by offering:
• time
• expertise
• funding
• other resources
Why was it set up?
The Jersey Biodiversity Partnership was set up in 2006 for the purpose of implementing a range of action plans designed to target those species and habitats which are considered to be threatened, or in need of special attention and to provide a range of strategies and targets for their conservation.
How will the partnership reach its aims?
The partnership aims to protect, conserve and enhance a variety of wildlife species and habitats in Jersey through the successful implementation of the Jersey Biodiversity Strategy and associated Jersey Biodiversity Action Plans.
These aims will be achieved by focusing on the following specific goals:
• improving the flow of information and communication
• encouraging participation by all sectors of society
• promoting awareness of the importance of biodiversity
• supporting partner organisations in their legal and other responsibilities towards biodiversity
United Nations Decade on Biodiversity 2011 to 2020
The United Nations decade of biodiversity is a tool used by partners to put the Global Strategic Plan for Biodiversity 2011–2020 and the Aichi Targets into action. The Jersey Biodiversity Partnership signed up to the United Nations Decade on Biodiversity in 2011. This means that we have committed to saving biodiversity and enhance its benefits for people.
Why do we need action for biodiversity?
Biodiversity is the variety of all living things. It is the ecosystems in which they live and the ways they interact with each other. Biodiversity continually adapts in order to survive under constantly changing conditions. We enjoy many benefits from our healthy and diverse ecosystems, such as:
• clean air for us to breathe
• food to eat
• improved water quality
• medicines to keep us well
• productive soils and nutrient cycling
• regulated local climate which prevents flooding and pollution
• enhances our emotional and physical health and well being
This is why preserving our natural plants and animals and the habitats they rely on is so important.
Examples of Jersey species that are in decline
We measure the number of butterflies as they represent what is happening with all invertebrate fauna. Butterfly numbers and diversity are declining in Jersey and we know this is also the case with other invertebrate species. Three quarters of Jersey's land surface is urban and agricultural landscape and we are seeing butterfly numbers in decline in these areas, this is also being seen in other European countries. However, there is a measured increase in butterflies on most of the island's protected and managed semi-natural sites which is encouraging.
Breeding bird data can act as a measure for understanding the condition of our environment. Jersey's current dataset suggests that over 19 years comprising of 32 species of breeding birds on farmland/suburban habitats is declining rapidly. In contrast populations comprising of 10 bird species on semi-natural habitats is slowly increasing.
Who are the partners?
The following groups are among those included in the partnership:
• Action for Wildlife Jersey
• Amphibian and Reptile Conservation Trust
• Birds on the Edge
• British Divers Marine Life Rescue
• Durrell Wildlife Conservation Trust
• Ecoscape
• Guernsey Biological Record Centre
• Jersey Amphibian and Reptile Group
• Jersey Barn Owl Network
• Jersey Bat Group
• Jersey Biodiversity Centre
• Jersey Butterfly Monitoring Scheme
• Jersey Hedgehog Preservation Group
• Jersey National Park
• Jersey Marine Conservation
• Jersey Trees for Life
• JSPCA Animal Shelter
• Little Green Man
• Littlefeet Environmental
• National Trust for Jersey
• National Plant Monitoring Scheme
• New Era Veterinary Hospital
• Nurture Ecology
• Samarès Manor
• Sangan Island Conservation
• Seedy Sunday
• Société Jersiaise
• St Helier in Bloom
• St Martin in Bloom
• United Nations Decade on Biodiversity
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57
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cf5cd1df0ee2161e1684bdc019357275
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-2,102,678,648,388,261,400
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HPA016596
DCAF12 antibody from Sigma-Aldrich
CT102, DKFZP434O125, KIAA1892, MGC1058, TCC52, WDR40A
Immunohistochemistry
Recommended by provider
Protein array
Recommended by provider
Antibody data
Product number
HPA016596
Provider
Sigma-Aldrich
Proper citation
Sigma-Aldrich Cat#HPA016596, RRID:AB_1852438
Product name
Anti-WDR40A antibody produced in rabbit
Provider product page
Sigma-Aldrich - HPA016596
Antibody type
Polyclonal
Antigen
WD repeat-containing protein 40A recombinant protein epitope signature tag (PrEST)
Description
affinity isolated antibody
Reactivity
Human
Antigen sequence
DDGHKDWIFSIAWISDTMAVSGSRDGSMGLWEVTD
DVLTKSDARHNVSRVPVYAHITHKALKDIPKEDTN
PDNCKVRALAFNNKNKELGAVSLD
Storage
-20C
Provider Type Product Number
- No reagents -
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57
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cf5cd1df0ee2161e1684bdc019357275
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1,174,684,527,388,331,800
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Category Archives: Noteworthy people
Pure ‘white’ race – did it ever exist? Part 1
(based mainly on David Mac Ritchie’s Ancient and Modern Britons Volume 1, ISBN 9781592322251)51tqkszqn0l-_sy344_bo1204203200_
In keeping with accuracy, Britain does not mean just England. I mean it as synonymous with British Isles (the collective name of the island containing England, Scotland & Wales – what used to be called Albion/ Prettania/ Brettania/ Alouíōn), Ireland (Northern & Republic – what used to be called Ierne/ Hibernia/ Iouernía), and the surrounding smaller islands.
When I first heard of this book I knew I wanted it. Now I’ve got it, it’s quickly becoming one of the most fascinating books on ‘race’ I’ve ever read. Mac Ritchie was a ‘white’ Scottish historian & folklorist, yet the information he delivers will probably be nothing short of miraculous to ‘black’ people interested in ‘black’ history.
Disclaimer: As informative as it is, it must be remembered it was written in the 1800s before knowledge of DNA was available to corroborate. It was also the time when scientific racism was at its peak. I just present this info as a potentially useful guideline and insight into the mindset of the past. If you want to see how true the claims are, please do your own research to independently verify.
Continue reading Pure ‘white’ race – did it ever exist? Part 1
Don’t tell me you haven’t heard about it…
black-panther-hr-poster.jpg
WARNING: SPOILER ALERT!!!
Last Saturday night (17/2/2018) I and some friends went to watch the new Black Panther movie. Admittedly I’d had some reservations, primarily because Continue reading Don’t tell me you haven’t heard about it…
Cheddar Man: DNA shows early Briton had dark skin
(Reposted from: https://www.bbc.co.uk/news/amp/science-environment-42939192)
Cheddar Man: DNA shows early Briton had dark skin
•
DNA shows early Brit had dark skin
Image caption DNA shows early Brit had dark skin
A cutting-edge scientific analysis shows that a Briton from 10,000 years ago had dark brown skin and blue eyes.
Researchers from London’s Natural History Museum extracted DNA from Cheddar Man, Britain’s oldest complete skeleton, which was discovered in 1903.
University College London researchers then used the subsequent genome analysis for a facial reconstruction.
It underlines the fact that the lighter skin characteristic of modern Europeans is a relatively recent phenomenon.
No prehistoric Briton of this age had previously had their genome analysed.
As such, the analysis provides valuable new insights into the first people to resettle Britain after the last Ice Age.
The analysis of Cheddar Man’s genome – the “blueprint” for a human, contained in the nuclei of our cells – will be published in a journal, and will also feature in the upcoming Channel 4 documentary The First Brit, Secrets Of The 10,000-year-old Man.
‘Cheddar George’ tweet on early Briton
Cheddar Man’s remains had been unearthed 115 years ago in Gough’s Cave, located in Somerset’s Cheddar Gorge. Subsequent examination has shown that the man was short by today’s standards – about 5ft 5in – and probably died in his early 20s.
Prof Chris Stringer, the museum’s research leader in human origins, said: “I’ve been studying the skeleton of Cheddar Man for about 40 years
“So to come face-to-face with what this guy could have looked like – and that striking combination of the hair, the face, the eye colour and that dark skin: something a few years ago we couldn’t have imagined and yet that’s what the scientific data show.”
Cheddar Man
Image captionA replica of Cheddar Man’s skeleton now lies in Gough’s Cave
Fractures on the surface of the skull suggest he may even have met his demise in a violent manner. It’s not known how he came to lie in the cave, but it’s possible he was placed there by others in his tribe.
The Natural History Museum researchers extracted the DNA from part of the skull near the ear known as the petrous. At first, project scientists Prof Ian Barnes and Dr Selina Brace weren’t sure if they’d get any DNA at all from the remains.
But they were in luck: not only was DNA preserved, but Cheddar Man has since yielded the highest coverage (a measure of the sequencing accuracy) for a genome from this period of European prehistory – known as the Mesolithic, or Middle Stone Age.
They teamed up with researchers at University College London (UCL) to analyse the results, including gene variants associated with hair, eye and skin colour.
Extra mature Cheddar
They found the Stone Age Briton had dark hair – with a small probability that it was curlier than average – blue eyes and skin that was probably dark brown or black in tone.
This combination might appear striking to us today, but it was a common appearance in western Europe during this period.
Steven Clarke, director of the Channel Four documentary, said: “I think we all know we live in times where we are unusually preoccupied with skin pigmentation.”
Prof Mark Thomas, a geneticist from UCL, said: “It becomes a part of our understanding, I think that would be a much, much better thing. I think it would be good if people lodge it in their heads, and it becomes a little part of their knowledge.”
Unsurprisingly, the findings have generated lots of interest on social media.
Cheddar Man’s genome reveals he was closely related to other Mesolithic individuals – so-called Western Hunter-Gatherers – who have been analysed from Spain, Luxembourg and Hungary.
Dutch artists Alfons and Adrie Kennis, specialists in palaeontological model-making, took the genetic findings and combined them with physical measurements from scans of the skull. The result was a strikingly lifelike reconstruction of a face from our distant past.
Pale skin probably arrived in Britain with a migration of people from the Middle East around 6,000 years ago. This population had pale skin and brown eyes and absorbed populations like the ones Cheddar Man belonged to.
Chris Stringer
Image caption Prof Chris Stringer had studied Cheddar Man for 40 years – but was struck by the Kennis brothers’ reconstruction
No-one’s entirely sure why pale skin evolved in these farmers, but their cereal-based diet was probably deficient in Vitamin D. This would have required agriculturalists to absorb this essential nutrient from sunlight through their skin.
“There may be other factors that are causing lower skin pigmentation over time in the last 10,000 years. But that’s the big explanation that most scientists turn to,” said Prof Thomas.
Boom and bust
The genomic results also suggest Cheddar Man could not drink milk as an adult. This ability only spread much later, after the onset of the Bronze Age.
Present-day Europeans owe on average 10% of their ancestry to Mesolithic hunters like Cheddar Man.
Britain has been something of a boom-and-bust story for humans over the last million-or-so years. Modern humans were here as early as 40,000 years ago, but a period of extreme cold known as the Last Glacial Maximum drove them out some 10,000 years later.
There’s evidence from Gough’s Cave that hunter-gatherers ventured back around 15,000 years ago, establishing a temporary presence when the climate briefly improved. However, they were soon sent packing by another cold snap. Cut marks on the bones suggest these people cannibalised their dead – perhaps as part of ritual practices.
Image copyright CHANNEL 4Ian Barnes
Image caption The actual skull of Cheddar Man is kept in the Natural History Museum, seen being handled here by Ian Barnes
Britain was once again settled 11,000 years ago; and has been inhabited ever since. Cheddar Man was part of this wave of migrants, who walked across a landmass called Doggerland that, in those days, connected Britain to mainland Europe. This makes him the oldest known Briton with a direct connection to people living here today.
This is not the first attempt to analyse DNA from the Cheddar Man. In the late 1990s, Oxford University geneticist Brian Sykes sequenced mitochondrial DNA from one of Cheddar Man’s molars.
Mitochondrial DNA comes from the biological “batteries” within our cells and is passed down exclusively from a mother to her children.
Prof Sykes compared the ancient genetic information with DNA from 20 living residents of Cheddar village and found two matches – including history teacher Adrian Targett, who became closely connected with the discovery. The result is consistent with the approximately 10% of Europeans who share the same mitochondrial DNA type.
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Norwegians tell Trump “We don’t want to come to your s***hole country”: Scandinavians express solidarity with Haiti and African nations
Reposted from: http://www.independent.co.uk/news/world/americas/us-politics/norwegians-tell-trump-we-dont-want-to-come-to-your-shole-country-a8156666.html
(Honestly I was putting off writing about tRump because he’s obviously an attention slut, the media is giving him more coverage than I think he deserves and everyone’s taking too long to notice his stupidity, but THIS was too good!)
Norwegians tell Trump: We don’t want to come to your s***hole country
Scandinavians express solidarity with Haiti and African nations
Continue reading Norwegians tell Trump “We don’t want to come to your s***hole country”: Scandinavians express solidarity with Haiti and African nations
In the name of God/s, part 11: Zoroastrianism
Apologies to you all for taking so long to do a new post. I’ve recently had to make a lot of changes in my personal life, as a result of which I will only be able to post no more than once a month. Nevertheless please enjoy as I still have many post ideas, and if there are any subjects you’d like me to write about please share with me in the comments.
Now on with the post:
• Founder/s: Zarathustra (sometimes spelt Zarathushtra) Spitara, more commonly known in the West as Zoroaster
• Approximate age: 3500-4000 years, definitely preceded Judaism
• Place of origin: Persia (Iran & western Afghanistan)
• Holy book/s: Avesta
• Original language of holy book/s: Avestan Persian, aka. Zend
• Demonym of adherents: Zoroastrians/ Zarathustrians
• Approximate number of current global adherents: 124-190,000
• Place of worship name/s: dar-e-mehr, fire temple, fire house, atash gah, agiyari
Note: other names of this religion are Mazdayasna, Zarathustraism, Mazdaism, Magianism & Behdin. Continue reading In the name of God/s, part 11: Zoroastrianism
aswathi thomas
a look into the mind of a crazy indian girl
science.casual
All science, mostly casual.
Humanist Association of Ghana
Challenging superstition in the pursuit of human dignity and compassion
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Preview: Stages of reproduction (1)
Summary
Adaptive Learning Enabled
• 4 Lesson Contents
• 21 Assessment Questions
• 4 PDFs
• 7 Achievable CAPS Goals
• 27 Achievable Custom Goals
Table of Contents
• Objectives
• What are the stages of reproduction
• The main processes
• Recap
• Assessment
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57
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cf5cd1df0ee2161e1684bdc019357275
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-7,385,508,000,460,440,000
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Skip to main content
Online immunocapture ICP-MS for the determination of the metalloprotein ceruloplasmin in human serum
Abstract
Objective
The human copper-protein ceruloplasmin (Cp) is the major copper-containing protein in the human body. The accurate determination of Cp is mandatory for the reliable diagnosis of several diseases. However, the analysis of Cp has proven to be difficult. The aim of our work was a proof of concept for the determination of a metalloprotein-based on online immunocapture ICP-MS. The immuno-affinity step is responsible for the enrichment and isolation of the analyte from serum, whereas the compound-independent quantitation with ICP-MS delivers the sensitivity, precision, and large dynamic range. Off-line ELISA (enzyme-linked immunosorbent assay) was used in parallel to confirm the elution profile of the analyte with a structure-selective method. The total protein elution was observed with the 32S mass trace. The ICP-MS signals were normalized on a 59Co signal.
Results
The human copper-protein Cp could be selectively determined. This was shown with pure Cp and with a sample of human serum. The good correlation with off-line ELISA shows that Cp could be captured and eluted selectively from the anti-Cp affinity column and subsequently determined by the copper signal of ICP-MS.
Introduction
Ceruloplasmin (Cp) is an enzyme belonging to the multi-copper oxidase family and contains six copper atoms [1, 2]. In human plasma from healthy subjects, more than 95% of the total copper is bound to Cp. Serum Cp levels of less than 200 mg/L are considered to be a diagnostic criterion for Wilson’s disease [3], an autosomal recessive inherited disorder of copper metabolism, which can be fatal, if not treated properly. In addition, the Menkes disease [4, 5] (“kinky hair syndrome”) can be confirmed by determination of Cp.
The diagnostic determination of Cp in serum or plasma is usually performed by turbidimetric or nephelometric [6] and other immunoassays [7]. In addition, some other methods have been published, such as SEC–ICP-MS [8], where a depletion cartridge was used to remove highly abundant proteins, such as albumin. In any case, standardization of Cp analysis turned out to be quite difficult and left some serious questions unanswered largely due to the lack of Cp reference materials. To resolve these issues, we explored the feasibility of an approach based on an immunocapture step, which was performed as clean-up and enrichment, followed by hetero-element detection by use of inductively coupled plasma mass spectrometry (ICP-MS).
Immunocapture, which is a variant of affinity extraction or affinity chromatography, can be regarded as one of the most powerful separation techniques available [9,10,11]. This approach is particularly valuable when the analyte is present in low concentrations, and the matrix is complex, such as in food analysis or human diagnostics. In the field of high-sensitivity protein analysis, usually only affinity-based techniques are feasible, e.g. enzyme-linked immunosorbent assay (ELISA) [12]. Unfortunately, the calibration of immunoassays is not trivial and many inexperienced users have problems to interpret the results properly. Particularly, the existence of “cross-reactivity” often leads to some confusion, although this is nothing else as an analytical interference, which is occurring in any instrumental method. Affinity extraction is often combined with instrumental analytical techniques, such as mass spectrometry [13, 14] and hence does not need much rethinking in relation to a more traditional analytical workflow. However, the most selective affinity techniques are commonly based on antibody/analyte interactions, requiring sufficient amounts of high-quality antibodies directed against the respective analyte. The availability of such antibodies may be limited and almost always the cost of a sufficient amount of antibodies is high. On the other hand, in the field of protein analysis, even researchers with many years of experience sometimes seem to underestimate the complexity of their samples and therefore do not sufficiently appreciate the importance of extensive sample-preparation steps.
In this work, we used an uncommon approach to produce sufficient amounts of antibodies in chicken eggs at a reasonable cost in an animal-friendly way. The developed antibodies were used for the enrichment and isolation of Cp, followed by its quantitative determination using ICP-MS.
Main text
Experimental setup
The schematic representation of immunocapture ICP-MS setup is shown in Fig. 1. The eluate was split into two equal parts for the collection on an ELISA plate as well as online ICP-MS analysis. More experimental details can be found in Additional files 1 and 2.
Fig. 1
figure 1
Schematic representation of the immunocapture ICP-MS setup
Results
In Fig. 2, ICP-MS data show elution peaks of the characteristic elements expected for pure Cp (S, Cu). The signals were normalized to 59Co, which was introduced continuously as a post-column internal standard. The stability of the elution process was demonstrated by the tracer (158Gd) which is not retained on the column and was therefore introduced in the elution buffer. Generally, ELISA and ICP-MS data showed comparable elution profiles.
Fig. 2
figure 2
Immunocapture elution signals of an injection of pure, human ceruloplasmin (90 µg). All ICP-MS signals were normalized to 59Co. 158Gd was a tracer for the elution buffer
A tentative quantification of Cp was attempted through comparing the ICP-MS signal of copper in Cp with that of standard elemental copper. The recovery of Cp was 94% (based on the nominal Cp concentration and 6 copper atoms per Cp).
In Fig. 3, the injection and elution of a real sample (human serum) are shown. The sulfur and the Cp-selective ELISA traces are somehow broadened, which is an indication that the elution of the protein part of the molecule is delayed by slower diffusion or non-specific binding. Due to the fact that the Cu signal is not affected, the shoulder in the sulfur signal is a hint for eluting serum proteins or of Cp fragments, which do not contain any copper. Considering that the quantitation of Cp should be achieved finally, the result is very interesting. Although the protein and the metal peaks are separated slightly, accurate quantitation based on ICP-MS should be achieved without difficulty. By this experiment, it can be demonstrated that the immunoaffinity approach is robust and can be applied to complex serum samples as well. Comparison with the ELISA results also demonstrates that Cp is eluted more or less as an intact protein. Using 100 µL of serum, the amount of Cp in the serum is calculated to be 166 µg (using standard copper solution and based on 6 copper atoms in Cp). Validation of the new method can be achieved once a certified reference material (CRM) of Cp will become available.
Fig. 3
figure 3
Immunocapture elution signals of an injection of human serum containing a natural level of ceruloplasmin (100 µL diluted with 10 mL of PBS). The ICP-MS signals were normalized to 59Co
Discussion
The selective detection of the copper-protein ceruloplasmin was achieved by an immunoaffinity ICP-MS approach. It could be shown that ceruloplasmin can be eluted by a glycine/HCl buffer (pH 2.2) and subsequently detected and tentatively quantified online in an ICP-MS system. For validation purposes, a fractionated immunoassay was performed. The elution curves monitored by ICP-MS and immunoassay correlate to a high extent and prove that copper and the protein part of the ceruloplasmin can be eluted from the affinity column. However, for the quantification of ceruloplasmin by ICP-MS it is irrelevant, whether copper is still bound to the ceruloplasmin in the elution buffer. The peak area of copper represents the amount of ceruloplasmin considering its stoichiometry. The copper:sulfur ratio is a good way to identify copper losses because sulfur is covalently bound to the protein, whereas copper may be exchanged or lost to a certain extent. Critical for the success of this approach is the use of buffers of extremely low metal content. Nevertheless, the introduction of an additional washing step with ultrapure lab water reduces the background signal by a factor of 10 and also facilitates the integration of the peaks.
Limitations
This work should be seen as a proof of concept. Validation and exploration of the applicability to other metalloproteins or sample types have to be performed in the future. Nevertheless, this work shows that online immunocapture ICP-MS is an interesting option for quantitative protein analysis.
Abbreviations
Cp:
ceruloplasmin
CRM:
certified reference material
ELISA:
enzyme-linked immunosorbent assay
HCl:
hydrochloric acid
ICP-MS:
inductively coupled plasma mass spectrometry
SEC:
size exclusion chromatography
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Authors’ contributions
BB and AHEK performed the experiments and analyzed the data. MGW and NJ conceived and designed the experiments. MGW wrote the first draft of the paper, which was subsequently corrected and complemented by BB, AHEK, and NJ. All authors read and approved the final manuscript.
Acknowledgements
Not applicable.
Competing interests
The authors declare that they have no competing interests.
Availability of data and materials
The datasets used and/or analyzed during the current study are available from the corresponding author on reasonable request.
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Ethics approval and consent to participate
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Funding
This work was supported by the EMRP project HLT05 “Metrology for Metalloproteins”. The EMRP was jointly funded by the EMRP participating countries within EURAMET and the European Union.
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Correspondence to Michael G. Weller.
Additional files
Additional file 1.
Table of the instrumental parameters of ICP-MS analysis.
Additional file 2.
Experimental details. Preparation of chicken antibodies against human ceruloplasmin. ELISA protocol for antibody testing and offline ceruloplasmin determination. Preparation of the immunocapture affinity column. ICP-MS protocol. Protocol of the immunocapture ICP-MS experiments.
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Bernevic, B., El-Khatib, A.H., Jakubowski, N. et al. Online immunocapture ICP-MS for the determination of the metalloprotein ceruloplasmin in human serum. BMC Res Notes 11, 213 (2018). https://doi.org/10.1186/s13104-018-3324-7
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Lineage for d1rkwb1 (1rkw B:2-72)
1. Root: SCOPe 2.07
2. 2299346Class a: All alpha proteins [46456] (289 folds)
3. 2304501Fold a.4: DNA/RNA-binding 3-helical bundle [46688] (14 superfamilies)
core: 3-helices; bundle, closed or partly opened, right-handed twist; up-and down
4. 2304502Superfamily a.4.1: Homeodomain-like [46689] (20 families) (S)
consists only of helices
5. 2304932Family a.4.1.9: Tetracyclin repressor-like, N-terminal domain [46764] (35 protein domains)
6. 2305004Protein Multidrug binding protein QacR [68964] (1 species)
7. 2305005Species Staphylococcus aureus [TaxId:1280] [68965] (24 PDB entries)
Uniprot P23217
8. 2305017Domain d1rkwb1: 1rkw B:2-72 [104969]
Other proteins in same PDB: d1rkwa2, d1rkwb2, d1rkwd2, d1rkwe2
complexed with pnt, so4
Details for d1rkwb1
PDB Entry: 1rkw (more details), 2.62 Å
PDB Description: crystal structure of the multidrug binding transcriptional repressor qacr bound to pentamadine
PDB Compounds: (B:) Transcriptional regulator qacR
SCOPe Domain Sequences for d1rkwb1:
Sequence; same for both SEQRES and ATOM records: (download)
>d1rkwb1 a.4.1.9 (B:2-72) Multidrug binding protein QacR {Staphylococcus aureus [TaxId: 1280]}
nlkdkilgvakelfikngynatttgeivklsesskgnlyyhfktkenlfleilnieeskw
qeqwkkeqika
SCOPe Domain Coordinates for d1rkwb1:
Click to download the PDB-style file with coordinates for d1rkwb1.
(The format of our PDB-style files is described here.)
Timeline for d1rkwb1:
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biology question #4502
Hannah, a 11 year old female from North Bay, Ontario asks on January 3, 2009,
Q:
My Dad told me about bioluminescence you know, the stuff that makes living organisms glow? Anyway, what exactly makes them light up like that? Is it their skin?
viewed 14620 times
the answer
Barry Shell answered on January 3, 2009, A:
A chemical reaction is what makes them light up. The creature or plant or fungus has special cells in which two or more chemicals combine to produce light. It could be within the skin, or it could be deeper inside the fish or creature, but the outer layers would be transparent and clear, so the light would come through. You can get the basics about bioluminescence at wikipedia. Follow the links at the bottom of that page for many more websites about bioluminescence.
Add to or comment on this answer using the form below.
(required)
(required if you would like a response)
Note: All submissions are moderated prior to posting.
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6,403,094,930,729,589,000
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Curr Biol. 2001 Dec 11;11(24):1903-13.
Different WASP family proteins stimulate different Arp2/3 complex-dependent actin-nucleating activities.
Author information
1
Department of Cellular and Molecular Pharmacology, University of California-San Francisco, 94143, USA.
Abstract
BACKGROUND:
Assembly and organization of actin filaments are required for many cellular processes, including locomotion and division. In many cases, actin assembly is initiated when proteins of the WASP/Scar family respond to signals from Rho family G proteins and stimulate the actin-nucleating activity of the Arp2/3 complex. Two questions of fundamental importance raised in the study of actin dynamics concern the molecular mechanism of Arp2/3-dependent actin nucleation and how different signaling pathways that activate the same Arp2/3 complex produce actin networks with different three-dimensional architectures?
RESULTS:
We directly compared the activity of the Arp2/3 complex in the presence of saturating concentrations of the minimal Arp2/3-activating domains of WASP, N-WASP, and Scar1 and found that each induces unique kinetics of actin assembly. In cell extracts, N-WASP induces rapid actin polymerization, while Scar1 fails to induce detectable polymerization. Using purified proteins, Scar1 induces the slowest rate of nucleation. WASP activity is 16-fold higher, and N-WASP activity is 70-fold higher. The data for all activators fit a mathematical model in which one activated Arp2/3 complex, one actin monomer, and an actin filament combine into a preactivation complex which then undergoes a first-order activation step to become a nucleus. The differences between Scar and N-WASP activity are explained by differences in the rate constants for the activation step. Changing the number of actin binding sites on a WASP family protein, either by removing a WH2 domain from N-WASP or by adding WH2 domains to Scar1, has no significant effect on nucleation activity. The addition of a three amino acid insertion found in the C-terminal acidic domains of WASP and N-WASP, however, increases the activity of Scar1 by more than 20-fold. Using chemical crosslinking assays, we determined that both N-WASP and Scar1 induce a conformational change in the Arp2/3 complex but crosslink with different efficiencies to the small molecular weight subunits p18 and p14.
CONCLUSION:
The WA domains of N-WASP, WASP, and Scar1 bind actin and Arp2/3 with nearly identical affinities but stimulate rates of actin nucleation that vary by almost 100-fold. The differences in nucleation rate are caused by differences in the number of acidic amino acids at the C terminus, so each protein is tuned to produce a different rate of actin filament formation. Arp2/3, therefore, is not regulated by a simple on-off switch. Precise tuning of the filament formation rate may help determine the architecture of actin networks produced by different nucleation-promoting factors.
PMID:
11747816
DOI:
10.1016/s0960-9822(01)00603-0
[Indexed for MEDLINE]
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What’s Behind the Drop in Tulum’s Sargassum Levels?
June 16, 2024
Today´s Paper
What’s Behind the Drop in Tulum’s Sargassum Levels?
What’s Behind the Drop in Tulum’s Sargassum Levels?
Tulum sees a significant drop in sargassum, collecting 646 tons in early 2024 versus 2,448 tons last year, signaling a potential reprieve for beaches and tourism.
What’s Behind the Drop in Tulum’s Sargassum Levels?
TULUM, México —In the first five months of 2024, a significant decrease in sargassum collection was observed in Tulum compared to the same period last year, according to data provided by the municipal Directorate of the Federal Maritime Terrestrial Zone (Zofemat).
Zofemat’s records show that from January to May of last year, 2,448 tons of sargassum were collected. In the same period this year, the figure is just 646 tons—almost four times less. This marked reduction highlights a notable decrease in the presence of sargassum on the beaches managed by Zofemat. Specifically, in January 2024, 43 tons were collected; February saw 50 tons; March recorded 81 tons; 193 tons in April; and 279 tons in May.
It is important to note that Zofemat is responsible for maintaining the beaches of the Tulum National Park and Punta Piedra, areas that have been heavily impacted by sargassum influxes. The decreased amount of sargassum collected could be welcomed news for coastal communities and tourists visiting the region. However, Zofemat in Tulum emphasizes the importance of continued vigilance and attention to combat any changes in the situation and ensure the preservation of the beaches and marine ecosystem.
As reported by The Tulum Times, the sargassum season for the Mexican Caribbean started intensely. Many hoteliers and tourism service providers who depend directly on the beaches feel they are not prepared to face it. Despite the encouraging reduction in sargassum collection, the unpredictability of sargassum blooms requires ongoing readiness and proactive measures.
Sargassum, a type of seaweed, has become a significant environmental issue for the Caribbean coast, affecting tourism and local economies. Ocean currents often carry the floating algae mats and can wash ashore in massive quantities, causing problems for beachgoers and marine life. The decay of sargassum on beaches can lead to foul odors and attract insects, making it a pressing concern for beach maintenance teams and local businesses.
The reasons behind this year’s reduced sargassum influx are not entirely clear. Factors such as ocean currents, wind patterns, and temperature changes can all influence the movement and accumulation of sargassum. Researchers and environmental scientists continue studying these patterns to predict better and manage future sargassum blooms.
What’s Behind the Drop in Tulum’s Sargassum Levels?
In Tulum, the response to the sargassum issue has included beach cleanup efforts and preventative measures. Barriers have been installed in the water to catch sargassum before it reaches the shore, and special boats are used to collect the seaweed at sea. These efforts, combined with the natural reduction observed this year, have helped to keep the beaches more accessible and enjoyable for visitors.
Local businesses, particularly those in the tourism sector, are cautiously optimistic about the reduced sargassum levels. Hotels and resorts have reported fewer guest complaints and a more pleasant beach experience. However, they remain aware of the potential for sudden changes in sargassum levels and the need for rapid response capabilities.
Sargassum’s environmental impact is not limited to the beaches. Large amounts of seaweed can affect marine ecosystems, smothering coral reefs and seagrass beds and depleting oxygen levels in the water as it decomposes. This can have cascading effects on marine life, from fish to sea turtles. As such, managing sargassum is not just about maintaining tourist appeal but also about protecting the health of the marine environment.
What’s Behind the Drop in Tulum’s Sargassum Levels?
The efforts in Tulum to manage sargassum reflect a broader regional challenge faced by many Caribbean destinations. Collaboration between local authorities, researchers, and the tourism industry is crucial to developing effective strategies. Public awareness and community involvement also play key roles in addressing this ongoing issue.
Tulum’s approach to sargassum management will likely continue to evolve as new methods and technologies become available. The lessons learned from recent years’ experiences will inform future actions and help ensure that Tulum remains a beautiful and sustainable destination for residents and visitors alike.
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Did you mean
s. van form
Search results - 88 results
A robust, cost-effective and widely applicable whole-genome sequencing protocol for capripoxviruses
Publication Type: Peer reviewed scientific article Authors: Mathijs, Elisabeth; Haegeman, Andy; De Clercq, Kris; Van Borm, Steven; Vandenbussche, Frank Source: Journal of Virological Methods (2022) ...
Coding-Complete Sequences of Recombinant Lumpy Skin Disease Viruses Collected in 2020 from Four Outbreaks in Northern Vietnam.
Philips, Wannes; Dam, Thi Vui; Andy Haegeman; Van Borm, Steven; Kris De Clercq Source: Microbiol Resour Announc, Volume 10, Issue 48 (2021) Abstract: (LSDV) causes a severe, systemic, and economically ...
Metagenomic sequencing determines complete infectious bronchitis virus (avian Gammacoronavirus) vaccine strain genomes and associated viromes in chicken clinical samples.
Publication Type: Peer reviewed scientific article Authors: Van Borm, Steven; Steensels, Mieke; Mathijs, Elisabeth; Vandenbussche, Frank; Thierry van den Berg; Lambrecht, Benedicte Source: Virus ...
Nearly Complete Genome Sequences of Two Bluetongue Viruses Isolated during the 2020 Outbreak in the Grand Duchy of Luxembourg.
Publication Type: Peer reviewed scientific article Authors: Vandenbussche, Frank; Bourg, Manon; Mathijs, Elisabeth; Lefebvre, David; De Leeuw, Ilse; Haegeman, Andy; Laetitia Aerts; Van Borm, Steven; ...
Complete Coding Sequence of a Lumpy Skin Disease Virus from an Outbreak in Bulgaria in 2016.
Publication Type: Peer reviewed scientific article Authors: Mathijs, Elisabeth; Vandenbussche, Frank; Ivanova, Emiliya; Haegeman, Andy; Laetitia Aerts; De Leeuw, Ilse; Van Borm, Steven; De Clercq, ...
Atypical Pathogenicity of Avian Influenza (H3N1) Virus Involved in Outbreak, Belgium, 2019
Publication Type: Peer reviewed scientific article Authors: Mieke Steensels; Gelaude, Philippe; Van Borm, Steven; Thierry van den Berg; Corrigan, Tim; Roupie, Virginie; Rauw, Fabienne; Lambrecht, ...
Complete Coding Sequence of a Lumpy Skin Disease Virus Strain Isolated during the 2016 Outbreak in Kazakhstan.
Sultanov, Akhmetzhan; Van Borm, Steven; De Clercq, Kris Source: Microbiol Resour Announc, Volume 9, Issue 4 (2020) Abstract: Lumpy skin disease virus (LSDV) causes an economically important disease in cattle. ...
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Venkatesh, YP and Vithayathil, PJ (1985) Influence of deamidation(s) in the 67-74 region of ribonuclease on its refolding. In: International Journal of Peptide & Protein Research, 25 (1). pp. 27-32.
Venkatesh, YP (1981) Microheterogeneity of Monodeamidated Ribonuclease-A (Ribonuclease-AA1). In: Indian Journal of Biochemistry & Biophysics, 18 (4). p. 126.
Venkatesh, YP and Vithayathil, PJ (1979) Deamidated derivatives of bovine pancreatic ribonuclease-a. In: Indian Journal of Biochemistry & Biophysics, 16 (1). p. 73.
This list was generated on Fri Dec 26 07:32:05 2014 IST.
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57
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Antoine Triller
Summary
Country: France
Publications
1. pmc The Neuronal Splicing Factor Nova Co-Localizes with Target RNAs in the Dendrite
Claudia Racca
Biologie Cellulaire de la Synapse Normale et Pathologique, Institut National de la Sante et de la Recherche Medicale, Ecole Normale Superieure Paris, France
Front Neural Circuits 4:5. 2010
2. pmc Cellular transport and membrane dynamics of the glycine receptor
Andrea Dumoulin
Biologie Cellulaire de la Synapse, Ecole Normale Superieure Paris, France
Front Mol Neurosci 2:28. 2009
3. doi request reprint New concepts in synaptic biology derived from single-molecule imaging
Antoine Triller
INSERM UR497, Ecole Normale Superieure, Biologie Cellulaire de la Synapse N and P, 46 rue d Ulm, 75005 Paris, France
Neuron 59:359-74. 2008
4. doi request reprint A common molecular basis for membrane docking and functional priming of synaptic vesicles
Lea Siksou
Ecole Normale Superieure, Biologie de la Synapse Normale et Pathologique, 46 rue d Ulm, 75005 Paris, France
Eur J Neurosci 30:49-56. 2009
5. ncbi request reprint Cytoskeleton regulation of glycine receptor number at synapses and diffusion in the plasma membrane
Cécile Charrier
Laboratoire de Biologie Cellulaire de la Synapse, Institut National de la Sante et de la Recherche Medicale, Unité 789, Ecole Normale Superieure, 75005 Paris, France
J Neurosci 26:8502-11. 2006
6. doi request reprint Gephyrin oligomerization controls GlyR mobility and synaptic clustering
Martino Calamai
INSERM U789 Biologie Cellulaire de Synapse and Département de Biologie, Ecole Normale Superieure, 75005 Paris, France
J Neurosci 29:7639-48. 2009
7. doi request reprint Activity-dependent tuning of inhibitory neurotransmission based on GABAAR diffusion dynamics
Hiroko Bannai
Biologie Cellulaire de la Synapse N and P, Ecole Normale Superieure Paris, INSERM U789, 46 Rue d Ulm 75005 Paris, France
Neuron 62:670-82. 2009
8. doi request reprint Quantitative nanoscopy of inhibitory synapses: counting gephyrin molecules and receptor binding sites
Christian G Specht
Biologie Cellulaire de la Synapse, Inserm U1024, Institute of Biology, Ecole Normale Supérieure ENS, 46 rue d Ulm, Paris 75005, France
Neuron 79:308-21. 2013
9. doi request reprint A crosstalk between β1 and β3 integrins controls glycine receptor and gephyrin trafficking at synapses
Cécile Charrier
Biologie Cellulaire de la Synapse, IBENS, Ecole Normale Superieure, Inserm U1024, CNRS UMR8197, Paris, France
Nat Neurosci 13:1388-95. 2010
10. ncbi request reprint Three-dimensional architecture of presynaptic terminal cytomatrix
Lea Siksou
INSERM U789, Ecole Normale Superieure, 75005 Paris, France
J Neurosci 27:6868-77. 2007
Collaborators
Detail Information
Publications61
1. pmc The Neuronal Splicing Factor Nova Co-Localizes with Target RNAs in the Dendrite
Claudia Racca
Biologie Cellulaire de la Synapse Normale et Pathologique, Institut National de la Sante et de la Recherche Medicale, Ecole Normale Superieure Paris, France
Front Neural Circuits 4:5. 2010
..These data demonstrate that HITS-CLIP can identify functional RNA localization elements, and they suggest new links between the regulation of nuclear RNA processing and mRNA localization...
2. pmc Cellular transport and membrane dynamics of the glycine receptor
Andrea Dumoulin
Biologie Cellulaire de la Synapse, Ecole Normale Superieure Paris, France
Front Mol Neurosci 2:28. 2009
....
3. doi request reprint New concepts in synaptic biology derived from single-molecule imaging
Antoine Triller
INSERM UR497, Ecole Normale Superieure, Biologie Cellulaire de la Synapse N and P, 46 rue d Ulm, 75005 Paris, France
Neuron 59:359-74. 2008
..In this primer, we will review the different approaches used to track single molecules in live neurons, compare them to bulk measurements, and discuss the different concepts that have emerged from their application to synaptic biology...
4. doi request reprint A common molecular basis for membrane docking and functional priming of synaptic vesicles
Lea Siksou
Ecole Normale Superieure, Biologie de la Synapse Normale et Pathologique, 46 rue d Ulm, 75005 Paris, France
Eur J Neurosci 30:49-56. 2009
..These results indicate that SV docking at the plasma membrane and functional priming are respective morphological and physiological manifestations of the same molecular process mediated by SNARE complexes and Munc13s...
5. ncbi request reprint Cytoskeleton regulation of glycine receptor number at synapses and diffusion in the plasma membrane
Cécile Charrier
Laboratoire de Biologie Cellulaire de la Synapse, Institut National de la Sante et de la Recherche Medicale, Unité 789, Ecole Normale Superieure, 75005 Paris, France
J Neurosci 26:8502-11. 2006
..Consequently, GlyR number at synapses may be rapidly modulated by the cytoskeleton through the regulation of lateral diffusion in the plasma membrane and of receptor stabilization at synapses...
6. doi request reprint Gephyrin oligomerization controls GlyR mobility and synaptic clustering
Martino Calamai
INSERM U789 Biologie Cellulaire de Synapse and Département de Biologie, Ecole Normale Superieure, 75005 Paris, France
J Neurosci 29:7639-48. 2009
..Since alterations in the oligomerization properties of gephyrin are related to the dynamics of GlyRs, the gephyrin splice variant ge(2,4,5) may be implicated in the modulation of synaptic strength...
7. doi request reprint Activity-dependent tuning of inhibitory neurotransmission based on GABAAR diffusion dynamics
Hiroko Bannai
Biologie Cellulaire de la Synapse N and P, Ecole Normale Superieure Paris, INSERM U789, 46 Rue d Ulm 75005 Paris, France
Neuron 62:670-82. 2009
..This transient activity-dependent reduction of inhibition would favor the onset of LTP during conditioning...
8. doi request reprint Quantitative nanoscopy of inhibitory synapses: counting gephyrin molecules and receptor binding sites
Christian G Specht
Biologie Cellulaire de la Synapse, Inserm U1024, Institute of Biology, Ecole Normale Supérieure ENS, 46 rue d Ulm, Paris 75005, France
Neuron 79:308-21. 2013
..The competition of glycine and GABAA receptor complexes for synaptic binding sites highlights the potential of single-molecule imaging to quantify synaptic plasticity on the nanoscopic scale. ..
9. doi request reprint A crosstalk between β1 and β3 integrins controls glycine receptor and gephyrin trafficking at synapses
Cécile Charrier
Biologie Cellulaire de la Synapse, IBENS, Ecole Normale Superieure, Inserm U1024, CNRS UMR8197, Paris, France
Nat Neurosci 13:1388-95. 2010
..This provides a mechanism for maintaining or adjusting the steady state of postsynaptic molecule exchanges and the level of glycinergic inhibition in response to neuron- and glia-derived signals or extracellular matrix remodeling...
10. ncbi request reprint Three-dimensional architecture of presynaptic terminal cytomatrix
Lea Siksou
INSERM U789, Ecole Normale Superieure, 75005 Paris, France
J Neurosci 27:6868-77. 2007
..This 3D analysis reveals the morphological constraints exerted by the presynaptic molecular scaffold. SVs are tightly interconnected in the axonal bouton, and this network is preferentially connected to the AZ...
11. doi request reprint Homeostatic regulation of synaptic GlyR numbers driven by lateral diffusion
Sabine Levi
Biologie Cellulaire de la Synapse, INSERM U789, Ecole Normale Superieure, 46 rue d Ulm, 75005 Paris, France
Neuron 59:261-73. 2008
..This provides a mechanism for a rapid homeostatic regulation of the inhibitory glycinergic component at mixed glycine-GABA synapses in response to increased NMDA excitatory transmission...
12. pmc Super-resolution dynamic imaging of dendritic spines using a low-affinity photoconvertible actin probe
Ignacio Izeddin
Laboratoire Kastler Brossel, CNRS UMR 8552, Department of Physics, Ecole Normale Superieure, Universite Pierre et Marie Curie Paris 6, Paris, France
PLoS ONE 6:e15611. 2011
....
13. ncbi request reprint Activity-dependent movements of postsynaptic scaffolds at inhibitory synapses
Cyril Hanus
Laboratoire de Biologie Cellulaire de la Synapses, Institut National de la Sante et de la Recherche Medicale, Ecole Normale Superieure, 75005 Paris, France
J Neurosci 26:4586-95. 2006
..Moreover, the action of the potassium channel blocker 4-aminopyridine and receptor antagonists indicate that the dynamics of postsynaptic gephyrin scaffolds are controlled by synaptic activity...
14. pmc Data in support of the identification of neuronal and astrocyte proteins interacting with extracellularly applied oligomeric and fibrillar α-synuclein assemblies by mass spectrometry
Amulya Nidhi Shrivastava
Ecole Normale Superieure, Institut de Biologie de l ENS IBENS, INSERM, CNRS, PSL Research University, 46 rue d Ulm, Paris 75005, France
Data Brief 7:221-8. 2016
..6019/pxd002256 to 10.6019/pxd002263. ..
15. pmc Multiple association states between glycine receptors and gephyrin identified by SPT analysis
Marie Virginie Ehrensperger
Laboratoire Kastler Brossel, Centre National de la Recherche Scientifique UMR8552, Ecole Normale Superieure, Universite Pierre et Marie Curie Paris 6, 75005 Paris, France
Biophys J 92:3706-18. 2007
..Within clusters, we identified two subpopulations of GlyR with distinct degrees of stabilization between receptors and scaffolding proteins...
16. pmc The residence time of GABA(A)Rs at inhibitory synapses is determined by direct binding of the receptor α1 subunit to gephyrin
Jayanta Mukherjee
Department of Neuroscience, Tufts University School of Medicine, Boston, Massachusetts 02111, Ecole Normale Superieure, Inserm U1024, 75230 Paris Cedex 05, France
J Neurosci 31:14677-87. 2011
....
17. pmc Regulation of glycine receptor diffusion properties and gephyrin interactions by protein kinase C
Christian G Specht
Biologie Cellulaire de la Synapse, Institut de Biologie de l Ecole Normale Supérieure, INSERM U, Paris, France
EMBO J 30:3842-53. 2011
..We propose that the regulation of GlyR dynamics by PKC thus contributes to the plasticity of inhibitory synapses and may be involved in maladaptive forms of synaptic plasticity...
18. doi request reprint The dynamics of synaptic scaffolds
Christian G Specht
INSERM U789, Biologie Cellulaire de la Synapse, Ecole Normale Supérieure ENS, Paris, France
Bioessays 30:1062-74. 2008
..Here, we review the dynamics of the synaptic scaffold and of adaptor proteins in relation to their roles in the organisation of the synapse as well as in the clustering and trafficking of receptor proteins...
19. doi request reprint Molecular dynamics of postsynaptic receptors and scaffold proteins
Marianne Renner
INSERM U789, Biologie Cellulaire de la Synapse, ENS, Paris, France
Curr Opin Neurobiol 18:532-40. 2008
....
20. ncbi request reprint Target-dependent use of co-released inhibitory transmitters at central synapses
Guillaume P Dugué
Laboratoire de Neurobiologie Moléculaire et Cellulaire, Centre National de la Recherche Scientifique, Unite Mixte de Recherche 8544, Ecole Normale Superieure, 75005 Paris, France
J Neurosci 25:6490-8. 2005
..Thus, postsynaptic selection of coreleased fast transmitters is used in the CNS to increase the diversity of individual neuronal outputs and achieve target-specific signaling in mixed inhibitory networks...
21. ncbi request reprint Analysis of synaptic ultrastructure without fixative using high-pressure freezing and tomography
Philippe Rostaing
INSERM U789, Ecole Normale Superieure, 46 rue d Ulm, 75005 Paris, France
Eur J Neurosci 24:3463-74. 2006
..Particularly, filamentous projections were observed linking the PSD to the actin cytoskeleton. Thus, synaptic ultrastructure can be analysed under more realistic conditions following HPF...
22. ncbi request reprint Regulation of gephyrin assembly and glycine receptor synaptic stability
Cecile Bedet
INSERM U789, the Laboratoire de Biologie Cellulaire de la Synapse, Ecole Normale Superieure, F 75005, Paris, France
J Biol Chem 281:30046-56. 2006
..These data suggest that the relative expression level of cellular variants influence the overall oligomerization pattern of gephyrin and thus the turnover of synaptic GlyR...
23. pmc Asymmetric redistribution of GABA receptors during GABA gradient sensing by nerve growth cones analyzed by single quantum dot imaging
Cedric Bouzigues
Laboratoire Kastler Brossel, Centre National de la Recherche Scientifique, Physics Department, Ecole Normale Superieure, and Université Pierre et Marie Curie Paris 6, 24, rue Lhomond, 75005 Paris, France
Proc Natl Acad Sci U S A 104:11251-6. 2007
..Altogether, our results reveal a microtubule-dependent polarized reorganization of chemoreceptors at the cell surface and suggest that this polarization serves as an amplification step in GABA gradient sensing by nerve GCs...
24. doi request reprint Adaptive and non-adaptive changes in activity-deprived presynaptic terminals
Süzel Horellou
Institute of Biology of the Ecole Normale Supérieure, 46 rue d Ulm, 75005, Paris, France INSERM U1024, Paris, France CNRS UMR8197, Paris, France
Eur J Neurosci 39:61-71. 2014
..The modification of the distribution, but not the amount, of RIM1/2 may explain the contradiction between the morphological and electrophysiological findings...
25. doi request reprint Syntaxin1A lateral diffusion reveals transient and local SNARE interactions
Claire Ribrault
Biologie Cellulaire de la Synapse, Institut de Biologie de l Ecole Normale Supérieure, Institut National de la Santé et de la Recherche Médicale Unité 1024 CNRS 8197, F 75005 Paris, France
J Neurosci 31:17590-602. 2011
..This work allows us to describe the diffusive behavior and kinetics of interactions between syntaxin1A and its partners that lead to its transient stabilization at the synapse...
26. ncbi request reprint Intracellular association of glycine receptor with gephyrin increases its plasma membrane accumulation rate
Cyril Hanus
Laboratoire de Biologie Cellulaire de la Synapse Normale et Pathologique, Institut National de la Sante et de la Recherche Medicale, Ecole Normale Superieure, 75005 Paris, France
J Neurosci 24:1119-28. 2004
..Therefore, our data strongly suggest that some GlyR clusters are associated with gephyrin on their way to the cell surface and that this association increases the accumulation of GlyR at the plasma membrane...
27. ncbi request reprint Imaging the lateral diffusion of membrane molecules with quantum dots
Hiroko Bannai
INSERM U789, Biologie Cellulaire de la Synapse N and P, Ecole Normale Superieure Paris, 46, rue d Ulm 75005 Paris, France
Nat Protoc 1:2628-34. 2006
..The experimental procedure described for neurons below takes about 45 min. This technique is applicable to various cultured cells...
28. ncbi request reprint Surface trafficking of receptors between synaptic and extrasynaptic membranes: and yet they do move!
Antoine Triller
INSERM UR497, Ecole Normale Superieure, 46 rue d Ulm, Paris F75005, France
Trends Neurosci 28:133-9. 2005
..This review is part of the TINS Synaptic Connectivity series...
29. doi request reprint Control of the postsynaptic membrane viscosity
Marianne Renner
Institut National de la Sante et de la Recherche Medicale, Biologie Cellulaire de la Synapse, 75005 Paris, France
J Neurosci 29:2926-37. 2009
..Therefore, lipid composition and actin-dependent protein compaction regulate viscosity of the PSM and, consequently, the molecular flow in and out of synapses...
30. ncbi request reprint The development of hippocampal interneurons in rodents
Lydia Danglot
Laboratoire de Biologie de la Synapse Normale et Pathologique, Unité Inserm U789, Ecole Normale Superieure, 46 rue d Ulm, 75005 Paris, France
Hippocampus 16:1032-60. 2006
..We will finally review potential mechanisms underlying the development of GABAergic interneurons...
31. doi request reprint Differential control of thrombospondin over synaptic glycine and AMPA receptors in spinal cord neurons
Laetitia Hennekinne
Ecole Normale Superieure, Institut de Biologie de l ENS, IBENS, Paris, France
J Neurosci 33:11432-9. 2013
..These results suggest a role of TSP-1 in controlling the balance between excitation and inhibition which could help the recovery of normal synaptic activity after injury responses. ..
32. ncbi request reprint Morphologically identified glycinergic synapses in the hippocampus
Lydia Danglot
Laboratoire de Biologie Cellulaire de la Synapse N and P, Institut National de la Santé et de la Recherche Médicale U497, Ecole Normale Superieure, 75005 Paris, France
Mol Cell Neurosci 27:394-403. 2004
..Finally, GlyR clusters could be detected at synaptic sites with the GABAA receptor gamma2 subunit and gephyrin, suggesting that mixed GABA/glycine synapses might exist in the hippocampus...
33. ncbi request reprint Single quantum dot tracking of membrane receptors
Cedric Bouzigues
Laboratoire Kastler Brossel, Physics Department, Ecole Normale Superieure, Paris, France
Methods Mol Biol 374:81-91. 2007
..Single QD tracking is nevertheless a general method, suitable to study many transmembrane proteins...
34. doi request reprint Ultrastructural organization of presynaptic terminals
Lea Siksou
Institute of Biology of the Ecole Normale Supérieure, 46 rue d Ulm, 75005 Paris, France
Curr Opin Neurobiol 21:261-8. 2011
....
35. pmc Bidirectional Control of Synaptic GABAAR Clustering by Glutamate and Calcium
Hiroko Bannai
Laboratory for Developmental Neurobiology, RIKEN Brain Science Institute BSI, 2 1 Hirosawa, Wako, Saitama 351 0198, Japan Division of Biological Science, Graduate School of Science, Nagoya University, Furo cho, Chikusa, Nagoya 464 8602, Japan Nagoya Research Center for Brain and Neural Circuits, Graduate School of Science, Nagoya University, Furo cho, Chikusa, Nagoya 464 8602, Japan Ecole Normale Supérieure, Institut de Biologie de l ENS IBENS, INSERM, CNRS, Ecole Normale Superieure, PSL Research University, 46 rue d Ulm, 75005 Paris, France
Cell Rep 13:2768-80. 2015
..These findings show that glutamate activates distinct receptors and spatiotemporal patterns of calcium signaling for opposing control of GABAergic synapses. ..
36. doi request reprint β-amyloid and ATP-induced diffusional trapping of astrocyte and neuronal metabotropic glutamate type-5 receptors
Amulya Nidhi Shrivastava
Biologie Cellulaire de la Synapse, Institut de Biologie de l Ecole Normale Supérieure, INSERM U1024 CNRS 8197, Paris 75005, France
Glia 61:1673-86. 2013
..Thus, Aβ oligomer- and mGluR5-dependent ATP release by astrocytes may contribute to the overall deleterious effect of mGluR5s in Alzheimer's disease. GLIA 2013;61:1673-1686. ..
37. doi request reprint Single-particle tracking methods for the study of membrane receptors dynamics
Damien Alcor
Biologie Cellulaire de la Synapse, INSERM U789, Ecole Normale Superieure, Paris, France
Eur J Neurosci 30:987-97. 2009
..Constraints, limitations and future developments are discussed...
38. pmc The Role of Synaptopodin in Membrane Protein Diffusion in the Dendritic Spine Neck
Lili Wang
Biologie Cellulaire de la Synapse, Inserm U1024, CNRS 8197, Institute of Biology, Ecole Normale Supérieure ENS, Paris, France
PLoS ONE 11:e0148310. 2016
..Our data complement models that consider the impact of the spine neck as a function of its shape, by showing that the internal organisation of the neck imposes additional physical barriers to membrane protein diffusion. ..
39. ncbi request reprint Impaired synaptic function in the microglial KARAP/DAP12-deficient mouse
Anne Roumier
Laboratoire de Biologie Cellulaire de la Synapse Normale et Pathologique, Institut National de la Santé et de la Recherche Médicale INSERM U497, Ecole Normale Superieure, 75230 Paris Cedex 05, France
J Neurosci 24:11421-8. 2004
..KARAP/DAP12 may thus alter microglial physiology and subsequently synaptic function and plasticity through a novel microglia-neuron interaction...
40. ncbi request reprint Synaptic structure and diffusion dynamics of synaptic receptors
Antoine Triller
Biologie Cellulaire de la Synapse N and P, INSERM U497, Ecole Normale Superieure, Paris, France
Biol Cell 95:465-76. 2003
....
41. pmc α-synuclein assemblies sequester neuronal α3-Na+/K+-ATPase and impair Na+ gradient
Amulya Nidhi Shrivastava
Ecole Normale Superieure, Institut de Biologie de l ENS IBENS INSERM CNRS PSL Research University, Paris, France
EMBO J 34:2408-23. 2015
..Thus, interactions of α3-NKA with extracellular α-syn assemblies reduce its pumping activity as its mutations in RDP/AHC...
42. doi request reprint The Susd2 protein regulates neurite growth and excitatory synaptic density in hippocampal cultures
Yann Nadjar
Ecole Normale Superieure, IBENS, Inserm U1024, 75005 Paris, France
Mol Cell Neurosci 65:82-91. 2015
..Our results demonstrate a dual role for Susd2 at different developmental stages, and raise the question whether Susd2 and other CCP-containing proteins expressed in the CNS could be function-related. ..
43. ncbi request reprint Preservation of immunoreactivity and fine structure of adult C. elegans tissues using high-pressure freezing
Philippe Rostaing
Biologie Cellulaire de la Synapse, Ecole Normale Superieure, Paris, France
J Histochem Cytochem 52:1-12. 2004
..elegans tissues by using postembedding immunogold labeling...
44. doi request reprint Synaptic stability and plasticity in a floating world
Kimberly Gerrow
Biologie Cellulaire de la Synapse, Institute de Biologie de l Ecole Normale Supérieure, 46 rue d Ulm, 75005 Paris, France
Curr Opin Neurobiol 20:631-9. 2010
..We will briefly review here recent data on this mechanism, which ultimately tunes the number of receptors at synapses and therefore synaptic strength...
45. ncbi request reprint Diffusion dynamics of glycine receptors revealed by single-quantum dot tracking
Maxime Dahan
Laboratoire Kastler Brossel, CNRS UMR 8552, Ecole Normale Supérieure and Université Pierre et Marie Curie, 24 rue Lhomond, 75005 Paris, France
Science 302:442-5. 2003
..The entry of GlyRs into the synapse by diffusion was observed and further confirmed by electron microscopy imaging of QD-tagged receptors...
46. ncbi request reprint Differentiation-dependent sensitivity to apoptogenic factors in PC12 cells
Sheela Vyas
INSERM U497, Ecole Normale Superieure, 46, rue d Ulm, Paris 75005, France
J Biol Chem 279:30983-93. 2004
....
47. ncbi request reprint Diffusion trajectory of an asymmetric object: information overlooked by the mean square displacement
Claire Ribrault
INSERM, U789, Biologie Cellulaire de la Synapse N and P, Paris, France
Phys Rev E Stat Nonlin Soft Matter Phys 75:021112. 2007
..Here we present a theoretical basis for the analysis of the trajectories of a single particle with anisotropic diffusion coefficients. We discuss the relevance of this method for motion of biomolecules in the membrane of living cells...
48. doi request reprint Synaptic receptor dynamics: from theoretical concepts to deep quantification and chemistry in cellulo
Charlotte Salvatico
Ecole Normale Superieure, Institut de Biologie de l ENS IBENS, Inserm U1024, CNRS 8197, Biologie Cellulaire de la Synapse, 46 rue d Ulm, Paris 75005, France
Neuropharmacology 88:2-9. 2015
..This deep quantification of synapses provides access to the chemical determinants that regulate the numbers of receptors and hence the function of synapses at a mechanistic level...
49. ncbi request reprint Herpes simplex virus type 1 glycoprotein B sorting in hippocampal neurons
Corinne Potel
Laboratoire de Virologie, UPRES EA 3622, Faculté de Médecine Cochin, Universite Paris V, bâtiment Gustave Roussy, porte 636, 27 rue du Faubourg Saint Jacques, 75014 Paris, France
J Gen Virol 84:2613-24. 2003
..These results suggest that the cytoplasmic tail of gB plays a role in maturation and transport and subsequently in axonal sorting in differentiated hippocampal neurons...
50. pmc Docosahexaenoic acid protects from dendritic pathology in an Alzheimer's disease mouse model
Frederic Calon
Department of Medicine, University of California, Los Angeles, 90095, USA
Neuron 43:633-45. 2004
..Since n-3 PFAs are essential for p85-mediated CNS insulin signaling and selective protection of postsynaptic proteins, these findings have implications for neurodegenerative diseases where synaptic loss is critical, especially AD...
51. ncbi request reprint Tumor necrosis factor-alpha and neuronal development
Alain Bessis
Laboratoire de Biologie Cellulaire de la Synapse Normale et Pathologique, INSERM U497 Ecole Normale Supérieure, Paris, France
Neuroscientist 11:277-81. 2005
..TNFalpha is also likely to induce immediate and delayed prodeath effects in adult and pathological tissues. Data obtained in embryonic systems will thus help to develop new therapeutic approaches to pathological neuronal death in adults...
52. ncbi request reprint Gephyrin interacts with Dynein light chains 1 and 2, components of motor protein complexes
Jens C Fuhrmann
Max Planck Institute for Brain Research, Department of Neurochemistry, D 60528 Frankfurt Main, Germany
J Neurosci 22:5393-402. 2002
..Because Dlc-1 and Dlc-2 have been described as stoichiometric components of cytoplasmic dynein and myosin-Va complexes, our results suggest that motor proteins are involved in the subcellular localization of gephyrin...
53. pmc Modeling synaptic dynamics driven by receptor lateral diffusion
David Holcman
Department of Mathematics, Weizmann Institute of Science, Rehovot, Israel
Biophys J 91:2405-15. 2006
....
54. ncbi request reprint Otoferlin, defective in a human deafness form, is essential for exocytosis at the auditory ribbon synapse
Isabelle Roux
Inserm UMRS587, Unité de Génétique des Déficits Sensoriels, College de France, Institut Pasteur, 25 rue du Dr Roux, 75015 Paris, France
Cell 127:277-89. 2006
..Thus, otoferlin is essential for a late step of synaptic vesicle exocytosis and may act as the major Ca(2+) sensor triggering membrane fusion at the IHC ribbon synapse...
55. ncbi request reprint Activation of presynaptic GABA(A) receptors induces glutamate release from parallel fiber synapses
Brandon M Stell
Laboratoire de Physiologie Cérébrale, Unité de Formation et de Recherche Biomédicale, Universite Paris Descartes, 75006 Paris, France
J Neurosci 27:9022-31. 2007
..From these data, we conclude that GABA(A)Rs located on parallel fibers depolarize parallel fiber terminals beyond the threshold for Na+ channel activation and thereby induce glutamate release onto MLIs and Purkinje cells...
56. pmc Potentiation of electrical and chemical synaptic transmission mediated by endocannabinoids
Roger Cachope
Dominick P Purpura Department of Neuroscience, Albert Einstein College of Medicine, Bronx, NY 10461, USA
Neuron 56:1034-47. 2007
..Similar interactions between endocannabinoid and dopaminergic systems may be widespread and potentially relevant for the motor and rewarding effects of cannabis derivatives...
57. doi request reprint Despite GABAergic neurotransmission, GABAergic innervation does not compensate for the defect in glycine receptor postsynaptic aggregation in spastic mice
Emilie Muller
UMR 7102 Neurobiologie des Processus Adaptatifs, Universite Pierre et Marie Curie, Bat B, Case 1, 9 quai Saint Bernard, 75252 Paris Cedex 05, France
Eur J Neurosci 27:2529-41. 2008
..They also indicate that GABAergic neurotransmission does not compensate for defects in GlyR postsynaptic aggregation leading to spastic syndrome in C57BL/6J SPA mice...
58. doi request reprint Developmental neuronal death in hippocampus requires the microglial CD11b integrin and DAP12 immunoreceptor
Shirley Wakselman
Laboratoire de Biologie Cellulaire de la Synapse, Institut National de Santé et de Recherche Médicale, Unité 789, 75230 Paris Cedex 05, France
J Neurosci 28:8138-43. 2008
..Thus, our data show that the process of developmental neuronal death triggered by microglia is similar to the elimination of pathogenic cells by the innate immune cells...
59. pmc Prenatal activation of microglia induces delayed impairment of glutamatergic synaptic function
Anne Roumier
INSERM, U789, Laboratoire de Biologie Cellulaire de la Synapse, Paris, France
PLoS ONE 3:e2595. 2008
..Synaptic dysfunctions may be at the origin of cognitive impairments, however the link between prenatal inflammation and synaptic defects remains to be established...
60. ncbi request reprint Lysosomal amino acid transporter LYAAT-1 in the rat central nervous system: an in situ hybridization and immunohistochemical study
Cendra Agulhon
Institut National de la Santé et de la Recherche Médicale INSERM U513, CHU Henri Mondor, 94000 Creteil, France
J Comp Neurol 462:71-89. 2003
..Furthermore, its cell expression pattern suggests that it may contribute to specialized cellular function in the rat CNS such as neuronal metabolism, neurotransmission, and control of brain amino acid homeostasis...
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specificity in protein-nucleic acid interaction - involvement of nucleic-acids in non-enzymatic peptide condensation
Basu, HS and Podder, SK (1981) specificity in protein-nucleic acid interaction - involvement of nucleic-acids in non-enzymatic peptide condensation. In: Indian Journal of Biochemistry & Biophysics, 18 (4). pp. 251-253.
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Official URL: http://imsear.hellis.org/handle/123456789/26955
Item Type: Journal Article
Additional Information: Copyright of this article belongs to National Institute of Science Communication and Information Resources.
Department/Centre: Division of Biological Sciences > Biochemistry
Depositing User: Ms V Mangala
Date Deposited: 17 Feb 2012 05:53
Last Modified: 17 Feb 2012 05:53
URI: http://eprints.iisc.ac.in/id/eprint/43274
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EP3080605B1 - Method for labeling dna fragments to reconstruct physical linkage and phase - Google Patents
Method for labeling dna fragments to reconstruct physical linkage and phase Download PDF
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Publication number
EP3080605B1
EP3080605B1 EP14870464.6A EP14870464A EP3080605B1 EP 3080605 B1 EP3080605 B1 EP 3080605B1 EP 14870464 A EP14870464 A EP 14870464A EP 3080605 B1 EP3080605 B1 EP 3080605B1
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dna
sequence
nucleic acid
cases
polynucleotide
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German (de)
French (fr)
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EP3080605A4 (en
EP3080605A1 (en
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Daniel ROKHSAR
Richard E. Green
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University of California
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University of California
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Flexible protein annotation with sequence- and secondary structure information
Bannert C (2008)
Bielefeld (Germany): Bielefeld University.
Bielefelder E-Dissertation | Englisch
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Autor*in
Bannert, Constantin
Betreuer*in
Stoye, JensUniBi ; Koch, Ina
Abstract / Bemerkung
Eine Standardproblem der Sequenzanalyse in der Bioinformatik ist die Verwandtschaftssuche, bei der eine Datenbank nach verwandten Genen zu einer Anfragesequenz durchsucht wird. Obwohl es hierfür bereits verschiedene Ansätze gibt, ist noch Raum für Erweiterungen vorhanden. Eine Möglichkeit ist es, die Information in den Quelldaten besser auszunutzen. Eine andere Möglichkeit ist die Erweiterung entsprechender Software durch neue Optionen. Der "Jumping Alignment" Algorithmus (Jali) ist eine Methode zur Datenbanksuche. Er arbeitet auf multiplen Sequenzalignments. Im Gegensatz zu älteren Methoden kann Jali die Information in den Zeilen und den Spalten des multiplen Alignments verwenden. Erste Evaluierungen von Jali waren vielversprechend. Wir evaluieren Jali nochmals mit anderen Daten. Wir analysieren einige "Jumping alignments" mit integrierter Sekundärstrukturinformation und untersuchen, ob der Algorithmus in der Lage ist, die Sekundärstruktur zu berücksichtigen. Wir zeigen eines der seltenen Beispiele, wo dies der Fall ist. In einem zweiten Experiment simulieren wir die Evolution von zehn künstlich erzeugten Proteinfamilien und testen Jali damit. Unsere Ergebnisse zeigen, dass Jali durch seine Sprungfähigkeit an Flexibilität bei der Verwandtschaftssuche gewinnt; besonders dann, wenn die zu Grunde liegenden multiplen Alignments suboptimal sind. Viele Alignment-basierte Methoden zur Verwandtschaftssuche haben bestimmte Beschränkungen. Sie sind nicht darauf ausgelegt, mit Duplikationen oder Umordnungen in den Eingangssequenzen umzugehen. Außerdem ist deren Ausgabe oft nur eine wenig informative Liste mit numerischen Bewertungen der einzelnen Alignments. Wir entwickeln eine neue Methode "Passta", die diese Einschränkungen umgeht. Die erste Phase des Protokolls dient als Filter, der Datenbank-Targets ausfiltern soll, die nicht mit der Anfragesequenz verwandt sind. Die Kandidatenmenge wird dann an die Phase Zwei weitergegeben, die die eigentliche Annotation der Anfragesequenz mit Alignments von Sekundärstrukturelementen (SSEs) durchführt. Diese Alignments werden als Knoten in einem Graph repräsentiert, der optimale Pfad entspricht prinzipiell einer Auswahl der besten Alignments im Graph. Bevor wir Passta evaluieren, trainieren wir einige Parameter der Methode und besprechen interessante Ergebnisse. Wir kalibrieren ausserdem einen wichtigen Parameter der Methode und zeigen dabei identifizierte SCOP-Familien mit Duplikationen oder Umordnungen. Das letzte Kapitel enthält eine Evaluierung von Passta mit Jali und BLAST. Leider zeigen die Ergebnisse, dass die erste Phase von Passta nicht besonders effizient arbeitet. Der Hauptgrund ist, dass die verwendeten Sekundärstrukturalignments oft kurz und dann unspezifisch sind. Wir können aber auch das Potenzial von Phase Zwei zeigen: Wenn wir alle verwandten Sequenzen der Kandidatenmenge hinzufügen, die von Phase Eins verworfen wurden, so ist Phase Zwei in der Lage, mit etablierten Methoden wie Jali und BLAST zu konkurrieren.
The number of known gene sequences is still rising at an increasing pace. A standard task in sequence analysis is homology recognition, where a database is searched for homologous sequences. Even though already several software tools for homology recognition exist, there is still room for improvement. One possibility is to use more of the information in the source data. Another possibility is to add new features to support research on specific questions. The Jumping Alignment algorithm (Jali) is a method for database searching. It works on multiple sequence alignments. In contrast to previous approaches, Jali is able to consider the information in the rows and the columns of a multiple alignment. Initial evaluations of Jali showed promising results. We evaluate Jali once more to see if the good results can be reproduced and investigate the reason. We analyze a set of jumping alignments with underlying secondary structure information for cases of "structural significance", where Jali seems to recognize the secondary structure in the alignment. Even though we found a few examples, these cases are rare. In a second experiment, we simulate the evolution of ten protein superfamilies and evaluate Jali on these families. The findings suggest that jumping offers Jali more flexibility in homology recognition, especially in conjunction with suboptimal alignments. Many alignment-based approaches in homology recognition share certain limitations. They are not well suited to cope with duplications or rearrangements in the input sequences. In addition, their output is usually a list of scores that is not very informative. We develop a new method "Passta" that circumvents these limitations. The first stage of the protocol (Pass One) serves as filter. Pass One tries to find a set of targets that are related to a given query. This candidate set is then submitted to Pass Two, where the query is annotated with alignments of Secondary Structure Elements (SSEs). In a graph-based approach, we select those alignments that reproduce the query in an optimal way. Prior to a systematic evaluation of Passta, we train some of its parameters and discover interesting differences in the behavior of the three SSE classes coil, helix, and strand. We also calibrate the rearrangement cost parameter of Pass Two and use our method to find SCOP families with rearrangements or duplications, with nice results. Finally, we present a comparative evaluation of Passta with Jali and BLAST. Unfortunately the results show that Pass One is not working very well. The main reason is that SSEs are short sequence fragments and alignments with SSEs are often unspecific. We are however able to show the potential of Pass Two: When we add the true positive targets missed by Pass One, Pass Two is able to compete with Jali and BLAST.
Stichworte
Proteine , Sekundärstruktur , Annotation , Sequenzanalyse (Chemie) , Alignment (Biochemie) , Datenbank , Passta , Jumping Alignment Algorithmus (Jali) , Proteinfamilie , Sekundärstrukturelemente (SSE) , SCOP , Jumping alignment
Jahr
2008
Page URI
https://pub.uni-bielefeld.de/record/2305571
Zitieren
Bannert C. Flexible protein annotation with sequence- and secondary structure information. Bielefeld (Germany): Bielefeld University; 2008.
Bannert, C. (2008). Flexible protein annotation with sequence- and secondary structure information. Bielefeld (Germany): Bielefeld University.
Bannert, C. (2008). Flexible protein annotation with sequence- and secondary structure information. Bielefeld (Germany): Bielefeld University.
Bannert, C., 2008. Flexible protein annotation with sequence- and secondary structure information, Bielefeld (Germany): Bielefeld University.
C. Bannert, Flexible protein annotation with sequence- and secondary structure information, Bielefeld (Germany): Bielefeld University, 2008.
Bannert, C.: Flexible protein annotation with sequence- and secondary structure information. Bielefeld University, Bielefeld (Germany) (2008).
Bannert, Constantin. Flexible protein annotation with sequence- and secondary structure information. Bielefeld (Germany): Bielefeld University, 2008.
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Home Page / Applications / Applications Detail
In Vitro Cell Transfection Reagent Product Selection Guide
Cell transfection reagents have become routine reagents for studying and controlling gene function in eukaryotic cells. Transfection reagents are widely used in gene function research, gene expression regulation, and mutation analysis, as well as gene therapy, cell therapy, protein production, and vaccine production. So what is transfection? And how to choose a kind of transfection reagent based on your experiments?
What are the types of transfection?
The features of transfection reagents from Yeasen
How to choose a kind of transfection reagent based on your experiments?
Application case
Reference for transfection conditions
FAQs
Regard Reading
What are the types of transfection?
According to whether the nucleic acid is integrated into the host cell chromosome after transfection, it is divided into "transient" (transient transfection) and "stable" (stable transfection). The transfection efficiency, cytotoxicity, effects on normal physiology, and gene expression levels of different transfection methods are different. The principles, applications, and characteristics are compared in the following table:
Table 1 Comparison of different transfection methods
Technology
Principles
Advantages
Disadvantages
Chemical transfection method
Cationic liposomes
Positively charged liposomes form complexes with negatively charged phosphate groups of nucleic acids and are endocytosed by cells.
• Quick and easy operation
• Results are reproducible
• High transfection efficiency
• Transfectable DNA, RNA, and protein
• Suitable for the production of transient and stable proteins
• Can be used for in vivo transfection
• Requires optimization of conditions (some cell lines are sensitive to cationic liposomes)
• Some cell lines are not easily transfected
• The presence of serum interferes with complex formation, resulting in low transfection efficiency
• Depletion of serum in the medium increases cytotoxicity
Calcium Phosphate Coprecipitation
Calcium phosphate DNA complexes adsorb to cell membranes and are endocytosed by cells
• Cheap and easy to obtain
• Suitable for the production of transient and stable proteins
• High transfection efficiency (not limited to cell lines)
• Requires careful reagent preparation – CaPO4 solutions are sensitive to changes in pH, temperature, and buffer salt concentration
• poor repeatability
• Cytotoxic, especially against primary cells
• RPMI medium cannot be used due to its high concentration of phosphate
• Not suitable for transfection in animals.
Dextran
The complex formed by the interaction of the positively charged DEAE-dextran and the negatively charged phosphate backbone of the nucleic acid is endocytosed by the cell.
• Easy to use
• Results are reproducible
• Cheap
• Chemically toxic to certain cells
• For transient transfection only
• Low transfection efficiency, especially in primary cells.
Other cationic polymers
The positively charged polymer forms a positively charged complex with the negatively charged phosphate group of the nucleic acid, then interacts with the negatively charged proteoglycan on the cell surface, and enters the cell through endocytosis.
• Stable in serum, insensitive to temperature
• High transfection efficiency (limited cell lines)
• Results are reproducible
• Toxic to some cells
• Not biodegradable (dendrimer)
• Mostly used for transient transfection, less used for stable transfection
Biotransfection method
Viral transfection
Instinct infects cells and delivers genetic material
• High transfection efficiency
• For difficult-to-transfect cell lines
• Can be used for in vivo transfection
• Can be used to construct stable or transient expression cell lines
• Transfected cell lines must contain viral receptors
• Gene insertion size is limited (~10 kb for viral vectors, ~100 kb for non-viral vectors)
• Technically difficult and time-consuming to construct recombinant proteins
• There are biosafety issues (activation of underlying disease, immunogenic response, cytotoxicity, insertional mutagenesis, malignant transformation of cells)
Physical transfection method
Electric transfer
The high pulse voltage disrupts the cell membrane potential, and the DNA is introduced through the pores formed in the membrane.
• The principle is simple
• Optimized conditions to produce reproducible results
• no carrier required
• Unlimited cell types and conditions
• Optimized conditions for rapid transfection of large numbers of cells
• Special equipment required
• Electro-to-pulse and voltage parameters need to be optimized
• Great damage to cells
• The cell death rate is high and therefore requires a large number of cells
• Irreversibly damages cell membranes, lysing cells
Biotransmission Particle Delivery (Particle Bombardment)
The DNA is precipitated with microscopic heavy metal particles, and then the coated particles are projected into the cells with a ballistic device, and the DNA is gradually released and expressed in the cells.
• Unlimited cell types and conditions
• Can be used for transfection in animals
• Direct method and reliable results
• Unlimited size and number of imported genes
• Requires expensive equipment
• physical damage to the sample
• The cell death rate is high and therefore requires a large number of cells
• Need to prepare particles
• Relatively low transfection efficiency
• Expensive for research applications
Microinjection
Micromanipulation is used to inject DNA directly into the nucleus of the target cell.
• Unlimited cell types and conditions
• single cell transfection
• Direct method and reliable results
• Unlimited size and number of imported genes
• No carrier required
• Requires expensive equipment
• Technically demanding and labor-intensive (only one cell can be transfected at a time)
• A limited number of transfected cells
• Often causes cell death
The features of transfection reagents from Yeasen
For DNA transfection reagents and RNA transfection reagents, Yeasen Biotechnology has a strong R&D and production team, continuously optimizes formulas, improves production processes, and has launched a variety of products based on cationic liposomes and cationic polymers. Scientific research institutions and enterprises provide a full range of products, and the product line covers all fields involved in transfection reagents.
Hieff Trans™ Liposomal Transfection Reagent
Hieff Trans™ Suspension Cell-Free Liposomal Transfection Reagent
40802ES
40805ES
Hieff Trans™ in vitro siRNA/miRNA Transfection Reagent
Polyethylenimine Linear(PEI) MW40000（rapid lysis）
40806ES
40816ES
• High efficiency: suitable for transient transfection or stable transfection of cell lines.
• Low toxicity: Transfected cells remain well-viable.
• Wide adaptability: comprehensive coverage of common cells and difficult-to-transfect primary cells.
• Easy to operate: suitable for medium in the presence of serum, without changing the medium before and after transfection.
• Cost-effective: economical and practical, high transfection efficiency, low price.
How to choose a kind of transfection reagent based on your experiments?
The selection of transfection reagents needs to be selected according to the different experimental purposes and experimental contents, such as the transfected substances, specific cells, convenience of operation and other factors.
Product
Hieff Trans™ Liposomal Transfection Reagent
Hieff Trans™ Suspension Cell-Free Liposomal Transfection Reagent
Hieff Trans™ in vitro siRNA/miRNA Transfection Reagent
Polyethylenimine Linear(PEI) MW40000（rapid lysis）
Cell type
conventional cell
conventional cell
conventional cell
conventional cell
/
/
difficult-to-transfect cells
difficult-to-transfect cells
Nucleic acid type
DNA
DNA
/
DNA
siRNA
siRNA
siRNA
/
/
/
miRNA
/
/
/
mimic miRNA
/
/
/
antimiRNA
/
DNA/siRNA co-transfection
DNA/siRNA co-transfection
/
/
virus packaging
virus packaging
/
virus packaging
Application case
Hieff Trans™ Liposomal Transfection Reagent
Hieff Trans™ is supplied in sterile liquid form. Generally, for 24-well plate transfection, about 1.5 μL each time, 1 mL of Hieff Trans™ can do about 660 transfections; for 6-well plate, about 6 μL each time, 1 mL of Hieff Trans™ can do about 660 transfections. 160 transfections;
For more details, please see Confidence in transfection with Hieff Trans™ Lipofectamine Reagent
Polyethylenimine Linear (PEI) MW40000 (rapid lysis)
PEI 40000 is a highly charged cationic polymer with a molecular weight of 40,000 that binds negatively charged nucleic acid molecules very easily, forming a complex and allowing the complex to enter cells. PEI 40000 is a transient transfection reagent with low cytotoxicity, high transfection efficiency, and high gene expression efficiency in cells such as HEK293 and CHO. Linear PEI transfection reagents have been validated for a wide range of cell lines including HEK-293, HEK293T, CHO-K1, COS-1, COS-7, NIH/3T3, Sf9, HepG2, and Hela cells. The transfection efficiency is as high as 80%~90%.
For more details, please see New favorite for transfection —— Linear PEI MW 40000, a more efficient transfection reagent
Hieff Trans™ in vitro siRNA/miRNA Transfection Reagent
This product can achieve over 90% expression efficiency of 1 nM siRNA in a wide range of cell lines, avoiding off-target effects. Suitable for transfection of a variety of cells, including Hela, MCF-7, HepG2, CHO and other adherent cells; and difficult-to-transfect suspension cell lines, such as K562 or THP-1 cells, can achieve 80% silencing efficiency; Including some primary cells, primary human fibroblasts and primary human hepatocytes, etc., the silencing efficiency of 80% can be achieved.
Reference for transfection conditions
In addition to the instructions for each product, customers operate according to their specific experimental content, and there will be different differences in the amount of use. According to the in vitro cell transfection conditions reported by customers after using the product, they have been sorted out for your reference.
Product Name/Item Number
Hieff Trans™ Liposomal Transfection Reagent/40802ES
Cell
Culture vessel
Cell plating densities
DNA
Hieff trans
Transfection efficiencies
A549
6 well
90%
0.7 μg
1.15 μL
+++
BV 2
24 well
95%
0.2 μg
0.2 μL
++
C2C12
24 well
80% - 90%
1 μg
5 μL
++
DF 1
24 well
80% - 90%
0.5 μg
0.5 μL
+++
H520
6 well
80%
1.2μg
6 μL
++
HaCaT
96 well
70%
100 ng
1 μL
++
HCT116
6 well
90%
4 μg
10 μL
++
HEK 293
6 well
95%
2 μg
10 μL
80 - 90%
HEK 293FT
24 well
85%
1 μg
4 μL
90%
HEK 293T
12 well
1×105
1 μg
2 μL
+++
HEK 293T（suspension）
30 ml
80%
30 μg
60 μL
++
Hela
12 well
90%
0.2μg
0.6 μL
90%
Hela
12 well
80%
1 μg
3 μL
+++
HepG2
12 well
80%
1 μg
3 μL
++
HUVEC
24 well
80%
1 μg
2 μL
++
MCF10A
10 cm dish
60%
5 μg
15 μL
++
N2A
24 well
70% - 80%
300 ng
900 μL
+
NCI H1975
6 well
80%
4 μg
10 μL
+++
NIH 3T3
6 well
90%
4 μg
10 μL
+++
Raw 264.7
35 mm dish
80%
1 μg
2 μL
90%
Vero
6 well
80%
3 μg
9 μL
+++
Cell
Culture vessel
Cell plating densities
siRNA
Hieff trans
Transfection efficiencies
HK2
6 well
65%
100 pmol
6 μL
+++
FAQs
1 Hieff Trans™ Liposomal Transfection Reagent
1.1 Q: Can serum be present when preparing nucleic acid transfection reagent complexes?
A: The presence of serum will affect the formation of liposomes. It is recommended to use a serum-free medium (generally MEM medium) when preparing nucleic acid transfection reagent complexes.
1.2 Q: What should I pay attention to when using Hieff Trans™ Liposomal Nucleic Acid Transfection Reagent?
A:
1) When the cells are transfected, the cell density is preferably 80%-95%, and the specific plating density is determined according to the situation of the cells;
2) Using high-purity DNA helps to obtain higher transfection efficiency;
3) DNA and transfection reagents are required to be diluted with the serum-free medium when preparing transfection complexes;
4) Antibiotics cannot be added to the medium during transfection;
5) Reagents should be stored at 2-8°C, and care should be taken to avoid repeatedly opening the lid for a long time;
6) The DNA concentration and the number of cationic liposome reagents should be optimized for the first use to obtain the maximum transfection efficiency. The ratio of DNA to transfection reagent is generally recommended to be 1:2-1:3.
1.3 Q: Does it need to be terminated after transfection?
A: No need. Liposome complexes are stable for 6 hours. If the cell medium is not changed before transfection, in order to ensure the nutrients required for normal cell growth, it is necessary to change to a new medium after 4-6 hours. However, if the medium has been changed before transfection, it is not necessary to change the medium after liposome transfection.
1.4 Q: Can co-transfection of DNA and siRNA be performed? How's the effect?
A: Yes, when DNA and siRNA are co-transfected, the siRNA transfection efficiency will be slightly worse.
1.5 Q: Can the transfection reagent be used for the transfection of lentiviral packaging?
A: Lentiviral packaging is possible.
1.6 Q: Can suspension cells be transfected with Hieff Trans™ Liposomal Nucleic Acid Transfection Reagent?
A: Hieff Trans™ Liposome Nucleic Acid Transfection Reagent can be used for suspension cell transfection, see Protocol for details. In addition, we also introduced a transfection reagent specifically for suspension cells (Cat No. 40805, Hieff Trans™ Suspension Cell-Free Liposomal Transfection Reagent)
2 Hieff Trans™ in vitro siRNA/miRNA Transfection Reagent
2.1 Q: Does the transfection reagent need to be changed after transfection?
A: This problem can be divided into two cases: 1. If there is no medium change before transfection, the medium should be changed about 6 hours after transfection to ensure the nutrients required for cell growth; 2. If there is a medium change before transfection , can be operated according to the normal operation of cultured cells? ? After the liquid change operation?
2.2 Q: Can transfection reagents be frozen?
A: It cannot be frozen, because the transfection reagent is a PEI cationic transfection reagent. Freezing at low temperatures will destroy the activity of the PEI transfection reagent. Therefore, it is best to store it at 2-8 °C to maintain the best transfection. efficacy.
Product information
Product name SKU Specifications
Hieff Trans™ Liposomal Transfection Reagent 40802ES02 0.5 mL
40802ES03 1.0 mL
40802ES08 5×1mL
Hieff Trans™ Suspension Cell-Free Liposomal Transfection Reagent (Inquire) 40805ES02 0.5 mL
40805ES03 1.0 mL
40805ES08 5×1 mL
Hieff Trans™ in vitro siRNA/miRNA Transfection Reagent (Inquire) 40806ES02 0.5 mL
40806ES03 1.0 mL
Polyethylenimine Linear(PEI) MW40000（rapid lysis） 40816ES02 100 mg
40816ES03 1 g
40816ES08 5×1 g
Some of the articles published using our products
[1] Liu R, Yang J, et al. Optogenetic control of RNA function and metabolism using engineered light-switchable RNA-binding proteins. Nat Biotechnol. 2022 Jan 3. (IF:55)
[2] Luo J, Yang Q, et al. TFPI is a colonic crypt receptor for TcdB from hypervirulent clade 2 C. difficile. Cell. 2022 Mar 17.（IF:41.582）
[3] Zhou J, Chen P, et al. Cas12a variants designed for lower genome-wide off-target effect through stringent PAM recognition. Mol Ther. 2022 Jan 5.(IF:11.454)
[4] Chen S, Cao X, et al. circVAMP3 Drives CAPRIN1 Phase Separation and Inhibits Hepatocellular Carcinoma by Suppressing c-Myc Translation. Adv Sci (Weinh). 2022 Jan 24.(IF:16.808)
[5] Gu C, Wang Y, et al. AHSA1 is a promising therapeutic target for cellular proliferation and proteasome inhibitor resistance in multiple myeloma. J Exp Clin Cancer Res. 2022 Jan 6.(IF:11.161)
[6] Zhang Y, Yu X, et al. Splicing factor arginine/serine-rich 8 promotes multiple myeloma malignancy and bone lesion through alternative splicing of CACYBP and exosome-based cellular communication. Clin Transl Med. 2022 Feb.(IF:11.492)
[7] Qin J, Cai Y, et al. Molecular mechanism of agonism and inverse agonism in ghrelin receptor. Nat Commun. 2022 Jan 13.(IF:14.9)
[8] Tang X, Deng Z, et al. A novel protein encoded by circHNRNPU promotes multiple myeloma progression by regulating the bone marrow microenvironment and alternative splicing. J Exp Clin Cancer Res. 2022 Mar 8.(IF:11.161)
[9] Xie F, Su P, et al. Engineering Extracellular Vesicles Enriched with Palmitoylated ACE2 as COVID-19 Therapy. Adv Mater. 2021 Oct 19. (IF:30.849)
[10] Liang Y, Lu Q, et al. Reactivation of tumour suppressor in breast cancer by enhancer switching through NamiRNA network. Nucleic Acids Res. 2021 Sep 7.(IF:16.9)
[11] Fan Y, Wang J, et al. CircNR3C2 promotes HRD1-mediated tumor-suppressive effect via sponging miR-513a-3p in triple-negative breast cancer. Mol Cancer. 2021 Feb 2.(IF:27.403)
[12] Dai L, Dai Y, et al. Structural insight into BRCA1-BARD1 complex recruitment to damaged chromatin. Mol Cell. 2021 Jul 1.(IF:17.97)
[13] Zhang K, Wang A, et al. UBQLN2-HSP70 axis reduces poly-Gly-Ala aggregates and alleviates behavioral defects in the C9ORF72 animal model. Neuron. 2021 Jun 16.(IF:17.17)
[14] Li T, Chen X, et al. A synthetic BRET-based optogenetic device for pulsatile transgene expression enabling glucose homeostasis in mice. Nat Commun. 2021 Jan 27.(IF:14.92)
[15] Yan F, Huang C, et al. Threonine ADP-Ribosylation of Ubiquitin by a Bacterial Effector Family Blocks Host Ubiquitination. Mol Cell. 2020 May 21.(IF:17.97)
[16] Sun X, Peng X, et al. ADNP promotes neural differentiation by modulating Wnt/β-catenin signaling. Nat Commun. 2020 Jun 12.(IF:14.911)
[17] Yang X, Wang H, et al. Rewiring ERBB3 and ERK signaling confers resistance to FGFR1 inhibition in gastrointestinal cancer harbored an ERBB3-E928G mutation. Protein Cell. 2020 Dec.(IF:14.872)
[18] Zou Y, Wang A, et al. Analysis of redox landscapes and dynamics in living cells and in vivo using genetically encoded fluorescent sensors. Nat Protoc. 2018 Oct.(IF:13.490)
[19] Hao H, Hu S, et al. Loss of Endothelial CXCR7 Impairs Vascular Homeostasis and Cardiac Remodeling After Myocardial Infarction: Implications for Cardiovascular Drug Discovery. Circulation. 2017 Mar 28.(IF:29.69)
Regard Reading
Transfection Reagent – Hieff Trans™ and PEI
Linear PEI MW 40000, a more efficient transfection reagent
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Tag: "traveling" at biology news
Monkeys don't go for easy pickings
...tive ones. Although the sakis took more risks by traveling further by expending more energy and exposing themselves to predators for longer periods choosing more fruit-rich sites allowed the group to limit feeding competition amongst themselves and to stick together to maintain intergroup dominance. The...
Tumor painting revolutionizes fight against cancer
... prostate cancer model, as few as 200 cancer cells traveling in a mouse lymph channel could be detected. Chlorotoxin:Cy5.5 is applicable to many cancers, but is especially helpful to surgeons operating on brain tumors. Not only would it reveal whether theyd left behind any bits of tumor, it would also help t...
Coaching computer canines in clambering
...e Schaal's dogs can now move, but not very fast: traveling at 1.6 centimeters a second, a little faster than the old 1.2 cm/sec of the old Mars Sojourner robot. The goal in the next phase of the study is to triple the speed and double the difficulty of the terrain - have the dogs not just traverse rocky gr...
Female iguanas pay high costs to choose a mate
...ible for females to assess many candidates without traveling far. Vitousek and colleagues measured how much energy female iguanas expend on mate choice in the wild using miniaturized data loggers developed by Anthony Woakes at the University of Birmingham. They found that females devote a surprising amount ...
18-year-old Singaporean student to present stem cell research paper at conferences in US and UK
Most young Singaporean students who will be traveling next week and during July will be vacationing, relaxing and sightseeing. But not 18-year old Nicholas Tan Xue-Wei, who will soon depart for the U.S. to attend and present a research paper at The 2007 World Congress in Computer Science, Computer E...
New bacterium discovered -- related to cause of trench fever
... England Journal of Medicine. The woman had been traveling in the Peruvian Andes. She suffered from potentially life-threatening anemia, an enlarged spleen and a high fever for several weeks, as do victims of malaria and typhoid. The Andes are also home to another Bartonella species, spread by sand flies. Th...
Cellular message movement captured on video
... filmed red-fluorescence-tagged paxillin molecules traveling from cells outer membrane along green-fluorescence-labeled traces of cytoskeleton. Even without video evidence, scientists have confirmed over the past 10 years that higher organisms use paxillin as a transmitter of locomotion and gene-expression sig...
Computer science professor awarded $400,000 from National Science Foundation
...rent travel situations using GPS receivers in cars traveling all over this area, said Wenk. Additionally, the CAREER award could help create advancements in the medical industry as Wenk and her students look to develop novel computational tools to analyze two-dimensional electrophoresis gels. The gels pro...
Molecular motors may speed nutrient processing
...ties. At the time, Tyska knew that the core bundle traveling up the center of the microvillus was an array of the structural protein actin, and that the ladder-like "rungs" connecting the actin bundle to the cell membrane were composed of the motor protein myosin-1a. This myosin, though related to the myosin i...
Dinosaur hearing, listening to muscle noise, quieter cubicles
... sensors follow the passing of natural shear waves traveling along the muscle fibers. By the way, the Scripps scientists were originally interested in underwater noise effects and only later adapted their work to noise in muscle. (2pUW9; contact Karim Sabra, [email protected] ) MEASURING VOCAL STRESSES...
Simple equations track Listeria trails
...enoy as soon as he saw Theriots movies of Listeria traveling in the two-dimensional world of a microscope slide. Some bacteria spun in circles, others followed a sine curve, some followed a path like the cloverleaf exchange on a highway. The circles, he thought, were easy to explain. If an actin filament pushe...
Newborn neurons like to hang with the 'in' crowd
...pecialized structures called synapses. As a signal traveling along a nerve branch arrives at the pre-synaptic area, it releases a chemical signal. The signaling molecules travel across the synapse and induce a signal on the neighboring, receiving nerve fiber or dendrite. A typical neuron sports about 7,000 syn...
Academy paleontologist and Alaska artist in line for natural history awards
...ues songs about fish and is the art director for a traveling exhibition that opens June 2 at the Academy called Amazon Voyages: Vicious Fishes and Other Riches. For more on Troll, see www.trollart.com . "These individuals have broken new ground into the history and exotica of life," said Academy President a...
US conservation efforts bring more marine turtles to UK
...ch in the Americas and can spend nearly four years traveling thousands of miles to British waters. Scientists do not know why some juvenile turtles make the journey to Northern Europe, but believe they may simply be driven by the North Atlantic current system. The eggs of Kemps ridley turtles were harvested ...
Ocean's 'twilight zone' may be a key to understanding climate change
...day, but they are swept sideways by ocean currents traveling many thousands of meters per day. To collect sinking particles, oceanographers use cones or tubes that hang beneath buoys or float up from sea floor. That, Buesseler said, "is like putting out a rain gauge in a hurricane." While many studies have i...
National Academies advisory: Invasive aquatic species in the Great Lakes
...digenous aquatic species into the lakes by vessels traveling the St. Lawrence Seaway. The committee's final report will comment on the strengths and weaknesses of various options and recommend those that seem most promising. DETAILS: 9 a.m. to 5:30 p.m. on May 7 at the Marriott Toronto Downtown Eaton Centr...
University of Alberta researchers unravel intricate animal patterns
...e classical, such as stationary pulses, ripples or traveling trains but they also describe new patterns that ha...eported before such as zigzag pulses, feathers and traveling breathers. This model doesnt apply to specific species, says Eftimie. "However, we can think of th...
Health disparities -- Genetics, society and race play an important role in access to healthcare
... to be older, living in an unsafe neighborhood and traveling at least 45 minutes to get to the doctor. Researchers at the University of Southern California's Keck School of Medicine cite two general types of personal risk factors associated with late cancer diagnosis: socio-economic, or cultural, factors re...
Marine scientists monitor longest mammal migration
...bor, Maine. The scientists found some humpbacks traveling from Antarctica across the equator to as far north as Costa Rica to overwinter, a distance of approximately 8,300 kilometers or about 5,157 miles. The authors noticed that the presence of cold water along the equator coincided with the occurrence of...
A changing climate for protected areas
...oving beyond their traditional ranges, potentially traveling out of current protected areas such as national parks. The study found that existing protected areas remain effective in the early stages of climate change, while adding new protected areas or expanding current ones would maintain species protection ...
1 2 3 4 5
(Date:8/21/2014)... , Aug. 21, 2014 /PRNewswire-iReach/ -- ... it has agreed to a partnership with Gabriel ... fastest growing Certified Nursing Assistant ... Health Institute an exclusive member of Binary,s LiveScan ... Binary Biometrics will improve its service capabilities ...
(Date:8/21/2014)... In a finding that has implications for life in ... in the solar system, LSU Associate Professor of Biological ... National Science Foundation, or NSF, this week published a ... lake that lies 800 meters (2600 feet) beneath the ... microbial ecosystems.", Given that more than 400 subglacial lakes ...
(Date:8/21/2014)... Oct. 18-22, 2014 , WHERE: , San ... Diego, CA 92101 , WHAT: , Invited ... the latest research in human genetics. Examples of ... abstracts on rare genetic variants in health and ... for sun sensitivity (Saturday, Oct. 18, 5:30-7:30 pm) ...
Breaking Biology News(10 mins):LiveScan Provider Binary Biometrics Announces Partnership with Preeminent CNA School, Gabriel Health Institute to Expand Services in Orlando Region 2LiveScan Provider Binary Biometrics Announces Partnership with Preeminent CNA School, Gabriel Health Institute to Expand Services in Orlando Region 3800 meters beneath Antarctic ice sheet, subglacial lake holds viable microbial ecosystems 2800 meters beneath Antarctic ice sheet, subglacial lake holds viable microbial ecosystems 3800 meters beneath Antarctic ice sheet, subglacial lake holds viable microbial ecosystems 4American Society of Human Genetics 2014 Annual Meeting 2
Other Tags
insomniabewarevigonivillameansecologyprotectingmultinationalscholarshipprofessorsmapscustomisedpoliciesprogramjointlaunch
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Conservation of gene expression during embryonic lens formation and cornea-lens transdifferentiation in Xenopus laevis
Jonathan J. Schaefer, Guillermo Oliver, Jonathan J. Henry*
*Corresponding author for this work
Research output: Contribution to journalArticlepeer-review
56 Scopus citations
Abstract
Few molecular comparisons have been made between the processes of embryo-genesis and regeneration or transdifferentiation that lead to the formation of the same structures. In the amphibian, Xenopus laevis, the cornea can undergo transdifferentiation to form a lens when the original lens is removed during tadpole larval stages. Unlike the process of embryonic lens induction, cornea-lens transdifferentiation is elicited via a single inductive interaction involving factors produced by the neural retina. In this study, we compared the expression of a number of genes known to be activated during various phases of embryonic lens formation, during the process of cornea-lens transdifferentiation. mRNA expression was monitored via in situ hybridization using digoxigenin-labeled riboprobes of pax-6, Xotx2, xSOX3, XProx1, and γ6-cry. We found that all of the genes studied are expressed during both embryogenesis and cornea-lens transdifferentiation, though in some cases their relative temporal sequences are not maintained. The reiterated expression of these genes suggests that a large suite of genes activated during embryonic lens formation are also involved in cornea-lens transdifferentiation. Ultimately functional tests will be required to determine whether they actually play similar roles in these processes. It is significant that the single inductive event responsible for initiating cornea-lens transdifferentiation triggers the expression of genes activated during both the early and late phases of embryonic lens induction. These findings have significant implications in terms of our current understanding of the 'multistep' process of lens induction.
Original languageEnglish (US)
Pages (from-to)308-318
Number of pages11
JournalDevelopmental Dynamics
Volume215
Issue number4
DOIs
StatePublished - 1999
Keywords
• Cornea-lens transdifferentiation
• Lens induction
• Lens regeneration
• XProx1
• Xenopus laevis
• Xotx2
• pax-6
• xSOX3
• γ6-cry
ASJC Scopus subject areas
• Developmental Biology
Fingerprint Dive into the research topics of 'Conservation of gene expression during embryonic lens formation and cornea-lens transdifferentiation in Xenopus laevis'. Together they form a unique fingerprint.
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Dictionary » S » Side
Side
side
1. Of or pertaining to a side, or the sides; being on the side, or toward the side; lateral. One mighty squadron with a side wind sped. (Dryden)
2. Hence, indirect; oblique; collateral; incidental; as, a side issue; a side view or remark. The law hath no side respect to their persons. (hooker)
3. [AS. Sid. Cf Side] long; large; extensive. His gown had side sleeves down to mid leg. (Laneham) Side action, in breech-loading firearms, a mechanism for operating the breech block, which is moved by a lever that turns sidewise. Side arms, weapons worn at the side, as sword, bayonet, pistols, etc. Side ax, an ax of which the handle is bent to one side. Side-bar rule, a rule authorised by the courts to be granted by their officers as a matter of course, without formal application being made to them in open court; so called because anciently moved for by the attorneys at side bar, that is, informally. Side box, a box or inclosed seat on the side of a theater. To insure a side-box station at half price. (Cowper) side chain, one of two safety chains connecting a tender with a locomotive, at the sides. Side cut, a canal or road branching out from the main one. Side dish, one of the dishes subordinate to the main course. Side glance, a glance or brief look to one side. Side hook, a cutting tool, used in a lathe or planer, having the cutting edge at the side instead of at the point. Side wind, a wind from one side; hence, an indirect attack, or indirect means.
Please contribute to this project, if you have more information about this term feel free to edit this page
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Ruprecht Karls Universität Heidelberg
Pintu Patra
Research Interests
• Stochastic Processes
• Microbial Population Dynamics
• Self-organisation in Biological Systems
• Biological Networks
• Theoretical Evolution
Publications
• Mechanism of Kin-Discriminatory Demarcation Line Formation between Colonies of Swarming Bacteria
P Patra, CN Vassallo, D Wall, OA Igoshin
Biophysical journal 113 (11), 2477-2486 (2017)
• Colony Expansion of Socially Motile Myxococcus xanthus Cells Is Driven by Growth, Motility, and Exopolysaccharide Production
P Patra, K Kissoon, I Cornejo, HB Kaplan, OA Igoshin
PLoS Comput Biol 12 (6), e1005010 (2016)
• Emergence of phenotype switching through continuous and discontinuous evolutionary transitions
P Patra, S Klumpp
Physical biology 12 (4), 046004 (2015)
• Phenotypically heterogeneous populations in spatially heterogeneous environments
P Patra, S Klumpp
Physical Review E (Rapid Communications) 89 (3), 030702 (2014)
• Population Dynamics of Bacterial Persistence
P Patra, S Klumpp
PLoS ONE 8 (5), e62814 (2013)
• Interplay between population dynamics and drug tolerance of Staphylococcus aureus persister cells
S Lechner, P Patra, S Klumpp, R Bertram
Journal of molecular microbiology and biotechnology 22 (6), 381-391 (2012)
Short Vita
since November 2017
Post doctoral researcher at the Institute for Theoretical Physics with Prof. Dr. Ulrich Schwarz, Heidelberg, Germany
Janaury 2015 - October 2017
Post doctoral researcher at the Department of Bioengineering, Rice Unviersity with Prof. Dr. Oleg A Igoshin , Houston, United States of America
May 2014 - October 2014
Post doctoral researcher at the Max Plack Institute of Colloids and Interfaces with Prof. Dr. Stefan Klumpp, Potsdam, Germany
August 2010 - Feb 2014
PhD studies at Max Plack Institute of Colloids and Interfaces under the supervision of Prof. Dr. Stefan Klumpp, Potsdam, Germany
August 2010
Master of Science in Physics at Indian Institute of Technology, Madras, India
Address
Pintu Patra
Institute for Theoretical Physics
Ruprecht-Karls-University of Heidelberg
Philosophenweg 19
69120 Heidelberg, Germany
BioQuant - Center for Quantitative Biology
Im Neuenheimer Feld 267
Room 163
69120 Heidelberg, Germany
email: pintu.patra at bioquant.uni-heidelberg.de
phone: +49-(0)6221-54-51253
fax: +49-(0)6221-54-51482
http://www.thphys.uni-heidelberg.de/~biophys
zum Seitenanfang
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Collisions during DNA replication and transcription contribute to mutagenesis
June 29, 2016, Baylor College of Medicine
DNA
Credit: NIH
When a cell makes copies of DNA and translates its genetic code into proteins at the same time, the molecular machinery that carries on replication and the one that transcribes the DNA to the mRNA code move along the same DNA double strand as their respective processes take place. Sometimes replication and transcription proceed on the same direction, but sometimes the processes are in a collision course. Researchers at Baylor College of Medicine and the University of Wisconsin have determined that these collisions can significantly contribute to mutagenesis. Their results appear today in Nature.
"We first developed a laboratory assay that would allow us to detect a wide range of mutations in a specific gene in the bacteria Bacillus subtilis," said corresponding author Dr. Jue D. Wang, who was an associate professor of molecular & human genetics at Baylor when a portion of the work was completed and is currently with the University of Wisconsin, Madison. "In some bacteria, we introduced the gene so the processes of replication and would proceed on the same direction. In other bacteria the gene was engineered so the processes would collide head-on."
The researchers discovered that when replication and transcription were oriented toward a head-on collision path the mutation rate was higher than when their paths followed the same direction. Furthermore, most of the mutations caused by replication transcription conflicts were either insertions/deletions or substitutions in the promoter region of the gene, the region that controls gene expression.
"People have mostly been looking at mutations in the DNA sequence that codes for protein, but in this paper we found that the promoter, the regulatory element of gene expression, is very susceptible to mutagenesis," said Wang, "and this susceptibility is facilitated by head-on transcription and DNA ."
Promoters control how much of a gene is transcribed; for instance, particular mutations in promoters may enhance or reduce the production of proteins, or silence them completely. These genetic changes in gene expression may affect an organism's health.
"The mutation mechanism we identified is not just applicable to our experimental system, but can potentially contribute to that alter in a genome-wide scale, from bacteria to humans," said Wang.
Explore further: Head-on collisions between DNA-code reading machineries accelerate gene evolution
More information: T. Sabari Sankar et al, The nature of mutations induced by replication–transcription collisions, Nature (2016). DOI: 10.1038/nature18316
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Tag Archives: Hi-C
Data Management – Illumina NovaSeq Geoduck Genome Sequencing
As part of the Illumina collaborative geoduck genome sequencing project, their end goal has always been to sequence the genome in a single run.
They’ve finally attempted this by running 10x Genomics, Hi-C, Nextera, and TruSeq libraries in a single run of the NovaSeq.
I downloaded the data using the BaseSpace downloader using Chrome on a Windows 7 computer (this is not available on Ubuntu and the command line tools that are available from Illumina are too confusing for me to bother spending the time on to figure out how to use them just to download the data).
Data was saved here:
Generated MD5 checksums (using md5sum on Ubuntu) and appended to the checksums file:
Illumina was unable to provide MD5 checksums on their end, so I was unable to confirm data integrity post-download.
Illumina sample info is here:
Will add info to:
List of files received:
10x-Genomics-Libraries-Geo10x5-A3-MultipleA_S10_L001_R1_001.fastq.gz
10x-Genomics-Libraries-Geo10x5-A3-MultipleA_S10_L001_R2_001.fastq.gz
10x-Genomics-Libraries-Geo10x5-A3-MultipleA_S10_L002_R1_001.fastq.gz
10x-Genomics-Libraries-Geo10x5-A3-MultipleA_S10_L002_R2_001.fastq.gz
10x-Genomics-Libraries-Geo10x5-A3-MultipleB_S11_L001_R1_001.fastq.gz
10x-Genomics-Libraries-Geo10x5-A3-MultipleB_S11_L001_R2_001.fastq.gz
10x-Genomics-Libraries-Geo10x5-A3-MultipleB_S11_L002_R1_001.fastq.gz
10x-Genomics-Libraries-Geo10x5-A3-MultipleB_S11_L002_R2_001.fastq.gz
10x-Genomics-Libraries-Geo10x5-A3-MultipleC_S12_L001_R1_001.fastq.gz
10x-Genomics-Libraries-Geo10x5-A3-MultipleC_S12_L001_R2_001.fastq.gz
10x-Genomics-Libraries-Geo10x5-A3-MultipleC_S12_L002_R1_001.fastq.gz
10x-Genomics-Libraries-Geo10x5-A3-MultipleC_S12_L002_R2_001.fastq.gz
10x-Genomics-Libraries-Geo10x5-A3-MultipleD_S13_L001_R1_001.fastq.gz
10x-Genomics-Libraries-Geo10x5-A3-MultipleD_S13_L001_R2_001.fastq.gz
10x-Genomics-Libraries-Geo10x5-A3-MultipleD_S13_L002_R1_001.fastq.gz
10x-Genomics-Libraries-Geo10x5-A3-MultipleD_S13_L002_R2_001.fastq.gz
10x-Genomics-Libraries-Geo10x6-B3-MultipleA_S14_L001_R1_001.fastq.gz
10x-Genomics-Libraries-Geo10x6-B3-MultipleA_S14_L001_R2_001.fastq.gz
10x-Genomics-Libraries-Geo10x6-B3-MultipleA_S14_L002_R1_001.fastq.gz
10x-Genomics-Libraries-Geo10x6-B3-MultipleA_S14_L002_R2_001.fastq.gz
10x-Genomics-Libraries-Geo10x6-B3-MultipleB_S15_L001_R1_001.fastq.gz
10x-Genomics-Libraries-Geo10x6-B3-MultipleB_S15_L001_R2_001.fastq.gz
10x-Genomics-Libraries-Geo10x6-B3-MultipleB_S15_L002_R1_001.fastq.gz
10x-Genomics-Libraries-Geo10x6-B3-MultipleB_S15_L002_R2_001.fastq.gz
10x-Genomics-Libraries-Geo10x6-B3-MultipleC_S16_L001_R1_001.fastq.gz
10x-Genomics-Libraries-Geo10x6-B3-MultipleC_S16_L001_R2_001.fastq.gz
10x-Genomics-Libraries-Geo10x6-B3-MultipleC_S16_L002_R1_001.fastq.gz
10x-Genomics-Libraries-Geo10x6-B3-MultipleC_S16_L002_R2_001.fastq.gz
10x-Genomics-Libraries-Geo10x6-B3-MultipleD_S17_L001_R1_001.fastq.gz
10x-Genomics-Libraries-Geo10x6-B3-MultipleD_S17_L001_R2_001.fastq.gz
10x-Genomics-Libraries-Geo10x6-B3-MultipleD_S17_L002_R1_001.fastq.gz
10x-Genomics-Libraries-Geo10x6-B3-MultipleD_S17_L002_R2_001.fastq.gz
HiC-Libraries-GeoHiC-C3-N701_S18_L001_R1_001.fastq.gz
HiC-Libraries-GeoHiC-C3-N701_S18_L001_R2_001.fastq.gz
HiC-Libraries-GeoHiC-C3-N701_S18_L002_R1_001.fastq.gz
HiC-Libraries-GeoHiC-C3-N701_S18_L002_R2_001.fastq.gz
Nextera-Mate-Pair-Library-GeoNMP10-B2-AD013_S7_L001_R1_001.fastq.gz
Nextera-Mate-Pair-Library-GeoNMP10-B2-AD013_S7_L001_R2_001.fastq.gz
Nextera-Mate-Pair-Library-GeoNMP10-B2-AD013_S7_L002_R1_001.fastq.gz
Nextera-Mate-Pair-Library-GeoNMP10-B2-AD013_S7_L002_R2_001.fastq.gz
Nextera-Mate-Pair-Library-GeoNMP11-C2-AD014_S8_L001_R1_001.fastq.gz
Nextera-Mate-Pair-Library-GeoNMP11-C2-AD014_S8_L001_R2_001.fastq.gz
Nextera-Mate-Pair-Library-GeoNMP11-C2-AD014_S8_L002_R1_001.fastq.gz
Nextera-Mate-Pair-Library-GeoNMP11-C2-AD014_S8_L002_R2_001.fastq.gz
Nextera-Mate-Pair-Library-GeoNMP12-D2-AD015_S9_L001_R1_001.fastq.gz
Nextera-Mate-Pair-Library-GeoNMP12-D2-AD015_S9_L001_R2_001.fastq.gz
Nextera-Mate-Pair-Library-GeoNMP12-D2-AD015_S9_L002_R1_001.fastq.gz
Nextera-Mate-Pair-Library-GeoNMP12-D2-AD015_S9_L002_R2_001.fastq.gz
Nextera-Mate-Pair-Library-GeoNMP9-A2-AD002_S6_L001_R1_001.fastq.gz
Nextera-Mate-Pair-Library-GeoNMP9-A2-AD002_S6_L001_R2_001.fastq.gz
Nextera-Mate-Pair-Library-GeoNMP9-A2-AD002_S6_L002_R1_001.fastq.gz
Nextera-Mate-Pair-Library-GeoNMP9-A2-AD002_S6_L002_R2_001.fastq.gz
Trueseq-stranded-mRNA-libraries-GeoRNA1-A1-NR006_S1_L001_R1_001.fastq.gz
Trueseq-stranded-mRNA-libraries-GeoRNA1-A1-NR006_S1_L001_R2_001.fastq.gz
Trueseq-stranded-mRNA-libraries-GeoRNA1-A1-NR006_S1_L002_R1_001.fastq.gz
Trueseq-stranded-mRNA-libraries-GeoRNA1-A1-NR006_S1_L002_R2_001.fastq.gz
Trueseq-stranded-mRNA-libraries-GeoRNA3-C1-NR012_S2_L001_R1_001.fastq.gz
Trueseq-stranded-mRNA-libraries-GeoRNA3-C1-NR012_S2_L001_R2_001.fastq.gz
Trueseq-stranded-mRNA-libraries-GeoRNA3-C1-NR012_S2_L002_R1_001.fastq.gz
Trueseq-stranded-mRNA-libraries-GeoRNA3-C1-NR012_S2_L002_R2_001.fastq.gz
Trueseq-stranded-mRNA-libraries-GeoRNA5-E1-NR005_S3_L001_R1_001.fastq.gz
Trueseq-stranded-mRNA-libraries-GeoRNA5-E1-NR005_S3_L001_R2_001.fastq.gz
Trueseq-stranded-mRNA-libraries-GeoRNA5-E1-NR005_S3_L002_R1_001.fastq.gz
Trueseq-stranded-mRNA-libraries-GeoRNA5-E1-NR005_S3_L002_R2_001.fastq.gz
Trueseq-stranded-mRNA-libraries-GeoRNA7-G1-NR019_S4_L001_R1_001.fastq.gz
Trueseq-stranded-mRNA-libraries-GeoRNA7-G1-NR019_S4_L001_R2_001.fastq.gz
Trueseq-stranded-mRNA-libraries-GeoRNA7-G1-NR019_S4_L002_R1_001.fastq.gz
Trueseq-stranded-mRNA-libraries-GeoRNA7-G1-NR019_S4_L002_R2_001.fastq.gz
Trueseq-stranded-mRNA-libraries-GeoRNA8-H1-NR021_S5_L001_R1_001.fastq.gz
Trueseq-stranded-mRNA-libraries-GeoRNA8-H1-NR021_S5_L001_R2_001.fastq.gz
Trueseq-stranded-mRNA-libraries-GeoRNA8-H1-NR021_S5_L002_R1_001.fastq.gz
Trueseq-stranded-mRNA-libraries-GeoRNA8-H1-NR021_S5_L002_R2_001.fastq.gz
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Assembly – Geoduck Hi-C Assembly Subsetting
Steven asked me to create a couple of subsets of our Phase Genomics Hi-C geoduck genome assembly (pga_02):
• Contigs >10kbp
• Contigs >30kbp
I used pyfaidx on Roadrunner and the following commands:
faidx --size-range 10000,100000000 PGA_assembly.fasta > PGA_assembly_10k_plus.fasta
faidx --size-range 30000,100000000 PGA_assembly.fasta > PGA_assembly_30k_plus.fasta
Ran Quast afterwards to get stats on the new FastA files just to confirm that the upper cutoff value was correct and didn’t get rid of the largest contig(s).
Results:
faidx Output folder: 20180512_geoduck_fasta_subsets/
10kbp contigs (FastA): 20180512_geoduck_fasta_subsets/PGA_assembly_10k_plus.fasta
30kbp contigs (FastA): 20180512_geoduck_fasta_subsets/PGA_assembly_30k_plus.fasta
Quast output folder: results_2018_05_14_06_26_26/
Quast report (HTML): results_2018_05_14_06_26_26/report.html
Everything looks good. The main thing I wanted to confirm by running Quast was that the largest contig in each subset was the same as the original PGA assembly (95,480,635bp.
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Data Management – Geoduck Phase Genomics Hi-C Data
We received sequencing/assembly data from Phase Genomics.
The data contains two assemblies, produced on two different dates.
All data is here: 20180421_geoduck_hi-c
All FASTQ files (four files; Geoduck_HiC*.gz) were copied to Nightingales:
MD5 checksums were verified and appended to the Nightingales checksum file:
Nightingales sequencing inventory was updated (Google Sheet):
The two assemblies (and assembly stats) they provided are here:
I’ve updated the project-geoduck-genome GitHub wiki with this info.
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TG-SDS Buffer, 10X Powder Pack Each pack makes 1 L of 10X Tris-Glycine-SDS Buffer concentrate for dilution to a 1X working solution.
TG-SDS Buffer, 10X Powder Pack
TG-SDS Buffer, 10X Powder Pack is rated 5.0 out of 5 by 1.
• y_2020, m_10, d_30, h_17
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5
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1
0
Application: TG-SDS Buffer, 10X Powder Pack is each pack makes 1 L of 10X Tris-Glycine-SDS Buffer concentrate for dilution to a 1X working solution
For Research Use Only. Not Intended for Diagnostic or Therapeutic Use.
* Refer to Certificate of Analysis for lot specific data (including water content).
10X Tris-Glycine-SDS Buffer. Each pack provides an adequate amount of material to make 1 L of 10X concentrate that can be diluted to a 1X solution containing 25 mM Tris, 192 mM glycine, 0.1% SDS, pH 8.3. Researchers may check and adjust the final pH using a sensitive pH meter.
Also available:
TRIS Glycine buffer solution (sc-296648)
References
1. Towbin, H., et al. 1979. Proc. Natl. Acad. Sci. U.S.A. 76: 4350-4354. PMID: 388439
Formulation :
10X
Physical State :
Solid
Solubility :
Soluble in water
pH :
8.3
Storage :
Store at room temperature
For Research Use Only. Not Intended for Diagnostic or Therapeutic Use.
Download SDS (MSDS)
Certificate of Analysis
Adobe Acrobat Reader is required to reliably view,
print and comment on PDF documents
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Rated 5 out of 5 by from TG TG-SDS Buffer, 10X Powder Pack was utilized in many articles for the electrophoretic transfer of proteins. -SCBT Publication Review
Date published: 2015-02-15
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Santa Cruz Biotechnology, Inc. is a world leader in the development of products for the biomedical research market. Call us Toll Free at 1-800-457-3801.
Copyright © 2007-2020 Santa Cruz Biotechnology, Inc. All Rights Reserved. "Santa Cruz Biotechnology", and the Santa Cruz Biotechnology, Inc. logo, "Santa Cruz Animal Health", "San Juan Ranch", "Supplement of Champions", the San Juan Ranch logo, "Ultracruz", "Chemcruz", "Immunocruz", "Exactacruz", and "EZ Touch" are registered trademarks of Santa Cruz Biotechnology, Inc.
All trademarks are the property of their respective owners.
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Lele et al., 2002 - parachute/n-cadherin is required for morphogenesis and maintained integrity of the zebrafish neural tube. Development (Cambridge, England) 129(14):3281-3294
Fig. 1
pac mutants exhibit abnormal brain and tail morphogenesis. (A,C,E,G) Wild-type siblings, (B,D,F,H,I) pacfr7 mutants. (A,B) Eight-somite stage, frontal view, arrows in B indicate broadened neural tube at midbrain-hindbrain level. (C-I) 24 hpf. (C,D) lateral overview; arrows in D indicate sites of phenotypic defects in the midbrain-hindbrain region and tip of tail. (E,F) Magnification of head region; arrowheads in E,F indicates the position of the midbrain-hindbrain boundary, arrows in F indicate loose cell aggregates in ventricle. (G-I) Magnification of tip of tail; lateral view (G,H) and dorsal view (I); arrows in H,I indicate region with split dorsal fin.
Fig. 2
The pac mutation affects cell-cell adhesion in the midbrain-hindbrain region. (A-C) Bodipy ceramide staining; 24 hpf; confocal microscopic cross sections at hindbrain levels; (A) wild-type sibling, (B,C) pacfr7 mutant. Red arrowheads indicate rounded cells, blue arrows indicate ectopic rosette-like structures in dorsal regions of the pac mutant, and white arrows indicate ventricle lumen of the neural tube and ectopic lumina in dorsal rosette-like structures in pac. Insets in A,B show longitudinal sections through the mid- and hindbrain. The midbrainhindbrain boundary (mhb) is indicated by white arrowheads and levels at which the crosssections are taken are indicated by white arrows. Note the less pronounced mhb in pac mutant (B). (D-K) Chimeric embryos after transplantation of wild-type or pac mutant cells into wildtype or pac mutant hosts, as indicated: 24 hpf; lateral view of the mid- and hindbrain (D-F) and transverse sections at midbrain-hindbrain level (G-K). Note the tighter organization of the aggregate in I compared with K. Arrows in E,F,J,K indicate isolated cells. Note that in K, isolated pac mutant cells have a rounded shape, in contrast to their elongated wild-type neighbors (compare with alar wild-type cells in G).
Fig. 3
pac encodes N-cadherin. Map positions of the pactm101B mutation and the ncad gene on linkage group 20. Cartoon of the structure of Ncad protein. As indicated, Ncad encoded by pacm101B and pacfr7 displays premature terminations in the extracellular region, shortly after the EC3 domain. (C-F) Expression pattern of ncad. (C) Eight-cell stage, lateral view. (D) 80% epiboly stage, lateral view. (E) Fifteen-somite stage, lateral view. (F) 24 hpf, cross-section at trunk level. ncad expression is restricted to neural tube and slow muscle fibers. (G) RT-PCR analysis of ncad transcripts from pacpaR2.10 mutants, and structure of their 5′ regions. From pacpaR2.10 RNA, no wildtype, but only a predominant smaller transcript (*S) and different larger ncad transcripts (*L) were amplified. (H) Western blot analysis of protein extracts from a pacpaR2.10 and a wild-type sibling embryo with a polyclonal antibody against EC domains 4,5 of zebrafish Ncad (Bitzur et al., 1994). The wild-type extract gives an Ncad-positive band of the expected size, whereas no such band is seen in extracts from the pacpaR2.10 mutant. Before antibody incubation, the blot had been stained with Ponceau Red, showing that equal amounts of proteins were loaded in both lanes. Similar analyses failed to detect Ncad protein from pacfr7 mutants, as expected, because, according to the cDNA sequence, pacfr7 mutant protein terminates after the third EC domain. (I) Phenocopy of the pac mutant phenotype with anti-ncad morpholino ncad-MO1 (right, compare with Fig. 1F) and with the four-mismatch control MO (left) (see Materials and Methods). Embryos at 24 hpf, lateral view of head region.
PHENOTYPE:
Fish:
Knockdown Reagent:
Observed In:
Stage: Prim-5
Fig. 4
Lack of Ncad causes neurulation defects. (A-N) Whole-mount in situ hybridization for the markers indicated in the top right-hand corner. Dorsal views with anterior towards the left in A-H; optical cross sections dorsal upwards in I-N; all paired panels compare a pac mutant (right) with a wild-type sibling (left). (O,P) Mid-hindbrain cross-sections of wild-type embryos co-transplanted with cells from two different donors, as indicated in the bottom right-hand corner; donor cells are stained in cyan or brown. (A,B) foxd3, three-somite stage; note the identical mediolateral extent of the neural plate in wild-type and pac. (C,D) sna2, five-somite stage; arrows indicate the width of neural plate delineated by sna2 stripes, larger in pac. (E,F) emx1 (blue; marking telencephalon) + lim5 (red; marking posterior diencephalon) (Toyama et al., 1995a), 10- somite stage. In F, cells in the fused part of the lim5 expression domain are located ventrally, cells in the bilateral parts dorsally. (G,H) wnt1, 26 hpf; arrows indicate fused (G) and bilateral (H) expression domains in the midbrain. (I,J) pax6 + shh; 12-somite stage; section at hindbrain level. The alar plate devoid of pax6 staining is outlined by dots. (K,L) pax7, 16-somite stage; optical section at hindbrain level. Arrow in K indicates a pax7 stripe in the interface of basal and alar plate. (M,N) pax2.1, 24 hpf; optical cross-section through midbrain-hindbrain boundary region; arrow indicates the region where basal and alar plate have morphologically separated. (O,P) Chimeric embryos, 24 hpf, cross-section at midbrain (P) and hindbrain (O) levels. Note that in P, wild-type cells (in brown) populate the basal plate, while pacpaR2.10 mutant cells (in cyan) remain alar, although both cell types had initially been transplanted to the same presumptive basal region of the host embryo.
Fig. 5
Lack of Ncad causes neuronal positioning defects. In situ hybridization (A-L), retrograde labeling of reticulospinal neurons (M-O) and tracing of cellular clones after labeling single neuroectodermal cells at the gastrula stage (P-R). All paired panels in A-L compare a pac mutant (right) with a wild-type sibling (left). (A-F) Dorsal views of the mid- and hindbrain, anterior towards the left; (G,H,K,L) sagittal views of the mid- and hindbrain, anterior towards the left; (I,J) optical cross-sections at hindbrain level, dorsal upwards. (A,B) pax2.1 (blue) and krox20 (red), 18-somite stage. (C,D) zcoe2, 18-somite stage, arrows in D indicate misplaced motoneurons in the midbrain-hindbrain boundary region. (E,F) lim1; 26 hpf; arrows in E indicate the rhombomeric pattern, altered in pac (F). In addition, note that the number of lim1-positive cells in the mutant is strongly increased. (G,H) phox2a, 36 hpf; arrows indicate ventral and dorsally misplaced motoneurons. (I,J) isl1, 24 hpf; arrows indicate motoneurons, arrowheads indicate Rohon-Beard sensory neurons. (K,L) pax2.1, 26 hpf; arrow in L indicates scattered interneurons in hindbrain area. ov, otic vesicle. (M-N) Pattern of reticulospinal neurons (specified in M) in wild-type (M) and two different pacpaR2.10 mutant embryos (N,O; Mauthner neurons are indicated by ‘M’); dorsal view on midbrain-hindbrain region at 120 hpf. Patterns in mutants appear randomized, and differ from individual to individual. Although each labeling is unlikely to label all reticulospinal neurons, the patterns observed clearly lack bilateral symmetry at least for the Mauthner neuron (identified by its characteristic elongated shape and large diameter axon, out of focus on O). (P-R) Representative clones (brown) deriving from labeled single cell of the hindbrain region of a wild-type (P) and two pacpaR2.10 mutant gastrulae (Q,R). Dorsal view of the hindbrain at 24 hpf. Arrows indicate the length of the clones along AP axis. Insets show overviews of the activated embryos, indicating the position of the clones in each embryo (arrows).
Fig. 6
Lack of Ncad leads to ectopic neurons in dorsal regions of mid-hindbrain and axonal projection defects. Anti-acetylated tubulin immunostaining in (A,C,E,G) wild type and (B,D,F,H) pac fr7 mutant; 60 hpf; dorsal/ventral views (A,B,E,F) and lateral view (C,D) of the head, and lateral view of the trunk anterior of the anus (G,H). (A-D) Arrow in A indicates tectal commissures missing in B. Arrows in B,D indicate large dorsal neurons projecting axons to each other (B) and ventrally (D). (E,F) Arrows indicate optic nerves crossing the midline in optic chiasma in E, but not in F. (G,H) Left arrow in H indicates branching intersomitic axon, right arrow indicates two converging axons from different motoneurons.
Fig. 7
pac mutants display loss of membrane-associated β-catenin and enhanced cell proliferation in dorsal regions of midbrain and hindbrain. (A,B) Anti-b catenin immunostaining on 2 mm confocal cross-sections through the hindbrain of wild-type (A) and pac paR2.10 mutant sibling (B); 12-somite stage. (C-F) Anti-phospH3 immunostaining of wild-type sibling (C,E) and pacfr7 mutant (D,F) embryos of the 12-somite stage; flat mounts of whole embryos (C,D), and representative cross-sections at the hindbrain level (E,F). Mitotic cells in the lateralmost position (indicated by arrowheads) are not part of the neural tube and are probably migrating neural crest cells. In A,B,E,F, the neural tube is outlined by dots. Arrows in F point to ectopic phospH3-positive cells in alar region of mutant.
Acknowledgments:
ZFIN wishes to thank the journal Development (Cambridge, England) for permission to reproduce figures from this article. Please note that this material may be protected by copyright.
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Planet Earth
Neanderthal-human mating, months later....
Gene ExpressionBy Razib KhanJul 18, 2011 7:27 PM
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Image credit:ICHTO
Recently something popped up into my Google news feed in regards to "Neanderthal-human mating." If you are a regular reader you know that I'm wild for this particular combination of the "wild thing." But a quick perusal of the press release
told me that this was a paper I had already reviewed when it was published online in January
. I even used the results in the paper to confirm
Neanderthal admixture
in my own family (we've all been genotyped). One of my siblings is in fact a hemizygote
for the Neanderthal alleles on the locus in question! I guess it shows the power of press releases upon the media. I would offer up the explanation that this just shows that the more respectable press doesn't want to touch papers which aren't in print, but that's not a good explanation when they are willing to hype up stuff which is presented at conferences at even an earlier stage. A second aspect I noted is that except for Ron Bailey
at Reason all the articles
which use a color headshot use a brunette reconstruction, like the one here which is from the Smithsonian. But the most recent research (dating to 2007) seems to suggest that the Neanderthals may have been highly depigmented
. This shouldn't be too surprising when one considers that they were resident in northern climes for hundreds of thousands of years. But there are some new tidbits, from researchers in the field of study:
"There is little doubt that this haplotype is present because of mating with our ancestors and Neanderthals," said Nick Patterson of the Broad Institute of MIT and Harvard University. Patterson did not participate in the latest research. He added, "This is a very nice result, and further analysis may help determine more details." David Reich, a Harvard Medical School geneticist, added, "Dr. Labuda and his colleagues were the first to identify a genetic variation in non-Africans that was likely to have come from an archaic population. This was done entirely without the Neanderthal genome sequence, but in light of the Neanderthal sequence, it is now clear that they were absolutely right!" The modern human/Neanderthal combo likely benefitted our species, enabling it to survive in harsh, cold regions that Neanderthals previously had adapted to. "Variability is very important for long-term survival of a species," Labuda concluded. "Every addition to the genome can be enriching."
Since Nick comments here on occasion I probably should have asked him what he thought of these results back in January, but it goes to show that I'm not thinking like a journalist. Yet.
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57
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cf5cd1df0ee2161e1684bdc019357275
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-2,891,517,357,935,664,000
|
Genetics
Jellybeans Activity
• Precision Health
• SDG 3: Good Health and Well-Being
• Resource Plan Supporting Material
• 14 - 15 years
• Science
An additional resource that is used in this topic.
Please login or enter student code to download the resource files.
Resource Publisher
Qatar Genome
Qatar Genome Programme (QGP) is a population-based research project that aims to study the genetic makeup of the Qatari population with the aim of introducing precision medicine and personalized healthcare. Its large-scale genomic research, based on data collected by Qatar Biobank, has made Qatar one of the few countries in the world conducting research of this nature.
Other Resources
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cf5cd1df0ee2161e1684bdc019357275
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-8,424,687,385,350,203,000
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Oxidative regulation mechanisms in the mitochondrial intermembrane space
Manganas, Phanee (2017) Oxidative regulation mechanisms in the mitochondrial intermembrane space. PhD thesis, University of Glasgow.
Full text available as:
[thumbnail of 2017manganasphd.pdf] PDF
Download (36MB)
Printed Thesis Information: https://eleanor.lib.gla.ac.uk/record=b3288972
Abstract
Oxidative stress occurs when cells are unable to cope with the levels of various reactive
oxygen species (ROS) that arise as part of regular cellular metabolism or in response to
ionising radiation (H2O2, O2-, OH-). The most well studied ROS is H2O2, due to its dual
role as a mediator of oxidative stress and a signalling molecule for many cellular pathways.
Cells possess a number of different mechanisms to combat ROS, in order to prevent their
levels from becoming toxic.
In this thesis, we studied three different aspects of the antioxidant defence in
Saccharomyces cerevisiae. In the first part, we explored the role of erythroascorbic acid –
the yeast analogue of ascorbic acid (vitamin C) – and attempted to determine its role as an
antioxidant in yeast. Our results were inconclusive, though there were indications that the
presence of erythroascorbic acid may have a protective effect on the mitochondrial inner
membrane potential (ΔΨ), protecting it from depolarisation.
The second part focused on elucidating the mitochondrial targeting of the main H2O2
sensor Gpx3 and, more specifically, whether the Yap1-binding proteins, Ybp1 and Ybp2,
have an effect on the import of Gpx3 in yeast mitochondria. Our results show a slight
effect of Ybp1 (but not Ybp2) on the import of Gpx3, indicating that Ybp1 may act as a
chaperone for the more efficient targeting of Gpx3 from the cytosol to the outer
mitochondrial membrane and, as a result, its eventual translocation into the IMS.
The final part of this thesis focused on elucidating the import of Trx1 and Trr1 in the
mitochondrial IMS, as well as their function in this particular subcompartment. The
discovery of two members of the thioredoxin system in the IMS is important, due to the
absence of a known reducing mechanism in this oxidising compartment. Our results
determined that several well-known import factors are dispensable for the import of either
Trx1 or Trr1, indicating that they follow a yet unknown pathway for their translocation
into the IMS. Importantly, we showed that Trx1 is reduced (and thus, active) in the IMS
and that it can interact in vitro with both components of the MIA machinery (Mia40 and
Erv1), while in organello experiments showed that Trx1 most probably interacts with a
large number of Mia40 substrates.
Item Type: Thesis (PhD)
Qualification Level: Doctoral
Keywords: mitochondria, intermembrane space, import, oxidation, oxidative stress response, reductive pathways, thioredoxin.
Subjects: Q Science > Q Science (General)
Q Science > QH Natural history > QH301 Biology
Q Science > QH Natural history > QH345 Biochemistry
Colleges/Schools: College of Medical Veterinary and Life Sciences > School of Molecular Biosciences
Supervisor's Name: Tokatlidis, Professor Kostas
Date of Award: 2017
Depositing User: Phanee Manganas
Unique ID: glathesis:2017-8568
Copyright: Copyright of this thesis is held by the author.
Date Deposited: 03 Nov 2017 16:35
Last Modified: 15 Nov 2017 14:50
URI: https://theses.gla.ac.uk/id/eprint/8568
Related URLs:
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cf5cd1df0ee2161e1684bdc019357275
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531,268,446,006,279,700
|
There are less young corals in areas that they've been known to grow in—but new research finds that they could be thriving in cooler waters instead.
Advertisement
Fish Swimming Around a Wild Coral Reef
Credit: Georgette Douwma / Getty Images
Once synonymous with tropical destinations, vibrant corals are now found growing more frequently in cooler regions farther away from equatorial waters, according to new research published in the journal Marine Ecology Progress Series. A team of researchers from the Bigelow Laboratory for Ocean Sciences worked alongside an international team comprised of 17 different institutions from six different countries to discover the newfound trend, mostly studying the corals found in the wild near French Polynesia. Together, the teams comprised a database of information dating back to 1974, finding that young corals on tropical reefs have declined by 85 percent. Meanwhile, in the same span of time, it seems that the amount of coral specimens thriving on subtropical reefs have doubled.
"Climate change seems to be redistributing coral reefs, the same way it is shifting many other marine species," Nichole Price, a senior research scientist at Bigelow Laboratory for Ocean Sciences and lead author of the paper, said in a statement. "The clarity in this trend is stunning, but we don't yet know whether the new reefs can support the incredible diversity of tropical systems."
Because much of the ocean has experienced some form of warming due to climate change, researchers found that corals are growing in cooler waters as far as 35 degrees north and south of the equatorial stretch of ocean where they've historically thrived. This change may also lure other ocean wildlife, including fish and other aquatic species, to new ecosystems away from tropical regions. Not all coral is able to adapt in new locations, however, because only some coral larvae can swim farther and drift in currents to new areas away from traditional breeding grounds.
"We are seeing ecosystems transition to new blends of species that have never coexisted, and it's not yet clear how long it takes for these systems to reach equilibrium," Satoshi Mitarai, a co-author of the study and a professor at the Okinawa Institute of Science and Technology Graduate University, said in the same press release. "The lines are really starting to blur about what a native species is, and when ecosystems are functioning or falling apart."
While the study reports promising findings for those worried about the gradual decline in healthy ocean corals, researchers are unsure if all of the species that enable corals to thrive will be able to migrate as well. The teams behind this sweeping study hope that other scientists will add to their newly created database in the future. "So many questions remain about which species are and are not making it to these new locations, and we don't yet know the fate of these young corals over longer time frames," Price said. "The changes we are seeing in coral reef ecosystems are mind-boggling, and we need to work hard to document how these systems work and learn what we can do to save them before it's too late."
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57
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cf5cd1df0ee2161e1684bdc019357275
|
-1,842,444,772,604,558,300
|
.
The Open Protein Structure Annotation Network
PDB Keyword
.
PF08188
Table of contents
1. 1. Topsan Members
2. 2. Summary
Live PFAM
Name: Accession: PF08188 (PFAM live)
# sequence matches: # architectures:
# taxonomy ids: PDB:
GO Terms
GO:0000228 nuclear chromosome component
GO:0035092 sperm chromatin condensation process
GO:0003677 DNA binding function
Topsan Members
Tag pages as 'PF08188' to appear in this list.
No TOPSAN member(s) found.
Summary
Reviews
References
No references found.
Tag page
Files (0)
You must login to post a comment.
All content on this site is licensed under a Creative Commons Attribution 3.0 License
Powered by MindTouch
|
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57
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7,997,253,284,022,252,000
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The Unexpected Truth About Diffusion and Osmosis Lab Report
The Tried and True Method for Diffusion and Osmosis Lab Report in Step by Step Detail
The energy which drives the procedure is usually discussed when it comes to osmotic pressure. Water is easily the most versatile solvent known. Thu your instructor provides you have to have in water that may cross the mass of osmosis packet. https://writingalab.report/ Use the pond water to produce your wet mount.
There are many sorts of diffusion. It results because of the random movement of particles. Cellular diffusion is the procedure which causes molecules to move in and from a cell. The diffusion of water is referred to as osmosis. It is called osmosis. For instance, if the particles are excessively large, like the starch molecules, they won’t be permitted to enter or exit the cell. Particles in solution are usually free to.
You shouldn’t be in a position to summarise osmosis lab report the appropriate location. https://gradschool.duke.edu/academics/programs-degrees/cell-and-molecular-biology Although the experiment resulted powerful there are lots of issues which. This experiment is an enjoyable and straightforward approach to observe the consequences of plant osmosis on a plant by comparing two unique potatoes put in various types of. Future experiments might discover the saturation point that is a point once the concentration is so high that osmosis doesn’t boost any further.
Osmosis is a crucial function to the increase and stability of plant life. lab report online It is a special kind of diffusion. It is the diffusion of water. Compared to the solution inside of the egg and then explain how it will be involved. You might have heard of osmosis in biology class due to its vital role in the survival of plant life.
Osmosis is especially critical to photosynthesis. It’s even feasible to reversing osmosis! Osmosis is especially essential to photosynthesis. It continues until there is an equal pressure of fluid on either side of the membrane. You may have known of osmosis in biology class on account of the critical part in the survival of vegetation.
The Basic Principles of Diffusion and Osmosis Lab Report That You Can Learn From Beginning Immediately
Cells utilize diffusion so as to carry out simple tasks. The cell is going to be inverted into a beaker of water containing iodine. To observe the procedure for osmosis and the way it occurs in cells.
Molarity A style of expressing concentration is known as molarity. A remedy is isotonic in the event the concentration of dissolved substances is the exact same as the concentration within the cell. In the event the concentrations are the exact same, being isotonic, there would not be any osmosis occurring, and for that reason no change in mass. If two solutions have the exact same solute concentration, the solutions are reported to be isotonic. A hypertonic solution is going to have greater concentration of solutes than the cell and will get a greater osmotic pressure away from the cell than inside the cell.
The simulated blood might cause stains. All the blood within the body must pass through the kidneys. Each kidney is approximately the size of somebody’s fist. The kidneys are extremely important organs within the body since they are necessary to maintaining homeostasis. Kidney disease can’t be cured.
The most frequently encountered paper writing service that the majority of our clients require is essay writing. Browsing our essay writing samples can offer you a sense whether the standard of our essays is the quality you’re looking for. If it’s the first time you’re likely to use our article writing service, you most likely have plenty of questions. Your lab report will be finished on lab 2. In each trial, 6 unique kinds of solutions should be made.
The remedy with a rather low concentration is called a hypotonic solution, and also the one with a bigger concentration is known as hypertonic. These exercises are intended to. The remainder of the experiment is secure and simple for children of all ages, but slicing the potato ought to be achieved by an adult. The outer field of the cell is softer. Passive transport doesn’t require an output of energy. A form of cell transport particularly is passive transport. The dissolving agent of a remedy is known as a solvent.
Have a look at the german article, it supplies a indication of the way the post ought to be written and reformatted. Most significantly, our results are not just from osmosis. It’s possible to discover the consequence of osmosis. Affects of diffusion and water in the netherlands carries totally free energy. You’ll also learn to calculate water potential. You will also learn how to compute water potential. Water potential proved to be a key element in every component of the experiment.
The procedure for water moving through a semipermeable membrane is known as osmosis. The process began with the removal of a little round piece of agar from every one of both petri dishes with the usage of a straw. The assisted procedure is called facilitated diffusion.
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Wels Catfish Genome Sequenced and Assembled
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By deciphering the genetic code of the barbelled giant, scientists expect to better understand the secrets of the Wels catfish's exceptionally rapid growth, enormous appetite and longevity. Credit: Anti Vasemägi/EMÜ.
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An international research team led by scientists from Estonian University of Life Sciences has for the first time sequenced and assembled the genome of the wels catfish (Silurus glanis). The maximum reported size of the wels catfish is 5 m and up to 300 kg, which makes it one of the largest freshwater fish species in the whole world. By deciphering the genetic code of the barbelled giant, scientists expect to better understand the secrets of the wels catfish’s exceptionally rapid growth, enormous appetite and longevity.
The wels catfish lives in large European rivers and lakes. Catfish is hunting mainly at night and is not a picky eater, with invertebrates, fish, frogs, rodents and birds in its regular diet. When the water is warm and food is plentiful, the catfish grows extremely rapidly: ten-year-old fish can reach one and a half metres length. Given that a catfish can live up to 80 years, it is no wonder it has rightly become the prized trophy fish and a central character in many legends among anglers.
Due to its rapid growth and tender, boneless flesh, the catfish is increasingly gaining popularity for recreational fishing and aquaculture. The greatest number of wels catfish are being caught from the inland waters of Russia, Kazakhstan and Turkey, and its aquaculture production is currently approximately 2000 tonnes per year. At the same time, the lack of genetic information in wels catfish has inhibited application of modern selective breeding methods that utilize genomic information instead of phenotypic traits to estimate the breeding values of fish. "Assembled wels catfish genome allows researchers to find genomic regions and gene variants that impact growth rate, age at sexual maturity, disease resistance and other relevant traits for aquaculture,” explained Riho Gross, Chair professor of Aquaculture at Estonian University of Life Sciences, who led the research.
According to Anti Vasemägi, senior researcher of Estonian University of Life Sciences and professor of Swedish University of Agricultural Sciences, who participated in the work, the size of wels catfish genome can be compared to that of other bony fishes (800 million base pairs), and contains a little more than 21 000 genes. He added that the genome assembly will serve as a springboard for future research aimed at addressing the bottlenecks in catfish aquaculture and challenges linked to conservation of wild populations.
Reference: Reference: Ozerov MYu, Flajšhans M, Noreikiene K, Vasemägi A, Gross R. Draft genome assembly of the freshwater apex predator wels catfish (Silurus glanis) using linked-read sequencing. G3: Genes|Genomes|Genetics. 2020:g3.401711.2020. doi:10.1534/g3.120.401711.
This article has been republished from the following materials. Note: material may have been edited for length and content. For further information, please contact the cited source.
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Detection de legionella par cytometrie sur phase solide?
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Poster un nouveau sujet Répondre au sujet medmatiq Index du Forum » Médecine » 2èm cycle " 3 , 4 et 5 ème année " » Microbiologie - Maladies infectieuses
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biouided
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Féminin Bélier (21mar-19avr)
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MessagePosté le: Ven 12 Déc - 07:24 (2008) Répondre en citant
on dit que les techniques de detection des legionella par immunofluorescent (IF) ou l'hybridation in situ fluorescente (FISH) avec la détection par microscopie d'epifluorescence ne peuvent pas être appliquées à la détection des événements rares.
que ce qu'on veut dire là par enenements rar ????????????????
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biouided
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Expression of Bacillus thuringiensis (B.t.) insecticidal crystal protein gene in transgenic potato
Abstract. The crystal proteins, d-endotoxins, of Bacillus thuringiensis are specifically lethal to Lepidopteran insects. A truncated B.t. toxin gene, cryIA(a), encoding an insecticidal crystal protein (ICP) directed by the cauliflower mosaic virus 35S promoter was transferred to potato plants by an Agrobacterium-mediated transformation system. The integration of the cryIA(a) gene into potato genome was determined by Southern blot analysis and polymerase chain reaction (PCR). The copy number of the integrated gene was estimated by inverse polymerase chain reaction (IPCR). The cryIA(a) RNA transcripts in transgenic potato plants were demonstrated by Northern blot analysis. Seven out of thirty transgenic plants expressed the cryIA(a) gene. Those transgenic plants containing multiple transgene copies did not express cryIA(a) gene. Nevertheless, transgenic potato plants grown in the greenhouse contained 7_52 ng ICP per gram fresh leaf.
Abbreviations: ICP, insecticidal crystal protein; IPCR, inverse polymerase chain reaction; PCR, polymerase chain reaction; PSC, potato suspension cultures; RB, T-DNA right border; LB, T-DNA left border; NPTII, neomycin phosphotransferase II.
Introduction
The potato (Solanum tuberosum L.) is one of the major crops in agricultural production. Current efforts to develop insect-resistant crops through biotechnology are based primarily on transforming plants with a single gene encoding insecticidal enzyme or toxin. The most widely used genes in this approach are the d-endotoxin gene of Bacillus thuringiensis, a sporeforming, gram-positive bacterium. The insecticidal crystal protein (ICP) from the B. thuringiensis var. kustaki is a specific toxin for lepidopteran insects yet exhibits no toxicity toward humans, other vertebrates, or beneficial insects (Delannay et al., 1989). Formulated bacterial products have been used as insecticides for a long time. However, practical usages of such microbial products are limited because of their relatively high cost and poor persistence under field conditions, resulting in a need for multiple applications (Sneh et al., 1983).
Lepidopteran-active ICPs are protoxins of MW. 130_160 kDa. These protoxins emerge when exposed to an alkaline medium (pH 9_12), such as that found in the insect midgut. These protoxins are proteolytically cleaved into smaller, active forms (MW 60_70 kDa) derived from
the N-terminal half of the protein (Hofte et al., 1989). Although the mode of toxin action is largely unknown, it is assumed to bind specific proteins on the membrane of the insect gut (Hofmann et al., 1988).
The B.t. toxin cryIA gene of B. thuringiensis has been engineered and transferred into several plant species to yield resistance against certain lepidopteran insects. The truncated genes, which produce insecticidally active protein, have been expressed in potato (Adang et al., 1993; Perlak et al., 1993), tomato (Delannay et al., 1989), tobacco (Barton et al., 1987; Fischhoff et al., 1987; Vaeck et al., 1987), cotton (Perlak et al., 1990), corn (Koziel et al., 1993), and rice (Fujimoto et al., 1993). The use of a native d-endotoxin coding region, which has a high A-T content, appears to lead to an abnormally low expression in plants. Modifications of the coding region sequence to increase the G-C content of the native gene resulted in a dramatic increase in the expression of the insecticidal protein (Perlak et al., 1991).
As a first step toward the development of an insect resistant potato, attempts were made to transfer the truncated cryIA(a) gene directed by the cauliflower mosaic virus 35S promoter into potato plants through Agrobacterium-mediated transformation. These transgenic potato plants could provide alternatives to hazardous synthetic chemical insecticides for controlling lepidopteran pests.
4Corresponding author.
--------------------------------------------------------------------------------
Botanical Bulletin of Academia Sinica, Vol. 37, 1996
Materials and Methods
Plasmid Construction
The 2 kb truncated cryIA(a) gene was isolated from the plasmid DNA of B. thuringiensis var. karstaki by PCR (Schnepf et al., 1985). Two sequences in the B.t. coding region were chosen to amplify a 2 kb fragment within the gene. These two sequences were: 5' primer (TGGAGGTAACTTATGGATAACAATCCG) and the 3' primer (TCACTCAACTAAATTGGATACTTGATCA). The 5' and 3' primers include a plant translation initiation site (ATG) and a stop codon (UGA), respectively. PCR was carried out in a 50-ml reaction mixture containing 50 mM KCl, 10 mM Tris-HCl (pH 9.0), 0.25 mM MgCl2, 0.01% (W/V) gelatin, 0.1% (W/V) Triton X100, 0.2 mM of each deoxynucleoside triphosphate (dATP, dCTP, dGTP, dTTP), and 2.5 units of Taq DNA polymerase (Promega). The sample was preheated at 94°C for 1.5 min; annealed at 37°C for 2 min; and extended at 72°C for 5 min. This process was followed by 13 cycles of denaturation at 94 °C for 1 min; annealing at 40°C for 2 min; and extension at 72°C for 5 min. The PCR amplified 2 kb DNA fragment containing the essential region, the N-terminal region, of the B.t. gene was then modified to blunt end with Klenow fragment before ligation with pTZ19U plasmid at the SmaI site. The resulting clone U73 was then used as a source of the B.t. gene. The B.t. gene HincII-SstI (SstI partial digestion) restriction fragment from the U73 was subcloned into the SmaI and SstI site of the plant expression vector pBI121 (Jefferson, 1987) in which the GUS gene was deleted to create the new plasmid pBT121A (Figure 1). The pBT121A plasmid contained NPTII coding sequence for transformant selection in a kanamycin medium.
Transgenic Potato Plants
Triparental mating was used to mobilize pBT121A constructs into Agrobacterium tumefaciens C58C1 harboring
helper plasmid pGV2260 (which provides vir functions) (kindly provided by Dr. Marc Van Montagu, Laboratorium voor Genetica, Belgium). Potato (Solanum tuberosum L.) cv. ADH69 microtubers grown in vitro were transformed with Agrobacteria, and kanamycin-resistant plants were regenerated (Chang and Chan, 1991).
DNA Analysis
DNA was isolated from leaves of putative transgenic plants according to the CTAB method (Hurray and Thompson, 1980). DNA blot analysis was performed as described by Maniatis et al. (1982). About 0.8 kb of the cryIA(a) DNA was used as probe generated from the EcoRI digestion of pBT121A and labeled with [a-32P]dCTP using the random primer method (Feinberg and Vogelstein, 1983). To determine the copy number of transgenes integrated into transgenic plants, inverse polymerase chain reaction (IPCR) of genomic DNA for NPTII DNA was performed according to the method previously described (Does et al., 1991).
cryIA(a) RNA Analysis
Total RNA was purified from leaves according to the method of Belanger et al. (1986). RNA blot analysis was performed as described by Thomas (1983). The EcoRI fragment of pBT121A containing the cryIA(a) DNA was used as a probe.
NPTII Dot Blot Assay
The NPTII activity in the putative transgenic plants was assayed for at least three replicates using the method described by Chan et al. (1993).
ICP Protein Determination
Truncated ICP was used as a standard on the immunoblot. This protein was produced under the influence of the lac promoter on pUN4 (Chen, 1992). Polyclonal rabbit antibodies specific for the B. thuringiensis subsp. kurstaki ICP were used to determine the quantity of ICP accumulated in the crude extract of leaf samples. Extracts were made by grinding leaf tissue in liquid nitrogen followed by addition of extraction buffer (50 mM Na2CO3, pH 9.5, 100 mM NaCl, 0.05% Triton X-100, 0.05% Tween-20, 1 mM phenylmethyl sulfonyl fluoride (PMSF), and 1 mM leupeptin). Protein contents were determined using the Bradford method (Bradford, 1976). Western blot analysis was done as described by Yu et al. (1991). Protein dot-blot analysis was performed as described previously (Chan et al., 1994).
Results
Introduction of a Truncated cryIA(a) Gene into Potato Plants
Three to four month old microtubers grown in vitro were inoculated with Agrobacterium tumefaciens C58C1 (pGV2260 + pBT121A) and then cultured on a kanamy
Figure 1. Map of the binary vector pBT121A containing the 35S/cryIA(a) chimeric gene.
--------------------------------------------------------------------------------
Chan et al. — cryIA(a) gene expression in transgenic potato
cin selection medium. Thirty putative transformants out of the one-hundred treated microtubers were obtained and designated as P1 to P30. Southern blot analysis of HindIII digested genomic DNA from leaves of three putative transformants (P5, P7, and P10) were performed in order to demonstrate the integration of 35S/cryIA(a) in the genome of ADH69 (Figure 2). One band of approximately 11 kb appeared for P5 (Figure 2A, lane 2), 14 kb for P7 (Figure 2A, lane 3), and 6.5 kb for P10 (Figure 2A, lane 4). The probe did not hybridize with the DNA of the non-transformed control (Figure 2A, lane 5). These results indicate that the cryIA(a) DNA was integrated into the genome of the transformants. All other putative transformants were evaluated to determine whether the chimeric gene was integrated into the genome and to determine its copy number by IPCR analysis. IPCR analysis of genomic DNA using primers for amplifying the NPTII gene showed that most of the transformants—except P13, P16, P22, and P23— contain one copy of NPTII genes. No amplified DNA fragment was obtained for the non-transformant or for one putative transformant, P4 (data not shown). It is possible that P4 might be a non-transformant escaped from the selection medium. P13 and P23 showed two copies of the chimeric gene (Figure 2B) while P16 and P22 showed three and four copies, respectively (Figure 2B). When using DNA samples of the remaining 29 transgenic potatoes as template and priming them with the 3' and 5' ends of the cryIA(a) gene for PCR analysis, only 24 transformants had the amplified fragment (data not shown).
Expression of 35S/cryIA(a)/nos in Potato Variety ADH69
To examine the expression of the cryIA(a) gene in the 24 transgenic potato plants, total RNA isolated from leaves was hybridized with the coding region of the truncated cryIA(a) gene. The results indicated that cryIA(a) RNA transcripts were present in leaves of seven transgenic potato plants and the level of expression varied (Figure 3). No RNA transcript could be detected in P16. The remaining 17 transformants, including P13, P22, and P23, did not hybridize with the probe (data not shown). The NPTII transcript could be detected when these blots were rehybridized with a NPTII probe, indicating that the total RNA was not degraded (data not shown). In addition, staining of ribosomal RNA (rRNA) with ethidium bromide showed that the amount of total RNA applied was approximately the same among the different transgenic plants (Figure 3). The results of Northern blot analysis imply that cryIA(a) RNA can not be expressed well in those transgenic plants containing multiple transgene copies (P13, P16, P22, and P23); however, the NPTII RNA transcript can be detected in these transformants.
Expression of NPTII in the Transgenic Potato Plants
Plasmid pBT121A containing the NPTII-coding region was driven by the nopaline synthase promoter. Accordingly, selection for plants carrying the foreign genes was achieved using media containing kanamycin. To determine if the NPTII mRNA resulted in the synthesis of
A
B
Figure 2. (A) DNA blot analysis for detection of cryIA(a) DNA in the putative transgenic potato plants. Five µg of DNA digested with HindIII were loaded into each well. The EcoRI 0.8 kb fragment from pBT121A containing cryIA(a) DNA was used as a probe. Lane 1, lDNA cut with HindIII; Lanes 2_4, independent transgenic plant, P5, P7, P10, respectively. Lane 5, DNA from a non-transformed control plant. (B) Analysis of the IPCRs for 5 transformed plants (P5, P13, P16, P22, P23) and a non-transformed control plant (CK). One µg of plant DNA was used per reaction. Lane 1, fX174 marker; Lanes 2_3, plasmid pBT121A as the positive control (PK). M: MstII; S: SstII.
--------------------------------------------------------------------------------
Botanical Bulletin of Academia Sinica, Vol. 37, 1996
detectable in six transformants under this condition. P10 transformant produced the highest levels of CryIA(a) protein compared to the others listed in the Table 1. The yield of the CryIA(a) protein was estimated to be about 52 ng per g of fresh leaf tissue in P10, which was about six times higher than plant P17. P16, which contained the cryIA(a) gene but had no protein according to immunoblot analysis, produced no detectable level of ICP in the plant (Table 1). No cross reaction could be observed with a non-transformed control plant.
Figure 3. Northern blot of total RNA from transgenic potato leaves hybridized with the cryIA(a) DNA fragment. Ethidium bromide staining of gel prior to blotting showed that RNA was intact as judged by ribosomal RNA (rRNA) bands and that each lane contained an approximately equal amount of RNA. B.t. = cryIA(a).
Table 1. Comparison of cryIA(a) ICP levels in independent transgenic potatoes.
ICP line ng ICP/g fresh weight
(mean ± SEM)
P5 41 ± 5
P7 39 ± 6
P10 52 ± 7
P12 32 ± 8
P14 28 ± 7
P16 nd
P17 7 ± 4
P21 11 ± 3
CK 2 ± 1
*Values were obtained by dot-blot and densitometry assay and converted to ng ICP per gram fresh weight. Leaf samples were obtained from nodes 1 to 5. Values shown are average of 4 samples. nd: not detectable; CK: non-transformant.
Figure 4. Neomycin phosphotransferase II dot blot assay. Thirty mg protein extracts from leaves and extracts of 5 randomly selected transgenic potato plants were reacted with [g-32P]-ATP, dot blotted on Whatmann P81 papers and autoradiographed. Row A: reactions with kanamycin. Row B: reaction without kanamycin. Lane 1, protein extracts from non-transformed control plant (CK); Lanes 2_5, protein extracts from transgenic potato, respectively.
NPTII protein, protein was extracted from leaves of transgenic plants. NPTII activity was further monitored in 15 randomly chosen transgenic plants. All of the 15 transgenic plants demonstrated NPTII activity. No activity was observed in the non-transformed control group (Figure 4). These results clearly demonstrated that NPTII protein can be transcribed well in these transgenic plants.
Expression of CryIA(a) Protein in Transgenic Potato Plants
To determine the expression of CryIA(a) protein, immunoblot analysis was performed with extracts obtained from leaves of transgenic potato plants to ascertain levels of the CryIA(a) protein accumulated in transgenic plants. No signal, except the purified CryIA(a) protein from E. coli (the positive control), was detected for all transformants. The lack of signal could be attributable to a low level expression of the cryIA(a) gene in transgenic plants. Therefore, a high protein concentration (500 mg) was applied to the dot-blot apparatus and subjected to immunoblot analysis. In addition, we chose six transgenic plants in which cryIA(a) mRNA expression could be achieved and P16, no cryIA(a) mRNA transcript, to be the materials As shown in Figure 5, the CryIA(a) protein was
Figure 5. ICP protein dot blot assay. Protein extracts (500 mg) from approximately one gram of transgenic potato leaf tissue were dot blotted on nitrocellulose membrane, and the ICP protein was detected by an alkaline phosphatase conjugated goat anti-rabbit antibody after the binding of an antibody against ICP.
--------------------------------------------------------------------------------
Chan et al. — cryIA(a) gene expression in transgenic potato
Discussion
The 35S/cryIA(a)/nos chimeric gene was transferred into and expressed in potato plants. Twenty-nine transformants which survived on selection medium, expressed the NPTII activity (Figure 4). Using DNA samples of the 29 transgenic plants as templates to amplify the cryIA(a) gene fragment, five transformants showed no evidence of amplification. Although the possible cause of this phenomenon is still unclear, it is possible that the gene might be lost due to the replication and repair of transgenes prior to integration (Gheysen et al., 1991).
Most transgenic plants carrying the cryIA(a) gene did not express it with the exception of seven transformants (Table 1). The correlation between gene copy number and its expression in transformants has been reported to be positive (Gendloff et al., 1990; Hobbs et al., 1992), indeterminate (Dean et al., 1989), or negative (Hobbs et al., 1990, 1992). The results in this study indicated that transformants with higher ICP activity all had single copy while those transformants with no ICP activity (like P13, P16, P22, and P23) all had multiple copies of the T-DNA containing cryIA(a) gene (Figure 2B). We do not know what causes this phenomenon. In this experiment the rRNA was used as an internal control and a similar amount of RNA was loaded into each well. This negative correlation suggested a possibility that the lack of cryIA(a) mRNA transcripts might result from epigenetic silencing of gene expression by induction of repeated DNA sequence. A similar observation was reported earlier by van der Krol et al. (1990) and Napoli et al. (1990), who showed that transformation of additional homologous genes caused a gene-specific collapse in expression. The mechanism of co-suppression by transgenes may involve interference of RNA strands with the transcription process itself or DNA methylation of the endogenous gene. DNA methylation has been shown to be a mechanism for inactivation of chimeric transgenes (Hobbs et al., 1990; Matzke et al., 1989) and the demethylating agent 5-azacytidine has been used to reactivate silent transgenes (Bochardt et al., 1992). In addition, treatment of Agrobacterium with 5-azacytidine was efficient in increasing transformation frequencies (Palmgren et al., 1993). The suppression of cryIA(a) caused by these processes is being studied in our laboratory.
Among the seven transformants which expressed cryIA(a) gene, the levels of mRNA transcripts varied. The variation in transgene expression might be the result of a position effect in the genome. Low levels of cryIA(a) gene expression in plants might also be attributable to mRNA instability as suggested by Murray et al. (1991). A similar construct, 35S/cryIA(a)/nos, was involved in their studies. This RNA instability might also be due to an incomplete functioning of a polyadenylation signal. Furthermore, plant codon usage, in general, prefer G + C content in the codon position III (Murray et al., 1989), but the truncated cryIA(a) gene used in our study has a high A + T content, which may lead to low gene expression. However, a major
block to cryIA(a) gene expression in plants might be related to translation, which in turn effects the accumulation of cryIA(a) mRNA. Several lines of evidence show that insect-resistant plants containing the modified cryIA(b) have higher amounts of RNA than those with the truncated wild type gene (Fujimoto et al., 1993; Perlak et al., 1991). Those modified ICPs are more abundant in the transgenic plants.
Transgenic plants expressing insecticidal crystal genes are a powerful tool in an integrated pest management program. Several strategies have been proposed to increase insect-resistance in the field. The first involves the use of a tissue-specific, chemically-responsive (Williams et al., 1992), or wound-inducible promoter for B.t. expression. The second strategy is to modify the B.t. coding usage leading to a higher expression in the plant. The third, and final, strategy for enhancing the insect-resistant effect is to induce expressions of various B.t. genes in the same plant. Although in our study the level of CryIA(a) in transgenic potato plants was relatively low, it still amounted to 7_52 ng/g of fresh weight tissue. Several studies have also shown other transgenic plants expressing the truncated CryIA(b) at a level similar to our transgenic potatoes (Barton et al., 1987; Fischhoff et al., 1987; Vaeck et al., 1987). Since the LC50 (50% insect lethal of ICP concentration) for lepidopteran pests is about 25_40 ng/g (Vaeck et al., 1987), it is highly possible that transgenic potato plants will have significant defences against lepidopteran pests with further improvement in gene expression.
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GENERAL CHARACTERISTICS
The leading biorational pesticide, Bacillus thuringiensis, is a ubiquitous gram-positive, spore-forming bacterium that forms a parasporal crystal during the stationary phase of its growth cycle. B. thuringiensis was initially characterized as an insect pathogen, and its insecticidal activity was attributed largely or completely (depending on the insect) to the parasporal crystals. This observation led to the development of bioinsecticides based on B. thuringiensis for the control of certain insect species among the orders Lepidoptera, Diptera, and Coleoptera (for a review, see reference 33). There are more recent reports of B. thuringiensis isolates active against other insect orders (Hymenoptera, Homoptera, Orthoptera, and allophaga) and against nematodes, mites, and protozoa (109, 110). B. thuringiensis is already a useful alternative or supplement to synthetic chemical pesticide application in commercial agriculture, forest management, and mosquito control. It is also a key source of genes for transgenic expression to provide pest resistance in plants. In 1989, Ho¨fte and Whiteley reviewed the known cry genes and proposed a systematic nomenclature for them (164). Since then, the number of sequenced crystal protein genes (encoding Cry and Cyt proteins) has grown from 14 to well more than 100. In our accompanying work (79), we propose a revised
nomenclature to accommodate this wealth of new sequence data. The present work reviews the extensive progress during the past decade in determining the gene expression, structure, and mechanism of action for these classes of proteins. The proposed revised nomenclature will be used throughout. ECOLOGY AND PREVALENCE
B. thuringiensis seems to be indigenous to many environments (36, 65, 255). Strains have been isolated worldwide from many habitats, including soil (59, 88, 154, 255, 354), insects (59), stored-product dust (54, 65, 87, 267), and deciduous and coniferous leaves (175, 354). Isolation typically involves heat treatment to select for spores, sometimes with an acetate enrichment step (382) or antibiotic selection (89). The diversity in flagellar H-antigen agglutination reactions is one indication of the enormous genetic diversity among B. thuringiensis isolates.
The Pasteur Institute has catalogued 55 different flagellar serotypes and eight nonflagellated biotypes (202, 205). There is considerable evidence that B. thuringiensis and Bacillus cereus should be considered a single species. Classical biochemical and morphological methods of classifying bacteria have consistently failed to distinguish B. thuringiensis from B. cereus (31, 139, 177, 229, 305). Modern molecular methods— including chromosomal DNA hybridization (179), phospholipid and fatty acid analysis (40, 178), 16S rRNA sequence comparison (20, 318), amplified fragment length polymorphism analysis (181), and genomic restriction digest analysis (56, 57)—likewise support the single-species hypothesis. An attempt to distinguish B. thuringiensis isolates from B. cereus by analysis of a 16S rRNA variable region largely failed, yielding as many false positives and negatives as accurate identifications (373). The production of the parasporal crystal, the defining quality of B. thuringiensis, is too narrow a criterion for taxonomic purposes (237). Indeed, some B. cereus strains hybridize to cry1A-specific probes (56). Although we will employ the official nomenclature with two species names for these organisms, it is perhaps best to think of them as members of B. cereus sensu lato. The remarkable diversity of B. thuringiensis strains and toxins is due at least in part to a high degree of genetic plasticity. Most B. thuringiensis toxin genes appear to reside on plasmids (138), often as parts of composite structures that include mobile genetic elements (195, 218). Many cry gene-containing plasmids appear to be conjugative in nature (137). B. thuringiensis has developed a fascinating array of molecular
mechanisms to produce large amounts of pesticidal toxins during the stationary phase of growth (8, 30). One can only speculate about the ecological value to the bacterium of using several cry gene expression systems. However, coexpression of multiple toxins is likely to increase the host range of a given strain or of a population exchanging toxin genes. One report
has suggested plasmid transfer between different B. thuringiensis strains during growth within an insect (170). We are not aware of any critical experiments directed towards understanding bacterial toxin gene expression within the gut of a susceptible pest. Persistence of B. thuringiensis spores in the laboratory, greenhouse, and field or forest environment has been reasonably well studied (299, 403, 405). B. thuringiensis spores can survive for several years after spray applications (6), although rapid declines in population and toxicity have been noted.
Methods of detection have generally been limited to spore counts.
Meadows (266) has analyzed three prevailing hypothetical niches of B. thuringiensis in the environment: as an entomopathogen, as a phylloplane inhabitant, and as a soil microorganism.
Available data are still insufficient to choose among these and other possibilities, although B. thuringiensis seems to have been more readily isolated from insect cadavers or storedproduct
dusts than from soil (36, 65). It is also noteworthy that B. thuringiensis and B. cereus are able to multiply in the insect hemocoel and to provoke septicemia (156, 157, 358). Early work recognized the presence of a number of extracellular compounds that might contribute to virulence, including phospholipases (434), other heat-labile toxin activities (reviewed in
reference 332), and b-exotoxins (221). More recent characterization has shown that proteases (232), chitinases (356), and the secreted vegetative insecticidal proteins (VIPs) (108) (see
below) may contribute to virulence. B. cereus and B. thuringiensis also produce antibiotic compounds that have antifungal activity (357); one of these products can act to synergize crystal protein-induced intoxication of certain lepidopterans (253).
The Cry toxins are, therefore, the most prominent of a number of virulence factors allowing the development of the bacteria in dead or weakened insect larvae. Such data are at least suggestive that many strains of B. thuringiensis and some strains of B. cereus can be regarded as opportunistic insect pathogens. A more thorough understanding of the true ecological roles of B. thuringiensis would be of great importance, both for improving the reliability of risk assessment and for developing efficient methods for isolating novel B. thuringiensis strains containing useful d-endotoxin genes.
A number of pesticidal proteins unrelated to the Cry proteins are produced by some strains of B. thuringiensis during vegetative growth (108, 401). These VIPs do not form parasporal
crystal proteins and are apparently secreted from the cell. The VIPs are presently excluded from the Cry protein nomenclature because they are not crystal-forming proteins.
The term VIP is a misnomer in the sense that some B. thuringiensis Cry proteins are also produced during vegetative growth as well as during the stationary and sporulation phases, most notably Cry3Aa (see “cry gene expression”). The location of the vip genes in the B. thuringiensis genome has not been reported, although it would not be surprising to find them
residing on large plasmids that encode cry genes. The vip1A gene encodes a 100-kDa protein that is apparently processed from its N terminus to yield an ;80-kDa protein upon secretion. The 80-kDa Vip1A protein is reported to be toxic to western corn rootworm larvae in conjunction with the Vip2A protein, whose coding region is located immediately upstream (401). Interestingly, Vip1A shows sequence similarity to the protective antigen of the tripartite Bacillus anthracis toxin (298).
The vip3A gene encodes an 88-kDa protein that is produced during vegetative growth but is not processed upon secretion. Genes encoding Vip3A-type proteins appear to be common among strains of B. thuringiensis and B. cereus (108). This protein is reported to exhibit toxicity towards a wide variety of lepidopteran insect pests, including Agrotis ipsilon, Spodoptera frugiperda, Spodoptera exigua, and Helicoverpa zea (108). When fed to susceptible insects at lethal concentrations, Vip3A causes gut paralysis and lysis of midgut epithelial cells: the physical manifestations of Vip3A intoxication resemble those of the Cry proteins (431).
GENETICS AND MOLECULAR BIOLOGY
The B. thuringiensis Genome
B. thuringiensis strains have a genome size of 2.4 to 5.7
million bp (56). Physical maps have been constructed for two
B. thuringiensis strains (57, 58). Comparison with B. cereus
chromosomal maps suggests that all of these chromosomes
have a similar organization in the half near the replication
origin while displaying greater variability in the terminal half
(57). Most B. thuringiensis isolates have several extrachromosomal
elements, some of them circular and others linear (56).
It has long been recognized that the proteins comprising the
parasporal crystal are generally encoded by large plasmids
(138). Sequences hybridizing to cry gene probes occur commonly
among B. thuringiensis chromosomes as well (58), although
it is unclear to what degree these chromosomal homologs
contribute to production of the crystal.
The Transposable Elements of B. thuringiensis
The B. thuringiensis species harbors a large variety of transposable
elements, including insertion sequences and transposons.
The general characteristics of these elements have
been extensively reviewed by Mahillon et al. (248). Here, the B.
thuringiensis transposable elements are described with regard
to their structural association with the cry genes.
The first studies on the structural organization of the cry1A
gene environment showed that genes of this type were flanked
by two sets of inverted repeated sequences (195, 218). Nucleotide
sequence analysis revealed that these repetitive elements
were insertion sequences that have been designated IS231 and
IS232 (219, 237). IS231 belongs to the IS4 family of insertion
sequences (315), and IS232 belongs to the IS21 family of insertion
sequences (268). Because these elements can transpose
(152, 268), it is likely that they provide mobility for the cry
genes with which they form typical composite transposons.
However, this hypothesis has not been tested experimentally.
Several IS231 variants have been isolated from various B.
thuringiensis strains (249, 314, 316) and have been detected in
representative strains from well more than half of the known B.
thuringiensis serovars (212). In B. thuringiensis subsp. israelensis,
an IS231 element (IS231W) is adjacent to the cry11Aa gene
(4, 316). Although IS231 elements are frequently associated
with cry genes, IS231-related DNA sequences have also been
found in strains of B. cereus (190, 212) and Bacillus mycoides
(212). In contrast, IS232 has a much smaller range among the organisms surveyed so far, appearing in only 7 of 61 B. thuringiensis
serovars (212).
The cry4A gene of the israelensis subspecies is flanked by two
repeated sequences in opposite orientations (45). These sequences,
designated IS240, display features characteristic of
insertion sequences (83). The IS240 transposase is homologous
to those of the insertion sequences belonging to the IS6 family.
IS240 is widely distributed in B. thuringiensis and is invariably
present in known dipteran-active strains (319). Related sequences
have also been detected in B. mycoides and B. cereus
(212). An IS240 variant has been found upstream of the cry11B
gene in the B. thuringiensis subsp. jegathesan (86) and from a
plasmid of the dipteran-active strain B. thuringiensis subsp.
fukuokaensis (103).
Insertion sequences have been found upstream of the cry1Ca
gene (351) and downstream of a cryptic cry2Ab gene (160).
These elements encode putative transposases that have significant
similarities with the transposase of the IS150 element
from Escherichia coli. These potential transposable elements of
B. thuringiensis consequently belong to the IS3 family of insertion
sequences.
The first transposable element identified in the genus Bacillus
was isolated from B. thuringiensis following its spontaneous
insertion into a conjugative plasmid transferred from Enterococcus
faecalis (217). The genetic and structural characteristics
of this transposable element fulfilled the criteria of a Tn element,
and it was designated Tn4430 (216). Its transposase is
homologous to those of the Tn3 family. In contrast to Tn3,
however, the site-specific recombinase that mediates Tn4430
cointegrate resolution is not a resolvase but an integrase (247).
Tn4430 is frequently found in the vicinity of genes of the cry1A
type in various lepidopteran-active strains (196, 218, 328).
However, Tn4430-like sequences have also been detected in
several strains of B. cereus (56).
A transposable element designated Tn5401 was isolated
from a coleopteran-active B. thuringiensis strain following its
spontaneous insertion into a recombinant plasmid (27). Although
nucleotide sequence analysis indicates that the structural
organization of Tn5401 is similar to that of Tn4430, the
transposases and the site-specific recombinases of these transposons
are only distantly related (27). Tn4430 and Tn5401 are
not known to coexist in any B. thuringiensis strain (27). In B.
thuringiensis subsp. tenebrionis, Tn5401 is located just downstream
of the cry3Aa gene (3). It is noteworthy that Tn5401 has
been successfully used to construct a transposon insertion library
in B. thuringiensis (251).
Two open reading frames encoding polypeptides homologous
to the transposase and to the resolvase of the Tn3 family
of transposons have been identified upstream of the cry16A
gene found in Clostridium bifermentans (23, 82). This observation suggests that a Tn element is structurally associated with
this cry gene.
Regarding the role of the transposable elements in B. thuringiensis,
it is postulated that they are involved in the amplification
of the cry genes in the bacterial cell, but this hypothesis
has not been clearly tested. A second possible role is one of
mediating the transfer of plasmids by a conduction process
involving the formation of cointegrate structures between selfconjugative
plasmids and chromosomal DNA or nonconjugative
plasmids. Indeed, conjugation experiments suggest that
Tn4430 mediates the transfer of nonconjugative plasmids by a
conduction process (147). Thus, a major adaptive function for
these transposable elements may be the horizontal dissemination
of genetic material, including cry genes, within the B.
cereus-B. thuringiensis species.
cry Gene Expression
A common characteristic of the cry genes is their expression
during the stationary phase. Their products generally accumulate
in the mother cell compartment to form a crystal inclusion
that can account for 20 to 30% of the dry weight of the sporulated
cells. The very high level of crystal protein synthesis in B.
thuringiensis and its coordination with the stationary phase are
controlled by a variety of mechanisms occurring at the transcriptional,
posttranscriptional, and posttranslational levels.
Agaisse and Lereclus (8) and Baum and Malvar (30) have
recently reviewed the regulation of cry gene expression in detail.
We present here a broad outline of these regulatory mechanisms.
Transcriptional Mechanisms
The cry genes have long been considered typical examples of
sporulation-specific genes. However, recent studies on the expression
of the cry3Aa gene have revealed that this assumption is not always valid. It is therefore necessary to distinguish,
among the cry genes expressed during the stationary phase,
those that are dependent on sporulation from those that are
not.
Sporulation-dependent cry Gene Expression. Extensive
studies of the sporulation of B. subtilis have provided detailed
information on the complex mechanisms that temporally and
spatially control this differentiation process (for reviews, see
references 104 and 231). At the transcriptional level, the development
of sporulation is controlled by the successive activation
of sigma factors, which bind the core RNA polymerase
to direct the transcription from sporulation-specific promoters
(275). These factors are the primary sigma factor of vegetative
cells, sA, and five factors called sH, sF, sE, sG, and sK, which
appear in that order in a temporally regulated fashion during
development. The sA and sH factors are active in the predivisional
cell, sE and sK are active in the mother cell, and sF
and sG are active in the forespore.
The cry1Aa gene is a typical example of a sporulation-dependent cry gene expressed only in the mother cell compartment
of B. thuringiensis. Two transcription start sites have been
mapped (BtI and BtII), defining two overlapping, sequentially
activated promoters (417). BtI is active between about T2 and
T6 of sporulation and BtII is active from about T5 onwards
(where Tn is n hours after the end of the exponential phase).
Brown and Whiteley (52, 53) isolated two sigma factors, s35
and s28, that specifically direct transcription of cry1Aa from BtI
and BtII, respectively. In vitro transcription experiments have
also indicated that at least two other cry genes (cry1Ba and
cry2Aa) contain either BtI alone or BtI with BtII (52).
The genes encoding s35 and s28 have been cloned and sequenced
(1). Their deduced amino acid sequences show 88 and
85% identity with sE and sK of B. subtilis, respectively. B.
thuringiensis sE and sK mutants were constructed, and cry1Aa
gene expression was analyzed in these mutants (48). The results
indicated that these two sigma factors regulated expression
of a cry1Aa9-9lacZ transcriptional fusion in vivo. The sK
mutant produced about 50% less b-galactosidase than the
wild-type strain, whereas no b-galactosidase synthesis was obtained
in the sE mutant. The latter result was anticipated,
because sE controls sK synthesis.
Several cry gene promoters have been identified, and their
sequences have been previously determined (50, 51, 94, 428,
430). Consensus sequences for promoters recognized by B.
thuringiensis RNA polymerase containing sE or sK have been
deduced from alignment of the promoter regions of these
genes (8, 30). The results are that, in addition to the transcription
of cry1Aa, cry1Ba, and cry2Aa, the transcription of many
other cry genes (e.g., cry4Aa, cry4Ba, cry11Aa, cry15Aa, etc.) is
likely to be sE- or sK-dependent. Analysis of cry4Aa, cry4Ba,
and cry11Aa gene fusions in a B. thuringiensis sigE mutant
confirms that SigE is required for their expression during
sporulation (304). In addition, from a genetic analysis of B.
subtilis, Yoshisue et al. (430) reported that the expression of
cry4B is reduced in a spoIIID mutant strain, thus suggesting
that SpoIIID, a DNA-binding protein, positively regulates the
SigE-dependent transcription of cry4B. The cry18Aa gene isolated
from Bacillus popilliae is successively transcribed by sE
and sK forms of RNA polymerase from a single promoter
during sporulation (433).
The expression of all these cry genes is therefore considered
to be sporulation dependent. However, low-level transcription
of the cry4Aa, cry4Ba, and cry11Aa genes in B. thuringiensis has
been detected during the transition phase, beginning at about
T22 and lasting until the onset of sporulation (304, 429). This
expression may be due to the sH RNA polymerase, and it is
suggested that Spo0A represses this weak expression, specific
to the transition phase, when the cells enter the sporulation
phase (304).
Sporulation-independent cry gene expression. The cry3Aa
gene, isolated from the coleopteran-active B. thuringiensis var.
tenebrionis, was found to be expressed during vegetative
growth, although at a lesser extent than during the stationary
phase (95, 252, 339). Analysis of lacZ transcriptional fusions
and primer extension experiments indicates that the cry3Aa
promoter is weakly but significantly expressed during vegetative
growth, is activated from the end of exponential growth
until stage II of sporulation (about T3), and remains active
until stage IV of sporulation (about T7) (10, 324). The cry3Aa
promoter, although located unusually far upstream of the start
codon (position 2558), resembles promoters recognized by the
primary sigma factor of vegetative cells, sA (10). A similar
promoter was found 542 bp upstream of the start codon of the
cry3Bb gene (30). The expression of cry3Aa is not dependent
on sporulation-specific sigma factors either in B. subtilis (7) or
in B. thuringiensis (324). Moreover, cry3Aa expression is increased
and prolonged in mutant strains unable to initiate
sporulation (7, 213, 251, 324). The results indicate that cry3Aa
expression is activated by a non-sporulation-dependent mechanism
arising during the transition from exponential growth to
the stationary phase. The positive effect of mutations preventing
the initiation of sporulation suggests that there is an event
during sporulation (e.g., the disappearance of sA in the mother
cell) that turns off cry3Aa expression (7, 324).
Posttranscriptional Mechanisms
The stability of mRNA is an important contributor to the
high level of toxin production in B. thuringiensis. The half-life
of cry mRNA, about 10 min, is at least fivefold greater than the
half-life of an average bacterial mRNA (135).
Wong and Chang showed that the putative transcriptional
terminator of the cry1Aa gene (a stem-loop structure) acts as a
positive retroregulator (416). The fusion of a DNA fragment
carrying this terminator with the 39 end of heterologous genes
increases the half-life of their transcripts two- to threefold,
which in turn increases the expression of their gene products.
It has been demonstrated in other systems that the processive
activities of 39-59 exoribonucleases are impeded by 39 stemloop
structures (for a review, see reference 279). It is likely,
then, that the cry1Aa transcriptional terminator increases the
cry mRNA stability by protecting it from exonucleolytic degradation
from the 39 end. Similar terminator sequences, potentially
able to form stable stem-loop structures, are found
downstream from various cry genes and may contribute to their
high-level expression by stabilizing the transcripts. However,
alternative processes could determine the rate of mRNA degradation,
and the direct involvement of these sequences on
mRNA stability has not been tested by deleting them from a
cry gene and measuring stability of the message.
Between the cry3Aa promoter, located from positions 2560
to 2600, and the translational start codon is a region involved
at a posttranscriptional level with the accumulation of cry3Aa
mRNA as a stable transcript with a 59 end corresponding to
nucleotide position 2129 (10). Deletion of 60 bp extending
from nucleotide positions 2189 to 2129 has no detectable
effect on the expression level or on the position of the 59 end
of the transcript (10). It is likely, then, that the initial transcript,
begun hundreds of bases upstream, is processed posttranscriptionally.
Insertion of the cry3Aa 59 untranslated region (extending
from nucleotides 2129 to 212) between the B. subtilis xylA promoter and a lacZ reporter gene increases about 10-fold
both the stability of the lacZ fusion mRNA and the production
of b-galactosidase (9). Deletion and mutation analysis indicate
that the sequence required for the stabilizing effect is a perfect
Shine-Dalgarno sequence (GAAAGGAGG) mapping at a position
between 2125 and 2117; this sequence has been designated
STAB-SD (9). The stability of the cry3Aa mRNA could
result from an interaction between the 39 end of 16S rRNA and
STAB-SD. The binding of a 30S ribosomal subunit to this
sequence may protect the mRNA against 59-39 ribonuclease
activity, resulting in a stable transcript with a 59 end at nucleotide
position 2129 (i.e., the limit of 30S subunit protection).
Potential STAB-SD sequences are also present in similar positions
upstream of the cry3Ba, cry3Bb, and cry3Ca genes (96,
200).
Posttranslational Mechanisms
The Cry proteins generally form crystalline inclusions in the
mother cell compartment. Depending on their protoxin composition,
the crystals have various forms: bipyramidal (Cry1),
cuboidal (Cry2), flat rectangular (Cry3A), irregular (Cry3B),
spherical (Cry4A and Cry4B), and rhomboidal (Cry11A). This
ability of the protoxins to crystallize may decrease their susceptibility
to premature proteolytic degradation. However, the
crystals have to be solubilized rapidly and efficiently in the gut
of insect larvae to become biologically active. The structure
and the solubility characteristics of a crystal presumably depend
on such factors as the secondary structure of the protoxin,
the energy of the disulfide bonds, and the presence of
additional B. thuringiensis-specific components.
Studies have shown that several cry1 genes cloned in E. coli
(129) or B. subtilis (344) were able to direct the synthesis of
biologically active inclusions, suggesting that the 130- to 140-
kDa Cry1 protoxins can spontaneously form crystals. It is generally
assumed that the cysteine-rich C-terminal half of the
Cry1 protoxins contributes to crystal structure through the
formation of disulfide bonds (39). A similar mechanism of
protein self-assembly may be responsible for the crystal formation
of other 130- to 140-kDa protoxins (e.g., Cry4, Cry5, and
Cry7). The cysteine-rich C-terminal region is absent from the
73-kDa Cry3A protoxins. This protein forms a flat, rectangular
crystal inclusion in which the polypeptides do not appear to be
linked by disulfide bridges (35). Because this protein is able to
form identical crystals in both B. thuringiensis and B. subtilis, it
is possible that specific host factors are not required for the
protein assembly. Analysis of the three-dimensional structure
of the Cry3A toxin revealed the presence of four intermolecular
salt bridges, which might participate in the formation of
the crystal inclusion (222).
Various studies performed with E. coli and B. thuringiensis
have demonstrated that crystallization of Cry2A (71 kDa) and
Cyt1A (27 kDa) requires the presence of accessory proteins
(for recent reviews, see references 8 and 30). These proteins
may act at a posttranslational level to stabilize the nascent
protoxin molecule and to facilitate crystallization. However,
the precise mechanism of their role in crystal formation has not
been determined.
Kostichka et al. (192) have reported that a Cry1Ia toxin
could be found in the supernatant of B. thuringiensis cultures as
a processed polypeptide of 60 kDa. The authors hypothesize
that Cry1Ia is an exported protein and therefore interacts with
the cellular protein export machinery. Such a characteristic,
together with the fact that this toxin is synthesized early in
sporulation (192), may have implications for the significance of
these toxins in the ecology of B. thuringiensis. Similarly, the Cry16Aa toxin of C. bifermentans seems to be secreted during
sporulation (23).
TOXIN STRUCTURE
To date, the structures of three crystal proteins—Cry3A
(222), Cry1Aa (148), and Cyt2A (223)—have been solved by
X-ray crystallography. An analysis in the accompanying review
demonstrates that Cry3A and Cry1Aa show about 36% amino
acid sequence identity (79). This similarity is reflected in their
three-dimensional structures; the corresponding domains can
virtually be superimposed. Cyt2A, however, shows less than
20% amino acid sequence identity with Cry1Aa and Cry3A,
and a similar alignment score would be obtained if the Cyt2A
sequence were randomized. Not surprisingly, the Cyt2A structure
is radically different from the other two structures. The
structures of Cry1Aa, Cry3A, and Cyt2A are compared in Fig. 1.
The Cyt toxins, unlike the Cry d-endotoxins, are able to lyse
a wide range of cell types in vitro (164). Cyt2A consists of a
single domain in which two outer layers of alpha-helix wrap
around a mixed beta-sheet. Cyt1A is believed to have a similar
structure.
Cry3A and Cry1Aa, in contrast to Cyt2A, both possess three
domains. Domain I consists of a bundle of seven antiparallel
a-helices in which helix 5 is encircled by the remaining helices.
Domain II consists of three antiparallel b-sheets joined in a
typical “Greek key” topology, arranged in a so-called b-prism
fold (330, 343). Domain III consists of two twisted, antiparallel
b-sheets forming a b-sandwich with a “jelly roll” topology.
Structural and Sequence Similarities among Toxins
Ho¨fte and Whiteley (164) drew attention to the five blocks
of amino acids conserved among most of the Cry toxins then
known. Complete amino acid sequence alignment of the Cry
proteins in our data set reveals the same five tracts, or conserved
blocks, in most of them (Fig. 2 and 3). Comparison of the carboxyl-terminal halves of sequences with more than
1,000 residues suggests the presence of three additional blocks
lying outside the active toxic core.
Figure 4 shows an unrooted phylogenetic tree, constructed
by an unweighted pair-group method using arithmetic averages
algorithm from the multiply aligned Cry and Cyt protein sequences.
Five sequence similarity groups are apparent, together
with a single outlying sequence (Cry15). The conserved
blocks are distributed in a fashion consistent with these similarity
groups. The group consisting of Cry1, Cry3, Cry4, Cry7 to
Cry10, Cry16, Cry17, Cry19, and Cry20 contains all five of the
core blocks. A second group consisting of Cry5, Cry12 to
Cry14, and Cry21 contains recognizable homologs of blocks 1,
2, 4, and 5. Block 1 shows more variability within this second
group of sequences than within the first. The proteins within
this second subgroup also possess a block 2 variant; block 2
sequences show greater sequence similarity within the two
groups than between them (Fig. 2). Block 3 is completely
absent from this second group of Cry proteins; an unrelated
sequence, highly conserved within the second subgroup but
absent from the first, lies between blocks 2 and 4. For both
groups, when a protein possesses the C-terminal extension,
blocks 6, 7, and 8 are invariably present (Fig. 2). Members of
a third sequence similarity group, composed of Cry2, Cry11,
and Cry18, possess block 1 and a truncated variant of the block
2 core (Fig. 2) but lack convincing homologs of the other
conserved blocks (215). An alternating arginine tract not otherwise
homologous to block 4 is found near the C terminus of
Cry11 and Cry18. A weak homolog of block 5 may also be
present among the proteins in this group, but its significance, if
any, is uncertain (Fig. 2). The other proteins in the data set—
Cyt1, Cyt2, Cry6, Cry15, and Cry22—have no recognizable
homologs to the conserved blocks seen in the three groups
noted above.
The conservation of blocks 1 through 5 is at least consistent
with the notion that the proteins within the first subgroup,
which includes Cry1 and Cry3, might adopt a similar threedomain
tertiary structure. It is possible, too, that the second
subgroup—Cry5, Cry12 to Cry14, and Cry21—could possess a
variation of the same structural theme. The degree of sequence
similarity found in the Cry2, Cry11, and Cry18 group of proteins
suggests that a fold similar to that in domain I of Cry3A
may be present. Indeed, the crystal structure of Cry2Aa, which
has been solved but not yet published (423a), confirms this
prediction. Somewhat more surprisingly, Cry2A also possesses
second and third domains strikingly similar to those of Cry3A,
despite the apparent absence of primary sequence homology
between the two proteins over this region.
Block 1 encompasses helix 5 of domain I. As mentioned
below (see “Structure-Function Interpretations”), this helix
has been implicated in pore formation, a role that might explain
its highly conserved nature. The central location of helix
5 within domain I also suggests an essential role in maintaining
the structural integrity of the helical bundle.
Block 2 includes helix 7 of domain I and the first b-strand of
domain II. These two structures comprise the region of contact
between the two domains. There are three structurally equivalent
salt bridges present between domain I and domain II in
Cry1Aa and Cry3A (148); the residues involved lie within block
2. These interactions could be important if domain I changes
its orientation relative to the rest of the molecule upon binding
of the toxin to its receptor. Alternatively, the salt bridges could
be responsible for maintaining the protein in a globular form
during solubilization and activation.
Blocks 3, 4, and 5 each lie on one of the three buried strands
within domain III. Block 3 contains the last b-strand of domain
II, a structure involved in interactions between domains I and
III. The central two arginines of block 4 may be involved in
intermolecular salt bridges affecting crystal or oligomeric aggregation
(148, 222). As Grochulski et al. have noted, however, the first and last arginines are solvent exposed (148). These
residues have been implicated in channel function (68, 336,
414).
An alternative way of looking at protein families is to examine
the relatedness of structural or functional segments independently
(47, 378). This type of analysis helped show a correlation
between domain II sequence features shared by
distantly related toxins and the cross-resistance profile of a
diamondback moth mutant (369).
Structure-Function Interpretations
The long hydrophobic and amphipathic helices of domain I
suggest that this domain might be responsible for the formation
of lytic pores in the intestinal epithelium of the target
organism, one of the proposed mechanisms of Cry toxin activity
(see “Mechanism of action”). Domain I bears many striking
similarities to the pore-forming or membrane-translocating domains
of several other bacterial protein toxins, including colicin
A, diphtheria toxin, and—to a lesser extent—Pseudomonas
exotoxin A (287). The pore-forming domain of colicin A consists
of two central alpha-helices (a8 and a9) surrounded by
eight antiparallel alpha-helices (288). Pore formation is believed
to involve insertion of the hydrophobic a8-a9 helical
hairpin into the membrane (101, 220). Similarly, diphtheria
toxin is believed to enter the membrane via a hydrophobic
helical hairpin following a pH-induced change in conformation
(432). By analogy to these mechanisms, an “umbrella” model
has been proposed, in which the Cry proteins also contain a
hydrophobic helical hairpin (a4-a5) that initiates pore formation
(222). Schwartz et al. (334) created disulfide bonds within
domain I and between domains I and II in order to restrict
intramolecular movements. Their results are consistent with
the model described above in which helices 4 and 5 insert into
the membrane while the rest of domain I flattens out on the
membrane surface in an umbrella-like molten globule state.
However, the lack of protein structural analysis in this work
leaves open the possibility that the disulfide bonds blocked the
ability of these mutant proteins to penetrate the membrane.
Similarly, little can be surmised as to the final structure of
the lytic pore; a structure involving amphipathic helices (with
the hydrophilic faces forming the lumen of the pore) seems the
most probable. Given, however, that most domain I helices are
largely amphipathic and theoretically long enough to span a
membrane, little can be concluded. Even helix 2, which is split
by a short nonhelical stretch, could traverse a membrane as
part of a channel. Comparison of the Cry3A domain I helices
with other known classes of amphipathic helices suggests that
many of the helices (in particular a1, a5, and a6) show features
characteristic of lytic peptides (378).
In contrast, Hodgman and Ellar (159) have proposed a
“penknife” model for pore formation. In this model, based on
the similarly named proposal for colicin A insertion (159), the
strongly hydrophobic helices a5 and a6, which are joined by a
loop at the top of the structure, open in a penknife fashion and
insert into the membrane. The remainder of the molecule
would remain at the membrane surface or on the receptor.
Both the umbrella and penknife models are reviewed and
illustrated by Knowles (185).
The surface-exposed loops at the apices of the three
b-sheets of domain II, because they show similarities to immunoglobin
antigen-binding sites, were initially put forward as
candidates for involvement in receptor binding. Site-directed
mutagenesis and segment swapping experiments, as described
under “Mechanism of action,” have provided evidence in support
of this model. It is interesting to note that domain II has
FIG. 4. Sequence similarity groups found among Cry and Cyt proteins. Sequences
were aligned by using CLUSTAL W and a phylogenetic tree was constructed
by NEIGHBOR as described in the accompanying work (79). The tree
was visualized as a radial phylogram by using the TREEVIEW application. The
proposed similarity groups are indicated by shading.
a fold similar to that of the plant lectin jacalin (330). Jacalin is
known to bind carbohydrates via the exposed loops at the apex
of its b-prism fold, whereas at least one Cry protein (Cry1Ac)
is believed to recognize carbohydrate moieties on its receptor
(188).
The b-sandwich structure of domain III could play a number
of key roles in the biochemistry of the toxin molecule. Li et al.
(222) suggest that domain III functions in maintaining the
structural integrity of the toxin molecule, perhaps by protecting
it from proteolysis within the gut of the target organism—but
of course all three domains would have to share this characteristic.
From studies in other systems where toxin-receptor
interaction leads to pore formation, it is known that b-strand
structures can participate in receptor binding (11, 71), membrane
penetration (283), and ion channel function (241, 242,
427). None of these roles has been ruled out for domain III of
Cry proteins; indeed, there is at least some evidence suggesting
a role for domain III in receptor binding in certain systems (see
“Mechanism of action” below).
Although solving the structure of one of the Cyt toxins has
not really clarified their toxic mechanism, the predominantly
b-sheet structure of Cyt2A suggests a pore based on a b-barrel
(223). Three of the strands are sufficiently long to span the
hydrophobic core of the membrane, and the sheet formed by
them shows an amphiphilic or hydrophobic character. Theoretically
the number of monomers required to form a barrel of
sufficient size would be four to six. Various laboratories (75,
243, 244) have observed that Cyt1A (which is believed to have
a common structure with Cyt2A) aggregates on the surface of
the target cell but not in solution prior to binding to the cell
surface. Using synthetic peptides, Gazit et al. (125) provided
further evidence that the Cyt1A toxin self-assembles within the
membrane and also identified two a-helices (A and C) that
appeared to be involved in both membrane interaction and
intermolecular assembly. Mathematical modeling hypothesized
that Cyt1A exists as a 12-toxin oligomer (243). No receptor-
binding motif could be identified in the Cyt2A structure,
although the use of monoclonal antibodies has identified a
putative cell binding region on Cyt1A (76). Using a number of
different biophysical techniques, Butko et al. (55) have also
studied the interaction of Cyt1A with lipid membranes. They
observed a considerable loosening of the tertiary structure of
the toxin upon lipid binding but could find no evidence that the
toxin actually enters the membrane. The authors suggest that
Cyt1A exerts its effect via a general, detergent-like perturbation
of the membrane.
MECHANISM OF ACTION
General Features
The mechanism of action of the B. thuringiensis Cry proteins
involves solubilization of the crystal in the insect midgut, proteolytic
processing of the protoxin by midgut proteases, binding
of the Cry toxin to midgut receptors, and insertion of the
toxin into the apical membrane to create ion channels or pores.
Crystals are comprised of protoxins. For the protoxins to become
active, a susceptible insect must eat them. For most
lepidopterans, protoxins are solubilized under the alkaline
conditions of the insect midgut (162). Differences in the extent
of solubilization sometimes explain differences in the degree of
toxicity among Cry proteins (18, 98). A reduction in solubility
is speculated to be one potential mechanism for insect resistance
(265). For at least one protein, Cry3A, nicking by chymotrypsin-
like enzymes in the midgut may be necessary for
solubilization (60).
After solubilization, many protoxins must be processed by
insect midgut proteases (203, 379) to become activated toxins.
The major proteases of the lepidopteran insect midgut are
trypsin-like (204, 270) or chymotrypsin-like (174, 280, 297).
The Cry1A protoxins are digested to a 65-kDa toxin protein in
a processive manner starting at the C terminus and proceeding
toward the 55- to 65-kDa toxic core (69, 73). The carboxyterminal
end of the protoxin, which initially appears to be
wound around the toxin in an escargot-like manner, is clipped
off processively in 10-kDa sections during processing of the
protoxin (74). An interesting and unexpected finding is that
DNA is intimately associated with the crystal and appears to
play a role in proteolytic processing (38, 76a). The mature
Cry1A toxin is cleaved at R28 at the amino-terminal end (277);
Cry1Ac, at least, is cleaved at K623 on the carboxy-terminal
end (37). Two stages of processing have been detected for
Cry1Ia with trypsin or Ostrinia nubilalis midgut proteases: a
fully toxic intermediate, with an N terminus at protoxin residue
45 and a C terminus at residue 655 or 659, is further processed
to a partially toxic core, with an N terminus clipped to residue
156 (340).
Activated Cry toxins have two known functions, receptor
binding and ion channel activity. The activated toxin binds
readily to specific receptors on the apical brush border of the
midgut microvillae of susceptible insects (161–163). Binding is
a two-stage process involving reversible (161, 162) and irreversible
(166, 307, 395) steps. The latter steps may involve a
tight binding between the toxin and receptor, insertion of the
toxin into the apical membrane, or both. It has been generally
assumed that irreversible binding is exclusively associated with
membrane insertion (166, 307, 395). Certainly the recent report
that truncated Cry1Ab molecules containing only domains
II and III can still bind to midgut receptors, but only reversibly,
supports the notion that irreversible binding requires the insertion
of domain I (116). Yet at least some published data is
consistent with the notion of tight binding to purified receptors.
Tight binding of Cry1Aa and Cry1Ab to purified Manduca
sexta aminopeptidase N (APN) has been observed (256), and
Cry1Ac may also show some degree of irreversible binding to
M. sexta APN. There are likewise indications of irreversible
binding for Cry1Ac to purified Lymantria dispar APN (172,
389). Finally, Vadlamudi et al. (385) calculated similar binding
constants when toxin bound to brush border membrane vesicles
(BBMV) and to nitrocellulose-immobilized receptor (i.e.,
a ligand blot).
In M. sexta, the Cry1Ab receptor is believed to be a cadherin-
like 210-kDa membrane protein (119, 180, 385), while
the Cry1Ac and Cry1C receptors have been identified as APN
proteins with molecular masses of 120 and 106 kDa, respectively
(183, 234, 329). Incorporation of purified 120-kDa APN
into planar lipid bilayers catalyzed channel formation by
Cry1Aa, Cry1Ac, and Cry1C (335). These receptor assignments
can be difficult to reconcile with some ligand blot binding
data, however (90, 208). There is also some evidence that
domain II from either Cry1Ab or Cry1Ac can promote binding
to the larger protein, while domain III of Cry1Ac promotes
binding to the presumed APN (91). Alkaline phosphatase has
also been proposed to be a Cry1Ac receptor (329). The recent
cloning of the putative 210-kDa (386) and 120-kDa (184)
Cry1Ac receptors opens exciting possibilities for studies on
toxin-receptor interactions. In Heliothis virescens, three aminopeptidases
bound to Cry1Ac on toxin affinity columns. One of
them, a 170-kDa APN, bound Cry1Aa, Cry1Ab, and Cry1Ac,
but not Cry1C or Cry1E. N-Acetylgalactosamine inhibited the
binding of Cry1Ac but not that of Cry1Aa or Cry1Ab. The
three Cry1A toxins each recognized a high-affinity and a low- affinity binding site on this 170-kDa APN (235). In gypsy moth
(L. dispar), the Cry1Ac receptor also seems to be APN, while
Cry1Aa and Cry1Ab bind to a 210-kDa brush border membrane
vesicle (BBMV) protein (388, 389). In Plutella xylostella
(236) and Bombyx mori (425) as well, APN appears to function
as a Cry1Ac binding protein. An M. sexta gene encoding a
Cry1Ab-binding APN has also been cloned, as has its P. xylostella
homolog (92).
Insertion into the apical membrane of the columnar epithelial
cells follows the initial receptor-mediated binding, rendering
the toxin insensitive to proteases and monoclonal antibodies
(415) and inducing ion channels or nonspecific pores in the
target membrane. In vitro electrophysiological studies of voltage-
clamping of lipid bilayers (338, 348) and sections of whole
insect midguts (67, 68, 153, 225, 307) support the functional
role of the toxin in pore or ion channel formation. The nature
of the ion channel or pore-forming activity of Cry toxins in the
insect is still controversial. It is alternatively described as a
large lytic pore that is not specific for particular ions (see
reference 187 and “Structure-function interpretations”) or as
an ion-specific channel that disrupts the membrane potential
but does not necessarily lyse midgut epithelial cells (see below).
Several recent reviews have considered the mechanism or
mode of action of Cry toxins (126, 134, 158, 185, 186, 378, 412,
424). Some of these reviews have presented models for the
mode of action. The present review considers the newest primary
data on receptor binding and ion channel activity and
critically evaluates the extant models.
General Receptor Binding and Kinetic Considerations
Soon after methods were developed for preparing insect
BBMV (411), BBMV became the subjects of toxin binding
studies (323, 413). Several groups were able to correlate a
toxin’s insect specificity with its affinity for specific receptors on
BBMV of susceptible insects (162, 163, 395). In vivo experiments
have also confirmed that Cry proteins bind to microvillae
in the midgut (49, 93, 426).
A set of in vitro-constructed reciprocal recombinants between
Cry1Aa and Cry1Ac (130, 131) provided evidence that
insect specificity was localized in the central domain of the
toxin for some insects (B. mori and Trichoplusia ni) and the
central and C-terminal domains for others (H. virescens). Visser
et al. (397) reviewed the use of domain substitutions to
locate specificity regions. Van Rie et al. (395) demonstrated
that receptor binding correlated with insect specificity, and Lee
et al. (209) demonstrated that the specificity and binding domains
were colinear for Cry1Aa against B. mori. Examination
of the crystal structure of Cry3A (222) suggested a physical
basis for receptor binding (see “Toxin structure,” above) by the
loops of domain II. This suggestion has now been substantiated
by site-directed mutagenesis.
Early work by Hoffman et al. (162), Van Rie et al. (395), and
others employed competition binding studies to demonstrate a
correlation between toxin affinity and insecticidal activity. In a
paradoxical finding, however, Wolfersberger (413) observed
that Cry1Ab was more active than Cry1Ac against gypsy moth
larvae, despite exhibiting a relatively weaker binding affinity.
Other examples of this phenomenon—a lack of correlation
between receptor binding affinity and insecticidal activity—are
now known (123, 327, 395). Liang et al. (224) evaluated binding
affinity and dissociation (both reversible and irreversible
binding) of Cry1Aa, Cry1Ab, and Cry1Ac with gypsy moth
BBMV. While they confirmed that the affinity of Cry1Ab was
not directly related to toxin activity, they did observe a direct correlation between the irreversible binding rate and toxicity.
Ihara et al. had earlier stressed the importance of considering
irreversible binding in explaining the difference in toxicity of
Cry1Aa and Cry1Ab to B. mori (166).
Prior to the work of Liang et al. (224), kinetic analysis of Cry
toxin-receptor binding relied on the Hill (161) or Scatchard
(395) equations that assume a strictly reversible binding:
where T is a Cry toxin, R is a receptor for this toxin, T[R is a
toxin that is reversibly bound to the receptor, Kd1 is the dissociation
constant k1 is the on rate, and k21 is the off rate.
In reality, the toxin becomes irreversibly associated with the
apical membrane by insertion (415), giving the following kinetic
diagram (224) (including two models for the inserted
state of the toxin):
where T, R, and T[R are as described for equation 1; *T is an
irreversibly bound toxin, presumably inserted into the membrane
but not associated with a receptor; and *TR is an irreversibly
bound toxin which is still associated with a receptor.
Given the irreversible rate component k2, the reaction cannot
reach equilibrium; as the toxin-receptor complex is formed,
it is drained away by insertion. Therefore, competition or binding
experiments under conditions where insertion can take
place (equation 2) do not yield true Kd values (224). Since
equilibrium conditions are not obtained, equation 2 should not
be considered any more valid for calculation of a classical
dissociation constant, Kd, than equation 1. Alternate values,
such as the 50% inhibitory concentration (224, 257) or Kcom,
the so-called competition constant (206, 208, 308, 422), have
been used for Kd under these conditions. Under some conditions
insertion should not occur, i.e., ligand blotting of 125Ilabeled
Cry1Ac to purified gypsy moth 120-kDa receptor (207)
or binding of unlabeled Cry1Ac to purified M. sexta 120-kDa
receptor fixed to dextran surfaces in surface plasmon resonance
analysis (256). In both cases, the calculated Kd was 100
times that obtained with BBMV, suggesting that the effect of k2
upon the reversible reaction is considerable. In contrast, competition
binding of Cry1Ab to the 210-kDa receptor on a ligand
blot differed little from calculated competition binding to M.
sexta BBMV (385) or to the cloned 210-kDa receptor expressed
in human embryonic 293 cells (386) (708 pM, 1,000
pM, and 1,015 pM, respectively). It may be that the rate of
insertion, k2, is negligible for the 210-kDa receptor, perhaps
due to either extremely tight binding to this receptor or a
failure to insert.
Role of Domain II Loop Regions
The prediction that domain II is involved in receptor binding
(131, 222) has led to extensive substitution of loop residues in
this domain in Cry3A, Cry1A, and Cry1C by mutagenesis (Fig.
5). Data on the effects of mutations in sequences encoding
domain II loop regions of selected Cry toxins are summarized
in Table 1. Perusal of these data indicates that mutations may
have either a negative or positive effect on binding and toxicity
and that mutations in different loop regions, sometimes involving
the same type of amino acid residue, can have a different
effect on binding. Minor changes in binding usually do not have
a major effect on toxicity, but a major positive or negative effect has a corresponding positive or negative effect on toxicity.
Furthermore, either binding affinity (as measured by competition
binding) or irreversible binding may effect toxicity, and for
a few mutant proteins one of these parameters may be positive
(increased affinity) while the other may be negative (increased
dissociation), with an overall negative effect on toxicity. It is
apparent that the same mutation in a toxin can have quite
different results on different insects. A more complete description
of domain II loop mutations is given in a recent review
(311).
In summary, the binding picture for domain II is complex.
Results clearly suggest that all of the loops of domain II can
participate in receptor binding, although perhaps not all at the
same time for a given insect or receptor. Different toxins may
have the same amino acid sequence in the loops of domain II
(e.g., Cry1Ab and Cry1Ac) yet bind to different receptors, at
least on ligand blots. The available data seem to show an
intriguing similarity between the receptor binding loops of
domain II and other known protein-protein epitopes; i.e., a
hydrophobic residue capable of tight binding to the receptor is
surrounded by hydrophobic or charged residues. Similar interactions
have been noted in several other systems (for a general
review, see reference 300). A striking demonstration of the
importance of a hydrophobic residue in irreversible binding
was a series of mutations in F371 of Cry1Ab loop 2 to residues
of lower hydrophobicity. This reduction in hydrophobicity was
correlated with the gradient of reduced irreversible binding
and toxicity (309).
Not included above is a discussion of work on two putative
surface loops of domain II of Cry1C (loop 1, 317GRNF320, and
loop 2, 374QPWP377) (350). This study did not evaluate the
effect of mutational alteration of loop residues on binding, but
examined cytotoxicity with cultured Spodoptera Sf9 cells and
toxicity with Aedes aegypti larvae. The results indicated that
specificity differences for Cry1C between Sf9 cells and A. aegypti
larvae could be changed radically by single point mutations
in the loops. For example, an R-to-I mutation at position
318 (R318I) abolished mosquitocidal activity but retained 80%
cytotoxicity to Sf9 cells. Likewise, several mutations caused a
loss of mosquitocidal activity with only a marginal loss of cytolytic
activity against Sf9 cells. Substitutions that altered the
charge, such as Q374E, completely abolished activity against
both cells and mosquito larvae.
Role of Domain III in Receptor Binding
Domain III has also been implicated in receptor binding. As
mentioned above, several groups (130, 331) have suggested a
role for domain III of Cry1Ac in H. virescens specificity. Masson
et al. (258) extended the suggestion to include CF-1 cells.
Aronson et al. (19) mutated a hypervariable region of domain
III (residues 500 to 509) of Cry1Ac. Mutations S503A and
S504A resulted in lower toxicity to M. sexta, with a corresponding
decrease in binding to BBMV proteins on ligand blots. Lee
et al. (211) analyzed homolog scanning mutants that exchanged
domain III between Cry1Aa and Cry1Ac. Hybrid proteins
containing the Cry1Aa domain III bound a 210-kDa receptor
while hybrid proteins containing the Cry1Ac domain III
bound a 120-kDa receptor in gypsy moth. Domain switching
experiments have also suggested a role for Cry1Ab domain III
in binding to S. exigua (90). Finally, there is one report suggesting
a biotin-binding activity for domain III (99), although a
role for this activity in receptor binding has not been demonstrated
directly.
Membrane Insertion
Mutations in domain I have been shown to affect the ability
of the toxin to dissociate from the binding complex. Wu and
Aronson (419) created several mutations in domain I of
Cry1Ac. The A92D and R93G mutations (at the base of a3)
dramatically reduced toxicity to M. sexta. A loss of toxicity by
the A92D mutation was also observed in Cry1Aa and Cry1Ab.
A series of substitution residues at the 92 and 93 positions
revealed that at position 92 only a negatively charged residue
caused a loss of toxicity. Any substitution of R93 except the
positively charged Lys caused a loss of toxicity. The authors
concluded that a positively charged surface is important for
toxicity. Chen et al. (67) repeated the mutation at the A92
position in Cry1Ab with A92E. In agreement with Wu and
Aronson’s result (419), toxicity was almost completely lost.
Although competition binding of the mutant toxin to M. sexta
was not affected, irreversible binding was severely disrupted.
Chen et al. (67) further demonstrated that Y153 mutations (at
the loop between the bottoms of a4 and a5, on the same
surface as A92E) introducing a negative charge had a negative
effect on membrane insertion.
In summary, binding studies reveal three types of mutants.
Certain mutations in domain II (A mutants) affect competition
but not dissociation. Examples are Cry1Ab 368RRP370 (309)
and Cry1Ab loop 3 mutations F440A and G439A (310). Certain
other mutations in domain II (B mutants) affect dissociation
but not competition. Examples are Cry1Ab F371A (and most
other substitutions except Trp) and G439A (307). In domain I,
certain mutations (C mutants) affect insertion of toxin into the
membrane. The distinction between B and C mutants may be
arbitrary; it assumes different functions for domains I and II, a
point still lacking definitive proof. Examples of C mutants are
Cry1Ac A92D or R93G (419) and Cry1Ab A92E or Y153D (67).
In the above cases, all of these effects were observed in the
same toxin (Cry1Ab) and insect (M. sexta) system. Cry3A loop
3 mutants have also been described in which effects on both
competition and dissociation were observed (422).
Masson et al. (256) describe differences in off rates for two
Cry1Ac toxins that differ in three residues: L366F, F439S, and a
deletion of D442. While these differences might be due to other
causes, it is interesting that position 366 and positions 439 to
442 occur in loops 2 and 3, respectively. Wells (402) describes
human growth hormone mutants in which alanine substitution
of positively charged residues affects on rates, and other alanine-
scanning mutants in large hydrophobic residues affect off
rates. A similar pattern is observed in the Cry toxin mutations
of the receptor binding loops. Positive residues may be involved
in long-range orientation of the toxin to the receptor,
affecting the on rate. In some cases, large hydrophobic residues
were involved in tight binding, and their mutants affected the
off rate; in other cases, mutations in large hydrophobic residues
affected competition binding (that is, on rates).
Ion Channel Activity
The ion channel activity of Cry toxins has been explored by
a wide variety of techniques. The toxin has been studied with
complete proteins, with domain I in isolation, with synthetic
peptides mimicking particular a-helices, and with mutants that
disrupt ion channel function.
Considerable work has been reported on the effects of Cry
toxins on insect tissue culture cells. Work with CF-1 cells has
led to the colloidal osmotic lysis model for the cytolytic activity
of Cry toxins (187). This model proposes that an influx of
water, along with ions, results in cell swelling and eventually
lysis. When exposed to microgram amounts of activated toxin,
cells leaked a variety of electrolytes tested, including CrO4
22,
uridine, and Rb1. Under these conditions, then, Cry toxins
form a nonspecific pore. Wolfersberger (412) lists the problems
that arise from experiments with established cell cultures.
The cells are normally maintained at a pH of 6.8—not the basic
pH found in the lumen of many insect midguts. They lack
normal midgut receptors (161) and do not respond as specifically
to toxins as does the whole insect (410). They are tolerant
to nearly 1,000-fold-greater levels of toxin than insects under
physiological conditions (187). From experiments on tissue
culture cells it is clear, however, that Cry toxins have a fairly
general capacity to insert into membranes and form large,
nonspecific pores under certain conditions, including hightoxin
concentrations, long incubation times, and relatively low
pHs.
Several techniques have been employed to study the ion
channel activity of the B. thuringiensis Cry proteins. Harvey and
Wolfersberger (153) used electrophysiological analysis of sections
of whole midgut of M. sexta to measure short circuit current inhibition (ISC). The mechanism of ISC is explained in
the excellent review by Wolfersberger (412). Results of recent
studies (67, 68), using nanomolar concentrations of toxin, have
supported the validity of the voltage clamping technique as an
assessment of Cry toxin activity correlating well with bioassays.
Several groups have examined Cry toxin ion channel activity
in planar lipid bilayer (PLB) systems. Slatin et al. (348) examined
Cry1Ac and Cry3A in PLB membranes of various compositions
and found that toxins formed cation-selective channels.
Cry1Ac ion channels exhibited multiple opening and
closing states (indicating more than one single-channel conductance
level or cooperative gating). Cry1Ac channels were
commonly 600 pS in size (in 300 mM KCl), while Cry3A
formed larger channels of 4,000 pS. Channels did not form at
pH 7 but did form at pH 9.7.
In a pivotal paper on Cry protein ion channel activity,
Schwartz et al. (338) reported a pH effect on the type and size
of ion channels made by Cry1C in PLBs. Under alkaline conditions
(pH 9.5), cationic channels of 100 to 200 pS were
formed, exhibiting multiple conductance states. Under acidic
conditions (pH 6.0), anionic channels of different sizes (8 to
120 pS) were observed. These channels were inhibited by zinc
added to the cis chamber, but not to the trans chamber, indicating
directionality of the channel. The authors note that
behavior of the toxins at pH 6 is similar to that recorded in
native membranes of cultured insect cells (grown at pH 6.3)
(337). This observation may clarify the nonselectivity of Cry
proteins on cultured insect cells (187). The physical basis of
pH-dependent selectivity may be related to the observation
that a-helical content, as measured by circular dichroism,
changes radically with pH (72, 111, 189). It is speculated that
pH can alter the pitch or arrangement of the a-helices of
domain I and change the nature of the ion channel. In general,
the role of pH in ion specificity is thought to be by titration of
charged amino acids lining the aqueous pore, but pH changes
on Cry channels have global effects on ion specificity and pore
size.
Channel formation in PLBs has also been observed with
N-terminal fragments (essentially domain I) of Cry1Ac (399)
and Cry3Bb (398), and with a5 helix peptides of Cry1Ac (80)
and Cry3A (127, 128). The a7 helix alone did not form channels,
but in the presence of the a5 helix it assembled and
penetrated membranes better than did a5 complexes alone
(126). Channels formed by the a5 helix, unlike those formed by
full-length toxins, are small (60 pS) and hemolytic (127) and
prefer acidic phospholipid vesicles (80, 127). The channels
formed with Cry1Ac N-terminal fragments differed from those
formed by whole toxins in having only a single conductance
state, being less cation selective, and showing no toxicity to
whole insects. They did, however, have similar conductance
levels (200 to 600 pS). They also exhibited twice the Rb1 efflux
from phospholipid vesicles as did full-length toxins (399). In
contrast, N-terminal fragments of Cry3Bb were quantitatively
similar to the full-length toxin, but exhibited less Rb1 efflux
than full-length toxins with phospholipid vesicles. In summary,
these results show qualitative support for the model that domain
I constitutes, or at least participates in, the ion channel.
Domain III has also been reported to play a role in ion
channel activity. Chen et al. (68) analyzed an alternating arginine
region in b-sheet 17 (conserved block 4), a sequence
superficially similar to the positively charged face on the S-4
helix in classical ion channels. While alteration of the central
arginines caused structural alterations in Cry1Aa, conservative
substitutions of the outermost arginines were stable and led to
reduction of activity, as measured by bioassays and by voltage
clamping of M. sexta midgut sections. These altered toxins were
also examined by the BBMV permeability-light scattering assay
(414) and in lipid bilayers for conductance (336). Both
methods detect an alteration of ion channel activity caused by
these conservative alterations in this b-sheet of domain III.
Reconstitution systems involving BBMV fused with lipid
bilayers have been recently reported from two laboratories.
Martin and Wolfersberger (254) measured Cry1Ac channels in
PLBs that were fused with M. sexta BBMV. The addition of 1.5
nM of toxin resulted in very large channels (.260 nS) at pH
9.6. The smallest toxin-dependent increase in conductance was
13 nS, which may represent a single membrane pore. Thus,
these channels were capable of very large changes in conductance
state (in 13-nS increments) but were never observed to
close. Channel behavior was also pH dependent. At pH 8.8,
smaller channels of 2 to 3 nS were observed. The authors
concluded that pores of the largest size would be 2.2 nm in
diameter (more than twice the diameter previously measured
in bilayers), and that such differences in properties favor active
involvement of BBMV proteins in the pore formation. More
recently Carroll and Ellar (62) measured the size changes of M.
sexta BBMV in an environment of high osmotic pressure and
high Cry1Ac concentrations. The rate of Cry1Ac-induced
swelling varied with the radius of the solutes used, allowing for
an estimate of Cry1Ac pore size. Under these conditions, large
pores were formed (2.4 nm at pH 8.7 and 2.6 nm at pH 9.8).
Lorence et al. (230) also have reported intrinsic ion channels
in S. frugiperda BBMV. These cationic channels were small (31,
47, and 76 pS), of low selectivity (permeability relative to K1 is
.80% for Na1, Li1, Cs1, Rb1, and NH4
1), and were inhibited
by standard channel blockers. The addition of Cry1C or
Cry1D toxin resulted in large cationic channels of 50, 106, and
360 pS that showed greater K1 selectivity but were not exclusively
K1 channels. The Cry1D channels formed in whole S.
frugiperda BBMV were reported to be blocked by Ba1 and
Ca21 and less so by triethanolamine, in agreement with an
earlier report on the blocking of inhibition of ISC on M. sexta
midguts (77). These experiments were performed at pH 9.0; no
anionic channels were observed under these conditions. The
latter result differs from light scattering results from M. sexta
BBMV with Cry1Ac at pH 7.5 (61). Interestingly, while the
insecticidal activity against first-instar S. frugiperda for Cry1C
was greater than that for Cry1D, the channel-forming activities
for Cry1C and Cry1D on BBMV taken from second-instar
larvae were equal and that for Cry1C was less than that for
Cry1D on BBMV from fifth-instar larvae. Clearly the fused
BBMV-lipid bilayer studies raise interesting questions and
open new avenues for understanding Cry toxin action.
Mutants with Enhanced Activity
A primary goal of protein engineering of the Cry proteins is
to create better pesticides through rational design. A few examples
of this effort are now starting to appear. A mutation
(H168R) in helix a5 of Cry1Ac, domain I, caused a twofold
increase in toxicity against M. sexta (419). Further characterization
of this mutant (165) revealed that the increased toxicity
was correlated with the rate of irreversible binding (kobs). Jellis
et al. (171) have also described multiple mutations in domain
I that increased toxicity; however, the mechanism of action of
these mutants has not been addressed. An R204A mutation in
domain I of Cry4B resulted in a threefold increase in activity
against mosquitoes, perhaps by removing a site of proteolytic
instability (16).
Several mutations in domain II have led to increased toxicity.
Loop 3 (481MQGSRG486) of domain II Cry3A was mutated
to alanines, and a 2.4-fold increase in toxicity against Tenebrio molitor was observed (422). An increase in irreversible binding
was correlated with this increase in toxicity. Other mutations in
loop 1 of Cry3A have significantly improved toxicity against T.
molitor (11.4-fold); Chrysomela scripta, cottonwood leaf beetle
(2.5-fold); and Leptinotarsa decemlineata, Colorado potato
beetle (1.9-fold) (423). An increase in irreversible binding was
correlated with the increase in toxicity for these mutants as
well. In Cry1Ab, a combination of mutations in the a8 loop and
loop 2 resulted in a 32-fold increase in toxicity to L. dispar over
the background gene product and a 4-fold improvement over
the previously best-known gene product (Cry1Aa) (308). The
mechanism of increase in toxicity is correlated to improvement
in initial binding affinity in this case.
In summary, the B. thuringiensis Cry protein behaves as a
bona fide ion channel in lipid bilayers and in the midgut epithelium.
As such it represents one of the few ion channels that
has a known structure. The contradictory results and confusion
concerning the selectivity and size of the pore may be due to
the range of experimental conditions employed but more importantly
may reflect the adaptability of the toxin to different
physiological conditions which exist in its functional environments.
In the alkaline midgut, the toxin may function as a
cation channel (338), taking advantage of the large K1 gradient
that exists in some insect midgut environments. As the pH
falls due to cell lysis or leakage, the toxin may function as an
anion channel (338), further wounding the epithelial cells. In
large amounts, the Cry protein may form very large leakage
pores, resulting in cell lysis and disruption of the midgut epithelium.
Continued intensive research effort, now under way,
will clarify the mechanism of action of the Cry proteins.
Effect of Synergistic Interactions on Toxin Potency
B. thuringiensis subsp. israelensis. Wu and Chang (420) were
the first to observe that when protein fractions from the purified
inclusion body of B. thuringiensis subsp. israelensis were
mixed and assayed against A. aegypti larvae, the activity of
some combinations was greater than would have been expected
from the activity of the individual fractions. Other reports
followed, confirming synergistic interactions among various
toxins of B. thuringiensis subsp. israelensis (15, 64, 70, 78,
85, 303, 421). In evaluating these studies, it is difficult to establish
the precise contribution of each toxin (either alone or in
combination) towards the overall toxicity of the inclusion. Part
of the problem is the large variation in reported toxicities for
individual toxins, probably due to differences in experimental
conditions. Complicating factors include host-dependent differences
in the size, quality, and solubility of crystals among the
various expression systems used (15); differences in presenting
the proteins to the larvae (soluble or reprecipitated form);
variation in bioassay conditions, including larval age and diet;
and natural variation in insect populations (317).
A recent study (78) attempted to overcome these problems
by assaying the toxins under constant experimental conditions.
From these data, it can be deduced that the order of relative
activities of the individual toxins against A. aegypti larvae
(based on the 50% lethal concentration [LC50]) is (from greatest
to least) Cry11A, Cry4B, Cry4A, and Cyt1A. Synergistic
interactions were demonstrated with all combinations of toxins
used, although the extent of this interaction was dependent on
the combination. No combination, however, was as active as
was the native B. thuringiensis var. israelensis inclusion. There
might be additional factors important for toxicity associated
with the native crystal. It is also possible that native crystals
might be ingested or solubilized more efficiently than those
from the recombinant strains are. Additionally, the presentation
of all four toxins in a single crystal might be more efficient
than a mixture of four inclusions.
In an alternative approach to study the relative contributions
of the B. thuringiensis var. israelensis toxins to the overall toxicity,
strains have been made in which either the cry11A gene or
the cyt1A gene were genetically inactivated. The effect of inactivating
cry11A (301) was to halve the toxicity of the resulting
strain to A. aegypti larvae. In contrast, inactivating the cyt1A
gene (84) produced a strain with similar toxicity to the native
strain, suggesting that Cyt1A was not essential for mosquitocidal
activity. In interpreting those results, however, one
should keep in mind the relative activities of the individual
toxins (78). If the crystals produced by the cyt1A null mutant
contain relatively greater proportions of the more active toxins
than those found in wild-type crystals, one would expect the
mutant strain to be considerably more toxic than the wild-type
strain. The fact that the presence of Cyt1A in crystals does not
dilute their potency suggests that this protein is indeed an
important component of the B. thuringiensis subsp. israelensis
mosquitocidal arsenal. As such, Cyt1A may provide a redundant
set of synergistic interactions.
Little is known about the mechanism of this synergistic interaction.
A comparison of the dose-response curves for the
individual B. thuringiensis subsp. israelensis toxins (78) shows a
clear difference between Cyt1A and the Cry toxins. Thus,
Cyt1A may act in a different way than the Cry toxins. Cyt1A
has a completely different structure than the Cry toxins (223)
and appears to interact with a different type of receptor (375).
Ravoahangimalala and Charles (312) found that Cyt1A, when
added alone to midgut tissue sections of Anopheles gambiae,
bound to the microvilli of all midgut and anterior stomach cells
(with the exception of the peritrophic membrane-secreting cardia
cells). In contrast, the Cry toxins bound only weakly to
anterior stomach cells. When the complete set of B. thuringiensis
subsp. israelensis toxins were added to insects in vivo, Cyt1A
was not found to be bound to the anterior stomach cells (313).
Although this negative result could have been an artifact, it
might also represent a strong association between the Cry and
Cyt toxins that could form the basis of a synergistic interaction.
An additional consequence of this synergism is discussed under
“Resistance Management” below.
Much of the work discussed above was concerned with activity
against A. aegypti larvae. Synergism has also been established
between different toxin combinations against both Culex
pipiens and Anopheles stephensi (85, 303).
Other B. thuringiensis strains. Synergistic interactions between
toxins other than those from B. thuringiensis subsp. israelensis
were reported in 1991 by van Frankenhuyzen et al.
(393). Interactions were observed between the individual Cry1
toxins of HD-1 against a number of forest-defoliating insects.
The data presented in that report (393) were later reevaluated
by Tabashnik (363), who applied a more rigorous mathematical
treatment to the toxicity data and concluded that synergism
could not, in fact, be satisfactorily demonstrated. Recently,
however, synergism has been observed between Cry1 proteins.
The relative toxicities of Cry1Aa, Cry1Ab, and Cry1Ac against
L. dispar and B. mori were investigated in force-feeding experiments
(207). While synergism was observed between Cry1Aa
and Cry1Ac for L. dispar by using the mathematical approach
of Tabashnik (363), an antagonistic effect was exhibited between
Cry1Aa and Cry1Ab. No synergistic effect on B. mori
was observed with any toxin combination. The authors also
noted that synergistic interactions were observed both in the
bioassay and in ISC. The authors speculated that the pores
formed by different toxins act in a cooperative way or that a
more efficient pore is formed from a hetero-oligomer of dif- ferent toxins. The presence of certain toxins might enhance the
activity of another by preventing nonproductive binding. Whatever
the actual mechanism, it is clear that the interaction is
insect specific, a fact that may reflect differences in receptor
affinities for each toxin.
In addition to synergistic interactions between different toxins,
similar potentiating effects on toxicity have been observed
between certain toxins and spores (85, 100, 173, 271, 273, 372)
and also between toxins and other bacteria (100). In each case,
septicemia caused by the spores or bacteria infecting the insect,
whose midgut has become ulcerated as a result of the toxin, is
believed to be the cause of this observed synergism. In addition,
the presence of the B. thuringiensis spore with the Cry
proteins may even reduce the likelihood of insect resistance
development in some instances (272).
BIOTECHNOLOGY OF B. THURINGIENSIS
Application of Cry Proteins for Pest Control
and Plant Protection
B. thuringiensis is now the most widely used biologically
produced pest control agent. In 1995, worldwide sales of B.
thuringiensis were projected at $90 million (353), representing
about 2% of the total global insecticide market (199). Rowe et
al. (322) reported that the annual worldwide distribution of B.
thuringiensis amounts to 2.3 3 106 kg. As of early 1998, there
were nearly 200 registered B. thuringiensis products in the
United States (Table 2) (381). While the use of biological
pesticides in agriculture remains significantly behind that of
synthetic chemical pesticides, several environmental and safety
considerations favor the future development of B. thuringiensis.
Cry proteins that have been studied thus far are not pathogenic
to mammals, birds, amphibians, or reptiles, but are very specific
to the groups of insects and invertebrate pests against
which they have activity. Cry-based pesticides generally have
low costs for development and registration. B. thuringiensis
subsp. israelensis, for example, had a development cost estimated
at 1/40 that of a comparable novel synthetic chemical
pesticide (32). Finally, the mode of action for the Cry proteins
differs completely from the modes of action of known synthetic
chemical pesticides, making Cry proteins key components of
integrated pest management strategies aimed at preserving
natural enemies of pests and managing insect resistance.
Forestry
The transfer of emphasis to environmentally friendly pesticides
that have minimal effects on natural enemies of Lepidoptera
(14) has already begun in the forests of the United States,
where B. thuringiensis has become the major pesticide used
against the gypsy moth (239). B. thuringiensis products for the
forest industry have been based primarily on B. thuringiensis
HD-1 subsp. kurstaki (102), which produces Cry1Aa, Cry1Ab, Cry1Ac, and Cry2Aa toxins. The gypsy moth is by no means the
only forest pest that can be controlled successfully with B.
thuringiensis (392, 393). Currently targeted pests include the
spruce budworm (Canada), the nun moth (Poland), the Asian
gypsy moth (United States, Canada, and the Far East), the
pine processionary moth (Spain and France), and the European
pine shoot moth (South America) (46).
Control of Mosquitoes and Blackflies
Since its discovery in 1977 (136), B. thuringiensis subsp. israelensis
has proved to be one of the most effective and potent
biological pesticides (for reviews, see references 32 and 81). Its
discovery came at an auspicious moment because of the
mounting resistance of mosquitoes and blackflies to synthetic
chemical pesticides. Five B. thuringiensis subsp. israelensis cry
and cyt genes encode dipteran-active toxins: cry4A, cry4B,
cry10A, cry11A, and cyt1A (cytolysin). In addition, the Cyt1A
cytolysin may synergize the activity of other Cry toxins (see
“Effect of synergistic interactions on toxin potency”). These
five genes are all found on a large plasmid of about 72 MDa
that can be transferred to other B. thuringiensis strains by a
conjugation-like process (137). Interestingly, this same set of
toxins has also been discovered in isolates from several other
B. thuringiensis serotypes (286), suggesting that the conjugation
process analyzed in the laboratory may have environmental
significance for horizontal transfer of cry genes among B. thuringiensis
populations.
Given the severe impact of mosquito- and blackfly-borne
human diseases, there is considerable interest in identifying
additional dipteran-active toxins. Mosquitocidal activity has
been reported for Cry2Aa (408), Cry1Ab (150, 151), and
Cry1Ca (352). The cytolytic Cyt1A and Cyt2A crystal proteins
also show some degree of dipteran specificity in vivo (191).
New mosquitocidal cry genes have also been recently reported
(e.g., cry11B and cry16A [85]), as well as several new isolates
containing uncharacterized cry genes with mosquitocidal activity
(289, 306). A surprising source of additional Cry-related
mosquitocidal proteins is the bacterium C. bifermentans subsp.
malaysia (23, 82), the toxins of which we have designated
Cry17A, Cry18A, and Cry19A in the accompanying paper (79).
Developing New Cry Biopesticides Based
on B. thuringiensis
B. thuringiensis has evolved to produce large quantities of
crystal proteins (for reviews, see references 8 and 30), making
it a logical host for developing improved Cry biopesticides.
Natural isolates of B. thuringiensis can produce several different
crystal proteins, each of which may exhibit different, perhaps
even undesirable, target specificity (164, 199). On the
other hand, certain combinations of Cry proteins have been
shown to exhibit synergistic effects (64, 78, 207, 303, 421).
Accordingly, genetic manipulation of B. thuringiensis—to create
combinations of genes more useful for a given purpose
than those known to occur in natural isolates—may be desirable.
A conjugation-like system has been used to transfer Cryencoding
plasmids from one strain to another (137), but most
cry genes are not readily transmissible by this process. Nevertheless,
a number of transconjugant and naturally occurring
strains producing Cry proteins distinct from those of B. thuringiensis
HD-1 subsp. kurstaki, including strains of B. thuringiensis
subsp. aizawai and B. thuringiensis subsp. morrisoni, have
been registered with the U.S. Environmental Protection
Agency.
A breakthrough development for engineering B. thuringiensis
and B. cereus came in 1989 when several groups independently
applied electroporation technology to transform vegetative
cells with plasmid DNA (34, 42, 214, 246, 259, 333).
These protocols differed in cell preparation methods, buffer
components, and electric pulse parameters, but each could
achieve frequencies of 102 to 105 transformants per mg of
plasmid DNA with a wide variety of hosts and vectors. Macaluso
and Mettus (238) added the important observation that
some B. thuringiensis strains restrict methylated DNA. Plasmid
DNA isolated from Bacillus megaterium or Dcm2 strains of E.
coli transformed B. thuringiensis with much higher frequencies
than did DNA isolated from B. subtilis or Dcm1 strains of E.
coli. Their data also provided evidence that several restriction
systems exist within the B. thuringiensis species. The use of
unmethylated DNA with the Macaluso and Mettus protocol
allows transformation frequencies as high as 3 3 106 to be
achieved.
A variety of shuttle vectors, some employing B. thuringiensis
plasmid replicons (17, 28, 63, 122), has been used to introduce
cloned cry genes into B. thuringiensis (124). Alternatively, integrational
vectors have been used to insert cry genes by homologous
recombination into resident plasmids (2, 219) or the
chromosome (176). Plasmid vector systems employing B. thuringiensis
site-specific recombination systems have been developed
to construct recombinant B. thuringiensis strains for new
bioinsecticide products (26, 29, 325, 326).
Homologous recombination has been used to create null
mutants in vivo. Applications of this technique have included
disruptions of cry and cyt genes to assess their contribution to
pesticidal activity (85, 301) and inactivation of protease production
genes to increase crystal production and stability (97,
370). Recent progress in understanding cry gene expression has
allowed the construction of asporogenous B. thuringiensis
strains that nevertheless produce crystals; these crystals remain
encapsulated in the mother cell compartment (48, 213). Much
remains unclear about the fate of naked Cry toxins in the
environment, although they appear to be quite sensitive to
degradation by natural soil microbes (404). It is a plausible but
untested hypothesis that encapsulation within the mother cell
can improve toxin persistence in sprayed applications.
Alternative Delivery Systems for Cry Proteins
Crystal genes were introduced into E. coli, B. subtilis, B.
megaterium, and Pseudomonas fluorescens long before there
was an efficient transformation system available for B. thuringiensis
(for a review, see reference 124). Fermentations of
recombinant pseudomonads have been used to produce concentrated
aqueous biopesticide formulations consisting of Cry
inclusions encapsulated in dead cells. These encapsulated
forms of the Cry proteins have been reported to show improved
persistence in the environment (121). Fermentations of
pseudomonads producing different Cry proteins can be combined
in a single formulation to expand the range of target
insects controlled. The production or activity of certain Cry
proteins in P. fluorescens has been improved by the use of
chimeric cry genes containing a substantial portion of the
Cry1Ab carboxyl-terminal region (376, 377). It is anticipated
that engineered forms of the Cry proteins showing improved
potency or yield, regardless of their host, will make Cry biopesticides
a more attractive and practical alternative to synthetic
chemical control agents.
The primary rationale for using live endophytic or epiphytic
bacteria as hosts is to prolong the persistence of Cry proteins
in the field by using a host that can propagate itself at the site
of feeding and continue to produce crystal protein. The cry1Ac gene, for example, has been introduced into the endophytic
bacterium Clavibacter xyli on an integrative plasmid (201), and
the resulting recombinant strain has been used to inoculate
corn for the control of European corn borer infestation (380).
Endophytic isolates of B. cereus have been used as hosts for the
cry2Aa gene (245), and a B. megaterium isolate that persists in
the phyllosphere (43) has been used as a host for cry1A genes.
Similarly, cry genes have been transferred into other plant
colonizers, including Azospirillum spp., Rhizobium leguminosarum,
Pseudomonas cepacia, and P. fluorescens (281, 282, 347,
361, 384). Alternative delivery systems have also been sought
for the dipteran-active toxins of B. thuringiensis subsp. israelensis
to increase their persistence in the aquatic feeding zone.
Such hosts include Bacillus sphaericus (22, 302), Caulobacter
crescentus (374), and the cyanobacteria Agmenellum quadruplicatum
(359) and Synechococcus spp. (355).
Expression of B. thuringiensis cry Genes in Plants
Several cry genes have been introduced into plants, starting
with tobacco (24, 387) and now including many major crop
species (5, 120, 193, 278, 294, 296, 391). Because this subject
has been well reviewed in recent years (107, 290), we will limit
our discussion to a few important points.
When unmodified crystal protein genes are fused with expression
signals used in the plant nucleus, protein production
is quite poor compared to that of similar transcription units
containing typical plant marker genes (390). Nucleus-directed
expression of full-length unmodified genes has been reported
for some plants (114, 115). However, truncation of the unmodified
genes to synthesize only the toxic portion of the protein
typically results in much improved, but still comparatively low,
expression (24, 114, 387).
The relatively A1T-rich Bacillus DNA contains a number of
sequences that could provide signals deleterious to gene expression
in plants, such as splice sites, poly(A) addition sites,
ATTTA sequences, mRNA degradation signals, and transcription
termination sites, as well as a codon usage biased away
from that used in plants. When the Bacillus sequences are
extensively modified, with synonymous codons to reduce or
eliminate the potentially deleterious sequences and generate a
codon bias more like that of a plant, expression improves
dramatically (5, 120, 193, 294, 296). In some cases, less extensive
changes in the coding region have also led to fairly dramatic
increases in expression (295, 390, 391). The study of van
Aarssen et al. (390) is noteworthy in that it points to fortuitous
splicing signals in the Bacillus coding region as being a significant
barrier to expression of cry1Ab in plants. In contrast to
expression from the nucleus, an unmodified cry1Ac gene was
expressed at very high levels in the chloroplasts of tobacco
(260).
The year 1996 marked a milestone in agricultural biotechnology:
for the first time, varieties of potato, cotton, and corn
containing modified cry genes were sold to growers. The production
of Cry proteins in planta can offer several benefits.
Because the toxins are produced continuously and apparently
persist for some time in plant tissue (345, 346), fewer applications
of other insecticides are needed, reducing field management
costs. Like B. thuringiensis-based biopesticides, such “enhanced
seed systems” are less harmful to the environment than
synthetic chemical insecticides and typically do not affect beneficial
(e.g., predatory and parasitic) insects. The plant delivery
system also expands the range of pests targeted for control with
Cry proteins, including sucking and boring insects, root-dwelling
insects, and nematodes.
In addition to concerns regarding the development of natural
resistance towards the B. thuringiensis toxins, the impact of
gene flow to wild relatives needs to be assessed. Preliminary
experiments documented the possibility of cross hybridization
among members of the family Brassicaceae and an increased
survivorship of Brassica napus with a B. thuringiensis transgene
under certain conditions (360). From these data it could be
inferred that transgenic B. napus may transfer its insecticidal B.
thuringiensis gene into wild relatives (360). However, analysis
with respect to the stable inheritance and expression of the insect-resistant phenotype in the offspring of any such hybrids
is needed to determine the likelihood and impact of such a
transfer.
Insect Resistance to B. thuringiensis Toxins
Laboratory-selected strains. Over 500 species of insects
have become resistant to one or multiple synthetic chemical
insecticides (132). In the past it was hoped that insects would
not develop resistance to B. thuringiensis toxins, since B. thuringiensis
and insects have coevolved. Starting in the mid-1980s,
however, a number of insect populations of several different
species with different levels of resistance to B. thuringiensis
crystal proteins were obtained by laboratory selection experiments,
using either laboratory-adapted insects or insects collected
from wild populations (112, 364). The degree of resistance
observed in an insect population is typically expressed as
the resistance ratio (number of LC50-resistant insects/number
of LC50-sensitive insects), and while resistance ratios determined
by different types of bioassay are correlated, they are
known to give different values (293), so that some care is
required in comparing results. Examples of laboratory-selected
insects resistant to individual Cry toxins include the Indianmeal
moth (Plodia interpunctella) (262), the almond moth
(Cadra cautella) (263), the Colorado potato beetle (Leptinotarsa
decemlineata) (406), the cottonwood leaf beetle (C.
scripta) (25), the cabbage looper (T. ni) (106), the cotton leafworm
(Spodoptera littoralis) (276), the beet armyworm (S. exigua)
(272), the tobacco budworm (H. virescens) (145, 210,
362), the European corn borer (O. nubilalis) (41), and the
mosquito Culex quinquefasciatus (133). Instances of resistance
discussed in the text below are summarized in Table 3.
In 1985, McGaughey (262) reported that Indianmeal moth
populations from grain storage bins that had been treated for
1 to 5 months with a B. thuringiensis subsp. kurstaki formulation
had a small but significant increase in LC50s relative to populations
in untreated bins. Laboratory experiments with colonies
collected from treated bins demonstrated measurable increases
in resistance after only two generations of selection.
After 15 generations of selection, insects from the treated
colony showed LC50s nearly 100-fold greater than those shown
by control colonies. The resistance trait proved to be recessive.
When selection was removed before resistance became fixed,
resistance levels decreased (263). A later study determined
that resistance was correlated with a 50-fold decrease in binding
affinity of a receptor for the Cry1Ab protein, one of the
toxins in the B. thuringiensis formulation used for selection
(396). In contrast, this Cry1Ab-resistant population showed an
increased susceptibility to Cry1Ca, a protein not present in the
selective formulation, and a corresponding increase in binding
sites on the midgut for the Cry1Ca protein.
Several additional colonies of P. interpunctella were selected
for resistance to B. thuringiensis strains having, in some cases,
toxin compositions different from the one described above
(264). The LC50s for several toxins were determined for each
colony. While resistance ratios for Cry1Ac and Cry1Ab were
most dramatic (24 to .2,000), resistance ratios of .10 were
also found for Cry1Aa, Cry1Ba, Cry1Ca, and Cry2Aa in some
of the colonies. A high level of resistance to Cry1Ac in three of
the colonies was noteworthy, because the selective B. thuringiensis
strains were reported not to produce that toxin. The
toxin binding characteristics of Cry1Ac to BBMV proteins and
tissue sections of several of these colonies have been studied
(274). Binding to an 80-kDa BBMV protein appeared unaltered
in ligand blots using BBMV from sensitive and several
resistant insect colonies. By contrast, the binding of fluorescein
isothiocyanate-labeled Cry1Ac toxin to midgut cells from insects
selected with Dipel or HD-133 was much reduced compared
to results with sensitive insects. For a P. interpunctella
colony under selection with B. thuringiensis subsp. entomocidus
HD-198, resistance to Cry1Ac was correlated with reduced in
vitro activation of Cry1Ac protoxin by midgut extracts from
resistant larvae (285). Examination of midgut enzymes in protease
activity blots revealed that one of the two major trypsinlike
proteases found in P. interpunctella was missing in the
mutant. A similar result was also observed for a colony resistant
to B. thuringiensis subsp. aizawai HD-133. In genetic
crosses, the protease-deficient and Cry1Ac-resistant phenotypes
cosegregated as a recessive trait (284).
Colonies of H. virescens with different levels of resistance
and different resistance mechanisms have also been obtained
in selection experiments with B. thuringiensis strains and proteins.
In an H. virescens population selected on Cry1Ab protoxin
expressed by an engineered P. fluorescens strain, resistance
to Cry1Ab increased to 20-fold after seven generations.
Resistance further increased to 71-fold after four additional
generations of selection with Dipel, a formulated B. thuringiensis
product containing several crystal proteins, including
Cry1Ab (362). The toxin showed a lower binding affinity to a
higher number of binding sites within the insect gut, but the
change in binding characteristics was considered insufficient to
explain the resistance (240).
Selection of another H. virescens population with Cry1Ac
protoxin as produced by a natural B. thuringiensis strain resulted
in a 50-fold resistance to Cry1Ac, a 13-fold resistance to
Cry1Ab, and a 53-fold resistance to Cry2Aa (145). Larvae from
this population could not survive on transgenic tobacco plants
with moderate (0.01%) levels of Cry1Ab (194). Altered toxin
binding was not implicated as a factor in resistance, an observation
that again suggests the existence of multiple resistance
mechanisms.
Very high levels of resistance to Cry1Ac (over 10,000-fold)
and to Cry1Ab (more than 2,000-fold) were obtained in H.
virescens by selection with Cry1Ac (144). The H. virescens colony
was highly cross-resistant to Cry1Aa and Cry1Fa but displayed
minimal resistance to Cry1Ba and Cry1Ca. A recent
study (146) showing that Cry1Fa and Cry1Ab compete for the
same receptor, at least in P. xylostella, provides a plausible
explanation for this observation. Larvae of this resistant H.
virescens strain survived significantly better than susceptible
larvae (144) on transgenic tobacco plants reported to produce
levels of Cry1Ab up to 0.007% of soluble protein (400). Surprisingly,
the binding of Cry1Ac (the selective toxin) and
Cry1Ab was unchanged while the binding of Cry1Aa was dramatically
reduced (210). It had already been demonstrated that
Cry1Ac also binds to the Cry1Aa binding site in H. virescens
(395). Consequently, it was proposed that the altered Cry1Aa
binding site caused resistance to all three Cry1A toxins and
that the additional binding sites recognized by Cry1Ab and
Cry1Ac might not be involved in toxicity (210). The allele
conferring most of the resistance phenotype of this strain has
been mapped to a 10-centimorgan region on linkage group 9 of
H. virescens at a locus termed BTR4 (155). The initial frequency
of this resistance allele in wild H. virescens populations
in the Southeastern United States was estimated to be between
1 in 500 and 1 in 667 (143), which is consistent with estimates
based on initial populations of insects used in selection experiments
(1 in 200 to 1 in 2,000) (142).
Selection experiments using Cry1Ca have generated resistant
strains of Spodoptera species. An S. littoralis colony with
.500-fold resistance was obtained (276). These insects were
cross-resistant to Cry1Da (7-fold) and Cry1Ea (34-fold). However, their susceptibility to Cry1Fa was unchanged, consistent
with the observation that Cry1Fa and Cry1Ca compete for
different receptors, at least in P. xylostella (146). An analysis of
the inheritance of resistance in this S. littoralis strain indicates
it is partially recessive and probably multifactorial (66). Moar
et al. (272) developed an S. exigua strain resistant to Cry1Ca
toxin. The basis of resistance could not be entirely explained by
changes in toxin binding characteristics. This insect strain was
cross-resistant to Cry1Ab, Cry2Aa, Cry9C, and a Cry1Ea-
Cry1Ca hybrid protein (44).
Given the multiple steps in processing the crystal to an active
toxin (see “Mechanism of Action”), it is not surprising that
insect populations might develop various means of resisting
intoxication. It is important, however, to keep in mind that
selection in the laboratory may be very different from selection
that occurs in the field. Insect populations maintained in the
laboratory presumably have a considerably lower level of genetic
diversity than field populations. Several laboratory experiments
to select for B. thuringiensis resistance in diamondback
moths failed, although the diamondback moth is the only
known insect reported so far to have developed resistance to B.
thuringiensis in the field. It is possible that the genetic diversity
of the starting populations was too narrow and thus did not
include resistance alleles. In the laboratory, insect populations
are genetically isolated; dilution of resistance by mating with
susceptible insects, as observed in field populations, is excluded.
In addition, the natural environment may contain factors
affecting the viability or fecundity of resistant insects,
factors excluded from the controlled environment of the laboratory.
Resistance mechanisms can be associated with certain
fitness costs that can be deleterious under natural conditions
(383). Natural enemies, such as predators and parasites, can
influence the development of resistance to B. thuringiensis by
preferring either the intoxicated, susceptible or the healthy,
resistant insects. In the former case, one would expect an
increase in resistance development, while in the latter, natural
enemies can help to retard resistance development to B. thuringiensis.
Nevertheless, selection experiments in the laboratory
are valuable because they reveal possible resistance mechanisms
and make genetic studies of resistance possible.
Field-selected strains. The first case of field-selected resistance
to B. thuringiensis was reported from Hawaii, where
populations of diamondback moth (P. xylostella) showed different
levels of susceptibility to a formulated B. thuringiensis
product (Dipel). Populations from heavily treated areas
proved more resistant than populations treated at lower levels,
with the highest level of resistance at 30-fold (365). Laboratory
selection rapidly increased resistance to .1,000-fold (366). A
study of the resistance mechanism showed a reduced binding
of the Cry1Ac protein to gut BBMV (365). However, immunohistochemical
(105) and surface plasmon resonance (257)
analyses demonstrated the presence of at least some receptor
molecules on the midgut of this resistant insect strain. The
resistance trait is conferred largely by a single autosomal recessive
locus (367, 368). This “Hawaii” resistance allele simultaneously
confers cross-resistance to Cry1Aa, Cry1Ab, Cry1Ac,
Cry1Fa, and Cry1Ja but not to Cry1Ba, Cry1Bb, Cry1Ca,
Cry1Da, Cry1Ia, or Cry2Aa (369). At least one Cry1A-resistant
diamondback moth strain has been shown to be very susceptible
to Cry9C (198). The toxins in the cross-resistance group
have significant amino acid sequence similarity in domain II, a
region believed to be important for receptor binding in many
systems (see “Mechanism of Action”). Furthermore, Cry1Aa,
Cry1Ac (21), and Cry1F (146), but not Cry1B or Cry1C (113),
compete for the Cry1Ab binding site in P. xylostella, observations
that clearly correspond to the cross-resistance data. A
phenotypically similar resistant strain collected in Pennsylvania
carries a resistance allele at the same multitoxin resistance
locus (368).
A P. xylostella strain collected in Florida showed very high
resistance to a B. thuringiensis subsp. kurstaki formulation and
low-level resistance to B. thuringiensis subsp. aizawai (341).
The strain has been estimated to have .200-fold resistance to
Cry1Aa, Cry1Ab, and Cry1Ac and 60-fold resistance to the
HD-1 spore but near wild-type sensitivity to Cry1B, Cry1C, and
Cry1D. Binding of Cry1Ab, but not Cry1B, was reduced with
midgut tissue sections and native BBMV prepared from the
resistant strain (372). The existence of a single-locus resistance
allele with autosomal, incompletely recessive inheritance best
fits the genetic data for B. thuringiensis var. kurstaki resistance
in this strain (371). A simple and plausible explanation is that
the multitoxin resistance locus altered in the Hawaii and Pennsylvania
strains is also affected in the Florida population, but
this possibility has not been tested. The resistance phenotype
was not associated with any fitness costs and, after an initial
decrease in resistance during the first three generations, remained
stable at a high level even in the absence of selection
(371). Diamondback moth populations with a similar resistance
phenotype—high-level resistance to B. thuringiensis
subsp. kurstaki formulations and low-level resistance to B. thuringiensis
subsp. aizawai—have also been isolated in Indonesia
(341), Malaysia (167), Central America (292), and several
states within the continental United States (341). Data are
insufficient, however, to compare these strains to the resistant
Hawaii, Pennsylvania, or Florida populations in stability, inheritance,
or mechanism of resistance.
A field population of diamondback moths from the Philippines
showed partial resistance to Cry1Aa, Cry1Ab, and
Cry1Ac, but full sensitivity to Cry1C, Cry1F, and Cry1J (368).
Binding to resistant-strain BBMV was reduced for Cry1Ab but
apparently unaffected for Cry1Aa, Cry1Ac, or Cry1C. Interestingly,
the Cry1Ab single-resistance phenotype appeared to be
due to an autosomal, recessive mutation at the multitoxin
resistance locus implicated in the resistant Hawaii and Pennsylvania
strains, although the Philippines allele conferred no
cross-resistance. Inheritance of resistances to Cry1Aa and
Cry1Ac was expressed in an autosomal dominant and semidominant
fashion, respectively, at the test dose employed
(368). Cry1Ab binding was also implicated in the resistance
mechanism of a strain isolated earlier from the same region of
the Philippines (49, 113), although the cross-resistance phenotypes
and inheritance patterns of this earlier isolate were not
rigorously analyzed.
Resistance to B. thuringiensis subsp. kurstaki products and
resulting failure in diamondback moth control has resulted in
extensive use of B. thuringiensis subsp. aizawai-based insecticides
in certain locations. Insects in two colonies from Hawaii
have up to a 20-fold resistance to Cry1Ca compared to several
other colonies, including one obtained earlier from the same
location, as well as moderately high resistance to Cry1Ab and
kurstaki subspecies-based formulations (228). Following additional
selection in the laboratory, Cry1Ca resistance increased
to 60-fold over control levels. The Cry1C resistance trait was
shown to segregate independently from the Cry1Ab resistance
determinant, behaving as an additive autosomal trait, appearing
recessive at high test doses of toxin and dominant at low
test doses (227).
A Malaysian strain simultaneously highly resistant to the
kurstaki subspecies and the aizawai subspecies was apparently
mutated in several loci (418). A Cry1Ab resistance allele, associated
with reduced binding to BBMV receptors, was partially
responsible for resistance to both subspecies. In contrast, binding of Cry1Aa, Cry1Ac, and Cry1C showed no gross alterations
compared with BBMV from the sensitive strain. Genetic
determinants responsible for subspecies kurstaki-specific and
subspecies aizawai-specific resistance segregated separately
from each other and from the Cry1Ab resistance allele in
genetic experiments (418).
These studies suggest that a single locus, perhaps encoding a
common receptor for many of the Cry1A toxins, can mutate to
multitoxin resistance in P. xylostella. A different type of mutation
at the same locus might alter the binding site for Cry1Ab,
while leaving binding sites for other toxins on the same receptor
unaffected. Unlinked loci affecting other events in toxicity,
either before or after the binding step, can mutate to provide
specific resistance to other Cry toxins. Additional studies along
the lines of that conducted by Tabashnik et al. (368), using
other resistant strains, are urgently needed to clarify the genetic
and mechanistic picture.
It is clear, however, that the case history of P. xylostella
presents a cautionary tale for the use of B. thuringiensis and its
toxins in agriculture. After less than 2 decades of intensive
subspecies kurstaki use in crucifer agriculture, resistant insects
have evolved in numerous geographically isolated regions of
the world, and subspecies aizawai resistance is beginning to
appear even more rapidly. Injudicious use of Cry toxins could
rapidly render them ineffective against other major crop pests,
squandering a precious resource at a time when synthetic organic
pesticides are already increasingly ineffective. Various
alleles showing cross-resistance, dominant inheritance, or stability
in the absence of selection have been detected in resistant
field lines of P. xylostella, phenomena with far-reaching
implications for resistance management. These observations
underscore a critical need for increased emphasis and funding
on an international scale for all aspects of Cry toxin research.
Resistance Management
Resistance management strategies try to prevent or diminish
the selection of the rare individuals carrying resistance genes
and hence to keep the frequency of resistance genes sufficiently
low for insect control. Strategy development generally relies
heavily on theoretical assumptions and on computer models
simulating insect population growth under various conditions
(12, 141, 168, 250, 320, 321, 364). Proposed strategies include
the use of multiple toxins (stacking or pyramiding), crop rotation,
high or ultrahigh dosages, and spatial or temporal refugia
(265, 364). Only recently have some of the proposed tactics
been experimentally evaluated on a small scale (342). Retrospective
analysis of resistance development does support the
use of refugia (364). It is clear that the real value of the
different proposed tactics can only be tested in larger-scale
field trials.
It is expected that each pest-crop complex may require a
specific implementation of certain resistance management
strategies that may have to address the use of both B. thuringiensis
sprays and transgenic crops. Experience with transgenic
crops expressing cry genes grown under different agronomic
conditions is essential to define the requirements of resistance
management. It is equally important to design a resistance
management strategy acceptable to everyone involved: technology
suppliers, seed companies, extension workers, crop consultants,
regulators, and, most of all, growers (182).
In transgenic plants, selection pressure could be reduced by
restricting the expression of the crystal protein genes to certain
tissues of the crop (those most susceptible to pest damage) so
that only certain parts of the plant are fully protected, the
remainder providing a form of spatial refuge (but see the
concerns raised in reference 250). It has been proposed that
cotton lines in which cry gene expression is limited to the young
bolls may not suffer dramatic yield loss from Heliothis larvae
feeding on other plant structures, since cotton plants can compensate
for a high degree of pest damage (140). Crystal protein
gene expression could be triggered by the feeding of the insect
itself in a transgenic plant, with resident cry genes controlled by
wound-inducible promoters (291). If plants were to express B.
thuringiensis toxin only in response to specific damage thresholds,
it might provide a mechanism to diminish toxin exposure
to insects. Alternatively, toxin expression could be induced by
the application of a chemical (409). In this way, a farmer would
have the option to have Cry toxin present in the crops only
when insect densities exceed an economic threshold.
Another management option is the rotation of plants or
sprays of a particular B. thuringiensis toxin with those having
another toxin type that binds to a different receptor. This
strategy has potential value when a fitness cost is associated
with resistance. Such fitness costs have been reported in P.
xylostella lines, in which resistant males have lower mating
success than their nonresistant competitors (149). Insects resistant
to one Cry toxin type would be at a disadvantage during
the next growth season when a different toxin type is used,
resulting in a decrease of the frequency of the corresponding
resistance gene. Ideally, reversion to susceptibility for this Cry
toxin type should occur within the growth season. Tabashnik et
al. (365) noticed that revertant diamondback moth populations
responded rapidly to reselection and susceptibility was not fully
restored.
If transgenic plants can express a cry gene at doses high
enough to kill even homozygous resistant insects, that crop will
become a nonhost. While such an ultrahigh dose might be
impractical with a sprayable product due to high cost, incomplete
coverage, toxin breakdown, and plant growth, it may be
possible with toxin-engineered plants, taking into account the
currently attainable levels of Cry expression in planta (169).
For example, a Colorado potato beetle population 100-fold
resistant to a Cry3A-containing B. thuringiensis spray could not
survive on potato plants expressing the same protein (13, 407).
It remains to be seen if a combination of toxins with ultrahigh
expression can overcome all homozygous resistance alleles,
changing the crops into nonhost plants.
A very attractive resistance management tactic is the combination
of a high-dose strategy with the use of refugia (toxinfree
areas). The principle is to express Cry toxins at such a dose
that nearly all heterozygotic carriers of resistance alleles will be
killed. Survivors would most likely mate with the sensitive
insects harbored in the nearby refuge. Consequently, a population
of homozygous resistant insects would be unlikely to
emerge. B. thuringiensis resistance is in fact a recessive trait in
at least some insect species (364); with the high levels of expression
now attainable in planta (e.g., a dose 50-fold higher
than the LC50) (193), and with essentially complete foliar coverage,
it may be reasonable to attain nearly total killing of
heterozygotes. Indeed, Metz et al. (269) demonstrated that F1
larvae from a cross between a susceptible laboratory P. xylostella
colony and a field-resistant colony did not survive on
transgenic broccoli expressing Cry1Ac (341). It has been reported
that the inclusion of refuge plants in cages with transgenic
broccoli plants resulted in slower evolution of resistance
in populations of P. xylostella (342). Supporting evidence also
comes from selection experiments using B. thuringiensis subsp.
aizawai and a diamondback moth population that had evolved
resistance to Cry1Ab and Cry1Ca in the field. In these studies,
a 10% refuge delayed resistance over a nine-generation test
(226). Depending on the crop, refugia may be naturally present or may need to be created by the planting of nontransgenic
plots. Refugia should be uncontaminated, and there should be
random mating between resistant and nonresistant insects
(141). Refugia that are temporally and spatially contiguous
with the transgenic crop could fulfill these requirements (118).
See the work of Gould (142) for a broader discussion from a
perspective of population dynamics and evolution.
A specific planting strategy that has been recommended to
reduce selection is the use of seed mixtures of toxin-expressing
and toxin-free plants to provide prepackaged refugia. The seed
mix strategy, still controversial, would probably only be effective
for insect species whose larvae move very little between
plants (250, 364) or whose adults acquire a mate visually over
a short distance (320).
Another valuable option for resistance management, in
combination with the use of refugia, is the expression of multiple
Cry proteins in crops or incorporation of multiple proteins
in B. thuringiensis sprays, provided these toxins have different
modes of action (321) with respect to the insect’s
mechanism of resistance. Cry toxins that recognize different
receptors in the same target species could be deployed in this
strategy, since they are less prone to cross-resistance. As noted
above, diamondback moth populations resistant to field applications
of Cry1A-containing B. thuringiensis formulations
showed minimal cross-resistance to other crystal proteins such
as Cry1Ba, Cry1Bb, Cry1Ca, Cry1Da, Cry1Ia, Cry2A, and
Cry9Ca, while they were cross-resistant to Cry1Fa and Cry1Ja
(198, 365, 369, 372). There are several other insect species in
which Cry toxins with different receptor specificities are known
(93, 105, 113, 163, 198, 394, 395). For many insect species,
multiple Cry1A proteins would not be an appropriate choice,
since some of these proteins share binding sites with one another
(94, 106, 395, 413) and even with other toxins of the Cry1
class (97). Yet for other insects, Cry1A proteins have been
shown, at least on ligand blots, to recognize different binding
proteins (211, 385, 386, 388). Additionally, B. thuringiensis Cry
toxins could be combined with other insecticidal proteins. The
multiple-attack strategy assumes that within a population, if
insects homozygous for one resistance gene are rare, then
insects homozygous for multiple resistance genes are extremely
rare. Crops or sprays deploying multiple toxins would still
control even insects homozygous for one or two resistance
genes yet heterozygous for another gene. A critical condition
for the success of this strategy is that each of the insecticides on
its own should have high mortality for susceptible homozygotes
(321). An example is O. nubilalis, in which Cry1Ab and
Cry1Ba, both highly active, bind to different receptors (94). A
strong argument for the utility of multiple-gene pyramiding is
found in the recent results of Georghiou and Wirth (133).
Their field-collected C. quinquefasciatus populations readily
developed resistance in the laboratory to a single B. thuringiensis
subsp. israelensis toxin (Cry11A) but remained remarkably
sensitive when selection was with the full complement of toxins
from this variety.
Due to the urgent need for a more complete understanding
of the parameters of effective resistance management, companies
developing B. thuringiensis biopesticidal sprays and transgenic
plants formed the B. thuringiensis Management Working
Group in 1988 to promote research on the judicious use of B.
thuringiensis products. It is hoped that an increased understanding
of the complex interplay among Cry toxins, their bacterial
hosts, their target organisms, and the ecosystems they
share will allow for the long-term, effective use of Cry toxins
for pest management.
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DNA amplification using Taq DNA polymerase is one of the most widely used techniques in
molecular biology and biotechnology. The aim of this study was to amplify the gene of this enzyme
from a thermophilic bacteria called Thermus aqauticus and clone it into a vector for future use. Using
specific primers the cDNA of Taq DNA polymerase was amplified and ligated into the cloning vector
pTZ57R using TA cloning technique. The recombinant plasmids were identified using restriction
enzyme digestion. The presence of the Taq DNA polymerase gene was confirmed by DNA
sequencing. In conclusion, Taq DNA polymerase gene has been cloned in our laboratory and can be
used for the production of large quantities of this enzyme.
INTRODUCTION
Taq DNA Polymerase is an enzyme
obtained from a heat stable bacteria called
Thermus aquaticus having a molecular
weight of about 66,000-94,000 daltons (1).
This enzyme is used for the amplification
of selective DNA segments using polymerase
chain reaction (PCR 2). The Taq DNA
polymerase isolated from thermus aquaticus
was the first characterized thermostable
enzyme and is one of the most widely used
enzymes of this category. This thermostable
enzyme enables the amplification
reaction to be performed at higher temperatures
and makes the automation of PCR
possible (3). The full length 94 kDa Taq
polymerase has maximal activity and half
life of 9 min at 97.5 C (4).
More than 50 DNA polymerase genes
have been cloned and sequenced from
various organisms including thermophiles
and archaea (5). Although some laboratories
have reported the cloning of Taq DNA
polymerase (6), no study has been conducted
in Iran. Because of the economic value of
this enzyme, obtaining this clone from
external sources for laboratory production
of Taq DNA polymerase is extremely
difficult. Therefore, in order to produce
Taq DNA polymerase, reduce the cost of
research in our laboratory, and having the
gene of this enzyme for future modifications,
we decided to amplify and clone Taq
DNA polymerase gene. For this purpose,
TA cloning technique was used, which has
not been utilized by any previous study
reporting cloning of this gene
MATERIALS AND METHODS
Bacterial strains and plasmids
Thermus aquaticus strain YT-1 (ATCC-
25104) a gift from Dr. Kutellu Ulgen (Turky, Bogazici University), was used as
a source to isolate the thermostable Taq
DNA polymerase gene. E. coli XL1-Blue
strain was used as a host for recombinant
plasmids. The plasmid pTZ57R obtained
from Fermentas company was utilized as a
cloning vector.
Growth conditions
E. coli strains were grown at 37 C in
Luria Bertani (LB) broth or plated on LB
agar containing 80 g/ml ampicillin as
described by Sambrook et al. (7).
Genomic DNA preparation
The Genomic DNA from Thermus
aquaticus strain YT-1 was isolated using
high pure PCR template preparation kit,
which was purchased from Roche Co.
(Germany). Electrophoresis in 0.7%
agarose gel was used to confirm the size of
the isolated DNA (7).
Amplification protocol
A pair of primers were designed based
on the 5' and 3' ends of this gene and were
utilized for PCR amplification. The
sequence of these primers were as follows:
Forward: 5′-CACGAATTCGGGGATGCT
GCCCCT CTTTGAGCCCAAG-3′
Reverse: 5′-GTGAGATCTATCACTCCT
TGGCGGAGAGCCAGTC-3′
PCR amplification was performed using
the following reagents: 1 X PCR reaction
buffer (50 mM KCl, 20 mM Tris- HCl (pH
8.4), primers (each 2.5 µM), 3 mM MgCl2,
0.5 mM dNTPs, 0.4 ìg template DNA, 1X
Q solution, 5 Unit Taq polymeras (QIAGEN,
Germany). The final reaction volume was
50 µl. PCR cycles were as follows: one
cycle of 5 min at 94 C, 35 cycles of: l min
at 94 C, 2 min at 55 C, 3 min 72 C, and
one cycle of 20 min at 72 C (8).
Confirmation of PCR product
The amplified PCR product was analyzed
by electrophoresis in 0.7% agarose gel. In
addition to checking its sized, using HindIII
Figure 1. Amplification of the Taq polymerase gene.
Figure 2. Restriction digestion of the PCR product.
restriction enzyme the amplifi-cation of
Taq DNA polymerase gene was confirmed.
Finally, after cloning of this PCR
fragment, its sequencing was carried out
using T7 primer in Fazapajooh Co.
Ligation
The PCR product was extracted by QIA
quick gel extraction kit obtained from
Germany. The concentration of the insert
was determined using DNA (HindIII
digested). This insert was then ligated into
pTZ57R vector using InsT/A clone PCR
product cloning kit (Fermentas, Germany).
Ligation was performed in 10 µl volumes
under the following conditions: The molar
ratio of 3/1 for insert to vector, 1X ligase
buffer, 1X PEG 4000, BSA (0.44 ng), 5
Units T4 DNA ligase (Fermentas), and
dH2O. The reaction mixtures were
incubated over night at 16 ºC.
Transformation and plasmid preparation
The ligated mixture were transformed to
XL1-Blue competent cells (CaCl2 method)
using heat shock method (42 oC, 45 sec).
These mixtures were then plated on LB
agar containing 100 µg/ml ampicillin and
incubated at 37 oC overnight. The obtained
colonies were used for plasmid preparation
(7). Restriction enzymes, EcoRI, BamHI,
KpnI and HindIII were used for the
digestion of these plasmids
RESULTS
The isolated DNA from from Thermus
aquaticus colonies used as a template for
PCR amplification of Taq DNA polymerase
gene. The electrophoresis of this
product is shown in Figure 1 matching the
expected size of the gene which is 2500
bp. Digestion of this DNA with HindIII
restriction enzyme gave the expected
two bands of 1900 bp and 600 bp as is
shown in Figure 2 (Lanes 2 and 3).The
amplified product corresponding to Taq
DNA polymerase gene was ligated into
pTZ57R vector. The presence of the insert
within the plasmid was confirmed by
restriction enzyme digestion. HindIII
enzyme produced two bands (1974 bp and
3400 bp), KpnI enzyme also produced two
bands (617 and 4800 bp), and double
digestion with BamHI and EcoRI enzymes
Figure 3. Restriction analysis of colonies for the presence of
the recombinant plasmids.
resulted in three bands (719, 1700 and
2900 bp) as shown in Figure 3 (Lane 2, 3
and 4). A segment of the recombinant
plamid was also sequenced (Figure 4).
DISCUSSION
Because of the widespread use of Taq
DNA polymerase, we decided to amplify
and clone its gene. Several attempts
varying the experimental conditions, such
as PCR cycles and MgCl2 concentrations
were made for its amplification without
any success. Surprisingly, by changing the
brand of Taq DNA polymerase, the desired
product was obtained. Considering that
Taq DNA polymerase should act the same
when purchased from any company, our
results indicate that some of the local
companies sell faulty products and one has
to be selective in ordering reagents from
these sources.
Desai and Pfaffle have reported the
cloning of Taq DNA polymerase into
pUC18 plasmid (8). Other reports are also
available regarding the cloning of this gene
(6, 9). However, our study is the first to
clone the Taq DNA polymerase gene using
TA cloning method. This is a more
convenient and much faster procedure as
compared to those used in other studies.
The sequencing of the obtained clone in
our laboratory indicated that for the first
time in Iran, Taq DNA polymerase gene
has been successfully cloned. This would
allow us to perform many studies including
expression of this gene, mass production of
the enzyme and introducing mutations for
enhancing its performance.
Ben
Administrateur
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MessagePosté le: Lun 15 Déc - 16:20 (2008) Répondre en citant
Mort de Rire , tu es un legionnellogue ?????
Sage
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plutôt legionnellophile :lol:
_________________
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sidali
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non!!!!!je crois legianglaiophile happy
quelle sujet!!!il lui a fallu tout une page;je crois que c'est un record scof:le sujet le plus long
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Je voulais faire quote, m'ai j'avais peur de xooit qu'il me chasse
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cf5cd1df0ee2161e1684bdc019357275
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D I S C O V E R L I F E
Bee Hunt! Odonata Lepidoptera
HomeAll Living ThingsIDnature guidesGlobal mapperAlbumsLabelsSearch
AboutNewsEventsResearchEducationProjectsStudy sitesHelp
Basidiomycota
MUSHROOMS; RUSTS; SMUTS; BASIDIOMYCETES; CLUB FUNGI
Life Fungi
Kinds
Overview
Fungi that, if multicellular, bear the products of meiosis on club-shaped basidia and possess a long-lasting dikaryotic stage. Some are unicellular.
Phylogeny
Links to other sites
Acknowledgements
I thank John Pickering for his assistance with the development of this page.
Supported by
go to Discover Life's Facebook group
Updated: 2020-11-27 15:42:39 gmt
Discover Life | Top
© Designed by The Polistes Corporation
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WoRMS banner
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WoRMS taxon details
Checked: verified by a taxonomic editorHymeniacidon perlevis (Montagu, 1814)
AphiaID: 132663
Classification: Biota > Checked: verified by a taxonomic editorAnimalia (Kingdom) > Checked: verified by a taxonomic editorPorifera (Phylum) > Checked: verified by a taxonomic editorDemospongiae (Class) > Checked: verified by a taxonomic editorHalichondrida (Order) > Checked: verified by a taxonomic editorHalichondriidae (Family) > Checked: verified by a taxonomic editorHymeniacidon (Genus) > Checked: verified by a taxonomic editorHymeniacidon perlevis (Species)
Status accepted
Rank Species
Parent Checked: verified by a taxonomic editorHymeniacidon Bowerbank, 1858
Synonymised
names
Checked: verified by a taxonomic editorAxinella cristagalli Maas, 1894 (genus transfer)
Checked: verified by a taxonomic editorHalichondria macularis Johnston, 1846 (genus transfer and junior synonym)
Checked: verified by a taxonomic editorHymeniacidon aurea (Montagu, 1814) (junior synonym)
Checked: verified by a taxonomic editorHymeniacidon caruncula Bowerbank, 1858 (junior synonym)
Checked: verified by a taxonomic editorHymeniacidon consimilis Bowerbank, 1866 (junior synonym)
Checked: verified by a taxonomic editorHymeniacidon mammeata Bowerbank, 1866 (junior synonym)
Checked: verified by a taxonomic editorHymeniacidon perleve (Montagu, 1814) (Spelling vatiation)
Checked: verified by a taxonomic editorHymeniacidon sanguinea (Grant, 1826) (junior synonym)
Checked: verified by a taxonomic editorHymeniacidon virgulata Bowerbank, 1882 (junior synonym)
Checked: verified by a taxonomic editorIsodictya uniformis Bowerbank, 1866 (genus transfer and junior synonym)
Checked: verified by a taxonomic editorPolymastia mammeata (Bowerbank, 1866) (genus transfer and junior synonym)
Checked: verified by a taxonomic editorRaphiodesma simplisissima Bowerbank, 1874 (genus transfer & junior synonym)
Checked: verified by a taxonomic editorReniera uniformis (Bowerbank, 1866) (genus transfer & junior synonym)
Checked: verified by a taxonomic editorSpongia aurea Montagu, 1814 (genus transfer and junior synonym)
Checked: verified by a taxonomic editorSpongia perlevis Montagu, 1814 (genus transfer)
Checked: verified by a taxonomic editorSpongia sanguinea Grant, 1826 (genus transfer and junior synonym)
Checked: verified by a taxonomic editorStylinos uniformis (Bowerbank, 1866) (genus transfer and junior synonym)
Checked: verified by a taxonomic editorStylotella uniformis (Bowerbank, 1866) (genus transfer and junior synonym)
Sources basis of record Erpenbeck, D.; Van Soest, R.W.M. 2002. Family Halichondriidae Gray, 1867. Pp. 787-816. In Hooper, J. N. A. & Van Soest, R. W. M. (ed.) Systema Porifera. A guide to the classification of sponges. 1 (Kluwer Academic/ Plenum Publishers: New York, Boston, Dordrecht, London, Moscow). [details]
[show all]
Vernacular
Names
Language Name
Dutch Unreviewed: has not been verified by a taxonomic editorbleke piekjesspons [details]
Environment marine, brackish, fresh, terrestrial
Fossil range recent only
Distribution Checked: verified by a taxonomic editortype locality United Kingdom Exclusive Economic Zone [details]
From editor or global species database
North Atlantic Ocean
Checked: verified by a taxonomic editorAzores [from synonym] [view taxon] [details]
Checked: verified by a taxonomic editorCanary Islands Exclusive Economic Zone [details]
Checked: verified by a taxonomic editorEuropean waters (ERMS scope) [from synonym] [view taxon] [details]
Checked: verified by a taxonomic editorIrish Exclusive economic Zone [from synonym] [view taxon] [details]
Checked: verified by a taxonomic editorUnited Kingdom Exclusive Economic Zone [details]
North Sea
Checked: verified by a taxonomic editorBelgian Exclusive Economic Zone [from synonym] [view taxon] [details]
Checked: verified by a taxonomic editorOosterschelde [from synonym] [view taxon] [details]
Norway
Checked: verified by a taxonomic editorSvalbard [from synonym] [view taxon] [details]
South Atlantic Ocean
Checked: verified by a taxonomic editorCongolese Exclusive Economic Zone (inaccurate[details]
Spain
Checked: verified by a taxonomic editorNorth Coast of Spain [from synonym] [view taxon] [details]
United Kingdom
Checked: verified by a taxonomic editorUnited Kingdom [from synonym] [view taxon] [details]
(no group)
Checked: verified by a taxonomic editorAdriatic Sea [from synonym] [view taxon] [details]
Checked: verified by a taxonomic editorAegean Sea [details]
Checked: verified by a taxonomic editorAlboran Sea [details]
Checked: verified by a taxonomic editorAngolan (inaccurate[details]
Checked: verified by a taxonomic editorAzores Canaries Madeira [details]
Checked: verified by a taxonomic editorCeltic Seas [details]
Checked: verified by a taxonomic editorGulf of Guinea West (inaccurate[details]
Checked: verified by a taxonomic editorIonian Sea [from synonym] [view taxon] [details]
Checked: verified by a taxonomic editorNorth Sea [details]
Checked: verified by a taxonomic editorNorth and East Barents Sea [details]
Checked: verified by a taxonomic editorNortheastern New Zealand (inaccurate[details]
Checked: verified by a taxonomic editorSouth European Atlantic Shelf [from synonym] [view taxon] [details]
Checked: verified by a taxonomic editorWestern Mediterranean [details]
From regional or thematic species database
Antigua and Barbuda
Trusted: edited by a thematic editorFreetown [details]
Arctic Ocean
Trusted: edited by a thematic editorArctic Ocean [details]
Australia
Trusted: edited by a thematic editorAustralia [details]
Cape Verde
Trusted: edited by a thematic editorCape Verde [details]
New Zealand
Trusted: edited by a thematic editorNew Zealand [details]
North Atlantic Ocean
Trusted: edited by a thematic editorNorth Atlantic [details]
South Africa
Trusted: edited by a thematic editorSouth Africa (country) [details]
(no group)
Trusted: edited by a thematic editorTunisian Exclusive Economic Zone [from synonym] [view taxon] [details]
Trusted: edited by a thematic editorWest Africa [details]
From other sources
Australia
Unreviewed: has not been verified by a taxonomic editorAustralia [details]
France
Unreviewed: has not been verified by a taxonomic editorWimereux [details]
Mediterranean Sea - Eastern Basin
Unreviewed: has not been verified by a taxonomic editorGreek Exclusive Economic Zone [details]
New Zealand
Unreviewed: has not been verified by a taxonomic editorNew Zealand [details]
North Atlantic Ocean
Unreviewed: has not been verified by a taxonomic editorAzores Exclusive Economic Zone [details]
Unreviewed: has not been verified by a taxonomic editorEuropean waters (ERMS scope) [details]
Unreviewed: has not been verified by a taxonomic editorIrish Exclusive economic Zone [details]
Unreviewed: has not been verified by a taxonomic editorUnited Kingdom Exclusive Economic Zone [details]
North Sea
Unreviewed: has not been verified by a taxonomic editorBelgian Exclusive Economic Zone [details]
South Africa
Unreviewed: has not been verified by a taxonomic editorSouth Africa (country) [details]
(no group)
Unreviewed: has not been verified by a taxonomic editorNew Zealand Exclusive Economic Zone [details]
Specimens
[show all]
Host of Checked: verified by a taxonomic editorPseudoclausia longiseta Bocquet & Stock, 1963 [via synonym] (parasitic: ectoparasitic)
Checked: verified by a taxonomic editorBradypontius papillatus (Scott T., 1888) (parasitic: ectoparasitic)
Checked: verified by a taxonomic editorAsterocheres faroensis Crescenti, Baviera & Zaccone, 2010 (parasitic: ectoparasitic)
Links Unreviewed: has not been verified by a taxonomic editorTo Barcode of Life (34 barcodes)
Unreviewed: has not been verified by a taxonomic editorTo Biodiversity Heritage Library (6 publications)
Unreviewed: has not been verified by a taxonomic editorTo Encyclopedia of Life
Unreviewed: has not been verified by a taxonomic editorTo GenBank (130 nucleotides; 120 proteins)
Unreviewed: has not been verified by a taxonomic editorTo Marine Species Identification Portal
Unreviewed: has not been verified by a taxonomic editorTo PESI
Unreviewed: has not been verified by a taxonomic editorTo USNM Invertebrate Zoology Porifera Collection
Notes
From editor or global species database
Checked: verified by a taxonomic editorTaxonomy The quoted (South) African material is unlikely to be conspecific with Hymenacidon perlevis. Probably, the specimens belong to Hymeniacidon stylifera (Stephens, 1915). [details]
From other sources
Unreviewed: has not been verified by a taxonomic editorAdditional Material South Africa - SAM-H4904 (Ts 305), Jacobs Bay, near Saldanha Bay (32°31’S, 17°30’E), depth 3–5 m, collected by T. Samaai, 20
October 1997. Ts 329, Ts 331, Ts 337, Ts 338, Ts 343c,
Elands Bay (32°20’S, 18°20’E), depth 3–6 m, collected by T.
Samaai, 15 November 1997. Ts 359, Ts 370, Ts 381, Ts 391,
Groenrivier (30°29’S, 17°20’E), depth 3 m. Collected by
T. Samaai, 20 December 1997. [details]
LSID urn:lsid:marinespecies.org:taxname:132663
Taxonomic
Edit history
Date action by
2004-12-21 15:54:05Z created van Soest, Rob
2014-02-16 18:30:10Z changed van Soest, Rob
[Taxonomic tree] [Occurrence map] [Google] [Google scholar] [Google images]
Citation: van Soest, R. (2014). Hymeniacidon perlevis (Montagu, 1814). In: Van Soest, R.W.M; Boury-Esnault, N.; Hooper, J.N.A.; Rützler, K.; de Voogd, N.J.; Alvarez de Glasby, B.; Hajdu, E.; Pisera, A.B.; Manconi, R.; Schoenberg, C.; Janussen, D.; Tabachnick, K.R., Klautau, M.; Picton, B.; Kelly, M.; Vacelet, J.; Dohrmann, M.; Díaz, M.-C.; Cárdenas, P. (2014) World Porifera database. Accessed through: World Register of Marine Species at http://www.marinespecies.org/aphia.php?p=taxdetails&id=132663 on 2015-03-05
Creative Commons License The webpage text is licensed under a Creative Commons Attribution 4.0 License
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SRC-2 at center of survival adaptations to food shortages
When fasting or facing a food shortage, the body engages metabolic and behavioral adaptations to survive. How the brain coordinates and regulates these responses has not been clear, but researchers at Baylor College of Medicine and collaborating institutions have discovered that a molecule known as steroid receptor coactivator-2 (SRC-2) is crucial to coordinate the biological responses to the lack of food.
The team shows in the journal Cell Reports that SRC-2 specifically in POMC neurons in the hypothalamus, a brain region involved in various aspects of metabolism, including energy management, helps animals modify their metabolism and certain behaviors to survive until food is available again. Interestingly, SRC-2 also showed to be involved in weight gain when food was abundant, leading to obesity. The findings open new possibilities for designing strategies for weight management.
“When food is not easily available or during fasting, organisms modify certain aspects of their metabolism to be able to function and of their behavior to improve the odds of restoring the much needed nutrition,” said corresponding author by Dr. Yong Xu, professor of pediatrics – nutrition and molecular and cellular biology at Baylor. “In this study, we show that SCR-2 in POMC neurons in the hypothalamus is at the center of these adaptations.”
Xu and his colleagues looked into two important metabolic components: energy expenditure and blood glucose balance.
“One way to adapt to lack of food is to reduce how much energy the body spends. It is also important that the body maintains a glucose balance that sustains brain activity,” Xu said. “We found that SRC-2 is required to retain the ability to reduce energy expenditure and to maintain glucose levels that allow the animal to survive.”
The researchers also looked into behavioral adaptations that help the animal find food.
“When an animal living in the wild has not eaten in a while, it needs to venture into its environment to search for food, which at the same time exposes it to predators, creating anxiety,” Xu said. “We found that SRC-2 helps overcome the anxiety triggered by the need to go out to feed, facilitating the search for food.”
In addition, the researchers found that SRC-2 is required to delay the normal satiety signal that stops the animal from eating. “Delaying the satiety signal stimulates the animal to engage in continuous feeding behavior longer, eating as much as possible, quickly, to reduce the time they are exposed to a dangerous environment.”
During most of evolution, having enough food has been, and still is, the first priority of animals in the wild. Xu and colleagues propose that SRC-2 is evolutionarily conserved, meaning that it is at the center of the regulation of animal metabolic and behavioral adaptations that help organisms survive when food is not easily available.
On the other hand, when the environment changes so that food is readily available, animals can eat without limitations. “In this case, SRC-2 becomes detrimental to the animals. It facilitates overeating, leading to weight gain and obesity,” Xu said.
At the mechanistic level, Xu and colleagues showed that SRC-2 controls the ability of POMC neurons to transmit electric signals to communicate with other neurons. SRC-2 also mediates its effects by regulating the expression of multiple genes.
Other contributors to this work include Yongjie Yang, Yanlin He, Hailan Liu, Wenjun Zhou, Chunmei Wang, Pingwen Xu, Xing Cai, Hesong Liu, Kaifan Yu, Zhou Pei, Ilirjana Hyseni, Makoto Fukuda, Zheng Sun, Jianming Xu and Bert W. O’Malley, all at Baylor College of Medicine. Qingchun Tong is affiliated with the University of Texas Health Science Center at Houston.
The work was supported by grants from the National Institutes of Health (R01DK114279, R01DK109934, R21NS108091, R00DK107008, R01DK104901, R01DK126655, K01DK119471, R01DK115761, R01DK117281, R01DK125480, R01DK120858, R01DK111436, R01ES027544, RF1AG069966, HL153320, AG070687, R01HD07857, R01HD008818, P01DK059820; P01DK113954 and P20 GM135002). Further support was provided by USDA/CRIS (51000-064-01S), American Diabetes Association (1-17-354 PDF-138) and American Heart Association awards (16POST27260254).
/Public Release. View in full here.
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57
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cf5cd1df0ee2161e1684bdc019357275
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1,290,252,037,163,645,200
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You are using an outdated browser. Please upgrade your browser to improve your experience.
Tbio
RAP2B
Ras-related protein Rap-2b
Protein Summary
Description
Small GTP-binding protein which cycles between a GDP-bound inactive and a GTP-bound active form. Involved in EGFR and CHRM3 signaling pathways through stimulation of PLCE1. May play a role in cytoskeletal rearrangements and regulate cell spreading through activation of the effector TNIK. May regulate membrane vesiculation in red blood cells. This intronless gene belongs to a family of RAS-related genes. The proteins encoded by these genes share approximately 50% amino acid identity with the classical RAS proteins and have numerous structural features in common. The most striking difference between the RAP and RAS proteins resides in their 61st amino acid: glutamine in RAS is replaced by threonine in RAP proteins. Evidence suggests that this protein may be polyisoprenylated and palmitoylated. [provided by RefSeq, Jul 2008]
Uniprot Accession IDs
Gene Name
Ensembl ID
• ENST00000323534
• ENSP00000319096
• ENSG00000181467
Illumination Graph
Knowledge Table
Most Knowledge About
Knowledge Value (0 to 1 scale)
interacting protein
0.99
transcription factor binding site profile
0.94
transcription factor perturbation
0.88
kinase perturbation
0.81
molecular function
0.81
IDG Development Level Summary
Tdark
These are targets about which virtually nothing is known. They do not have known drug or small molecule activities
- AND - satisfy two or more of the following criteria:
Pubmed score: 202.3 (req: < 5)
Gene RIFs: 26 (req: <= 3)
Antibodies: 252 (req: <= 50)
Tbio
These targets do not have known drug or small molecule activities
- AND - satisfy two or more of the following criteria:
Pubmed score: 202.3 (req: >= 5)
Gene RIFs: 26 (req: > 3)
Antibodies: 252 (req: > 50)
- OR - satisfy the following criterion:
Gene Ontology Terms: 12
Tchem
Target has at least one ChEMBL compound with an activity cutoff of < 30 nM - AND - satisfies the preceding conditions
Active Ligand: 0
Tclin
Target has at least one approved drug - AND - satisfies the preceding conditions
Active Drug: 0
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57
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cf5cd1df0ee2161e1684bdc019357275
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6,996,365,588,879,352,000
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Welcome, Guest
Full List
32199 publications found in the database
2004 (1316)
*Starting in 2010, coverage has been refocused on core journals.
2004 Publications
The role of CTLs in persistent viral infection: cytolytic gene expression in CD8+ lymphocytes distinguishes between individuals with a high or low proviral load of human T cell lymphotropic virus type 1
Vine, Alison M. et al. J. Immunol. 173(8), 5121-5129, 2004 PubMed
Microarray analyses identify JAK2 tyrosine kinase as a key mediator of ligand-independent gene expression
Wallace, Tiffany A. et al. Am J Physiol Cell Physiol 287(4), C981-991, 2004 PubMed
Signal pathways in up-regulation of chemokines by tyrosine kinase MER/NYK in prostate cancer cells
Wu, Yi-Mi et al. Cancer Res. 64(20), 7311-7320, 2004 PubMed
Identification of differentially expressed genes in scrapie-infected mouse brains by using global gene expression technology
Xiang, Wei et al. J. Virol. 78(20), 11051-11060, 2004 PubMed
Papillomavirus-like particles stimulate murine bone marrow-derived dendritic cells to produce alpha interferon and Th1 immune responses via MyD88
Yang, Rongcun et al. J. Virol. 78(20), 11152-11160, 2004 PubMed
Budesonide exerts its chemopreventive efficacy during mouse lung tumorigenesis by modulating gene expressions.
Yao, R et al. Oncogene 23(46), 7746-52, 2004 PubMed
SAPKgamma/JNK1 and SAPKalpha/JNK2 mRNA transcripts are expressed in early gestation human placenta and mouse eggs, preimplantation embryos, and trophoblast stem cells
Zhong, W. et al. Fertil Steril 82 Suppl 3, 1140-8, 2004 PubMed
Benchtop Genotyping
Jain, M et al. Genetic Engineering News 24(18), 2004
Noise filtering and nonparametric analysis of microarray data underscores discriminating markers of oral, prostate, lung, ovarian and breast cancer
Aris, V. M. et al. BMC Bioinformatics 5(1), 185, 2004 PubMed
< back | page: 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 57 58 59 60 61 62 63 64 65 66 67 68 69 70 71 72 73 74 75 76 77 78 79 80 81 82 83 84 85 86 87 88 89 90 91 92 93 94 95 96 97 98 99 100 101 102 103 104 105 106 107 108 109 110 111 112 113 114 115 116 117 118 119 120 121 122 123 124 125 126 127 128 129 130 131 132 | > next
|
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-456,399,501,938,503,100
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Intracellular membrane fusion
Duncan W. Wilson, Sidney W. Whiteheart, Lelio Orci, James E. Rothman
Research output: Contribution to journalArticle
30 Scopus citations
Abstract
Protein trafficking and membrane assembly are accomplished in eukaryotes by the specific targeting and fusion of vesicles. In this review we describe some of the molecules implicated as components of the fusion apparatus, and evidence that suggests the same factors are recruited for a variety of intracellular fusion events.
Original languageEnglish (US)
Pages (from-to)334-337
Number of pages4
JournalTrends in Biochemical Sciences
Volume16
Issue numberC
DOIs
Publication statusPublished - 1991
Externally publishedYes
Fingerprint
ASJC Scopus subject areas
• Biochemistry
• Molecular Biology
Cite this
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The first theory of evolution is 600 years older than Darwin
Tijana Radeska
Nasīr al-Dīn Tūsī
Nasīr al-Dīn Tūsī
Nasīr al-Dīn Tūsī was a Persian polymath and prolific writer: An architect, astronomer, biologist, chemist, mathematician, philosopher, physician, physicist, scientist, theologian and Marja Taqleed.
He was of the Ismaili, and subsequently Twelver Shī‘ah, Islamic belief. The Muslim scholar Ibn Khaldun (1332–1406) considered Tusi to be the greatest of the later Persian scholars.
Nasīr al-Dīn Tūsī
Nasīr al-Dīn Tūsī.
Tusi has about 150 works, of which 25 are in Persian and the remaining are in Arabic, and there is one treatise in Persian, Arabic and Turkish. During his stay in Nishapur, Tusi established a reputation as an exceptional scholar. Tusi’s prose writings represent one of the largest collections by a single Islamic author.
Writing in both Arabic and Persian, Nasir al-Din Tusi dealt with both religious (“Islamic”) topics and non-religious or secular subjects (“the ancient sciences”). His works include the definitive Arabic versions of the works of Euclid, Archimedes, Ptolemy, Autolycus, and Theodosius of Bithynia.
A Treatise on Astrolabe by Tusi, Isfahan 1505. By Danieliness at the English language Wikipedia, CC BY-SA 3.0, https://commons.wikimedia.org/w/index.php?curid=11449840
A Treatise on Astrolabe by Tusi, Isfahan 1505. Source by Danieliness
In his Akhlaq-i-Nasri, Tusi put forward a basic theory of the evolution of species almost 600 years before Charles Darwin was born. He begins his theory of evolution with the universe once consisting of equal and similar elements.
According to Tusi, internal contradictions began appearing, and as a result, some substances began developing faster and differently from other substances. He then explains how the elements evolved into minerals, then plants, then animals, and then humans. Tusi then goes on to explain how hereditary variability was an important factor for biological evolution of living things:
“The organisms that can gain the new features faster are more variable. As a result, they gain advantages over other creatures. […] The bodies are changing as a result of the internal and external interactions.”
The Astronomical Observatory of Nasir al-Dīn Tusi.
The Astronomical Observatory of Nasir al-Dīn Tusi.
Tusi discusses how organisms are able to adapt to their environments:
“Look at the world of animals and birds. They have all that is necessary for defense, protection and daily life, including strengths, courage and appropriate tools [organs] […] Some of these organs are real weapons, […] For example, horns-spear, teeth and claws-knife and needle, feet and hoofs-cudgel. The thorns and needles of some animals are similar to arrows. […] Animals that have no other means of defense (as the gazelle and fox) protect themselves with the help of flight and cunning. […] Some of them, for example, bees, ants and some bird species, have united in communities in order to protect themselves and help each other.”
Iranian stamp for the 700th anniversary of his death
Iranian stamp for the 700th anniversary of his death
Tusi recognized three types of living things: plants, animals, and humans. He wrote:
“Animals are higher than plants, because they are able to move consciously, go after food, find and eat useful things. […] There are many differences between the animal and plant species, […] First of all, the animal kingdom is more complicated. Besides, reason is the most beneficial feature of animals. Owing to reason, they can learn new things and adopt new, non-inherent abilities. For example, the trained horse or hunting falcon is at a higher point of development in the animal world. The first steps of human perfection begin from here.”
A stamp issued in the republic of Azerbaijan in 2009 honoring Tusi
A stamp issued in the republic of Azerbaijan in 2009 honoring Tusi.
Tusi then explains how humans evolved from advanced animals:
“Such humans [probably anthropoid apes] live in the Western Sudan and other distant corners of the world. They are close to animals by their habits, deeds and behavior. […] The human has features that distinguish him from other creatures, but he has other features that unite him with the animal world, vegetable kingdom or even with the inanimate bodies. […] Before [the creation of humans], all differences between organisms were of the natural origin. The next step will be associated with spiritual perfection, will, observation and knowledge. […] All these facts prove that the human being is placed on the middle step of the evolutionary stairway. According to his inherent nature, the human is related to the lower beings, and only with the help of his will can he reach the higher development level.”
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Reference
Search for REF=[9588].
9588
Reddy, G. S., Manasa, B. P., Singh, S. K. and Shivaji, S.
Paenisporosarcina indica sp. nov., a psychrophilic bacterium from a glacier, and reclassification of Sporosarcina antarctica Yu et al., 2008 as Paenisporosarcina antarctica comb. nov. and emended description of the genus Paenisporosarcina.
Int. J. Syst. Evol. Microbiol. 63: 2927-2933, 2013.
PMID: 23355696.
DOI: 10.1099/ijs.0.047514-0.
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Jump to first unread post. Pages: 1
Anonymous
Re: grade the vendors
#292880 - 04/15/01 12:06 AM (17 years, 6 months ago)
Well, that is only YOUR opinion.... so I hope people are smart enough not to judge by one 'ANONYMOUS' opinion, and an opinion that is WRONG. I have a 'HOMESTEAD' 1/4 print that is producing some the BEST mycelium I have ever seen, it was sucked into syringe, and shot into birdseed.... it is truly, absolutely phenominal, looks like pure feathers, not 1 contam either. Sure homestead makes like 1000% profit on their kits, but they also teach people to grow the CORRECT way using agar/petri's, and compost... I give homestead an A+ for a great kit for newbies.
Pavdog
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Anonymous
Re: grade the vendors
#293257 - 04/15/01 12:06 AM (17 years, 6 months ago)
Well, that is only YOUR opinion.... so I hope people are smart enough not to judge by one 'ANONYMOUS' opinion, and an opinion that is WRONG. I have a 'HOMESTEAD' 1/4 print that is producing some the BEST mycelium I have ever seen, it was sucked into syringe, and shot into birdseed.... it is truly, absolutely phenominal, looks like pure feathers, not 1 contam either. Sure homestead makes like 1000% profit on their kits, but they also teach people to grow the CORRECT way using agar/petri's, and compost... I give homestead an A+ for a great kit for newbies.
Pavdog
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Anonymous
Re: grade the vendors [Re: Anonymous]
#293461 - 04/15/01 08:51 AM (17 years, 6 months ago)
pavlow, yes its MY opinion. isnt that what this forum is for? why is the name "anonymous" any less valid than your's? is pavlow YOUR real name?? seems to me your as anonymous as i am. why dont you post under your real name? i guess your opinion is wrong too.. i havent been here in a while and the layout of this place has totally changed, my old password did not work. look at the posting options, theres one for posting "anonymous". so why the paranoia? theres no conspiracy here. as for my opinion being "wrong", i could _care less_ what you "think." I stand by my opinion of homestead because their product is crap. you even admit in your post that your homestead "print" was only a 1/4 and their kit has a 1000% markup. and you think thats great for a beginner? agar and petris is not the best method for beginners. why did YOU use the syringe method instead of the "correct" way as you mentioned? most beginners dont want to purchase a pressure cooker, petris, and agar,which is why 99.9% of all beginners here use the syringe method. duh. its faster,cheaper, and easier. maybe your friend at homestead would refund my money for the inviable "sporeprint" they sent me. I'd give them a c+ for that.
pgf, so who am i, obviously??
looks like nothing's changed here. the same old whiners and accusers. maybe the shroomery should put up a new forum "the paranoid accusations forum".
thanks _again_ for letting me voice my opinion.
much love,
"anon"
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InvisibleMcMan
Pooh-Bah
Registered: 12/05/00
Posts: 661
Loc: USA
Post deleted by users_request [Re: Anonymous]
#293547 - 04/15/01 12:42 PM (17 years, 6 months ago)
Post Extras: Print Post Remind Me! Notify Moderator
Anonymous
Re: grade the vendors [Re: McMan]
#293683 - 04/15/01 04:56 PM (17 years, 6 months ago)
Gee, thanks for steppin in mcman, it seems that you have already locked close to HALF the threads in this new forum, and I noticed that HALF the posts in those locked threads were written by you...
I thought the 'sporepimp' website was funny as hell, I wanted to make a reply, but couldn't because it was LOCKED.
You should chill a bit on the lockage..... I have never seen so many locked threads in a forum in such a short amount of time, especially among so few topics.
You seem more like a babysitter or a security guard
Is THIS thread gonna be locked now?
Let people debate if they want to....... even if they seem to be dicks about it.... let em
I think even the 'unknown user' above would agree with that.
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InvisibleThorA
Anti-Theist OVERLORD
Male User Gallery
Registered: 08/12/98
Posts: 9,943
Loc: Iceland
Re: grade the vendors [Re: Anonymous]
#293698 - 04/15/01 05:19 PM (17 years, 6 months ago)
Someone posting as Anonymous is NOT acceptable.... Its pretty obvious the individual is going to cause trouble hiding behind anonymity....
So let me say again, any post I see by anonymous will be deleted, simple as that.
This should be fixed in the near future, but until then Moderators will delete Anonymous posts.
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OfflineDystopian Harbinger
Cheech Wizard
Registered: 02/26/01
Posts: 139
Last seen: 14 years, 4 months
Re: grade the vendors [Re: Thor]
#293717 - 04/15/01 05:53 PM (17 years, 6 months ago)
Um, Thor....whats the difference between someone posting anon and someone creating 10 sock puppets? From the majority of problems I have seen here causing "trouble" from "anonymity" has never been the problem. Threatening to delete an anon post because of the fact that it has no name attached to it is as close as I have seen to opressive, heavy-handed behavior on this board yet. I understand that as a moderator you 'have the whip' so to speak but dont you feel thats a bit...excessive?!?!?!?
If mankind minus one were of one opinion, then mankind is no more justified in silencing the one than the one - if he had the power - would be justified in silencing mankind.
John Stuart Mill (1806 - 1873)
--------------------
At times one remains faithful to a cause only because its opponents do not cease to be insipid.
-Nietzsche
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InvisibleThorA
Anti-Theist OVERLORD
Male User Gallery
Registered: 08/12/98
Posts: 9,943
Loc: Iceland
Re: grade the vendors [Re: Dystopian Harbinger]
#293722 - 04/15/01 06:01 PM (17 years, 6 months ago)
There is a big difference between registered users and anon users.... Moderators can block registered users who cause trouble, we can't do anything about Anonymous ones....
In fact the shroomery originally started with allowing anon users and it became chaos.
Even if its sock puppets, they still have to behave, if they don't they get banned... But with anon users this is not the case, so obviously we can't allow them.
Let me remind you all that anon users are NOT supposed to be able to post, this is being looked into as we speak, and soon this wont be a problem.
I can't believe you would see this as oppressive, anon users would eventually turn this place into utter crap if they were allowed to do so.
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InvisibleLallafa
p_g monocle
User Gallery
Registered: 04/13/01
Posts: 2,598
Loc: underbelly
Re: grade the vendors [Re: Thor]
#293852 - 04/15/01 10:08 PM (17 years, 6 months ago)
z
Edited by Lallafa (02/25/10 10:33 AM)
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Team:ESBS-Strasbourg/proteolux/scientific/proteoluxpro
From 2010.igem.org
(Difference between revisions)
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<font size="1">Figure 3: Light controlled intrabody formation and specific target protein degradation.
<font size="1">Figure 3: Light controlled intrabody formation and specific target protein degradation.
A: Structure of an IgG antibody. Shown are the two long heavy (H) chains and the small light (L) chains. The constant domains are shown in green (C) and the variable domains in violet (V). The heavy chains consist of 3 constant domains (CH1, CH2 and CH3) and a variable domain VH. The light chains are composed of a constant (CL) and a variable (VL) domain. The chains are intra- and interconnected by disulfide bridges (yellow lines). B1.1 and B1.2: Fusion constructs for the light and heavy chains. B1.1: The blue light photoreceptor Zeitlupe (ZTL), the Phytochrome interacting factor (PIF) and the C-terminal degradation tag DAS are fused to the C-terminus of the light chain. B1.2: The gigantea (GI) sequence is fused in the hinge region of the antibody. The two conserved cysteine residues for the disulfide bridge are maintained, the two constant domains (CH2 and CH3) of the heavy chain are deleted. C: Blue light dependent photo conversion of ZTL. The absorption of blue light (475 nm) by the PAS-like LOV domain of ZTL leads to a conformational change allowing GI binding (D). D: Blue light induced formation of the active intrabody. The binding of GI to ZTL under blue light brings the light and heavy chain together and restores the natural disulfide bridge between the two. The two variable domains can now form an active antigen binding site that binds to the protein of interest. E: Red light induced protein degradation. PIF binds to PhyB under red light conditions bringing the DAS tag in proximity to the ClpXP protease leading to degradation of the protein of interest bound to the intrabody.</font></div>
A: Structure of an IgG antibody. Shown are the two long heavy (H) chains and the small light (L) chains. The constant domains are shown in green (C) and the variable domains in violet (V). The heavy chains consist of 3 constant domains (CH1, CH2 and CH3) and a variable domain VH. The light chains are composed of a constant (CL) and a variable (VL) domain. The chains are intra- and interconnected by disulfide bridges (yellow lines). B1.1 and B1.2: Fusion constructs for the light and heavy chains. B1.1: The blue light photoreceptor Zeitlupe (ZTL), the Phytochrome interacting factor (PIF) and the C-terminal degradation tag DAS are fused to the C-terminus of the light chain. B1.2: The gigantea (GI) sequence is fused in the hinge region of the antibody. The two conserved cysteine residues for the disulfide bridge are maintained, the two constant domains (CH2 and CH3) of the heavy chain are deleted. C: Blue light dependent photo conversion of ZTL. The absorption of blue light (475 nm) by the PAS-like LOV domain of ZTL leads to a conformational change allowing GI binding (D). D: Blue light induced formation of the active intrabody. The binding of GI to ZTL under blue light brings the light and heavy chain together and restores the natural disulfide bridge between the two. The two variable domains can now form an active antigen binding site that binds to the protein of interest. E: Red light induced protein degradation. PIF binds to PhyB under red light conditions bringing the DAS tag in proximity to the ClpXP protease leading to degradation of the protein of interest bound to the intrabody.</font></div>
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Latest revision as of 01:25, 30 November 2010
{|
Contact | Sitemap
ESBS-Strasbourg
ProteOlux ®
Proteolux P
As shown previously the Proteolux system offers a light-inducible specific mechanism to degrade tagged protein. This system may be applied to any protein expressed in the cytoplasm of the host cell. For the original system a homologue recombination step is necessary in order to fuse the PIF-DAS tag to the target protein in the host cell or organism. This step requires additional time in order to prepare the experiment and might further change the normal protein physiology, which should be observed, due to the creation of a fusion protein. It is known, that the function of a fusion protein can be different of the wild-type protein due to different stability of the mRNA after the homologue recombination leading to a different translation rate or the expressed protein does not fold correctly and forms aggregates in the cytoplasm. These drawbacks of the original system are solved in Proteolux’s P (Plus and Pro) system.
The Proteolux Plus and Pro system allows the observation of the native target protein functions without long experiment preparation and interference with the cell metabolism. The developed strategy is to use a specifically engineered intrabody against the target protein. The binding of the intrabody to the protein can lead to the direct inhibition of the protein function. In the case, that the protein is not directly inhibited and to prevent re-establishment of the protein function the intrabody-protein complex is targeted to the proteasome. The binding of the intrabody to the target protein has to be regulated to avoid constant degradation of the target protein. Therefore, Proteolux offers the Plus and Pro system of different complexity, according to the experimenter demand.
Intrabodies are antibody derived proteins that bind to an intracellular protein within the cell. The normal antibody (figure X) has to be modified due to the reducing environment within the cytoplasm that prevents disulfide bridge formation. Therefore, single-chain antibodies, which are fusion proteins of the variable region of the light chain (VL) and the heavy chain (VH) connected by a short linker, are often expressed.
Proteolux Pro ®
Light-controlled regulation of the intrabody activity.
The idea is to have an inactive intrabody which can be assembled on demand into its active form. Therefore, the structure of a general IgG antibody has to be regarded in greater detail (figure 1) [Garrett RH and Grisham CM, Biochemistry 2nd edition].
Figure 1: Overview over the structure of an IgG antibody. The active IgG antibody is composed of two heavy (H) chains (outer long chains) and the small light (L) chains (inner short chains). The constant domains are shown in green (C) and the variable domains in violet (V). The heavy chains consist of 3 constant domains (CH1, CH2 and CH3) and a variable domain VH. The light chains are composed of a constant (CL) and a variable (VL) domain. The Fab region which is composed of the variable domain and the CH1 domain is connected via a flexible hinge region to the Fc part of the antibody (CH2 and CH3 region). The chains are intra- and interconnected by disulfide bridges (yellow lines). There are two disulfide bridges that interconnect the two heavy chains and each variable chain is connected to one heavy chain via one disulfide bridge. The active antibody is only formed when the light chain is connected to the heavy chain in order to form the antigen binding site, which is situated between the variable domains.
The formation of the antigen binding site is dependent on the correct binding of the VL to the VH domain, which is enhanced by a strong affinity between the constant regions and the disulfide bridge between the light and the heavy chain. In the Proteolux Pro system, this permanent disulfide bridge is replaced by a light inducible interaction between two proteins. In order to avoid interference with the PhyB-PIF interaction, other interaction partners were searched which are active under light conditions that do not activate phytrochrome B (figure 2).
Figure 2: Absorption spectrum of phytrochome B containing the PCB chromophore. The absorption maxima of the two red light forms are visible as two distinct peaks at 658 nm for the red light form and at 720 nm for the far-red light form. The absorbance is lowest in the blue/green light part of the spectrum between 450nm and 550nm. Therefore, it is save to work under blue/green light conditions to avoid the activation of phytrochrome B.
The absorbance spectrum of phytrochrome B reveals that it does not absorb under light conditions between 450 nm and 550 nm which correlates to blue/green light. Therefore, the blue light (475 nm) regulated interaction between the Arabidopsis thaliana photoreceptor Zeitlupe (ZTL, Gene ID: 835842) and Gigantea (GI, Gene ID: 838883) is used to replace the disulfide bridge function. Zeitlupe contains a light sensing PAS-like LOV domain at its N-terminal end and a C-terminal Kelch repeat domain, which is involved in protein-protein interaction [Lariguet P and Dunand C, 2005; http://www.uniprot.org/uniprot/Q94BT6]. The GI protein has a more than 4 fold affinity to ZTL under blue light conditions [Kim WY, 2007].
In order to prevent the strong affinity between the constant domains of the light and the heavy chain, only the low affinity variable domains are used in the construction.
The ZTL sequence is fused together with the normal PIF-DAS-tag to the C-terminus of the VL domain and the GI sequence followed by a GST sequence to the C-terminus of the VH domain. The GST dimerizes and connects therefore two VH domains. This allows the formation of bivalent intrabodies with higher protein binding capacity.
The expression of such a modified intrabody allows the formation of the active intrabody only under blue light conditions. The protein expressing phenotype can be analyzed under far-red light conditions. When the protein should be degraded, the intrabody formation is triggered under blue light (475nm) resulting in the formation of an active antibody binding site and fixation of the target protein by the intrabody. To ensure, that the protein is not active anymore the intrabody-protein complex can be tethered to the protease using red light conditions. This procedure is summarized in figure 3.
Proteolux Pro offers the first light-controlled intrabody activity which can be used to analyze any protein in its native conformation without interference with the cell metabolism.
Figure 3: Light controlled intrabody formation and specific target protein degradation. A: Structure of an IgG antibody. Shown are the two long heavy (H) chains and the small light (L) chains. The constant domains are shown in green (C) and the variable domains in violet (V). The heavy chains consist of 3 constant domains (CH1, CH2 and CH3) and a variable domain VH. The light chains are composed of a constant (CL) and a variable (VL) domain. The chains are intra- and interconnected by disulfide bridges (yellow lines). B1.1 and B1.2: Fusion constructs for the light and heavy chains. B1.1: The blue light photoreceptor Zeitlupe (ZTL), the Phytochrome interacting factor (PIF) and the C-terminal degradation tag DAS are fused to the C-terminus of the light chain. B1.2: The gigantea (GI) sequence is fused in the hinge region of the antibody. The two conserved cysteine residues for the disulfide bridge are maintained, the two constant domains (CH2 and CH3) of the heavy chain are deleted. C: Blue light dependent photo conversion of ZTL. The absorption of blue light (475 nm) by the PAS-like LOV domain of ZTL leads to a conformational change allowing GI binding (D). D: Blue light induced formation of the active intrabody. The binding of GI to ZTL under blue light brings the light and heavy chain together and restores the natural disulfide bridge between the two. The two variable domains can now form an active antigen binding site that binds to the protein of interest. E: Red light induced protein degradation. PIF binds to PhyB under red light conditions bringing the DAS tag in proximity to the ClpXP protease leading to degradation of the protein of interest bound to the intrabody.
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Wikia
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DNA
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Redirected from Gene
DNA, or deoxyribonucleic acid, is an extremely complex molecule that serves as the "master molecule" of organic life by encoding for proteins that form cell structures. DNA molecules are made up of two intertwined chains of simpler molecules called bases, assembled on rails of sugar and phosphate molecules like rungs on a ladder.
Four different kinds of molecules form the rungs of the DNA ladder: adenine, thymine, guanine, and cytosine, which are typically referred to by their first letters, A, T, G, and C. In the DNA molecule, A always pairs with T, and G always pairs with C. DNA molecules replicate by "unravelling" their rails. Each rail keeps its associated base. Complementary bases (A for T, G for C) attach to the free bases until two new strands of DNA are created.
Unique to each individual, DNA is often used to identify individuals. By the 22nd century, Vulcans were obtaining DNA samples from every infant Vulcan and storing the DNA sequences in a massive database known as the Vulcan Genome Registry. In 2154, a Romulan back faction of the Vulcan High Command planted a DNA sample from T'Pau on the remains of a bomb exploded in the United Earth embassy, hoping to frame her and the Syrrannite movement for the bombing. However Doctor Phlox quickly determined that the DNA had been purposely planted on the bomb fragments.(ENT episode: "The Forge")
In 2369, following clues developed by his mentor, Richard Galen, Captain Jean-Luc Picard discovered that an ancient race of humanoids had seeded many planets with their DNA billions of years earlier.
The result of this DNA being spread across the galaxy is the humanoid form itself. This DNA creates a tendency toward a specific external form. The similarity created allows even for inter-species reproduction between species that evolved quadrants apart, however the internal workings even down to the base element of the blood can still be quite diverse. (TNG episode: "The Chase").
The following year, former Ferengi DaiMon Bok somehow resequenced the DNA of Jason Vigo in order to convince Captain Jean-Luc Picard that Vigo was in fact his son in order to take revenge on Picard over the loss of his son. This elaborate deception was uncovered by Doctor Beverly Crusher when Vigo began suffering seizures resulting from the DNA resequencing, and also due to the fact that Vigo suffered from Forrester-Trent Syndrome. Forrester-Trent Syndrome was inherited from one parent, and neither Picard or Miranda Vigo had the condition.(TNG episode: "Bloodlines")
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Instigator / Pro
26
1500
rating
87
debates
46.55%
won
Topic
Resolved: The Theory of Evolution is a sound theory of how life developed on Earth.
Status
Finished
All stages have been completed. The voting points distribution and the result are presented below.
Arguments points
3
21
Sources points
12
14
Spelling and grammar points
6
7
Conduct points
5
4
With 7 votes and 20 points ahead, the winner is ...
Lazarous
Parameters
More details
Publication date
Last update date
Category
Science
Time for argument
Two weeks
Voting system
Open voting
Voting period
Two months
Point system
Four points
Rating mode
Rated
Characters per argument
15,000
Contender / Con
46
1538
rating
4
debates
75.0%
won
Description
~ 1,239 / 5,000
Rounds:
1. Opening Statements
2. Rebuttal and Questions
3. Defense
4. Closing Arguments and Summary
Rules:
1. No round forfeits
2. It should go without saying, but keep it respectful
3. No new arguments in the final round
4. The BoP is evenly shared.
Definitions
1. Theory: In science, a theory is "an explanation of some aspect of the natural world that has been substantiated through repeated experiments or testing" [1]
2. Evolution: At the most basic level, evolution is defined as “the frequency of alleles within a gene pool from one generation to the next.”[2] Consequently, “genetic changes over many generations ultimately result in the emergence of new and different species from a single ancestral species” [3] As a result, “all known living, terrestrial organisms are genealogically related. All existing species originated gradually by biological, reproductive processes on a geological timescale” [4]
3. Sound: Based on strong scientific evidence
Sources
1. https://www.scientificamerican.com/article/just-a-theory-7-misused-science-words/
2. http://www.talkorigins.org/faqs/evolution-definition.html
3. Fairbanks, Daniel J. Evolving: The Human Effect and Why it Matters.
4. http://www.talkorigins.org/faqs/comdesc/
Round 1
Pro
Thank you, Lazarous, for accepting this debate. I’m looking forward to another exciting debate with you.
I am going to divide my arguments into two parts. In the first part, I will give an overview of evolution and what I believe to be the strongest lines of evidence for it. In the second part of my arguments, I will look at creationism and show how Young Earth Creationism is an utter failure.
PART 1: Evolution
The Theory of Evolution is one of the most misunderstood theories in science, yet it is also the backbone of modern biology. Indeed, as Theodosius Dobzhansky stated, "Nothing in biology makes sense, except in the light of evolution." The Theory of Evolution explains not only the biodiversity of life but is vitally important in fields such as medicine and ecology.
I. Misconceptions
I want to start off this debate by debunking common misconceptions about evolution.
1. Evolution is not true because it cannot explain the origins of life or the universe
Evolution is a theory on the biodiversity of life. It does not make any assertions to how life formed or how the universe came into being. This argument is an argument from ignorance. Just because we do not know yet how life got started or how the universe got here does not mean that evolution is false. This is like saying that the atomic theory of matter is false because we don't know the origins of the atom.
2. Evolution means atheism
Again, this is false. The vast majority of Christians accept evolution and many great evolutionary biologists like Theodosius Dobzhansky and Francis Collins are committed Christians. Theodosius Dobzhansky was an orthodox Christian, Francis Collins is proudly an evangelical, and many prominent evangelicals like William Lane Craig and Biologos accepts evolution.
II. Evolution by Natural Selection is an Observable Fact
A. “Micro” Evolution
We have observed evolution by natural selection both in the lab and in nature. When we expose bacteria to antibiotics, chance mutations enable them to form resistance to the antibiotic causing them to become stronger. The end result is bacteria with the favorable traits necessary to resist antibiotics resulting in deadlier diseases.
This is well-known as “micro-evolution” or “the change in allele frequencies in the gene pool.” This is so well-observed and documented that no creationist will deny this.
B. Speciation
Speciation is the emergence of new species from an ancestral species. This is probably the most important prediction of evolution. If evolution were true, then we should observe the formation of new species. As it turns out, speciation has been observed so many times [1] that even creationists accept it [2], although they try to rationalize it by denying that speciation perfectly fits the definition of evolution or by simply moving the goalpost.
You can think of speciation like language: As time goes on, new words are added, people spread out, words change meaning, and thus new languages are formed. This is how Latin turned into Spanish, French, Italian, Romanian, and the rest of the romance languages from a single ancestral language. You can think of the minor changes in pronunciation and meaning to be “microevolution” and the emergence of new languages as “macroevolution.”
III. Genetics
A. Genetic Comparison
1. Human Evolution
In my opinion, genetics offers the most profound case for evolution. The closer related a specie is the more genetic material they have in common. Using genetic markers, we can trace with stupendous accuracy on how humans and other species migrated. When I got my DNA sequenced from ancestry.com, I was shocked to see just how accurate it was. Not only were they able to tell the region of Europe where I descend from, they were also able to pinpoint exactly where my family settled in the United States and they were even able to tell when they came!
We can do this to trace human ancestry back to where humanity first evolved. Using mitochondria DNA, DNA that is passed on from mother to offspring, we can trace our maternal lineage back to Africa roughly 200,000 years ago [3].
Using the same principles that determine paternity, we discovered that humans and chimpanzees are about 95-99% similar, which suggests that the two species are closely related [4]. What’s more, is that we can determine when humans and chimpanzees diverged. This is dated to about 7-8 million years ago [4]. Of course, as more genetic information becomes available and more studies are done, the more refined this date will become.
2. HIV-SIV
Using the same principles listed above, we can use evolution and genetics to learn when and how new diseases evolved and use that information to learn how to treat them. HIV is a perfect example. In the 1980’s, people were dying left and right of this new disease. Where did it come from and how did it evolve? Let’s find out!
There are actually two main types of HIV: HIV 1 (most common) and HIV 2 (less common). Using genetics, we found that HIV evolved from SIV, a virus that infects non-human primates. Most likely, humans were butchering meat from an infected animal and that is how they initially came in contact. But there is a problem. Humans are naturally immune to SIV, so something had to happen. In his book Evolving: The Human Effect and Why it Matters, Dr. Fairbanks shows exactly how this happened [6]:
“The virus had to mutate into a form that could overcome natural immunity to SIV in humans. Mammals have a gene that encodes a protein called tetherin. This protein has evolved to confer resistance to retroviruses by tethering them to the inside of the cell they infect and preventing the virus from replicating. For SIV cpz to successfully infect a human, it had to overcome the suppressive effect of human tetherin.
The SIV cpz evolved by acquiring two anti-tetherin genenes called nef and vpu, one from each of the original monkey viruses that fused to form the chimpanzee virus. The nef gene mutated to overcome chimpanzee tetherin, but the vpu gene remained essentially insert. When the virus jumped to humans, human tetherin was so different that the nef gene could not overcome human tetherin. Instead, the vpu gene mutated to overcome human tetherin, allowing HIV-1 group M to infect humans.
A mutation in a second gene, called gag, was also required for the chimpanzee virus to jump to humans. Interestingly, a case in which HIV infected a chimpanzee is known, and the gag gene of this virus mutated back to the original form in the chimpanzee to successfully re-infect its ancestral host.”
B. ERVs
Endogenous retrovirus are viruses that incorporate themselves into our DNA. As I already pointed out, humans, bonobos, and chimps are 95-99% similar. This strongly suggests that we are closely related and share a recent common ancestor.
When we compare genetics, we can look at ERVs and use that to help us the dots. As it turns out, humans and chimps have thousands of ERVs in common [7]. So, either the ERV independently inserted itself into the same location thousands of times or we share a common ancestor who had it. The latter is far more likely.
IV. Fossil Record
A. Geological column
The geological column perfectly fits within the evolutionary framework. We never find a fossilized rabbit in the Precambrian layer and we never find a dinosaur fossil on top of a human fossil.
B. Transitional fossils
Where are all the transitional fossils? I’m glad you asked!
1. Archaeopteryx
Archaeopteryx is probably the first transitional fossil found. It was found only a few years after Darwin published The Origins of the Species. As noted by TalkOrigins, it has both bird and dinosaur like features that are hard to explain away [8].
The main bird traits are:
· long external nostrils.
· quadrate and quadratojugal (two jaw bones) not sutured together.
· palatine bones that have three extensions.
· all teeth lacking serrations.
· large lateral furrows in top rear body of the vertebrae
And the reptilian features are:
• no bill
• teeth on premaxilla and maxilla bones
• nasal opening far forward, separated from the eye by a large preorbital fenestra (hole)
• neck attached to skull from the rear
• center of cervical vertebrae that have simple concave articular facets
• long bony tail; no pygostyle
• ribs slender, without joints or uncinate processes, and not articulated with the sternum
• sacrum that occupies six vertebrae
• small thoracic girdle
• metacarpals free (except third metacarpal), wrist hand joint flexible
• claws on three unfused digits
• pelvic girdle and femur joint shaped like those of archosaurs in many details
• bones of pelvis unfused
and over 100 other differences from birds
V. Summary
Evolution has been vindicated time and time again. If my opponent wishes to overturn over 150 years of biology, then he is in for a tough ride. The mere fact that evolution has been observed numerous times is enough evidence to vote for pro and the genetic and fossil records are just the icing on the cake.
PART 2: Failures of Creationism
I identify three main predictions that the Bible makes in the first 5 chapters of Genesis. In the first chapter of Genesis, the Bible predicts the order in which the universe was created, the second key prediction is the age of the universe and the third key prediction is how long humans once lived. If any of these three are shown to be false, then the entire Genesis creation myth collapses.
V. Order of Creation
In the Genesis Creation myth, God created the universe in 6 days. The days of creation are:
Day 1: Light and darkness
Day 2: Sky and sea
Day 3: Vegetation and land
Day 4: Stars, sun, and moon
Day 5: Sea animals and birds
Day 6: Humans and land animals
The order that the Book of Genesis proposes is inconsistent with what we know in science. How can day and night exist before the Sun? How can the vegetation survive without the Sun? Without the Sun, the Earth would have been at or just above absolute zero.
Modern astronomy has witnessed the lifecycle of stars and solar systems. The way solar systems form is nothing like how it is described in the Bible. Stars form when clouds of gas collapse under its gravity. This is called a proto-star. When the star heats up enough it begins nuclear fusion. That’s when it is fully a star. Not only have we observed this process [9], but we have found young stars with planetary disks around them [10]. Even more impressive is that we discovered moon forming disks around new exoplanets [11]. Solar system formation is nothing like what’s described in the Bible.
VI. Age of the Universe
Creationist argue that the entire universe is less than 6,000 years old. A wealth of independent lines of evidence proves that the universe is billions of years old. Here I will give just two lines of evidence.
1. Distant starlight
Light travels at a speed of 299,792 kilometers per second. If an object is 1 light year away, it follows that the light from that object must have taken 1 year to reach the observer. The furthest distance we have seen is roughly 13 billion light-years away [12]. Logically it follows that the light took 13 billion years to reach us, thus the universe has to be at least 13 billion years old.
2. Radiometric dating
Radiometric dating is the most accurate way to tell the age of an object. We can test the accuracy of radiometric dating by cross-dating it with various isotopes as well as testing it on the age of known objects. This is incredibly useful in archeology. For example, researchers found an old Quran that dated back to the time of Muhammad [13]. When we apply these techniques to rocks and asteroids, we discovered that the Earth is approximately 4.6 billion years old [14], a far cry from 6,000 years old.
VII. Lifespan of Humans
As of today, the oldest person alive is 116 years old [14]. However, this is a baby compared to the antediluvian humans. In the Bible, the oldest person to die was Methuselah at 969. There is not a shred of evidence to suggest that humans lived that long and all evidence points to the contrary.
From what we know, life expectancy from the paleolithic era up to early modern England was less than 40-years-old [15].
VIII. Summary
The major predictions made in the Book of Genesis are a complete failure. The Theory of Evolution has been vindicated time and time again whereas Creationism can't even get off the ground. If you can't trust what was written in the very first chapter of the Bible, then you can't trust what's written in the rest. I think I made my point.
I look forward to your reply.
Sources
6. Fairbanks Evolving: The Human Effect and Why it Matters
9. Carrasco-González, C., et al. “Observing the Onset of Outflow Collimation in a Massive Protostar.” Science, vol. 348, no. 6230, 2015, pp. 114–117., doi:10.1126/science.aaa7216.
Con
First of all, I would like to thank Virtuoso for challenging me to this debate. I expect this will be quite interesting. In similar fashion, I will start my debate by debunking several misconceptions about evolution:
Misconceptions:
Misconception 1: Any genetic change through mutations constitutes evidence for Darwinian evolution.
• Oxford defines evolution as, “The process by which different kinds of living organisms are thought to have developed and diversified from earlier forms during the history of the earth” [1]. As acknowledged through the use of the word ‘developed’ in the above definition, Darwinian evolution requires that mutations increase genetic information over time. The human genome has 3.2 billion base pairs [2] while single celled organisms have as few as 160 thousand [3]. In order for this single cell to evolve into a human, the genome would have to increase in length by a factor of 20,000. Furthermore, Darwinian evolution must also produce new completely original biological structures (lungs, eyes, flukes etc.). All changes that result in a loss in genetic information are deteriorating the organism; therefore, these sorts of changes are the opposite of Darwinian evolution.
Misconception 2: Darwinian evolution is the only explanation for bio-diversification.
• Darwinian evolution is neither the only nor the most scientific explanation for the biodiversity observed in creatures today. Natural selection, speciation, and epigenetics are all examples of scientifically observed mechanisms that create biological variety through the sorting and loss of existing genetic information. The effects of these scientific forces are at best indifferent to Darwinian evolution, and frequently result in the loss of genetic information causing complex organisms to become simpler.
Introduction: Darwin tried to answer a fundamentally genetic question without any knowledge of genetics. Darwin published The Origin of Species in 1859 and yet DNA wasn’t even discovered until the 1950’s, nearly 100 years later. Darwin admitted, “Our ignorance of the laws of variation is profound” [4]. Evolution succeeds or fails at the genetic level, and yet Darwin, by his own admission, was basing his theory on a profound ignorance of genetics. Darwinian evolution is based on the premise that mutations cause information to increase and develop over time, and yet, the field of genetics now overwhelmingly supports that the genome is very complex, highly functional, and consistently deteriorating.
I. The scientific demise of the Chimp-Man story:
1. The Demise of ‘Junk DNA’: The evolutionary agenda has had profound effects on the assumptions made regarding DNA. John Mattrick claims, “the presence of non-protein-coding or so-called ‘junk DNA’ that comprises >90% of the human genome is evidence for the accumulation of evolutionary debris by blind Darwinian evolution, and argues against intelligent design, as an intelligent designer would presumably not fill the human genetic instruction set with meaningless information” [5]. Twenty-six years later the ENCODE Project Consortium analyzed the genome and concluded that, “These data enabled us to assign biochemical functions for 80% of the genome, in particular outside of the well-studied protein-coding regions” [6]. ENCODE Lead Analysis Coordinator Ewan Birney followed this release by claiming that, “It’s likely that 80 percent will go to 100 percent” [7]. Most if not all of the genome is functional; therefore, evolutionists were terribly wrong in declaring that most of the genome is ‘junk’.
2. DNA Similarities Debunked: The ENCODE project found that approximately 50% of the functional non-coding (junk) DNA compared in the 23 different mammals studied was not conserved (not similar between species) [8]. It is now clear that a comprehensive DNA comparison between apes and humans is in order. Evolutionists typically claim that ape and human genetics are 96-98% similar; however, these stats only compare 2% of the genome. Conveniently, this 2% of the genome happens to be the most similar 2%. When the entire genome is compared the result is profoundly different. A study published by Dr. Jeffrey Tomkins in the peer reviewed journal, Answers Research Journal revealed that, “Genome-wide, only 70% of the chimpanzee DNA was similar to human under the most optimal sequence-slice conditions” [9]. This really should come as no surprise since in 2002 evolutionist Roy Britten indicated a genome-wide similarity of about 70% between chimpanzees and humans [10]. Human DNA is profoundly different from chimpanzee DNA; therefore, Darwinian evolution proves to be terribly wrong in its predictions once again.
3. An Outrageous Number of Mutations: Considering that chimpanzee and human DNA is about 30% different and that there are about 3.2 billion base pairs in the human genome [2], there are approximately 960 million base pair differences between chimps and humans. Dr David Dewitt examined a sample size of 125 million of these base pair differences and found that, “there are about 40 million total separate mutation events that would separate the two species in the evolutionary view” [11]. Therefore, in order to account for the entire 30% of genetic disparity between chimps and humans roughly 307 million mutations would have to occur with the estimated 300,000 generations [11] since crimps and humans supposedly divided from their chimp like ancestors. This would require an average of 1,023 mutations to be locked in with each generation. This staggeringly large number of mutations being ‘locked in’ in such a small number of generations creates a problem known as “Haldane’s dilemma.”
4. Haldan’s Dilemma explained: After extensively studying the rate at which mutations can be locked into a population, Dr John Sanford explains, “Haldane realized that even if there was an abundant and continuous supply of beneficial mutations, natural selection must be very limited in its ability to amplify such mutations to the point of where they are ‘fixed’ within a sizeable population. He calculated that for a mammalian population such as man, given an evolutionary population size of 10,000, only about 1,000 beneficial mutations could be selectively fixed within 6 million years…. That scenario would require roughly 1,000 independent beneficial fixations per generation. Haldane said this was impossible: he estimated that at best there should be only about 1 fixation every 300 generations. This problem has been extensively investigated by Walter ReMine, who has used an entirely independent mathematical formulation of the problem and has reached exactly the same conclusions [12]…. Our experiments strongly validate the work of Haldane and ReMine. We see that, depending on the specific settings, only a few hundred to a few thousand selective fixations can realistically occur during 300,000 human generations (about 6 million years)… [13]. We are very confident that our numerical simulation experiments are the best way to understand this problem, Between Haldane, ReMine, and our own work, the matter is clearly settled. This means the ape-to-man story is not even remotely feasible” [14]. This problem is also recognized by evolutionists Rick Durrett and Deena Schmidt who calculated the time it would take for two codependent mutations to become fixed in a human population at “>100 million years” [15].
II. Dual Coding Genes: It has been found that some genes code for multiple unrelated proteins. Evolutionist Sen-Yu Chung examined the implications of dual coding and found that, “Dual coding is a costly arrangement because it limits the flexibility of amino acid composition. A silent change in one frame [coding sequence for one protein] is almost always guaranteed to be amino acid changing in the other…. Here we show that although dual coding is nearly impossible by chance, a number of human transcripts contain overlapping coding regions” [16]. Since dual coding both (a) “limits the flexibility of amino acid composition”, and is (b) “nearly impossible by chance”, dual coding genes should not be created or favored for selection under evolution; therefore, why is dual coding abundant in nature?
III. Genetic Entropy (genetic decay) – The Strongest Argument Yet: I began my debate by bringing a frequently ignored but all two crucial distinction to light. Darwinian evolution claims that mutations must result in a net increase in information over time. Only through an increase in information can a single-celled organism ever hope to become a human. Evolution and Genetic Entropy are mutually exclusive. If the genome decays over time then Darwinian evolution is the product of wishful thinking.
• Something for Nothing – The Darwinian Dream: Dr. Jerry Bergman studied a sample size of 453,732 mutations in search for a mutation possessing the ability to increase the genome. He found that a mere 4 in 10,000 of these mutations were “beneficial”, and after a review of these “beneficial” mutations it was found that these mutations were only beneficial in a very narrow sense, since they all involved a loss of function (loss of information). [17]. Dr Bergman did not find a single mutation possessing the ability to increase the genome as required for Darwinian evolution. One of the largest studies by Adam Boyko PhD et al, found that 27-29% of amino-acid-changing mutations are neutral or nearly neutral, 30-42% are moderately deleterious, and nearly all the remainder (~36%) are highly deleterious or lethal [18]. This study was also unable to identify any mutations possessing the characteristics required for evolution. It is now clear that mutations capable of increasing the genome are quite rare (perhaps nonexistent), but, assuming they do exist, let’s see if natural selection is capable of weeding out all the garbage and stacking these quite rare mutations (possessing the ability to add genetic information to the genome) on each other from generation to generation.
Hail Natural Selection Our Savior?: Natural selection is not an all powerful force. It is now known that natural selection possesses multiple limitations that severely hamper its abilities to produce the results claimed by evolution:
• Cost of Selection Limitation: Natural selection is highly limited on how many of a population it can kill off, since perpetual mass homicide will inevitably lead to extinction. John Sanford explains that, “For the human population, it becomes clear that that the maximum part of our population which can be ‘spent’ for all selection purposes is much less than 33%, and, according to Haldane, might realistically be in the range of 10%” [19]. Since 66-78% of all mutations are deleterious, natural selection can only hope to remove a maximum of half of these damaging mutations created each generation. The rare occurrences of mutations that add genetic information (as required by evolution) would be crushed under the massive load of deleterious mutations accumulating in the population each generation. Natural selection simply can’t remove the deleterious mutations fast enough to give evolution a chance.
• The Package Deal Limitation: Mutations can’t be selected individually by natural selection; rather, each organism is an inseparable package deal. John Stanford studied this issue in depth and concluded that, “the number of all types of new mutations, including conversions, must be much more than 100 per person per generation. These mutations, which include many macro-mutations, must clearly change thousands of nucleotides per person per generation” [20]. Since 66-78% of mutations are deleterious, even if a human were to receive a beneficial information-increasing mutation, this mutation would have 66 to 78 deleterious mutations stacked on top of it before being passed on to the next generation. Indeed, any increase to the genome one mutation can hope to achieve would be easily overwhelmed by the vast number of deleterious mutations, even within a single generation.
Indeed, either of these limitations, in combination with the well established rate of occurrence of beneficial and deleterious mutations, establishes solid ground for concluding that evolution is impossible. In combination, these limitations turns evolution into nothing more than wishful thinking.
Conclusion: Darwin was completely ignorant of the scientific laws of genetic inherency, and yet he made predictions about how genetics work. Darwinian evolution predicts highly dysfunctional genomes developing to a more complex state, and yet, the scientific evidence supports that genetics are highly functional and in a state of perpetual decay. Indeed, the genetic science is yielding results completely opposite of those required to support Darwinian evolution. Science demonstrates that the genome is complex, efficient, and consistently deteriorating over time. The only reasonable conclusion is that Darwinian evolution is not scientifically tenable.
1. https://www.lexico.com/en/definition/evolution
2. https://www.nature.com/scitable/topicpage/dna-sequencing-technologies-key-to-the-human-828/
3. https://www.nature.com/news/2006/061009/full/news061009-10.html
4. Darwin, Charles, 1809-1882. On The Origin of Species by Means of Natural Selection, or Preservation of Favored Races in the Struggle for Life. London :John Murray, 1859.
5. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4685169/
6. https://www.nature.com/articles/nature11247
7. https://www.discovermagazine.com/the-sciences/encode-the-rough-guide-to-the-human-genome
8. https://www.nature.com/articles/nature05874.pdf
9. Tomkins, Jeffrey, “Comprehensive Analysis of Chimpanzee and Human Chromosomes Reveals Average DNA Similarity of 70%” Answers Research Journal 6:1 (2013): p63.
10. https://www.researchgate.net/publication/292215627_Divergence_between_samples_of_chimpanzee_and_human_DNA_sequences_is_5_counting_indels
11. Dewitt, David, “What about the Similarity Between Human and Chimp DNA.” The New Answers Book 3, Master Books, Green Forest, (2016): p102.
12. ReMine, Walter, “Cost theory and the cost of substitution – a clarification” The In-depth Journal of Creation 19:1 (2005): p113-125.
13. https://76e3cb33-ff6d-43c4-be79-59e4727fae6c.filesusr.com/ugd/9d0974_b0a742f447ed479790e70515d9d94eb7.pdf
14. Dr. Sanford, John, Genetic Entropy. FMS Publications, (2014) p175-176.
15. https://www.genetics.org/content/180/3/1501
16. https://journals.plos.org/ploscompbiol/article?id=10.1371/journal.pcbi.0030091
17. Bergman, Jerry, “Research on the deterioration of the genome and Darwinism: why mutations result in degeneration of the genome” Intelligent design Conference, Biola University. (April 22-23, 2001).
18. https://journals.plos.org/plosgenetics/article?id=10.1371/journal.pgen.1000083
19. Dr. Sanford ref. 12, p64.
20. Dr. Sanford ref. 12, p38.
Round 2
Pro
Forfeited
Con
“Micro-Evolution”:
Key Question for Pro:What do you mean by evolution? If, by evolution, Pro simply means change in any direction, then we can agree that the genetic evidence for a perpetually degrading genome fulfills this definition of evolution, and is, as Pro put it, an “Observable Fact”; however, Darwinian evolution insists that organisms are becoming more complex (a concept which contradicts genetic science). Clearly the term evolution must be clearly defined before we can banter over whether micro-evolution is an “Observable Fact”.
Speciation: Creationists never disputed that organisms change; however, Darwinian evolution claims that all living creatures developed from a common single celled ancestor. The critical question we must ask when examining examples of bio-diversification is: Do these changes make the organism more complex as required for Darwinian evolution, or are they deleterious? Contrary to Pro’s attempts to paint this distinction as ambiguous, this distinction is black and white. Either mutations produce a net increase in information over time and Darwinian evolution is true or mutations produce a net decrease in information over time and Darwinian evolution is false.
• What Speciation Is and is Not:Pro falsely equates speciation to evolution. Speciation simply refers to which genetic traits are passed on or not passed on to the next generation. Dog breeders use speciation to narrow the gene pool in dog populations. Mutts generally possesses a much richer variety of genetic characteristics than their purebred counterparts and, therefore, can produce offspring with widely varied characteristics. Dog breeders use inbreeding and artificial selection to remove undesired genetic characteristics from a population. This produces breeds which can only produce certain characteristics (like floppy ears or stubby snouts for example) because these are the only genetic characteristics that breed possesses. If this had occurred in nature, it is likely we would consider Chihuahuas a different species from Great Danes (see picture here); however, these two ‘species’ clearly diversified through loss of genetic characteristics rather than the Darwinian claimed development of new information. This process is referred to as speciation; because, (through the process of removing different genetic characteristics in a given population) different populations of the same kind can express enough genetic separation to merit subcategorizing into species. Darwinian evolution requires that information be added over time; therefore, the scientifically proven process of speciation is the opposite of Darwinian evolution.
Key Question for Pro:Darwin contrived his theory around a faulty understanding of his observation of the speciation of finches; therefore, it would be most reasonable to say speciation was used to predict Darwinian evolution. How then, can Pro claim that Darwinian evolution was used to predict speciation?
Genetics:
Making an Ape Out of Man:
• Mitochondrial Eve:The theory that mankind originated from a mitochondrial Eve about 200,000 years ago originates from research done in 1988 [1] and was calculated using faulty mutation rates which have since been proven to be completely wrong. As evolutionist Ann Gibbons stated in 1998, “Mitochondiral DNA appears to mutate much faster than expected, prompting new DNA forensic procedures and raising troubling questions about the dating of evolutionary events…. Researchers have calculated that “mitochondrial Eve” … lived 100,000 to 200,000 years ago... Using the new clock, she would be a mere 6,000 years old” [2]. Alex Williams concurs with this conclusion saying, “We are unable to reproduce ourselves without making multiple genome copying errors every generation. As a result our genomes are decaying towards extinction from copy errors alone…. When decay in copy fidelity is projected backwards in time it reaches perfection around 4,000 BC, and when projected forwards, extinction from copy errors alone occurs in thousands, not millions, of years” [3]. Clearly mitochondrial DNA provided strong evidence against Darwinian evolution.
• Ape-Man Differences:I cited two high quality peer reviewed journals in my opening statement which both put the human-chimp DNA similarities at 70%, a far cry from Pro’s claimed 95-99%. Pro’s sources studied a mere 2% of the genome whereas the ENCODE project encompassed analysis of 100% of the human genome. This project included “more than 30 research groups and more than 400 scientists” [4]. Clearly the alleged 95-99% similarity is simply an exercise in lying with statistics.
• The Time Problem:I called Pro’s bluff on the supposed ability of chimp-human evolution to occur within 6 million years (or 8 million if Pro likes). As stated above, evolutionary time frames dictate that about 1,000 mutations must be fixed per generation to accomplish ape-man evolution. Realistically the mutation fixation rate is 1 mutation per 300 generations (this was verified by three independent studies cited above). At this rate, ape-man evolution would take nearly one-trillion years a far cry from Pro’s supposed 7-8 million years.
• ERV’s – Another Evolutionary Prediction Bites the Dust:Science is now catching up with the ill founded assumption that 8% of the genome is the result of endogenous retroviruses inserting sequences of DNA into the genetic code. Shaun Doyle accounts how, “The term ‘endogenous retrovirus’ is a bit of a misnomer. There are numerous instances where small transposable elements thought to be endogenous retroviruses have been found to have functions, which invalidates the ‘random retrovirus insertion’ claim…. Moreover, researchers have recently identified an important function for a large proportion of the human genome that has been labeled as ERVs. They act as promoters, starting transcription at alternative starting points, which enables different RNA transcripts to be formed from the same DNA sequence” [5]. Once again, Darwinian evolution manifests its inability to produce accurate predictions.
HIV – SIV:
• Virus Recombination:It is important to note that viruses have the ability to exchange genetic code. William Fleischmann explains that, “Recombination involves the exchange of genetic material between two related viruses during coinfection of a host cell.”[6]. Rather than creating information, this process simply allows a virus to borrow existing information from another organism.
• Evolution or Devolution?:Dr Carl Wieland examined the mutations leading to the rise of HIV and concluded that the net effect of these mutations lead to, “only a horizontal or even a negative change in informational content, and therefore does not relate to the sort of evolution postulated generally. It certainly does not involve any increase in functional complexity” [7].
Key Question for Pro:The evidence supports that HIV is simpler than the sum of its original genetic parts. Can you provide evidence that the mutations affecting HIV actually added complexity as required for Darwinian evolution to be tenable?
• Antibiotic Resistance at What Cost?:HIV expert Veronica Miller PhD experimented with the effect antibiotic resistance has on the fitness of HIV, “by ceasing all antiviral drug treatments to a patient. Without the drug, the few surviving original (‘wild’) types [of HIV] that had infected the patient could grow more easily. It turned out that they easily out-competed the vast numbers of resistant forms…. the wild types were also more dangerous—more efficient than the new strains.” [8]. The mutant antibiotic resistant strains of HIV are far inferior to the original wild strains demonstrating that these mutations are highly detrimental to the general health and fitness of the virus. Rather than supporting evolving to a higher state, these mutations represent genetic decay.
Key Question for Pro:Pleaseprovide your source backing the claim that antibiotic resistant diseases are “deadlier”? In 1346 the bubonic plague killed 60 percent of Europe’s population [9]. This has been unparalleled by any of Pro’s so called ‘deadlier’ diseases to date.
• A Very Poor Choice of Examples:Darwinism dictates that, our ultimate common ancestor, the very first single celled organism, be self-sufficient. Being the first and only living thing, this cell can’t rely on byproducts of any other organisms to assist in its survival. Alex Williams notes that, “First life… must be able to sustain itself indefinitely – and only the ‘high-tech’ autotrophs can do that!” [10]. Molecular geneticist Otto Yang defined viruses as simply, “packaged RNA or DNA”. Viruses are inert unless they come into contact with a living cell therefore they do not take self-generating or self-sustaining actions [11], and are generally not even considered to be alive. Under Darwinian presuppositions, viruses would be a highly degenerate relative of the first single celled life form. This brings us to a crucial question:
Key Question for Pro:Considering that, under Darwinian presuppositions, viruses are degenerate descendents of the first complex single cell, how are viruses supposed to demonstrate that organisms build complexity and become fish, mammals, and humans over time? Clearly the degenerate virus is one of the worst possible examples an evolutionist could possibly use to argue that organisms can develop complexity.
Fossil Record:
Pro is terribly wrong in claiming that, “The geological column perfectly fits within the evolutionary framework.” Indeed, I will only be able to scratch the surface in covering how incorrect this statement is:
• The Cambrian Explosion:Darwinian evolution holds that one type of life diversified over time giving rise to many life forms; however, the fossil record does not concur with Darwin in the slightest on this point. As Dr John Morris and Frank Sherwin account, “The Cambrian portion of the fossil record has preserved multitudes of invertebrate types that all appeared at the same time, each quite complex and quite different from the others. An honest look at when and where fossil types are found suggests that life began with a multitude of early life plans, not with a single plan that later branched out.” Dr Morris also notes that, “Cambrian trilobites abound, with eyes at least as proficient as those possessed by any animal living today.” [12]. Indeed, the fossil record preserves complex and unique organisms from the very beginning.
• Living Fossils:There are numerous examples of species considered to have gone extinct millions of years ago later found to still be alive today. Randy Guliuzza gives a classic example saying, “National Geographic recalls how ‘the primitive-looking coelacanth…was thought to have gone extinct with the dinosaurs 65 million years ago. But its discovery in 1938 by a South African museum curator on a local fishing trawler fascinated the world.’” [13]. Dr. Carl Werner filled an entire book with examples of living fossils and found that, “Examples of all the major groups of plants living today have been found in dinosaur layers, including flowering plants and trees (angiosperms), plants without fruits or flowers (conifers, cycads, and ginkgos); vascular spore-forming plants (ferns, horsetails, and club mosses), and simple moss (peat moss)” [14].
Archaeopteryx: Evolutionist Ernst Mayr explains how, “The earliest undisputed bird fossil is Archaeopteryx, found in the upper Jurassic (145 million years ago). There are two major proposals concerning the phylogeny of birds. According to the thecodont theory, birds originated from archosaurian reptiles more than 200 million years ago [i.e., birds evolved before Archaeopteryx]. According to the dinosaur theory, birds originated from theropod dinosaurs in the later Cretaceous (ca. 80-100 million years ago) [i.e., the origin of birds came long after Archaeopteryx]” [15]. Archaeopteryx is either insignificant, since birds had already fully evolved about 50 million years prior to archaeopteryx, or a massive problem, since archaeopteryx predates its earlier ancestors by about 50 million years. Evolutionists now consider Archaeopteryx to be a true bird [16]; therefore Pro’s claim that Archaeopteryx is a ‘missing link’ is a position no longer supported even by authorities on evolution.
150 Years of Science Overturns Evolution:Evolutionary geneticist Richard Lewontin said, “It is not that the methods and institutions of science somehow compel us to accept a material explanation of the phenomenal world [i.e., Darwinian evolution], but, on the contrary, that we are forced by our a priori adherence to material causes to create an apparatus of investigation and a set of concepts that produce material explanations, no matter how counter-intuitive, no matter how mystifying to the uninitiated” [17]. Evolutionary biologist Ernst Mayr said, “All of the atheists I know are highly religious; it just doesn’t mean believing in the Bible or God. Religion is the basic belief system of the person” [18]. Clearly Pro is falsely masquerading Darwinian evolution as science. These evolutionists understand what Pro seems to be missing; which is that, evolution is a 150 year old worldview that has never been proven by science.
Part 2: A series of irrelevant claims:The scientific viability of evolution is on trial here. I have no burden of proof to present or defend an alternative to evolution. The issues Pro brings up here do not scientifically vindicate Darwin’s theory.
1. https://i.b5z.net/i/u/736324/i/IN_SEARCH_FOR_ADAM___EVE.pdf
2. http://www.dnai.org/teacherguide/pdf/reference_romanovs.pdf
3. Williams, Alex, “Human genome decay and the origin of life”The In-depth Journal of Creation 28:1 (2014): p91.
4. https://ghr.nlm.nih.gov/primer/genomicresearch/encode
5. Doyle, Shaun, “Large scale function for ‘endogenous retroviruses’” The In-depth Journal of Creation 22:3 (2018) p 16.
6. https://www.ncbi.nlm.nih.gov/books/NBK8439/
7. Wieland, Carl. Has AIDS evolved? Creation 12:3 (1990) p29-32.
8. Safrati, Jonathan. Refuting Evolution 2. Creation Book Publishers, Powder Springs, Georgia, 2011 P38.
9. https://www.historytoday.com/archive/black-death-greatest-catastrophe-ever
10. Williams, Alex, “What life isn’t”The In-depth Journal of Creation 29:1 (2015): 112.
11. https://www.livescience.com/58018-are-viruses-alive.html
12. Morris, John, Frank Sherwin. The Fossil Record: Unearthing Nature’s History of Life. Institute for Creation Research, Dallas, Texas, 2010. P44
13. Guliuzza, Randy. Twenty Evolutionary Blunders: Danger and Difficulties of Darwinian Thinking. Institute for Creation Research, Dallas, Texas, 2017 P94.
14. Werner, Carl. Lifing Fossils: Evolution: The Grand Experiment Vol. 2. New Leaf Press, Green Forest, Arkansas, 2009. p230.
15. Mayr, Ernst. What Evolution Is. New York, Basic Books, (2001). p 65.
16. P.J. Currie et al., eds., Feathered Dragons: Studies on the Transition from Dinosaurs to Birds, Indian University Press, Bloomington, Indiana 2004.
17. Richard Lewontin, Billions and billions of demons (review of The Demon-Haunted World: Science as a Candle in the Dark by Carl Sagan, 1997), The New York Review, p. 31, 9 January 1997.
18. https://www.the-scientist.com/feature/ernst-mayr-darwins-disciple-50738
Round 3
Pro
Forfeited
Con
Since, regrettably Virtuoso was unable to complete his post last round, I will use the open mike to address a couple of issues Pro brought up of indirect relevance.
A Brash Claim: Dobzansky very foolishly made the absolute claim that “Nothing in biology makes sense, except in the light of evolution.” I think it is fair to say that I have already proven Dobzansky to be spectacularly wrong, but, for good measure, here is another compelling example of how false Dobzansky’s claim is:
• Soft Tissue: In 2005 Mary Schweitzer discovered soft tissue in a T-Rex bone traditionally dated to be 65 million years old. Mary Schweitzer et al said, “Soft tissues are preserved within hindlimb elements of Tyrannosaurus rex” [1]. Observable science demonstrates that soft tissue lasts perhaps thousands of years not millions. Kevin Anderson PhD explained that, “Matthew Collins, directs a lab that specializes in analysis of archaeological samples. His lab experimentally determined how quickly proteins, such as collagen, will degrade even under ideal conditions. From this data, the letter concludes that the warmer climate of the Hell Creek Formation (where the T. rex was found) would accelerate collagen degradation, resulting in only 1% remaining after less than 15,000 years” [2]. According to Mary Schweitzer, “The present state of knowledge holds that microbial attack, enzymatic degradation, cellular necrosis and other processes contribute to total degradation of recognizable materials in days to years” [3]. Clearly the biology here does not make sense in light of the claims of Darwinian evolution.
There are many things in biology that do not make sense in light of evolution. The implications evolution has on the actual practice of science are small to nil. Evolutionist Conrad Johnson PhD noted that research scientists, “rarely deal directly with macroevolutionary theory, be it biological or physical. For example, in my 25 years of neuroscience teaching and research I have only VERY rarely had to deal with natural selection, origins, macroevolution, etc. My professional work in science stems from rigorous training in biology, chemistry, physics, and math, not from world views about evolution. I suspect that such is the case for most scientists in academia, industry, and elsewhere” [4]. Evolution is also widely questioned by scientists. For example, over five hundred scientists signed a statement saying, “We are skeptical of claims for the ability of random mutation and natural selection to account for the complexity of life. Careful examination of the evidence for Darwinian theory should be encouraged” [5]. Contrary to Pro’s claims, the scientific tenability of Darwinism is widely questioned by scientists.
Order of Creation: We are debating the scientific tenability of Darwinian evolution. Establishing an alternative is outside of the scope of this debate. Clearly Pro’s claims here are straying far outside of the scope of this debate.
Star Formation and the Age of the Universe: The resolution is, “The Theory of Evolution is a sound theory of how life developed on Earth.” This debate is clearly not about the universe; therefore, only that which pertains to planet earth can possibly have relevance to this debate.
Pro’s Oversold Confidence in Radiometric Dating and the Age of the Earth:An old earth does not establish Darwinian evolution as scientifically feasible. However, since a young earth would render Darwinian evolution impossible let’s explore radiometric dating:
1) Carbon Dating: It is quite interesting that Pro should bring up the topic of carbon dating the Quran since Radiocarbon dating supports a young age for the earth. Radiocarbon has a relatively short half life, and all specimens dating older than 100,000 years should not contain any detectable amounts of radiocarbon [6]. And yet, we actually find radiocarbon in abundance in numerous places. Here are a couple examples:
• Coal: Coal is traditionally dated to be around 360 to 250 million years old. John R. Baumgardner, PhD tested ten different coal samples collected from a variety of coal fields and found significant amounts of carbon 14 in all ten samples [7].
• Wood:Andrew Snelling PhD found significant amounts of radiocarbon in wood dated to be 47.5 million years old [8].
• Diamonds: Natural diamonds are believed by evolutionists to be billions of years old. John Baumgardner, PhD, part of the RATE research group, tested six diamond samples from South Africa, Botswana, and Guinea and found significant amounts of carbon 14 present in all six diamonds [9]. These are just a few examples.
• Dinosaurs: Hugh Miller et al. tested 24 samples from 10 dinosaurs and found significant amounts of carbon 14 in all 24 samples [10]. All 24 samples dated less than 40,000 years old.
2) Potassium-Argon (K-Ar) Dating:K-Ar dating is considered to be among the most reliable dating methods available. Andrew Snelling PhD gives several examples of how ‘accurate’ K-Ar dating has proven to be [11]:
• Mt. Etna Basalt, Sicily:two rock formations were tested here. The first formation is known to have formed around 122 B.C. but yielded an age of 170,000-330,000 years. The second was formed in 1972 but was dated at 210,000-490,000 years. Not only were the results astronomically erroneous, but the younger rock dated the oldest. Therefore, K-Ar dating even failed to date these two deposits in the correct relative order.
• Mt. St. Helens, Washington:Rock formations formed in 1986 yielded a date of 2.8 million years.
• Hualalai basalt, Hawaii:Rock formations from 1800-1801 were tested at 1.32-1.76 million years.
• Mt. Ngauruhoe, New Zealand:Rocks formed in 1954 tested at up to 3.5 million years.
• Kilauea Iki basalt, Hawaii:Formations formed in 1959 tested at 1.7-15.3 million years.
These five independent examples clearly demonstrate that Potassium-argon dating fails to provide reliable results in rocks where the age is known. It is insanity to religiously trust dating methods that fail to accurately date rocks of known age.
3) Radiometric Dating Crosscheck:The RATE project rated a number of samples using potassium-argon (K-Ar), rubidium-strontium (Rb-Sr), samarium-neodymium (Sm-Nd), and lead-lead (Pb-Pb) dating methods from two independent sites. All four of these methods are considered highly reliable; therefore, all four methods should yield the same age. Samples from the first site ranged from 1.5 million years for K-Ar to 2.9 million years for Sm-Nd. Samples from the second site ranged from 665 million years for K-Ar to 1.4 million years for Pb-Pb [12]. The most so called ‘reliable’ radiometric dating methods don’t even agree with each other. In each case, the oldest dating method results were approximately twice the age of the youngest.
4) Helium Leakage Rates: Radiometric dating methods assume that historic radiometric decay rates have always been the same; however, this claim is unsubstantiated and even scientifically falsified. The radiometric decay of uranium and thorium produces lots of helium. Helium is a noble gas (meaning it does not combine with other atoms); therefore, helium is left to diffuse out of the rock. The Precambrian layer contains zirconium silicate crystals which contain both uranium and large amounts of helium [13]. As Dr Andrew Snelling et al succinctly stated, “The helium leakage rate has been determined in several experiments [14, 15, 16]. All measurements are in agreement. Helium diffuses so rapidly that all the helium in these zircon crystals should have leaked out in less than 100,000 years. The fact that so much helium is still there means they cannot be 1.5 billion year old, as uranium-lead dating suggests” [17]. The only logical conclusion is that radiometric decay rates were much faster sometime in the not-so-far past.
Radiometric Dating Concluded:Pro claimed that “we can test the accuracy of radiometric dating by cross-dating it with various isotopes.” Clearly, radiometric dating fails Pro’s litmus test. Evolutionary scientist William D. Stanfield PhD recognized that, “It is obvious that radiometric techniques may not be the absolute dating methods they are claimed to be. Age estimates on a given geological stratum by different radiometric methods are often quite different (sometimes by hundreds of millions of years)…. The uncertainties inherent in radiometric dating are disturbing to geologists and evolutionists” [18].
Lifespan of Humans: Once again, Pro’s claim here has no relevance to the debate.
Conclusion: If the earth is young then Darwinian evolution simply could not have happened, but, an old earth does not solve Pro’s problems. Pro claims that the earth is 4.6 billion years old and yet according to Haldane’s dilemma, it would take nearly 1 trillion years [19] just for ape and human evolution, and this assumes a steady supply of beneficial mutations, which as I have demonstrated is not even a remotely realistic assumption. That means Pro’s 4.6 billion year old date is far too short to give Darwinian evolution a chance. After considering that genetics overwhelmingly supports that the genome is in a perpetual state of decay, the earth could be infinitely old and Darwinian evolution would not have a chance.
1. https://science.sciencemag.org/content/307/5717/1952
2. Anderson, Kevin. Echoes of the Jurassic: Discoveries of Dinosaur Soft-Tissue. CRS Books, (2017) p8. https://www.bx.psu.edu/miller_lab/dist/buckley.pdf
3. https://www.researchgate.net/publication/6651395_Soft_tissue_and_cellular_preservation_in_vetebrate_skeletal_elements_from_the_Cretaceous_to_the_present
4. https://www.trueorigin.org/biologymyth.php
5. https://evolutionnews.org/2006/02/over_500_scientists_proclaim_t/
6. Bergman, John. Carbon-14 Evidence for a Recent Global Flood and a Young Earth. Institute for Creation Research and the Creation Research Society, 2005 p587-630
7. Bergman, John. Carbon-14 Evidence for a Recent Global Flood and a Young Earth. Institute for Creation Research and the Creation Research Society, 2005 p587-630
8. Snelling Andrew, “Conflicting ‘ages’ of Territorial basalt and contained fossilized wood, crinum, Central Queensland, Australia” The In-depth Journal of Creation 14:2 (2000): p99-122.
9. Baumgardner, J., 14C evidence for a recent global flood and a young earth; in ref. 6, ch. 8. 5th International Conference on Creationism, 2003.
10. https://researchopenworld.com/the-search-for-solutions-to-mysterious-anomalies-in-the-geologic-column/
11. Andrew Snelling, “Excess Argon: The ‘Achilles’ Heel’ of Potassium-Argon and Argon Argon Dating of Volcanic Rocks,” Impact, 1999.
12. S.A. Austin, Do radioisotope clocks need repair? Testing the assumptions of isochron dating using K-Ar, Rb-Sr, Sm-Nd, and Pb-Pb isotopes, in Vardiman et al., Radioisotopes and the Age of the Earth, P 325–392, 2005.
13. R.V. Gentry, G.L Glish, and E.H. McBay, “Differential Helium Retention in Zirons: Implications for Nuclear Waste Containment,” Geophysical Research Letter 9, no. 10 (1982: p. 1129-1130.
14. S.W. Reiners, K.A. Farley, and H.J. Hicks, “He Diffusion and (U-Th)/He Thermochronometry of Zircon: Initial Results from Fish Canyon Tuff and Gold Butte, Nevada,” Tectonophysics 349, no. 1-4 (2002): p. 297-308;
15. D. Russell Humphreys et al., “Helium Diffusion Rates Support Accelerated Nuclear Decay,” in proceeding of the Fifth International Conference on Creationism, R.L. Ivey Jr., ed. (Pittsburg, PA: Creation Science Fellowship, 2003), p. 175-196;
16. D. Russell Humphreys, “Young Helium Diffusion Age of Zircons Supports Accelerated Nuclear Decay,” in Radioisotopes and the Age of the Earth Creationist Research Initiative, L. Vardiman, A.A. Snelling, and E.F. Chaffin, eds. (El Cajon, CA: Institute for Creation Research, and Chino Valley, AZ: Creation Research Society, 2005), p. 25-100.
17. Snelling, Andrew et al. “What Are Some of the Best Evidences in Science for a Young Creation” The New Answers Book 4 (2015): p. 123.
18. William D. Stanfield, PhD., The Science of Evolution, Macmillan, New York, P 82-84, 1977.
19. calculation based on 6,000 years (the number of years it takes for 1 mutation to fix in a population - see source 11 and 15) multiplied by 153.5 million (the number of base pair differences between apes and humans divided by two (since both theoretical species can evolve simultaneously) - see source 2 and 11 in my opening argument
Round 4
Pro
I’d like to make a public apology to my opponent for my forfeitures. Things haven’t been going well for me recently and could not finish this debate. Please vote con.
Con
I hope things start going better for you Virtuoso. I believe that wraps this one up.
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Publication Details
Reference Category Journals
DOI / URL link
Title (Primary) Iron oxides stimulate microbial monochlorobenzene in situ transformation in constructed wetlands and laboratory systems
Author Schmidt, M.; Wolfram, D.; Birkigt, J.; Ahlheim, J.; Paschke, H.; Richnow, H.-H.; Nijenhuis, I.
Journal Science of the Total Environment
Year 2014
Department ISOBIO; WANA; ANA
Volume 472
Page From 185
Page To 193
Language englisch
Keywords Constructed wetland; Chlorobenzene; In-situ biodegradation; Transition/gradient zones; Iron and nitrate
UFZ wide themes RU3;
Abstract Natural wetlands are transition zones between anoxic ground and oxic surface water which may enhance the (bio)transformation potential for recalcitrant chloro-organic contaminants due to the unique geochemical conditions and gradients. Monochlorobenzene (MCB) is a frequently detected groundwater contaminant which is toxic and was thought to be persistent under anoxic conditions. Furthermore, to date, no degradation pathways for anoxic MCB removal have been proven in the field. Hence, it is important to investigate MCB biodegradation in the environment, as groundwater is an important drinking water source in many European countries. Therefore, two pilot-scale horizontal subsurface-flow constructed wetlands, planted and unplanted, were used to investigate the processes in situ contributing to the biotransformation of MCB in these gradient systems. The wetlands were fed with anoxic MCB-contaminated groundwater from a nearby aquifer in Bitterfeld, Germany. An overall MCB removal was observed in both wetlands, whereas just 10% of the original MCB inflow concentration was detected in the ponds. In particular in the gravel bed of the planted wetland, MCB removal was highest in summer season with 73 ± 9% compared to the unplanted one with 40 ± 5%. Whereas the MCB concentrations rapidly decreased in the transition zone of unplanted gravel to the pond, a significant MCB removal was already determined in the anoxic gravel bed of the planted system. The investigation of hydro-geochemical parameters revealed that iron and sulphate reduction were relevant redox processes in both wetlands. In parallel, the addition of ferric iron or nitrate stimulated the mineralisation of MCB in laboratory microcosms with anoxic groundwater from the same source, indicating that the potential for anaerobic microbial degradation of MCB is present at the field site.
Persistent UFZ Identifier https://www.ufz.de/index.php?en=20939&ufzPublicationIdentifier=14714
Schmidt, M., Wolfram, D., Birkigt, J., Ahlheim, J., Paschke, H., Richnow, H.-H., Nijenhuis, I. (2014):
Iron oxides stimulate microbial monochlorobenzene in situ transformation in constructed wetlands and laboratory systems
Sci. Total Environ. 472 , 185 - 193
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Back to blog
Discover the wonders of nature with World Wildlife Fund on Kahoot! Academy
Explore the importance of biodiversity and deepen science knowledge with this new collection of engaging kahoots from World Wildlife Fund’s Wild Classroom.
August 12, 2021
A lifelong love of nature begins with being curious about the world around us. Luckily, both learners and educators—including the 8 million educators and hundreds of millions of participating students on Kahoot! in the last year—are experts at staying curious, asking the big questions and stepping up to make a positive difference.
As part of our goal at Kahoot! to empower learners of all ages, we are committed to helping students develop the knowledge and skills they need to make the world a better place. This is why we are thrilled to be teaming up with World Wildlife Fund’s Wild Classroom to launch a brand-new collection of learning games on Kahoot! Academy.
Play the first kahoot in the collection here:
World Wildlife Fund’s Wild Classroom connects educators and families with free, curriculum-aligned educational resources to guide their exploration of the natural world and our place within it. Through lessons, activities, videos and other materials, Wild Classroom inspires learners of all ages to deepen their understanding and appreciation for wildlife and wild spaces. Students can also access tools to help them take action and advocate for conservation in their own communities, while practicing collaboration, responsibility and problem solving.
In WWF’s new collection of kahoots, students will explore biodiversity in ecosystems around the world, as well as investigate why it’s important, where it’s at risk and how we can protect it. Educators and parents can spark engagement with fascinating animal facts, while students learn about simple actions we can take to safeguard biodiversity and a healthy environment.
See the full collection from WWF on Kahoot! Academy here
At Kahoot!, we believe that fostering a deeper understanding of the natural world is fundamental for learners of all ages. World Wildlife Fund has been a leading voice for conservation for many years, so we’re excited to be joining forces to make learning about our environment even more engaging for learners.
“We are thrilled to join Kahoot! Academy and connect with educators and students wanting to learn about our planet’s wildlife and wild places,” said Katy Fenn, Director, Wild Classroom at World Wildlife Fund. “It’s very important for us to find ways to teach children about our environment and develop a foundation of empathy and a connection with nature. Kahoot! Academy gives us the opportunity to create content that is fun and entertaining while keeping kids thinking and asking questions.”
The kahoots in this collection are now available to play for free on Kahoot! Academy, a knowledge platform and online community, which allows educators and publishers to share and access content that supports engaging and meaningful learning experiences for learners of all ages, worldwide.
Go wild and play these kahoots with your kids or students today on the World Wildlife Fund Kahoot! Academy Premium partner page.
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eTheses Repository
Browse by Author/Supervisor
Up a level
Export as [feed] RSS 2.0 [feed] RSS 1.0 [feed] Atom
Number of items: 14.
Barnett, Rosemary Elizabeth (2012) A study assessing the comparative molecular toxicities of heavy metals to multiple strains of Daphnia magna. M.Res. thesis, University of Birmingham.
Duffy, Kate I. (2015) Application of metabolomics to the analysis of ancient organic residues. Ph.D. thesis, University of Birmingham.
White, Thomas Andrew (2014) Assessing toxicity in Daphnia magna: an oxidative lipidomic approach. Ph.D. thesis, University of Birmingham.
Hrydziuszko, Olga (2013) Development of data processing methods for high resolution mass spectrometry-based metabolomics with an application to human liver transplantation. Ph.D. thesis, University of Birmingham.
Weber, Ralf Johannes Maria (2011) Increased confidence of metabolite identification in high-resolution mass spectra using prior biological and chemical knowledge-based approaches. Ph.D. thesis, University of Birmingham.
Gavin, Alexander James Steel (2016) Investigating the mechanisms of silver nanoparticle toxicity in Daphnia magna: a multi-omics approach. Ph.D. thesis, University of Birmingham.
Senanayake, Eshan Lankapura (2015) Left ventricular hypertrophy and myocardial protection with perhexiline during cardiac surgery. M.D. thesis, University of Birmingham.
Taylor, Nadine Suzanne (2010) Novel approaches to toxicity testing in Daphnia magna. Ph.D. thesis, University of Birmingham.
Drury, Nigel Edward (2012) On perhexiline and its application to myocardial protection during cardiac surgery. Ph.D. thesis, University of Birmingham.
Easton, John M. (2009) Optimised analysis and visualisation of metabolic data using graph theoretical approaches. Ph.D. thesis, University of Birmingham.
Parsons, Helen Michelle (2010) Optimised spectral processing and lineshape analysis in 2-dimensional J-resolved NMR spectroscopy based metabolomics. Ph.D. thesis, University of Birmingham.
Payne, Tristan Graeme (2011) Profiling the metabolome using Fourier transform ion cyclotron resonance mass spectrometry, optimised signal processing, noise filtering and constraints methods. Ph.D. thesis, University of Birmingham.
Romer Roche, Isabella (2013) The ecotoxicological and environmental behaviour and transformations of silver nanoparticles. Ph.D. thesis, University of Birmingham.
Zhang, Jinkang (2015) Transcriptomic and metabolomic approaches to investigate molecular responses of human cell lines exposed to flame retardants. Ph.D. thesis, University of Birmingham.
This list was generated on Sat Jul 30 07:10:52 2016 IST.
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"rps_doc_lorem_ipsum": 0,
"rps_doc_stop_word_fraction": 0.13320079445838928,
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"rps_doc_frac_all_caps_words": 0.04572565108537674,
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"rps_doc_frac_no_alph_words": 0.32405567169189453,
"rps_doc_frac_unique_words": 0.5617647171020508,
"rps_doc_mean_word_length": 6.326470375061035,
"rps_doc_num_sentences": 62,
"rps_doc_symbol_to_word_ratio": 0,
"rps_doc_unigram_entropy": 4.787739276885986,
"rps_doc_word_count": 340,
"rps_doc_frac_chars_dupe_10grams": 0,
"rps_doc_frac_chars_dupe_5grams": 0.18967922031879425,
"rps_doc_frac_chars_dupe_6grams": 0.07438401132822037,
"rps_doc_frac_chars_dupe_7grams": 0,
"rps_doc_frac_chars_dupe_8grams": 0,
"rps_doc_frac_chars_dupe_9grams": 0,
"rps_doc_frac_chars_top_2gram": 0.1041376069188118,
"rps_doc_frac_chars_top_3gram": 0.1171548068523407,
"rps_doc_frac_chars_top_4gram": 0.1822408139705658,
"rps_doc_books_importance": -127.62769317626953,
"rps_doc_books_importance_length_correction": -127.62769317626953,
"rps_doc_openwebtext_importance": -97.68437194824219,
"rps_doc_openwebtext_importance_length_correction": -97.68437194824219,
"rps_doc_wikipedia_importance": -117.97618865966797,
"rps_doc_wikipedia_importance_length_correction": -117.97618865966797
},
"fasttext": {
"dclm": 0.0026775600854307413,
"english": 0.8069849014282227,
"fineweb_edu_approx": 1.9920732975006104,
"eai_general_math": 0.2501966953277588,
"eai_open_web_math": 0.48382025957107544,
"eai_web_code": 0.0017555999802425504
}
}
|
{
"free_decimal_correspondence": {
"primary": {
"code": "577.1",
"labels": {
"level_1": "Science and Natural history",
"level_2": "Biology and Anthropology",
"level_3": "Life (Biology)"
}
},
"secondary": {
"code": "572.8",
"labels": {
"level_1": "Science and Natural history",
"level_2": "Biology and Anthropology",
"level_3": "Anthropology"
}
}
},
"bloom_cognitive_process": {
"primary": {
"code": "2",
"label": "Understand"
},
"secondary": {
"code": "3",
"label": "Apply"
}
},
"bloom_knowledge_domain": {
"primary": {
"code": "2",
"label": "Conceptual"
},
"secondary": {
"code": "3",
"label": "Procedural"
}
},
"document_type_v1": {
"primary": {
"code": "2",
"label": "Academic/Research"
},
"secondary": {
"code": "7",
"label": "Search/Directory/Bibliography"
}
},
"extraction_artifacts": {
"primary": {
"code": "0",
"label": "No Artifacts"
},
"secondary": {
"code": "-1",
"label": "Abstain"
}
},
"missing_content": {
"primary": {
"code": "0",
"label": "No missing content"
},
"secondary": {
"code": "-1",
"label": "Abstain"
}
},
"document_type_v2": {
"primary": {
"code": "6",
"label": "Content Listing"
},
"secondary": {
"code": "3",
"label": "Academic Writing"
}
},
"reasoning_depth": {
"primary": {
"code": "1",
"label": "No Reasoning"
},
"secondary": {
"code": "2",
"label": "Basic Reasoning"
}
},
"technical_correctness": {
"primary": {
"code": "6",
"label": "Not Applicable/Indeterminate"
},
"secondary": {
"code": "4",
"label": "Highly Correct"
}
},
"education_level": {
"primary": {
"code": "4",
"label": "Graduate/Expert Level"
},
"secondary": {
"code": "5",
"label": "Indeterminate"
}
}
}
|
57
|
cf5cd1df0ee2161e1684bdc019357275
|
394,109,987,430,253,200
|
TBDB
WORLD Sign In Sign Out
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Samples and Conditions with significant expression of RV0781 /ptrBa : protease II
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P-Value for Experimental Condition: <=1e-10 1e-10 to 1e-8 1e-8 to 1e-6 1e-6 to 1e-4 1e-4 to 1e-2 >0.01
raw pcl GP cluster Download Table
Sample Name Experimental
Condition
Expression Value Intensity Significance Publication
H37Rv 0.05% SDS exposure for 1h rep 1SDS0.0812.940.15Manganelli R, et al. (2001)
H37Rv 0.05% SDS exposure for 1h rep 4SDS-0.3112.480.45Manganelli R, et al. (2001)
H37Rv 0.05% SDS exposure for 1h rep 2SDS0.1512.110.03Manganelli R, et al. (2001)
H37Rv 0.05% SDS exposure for 1h rep 5SDS0.2812.100.38Manganelli R, et al. (2001)
H37Rv 0.05% SDS exposure for 1h rep 3SDS0.3812.280.51Manganelli R, et al. (2001)
H37Rv 0.05% SDS exposure for 1h rep 6SDS0.3413.040.09Manganelli R, et al. (2001)
H37Rv sigE null 0.05% SDS exposure for 1h rep 5SDS0.4113.340.06Manganelli R, et al. (2001)
H37Rv sigE null 0.05% SDS exposure for 1h rep 4SDS0.4113.180.10Manganelli R, et al. (2001)
H37Rv sigE null 0.05% SDS exposure for 1h rep 1SDS0.7612.850.32Manganelli R, et al. (2001)
H37Rv sigE null 0.05% SDS exposure for 1h rep 2SDS0.9712.210.56Manganelli R, et al. (2001)
H37Rv sigE null 0.05% SDS exposure for 1h rep 6SDS0.7513.550.36Manganelli R, et al. (2001)
H37Rv sigE null 0.05% SDS exposure for 1h rep 3SDS1.1713.280.72Manganelli R, et al. (2001)
H37Rv diamide 1h rep 1Diamide-0.6913.121.16Manganelli R, et al. (2002)
H37Rv diamide 1h rep 2Diamide-0.8912.271.61Manganelli R, et al. (2002)
H37Rv diamide 1h rep 3Diamide-0.4912.390.86Manganelli R, et al. (2002)
H37Rv diamide 1h rep 4Diamide-0.1210.900.23Manganelli R, et al. (2002)
H37Rv diamide 1h rep 5Diamide-0.1313.200.40Manganelli R, et al. (2002)
H37Rv diamide 1h rep 6Diamide-0.0112.030.09Manganelli R, et al. (2002)
H37Rv sigma H null mutant diamide 1h rep 1Diamide-0.3413.230.78Manganelli R, et al. (2002)
H37Rv sigma H null mutant diamide 1h rep 2Diamide-0.4913.521.11Manganelli R, et al. (2002)
H37Rv sigma H null mutant diamide 1h rep 3Diamide-0.3212.680.62Manganelli R, et al. (2002)
H37Rv sigma H null mutant diamide 1h rep 4Diamide-0.5511.630.93Manganelli R, et al. (2002)
H37Rv sigma H null mutant diamide 1h rep 5Diamide-0.4312.880.66Manganelli R, et al. (2002)
H37Rv sigma H null mutant diamide 1h rep 6Diamide-0.1812.710.35Manganelli R, et al. (2002)
H37Rv wild type Vs H37Rv sigE null mutant rep 1Wild type vs Mutant-0.0812.050.14Manganelli R, et al. (2001)
H37Rv wild type Vs H37Rv sigE null mutant rep 2Wild type vs Mutant-0.1012.770.01Manganelli R, et al. (2001)
H37Rv vs H37 sigma H null mutant rep 1Wild type vs Mutant-0.9312.820.94Manganelli R, et al. (2002)
H37Rv vs H37 sigma H null mutant rep 2Wild type vs Mutant0.6112.771.14Manganelli R, et al. (2002)
H37Rv wild type Vs H37Rv sigE null mutant rep 3Wild type vs Mutant0.4013.500.86Manganelli R, et al. (2001)
H37Rv vs H37 sigma H null mutant rep 3Wild type vs Mutant-0.9613.071.35Manganelli R, et al. (2002)
H37Ra, 7H9 roll-replicate 1Strain comparison-0.089.330.32Gao Q, et al. (2005)
H37Ra, 7H9 roll-replicate 2Strain comparison-0.3310.060.59Gao Q, et al. (2005)
Strain H37Ra, replicate 4Strain comparison-0.2412.190.49Gao Q, et al. (2005)
H37Rv, 7H9 roll-replicate 1Strain comparison-0.329.990.30Gao Q, et al. (2005)
H37Rv, 7H9 roll-replicate 2Strain comparison-0.079.880.22Gao Q, et al. (2005)
H37Rv, 7H9 roll-replicate 3Strain comparison-0.4510.000.54Gao Q, et al. (2005)
H37Rv, 7H9 roll-replicate 4Strain comparison-0.119.620.09Gao Q, et al. (2005)
aceatate induction-1Acetate-1.389.271.67Yang Liu, et al. (Unpublished Results)
aceatate induction-2Acetate-0.029.240.15Yang Liu, et al. (Unpublished Results)
aceatate induction-3Acetate-0.749.621.33Yang Liu, et al. (Unpublished Results)
H37Ra, 7H9 roll-replicate 47H9 medium rolling-0.499.600.51Gao Q, et al. (2004)
H37Ra, 7H9 roll-replicate 3Strain comparison-0.099.870.12Gao Q, et al. (2005)
Strain 1254, replicate 4Strain comparison-0.5011.340.48Gao Q, et al. (2005)
Strain 1254, replicate 2Strain comparison0.0611.220.12Gao Q, et al. (2005)
Strain 1254, replicate 3Strain comparison0.1211.040.05Gao Q, et al. (2005)
Strain 1254, replicate 1Strain comparison-0.469.440.61Gao Q, et al. (2005)
Strain 9802501, replicate1Strain comparison-0.6210.260.56Gao Q, et al. (2005)
Strain 9802501, replicate 2Strain comparison-0.4410.650.47Gao Q, et al. (2005)
Strain 9802501, replicate 3Strain comparison-0.1410.630.00Gao Q, et al. (2005)
Strain 9802501, replicate 4Strain comparison-0.1711.500.22Gao Q, et al. (2005)
Strain 9802826, replicate 3Strain comparison-0.119.730.47Gao Q, et al. (2005)
Strain 9802826, replicate 4Strain comparison2.2510.050.62Gao Q, et al. (2005)
Strain 3160, replicate 1Strain comparison0.2410.180.23Gao Q, et al. (2005)
Strain 3160, replicate 2Strain comparison-0.3210.790.39Gao Q, et al. (2005)
Strain 3160, replicate 3Strain comparison0.3311.100.08Gao Q, et al. (2005)
Strain 3160, replicate 4Strain comparison0.3610.530.17Gao Q, et al. (2005)
Strain 1843, replicate 2Strain comparison-0.349.260.51Gao Q, et al. (2005)
Strain 1843, replicate 3Strain comparison-0.149.160.24Gao Q, et al. (2005)
Strain 1843, replicate 4Strain comparison-0.179.020.21Gao Q, et al. (2005)
Strain 1006, replicate 1Strain comparison-0.369.920.26Gao Q, et al. (2005)
Strain 1006, replicate 2Strain comparison-0.5310.300.48Gao Q, et al. (2005)
Strain 1006, replicate 3Strain comparison-0.908.970.67Gao Q, et al. (2005)
Strain 1006, replicate 4Strain comparison-0.259.480.29Gao Q, et al. (2005)
Strain 9700665, replicate 1Strain comparison-0.239.320.09Gao Q, et al. (2005)
Strain 9700665, replicate 2Strain comparison-0.249.490.38Gao Q, et al. (2005)
Strain 9700665, replicate 3Strain comparison-0.479.240.41Gao Q, et al. (2005)
Strain CDC1551, replicate 1Strain comparison-0.1512.170.24Gao Q, et al. (2005)
Strain CDC1551, replicate 2Strain comparison-0.0511.980.29Gao Q, et al. (2005)
Strain CDC1551, replicate 3Strain comparison0.0811.420.04Gao Q, et al. (2005)
Strain CDC1551, replicate 4Strain comparison-0.0411.830.14Gao Q, et al. (2005)
Strain M3061a, replicate 1Strain comparison-0.5911.040.77Gao Q, et al. (2005)
Strain M3061a, replicate 2Strain comparison-0.2110.080.18Gao Q, et al. (2005)
Strain M3061a, replicate 3Strain comparison-0.3310.460.40Gao Q, et al. (2005)
Strain M3061a, replicate 4Strain comparison-0.4710.750.39Gao Q, et al. (2005)
Strain 9800608, replicate 1Strain comparison-0.0110.320.31Gao Q, et al. (2005)
Strain 9800608, replicate 2Strain comparison0.139.780.23Gao Q, et al. (2005)
Strain 9800608, replicate 3Strain comparison-0.2610.640.32Gao Q, et al. (2005)
Strain 9800608, replicate 4Strain comparison0.0111.520.35Gao Q, et al. (2005)
Strain 9700665, replicate 4Strain comparison0.1311.680.23Gao Q, et al. (2005)
Strain 1843, replicate 1Strain comparison0.2311.000.24Gao Q, et al. (2005)
Strain 9802826, replicate 1Strain comparison0.1210.810.29Gao Q, et al. (2005)
Strain 9802826, replicate 2Strain comparison0.7711.370.40Gao Q, et al. (2005)
H37Rv, 7H9 shake-replicate 17H9 medium shaking0.1710.190.25Gao Q, et al. (2004)
H37Rv, 7H9 shake-replicate 27H9 medium shaking0.2010.420.32Gao Q, et al. (2004)
H37Rv, 7H9 shake-replicate 37H9 medium shaking0.2110.510.29Gao Q, et al. (2004)
H37Rv, 7H9 shake-replicate 47H9 medium shaking-0.029.580.35Gao Q, et al. (2004)
H37Ra, 7H9 shake-replicate 17H9 medium shaking-0.019.400.18Gao Q, et al. (2004)
H37Ra, 7H9 shake-replicate 27H9 medium shaking-0.829.710.60Gao Q, et al. (2004)
H37Ra, 7H9 shake-replicate 37H9 medium shaking0.089.040.04Gao Q, et al. (2004)
H37Ra, 7H9 shake-replicate 47H9 medium shaking-0.359.710.37Gao Q, et al. (2004)
H37Rv, Sauton's media-replicate 1Sauton's medium0.2611.260.20Gao Q, et al. (2004)
H37Rv, Sauton's media-replicate 2Sauton's medium0.4410.940.05Gao Q, et al. (2004)
H37Rv, Sauton's media-replicate 3Sauton's medium0.3611.490.23Gao Q, et al. (2004)
H37Rv, Sauton's media-replicate 4Sauton's medium0.4510.470.13Gao Q, et al. (2004)
H37Ra, Sauton's media-replicate 1Sauton's medium-0.4410.670.52Gao Q, et al. (2004)
H37Ra, Sauton's media-replicate 2Sauton's medium-0.3410.190.27Gao Q, et al. (2004)
H37Ra, Sauton's media-replicate 3Sauton's medium-0.6810.410.63Gao Q, et al. (2004)
H37Ra, Sauton's media-replicate 4Sauton's medium-0.7310.650.71Gao Q, et al. (2004)
H37Rv, Youman media-replicate 1Youman's medium-0.029.730.20Gao Q, et al. (2004)
H37Rv, Youman media-replicate 2Youman's medium0.079.820.16Gao Q, et al. (2004)
H37Rv, Youman media-replicate 3Youman's medium0.4010.920.21Gao Q, et al. (2004)
H37Rv, Youman media-replicate 4Youman's medium0.3810.250.09Gao Q, et al. (2004)
H37Ra, Youman media-replicate 1Youman's medium-0.129.440.12Gao Q, et al. (2004)
H37Ra, Youman media-replicate 2Youman's medium-0.0110.640.41Gao Q, et al. (2004)
H37Ra, Youman media-replicate 3Youman's medium-0.029.570.28Gao Q, et al. (2004)
H37Ra, Youman media-replicate 4Youman's medium-0.259.310.30Gao Q, et al. (2004)
H37Rv, Dubos media-replicate 1Dubos medium0.689.580.26Gao Q, et al. (2004)
H37Rv, Dubos media-replicate 2Dubos medium0.2710.340.12Gao Q, et al. (2004)
H37Rv, Dubos media-replicate 3Dubos medium0.2510.930.24Gao Q, et al. (2004)
H37Rv, Dubos media-replicate 4Dubos medium0.469.760.10Gao Q, et al. (2004)
H37Ra, Dubos media-replicate 1Dubos medium0.1911.180.32Gao Q, et al. (2004)
H37Ra, Dubos media-replicate 2Dubos medium0.5411.270.10Gao Q, et al. (2004)
H37Ra, Dubos media-replicate 3Dubos medium0.5011.140.20Gao Q, et al. (2004)
H37Ra, Dubos media-replicate 4Dubos medium0.0511.450.39Gao Q, et al. (2004)
MTB strain 1254 Ctrl vs 0.05 mM DETA/NO 40min rep 1Diethylenetriamine / nitric oxide adduct-0.0513.440.23Voskuil MI, et al. (2011)
MTB strain 1254 Ctrl vs 0.05 mM DETA/NO 40min rep 2Diethylenetriamine / nitric oxide adduct0.2213.420.15Voskuil MI, et al. (2011)
MTB strain 1254 Ctrl vs 0.05 mM DETA/NO 40min rep 3Diethylenetriamine / nitric oxide adduct-0.3214.070.59Voskuil MI, et al. (2011)
MTB strain 1254 Ctrl vs 0.05 mM DETA/NO 40min rep 4Diethylenetriamine / nitric oxide adduct-0.0713.720.28Voskuil MI, et al. (2011)
MTB strain 1254 Ctrl vs 0.05 mM DETA/NO 40min rep 5Diethylenetriamine / nitric oxide adduct0.4013.750.24Voskuil MI, et al. (2011)
MTB strain 1254 Ctrl vs 0.05 mM DETA/NO 40min rep 6Diethylenetriamine / nitric oxide adduct0.2212.220.18Voskuil MI, et al. (2011)
MTB strain 1254 Ctrl vs 0.005 mM DETA/NO 40min rep 1Diethylenetriamine / nitric oxide adduct-0.4513.950.95Voskuil MI, et al. (2011)
MTB strain 1254 Ctrl vs 0.005 mM DETA/NO 40min rep 2Diethylenetriamine / nitric oxide adduct0.3013.570.47Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs 0.005 mM DETA/NO 40min rep 3Diethylenetriamine / nitric oxide adduct-0.3313.290.69Voskuil MI, et al. (2011)
MTB strain 1254 Ctrl vs 1.0 mM DETA/NO 40min rep 1Diethylenetriamine / nitric oxide adduct-1.0212.211.51Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs 1.0 mM DETA/NO 40min rep 2Diethylenetriamine / nitric oxide adduct-0.9013.840.93Voskuil MI, et al. (2011)
MTB strain 1254 Ctrl vs 1.0 mM DETA/NO 40min rep 3Diethylenetriamine / nitric oxide adduct-0.8312.810.86Voskuil MI, et al. (2011)
MTB strain 1254 Ctrl vs 0.5 mM DETA/NO 40min rep 1Diethylenetriamine / nitric oxide adduct-0.9713.311.37Voskuil MI, et al. (2011)
MTB strain 1254 Ctrl vs 0.5 mM DETA/NO 40min rep 2Diethylenetriamine / nitric oxide adduct-0.7412.950.89Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs 5.0 mM DETA/NO 40min rep 2Diethylenetriamine / nitric oxide adduct-0.9813.461.30Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs 5.0 mM DETA/NO 40min rep 3Diethylenetriamine / nitric oxide adduct-0.9412.271.07Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs 5.0 mM DETA/NO 40min rep 4Diethylenetriamine / nitric oxide adduct-1.1112.761.21Voskuil MI, et al. (2011)
MTB strain 1254 Ctrl vs 2hr Hypoxia rep 1Hypoxia0.1912.090.02Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs 2hr Hypoxia rep 2Hypoxia0.1613.290.02Voskuil MI, et al. (2003)
H37Rv Ctrl vs 0.05 mM DETA/NO 40min rep 1Diethylenetriamine / nitric oxide adduct-0.1912.760.33Voskuil MI, et al. (2003)
H37Rv Ctrl vs 0.05 mM DETA/NO 40min rep 2Diethylenetriamine / nitric oxide adduct0.3512.710.19Voskuil MI, et al. (2003)
H37Rv Ctrl vs 0.05 mM DETA/NO 40min rep 3Diethylenetriamine / nitric oxide adduct0.1011.870.05Voskuil MI, et al. (2003)
H37Rv ctrl vs Rv3132-3134 KO 0.05 mM DETA/NO 40min rep 1Diethylenetriamine / nitric oxide adduct0.2012.410.35Voskuil MI, et al. (2003)
H37Rv ctrl vs Rv3132-3134 KO 0.05 mM DETA/NO 40min rep 2Diethylenetriamine / nitric oxide adduct-0.0812.070.21Voskuil MI, et al. (2003)
H37Rv ctrl vs Rv3132-3134 KO 0.05 mM DETA/NO 40min rep 3Diethylenetriamine / nitric oxide adduct0.1712.790.26Voskuil MI, et al. (2003)
H37Rv ctrl vs Rv3132-34 KO (complemented) 0.05 mM DETA/NO 40min rep 1Diethylenetriamine / nitric oxide adduct0.0112.800.11Voskuil MI, et al. (2003)
H37Rv ctrl vs Rv3132-34 KO (complemented) 0.05 mM DETA/NO 40min rep 2Diethylenetriamine / nitric oxide adduct-0.0312.690.14Voskuil MI, et al. (2003)
H37Rv ctrl vs Rv3132-34 KO (complemented) 0.05 mM DETA/NO 40min rep 3Diethylenetriamine / nitric oxide adduct0.0512.790.17Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs high aeration + 0.001 mM DETA/NO rep 1Diethylenetriamine / nitric oxide adduct0.009.550.01Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs high aeration + 0.005 mM DETA/NO rep 1Diethylenetriamine / nitric oxide adduct-0.079.990.37Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs high aeration + 0.01 mM DETA/NO rep 1Diethylenetriamine / nitric oxide adduct0.159.300.12Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs high aeration + 0.05 mM DETA/NO rep 1Diethylenetriamine / nitric oxide adduct0.049.000.09Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs low aeration + 0.001 mM DETA/NO rep 1Diethylenetriamine / nitric oxide adduct0.0110.120.13Voskuil MI, et al. (2003)
7H9_PA_50uM_4h_T0_02Palmitic acid0.697.381.14Yang Liu, et al. (Unpublished Results)
7h9 control 4hControl0.437.500.55Yang Liu, et al. (Unpublished Results)
7H9_PA_300uM_4h_T0_01Palmitic acid0.237.590.25Yang Liu, et al. (Unpublished Results)
7H9_PA100um_4h_T0_01Palmitic acid0.677.491.26Yang Liu, et al. (Unpublished Results)
PA_50uM_2h_T0_01Defined medium + Palmitic acid0.388.010.24Yang Liu, et al. (Unpublished Results)
AA_30uM_2h_06Arachidonic acid0.629.990.79Yang Liu, et al. (Unpublished Results)
PA_50uM_2h_02Palmitic acid0.559.480.50Yang Liu, et al. (Unpublished Results)
PA_50uM_2h_07Palmitic acid0.308.820.15Yang Liu, et al. (Unpublished Results)
OA_50uM_2h_08Oleic acid0.448.530.36Yang Liu, et al. (Unpublished Results)
AA_30uM_2h_05Arachidonic acid0.428.500.59Yang Liu, et al. (Unpublished Results)
PA_25uM_2h_T0_01Palmitic acid0.398.010.61Yang Liu, et al. (Unpublished Results)
PA_50uM_30 min_04Palmitic acid0.708.260.77Yang Liu, et al. (Unpublished Results)
PA_50uM_10min_T0_01Palmitic acid0.426.880.61Yang Liu, et al. (Unpublished Results)
AA_30uM_10 min_04Arachidonic acid0.229.210.21Yang Liu, et al. (Unpublished Results)
AA_30uM_30min_05Arachidonic acid0.488.530.72Yang Liu, et al. (Unpublished Results)
AA_30uM_1h_04Arachidonic acid0.458.110.78Yang Liu, et al. (Unpublished Results)
PA_50uM_1h_05Palmitic acid0.478.420.46Yang Liu, et al. (Unpublished Results)
AA_10uM_2h_T0_01Arachidonic acid0.308.200.54Yang Liu, et al. (Unpublished Results)
AA_3uM_2h_T0_01Arachidonic acid0.288.390.62Yang Liu, et al. (Unpublished Results)
PA_10uM_2h_T0_01Palmitic acid0.307.520.58Yang Liu, et al. (Unpublished Results)
PA_5uM_2h_T0_01Palmitic acid-0.146.560.31Yang Liu, et al. (Unpublished Results)
CK for AA-NA-4hControl0.217.020.42Yang Liu, et al. (Unpublished Results)
AA_30uM_4h_01Arachidonic acid0.837.811.23Yang Liu, et al. (Unpublished Results)
CK for AA-NA-24hControl0.387.250.87Yang Liu, et al. (Unpublished Results)
AA_30uM_24h_T0_01Arachidonic acid0.347.320.42Yang Liu, et al. (Unpublished Results)
PA_50uM_4h_T0_01Palmitic acid0.656.930.37Yang Liu, et al. (Unpublished Results)
PA_50uM_24h_T0_02Palmitic acid0.346.810.43Yang Liu, et al. (Unpublished Results)
CK_PA-NA--4hControl0.295.390.27Yang Liu, et al. (Unpublished Results)
PA_50uM_24h_T0_01Palmitic acid1.076.210.74Yang Liu, et al. (Unpublished Results)
CK_PA-Na-24h-1Control0.207.120.36Yang Liu, et al. (Unpublished Results)
CK-PA-Na-4h-2Control0.587.361.19Yang Liu, et al. (Unpublished Results)
PA_50uM_2h_06Palmitic acid0.378.860.22Yang Liu, et al. (Unpublished Results)
PA_50uM_2h_05Palmitic acid0.588.120.36Yang Liu, et al. (Unpublished Results)
PA_50uM_2h_08Palmitic acid1.417.471.09Yang Liu, et al. (Unpublished Results)
AA_30uM_2h_08Arachidonic acid0.308.520.47Yang Liu, et al. (Unpublished Results)
OA_50uM_2h_05Oleic acid0.128.250.16Yang Liu, et al. (Unpublished Results)
OA_50uM_2h_06Oleic acid-0.188.310.21Yang Liu, et al. (Unpublished Results)
CK for OA-4h-1Control-0.179.390.47Yang Liu, et al. (Unpublished Results)
OA_50uM_4h_02Oleic acid0.179.650.26Yang Liu, et al. (Unpublished Results)
CK-OA-Na-24h-1Control0.159.510.43Yang Liu, et al. (Unpublished Results)
AA_30uM_2h_09Arachidonic acid0.279.540.58Yang Liu, et al. (Unpublished Results)
PA_50uM_2h_01Palmitic acid0.289.660.24Yang Liu, et al. (Unpublished Results)
PA_50uM_2h_03Palmitic acid0.159.500.11Yang Liu, et al. (Unpublished Results)
OA_50uM_2h_07Oleic acid-0.139.190.17Yang Liu, et al. (Unpublished Results)
OA_100uM_2h_T0_01Oleic acid0.118.520.09Yang Liu, et al. (Unpublished Results)
CK for AA-Na-4h-2Control0.687.481.51Yang Liu, et al. (Unpublished Results)
AA_60uM_2h_T0_02Arachidonic acid0.426.910.28Yang Liu, et al. (Unpublished Results)
AA_30uM_24+AA_30uM_1h_01Arachidonic acid0.148.840.23Yang Liu, et al. (Unpublished Results)
AA_30uM_24h+AA_60uM_1h_01Arachidonic acid0.008.630.11Yang Liu, et al. (Unpublished Results)
PA_50uM_24h+PA_50uM_1h_01Palmitic acid0.119.020.10Yang Liu, et al. (Unpublished Results)
PA_50uM_24h+PA_100uM_1h_01Palmitic acid0.168.530.19Yang Liu, et al. (Unpublished Results)
AA_10uM_10min_01Arachidonic acid0.128.540.23Yang Liu, et al. (Unpublished Results)
PA_10uM_10min_02Palmitic acid-0.038.290.17Yang Liu, et al. (Unpublished Results)
PA_5 uM_10min_02Palmitic acid0.138.530.24Yang Liu, et al. (Unpublished Results)
AA_3uM_10min_02Arachidonic acid0.208.740.60Yang Liu, et al. (Unpublished Results)
L2A_30uM_2h_01Linoleic acid0.429.350.66Yang Liu, et al. (Unpublished Results)
L2A_30uM_4h_T0_01Linoleic acid0.3610.241.00Yang Liu, et al. (Unpublished Results)
L2A_30uM_2h_02Linoleic acid0.469.710.77Yang Liu, et al. (Unpublished Results)
CK for MDG-OA-Na-24hControl0.039.510.06Yang Liu, et al. (Unpublished Results)
CK-1-2h for AA-NA and LA-NAControl-0.136.330.34Yang Liu, et al. (Unpublished Results)
CK-2-2h for OA-NA and PA-NAControl-0.046.670.13Yang Liu, et al. (Unpublished Results)
CK-4h for AA-NA-0.03mMControl0.188.210.48Yang Liu, et al. (Unpublished Results)
CK-4h for OA-NA-0.05mMControl0.067.660.13Yang Liu, et al. (Unpublished Results)
OA_50uM_4h_01Oleic acid0.778.221.22Yang Liu, et al. (Unpublished Results)
OA_50uM_2h_01Oleic acid0.287.810.48Yang Liu, et al. (Unpublished Results)
AA_30uM_4h_02Arachidonic acid0.607.761.73Yang Liu, et al. (Unpublished Results)
L2A_30uM_2h_05Linoleic acid0.527.430.88Yang Liu, et al. (Unpublished Results)
AA_30uM_2h_07Arachidonic acid0.136.620.14Yang Liu, et al. (Unpublished Results)
OA_50uM_2h_02Oleic acid-0.247.110.46Yang Liu, et al. (Unpublished Results)
CK for OA/PA-Na-4hControl-0.256.460.65Yang Liu, et al. (Unpublished Results)
AA_30uM_4h_03Arachidonic acid0.338.160.71Yang Liu, et al. (Unpublished Results)
OA_50uM_4h_03Oleic acid0.538.701.00Yang Liu, et al. (Unpublished Results)
CK-for MDG-OA-4hControl0.048.090.01Yang Liu, et al. (Unpublished Results)
L2A_30uM_4h_T0_02Linoleic acid1.008.931.59Yang Liu, et al. (Unpublished Results)
CK-MDG-AA-Na-2hControl0.189.890.28Yang Liu, et al. (Unpublished Results)
CK for AA-NA-2h-2Control0.619.211.03Yang Liu, et al. (Unpublished Results)
CK-for OA-NA, 2hControl0.518.870.52Yang Liu, et al. (Unpublished Results)
CK-MDG-2h for PA-NAControl0.409.910.67Yang Liu, et al. (Unpublished Results)
CK-MDG-2h for PA-NA-2Control0.209.000.33Yang Liu, et al. (Unpublished Results)
CK-PA-Na-2h-01Control-0.068.200.18Yang Liu, et al. (Unpublished Results)
CK-for MDG-4h-PA-NAControl0.017.860.06Yang Liu, et al. (Unpublished Results)
CK-for MDG-24h-PA-NAControl0.157.570.33Yang Liu, et al. (Unpublished Results)
PA_100uM_2h_T0_01Palmitic acid0.547.590.35Yang Liu, et al. (Unpublished Results)
PA_300uM_2h_T0_01Palmitic acid0.557.830.59Yang Liu, et al. (Unpublished Results)
PA_50uM_4hPalmitic acid0.148.110.11Yang Liu, et al. (Unpublished Results)
PA_100uM_4h_T0_01Palmitic acid0.538.820.40Yang Liu, et al. (Unpublished Results)
PA_300uM_4h_T0_01Palmitic acid0.667.700.65Yang Liu, et al. (Unpublished Results)
PA_50uM_24h_T0Palmitic acid0.017.460.04Yang Liu, et al. (Unpublished Results)
PA_100uM_24h_T0_01Palmitic acid0.356.510.27Yang Liu, et al. (Unpublished Results)
PA_300uM_24h_T0_01Palmitic acid0.846.510.69Yang Liu, et al. (Unpublished Results)
AA_10uM_10 min_01Arachidonic acid0.148.950.32Yang Liu, et al. (Unpublished Results)
AA_3uM_10 min_01Arachidonic acid-0.048.140.16Yang Liu, et al. (Unpublished Results)
PA_5uM_10 min_01Palmitic acid0.626.770.84Yang Liu, et al. (Unpublished Results)
PA_10uM_10 min_01Palmitic acid0.018.150.07Yang Liu, et al. (Unpublished Results)
CK-PA-NA-2h-02, 100901Control0.018.090.04Yang Liu, et al. (Unpublished Results)
CK-PA-NA-2h-3, 101801Control0.167.510.52Yang Liu, et al. (Unpublished Results)
CK-PA-NA-101801-2Control0.338.570.97Yang Liu, et al. (Unpublished Results)
PA_50uM_2h_04Palmitic acid0.578.370.50Yang Liu, et al. (Unpublished Results)
AA_30uM_2h_03Arachidonic acid0.158.500.24Yang Liu, et al. (Unpublished Results)
CK_AA_NA-2hControl-0.019.580.07Yang Liu, et al. (Unpublished Results)
CK-AA-Na-2hControl0.058.500.11Yang Liu, et al. (Unpublished Results)
AA_30uM_2h_01Arachidonic acid0.218.930.51Yang Liu, et al. (Unpublished Results)
CK-AA0.03-2h-02Control0.118.990.32Yang Liu, et al. (Unpublished Results)
CK-AA-2hControl0.107.990.25Yang Liu, et al. (Unpublished Results)
AA_30uM_2h_02Arachidonic acid0.109.530.17Yang Liu, et al. (Unpublished Results)
AA_30uM_2h_04Arachidonic acid0.338.260.66Yang Liu, et al. (Unpublished Results)
PA_100uM_2h_T0_02Palmitic acid0.726.490.63Yang Liu, et al. (Unpublished Results)
PA_100uM_2h_03Palmitic acid-0.315.010.32Yang Liu, et al. (Unpublished Results)
PA_100uM_2h_04Palmitic acid-0.256.320.41Yang Liu, et al. (Unpublished Results)
AA_60uM_2h_T0_01Arachidonic acid0.336.690.34Yang Liu, et al. (Unpublished Results)
AA_60uM_2h_T0_03Arachidonic acid0.486.910.70Yang Liu, et al. (Unpublished Results)
PA_100uM_2h_T0_05Palmitic acid0.115.940.02Yang Liu, et al. (Unpublished Results)
PA_50uM_2h_T0_02Palmitic acid-0.107.110.17Yang Liu, et al. (Unpublished Results)
CK_LA_2hControl-0.208.190.43Yang Liu, et al. (Unpublished Results)
CK_LA_2h-2Control0.078.320.10Yang Liu, et al. (Unpublished Results)
L2A_30uM_2h_03Linoleic acid0.287.590.32Yang Liu, et al. (Unpublished Results)
CK_LA_2h-3Control0.258.350.45Yang Liu, et al. (Unpublished Results)
CK-LA-2h-4Control0.348.410.71Yang Liu, et al. (Unpublished Results)
L2A_30uM_2h_04Linoleic acid0.308.110.47Yang Liu, et al. (Unpublished Results)
OA_50uM_2h_03Oleic acid0.107.310.07Yang Liu, et al. (Unpublished Results)
OA_50uM_2h_10Oleic acid-0.017.070.03Yang Liu, et al. (Unpublished Results)
CK_OA_NA_0.05_2hControl0.037.570.03Yang Liu, et al. (Unpublished Results)
CK_OA_NA_2h-02Control0.147.320.19Yang Liu, et al. (Unpublished Results)
OA_50uM_2h_04Oleic acid0.078.120.08Yang Liu, et al. (Unpublished Results)
CK-OA_NA_2HControl-0.897.391.46Yang Liu, et al. (Unpublished Results)
OA_50uM_2h_09Oleic acid0.347.620.55Yang Liu, et al. (Unpublished Results)
PA_100uM_24h_01Palmitic acid-0.116.910.20Yang Liu, et al. (Unpublished Results)
PA_100uM_24h_02Palmitic acid0.235.820.05Yang Liu, et al. (Unpublished Results)
PA_100uM_24h_03Palmitic acid-1.083.990.76Yang Liu, et al. (Unpublished Results)
PA_50uM_24h_01Palmitic acid0.256.460.14Yang Liu, et al. (Unpublished Results)
PA_50uM_24h_02Palmitic acid-0.715.000.48Yang Liu, et al. (Unpublished Results)
AA_60uM_24h_01Arachidonic acid-0.369.090.86Yang Liu, et al. (Unpublished Results)
PA_50uM_24h_03Palmitic acid0.158.510.13Yang Liu, et al. (Unpublished Results)
AA_30uM_24h_02Arachidonic acid-0.007.930.01Yang Liu, et al. (Unpublished Results)
AA_30uM_24h_03Arachidonic acid-0.048.420.18Yang Liu, et al. (Unpublished Results)
AA_60uM_24h_02Arachidonic acid0.207.620.53Yang Liu, et al. (Unpublished Results)
AA_30uM_24h_04Arachidonic acid0.078.470.22Yang Liu, et al. (Unpublished Results)
AA_60uM_24h_03Arachidonic acid-0.037.990.15Yang Liu, et al. (Unpublished Results)
PA_50uM_10 min_02Palmitic acid0.298.660.29Yang Liu, et al. (Unpublished Results)
PA_50uM_10 min_03Palmitic acid0.078.570.00Yang Liu, et al. (Unpublished Results)
Acetate-3mM-2h-01Acetate0.416.640.74Yang Liu, et al. (Unpublished Results)
Acetate-3mM-2h-02Acetate0.156.840.18Yang Liu, et al. (Unpublished Results)
Acetate-3mM-2h-03Acetate0.287.030.49Yang Liu, et al. (Unpublished Results)
OA_50uM_10min_05Oleic acid0.236.940.16Yang Liu, et al. (Unpublished Results)
PA_50uM_10min_01Palmitic acid0.168.530.03Yang Liu, et al. (Unpublished Results)
PA_50uM_30min_01Palmitic acid0.596.790.71Yang Liu, et al. (Unpublished Results)
PA_50uM_1h_01Palmitic acid0.959.740.59Yang Liu, et al. (Unpublished Results)
OA_50uM_10min_01Oleic acid0.387.970.48Yang Liu, et al. (Unpublished Results)
OA_50uM_30min_01Oleic acid0.549.170.38Yang Liu, et al. (Unpublished Results)
OA_50uM_1h_01Oleic acid0.358.120.40Yang Liu, et al. (Unpublished Results)
OA_50uM_10min_02Oleic acid0.098.240.11Yang Liu, et al. (Unpublished Results)
AA_30uM_30min_06Arachidonic acid0.187.990.24Yang Liu, et al. (Unpublished Results)
OA_50uM_30min_02Oleic acid0.518.280.68Yang Liu, et al. (Unpublished Results)
OA_50uM_1h_02Oleic acid0.329.150.26Yang Liu, et al. (Unpublished Results)
OA_50uM_30min_03Oleic acid0.249.110.21Yang Liu, et al. (Unpublished Results)
OA_50uM_1h_03Oleic acid0.139.270.01Yang Liu, et al. (Unpublished Results)
PA_50uM_30min_02Palmitic acid0.108.810.02Yang Liu, et al. (Unpublished Results)
PA_50uM_1h_02Palmitic acid0.118.910.03Yang Liu, et al. (Unpublished Results)
PA_50uM_1h_03Palmitic acid0.228.970.10Yang Liu, et al. (Unpublished Results)
L2A_30uM_30min_01Linoleic acid0.338.900.32Yang Liu, et al. (Unpublished Results)
L2A_30uM_30min_02Linoleic acid0.348.260.38Yang Liu, et al. (Unpublished Results)
PA_50uM_30min_03Palmitic acid0.248.530.25Yang Liu, et al. (Unpublished Results)
OA_50uM_30min_04Oleic acid-0.526.960.41Yang Liu, et al. (Unpublished Results)
OA_50uM_1h_07Oleic acid0.118.760.03Yang Liu, et al. (Unpublished Results)
PA_50uM_30min_08Palmitic acid0.977.940.73Yang Liu, et al. (Unpublished Results)
PA_50uM_1h_10Palmitic acid-1.466.260.79Yang Liu, et al. (Unpublished Results)
L2A_30uM_10min_07Linoleic acid1.115.511.43Yang Liu, et al. (Unpublished Results)
L2A_30uM_10min_08Linoleic acid0.236.050.32Yang Liu, et al. (Unpublished Results)
PA_50uM_4h_07Palmitic acid0.675.250.35Yang Liu, et al. (Unpublished Results)
ETYA_30uM_1h_01Eicosatetraynoic Acid1.328.431.03Yang Liu, et al. (Unpublished Results)
Indomechacin-0.2mM-2hIndomethacin-0.434.310.21Yang Liu, et al. (Unpublished Results)
NDGA-0.4mM-2hNordihydroguaiaretic acid-2.474.581.11Yang Liu, et al. (Unpublished Results)
ETYA_3uM+AA_60min_02Eicosatetraynoic Acid + Arachidonic acid0.815.110.79Yang Liu, et al. (Unpublished Results)
ETYA_10uM+AA_60min_02Eicosatetraynoic Acid0.484.890.34Yang Liu, et al. (Unpublished Results)
TBA713-2Arachidonic acid0.875.140.84Yang Liu, et al. (Unpublished Results)
TBA714-2Arachidonic acid0.544.910.40Yang Liu, et al. (Unpublished Results)
Indomechacin-200uM-30minIndomethacin0.845.010.52Yang Liu, et al. (Unpublished Results)
NDGA-200uM-30minNordihydroguaiaretic acid0.335.620.21Yang Liu, et al. (Unpublished Results)
2-BA-1Benzoic acid0.378.640.16Yang Liu, et al. (Unpublished Results)
2-BA+OA-1Oleic acid-0.047.950.09Yang Liu, et al. (Unpublished Results)
CHP_25uM_1h_01Cumene Hydroperoxide0.076.760.12Yang Liu, et al. (Unpublished Results)
CHP+AA-1h-1Cumene Hydroperoxide + Arachidonic acid1.195.641.48Yang Liu, et al. (Unpublished Results)
CHP_25uM_2h_01Cumene Hydroperoxide-0.146.740.41Yang Liu, et al. (Unpublished Results)
CHP+AA-2h-1Cumene Hydroperoxide + Arachidonic acid0.036.340.09Yang Liu, et al. (Unpublished Results)
CHP+AA-30m-1Cumene Hydroperoxide + Arachidonic acid0.286.560.37Yang Liu, et al. (Unpublished Results)
CHP+AA-4h-1Cumene Hydroperoxide + Arachidonic acid-0.636.481.04Yang Liu, et al. (Unpublished Results)
CHP_25uM_24h_01Cumene Hydroperoxide-0.056.290.05Yang Liu, et al. (Unpublished Results)
CHP+AA-24h-1Cumene Hydroperoxide + Arachidonic acid-1.067.161.06Yang Liu, et al. (Unpublished Results)
2-BA_100uM_30min_01Benzoic acid-0.145.390.34Yang Liu, et al. (Unpublished Results)
2-BA_500uM_30min_01Benzoic acid-0.075.490.24Yang Liu, et al. (Unpublished Results)
CHP25uM_24h+50uMOA_30min_01Cumene Hydroperoxide-0.636.820.74Yang Liu, et al. (Unpublished Results)
Acetate-3mM-10m-01Acetate0.487.450.99Yang Liu, et al. (Unpublished Results)
Acetate-3mM-30m-01Acetate0.586.151.36Yang Liu, et al. (Unpublished Results)
Acetate-3mM-60m-01Acetate0.647.391.18Yang Liu, et al. (Unpublished Results)
Acetate-3mM-10m-02Acetate0.667.621.98Yang Liu, et al. (Unpublished Results)
Acetate-3mM-30m-02Acetate0.406.880.97Yang Liu, et al. (Unpublished Results)
Acetate-3mM-60m-02Acetate0.497.700.96Yang Liu, et al. (Unpublished Results)
Acetate-3mM-10m-03Acetate0.337.000.77Yang Liu, et al. (Unpublished Results)
Acetate-3mM-30m-03Acetate0.707.561.50Yang Liu, et al. (Unpublished Results)
Acetate-3mM-60m-03Acetate0.378.120.66Yang Liu, et al. (Unpublished Results)
L2A_30uM_10min_01Linoleic acid-0.307.120.54Yang Liu, et al. (Unpublished Results)
PA_50uM_10min_08Palmitic acid0.307.930.31Yang Liu, et al. (Unpublished Results)
L2A_30uM_30min_03Linoleic acid0.146.850.10Yang Liu, et al. (Unpublished Results)
PA_50uM_30min_10Palmitic acid0.276.660.27Yang Liu, et al. (Unpublished Results)
L2A_30uM_1h_01Linoleic acid0.388.320.26Yang Liu, et al. (Unpublished Results)
PA_50uM_1h_12Palmitic acid0.789.300.47Yang Liu, et al. (Unpublished Results)
L2A_30uM_10min_02Linoleic acid0.187.850.12Yang Liu, et al. (Unpublished Results)
L2A_30uM_30min_04Linoleic acid0.107.420.05Yang Liu, et al. (Unpublished Results)
L2A_30uM_1h_02Linoleic acid0.359.010.21Yang Liu, et al. (Unpublished Results)
AA_30uM_10m_01Arachidonic acid0.208.250.13Yang Liu, et al. (Unpublished Results)
AA_30uM_1h_01Arachidonic acid0.248.540.12Yang Liu, et al. (Unpublished Results)
L2A_30uM_10min_03Linoleic acid0.237.490.14Yang Liu, et al. (Unpublished Results)
AA_30uM_10min_02Arachidonic acid0.078.120.08Yang Liu, et al. (Unpublished Results)
L2A_30uM_30min_05Linoleic acid0.547.850.54Yang Liu, et al. (Unpublished Results)
AA_30uM_30min_04Arachidonic acid0.018.580.19Yang Liu, et al. (Unpublished Results)
PA_50uM_10min_10Palmitic acid0.277.280.12Yang Liu, et al. (Unpublished Results)
PA_50uM_30min_09Palmitic acid0.166.660.04Yang Liu, et al. (Unpublished Results)
PA_50uM_1h_11Palmitic acid-0.126.840.27Yang Liu, et al. (Unpublished Results)
OA_50uM_10min_03Oleic acid-0.587.450.87Yang Liu, et al. (Unpublished Results)
OA_50uM_30min_08Oleic acid0.186.970.03Yang Liu, et al. (Unpublished Results)
OA_50uM_1h_08Oleic acid0.086.510.00Yang Liu, et al. (Unpublished Results)
OA_50uM_10min_04Oleic acid0.468.070.45Yang Liu, et al. (Unpublished Results)
OA_50uM_30min_09Oleic acid0.537.480.41Yang Liu, et al. (Unpublished Results)
OA_50uM_1h_09Oleic acid0.095.810.04Yang Liu, et al. (Unpublished Results)
OA_50uM_10min_06Oleic acid0.187.170.13Yang Liu, et al. (Unpublished Results)
OA_50uM_30min_07Oleic acid-0.426.340.72Yang Liu, et al. (Unpublished Results)
OA_50uM_1h_10Oleic acid0.416.110.29Yang Liu, et al. (Unpublished Results)
L2A_30uM_1h_03Linoleic acid0.207.630.11Yang Liu, et al. (Unpublished Results)
AA_30uM_1h_02Arachidonic acid0.447.430.53Yang Liu, et al. (Unpublished Results)
AA_30uM_10min_03Arachidonic acid0.057.570.08Yang Liu, et al. (Unpublished Results)
AA_30uM_30min_08Arachidonic acid0.217.250.21Yang Liu, et al. (Unpublished Results)
AA_30uM_1h_03Arachidonic acid0.077.610.10Yang Liu, et al. (Unpublished Results)
PA_50uM_10min_09Palmitic acid0.567.680.54Yang Liu, et al. (Unpublished Results)
PA_50uM_30min_11Palmitic acid-0.017.570.21Yang Liu, et al. (Unpublished Results)
PA_50uM_1h_04Palmitic acid0.268.090.08Yang Liu, et al. (Unpublished Results)
OA_50uM_2h+(0.5%BSA+10mMGlu)_30min_01Oleic acid + Glucose + BSA0.099.920.36Yang Liu, et al. (Unpublished Results)
OA_50uM_2h+(1.0% BSA+10mMGlu)_30 min _01Oleic acid + Glucose + BSA0.169.390.48Yang Liu, et al. (Unpublished Results)
OA_50uM_2h+(1.5%BSA+10mMGlu)_30 min_01Oleic acid + Glucose + BSA0.249.260.73Yang Liu, et al. (Unpublished Results)
OA_50uM_2h+0.5%BSA_30min _01Oleic acid + BSA0.349.071.01Yang Liu, et al. (Unpublished Results)
OA_50uM_2h+1.0% BSA_30min_01Oleic acid + BSA0.159.860.29Yang Liu, et al. (Unpublished Results)
OA_50uM_2h+1.5% BSA_30min_01Oleic acid + BSA0.479.251.17Yang Liu, et al. (Unpublished Results)
ETYA_3uM_1h_02Eicosatetraynoic Acid0.586.650.87Yang Liu, et al. (Unpublished Results)
ETYA_10uM_1h_02Eicosatetraynoic Acid0.408.010.56Yang Liu, et al. (Unpublished Results)
ETYA_3uM+AA_1h_02Eicosatetraynoic Acid + Arachidonic acid0.126.020.16Yang Liu, et al. (Unpublished Results)
ETYA_10uM+AA_1h_02Eicosatetraynoic Acid0.249.160.20Yang Liu, et al. (Unpublished Results)
L2A_30uM_1h_07Linoleic acid1.668.081.71Yang Liu, et al. (Unpublished Results)
AA_30uM_30min_01Arachidonic acid0.648.160.84Yang Liu, et al. (Unpublished Results)
L2A_30uM_1h_08Linoleic acid0.627.071.01Yang Liu, et al. (Unpublished Results)
AA_30uM_30min_02Arachidonic acid0.097.830.06Yang Liu, et al. (Unpublished Results)
L2A_30uM_1h_09Linoleic acid0.697.040.88Yang Liu, et al. (Unpublished Results)
AA_30uM_30min_03Arachidonic acid0.056.650.02Yang Liu, et al. (Unpublished Results)
ETYA_30uM_10min-06Eicosatetraynoic Acid0.476.850.87Yang Liu, et al. (Unpublished Results)
Acetate-3mM-10m-07Acetate0.277.000.56Yang Liu, et al. (Unpublished Results)
Acetate-3mM-30m-08Acetate0.258.190.64Yang Liu, et al. (Unpublished Results)
Acetate-3mM-60m-04Acetate0.348.140.88Yang Liu, et al. (Unpublished Results)
7H9Cy3:MDGCy5-01Defined medium-0.848.530.92Yang Liu, et al. (Unpublished Results)
MDGCy3:7H9Cy5-01Defined medium0.329.290.35Yang Liu, et al. (Unpublished Results)
7H9Cy3:MDGCy5-02Defined medium-0.467.690.66Yang Liu, et al. (Unpublished Results)
7H9Cy3:MDGCy5-03Defined medium-0.388.540.56Yang Liu, et al. (Unpublished Results)
MDGCy3:7H9Cy5-02Defined medium0.148.940.13Yang Liu, et al. (Unpublished Results)
MDGCy3:7H9Cy5-03Defined medium0.239.010.25Yang Liu, et al. (Unpublished Results)
Strain95-OA-10M-01Oleic acid-0.129.220.22Yang Liu, et al. (Unpublished Results)
MDG:MD-glycerolDefined medium + glycerol1.635.721.74Yang Liu, et al. (Unpublished Results)
Acetate-3mM-30m-04Acetate0.117.840.15Yang Liu, et al. (Unpublished Results)
Acetate-3mM-10m_04Acetate0.168.440.23Yang Liu, et al. (Unpublished Results)
Acetate-3mM-30m-07Acetate-0.138.120.44Yang Liu, et al. (Unpublished Results)
Acetate-3mM-10m-06Acetate-0.197.300.41Yang Liu, et al. (Unpublished Results)
Glycerol_1%_10M_01Glycerol-0.277.640.61Yang Liu, et al. (Unpublished Results)
Glycerol_1%_30M_01Glycerol0.078.340.10Yang Liu, et al. (Unpublished Results)
Glycerol_1%Glycerol0.078.040.07Yang Liu, et al. (Unpublished Results)
Acetate-3mM-30m-05Acetate0.148.610.20Yang Liu, et al. (Unpublished Results)
Acetate-3mM-10m-05Acetate0.008.440.11Yang Liu, et al. (Unpublished Results)
Acetate-3mM-30m-06Acetate-0.098.180.28Yang Liu, et al. (Unpublished Results)
Test-1Control0.098.450.24Yang Liu, et al. (Unpublished Results)
Test-2Control0.807.791.22Yang Liu, et al. (Unpublished Results)
Test-3Control0.357.990.74Yang Liu, et al. (Unpublished Results)
Test-4Control0.257.870.59Yang Liu, et al. (Unpublished Results)
Test-5Oleic acid0.608.960.81Yang Liu, et al. (Unpublished Results)
Test-6Oleic acid0.258.440.23Yang Liu, et al. (Unpublished Results)
CHX-testCycloheximide + Oleic acid0.764.380.53Yang Liu, et al. (Unpublished Results)
Test-G+OAOleic acid-0.286.310.24Yang Liu, et al. (Unpublished Results)
Glucose_20mM_1h+OA_50uM_10minOleic acid + Glucose0.016.810.03Yang Liu, et al. (Unpublished Results)
Glucose_40mM_1h+OA_50uM_10minOleic acid + Glucose0.077.150.25Yang Liu, et al. (Unpublished Results)
OA_50uM_10min+Glu_40mM_20min_01Oleic acid + Glucose0.077.150.25Yang Liu, et al. (Unpublished Results)
OA50um_10min+10mM_G_20minOleic acid + Glucose0.016.550.06Yang Liu, et al. (Unpublished Results)
PA_50uM_1h_06Palmitic acid0.517.350.26Yang Liu, et al. (Unpublished Results)
PA_50uM_1h_07Palmitic acid0.117.340.06Yang Liu, et al. (Unpublished Results)
PA_50uM_1h_09Palmitic acid0.438.210.20Yang Liu, et al. (Unpublished Results)
AA_30uM_1h_05Arachidonic acid0.128.500.01Yang Liu, et al. (Unpublished Results)
AA_30uM_1h_06Arachidonic acid-0.317.980.45Yang Liu, et al. (Unpublished Results)
OA_50uM_30min_05Oleic acid0.308.800.13Yang Liu, et al. (Unpublished Results)
OA_50uM_30min_06Oleic acid0.198.310.02Yang Liu, et al. (Unpublished Results)
OA_50uM_1h_06Oleic acid0.148.090.05Yang Liu, et al. (Unpublished Results)
OA_50uM_1h_05Oleic acid0.369.020.17Yang Liu, et al. (Unpublished Results)
OA_50uM_1h_04Oleic acid-0.028.400.16Yang Liu, et al. (Unpublished Results)
L2A_30uM_10min_04Linoleic acid0.208.610.17Yang Liu, et al. (Unpublished Results)
L2A_30uM_10min_05Linoleic acid0.207.380.06Yang Liu, et al. (Unpublished Results)
PA_50uM_10min_04Palmitic acid0.467.590.29Yang Liu, et al. (Unpublished Results)
PA_50uM_10min_05Palmitic acid-0.196.590.36Yang Liu, et al. (Unpublished Results)
PA_50uM_10min_06Palmitic acid0.207.190.14Yang Liu, et al. (Unpublished Results)
AA_30uM_10 min_05Arachidonic acid0.068.460.05Yang Liu, et al. (Unpublished Results)
AA_30uM_10 min_07Arachidonic acid0.088.750.04Yang Liu, et al. (Unpublished Results)
AA_30uM_10 min_06Arachidonic acid-0.158.250.34Yang Liu, et al. (Unpublished Results)
L2A_30uM_10min_06Linoleic acid0.337.330.35Yang Liu, et al. (Unpublished Results)
PA_50uM_4h_01Defined medium + Palmitic acid0.158.760.06Yang Liu, et al. (Unpublished Results)
PA_50uM_4h_02Defined medium + Palmitic acid-0.528.210.50Yang Liu, et al. (Unpublished Results)
PA_50uM_4h_04Defined medium + Palmitic acid0.157.780.02Yang Liu, et al. (Unpublished Results)
PA_50uM_4h_03Defined medium + Palmitic acid0.468.280.25Yang Liu, et al. (Unpublished Results)
PA_50uM_4h_05Defined medium + Palmitic acid0.568.640.29Yang Liu, et al. (Unpublished Results)
PA_50uM_4h_06Defined medium + Palmitic acid0.467.470.13Yang Liu, et al. (Unpublished Results)
ETYA_30uM_10min-01Eicosatetraynoic Acid0.139.220.05Yang Liu, et al. (Unpublished Results)
ETYA_30uM_10min-02Eicosatetraynoic Acid-0.039.070.19Yang Liu, et al. (Unpublished Results)
ETYA_30uM_10min-04Eicosatetraynoic Acid0.149.210.03Yang Liu, et al. (Unpublished Results)
ETYA_30uM_10min-03Eicosatetraynoic Acid-0.039.510.18Yang Liu, et al. (Unpublished Results)
ETYA_30uM_10min-05Eicosatetraynoic Acid0.127.100.05Yang Liu, et al. (Unpublished Results)
PA_50uM_24h_04Defined medium + Palmitic acid0.287.490.38Yang Liu, et al. (Unpublished Results)
PA_50uM_24h_05Defined medium + Palmitic acid1.025.600.56Yang Liu, et al. (Unpublished Results)
PA_50uM_24h_06Defined medium + Palmitic acid-0.177.160.28Yang Liu, et al. (Unpublished Results)
L2A_30uM_30Min_06Linoleic acid0.168.850.00Yang Liu, et al. (Unpublished Results)
L2A_30uM_1h_04Linoleic acid0.638.140.51Yang Liu, et al. (Unpublished Results)
Succinate_10mM_30min_01Succinate-0.215.750.35Yang Liu, et al. (Unpublished Results)
MTB1254[fadA]_01Dipyridyl1.856.970.80Yang Liu, et al. (Unpublished Results)
MTB1254[1683]_01Dipyridyl1.248.590.34Yang Liu, et al. (Unpublished Results)
AA_30uM_30min_07Arachidonic acid0.228.370.06Yang Liu, et al. (Unpublished Results)
L2A_30uM_30min_07Linoleic acid0.058.210.04Yang Liu, et al. (Unpublished Results)
L2A_30uM_1h_05Linoleic acid0.257.710.22Yang Liu, et al. (Unpublished Results)
L2A_30uM_1h_06Linoleic acid0.398.770.32Yang Liu, et al. (Unpublished Results)
AA_30uM_1h_07Arachidonic acid-0.207.860.42Yang Liu, et al. (Unpublished Results)
AA_30uM_1h_08Arachidonic acid0.048.800.06Yang Liu, et al. (Unpublished Results)
PA_50uM_30 min_07Palmitic acid0.548.330.34Yang Liu, et al. (Unpublished Results)
PA_50uM_8h_01Palmitic acid0.167.940.06Yang Liu, et al. (Unpublished Results)
PA_50uM_12h_01Palmitic acid-0.067.450.17Yang Liu, et al. (Unpublished Results)
LAA_50uM_30min_01Linoleic acid0.367.490.41Yang Liu, et al. (Unpublished Results)
LAA_50uM_10min_01Linoleic acid-0.157.330.30Yang Liu, et al. (Unpublished Results)
PA_50uM_30 min_06Palmitic acid0.117.320.06Yang Liu, et al. (Unpublished Results)
PA_50uM_8h_03Palmitic acid0.007.810.00Yang Liu, et al. (Unpublished Results)
PA_50uM_8h_05Palmitic acid-0.059.360.20Yang Liu, et al. (Unpublished Results)
PA_50uM_12h_05Palmitic acid0.199.090.08Yang Liu, et al. (Unpublished Results)
PA_50uM_12h_03Palmitic acid0.159.160.00Yang Liu, et al. (Unpublished Results)
PA_50uM_8h_02Palmitic acid0.258.230.25Yang Liu, et al. (Unpublished Results)
PA_50uM_12h_02Palmitic acid0.109.180.07Yang Liu, et al. (Unpublished Results)
PA_50uM_12h_04Palmitic acid0.299.330.17Yang Liu, et al. (Unpublished Results)
PA_50uM_12h_06Palmitic acid0.129.600.00Yang Liu, et al. (Unpublished Results)
PA_50uM_8h_06Palmitic acid0.2210.210.10Yang Liu, et al. (Unpublished Results)
PA_50uM_8h_04Palmitic acid0.108.760.01Yang Liu, et al. (Unpublished Results)
OA_50uM_4h_04Oleic acid0.388.600.51Yang Liu, et al. (Unpublished Results)
OA_50uM_4h_05Oleic acid0.217.950.37Yang Liu, et al. (Unpublished Results)
AA_30uM_4h_04Arachidonic acid0.518.460.90Yang Liu, et al. (Unpublished Results)
AA_30uM_4h_05Arachidonic acid0.108.060.26Yang Liu, et al. (Unpublished Results)
AA_30uM_4h_06Arachidonic acid0.127.610.22Yang Liu, et al. (Unpublished Results)
AA_30uM_4h_07Arachidonic acid0.608.881.50Yang Liu, et al. (Unpublished Results)
OA_50uM_4h_06Oleic acid0.428.160.72Yang Liu, et al. (Unpublished Results)
OA_50uM_4h_07Oleic acid0.118.370.22Yang Liu, et al. (Unpublished Results)
L2A_30uM_4h_03Linoleic acid0.208.050.36Yang Liu, et al. (Unpublished Results)
L2A_30uM_4h_05Linoleic acid0.448.170.83Yang Liu, et al. (Unpublished Results)
Glucose_5mM_10min_01Glucose0.058.380.18Yang Liu, et al. (Unpublished Results)
Rv_OA_10minOleic acid-0.048.660.21Yang Liu, et al. (Unpublished Results)
Rv_Rv3524-1Wild type vs Mutant-0.087.860.31Yang Liu, et al. (Unpublished Results)
AA_30uM_4h_09Arachidonic acid0.379.130.94Yang Liu, et al. (Unpublished Results)
L2A_30uM_4h_07Linoleic acid0.238.900.51Yang Liu, et al. (Unpublished Results)
PA_50uM_24h_07Palmitic acid0.109.660.05Yang Liu, et al. (Unpublished Results)
PA_50uM_24h_08Palmitic acid0.1110.030.06Yang Liu, et al. (Unpublished Results)
LAA_50uM_10min_02Linoleic acid0.039.460.16Yang Liu, et al. (Unpublished Results)
OA_50uM_10min_07Oleic acid0.159.280.01Yang Liu, et al. (Unpublished Results)
OA_50uM_10min_08Oleic acid0.028.800.14Yang Liu, et al. (Unpublished Results)
7H9_MTB1254_OA50_10M_01Oleic acid-0.008.180.01Yang Liu, et al. (Unpublished Results)
7H9_MTB1254_OA100_10M_01Oleic acid0.027.780.04Yang Liu, et al. (Unpublished Results)
7H9_MTB1254[3524-1]_OA50_10M_01Oleic acid0.118.060.23Yang Liu, et al. (Unpublished Results)
7H9_MTB1254[3524-1]_OA100_10M_01Oleic acid-0.028.160.04Yang Liu, et al. (Unpublished Results)
MTB1254[3524-1]_OA_10min_03Oleic acid0.188.200.21Yang Liu, et al. (Unpublished Results)
MTB1254[3524-1]_OA_10min_04Oleic acid-0.267.240.41Yang Liu, et al. (Unpublished Results)
MTB1254[3524-1]_PA_12h_03Palmitic acid0.148.500.09Yang Liu, et al. (Unpublished Results)
MTB1254[3524-1]_PA_12h_04Palmitic acid0.158.120.03Yang Liu, et al. (Unpublished Results)
MTB1254[3524-1]_PA_12h_05Palmitic acid0.528.590.37Yang Liu, et al. (Unpublished Results)
MTB1254[3524-1]_PA_12h_06Palmitic acid0.298.540.09Yang Liu, et al. (Unpublished Results)
MTB1254[3524-1]_OA_10min_01Oleic acid0.218.450.18Yang Liu, et al. (Unpublished Results)
MTB1254[3524-1]_OA_10min_02Oleic acid0.057.970.09Yang Liu, et al. (Unpublished Results)
MTB1254[3524-1]_PA_12h_01Palmitic acid-0.248.290.36Yang Liu, et al. (Unpublished Results)
MTB1254[3524-1]T0_WtT0_02Control0.016.790.01Yang Liu, et al. (Unpublished Results)
MTB1254[3524-1]T0_WtT0_01Control0.097.560.13Yang Liu, et al. (Unpublished Results)
MTB1254[3524-1]_PA_12h_02Palmitic acid0.337.590.21Yang Liu, et al. (Unpublished Results)
PA_50uM_10min_07Palmitic acid0.068.310.09Yang Liu, et al. (Unpublished Results)
Rv_Rv3524-1_OA_10minOleic acid0.287.370.57Yang Liu, et al. (Unpublished Results)
Rv3524-1_OA_10minOleic acid0.148.150.15Yang Liu, et al. (Unpublished Results)
CA_50uM_10min_01Ceramide0.088.540.28Yang Liu, et al. (Unpublished Results)
AA_30uM_4h_08Arachidonic acid0.178.330.32Yang Liu, et al. (Unpublished Results)
L2A_30uM_4h_08Linoleic acid0.098.570.15Yang Liu, et al. (Unpublished Results)
OA_50uM_4h_08Oleic acid0.518.640.61Yang Liu, et al. (Unpublished Results)
OA_50uM_4h_09Oleic acid0.539.100.66Yang Liu, et al. (Unpublished Results)
PA_50uM_24h_09Palmitic acid-0.159.260.33Yang Liu, et al. (Unpublished Results)
PA_50uM_24h_10Palmitic acid-0.257.910.40Yang Liu, et al. (Unpublished Results)
L2A_30uM_4h_04Linoleic acid0.118.950.17Yang Liu, et al. (Unpublished Results)
L2A_30uM_4h_06Linoleic acid0.238.940.44Yang Liu, et al. (Unpublished Results)
MTB1254[3219-1]_01MOA0.098.770.12Yang Liu, et al. (Unpublished Results)
MTB1254[3219-2]_01MOA0.188.930.35Yang Liu, et al. (Unpublished Results)
MTB1254[3219-3]_01MOA0.129.370.20Yang Liu, et al. (Unpublished Results)
Rv[3524-1]_01Oleic acid-0.018.810.09Yang Liu, et al. (Unpublished Results)
Rv[3524-2]_01Oleic acid0.438.380.43Yang Liu, et al. (Unpublished Results)
PA_50uM_30 min_05Palmitic acid0.287.640.21Yang Liu, et al. (Unpublished Results)
PA_50uM_1h_08Palmitic acid0.377.770.17Yang Liu, et al. (Unpublished Results)
MTB1254[0485-14]_01Oleic acid-0.018.230.16Yang Liu, et al. (Unpublished Results)
Acetate-3mM-2h-04Acetate0.437.880.81Yang Liu, et al. (Unpublished Results)
Acetate-3mM-2h-05Acetate0.447.830.81Yang Liu, et al. (Unpublished Results)
Acetate-3mM-2h-06Acetate0.137.220.25Yang Liu, et al. (Unpublished Results)
Rv(pMV0481-1)Mutant vs mutant-0.087.670.28Yang Liu, et al. (Unpublished Results)
Rv(pMV0481-2)Mutant vs mutant0.198.430.43Yang Liu, et al. (Unpublished Results)
Tet_20uM_30M_01Tetracycline-0.437.480.57Yang Liu, et al. (Unpublished Results)
Tet_100uM_30M_01Tetracycline-0.537.280.58Yang Liu, et al. (Unpublished Results)
Spe_100uM_30M_01Spe0.018.520.04Yang Liu, et al. (Unpublished Results)
Rv(pMV261Km)_300uM PA_10mPalmitic acid0.238.860.43Yang Liu, et al. (Unpublished Results)
Rv(p0485-1)_300uM PA_10mPalmitic acid0.098.390.10Yang Liu, et al. (Unpublished Results)
Rv(p0485-2)_300uM PA_4hPalmitic acid0.329.770.71Yang Liu, et al. (Unpublished Results)
Rv(p0485-1)Mutant vs mutant0.269.610.51Yang Liu, et al. (Unpublished Results)
Rv(p0485-1)_OKMutant vs mutant0.269.610.51Yang Liu, et al. (Unpublished Results)
H37Rv wild type vs. H37Rv whiB7 null rep 4Wild type vs Mutant-0.246.010.82Morris RP, et al. (2005)
H37Rv wild type vs. H37Rv whiB7 null rep 5Wild type vs Mutant-0.275.260.95Morris RP, et al. (2005)
H37Rv wild type vs. H37Rv whiB7 null rep 6Wild type vs Mutant-0.403.510.87Morris RP, et al. (2005)
H37Rv wild type vs. H37Rv whiB7 null rep 1Wild type vs Mutant0.015.290.06Morris RP, et al. (2005)
H37Rv wild type vs. H37Rv whiB7 null rep 2Wild type vs Mutant-0.205.040.71Morris RP, et al. (2005)
H37Rv wild type vs. H37Rv whiB7 null rep 3Wild type vs Mutant-0.304.970.89Morris RP, et al. (2005)
H37Rv wild type vs. H37Rv whiB7 null with whiB7 over expression rep 1Wild type vs complemented null mutant0.426.580.59Morris RP, et al. (2005)
H37Rv wild type vs. H37Rv whiB7 null with whiB7 over expression rep 2Wild type vs complemented null mutant0.206.480.39Morris RP, et al. (2005)
H37Rv wild type vs. H37Rv whiB7 null with whiB7 over expression rep 3Wild type vs complemented null mutant0.316.630.48Morris RP, et al. (2005)
H37Rv wild type vs. H37Rv whiB7 null with whiB7 over expression rep 4Wild type vs complemented null mutant0.335.720.55Morris RP, et al. (2005)
H37Rv wild type vs. H37Rv whiB7 null with whiB7 over expression rep 5Wild type vs complemented null mutant0.116.830.14Morris RP, et al. (2005)
H37Rv wild type vs. H37Rv whiB7 null with whiB7 over expression rep 6Wild type vs complemented null mutant0.294.800.58Morris RP, et al. (2005)
H37Rv whiB7 null vs. H37Rv whiB7 null with whiB7 over expression rep 1Null mutant vs complemented null mutant0.516.210.73Morris RP, et al. (2005)
H37Rv whiB7 null vs. H37Rv whiB7 null with whiB7 over expression rep 2Null mutant vs complemented null mutant0.286.510.46Morris RP, et al. (2005)
H37Rv whiB7 null vs. H37Rv whiB7 null with whiB7 over expression rep 3Null mutant vs complemented null mutant0.305.280.55Morris RP, et al. (2005)
H37Rv whiB7 null vs. H37Rv whiB7 null with whiB7 over expression rep 4Null mutant vs complemented null mutant0.274.390.50Morris RP, et al. (2005)
H37Rv whiB7 null vs. H37Rv whiB7 null with whiB7 over expression rep 5Null mutant vs complemented null mutant0.466.600.67Morris RP, et al. (2005)
TBD040Oleic acid-0.178.070.35Yang Liu, et al. (Unpublished Results)
TBD043Oleic acid0.138.390.18Yang Liu, et al. (Unpublished Results)
TBD041Oleic acid0.268.220.45Yang Liu, et al. (Unpublished Results)
TBD042Wild type vs Mutant0.429.610.32Yang Liu, et al. (Unpublished Results)
TBD045Wild type vs Mutant0.159.370.12Yang Liu, et al. (Unpublished Results)
TBD044Wild type vs Mutant-0.149.510.37Yang Liu, et al. (Unpublished Results)
MTB1254_INH_20MINIsoniazid0.098.320.31Yang Liu, et al. (Unpublished Results)
MTB1254(3524-1)_INH_20MINIsoniazid0.018.440.02Yang Liu, et al. (Unpublished Results)
MTB1254(3524-2)_INH_20MINIsoniazid0.158.050.52Yang Liu, et al. (Unpublished Results)
TBD097Mutant vs mutant0.138.480.22Yang Liu, et al. (Unpublished Results)
TBD098Defined medium + Oleic acid-1.127.791.10Yang Liu, et al. (Unpublished Results)
TBD099Defined medium + Oleic acid0.218.180.17Yang Liu, et al. (Unpublished Results)
TBD091Defined medium + Oleic acid-0.109.560.33Yang Liu, et al. (Unpublished Results)
TBD092Defined medium + Oleic acid-0.149.530.31Yang Liu, et al. (Unpublished Results)
TBD094Oleic acid0.1310.170.33Yang Liu, et al. (Unpublished Results)
Tet_5ug_30M_01Tetracycline0.2610.320.55Yang Liu, et al. (Unpublished Results)
Tet_500ng_30M_01Tetracycline0.1910.530.65Yang Liu, et al. (Unpublished Results)
Tet_50ng_30M_01Tetracycline0.419.520.99Yang Liu, et al. (Unpublished Results)
MTB1254[0485-1]_ETYA_10m_01Glucose-0.078.470.21Yang Liu, et al. (Unpublished Results)
MTB1254[0485-1]_PA_30m_01Palmitic acid0.039.300.19Yang Liu, et al. (Unpublished Results)
MTB1254vsMTB1254(0485-1)Wild type vs Mutant0.028.630.04Yang Liu, et al. (Unpublished Results)
MTB1254[0485-1]_OA_10m_01Oleic acid0.368.810.21Yang Liu, et al. (Unpublished Results)
SDS_60min_01Defined medium + SDS0.0710.780.21Yang Liu, et al. (Unpublished Results)
MTB1254(B4-1)_PA_30MIN_01Defined medium + Palmitic acid0.1610.620.03Yang Liu, et al. (Unpublished Results)
MTB1254vsMTB1254B4Wild type vs Mutant-0.0710.100.30Yang Liu, et al. (Unpublished Results)
MTB1254vsMTB1254(0494-4)Wild type vs Mutant0.349.570.71Yang Liu, et al. (Unpublished Results)
MTB1254(B4-1)_OA_30MIN_01Oleic acid0.309.870.16Yang Liu, et al. (Unpublished Results)
MTB1254(0494-4)_OA_30MIN_01Oleic acid0.309.600.12Yang Liu, et al. (Unpublished Results)
MTB1254(0465-4)_SDS_60MIN_01SDS0.7710.010.45Yang Liu, et al. (Unpublished Results)
MTB1254[0485-1]_Act_2h_01Act0.329.770.46Yang Liu, et al. (Unpublished Results)
MTB1254[0485-1]_AA_10m_01Arachidonic acid0.079.940.07Yang Liu, et al. (Unpublished Results)
MTB1254[0485-1]_LA_10m_01Linoleic acid0.219.520.02Yang Liu, et al. (Unpublished Results)
MTB1254[0485-1]_PA_10m_01Palmitic acid0.339.460.15Yang Liu, et al. (Unpublished Results)
SDS_3h_01SDS0.0210.000.25Yang Liu, et al. (Unpublished Results)
MTB1254(B4-1)_OA_30MIN_02Oleic acid0.238.890.04Yang Liu, et al. (Unpublished Results)
MTB1254(B4-1)_PA_30MIN_02Palmitic acid0.288.020.17Yang Liu, et al. (Unpublished Results)
7H9MTB1254_SDS_90MIN_01SDS-0.128.890.37Yang Liu, et al. (Unpublished Results)
7H9MTB1254(0465-4)_SDS_90MIN_01SDS0.058.340.19Yang Liu, et al. (Unpublished Results)
MTB1254(B4-1)_OA_30MIN_03Oleic acid0.338.420.20Yang Liu, et al. (Unpublished Results)
MTB1254(B4-1)_OA_30MIN_04Oleic acid0.579.370.39Yang Liu, et al. (Unpublished Results)
MTB1254(B4-1)_PA_30MIN_03Palmitic acid0.298.810.09Yang Liu, et al. (Unpublished Results)
MTB1254(B4-1)_PA_30MIN_04Palmitic acid0.408.880.19Yang Liu, et al. (Unpublished Results)
MTB1254(B4-1)_OA_10MIN_01Oleic acid0.328.470.23Yang Liu, et al. (Unpublished Results)
MTB1254(B4-1)_PA_10MIN_01Palmitic acid0.438.910.31Yang Liu, et al. (Unpublished Results)
MTB1254(B4-1)_PA_10MIN_02Palmitic acid0.418.830.29Yang Liu, et al. (Unpublished Results)
MTB1254(B4-1)_OA_10MIN_02Oleic acid0.968.640.84Yang Liu, et al. (Unpublished Results)
MTB1254[0485-1]_PA_10m_02Palmitic acid-0.018.140.20Yang Liu, et al. (Unpublished Results)
MTB1254[0485-1]_OA_10m_02Oleic acid0.408.900.20Yang Liu, et al. (Unpublished Results)
MTB1254[0485-1]_PA_30m_02Palmitic acid0.258.730.02Yang Liu, et al. (Unpublished Results)
MTB1254[0485-1]_PA_30m_03Palmitic acid0.558.040.34Yang Liu, et al. (Unpublished Results)
MTB1254[0485-1]_PA_30m_04Palmitic acid0.787.980.51Yang Liu, et al. (Unpublished Results)
MTB1254[0485-1]_PA_10m_03Palmitic acid0.297.720.18Yang Liu, et al. (Unpublished Results)
MTB1254[0485-1]_PA_10m_04Palmitic acid0.437.630.37Yang Liu, et al. (Unpublished Results)
MTB1254[0485-1]_OA_10m_03Oleic acid0.077.090.10Yang Liu, et al. (Unpublished Results)
MTB1254[0485-1]_OA_10m_04Oleic acid0.056.990.02Yang Liu, et al. (Unpublished Results)
MTB1254[0485-1]_OA_30m_01Oleic acid0.598.260.33Yang Liu, et al. (Unpublished Results)
MTB1254[0485-1]_OA_30m_02Oleic acid0.527.360.32Yang Liu, et al. (Unpublished Results)
WT_65-4_SDS_01SDS-0.029.140.00Yang Liu, et al. (Unpublished Results)
WT_65-4_SDS_02SDS0.108.830.23Yang Liu, et al. (Unpublished Results)
MTB1254[0485-1]_PA_4h_01Palmitic acid0.688.130.40Yang Liu, et al. (Unpublished Results)
MTB1254[0485-1]_PA_4h_02Palmitic acid0.507.870.30Yang Liu, et al. (Unpublished Results)
MTB1254[0485-1]_PA_12h_01Palmitic acid0.287.550.14Yang Liu, et al. (Unpublished Results)
MTB1254[0485-1]_PA_12h_02Palmitic acid0.468.160.29Yang Liu, et al. (Unpublished Results)
MTB1254[0485-1]_PA_4h_03Palmitic acid0.187.870.04Yang Liu, et al. (Unpublished Results)
MTB1254[0485-1]_PA_4h_04Palmitic acid0.717.860.55Yang Liu, et al. (Unpublished Results)
MTB1254[0485-1]_PA_12h_04Palmitic acid0.387.830.18Yang Liu, et al. (Unpublished Results)
MTB1254[0485-1]_PA_12h_03Palmitic acid0.217.430.01Yang Liu, et al. (Unpublished Results)
WT_85-1_OA_10min_01Oleic acid0.268.850.71Yang Liu, et al. (Unpublished Results)
WT_85-1_OA_10min_02Oleic acid0.518.461.29Yang Liu, et al. (Unpublished Results)
WT_85-1_PA_10min_01Palmitic acid0.209.420.40Yang Liu, et al. (Unpublished Results)
WT_85-1_PA_10min_02Palmitic acid-0.018.190.02Yang Liu, et al. (Unpublished Results)
WT_WhiB4_OA_10min_01Oleic acid0.187.600.33Yang Liu, et al. (Unpublished Results)
WT_WhiB4_PA_10min_01Palmitic acid0.709.581.18Yang Liu, et al. (Unpublished Results)
Rv-MT90_100603_01Strain comparison-0.158.560.28Yang Liu, et al. (Unpublished Results)
Rv-MT96_100603_01Strain comparison-0.297.740.60Yang Liu, et al. (Unpublished Results)
Rv-MT106_100603_01Strain comparison-0.247.940.52Yang Liu, et al. (Unpublished Results)
Rv-MT71_100503_01Strain comparison0.048.240.06Yang Liu, et al. (Unpublished Results)
Rv-MT90_100503_01Strain comparison0.018.010.04Yang Liu, et al. (Unpublished Results)
Rv-MT96_100503_01Strain comparison0.048.260.12Yang Liu, et al. (Unpublished Results)
Rv-MT106_100503_01Strain comparison-0.058.500.14Yang Liu, et al. (Unpublished Results)
Rv-MT71_100603_01Strain comparison0.048.010.11Yang Liu, et al. (Unpublished Results)
Rv-MT71_100703_01Strain comparison0.097.830.14Yang Liu, et al. (Unpublished Results)
Rv-MT90_100703_01Strain comparison0.237.150.25Yang Liu, et al. (Unpublished Results)
Rv-MT96_100703_01Strain comparison0.167.260.22Yang Liu, et al. (Unpublished Results)
Rv-MT71_100803_01Strain comparison0.377.640.39Yang Liu, et al. (Unpublished Results)
Rv-MT90_100803_01Strain comparison0.256.910.21Yang Liu, et al. (Unpublished Results)
Rv-MT90_100903_01Strain comparison0.337.080.13Yang Liu, et al. (Unpublished Results)
Rv-MT71_100503_02Strain comparison-0.059.520.20Yang Liu, et al. (Unpublished Results)
Rv-MT90_100503_02Strain comparison0.049.060.01Yang Liu, et al. (Unpublished Results)
Rv-MT96_100503_02Strain comparison-0.128.990.32Yang Liu, et al. (Unpublished Results)
Rv-MT106_100503_02Strain comparison-0.168.940.46Yang Liu, et al. (Unpublished Results)
TBD622Wild type vs overexpression-0.228.780.30Yang Liu, et al. (Unpublished Results)
TBD625Null mutant vs complemented null mutant0.147.170.03Yang Liu, et al. (Unpublished Results)
WM_T0_01Wild type vs Mutant-0.309.260.50Yang Liu, et al. (Unpublished Results)
WM_1254[whiB4]_10d_01Growth curve0.089.330.02Yang Liu, et al. (Unpublished Results)
WM_1254_10d_01Growth curve0.049.410.02Yang Liu, et al. (Unpublished Results)
WM_1254_10d_02Growth curve-0.019.080.02Yang Liu, et al. (Unpublished Results)
WM_1254[whiB4]_10d_02Growth curve0.229.310.25Yang Liu, et al. (Unpublished Results)
WM_1254[whiB4]_10d_03Growth curve0.349.390.32Yang Liu, et al. (Unpublished Results)
PA_50uM+OA_10uM_2h_01Palmitic acid + Oleic acid0.118.980.14Yang Liu, et al. (Unpublished Results)
PA_50uM+OA_30uM_2h_01Palmitic acid + Oleic acid-0.319.340.38Yang Liu, et al. (Unpublished Results)
PA_50uM+OA_30uM_4h_02Palmitic acid + Oleic acid0.309.800.40Yang Liu, et al. (Unpublished Results)
PA_50uM+OA_10uM_2h_02Palmitic acid + Oleic acid-0.019.820.10Yang Liu, et al. (Unpublished Results)
PA_50uM+OA_30uM_2h_02Palmitic acid + Oleic acid0.068.940.03Yang Liu, et al. (Unpublished Results)
PA_50uM+OA_10uM_4h_01Palmitic acid + Oleic acid0.418.040.75Yang Liu, et al. (Unpublished Results)
PA_50uM+OA_10uM_4h_02Palmitic acid + Oleic acid0.298.550.45Yang Liu, et al. (Unpublished Results)
PA_50uM+OA_10uM_24h_01Palmitic acid + Oleic acid-0.238.880.69Yang Liu, et al. (Unpublished Results)
PA_50uM+OA_10uM_24h_02Palmitic acid + Oleic acid-0.148.970.41Yang Liu, et al. (Unpublished Results)
PA_50uM+OA_30uM_24h_01Palmitic acid + Oleic acid0.128.800.38Yang Liu, et al. (Unpublished Results)
PA_50uM+OA_30uM_24h_02Palmitic acid + Oleic acid-0.048.510.14Yang Liu, et al. (Unpublished Results)
PA_50uM+AA_30uM_30min_01Palmitic acid + Arachidonic acid0.258.600.11Yang Liu, et al. (Unpublished Results)
PA_50uM+AA_30uM_2h_01Palmitic acid + Arachidonic acid0.079.190.00Yang Liu, et al. (Unpublished Results)
PA_50uM+AA_30uM_2h_02Palmitic acid + Arachidonic acid-0.208.440.29Yang Liu, et al. (Unpublished Results)
WM_1254_14d_01Growth curve-0.267.680.30Yang Liu, et al. (Unpublished Results)
WM_1254_14d_02Growth curve-0.118.790.13Yang Liu, et al. (Unpublished Results)
WM_1254[whiB4]_14d_01Growth curve0.338.880.28Yang Liu, et al. (Unpublished Results)
WM_1254[whiB4]_14d_02Growth curve0.668.150.80Yang Liu, et al. (Unpublished Results)
MTB1254_SDS_90MIN_01SDS-0.249.400.44Yang Liu, et al. (Unpublished Results)
MTB1254whiB4_SDS_90MIN_01SDS0.149.410.14Yang Liu, et al. (Unpublished Results)
MTB1254/whiB4_SDS_90MIN_01SDS0.408.280.64Yang Liu, et al. (Unpublished Results)
PA_50uM+AA_30uM_30min_02Palmitic acid + Arachidonic acid0.289.060.10Yang Liu, et al. (Unpublished Results)
MT1254/whiB4_CK_01Wild type vs Mutant-0.088.830.14Yang Liu, et al. (Unpublished Results)
PA_50uM+OA_30uM_30min_01Palmitic acid + Oleic acid0.128.850.01Yang Liu, et al. (Unpublished Results)
PA_50uM+OA_30uM_30min_03Palmitic acid + Oleic acid0.238.790.03Yang Liu, et al. (Unpublished Results)
PA_50uM+OA_30uM_30min_04Palmitic acid + Oleic acid0.359.010.18Yang Liu, et al. (Unpublished Results)
PA_50uM+OA_30uM_30min_02Palmitic acid + Oleic acid-0.119.110.35Yang Liu, et al. (Unpublished Results)
PA_50uM+OA_10uM_2h_03Palmitic acid + Oleic acid0.249.710.13Yang Liu, et al. (Unpublished Results)
PA_50uM+OA_10uM_12h_02Palmitic acid + Oleic acid-0.139.790.43Yang Liu, et al. (Unpublished Results)
PA_50uM+OA_10uM_12h_01Palmitic acid + Oleic acid-0.019.560.07Yang Liu, et al. (Unpublished Results)
MTB1254_SDS_90MIN_02SDS-0.428.630.62Yang Liu, et al. (Unpublished Results)
MTB1254whiB4_SDS_90MIN_02SDS0.359.390.04Yang Liu, et al. (Unpublished Results)
PA_50uM+OA_30uM_2h_04Palmitic acid + Oleic acid-0.338.710.58Yang Liu, et al. (Unpublished Results)
PA_50uM+OA_30uM_2h_03Palmitic acid + Oleic acid-0.319.620.56Yang Liu, et al. (Unpublished Results)
PA_50uM+OA_10uM_4h_03Palmitic acid + Oleic acid0.399.440.54Yang Liu, et al. (Unpublished Results)
PA_50uM+OA_10uM_4h_04Palmitic acid + Oleic acid0.389.310.54Yang Liu, et al. (Unpublished Results)
PA_50uM+OA_30uM_4h_04Palmitic acid + Oleic acid1.039.030.91Yang Liu, et al. (Unpublished Results)
PA_50uM+OA_30uM_4h_03Palmitic acid + Oleic acid1.059.380.95Yang Liu, et al. (Unpublished Results)
MTB1254_SDS_90MIN_03SDS-0.309.320.45Yang Liu, et al. (Unpublished Results)
MTB1254_SDS_90MIN_04SDS-0.459.180.59Yang Liu, et al. (Unpublished Results)
MTB1254whiB4_SDS_90MIN_04SDS0.609.040.32Yang Liu, et al. (Unpublished Results)
MTB1254whiB4_SDS_90MIN_03SDS0.529.090.09Yang Liu, et al. (Unpublished Results)
PA_50uM+AA_30uM_2h_03Palmitic acid + Arachidonic acid0.408.020.69Yang Liu, et al. (Unpublished Results)
PA_50uM+AA_30uM_2h_04Palmitic acid + Arachidonic acid0.247.790.49Yang Liu, et al. (Unpublished Results)
PA_50uM+OA_30uM_4h_05Palmitic acid + Oleic acid0.278.460.48Yang Liu, et al. (Unpublished Results)
PA_50uM+OA_10uM_2h_04Palmitic acid + Oleic acid0.188.540.19Yang Liu, et al. (Unpublished Results)
PA_50uM+AA_30uM_30min_03Palmitic acid + Arachidonic acid-0.099.620.21Yang Liu, et al. (Unpublished Results)
PA_50uM+OA_10uM_30min_01Palmitic acid + Oleic acid-0.409.750.47Yang Liu, et al. (Unpublished Results)
PA_50uM+OA_10uM_30min_02Palmitic acid + Oleic acid-0.399.120.51Yang Liu, et al. (Unpublished Results)
PA_50uM+OA_10uM_30min_03Palmitic acid + Oleic acid0.199.420.04Yang Liu, et al. (Unpublished Results)
PA_50uM+OA_10uM_30min_04Palmitic acid + Oleic acid0.279.180.09Yang Liu, et al. (Unpublished Results)
WM_1254_20d_01Growth curve0.669.320.34Yang Liu, et al. (Unpublished Results)
WM_1254[whiB4]_20d_01Growth curve0.329.060.10Yang Liu, et al. (Unpublished Results)
PA_50uM+AA_30uM_30min_04Palmitic acid + Arachidonic acid-0.199.390.34Yang Liu, et al. (Unpublished Results)
WM_1254_vs_1254whiB4_20dayGrowth curve0.8010.511.88Yang Liu, et al. (Unpublished Results)
MTB1254[Rv0465c-4]_PA50+OA30_30m_01Palmitic acid + Oleic acid0.129.250.08Yang Liu, et al. (Unpublished Results)
Test_361-1Control-0.148.500.41Yang Liu, et al. (Unpublished Results)
Test_361-2Control0.118.930.17Yang Liu, et al. (Unpublished Results)
Test_361-3Control-0.147.660.34Yang Liu, et al. (Unpublished Results)
TBD425Defined medium + BSA-0.099.470.22Yang Liu, et al. (Unpublished Results)
TBD1111Defined medium + BSA0.228.530.47Yang Liu, et al. (Unpublished Results)
TBD1116Palmitic acid + Oleic acid0.288.300.34Yang Liu, et al. (Unpublished Results)
TBD1115Palmitic acid + Oleic acid0.299.340.09Yang Liu, et al. (Unpublished Results)
TBD1113Palmitic acid + BSA0.819.270.91Yang Liu, et al. (Unpublished Results)
TBD1114Palmitic acid + BSA0.169.070.12Yang Liu, et al. (Unpublished Results)
MAPP_5uM_30m_01MAPP0.109.050.25Yang Liu, et al. (Unpublished Results)
MAPP_5uM_4h_01MAPP-0.059.530.16Yang Liu, et al. (Unpublished Results)
OA_50uM+0.5%BSA_1h_01Oleic acid0.329.740.42Yang Liu, et al. (Unpublished Results)
OA_50uM+0.5%BSA_4h_01Oleic acid0.297.910.59Yang Liu, et al. (Unpublished Results)
PA_50uM+0.5%BSA_4h_01Palmitic acid + BSA0.419.390.64Yang Liu, et al. (Unpublished Results)
PA_50uM+0.5%BSA_1h_01Palmitic acid + BSA0.278.460.34Yang Liu, et al. (Unpublished Results)
TBD1266Wild type vs Mutant-0.048.640.00Yang Liu, et al. (Unpublished Results)
TBD1267Wild type vs Mutant0.148.040.38Yang Liu, et al. (Unpublished Results)
TBD1268Wild type vs Mutant-0.219.030.39Yang Liu, et al. (Unpublished Results)
TBD426Wild type vs Mutant-0.189.330.32Yang Liu, et al. (Unpublished Results)
PA_50uM+MAPP_30m_01Palmitic acid + MAPP0.239.140.05Yang Liu, et al. (Unpublished Results)
PA_50uM+MAPP_4h_01Palmitic acid + MAPP0.218.700.03Yang Liu, et al. (Unpublished Results)
TBD1275Wild type vs Mutant0.277.800.63Yang Liu, et al. (Unpublished Results)
TBD1276Wild type vs Mutant0.298.110.68Yang Liu, et al. (Unpublished Results)
TBD1277Wild type vs Mutant0.069.060.10Yang Liu, et al. (Unpublished Results)
MTB1254[Rv3524-2]_PA50+OA30_30m_01Palmitic acid + Oleic acid-0.458.510.66Yang Liu, et al. (Unpublished Results)
MTB1254[Rv3524-2]_PA50+OA30_30m_02Palmitic acid + Oleic acid0.188.820.01Yang Liu, et al. (Unpublished Results)
MTB1254[Rv3524-2]_PA50+OA30_2h_02Palmitic acid + Oleic acid-0.179.230.25Yang Liu, et al. (Unpublished Results)
MTB1254[Rv3524-2]_PA50+OA30_2h_01Palmitic acid + Oleic acid-0.119.330.24Yang Liu, et al. (Unpublished Results)
MTB1254[Rv3524-2-compl]_PA50+OA30_30m_02Palmitic acid + Oleic acid0.079.370.10Yang Liu, et al. (Unpublished Results)
MTB1254[Rv3524-2-compl]_PA50+OA30_2h_02Palmitic acid + Oleic acid-0.248.610.41Yang Liu, et al. (Unpublished Results)
TBE055Wild type vs Mutant0.038.520.03Yang Liu, et al. (Unpublished Results)
TBE056Wild type vs Mutant0.289.310.63Yang Liu, et al. (Unpublished Results)
TBE057Wild type vs Mutant0.077.960.08Yang Liu, et al. (Unpublished Results)
TBD1137Wild type vs Mutant-0.178.960.28Yang Liu, et al. (Unpublished Results)
TBE058Wild type vs Mutant-0.029.140.04Yang Liu, et al. (Unpublished Results)
TBE059Wild type vs Mutant-0.058.040.08Yang Liu, et al. (Unpublished Results)
TBE060Wild type vs Mutant-0.159.260.26Yang Liu, et al. (Unpublished Results)
MTB889_PA50_1h_01Palmitic acid0.058.780.11Yang Liu, et al. (Unpublished Results)
MTB889_PA50_1h_02Palmitic acid-0.199.290.31Yang Liu, et al. (Unpublished Results)
MTB1370_PA50_1h_02Palmitic acid0.008.990.17Yang Liu, et al. (Unpublished Results)
MTB1370_PA50_1h_01Palmitic acid0.038.170.01Yang Liu, et al. (Unpublished Results)
Test_261B4-1Control-0.017.520.05Yang Liu, et al. (Unpublished Results)
Test_ceramide_5uMCeramide0.169.930.61Yang Liu, et al. (Unpublished Results)
MTB889_PA50_1h_03Palmitic acid-0.348.470.38Yang Liu, et al. (Unpublished Results)
MTB1370_PA50_1h_03Palmitic acid0.099.810.09Yang Liu, et al. (Unpublished Results)
MTB1370_PA50_1h_04Palmitic acid0.169.140.04Yang Liu, et al. (Unpublished Results)
Starvation_T0Starvation-0.698.520.81Yang Liu, et al. (Unpublished Results)
Starvation_1254_6h_01Starvation-0.388.180.32Yang Liu, et al. (Unpublished Results)
Starvation_1254_12h_01Starvation-0.068.470.09Yang Liu, et al. (Unpublished Results)
Starvation_1254_24h_01Starvation0.028.660.04Yang Liu, et al. (Unpublished Results)
Starvation_1254_OA50_24h_01Starvation-0.248.710.27Yang Liu, et al. (Unpublished Results)
Starvation_1254_OA50_12h_01Starvation-0.589.110.47Yang Liu, et al. (Unpublished Results)
Starvation_1254_OA50_6h_01Starvation-1.258.130.98Yang Liu, et al. (Unpublished Results)
Starvation_1254_6h_02Starvation0.209.200.07Yang Liu, et al. (Unpublished Results)
Starvation_1254_12h_02Starvation-0.258.490.11Yang Liu, et al. (Unpublished Results)
Starvation_1254_24h_02Starvation-0.269.610.28Yang Liu, et al. (Unpublished Results)
Starvation_1254_OA50_24h_02Starvation-1.239.691.33Yang Liu, et al. (Unpublished Results)
Starvation_1254_OA50_6h_02Starvation-0.589.280.57Yang Liu, et al. (Unpublished Results)
Starvation_1254_OA50_12h_02Starvation-0.258.470.33Yang Liu, et al. (Unpublished Results)
Starvation_1254_6h_03Starvation-0.608.780.46Yang Liu, et al. (Unpublished Results)
Starvation_1254_6h_04Starvation0.209.780.04Yang Liu, et al. (Unpublished Results)
Starvation_1254_12h_04Starvation-0.297.970.27Yang Liu, et al. (Unpublished Results)
Starvation_1254_12h_03Starvation-0.348.850.28Yang Liu, et al. (Unpublished Results)
Starvation_1254_24h_03Starvation0.078.980.03Yang Liu, et al. (Unpublished Results)
Starvation_1254_24h_04Starvation-0.208.520.24Yang Liu, et al. (Unpublished Results)
Starvation_1254_OA50_6h_03Starvation-0.688.450.61Yang Liu, et al. (Unpublished Results)
Starvation_1254_OA50_6h_04Starvation-0.438.470.44Yang Liu, et al. (Unpublished Results)
Starvation_1254_OA50_12h_04Starvation-0.439.050.37Yang Liu, et al. (Unpublished Results)
Starvation_1254_OA50_12h_03Starvation-0.408.690.38Yang Liu, et al. (Unpublished Results)
Starvation_1254_OA50_24h_03Starvation-0.268.650.31Yang Liu, et al. (Unpublished Results)
Starvation_1254_OA50_24h_04Starvation-0.409.470.43Yang Liu, et al. (Unpublished Results)
Starvation_OA50_24h_01Starvation-0.828.110.91Yang Liu, et al. (Unpublished Results)
Starvation_OA50_6h_01Starvation0.008.590.13Yang Liu, et al. (Unpublished Results)
Starvation_OA50_6h_02Starvation-0.349.800.58Yang Liu, et al. (Unpublished Results)
MTB1248_PA50_1h_01Palmitic acid0.268.440.07Yang Liu, et al. (Unpublished Results)
MTB1248_PA50_1h_02Palmitic acid0.438.030.33Yang Liu, et al. (Unpublished Results)
MTB6548_PA50_1h_02Palmitic acid0.137.150.07Yang Liu, et al. (Unpublished Results)
MTB6548_PA50_1h_01Palmitic acid0.097.930.03Yang Liu, et al. (Unpublished Results)
TBD816Wild type vs Mutant0.229.220.32Yang Liu, et al. (Unpublished Results)
TBD817Wild type vs Mutant-0.038.980.17Yang Liu, et al. (Unpublished Results)
TBD818Wild type vs Mutant0.218.820.36Yang Liu, et al. (Unpublished Results)
TBD819Wild type vs Mutant-0.178.700.62Yang Liu, et al. (Unpublished Results)
Starvation_1254_PA50_6h_01Starvation0.478.810.23Yang Liu, et al. (Unpublished Results)
Starvation_1254_PA50+OA30_6h_01Starvation0.348.560.23Yang Liu, et al. (Unpublished Results)
Starvation_1254_PA50_24h_01Starvation-0.278.960.38Yang Liu, et al. (Unpublished Results)
Starvation_OA50_24h_02Starvation-0.378.230.49Yang Liu, et al. (Unpublished Results)
Starvation_OA50_24h_03Starvation-0.747.910.97Yang Liu, et al. (Unpublished Results)
Starvation_OA50_24h_04Starvation0.427.560.38Yang Liu, et al. (Unpublished Results)
Starvation_OA50_6h_04Starvation-0.727.941.00Yang Liu, et al. (Unpublished Results)
Starvation_OA50_6h_03Starvation-0.237.430.50Yang Liu, et al. (Unpublished Results)
Starvation_1254_6h_06Starvation-0.677.960.55Yang Liu, et al. (Unpublished Results)
Starvation_1254_24h_05Starvation-0.289.340.29Yang Liu, et al. (Unpublished Results)
Starvation_1254_24h_06Starvation0.108.340.05Yang Liu, et al. (Unpublished Results)
Starvation_1254_PA50_6h_02Starvation-0.048.940.12Yang Liu, et al. (Unpublished Results)
Starvation_1254_PA50+OA30_6h_02Starvation0.676.560.71Yang Liu, et al. (Unpublished Results)
Starvation_1254_PA50+OA30_24h_01Starvation-0.257.580.30Yang Liu, et al. (Unpublished Results)
Starvation_1254_PA50_24h_02Starvation0.858.180.63Yang Liu, et al. (Unpublished Results)
Starvation_1254_6h_05Starvation-0.368.450.32Yang Liu, et al. (Unpublished Results)
Starvation_1254_PA50+OA30_24h_02Starvation-0.648.220.66Yang Liu, et al. (Unpublished Results)
C2_ceramide_5uM_1h_01Ceramide0.219.600.35Yang Liu, et al. (Unpublished Results)
C2_ceramide_25uM_1h_01Ceramide0.587.930.76Yang Liu, et al. (Unpublished Results)
TBD662Wild type vs Mutant-0.069.440.02Yang Liu, et al. (Unpublished Results)
TBD663Wild type vs Mutant0.079.100.17Yang Liu, et al. (Unpublished Results)
TBD664Wild type vs Mutant0.409.450.57Yang Liu, et al. (Unpublished Results)
MDA_1254-pMV261_01MDA-0.138.290.18Yang Liu, et al. (Unpublished Results)
MDA_1254-pMV261_02MDA-0.098.110.10Yang Liu, et al. (Unpublished Results)
MDA_1254-pMV261_03MDA0.137.340.41Yang Liu, et al. (Unpublished Results)
MDA_1254-pMV261_04MDA-0.019.120.11Yang Liu, et al. (Unpublished Results)
MDA_1254-pMV261-3524_01MDA-0.028.490.09Yang Liu, et al. (Unpublished Results)
MDA_1254-pMV261-3524_02MDA0.128.740.26Yang Liu, et al. (Unpublished Results)
MDA_1254-pMV261-3524_03MDA0.028.820.13Yang Liu, et al. (Unpublished Results)
MDA_1254-pMV261-3524_04MDA0.289.030.64Yang Liu, et al. (Unpublished Results)
MDG_1254-pMV261_01Wild type vs Mutant-0.227.910.34Yang Liu, et al. (Unpublished Results)
MDG_1254-pMV261_02Wild type vs Mutant-0.168.420.21Yang Liu, et al. (Unpublished Results)
MDG_1254-pMV261_03Wild type vs Mutant-0.067.330.08Yang Liu, et al. (Unpublished Results)
MDG_1254-pMV261_04Wild type vs Mutant0.228.160.42Yang Liu, et al. (Unpublished Results)
MDG_1254-pMV261-3524_01Wild type vs Mutant-0.028.080.02Yang Liu, et al. (Unpublished Results)
MDG_1254-pMV261-3524_02Wild type vs Mutant0.087.300.25Yang Liu, et al. (Unpublished Results)
MDG_1254-pMV261-3524_03Wild type vs Mutant-0.118.090.12Yang Liu, et al. (Unpublished Results)
MDG_1254-pMV261-3524_04Wild type vs Mutant-0.056.990.04Yang Liu, et al. (Unpublished Results)
Starvation_1254_6h_07Starvation0.018.540.03Yang Liu, et al. (Unpublished Results)
Starvation_1254_6h_08Starvation0.118.740.07Yang Liu, et al. (Unpublished Results)
Starvation_1254_24h_07Starvation0.208.350.19Yang Liu, et al. (Unpublished Results)
Starvation_1254_24h_08Starvation0.448.950.32Yang Liu, et al. (Unpublished Results)
Starvation_1254_PA50_6h_03Starvation0.208.310.11Yang Liu, et al. (Unpublished Results)
Starvation_1254_PA50_6h_04Starvation0.468.660.34Yang Liu, et al. (Unpublished Results)
Starvation_1254_PA50_24h_03Starvation0.246.730.24Yang Liu, et al. (Unpublished Results)
Starvation_1254_PA50_24h_04Starvation0.658.770.44Yang Liu, et al. (Unpublished Results)
Starvation_1254_PA50+OA30_6h_03Starvation-0.028.530.06Yang Liu, et al. (Unpublished Results)
Starvation_1254_PA50+OA30_6h_04Starvation-0.208.370.23Yang Liu, et al. (Unpublished Results)
Starvation_1254_PA50+OA30_24h_03Starvation-0.507.270.51Yang Liu, et al. (Unpublished Results)
Starvation_1254_PA50+OA30_24h_04Starvation0.178.310.12Yang Liu, et al. (Unpublished Results)
MTB1254(B4-1-Compl)_OA_30MIN_01Oleic acid0.268.200.23Yang Liu, et al. (Unpublished Results)
MTB1254(B4-1-Compl)_OA_30MIN_02Oleic acid0.348.180.33Yang Liu, et al. (Unpublished Results)
MTB1254(B4-1-Compl)_OA_30MIN_03Oleic acid0.248.210.29Yang Liu, et al. (Unpublished Results)
MTB1254(B4-1-Compl)_OA_30MIN_04Oleic acid0.188.380.16Yang Liu, et al. (Unpublished Results)
MTB1254(B4-1-Compl)_PA_30MIN_04Palmitic acid0.167.640.13Yang Liu, et al. (Unpublished Results)
MTB1254(B4-1-Compl)_PA_30MIN_03Palmitic acid0.288.000.20Yang Liu, et al. (Unpublished Results)
MTB1254(B4-1-Compl)_PA_30MIN_02Palmitic acid0.148.490.06Yang Liu, et al. (Unpublished Results)
MTB1254(B4-1-Compl)_PA_30MIN_01Palmitic acid0.108.200.05Yang Liu, et al. (Unpublished Results)
MTB1254(B4-1)_PA_4h_01Palmitic acid-0.137.260.26Yang Liu, et al. (Unpublished Results)
MTB1254(B4-1)_PA_4h_02Palmitic acid-0.008.510.15Yang Liu, et al. (Unpublished Results)
MTB1254(B4-1-Compl)_PA_4h_01Palmitic acid0.058.820.16Yang Liu, et al. (Unpublished Results)
MTB1254(B4-1)_PA_4h_03Palmitic acid-0.068.570.20Yang Liu, et al. (Unpublished Results)
MTB1254(B4-1)_PA_4h_04Palmitic acid-0.069.310.15Yang Liu, et al. (Unpublished Results)
MTB1254(B4-1-Compl)_PA_4h_02Palmitic acid0.057.930.01Yang Liu, et al. (Unpublished Results)
MTB1254(B4-1-Compl)_PA_4h_03Palmitic acid-0.097.960.15Yang Liu, et al. (Unpublished Results)
MTB1254(B4-1-Compl)_PA_4h_04Palmitic acid-0.148.260.30Yang Liu, et al. (Unpublished Results)
MTB1254(B4-1-Compl)_PA_4h_05Palmitic acid-0.087.460.15Yang Liu, et al. (Unpublished Results)
MTB1254(B4-1-Compl)_PA_4h_06Palmitic acid0.197.440.18Yang Liu, et al. (Unpublished Results)
TBE283Control0.047.350.03Yang Liu, et al. (Unpublished Results)
TBE285Control0.746.440.88Yang Liu, et al. (Unpublished Results)
MTB1254_Bottom_14D_01Sediment vs pellicle-0.188.040.39Yang Liu, et al. (Unpublished Results)
MTB1254_Bottom_14D_02Sediment vs pellicle-0.068.190.18Yang Liu, et al. (Unpublished Results)
MTB1254_Bottom_14D_04Sediment vs pellicle-0.107.880.25Yang Liu, et al. (Unpublished Results)
MTB1254_Bottom_14D_03Sediment vs pellicle-0.188.300.38Yang Liu, et al. (Unpublished Results)
MTB1254_Pellicle_14D_01Sediment vs pellicle-0.288.190.60Yang Liu, et al. (Unpublished Results)
MTB1254_Pellicle_14D_02Sediment vs pellicle-0.048.210.20Yang Liu, et al. (Unpublished Results)
MTB1254_Pellicle_14D_04Sediment vs pellicle0.017.040.06Yang Liu, et al. (Unpublished Results)
MTB1254_Pellicle_14D_03Sediment vs pellicle-0.257.870.57Yang Liu, et al. (Unpublished Results)
MTB1254_Pellicle_10D_01Sediment vs pellicle-0.058.110.18Yang Liu, et al. (Unpublished Results)
MTB1254_Pellicle_10D_02Sediment vs pellicle0.058.270.04Yang Liu, et al. (Unpublished Results)
MTB1254_Pellicle_10D_04Sediment vs pellicle0.567.201.13Yang Liu, et al. (Unpublished Results)
MTB1254_Pellicle_10D_03Sediment vs pellicle0.108.740.05Yang Liu, et al. (Unpublished Results)
MTB1254_Pellicle_21D_01Sediment vs pellicle-0.057.690.20Yang Liu, et al. (Unpublished Results)
MTB1254_Pellicle_21D_02Sediment vs pellicle-0.178.080.38Yang Liu, et al. (Unpublished Results)
MTB1254_Pellicle_21D_04Sediment vs pellicle-0.197.940.37Yang Liu, et al. (Unpublished Results)
MTB1254_Pellicle_21D_03Sediment vs pellicle-0.228.250.40Yang Liu, et al. (Unpublished Results)
MTB1254_Bottom_10D_01Sediment vs pellicle0.677.850.58Yang Liu, et al. (Unpublished Results)
MTB1254_Bottom_10D_02Sediment vs pellicle0.337.890.18Yang Liu, et al. (Unpublished Results)
MTB1254_Bottom_10D_03Sediment vs pellicle0.507.620.37Yang Liu, et al. (Unpublished Results)
MTB1254_Bottom_10D_04Sediment vs pellicle0.428.030.32Yang Liu, et al. (Unpublished Results)
MTB1254_Bottom_21D_01Sediment vs pellicle0.288.310.05Yang Liu, et al. (Unpublished Results)
MTB1254_Bottom_21D_02Sediment vs pellicle-0.257.950.32Yang Liu, et al. (Unpublished Results)
MTB1254_Bottom_21D_04Sediment vs pellicle0.217.680.03Yang Liu, et al. (Unpublished Results)
MTB1254_Bottom_21D_03Sediment vs pellicle0.028.030.13Yang Liu, et al. (Unpublished Results)
MTB1254_Pellicle_42D_01Sediment vs pellicle-0.078.300.17Yang Liu, et al. (Unpublished Results)
MTB1254_Pellicle_42D_02Sediment vs pellicle-0.917.670.90Yang Liu, et al. (Unpublished Results)
MTB1254_Pellicle_42D_04Sediment vs pellicle0.247.840.18Yang Liu, et al. (Unpublished Results)
MTB1254_Pellicle_42D_03Sediment vs pellicle-0.657.860.61Yang Liu, et al. (Unpublished Results)
MTB1254_Bottom_42D_01Sediment vs pellicle0.718.050.43Yang Liu, et al. (Unpublished Results)
MTB1254_Bottom_42D_02Sediment vs pellicle0.949.040.43Yang Liu, et al. (Unpublished Results)
MTB1254_Bottom_42D_03Sediment vs pellicle0.298.130.05Yang Liu, et al. (Unpublished Results)
MTB1254_Bottom_42D_04Sediment vs pellicle0.407.690.27Yang Liu, et al. (Unpublished Results)
MTB1254_Pellicle_56D_01Sediment vs pellicle-1.106.870.92Yang Liu, et al. (Unpublished Results)
MTB1254_Pellicle_56D_02Sediment vs pellicle-1.816.891.19Yang Liu, et al. (Unpublished Results)
TBE733Control1.9610.426.30Yang Liu, et al. (Unpublished Results)
TBE734Control-0.007.240.14Yang Liu, et al. (Unpublished Results)
TBE735Oleic acid0.127.960.32Yang Liu, et al. (Unpublished Results)
TBE736Palmitic acid-0.087.340.34Yang Liu, et al. (Unpublished Results)
MTB1254_FA5_10min_01FA50.077.370.00Yang Liu, et al. (Unpublished Results)
MTB1254_FA5_10min_02FA50.247.510.26Yang Liu, et al. (Unpublished Results)
MTB1254_FA5_10min_03FA50.948.731.12Yang Liu, et al. (Unpublished Results)
MTB1254_FA5_10min_04FA50.866.111.43Yang Liu, et al. (Unpublished Results)
MTB1254TA1_OA-30min_01Oleic acid0.788.270.79Yang Liu, et al. (Unpublished Results)
MTB1254TA1_OA-30min_02Oleic acid1.278.521.12Yang Liu, et al. (Unpublished Results)
MTB1254TA1_OA-30min_03Oleic acid0.238.160.01Yang Liu, et al. (Unpublished Results)
MTB1254TA1_OA-30min_04Oleic acid0.166.820.07Yang Liu, et al. (Unpublished Results)
OA_50uM_24h_01Oleic acid-0.078.410.13Yang Liu, et al. (Unpublished Results)
OA_50uM_24h_02Oleic acid0.057.570.08Yang Liu, et al. (Unpublished Results)
OA_50uM_24h_03Oleic acid-0.057.620.11Yang Liu, et al. (Unpublished Results)
OA_50uM_24h_04Oleic acid0.308.160.81Yang Liu, et al. (Unpublished Results)
OA_50uM_24h_05Oleic acid0.127.790.32Yang Liu, et al. (Unpublished Results)
OA_50uM_24h_06Oleic acid0.047.090.10Yang Liu, et al. (Unpublished Results)
Starvation_1254_3d_01Starvation0.757.950.32Yang Liu, et al. (Unpublished Results)
Starvation_1254_3d_02Starvation0.388.190.09Yang Liu, et al. (Unpublished Results)
Starvation_1254_3d_03Starvation0.907.560.63Yang Liu, et al. (Unpublished Results)
Starvation_1254_3d_04Starvation1.108.350.44Yang Liu, et al. (Unpublished Results)
Starvation_1254_OA50_3d_02Starvation0.927.750.35Yang Liu, et al. (Unpublished Results)
Starvation_1254_OA50_3d_03Starvation0.617.900.36Yang Liu, et al. (Unpublished Results)
Starvation_1254_OA50_3d_01Starvation1.308.990.78Yang Liu, et al. (Unpublished Results)
Starvation_1254_OA50_3d_04Starvation1.569.110.95Yang Liu, et al. (Unpublished Results)
MTB1254_FA5_1h_01FA50.198.470.16Yang Liu, et al. (Unpublished Results)
Starvation_1254_5d_02Starvation0.737.200.39Yang Liu, et al. (Unpublished Results)
Starvation_1254_5d_01Starvation0.506.880.17Yang Liu, et al. (Unpublished Results)
Starvation_1254_5d_03Starvation0.537.100.18Yang Liu, et al. (Unpublished Results)
Starvation_1254_5d_04Starvation0.697.650.26Yang Liu, et al. (Unpublished Results)
Starvation_1254_OA50_5d_02Starvation-0.196.190.08Yang Liu, et al. (Unpublished Results)
Starvation_1254_OA50_5d_04Starvation1.127.900.45Yang Liu, et al. (Unpublished Results)
Starvation_1254_OA50_5d_03Starvation0.547.340.20Yang Liu, et al. (Unpublished Results)
Starvation_1254_OA50_5d_01Starvation0.287.390.13Yang Liu, et al. (Unpublished Results)
PA_50uM_3d_01Palmitic acid-0.176.180.44Yang Liu, et al. (Unpublished Results)
PA_50uM_3d_03Palmitic acid0.026.690.05Yang Liu, et al. (Unpublished Results)
PA_50uM_3d_05Palmitic acid-0.017.040.09Yang Liu, et al. (Unpublished Results)
PA_50uM_3d_06Palmitic acid-0.385.970.82Yang Liu, et al. (Unpublished Results)
PA_50uM_3d_04Palmitic acid-0.095.910.25Yang Liu, et al. (Unpublished Results)
PA_50uM_3d_02Palmitic acid-0.725.311.92Yang Liu, et al. (Unpublished Results)
TBF466Wild type vs Mutant0.146.000.15Yang Liu, et al. (Unpublished Results)
Rv_OA30_30mim_01Oleic acid0.867.690.68Yang Liu, et al. (Unpublished Results)
Rv_OA30_30mim_03Oleic acid-0.056.870.11Yang Liu, et al. (Unpublished Results)
Rv_TA_OA30_30mim_03Oleic acid0.287.900.23Yang Liu, et al. (Unpublished Results)
Rv_TA_OA30_30mim_01Oleic acid0.039.030.10Yang Liu, et al. (Unpublished Results)
BCG wild type vs BCG with empty pMV361 at OD 0.2 rep 1Control0.288.741.07Flores Valdez MA and Schoolnik GK (2010)
BCG wild type vs BCG with empty pMV361 at OD 0.2 rep 2Control0.229.630.83Flores Valdez MA and Schoolnik GK (2010)
BCG wild type vs BCG with empty pMV361 at OD 0.2 rep 3Control0.259.570.95Flores Valdez MA and Schoolnik GK (2010)
BCG wild type vs BCG with pMFdosR at OD 0.2 rep 1Wild type vs overexpression0.198.490.02Flores Valdez MA and Schoolnik GK (2010)
BCG wild type vs BCG with pMFdosR at OD 0.2 rep 2Wild type vs overexpression0.237.310.36Flores Valdez MA and Schoolnik GK (2010)
BCG wild type vs BCG with pMFdosR at OD 0.2 rep 3Wild type vs overexpression0.417.930.53Flores Valdez MA and Schoolnik GK (2010)
BCG wild type vs BCG with empty pMV361 at OD 0.2 rep 4Control-0.077.120.30Flores Valdez MA and Schoolnik GK (2010)
BCG wild type vs BCG with pMFdosR at OD 0.2 rep 4Wild type vs overexpression0.086.380.03Flores Valdez MA and Schoolnik GK (2010)
BCG wild type vs BCG with pMFdosR at OD 0.2 rep 5Wild type vs overexpression0.157.120.04Flores Valdez MA and Schoolnik GK (2010)
BCG wild type vs BCG with empty pMV361 at OD 0.4 rep 1Control0.148.550.61Flores Valdez MA and Schoolnik GK (2010)
BCG wild type vs BCG with empty pMV361 at OD 0.4 rep 2Control-0.087.770.37Flores Valdez MA and Schoolnik GK (2010)
BCG wild type vs BCG with empty pMV361 at OD 0.4 rep 3Control0.185.190.60Flores Valdez MA and Schoolnik GK (2010)
BCG wild type vs BCG with empty pMV361 at OD 0.4 rep 4Control0.017.010.03Flores Valdez MA and Schoolnik GK (2010)
BCG wild type vs BCG with empty pMV361 at OD 0.4 rep 5Control-0.108.550.49Flores Valdez MA and Schoolnik GK (2010)
BCG wild type vs BCG with pMFdosR at OD 0.4 rep 1Wild type vs overexpression-0.037.570.15Flores Valdez MA and Schoolnik GK (2010)
BCG wild type vs BCG with pMFdosR at OD 0.4 rep 2Wild type vs overexpression0.336.710.59Flores Valdez MA and Schoolnik GK (2010)
BCG wild type vs BCG with pMFdosR at OD 0.4 rep 3Wild type vs overexpression0.068.870.12Flores Valdez MA and Schoolnik GK (2010)
BCG wild type vs BCG with pMFdosR at OD 0.4 rep 4Wild type vs overexpression-1.030.500.92Flores Valdez MA and Schoolnik GK (2010)
MTB1254 WT vs Rv3662c-3665c KO in 7H9OADC, OD 0.3-1Oligopeptide permease deficient0.117.050.34Flores-Valdez MA, et al. (2009)
MTB1254 WT vs Rv3662c-3665c KO in 7H9OADC, OD 0.3-2Oligopeptide permease deficient-0.214.490.25Flores-Valdez MA, et al. (2009)
MTB1254 WT vs Rv3662c-3665c KO in 7H9OADC, OD 1.0-1Oligopeptide permease deficient0.204.800.47Flores-Valdez MA, et al. (2009)
MTB1254 WT vs Rv3662c-3665c KO in 7H9OADC, OD 1.0-2Oligopeptide permease deficient0.164.780.34Flores-Valdez MA, et al. (2009)
MTB1254 WT vs Rv3662c-3665c KO in 7H9OADC, OD 1.5-1Oligopeptide permease deficient0.076.410.13Flores-Valdez MA, et al. (2009)
MTB1254 WT vs Rv3662c-3665c KO in 7H9OADC, OD 1.5-2Oligopeptide permease deficient-0.126.430.46Flores-Valdez MA, et al. (2009)
MTB1254 WT vs Rv3662c-3665c KO in 7H9OADC, OD 0.3-3Oligopeptide permease deficient0.154.250.01Flores-Valdez MA, et al. (2009)
MTB1254 WT vs Rv3662c-3665c KO in 7H9OADC, OD 0.3-4Oligopeptide permease deficient-0.094.810.24Flores-Valdez MA, et al. (2009)
MTB1254 WT vs Rv3662c-3665c KO in 7H9OADC, OD 1.0-3Oligopeptide permease deficient-0.025.230.02Flores-Valdez MA, et al. (2009)
MTB1254 WT vs Rv3662c-3665c KO in 7H9OADC, OD 1.0-4Oligopeptide permease deficient0.165.510.34Flores-Valdez MA, et al. (2009)
MTB1254 WT vs Rv3662c-3665c KO in 7H9OADC, OD 1.5-3Oligopeptide permease deficient0.275.500.70Flores-Valdez MA, et al. (2009)
MTB1254 WT vs Rv3662c-3665c KO in 7H9OADC, OD 1.5-4Oligopeptide permease deficient-0.046.210.15Flores-Valdez MA, et al. (2009)
MTB1254 WT vs Rv3662c-3665c KO in 7H9OADC, OD 1.0-5Oligopeptide permease deficient0.186.370.39Flores-Valdez MA, et al. (2009)
MTB1254 WT vs Rv3662c-3665c KO in 7H9OADC, OD 1.0-6Oligopeptide permease deficient0.296.570.57Flores-Valdez MA, et al. (2009)
MTB1254 Opp KO complemented vs Opp KO in 7H9OADC, OD 1.0-2Oligopeptide permease deficient-0.016.290.05Flores-Valdez MA, et al. (2009)
MTB1254 Opp KO complemented vs Opp KO in 7H9OADC, OD 1.0-3Oligopeptide permease deficient-0.196.660.60Flores-Valdez MA, et al. (2009)
MTB1254 Opp KO complemented vs Opp KO in 7H9OADC, OD 1.0-4Oligopeptide permease deficient-0.092.580.33Flores-Valdez MA, et al. (2009)
MTB1254 WT vs Rv3662c-3665c KO in 7H9OADC, OD 1.5-6Oligopeptide permease deficient-0.036.360.11Flores-Valdez MA, et al. (2009)
MTB1254 WT vs Rv3662c-3665c KO in 7H9OADC-Exp2, OD 0.3-1Oligopeptide permease deficient0.317.011.07Flores-Valdez MA, et al. (2009)
MTB1254 WT vs Rv3662c-3665c KO in 7H9OADC-Exp2, OD 0.3-2Oligopeptide permease deficient0.096.810.25Flores-Valdez MA, et al. (2009)
MTB1254 WT vs Rv3662c-3665c KO in 7H9OADC-Exp2, OD1-1Oligopeptide permease deficient0.176.470.54Flores-Valdez MA, et al. (2009)
MTB1254 WT vs Rv3662c-3665c KO in 7H9OADC-Exp2, OD1-2Oligopeptide permease deficient0.206.310.52Flores-Valdez MA, et al. (2009)
MTB1254 WT vs Rv3662c-3665c KO in 7H9OADC-Exp2, OD1.5-1Oligopeptide permease deficient-0.035.020.20Flores-Valdez MA, et al. (2009)
MTB1254 WT vs Rv3662c-3665c KO in 7H9OADC-Exp2, OD1.5-2Oligopeptide permease deficient0.036.290.10Flores-Valdez MA, et al. (2009)
MTB1254 WT vs Rv3662c-3665c KO in 7H9OADC-Exp2, OD 0.3-3Oligopeptide permease deficient0.227.010.65Flores-Valdez MA, et al. (2009)
MTB1254 WT vs Rv3662c-3665c KO in 7H9OADC-Exp2, OD 0.3-4Oligopeptide permease deficient0.017.770.03Flores-Valdez MA, et al. (2009)
MTB1254 WT vs Rv3662c-3665c KO in 7H9OADC-Exp2, OD1-3Oligopeptide permease deficient0.057.220.11Flores-Valdez MA, et al. (2009)
MTB1254 WT vs Rv3662c-3665c KO in 7H9OADC-Exp2, OD1-4Oligopeptide permease deficient0.127.380.21Flores-Valdez MA, et al. (2009)
MTB1254 WT vs Rv3662c-3665c KO in 7H9OADC-Exp2, OD1.5-3Oligopeptide permease deficient0.177.380.55Flores-Valdez MA, et al. (2009)
MTB1254 WT vs Rv3662c-3665c KO in 7H9OADC-Exp2, OD1.5-4Oligopeptide permease deficient0.077.600.19Flores-Valdez MA, et al. (2009)
H37Rv dosR KO vs BCG with pMFdosR at OD 0.4 rep 1Null mutant vs overexpression0.417.210.36Flores Valdez MA and Schoolnik GK (2010)
H37Rv dosR KO vs BCG with pMFdosR at OD 0.4 rep 2Null mutant vs overexpression0.286.830.32Flores Valdez MA and Schoolnik GK (2010)
H37Rv dosR KO vs BCG with pMFdosR at OD 0.4 rep 3Null mutant vs overexpression0.157.280.03Flores Valdez MA and Schoolnik GK (2010)
H37Rv dosR KO vs BCG with pMFdosR at OD 0.4 rep 4Null mutant vs overexpression-0.017.800.06Flores Valdez MA and Schoolnik GK (2010)
H37Rv Vs M.bovis rep1Strain comparison0.2611.380.16Rehren G, et al. (2007)
H37Rv Vs M.bovis rep2Strain comparison0.6610.960.46Rehren G, et al. (2007)
H37Rv Vs M.bovis rep3Strain comparison-0.2610.020.32Rehren G, et al. (2007)
H37Rv Vs M.bovis rep4Strain comparison1.4810.190.94Rehren G, et al. (2007)
H37Rv vs. H37Rv SDS treated rep 3SDS0.688.870.09Pang X, et al. (2007)
H37Rv vs. H37Rv SDS treated rep 5SDS0.228.940.06Pang X, et al. (2007)
H37Rv vs. H37Rv delta mprAB mutant rep 3Wild type vs Mutant-1.048.971.10Pang X, et al. (2007)
H37Rv vs. H37Rv SDS treated rep 1SDS0.408.600.19Pang X, et al. (2007)
H37Rv vs. H37Rv SDS treated rep 2SDS-0.619.970.40Pang X, et al. (2007)
H37Rv vs. H37Rv SDS treated rep 4SDS-0.787.910.36Pang X, et al. (2007)
H37Rv vs. H37Rv SDS treated rep 6SDS-0.3510.400.16Pang X, et al. (2007)
H37Rv vs. H37Rv delta mprAB mutant rep 1Wild type vs Mutant-0.409.270.51Pang X, et al. (2007)
H37Rv vs. H37Rv delta mprAB mutant rep 2Wild type vs Mutant0.408.390.47Pang X, et al. (2007)
H37Rv vs. H37Rv delta mprAB mutant rep 4Wild type vs Mutant0.686.630.69Pang X, et al. (2007)
H37Rv vs. H37Rv delta mprAB mutant rep 5Wild type vs Mutant-0.8310.021.17Pang X, et al. (2007)
H37Rv vs. H37Rv delta mprAB mutant rep 6Wild type vs Mutant0.289.120.47Pang X, et al. (2007)
H37Rv delta mprAB mutant vs. H37Rv delta mprAB mutant SDS treated rep 1SDS3.0210.951.04Pang X, et al. (2007)
H37Rv delta mprAB mutant vs. H37Rv delta mprAB mutant SDS treated rep 2SDS-3.0010.121.67Pang X, et al. (2007)
H37Rv delta mprAB mutant vs. H37Rv delta mprAB mutant SDS treated rep 3SDS2.969.581.06Pang X, et al. (2007)
H37Rv delta mprAB mutant vs. H37Rv delta mprAB mutant SDS treated rep 4SDS-2.647.121.25Pang X, et al. (2007)
H37Rv delta mprAB mutant vs. H37Rv delta mprAB mutant SDS treated rep 5SDS1.7710.200.62Pang X, et al. (2007)
H37Rv delta mprAB mutant vs. H37Rv delta mprAB mutant SDS treated rep 6SDS-2.309.811.32Pang X, et al. (2007)
H37Rv SDS treated vs. H37Rv delta mprAB mutant SDS treated rep 1SDS2.5612.011.95Pang X, et al. (2007)
H37Rv SDS treated vs. H37Rv delta mprAB mutant SDS treated rep 2SDS-1.999.871.86Pang X, et al. (2007)
H37Rv SDS treated vs. H37Rv delta mprAB mutant SDS treated rep 3SDS0.9510.890.98Pang X, et al. (2007)
H37Rv SDS treated vs. H37Rv delta mprAB mutant SDS treated rep 4SDS-1.168.131.21Pang X, et al. (2007)
H37Rv SDS treated vs. H37Rv delta mprAB mutant SDS treated rep 5SDS0.859.701.15Pang X, et al. (2007)
H37Rv SDS treated vs. H37Rv delta mprAB mutant SDS treated rep 6SDS-2.0510.612.47Pang X, et al. (2007)
H37Rv wild type Vs Rv3676 null 1Wild type vs Mutant0.3911.230.44Rickman L, et al. (2005)
Rv3676 null Vs H37Rv wild type 1Wild type vs Mutant0.3911.230.44Rickman L, et al. (2005)
H37Rv wild type Vs Rv3676 null 2Wild type vs Mutant-0.168.980.01Rickman L, et al. (2005)
Rv3676 null Vs H37Rv wild type 2Wild type vs Mutant-0.168.980.01Rickman L, et al. (2005)
H37Rv wild type Vs Rv3676 null 3Wild type vs Mutant0.5311.210.49Rickman L, et al. (2005)
H37Rv wild type Vs Rv3676 null 5Wild type vs Mutant-0.8510.630.02Rickman L, et al. (2005)
Rv3676 null Vs H37Rv wild type 5Wild type vs Mutant-0.8510.630.02Rickman L, et al. (2005)
H37Rv wild type Vs Rv3676 null 6Wild type vs Mutant-0.5510.420.28Rickman L, et al. (2005)
Rv3676 null Vs H37Rv wild type 6Wild type vs Mutant-0.5510.420.28Rickman L, et al. (2005)
H37Rv wild type Vs Rv3676 null 7Wild type vs Mutant0.749.120.66Rickman L, et al. (2005)
Rv3676 null Vs H37Rv wild type 7Wild type vs Mutant0.749.120.66Rickman L, et al. (2005)
High iron wt vs high iron ideR Complement 3bIron-0.409.870.94Rodriguez GM, et al. (2002)
High iron wt vs low iron wt 1aIron-0.5310.270.90Rodriguez GM, et al. (2002)
High iron wt vs high iron ideR KO 1aIron0.1710.050.23Rodriguez GM, et al. (2002)
High iron wt vs low iron wt 2aIron-0.419.730.80Rodriguez GM, et al. (2002)
High iron wt vs high iron ideR KO 2aIron0.4110.450.55Rodriguez GM, et al. (2002)
High iron wt vs high iron ideR Complement 2aIron-0.659.981.36Rodriguez GM, et al. (2002)
High iron wt vs low iron wt 3aIron-0.349.600.72Rodriguez GM, et al. (2002)
High iron wt vs high iron ideR KO 3aIron0.3110.330.41Rodriguez GM, et al. (2002)
High iron wt vs low iron wt 3bIron-0.569.751.01Rodriguez GM, et al. (2002)
High iron wt vs low iron wt 1bIron-0.409.520.77Rodriguez GM, et al. (2002)
High iron wt vs high iron ideR KO 1bIron0.129.360.13Rodriguez GM, et al. (2002)
High iron wt vs high iron ideR Complement 1aIron-0.419.650.94Rodriguez GM, et al. (2002)
High iron wt vs low iron wt 2bIron-0.3310.050.67Rodriguez GM, et al. (2002)
High iron wt vs high iron ideR KO 2bIron0.3910.090.60Rodriguez GM, et al. (2002)
High iron wt vs high iron ideR Complement 2bIron-0.329.800.71Rodriguez GM, et al. (2002)
High iron wt vs high iron ideR KO 3bIron0.2810.170.20Rodriguez GM, et al. (2002)
High iron wt vs high iron ideR Complement 3aIron-0.589.371.24Rodriguez GM, et al. (2002)
High iron wt vs high iron ideR Complement 1bIron-0.499.171.28Rodriguez GM, et al. (2002)
H37Rv wild type Vs Rv3676 null 4Wild type vs Mutant0.868.080.64Rickman L, et al. (2005)
Rv3676 null Vs H37Rv wild type 4Wild type vs Mutant0.868.080.64Rickman L, et al. (2005)
Rv3676 null Vs H37Rv wild type 3Wild type vs Mutant0.5311.210.49Rickman L, et al. (2005)
MTB1254 ethanol vs. 5.0 ug/ml Erythromycin for 30 min rep 1Erythromycin0.219.560.38Morris RP, et al. (2005)
MTB1254 ethanol vs. 25 ug/ml Erythromycin for 30 min rep 1Erythromycin-0.038.870.20Morris RP, et al. (2005)
MTB1254 ethanol vs. 100 ug/ml Erythromycin for 30 min rep 1Erythromycin-0.047.740.10Morris RP, et al. (2005)
MTB1254 ethanol vs. 0.5 ug/ml Erythromycin for 30 min rep 3Erythromycin0.298.190.86Morris RP, et al. (2005)
MTB1254 ethanol vs. 1.0 ug/ml Erythromycin for 30 min rep 4Erythromycin0.258.220.66Morris RP, et al. (2005)
MTB1254 ethanol vs. 5.0 ug/ml Erythromycin for 30 min rep 4Erythromycin0.268.280.47Morris RP, et al. (2005)
MTB1254 ethanol vs. 25 ug/ml Erythromycin for 30 min rep 4Erythromycin-0.026.580.08Morris RP, et al. (2005)
MTB1254 ethanol vs. 100 ug/ml Erythromycin for 30 min rep 4Erythromycin0.107.410.05Morris RP, et al. (2005)
MTB1254 ethanol vs. 1.0 ug/ml Tetracyclin for 2 hr rep 4Tetracycline0.178.150.23Morris RP, et al. (2005)
MTB1254 ethanol vs. 1.0 ug/ml Tetracyclin for 2 hr rep 3Tetracycline0.048.620.04Morris RP, et al. (2005)
MTB1254 ethanol vs. 1.0 ug/ml Tetracyclin for 24 hr rep 3Tetracycline-0.498.020.77Morris RP, et al. (2005)
MTB1254 ethanol vs. 1.0 ug/ml Tetracyclin for 24 hr rep 4Tetracycline-0.198.240.35Morris RP, et al. (2005)
MTB1254 ethanol vs. 0.5 ug/ml Erythromycin for 15 min rep 1Erythromycin0.467.941.00Morris RP, et al. (2005)
MTB1254 ethanol vs. 1.0 ug/ml Erythromycin for 15 min rep 1Erythromycin-0.188.160.35Morris RP, et al. (2005)
MTB1254 ethanol vs. 5.0 ug/ml Erythromycin for 15 min rep 1Erythromycin-0.218.890.65Morris RP, et al. (2005)
MTB1254 ethanol vs. 25 ug/ml Erythromycin for 15 min rep 1Erythromycin0.277.660.57Morris RP, et al. (2005)
MTB1254 ethanol vs. 100 ug/ml Erythromycin for 15 min rep 1 Erythromycin0.347.710.72Morris RP, et al. (2005)
MTB1254 ethanol vs. 0.5 ug/ml Erythromycin for 15 min rep 2Erythromycin0.278.120.65Morris RP, et al. (2005)
MTB1254 ethanol vs. 1.0 ug/ml Erythromycin for 15 min rep 2Erythromycin0.227.520.53Morris RP, et al. (2005)
MTB1254 ethanol vs. 5.0 ug/ml Erythromycin for 15 min rep 2Erythromycin0.447.811.13Morris RP, et al. (2005)
MTB1254 ethanol vs. 25 ug/ml Erythromycin for 15 min rep 2Erythromycin0.349.020.63Morris RP, et al. (2005)
MTB1254 ethanol vs. 100 ug/ml Erythromycin for 15 min rep 2Erythromycin0.207.600.32Morris RP, et al. (2005)
MTB1254 ethanol vs. 0.5 ug/ml Erythromycin for 15 min rep 3Erythromycin-0.139.050.37Morris RP, et al. (2005)
MTB1254 ethanol vs. 1.0 ug/ml Erythromycin for 15 min rep 3Erythromycin-0.019.180.04Morris RP, et al. (2005)
MTB1254 ethanol vs. 5.0 ug/ml Erythromycin for 15 min rep 3Erythromycin-0.318.501.07Morris RP, et al. (2005)
MTB1254 ethanol vs. 25 ug/ml Erythromycin for 15 min rep 3Erythromycin0.016.810.02Morris RP, et al. (2005)
MTB1254 ethanol vs. 100 ug/ml Erythromycin for 15 min rep 3Erythromycin0.117.510.23Morris RP, et al. (2005)
MTB1254 ethanol vs. 0.5 ug/ml Erythromycin for 15 min rep 4Erythromycin-0.067.990.20Morris RP, et al. (2005)
MTB1254 ethanol vs. 1.0 ug/ml Erythromycin for 15 min rep 4Erythromycin0.279.030.76Morris RP, et al. (2005)
MTB1254 ethanol vs. 5.0 ug/ml Erythromycin for 15 min rep 4Erythromycin0.269.060.75Morris RP, et al. (2005)
MTB1254 ethanol vs. 25 ug/ml Erythromycin for 15 min rep 4Erythromycin0.857.371.73Morris RP, et al. (2005)
MTB1254 ethanol vs. 100 ug/ml Erythromycin for 15 min rep 4Erythromycin-0.038.480.06Morris RP, et al. (2005)
MTB1254 ethanol vs. 0.5 ug/ml Erythromycin for 30 min rep 1Erythromycin0.198.060.51Morris RP, et al. (2005)
MTB1254 ethanol vs. 0.5 ug/ml Erythromycin for 30 min rep 2Erythromycin0.219.160.67Morris RP, et al. (2005)
MTB1254 ethanol vs. 1.0 ug/ml Erythromycin for 30 min rep 1Erythromycin0.258.540.80Morris RP, et al. (2005)
MTB1254 ethanol vs. 1.0 ug/ml Erythromycin for 30 min rep 2Erythromycin0.419.731.17Morris RP, et al. (2005)
MTB1254 ethanol vs. 5.0 ug/ml Erythromycin for 30 min rep 2Erythromycin0.4410.730.78Morris RP, et al. (2005)
MTB1254 ethanol vs. 25 ug/ml Erythromycin for 30 min rep 2Erythromycin0.128.750.11Morris RP, et al. (2005)
MTB1254 ethanol vs. 100 ug/ml Erythromycin for 30 min rep 2Erythromycin0.579.110.55Morris RP, et al. (2005)
MTB1254 ethanol vs. 0.5 ug/ml Erythromycin for 30 min rep 4Erythromycin0.358.950.80Morris RP, et al. (2005)
MTB1254 ethanol vs. 1.0 ug/ml Erythromycin for 30 min rep 3Erythromycin0.048.290.05Morris RP, et al. (2005)
MTB1254 ethanol vs. 5.0 ug/ml Erythromycin for 30 min rep 3Erythromycin0.366.970.80Morris RP, et al. (2005)
MTB1254 ethanol vs. 25 ug/ml Erythromycin for 30 min rep 3Erythromycin0.279.220.23Morris RP, et al. (2005)
MTB1254 ethanol vs. 100 ug/ml Erythromycin for 30 min rep 3Erythromycin0.229.200.09Morris RP, et al. (2005)
MTB1254 ethanol vs. 1.0 ug/ml Tetracyclin for 2 hr rep 1Tetracycline0.437.690.59Morris RP, et al. (2005)
MTB1254 ethanol vs. 1.0 ug/ml Tetracyclin for 2 hr rep 2Tetracycline0.036.440.03Morris RP, et al. (2005)
MTB1254 ethanol vs. 1.0 ug/ml Tetracyclin for 24 hr rep 1Tetracycline-0.077.250.18Morris RP, et al. (2005)
MTB1254 ethanol vs. 1.0 ug/ml Tetracyclin for 24 hr rep 2Tetracycline-0.098.350.23Morris RP, et al. (2005)
MTB1254 ethanol vs. 0.5 ug/ml Tetracyclin for 15 min rep 1Tetracycline-0.168.230.70Morris RP, et al. (2005)
MTB1254 ethanol vs. 1.0 ug/ml Tetracyclin for 15 min rep 1Tetracycline-0.098.600.40Morris RP, et al. (2005)
MTB1254 ethanol vs. 5.0 ug/ml Tetracyclin for 15 min rep 3Tetracycline-0.228.760.59Morris RP, et al. (2005)
MTB1254 ethanol vs. 25 ug/ml Tetracyclin for 15 min rep 3Tetracycline0.257.490.36Morris RP, et al. (2005)
MTB1254 ethanol vs. 100 ug/ml Tetracyclin for 15 min rep 4Tetracycline-0.057.610.13Morris RP, et al. (2005)
MTB1254 ethanol vs. 0.5 ug/ml Tetracyclin for 15 min rep 4Tetracycline0.108.400.26Morris RP, et al. (2005)
MTB1254 ethanol vs. 1.0 ug/ml Tetracyclin for 15 min rep 4Tetracycline0.126.930.00Morris RP, et al. (2005)
MTB1254 ethanol vs. 5.0 ug/ml Tetracyclin for 15 min rep 4Tetracycline0.188.520.26Morris RP, et al. (2005)
MTB1254 ethanol vs. 25 ug/ml Tetracyclin for 15 min rep 4Tetracycline0.197.730.13Morris RP, et al. (2005)
MTB1254 ethanol vs. 100 ug/ml Tetracyclin for 15 min rep 1Tetracycline0.369.080.34Morris RP, et al. (2005)
MTB1254 ethanol vs. 0.5 ug/ml Tetracyclin for 30 min rep 1Tetracycline0.099.710.20Morris RP, et al. (2005)
MTB1254 ethanol vs. 1.0 ug/ml Tetracyclin for 30 min rep 1Tetracycline0.127.920.02Morris RP, et al. (2005)
MTB1254 ethanol vs. 5.0 ug/ml Tetracyclin for 30 min rep 1Tetracycline-0.128.450.41Morris RP, et al. (2005)
MTB1254 ethanol vs. 25 ug/ml Tetracyclin for 30 min rep 1Tetracycline0.217.400.17Morris RP, et al. (2005)
MTB1254 ethanol vs. 100 ug/ml Tetracyclin for 30 min rep 1Tetracycline0.228.200.24Morris RP, et al. (2005)
MTB1254 ethanol vs. 0.5 ug/ml Tetracyclin for 30 min rep 2Tetracycline0.078.350.12Morris RP, et al. (2005)
MTB1254 ethanol vs. 1.0 ug/ml Tetracyclin for 30 min rep 2Tetracycline0.399.200.79Morris RP, et al. (2005)
MTB1254 ethanol vs. 5.0 ug/ml Tetracyclin for 30 min rep 2Tetracycline0.278.080.44Morris RP, et al. (2005)
MTB1254 ethanol vs. 25 ug/ml Tetracyclin for 30 min rep 2Tetracycline0.228.780.24Morris RP, et al. (2005)
MTB1254 ethanol vs. 100 ug/ml Tetracyclin for 30 min rep 2Tetracycline0.118.970.09Morris RP, et al. (2005)
MTB1254 ethanol vs. 0.5 ug/ml Tetracyclin for 15 min rep 2Tetracycline-0.128.660.59Morris RP, et al. (2005)
MTB1254 ethanol vs. 1.0 ug/ml Tetracyclin for 15 min rep 2Tetracycline-0.029.660.11Morris RP, et al. (2005)
MTB1254 ethanol vs. 5.0 ug/ml Tetracyclin for 15 min rep 1Tetracycline-0.429.270.89Morris RP, et al. (2005)
MTB1254 ethanol vs. 25 ug/ml Tetracyclin for 15 min rep 1Tetracycline0.078.560.02Morris RP, et al. (2005)
MTB1254 ethanol vs. 100 ug/ml Tetracyclin for 15 min rep 2Tetracycline0.129.460.09Morris RP, et al. (2005)
MTB1254 ethanol vs. 0.5 ug/ml Tetracyclin for 15 min rep 3Tetracycline-0.107.670.41Morris RP, et al. (2005)
MTB1254 ethanol vs. 1.0 ug/ml Tetracyclin for 15 min rep 3Tetracycline0.119.200.23Morris RP, et al. (2005)
MTB1254 ethanol vs. 5.0 ug/ml Tetracyclin for 15 min rep 2Tetracycline0.059.120.02Morris RP, et al. (2005)
MTB1254 ethanol vs. 25 ug/ml Tetracyclin for 15 min rep 2Tetracycline0.168.340.21Morris RP, et al. (2005)
MTB1254 ethanol vs. 100 ug/ml Tetracyclin for 15 min rep 3Tetracycline-0.028.780.09Morris RP, et al. (2005)
MTB1254 ethanol vs. 0.5 ug/ml Tetracyclin for 30 min rep 3Tetracycline0.169.210.37Morris RP, et al. (2005)
MTB1254 ethanol vs. 1.0 ug/ml Tetracyclin for 30 min rep 3Tetracycline0.038.500.08Morris RP, et al. (2005)
MTB1254 ethanol vs. 5.0 ug/ml Tetracyclin for 30 min rep 3Tetracycline0.028.970.10Morris RP, et al. (2005)
MTB1254 ethanol vs. 25 ug/ml Tetracyclin for 30 min rep 3Tetracycline0.008.560.14Morris RP, et al. (2005)
MTB1254 ethanol vs. 100 ug/ml Tetracyclin for 30 min rep 3Tetracycline0.028.010.09Morris RP, et al. (2005)
MTB1254 ethanol vs. 0.5 ug/ml Tetracyclin for 30 min rep 4Tetracycline0.147.910.20Morris RP, et al. (2005)
MTB1254 ethanol vs. 1.0 ug/ml Tetracyclin for 30 min rep 4Tetracycline0.019.060.08Morris RP, et al. (2005)
MTB1254 ethanol vs. 5.0 ug/ml Tetracyclin for 30 min rep 4Tetracycline-0.158.620.36Morris RP, et al. (2005)
MTB1254 ethanol vs. 25 ug/ml Tetracyclin for 30 min rep 4Tetracycline0.248.070.16Morris RP, et al. (2005)
MTB1254 ethanol vs. 100 ug/ml Tetracyclin for 30 min rep 4Tetracycline0.238.060.16Morris RP, et al. (2005)
MTB1254 control vs. 25 ug/ml Streptomycin for 15 min rep 1Streptomycin-0.058.330.17Morris RP, et al. (2005)
MTB1254 control vs. 1.0 ug/ml Streptomycin for 15 min rep 1Streptomycin0.288.840.81Morris RP, et al. (2005)
MTB1254 control vs. 5.0 ug/ml Streptomycin for 15 min rep 2Streptomycin-0.367.770.88Morris RP, et al. (2005)
MTB1254 control vs. 1.0 ug/ml Streptomycin for 15 min rep 4Streptomycin0.157.970.36Morris RP, et al. (2005)
MTB1254 control vs. 1.0 ug/ml Erythromycin for 2 hr (ref) rep 4Erythromycin-0.058.040.09Morris RP, et al. (2005)
MTB1254 control vs. 1.0 ug/ml Streptomycin for 24 hr (ref) rep 4Streptomycin-0.397.320.60Morris RP, et al. (2005)
MTB1254 control vs. 100 ug/ml Streptomycin for 15 min rep 4Streptomycin0.098.680.13Morris RP, et al. (2005)
MTB1254 control vs. 1.0 ug/ml Erythromycin for 24 hr (ref) rep 5Erythromycin-0.458.630.45Morris RP, et al. (2005)
MTB1254 control vs. 0.5 ug/ml Streptomycin for 15 min rep 5Streptomycin0.097.840.14Morris RP, et al. (2005)
MTB1254 vs. MTB1254 rep1Control-0.049.080.12Morris RP, et al. (2005)
MTB1254 vs. MTB1254 rep2Control-0.169.550.62Morris RP, et al. (2005)
MTB1254 control vs. 1.0 ug/ml Erythromycin for 2 hr (ref) rep 1Erythromycin-0.348.500.30Morris RP, et al. (2005)
MTB1254 control vs. 1.0 ug/ml Streptomycin for 24 hr (ref) rep 1Streptomycin-0.307.990.43Morris RP, et al. (2005)
MTB1254 control vs. 1.0 ug/ml Streptomycin for 2 hr (ref) rep 1Streptomycin0.529.471.13Morris RP, et al. (2005)
MTB1254 control vs. 0.5 ug/ml Streptomycin for 15 min rep 1Streptomycin0.157.960.42Morris RP, et al. (2005)
MTB1254 control vs. 25 ug/ml Streptomycin for 15 min rep 2Streptomycin0.318.690.79Morris RP, et al. (2005)
MTB1254 control vs. 1.0 ug/ml Erythromycin for 24 hr (ref) rep 1Erythromycin-0.107.400.11Morris RP, et al. (2005)
MTB1254 control vs. 0.5 ug/ml Streptomycin for 15 min rep 2Streptomycin0.278.940.57Morris RP, et al. (2005)
MTB1254 vs. MTB1254 rep3Control-0.149.450.30Morris RP, et al. (2005)
MTB1254 vs. MTB1254 rep4Control0.048.770.17Morris RP, et al. (2005)
MTB1254 vs. MTB1254 rep5Control0.338.761.12Morris RP, et al. (2005)
MTB1254 vs. MTB1254 rep6Control0.179.340.62Morris RP, et al. (2005)
MTB1254 control vs. 0.5 ug/ml Streptomycin for 15 min rep 3Streptomycin0.089.020.20Morris RP, et al. (2005)
MTB1254 control vs. 1.0 ug/ml Streptomycin for 15 min rep 2Streptomycin0.258.700.98Morris RP, et al. (2005)
MTB1254 control vs. 5.0 ug/ml Streptomycin for 15 min rep 1Streptomycin0.178.620.61Morris RP, et al. (2005)
MTB1254 control vs. 25 ug/ml Streptomycin for 15 min rep 3Streptomycin0.038.780.03Morris RP, et al. (2005)
MTB1254 control vs. 100 ug/ml Streptomycin for 15 min rep 1Streptomycin-0.108.550.27Morris RP, et al. (2005)
MTB1254 control vs. 1.0 ug/ml Streptomycin for 2 hr (ref) rep 2Streptomycin-0.287.930.83Morris RP, et al. (2005)
MTB1254 control vs. 1.0 ug/ml Streptomycin for 24 hr (ref) rep 2Streptomycin-0.338.590.47Morris RP, et al. (2005)
MTB1254 control vs. 1.0 ug/ml Erythromycin for 2 hr (ref) rep 2Erythromycin-0.558.820.41Morris RP, et al. (2005)
MTB1254 control vs. 1.0 ug/ml Erythromycin for 24 hr (ref) rep 2Erythromycin-0.568.950.50Morris RP, et al. (2005)
MTB1254 control vs. 0.5 ug/ml Streptomycin for 15 min rep 4Streptomycin0.278.720.94Morris RP, et al. (2005)
MTB1254 control vs. 1.0 ug/ml Streptomycin for 15 min rep 3Streptomycin0.278.840.62Morris RP, et al. (2005)
MTB1254 control vs. 5.0 ug/ml Streptomycin for 15 min rep 3Streptomycin0.329.080.99Morris RP, et al. (2005)
MTB1254 control vs. 25 ug/ml Streptomycin for 15 min rep 4Streptomycin-0.058.820.12Morris RP, et al. (2005)
MTB1254 control vs. 100 ug/ml Streptomycin for 15 min rep 2Streptomycin0.077.750.12Morris RP, et al. (2005)
MTB1254 control vs. 1.0 ug/ml Streptomycin for 2 hr (ref) rep 3Streptomycin0.228.920.49Morris RP, et al. (2005)
MTB1254 control vs. 1.0 ug/ml Streptomycin for 24 hr (ref) rep 3Streptomycin-0.086.250.12Morris RP, et al. (2005)
MTB1254 control vs. 1.0 ug/ml Erythromycin for 2 hr (ref) rep 3Erythromycin-0.457.440.28Morris RP, et al. (2005)
MTB1254 control vs. 1.0 ug/ml Erythromycin for 24 hr (ref) rep 3Erythromycin-0.557.350.50Morris RP, et al. (2005)
MTB1254 control vs. 1.0 ug/ml Streptomycin for 15 min rep 5Streptomycin-0.097.350.23Morris RP, et al. (2005)
MTB1254 control vs. 5.0 ug/ml Streptomycin for 15 min rep 4Streptomycin-0.537.891.48Morris RP, et al. (2005)
MTB1254 control vs. 100 ug/ml Streptomycin for 15 min rep 3Streptomycin0.108.780.12Morris RP, et al. (2005)
MTB1254 control vs. 1.0 ug/ml Erythromycin for 24 hr (ref) rep 4Erythromycin-0.407.330.39Morris RP, et al. (2005)
MTB1254 control vs. 1.0 ug/ml Streptomycin for 2 hr (ref) rep 4Streptomycin-0.007.660.09Morris RP, et al. (2005)
MTB strain 1254 Ctrl vs 0.05 mM H202 40min rep 1H2O20.219.090.67Voskuil MI, et al. (2011)
MTB strain 1254 Ctrl vs 0.05 mM H202 40min rep 3H2O2-0.189.110.58Voskuil MI, et al. (2011)
MTB strain 1254 Ctrl vs 0.05 mM H202 40min rep 4H2O2-0.129.530.46Voskuil MI, et al. (2011)
MTB strain 1254 Ctrl vs 0.05 mM H202 40min rep 5H2O20.179.670.43Voskuil MI, et al. (2011)
MTB strain 1254 Ctrl vs 0.05 mM H202 40min rep 6H2O20.238.990.89Voskuil MI, et al. (2011)
MTB strain 1254 Ctrl vs 0.5 mM H202 40min rep 2H2O2-0.108.830.31Voskuil MI, et al. (2011)
MTB strain 1254 Ctrl vs 0.5 mM H202 40min rep 3H2O20.038.060.01Voskuil MI, et al. (2011)
MTB strain 1254 Ctrl vs 0.5 mM H202 40min rep 4H2O2-0.337.240.74Voskuil MI, et al. (2011)
MTB strain 1254 Ctrl vs 0.5 mM H202 40min rep 5H2O2-0.407.471.27Voskuil MI, et al. (2011)
MTB strain 1254 Ctrl vs 0.5 mM H202 40min rep 6H2O20.055.230.07Voskuil MI, et al. (2011)
MTB strain 1254 Ctrl vs 5.0 mM H202 40min rep 1H2O2-1.485.591.32Voskuil MI, et al. (2011)
MTB strain 1254 Ctrl vs 5.0 mM H202 40min rep 2H2O2-1.657.681.53Voskuil MI, et al. (2011)
MTB strain 1254 Ctrl vs 5.0 mM H202 40min rep 3H2O2-0.977.241.19Voskuil MI, et al. (2011)
MTB strain 1254 Ctrl vs 5.0 mM H202 40min rep 5H2O2-1.127.251.45Voskuil MI, et al. (2011)
MTB strain 1254 Ctrl vs 5.0 mM H202 4hr rep 1H2O20.798.870.14Voskuil MI, et al. (2011)
MTB strain 1254 Ctrl vs 5.0 mM H202 4hr rep 2H2O21.058.460.28Voskuil MI, et al. (2011)
MTB strain 1254 Ctrl vs 5.0 mM H202 4hr rep 3H2O20.099.290.20Voskuil MI, et al. (2011)
MTB strain 1254 Ctrl vs 10.0 mM H202 40min rep 1H2O2-1.817.791.37Voskuil MI, et al. (2011)
MTB strain 1254 Ctrl vs 10.0 mM H202 40min rep 2H2O2-1.965.831.66Voskuil MI, et al. (2011)
MTB strain 1254 Ctrl vs 10.0 mM H202 40min rep 3H2O2-2.477.471.92Voskuil MI, et al. (2011)
MTB strain 1254 Ctrl vs 10.0 mM H202 40min rep 5H2O2-2.195.611.81Voskuil MI, et al. (2011)
MTB strain 1254 Ctrl vs 10.0 mM H202 40min rep 4H2O2-1.217.701.15Voskuil MI, et al. (2011)
MTB strain 1254 Ctrl vs 50.0 mM H202 40min rep 2H2O20.167.960.06Voskuil MI, et al. (2011)
MTB strain 1254 Ctrl vs 50.0 mM H202 40min rep 1H2O20.148.470.07Voskuil MI, et al. (2011)
MTB strain 1254 Ctrl vs 50.0 mM H202 40min rep 3H2O2-0.039.440.16Voskuil MI, et al. (2011)
MTB strain 1254 Ctrl vs 50.0 mM H202 40min rep 5H2O2-0.118.500.17Voskuil MI, et al. (2011)
MTB strain 1254 Ctrl vs 200 mM H202 40min rep 1H2O20.628.800.50Voskuil MI, et al. (2011)
MTB strain 1254 Ctrl vs 200 mM H202 40min rep 3H2O20.928.270.88Voskuil MI, et al. (2011)
MTB strain 1254 Ctrl vs 200 mM H202 40min rep 4H2O21.098.681.04Voskuil MI, et al. (2011)
MTB strain 1254 Ctrl vs 200 mM H202 40min rep 5H2O21.067.691.20Voskuil MI, et al. (2011)
MTB strain 1254 Ctrl vs 200 mM H202 40min rep 6H2O20.789.390.72Voskuil MI, et al. (2011)
MTB strain1254 vs MTB strain 1254 for H2O2 exp control rep 4Control-0.058.370.17Voskuil MI, et al. (2011)
MTB strain1254 vs MTB strain 1254 for H2O2 exp control rep 5Control-0.349.750.96Voskuil MI, et al. (2011)
MTB strain1254 vs MTB strain 1254 for H2O2 exp control rep 6Control-0.198.000.57Voskuil MI, et al. (2011)
MTB strain 1254 Ctrl vs 0.005 mM DETA/NO 40min rep 4Diethylenetriamine / nitric oxide adduct-0.2912.430.98Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs 0.05 mM DETA/NO 40min rep 7Diethylenetriamine / nitric oxide adduct0.0113.050.17Voskuil MI, et al. (2011)
MTB strain 1254 Ctrl vs 0.5 mM DETA/NO 40min rep 3Diethylenetriamine / nitric oxide adduct-0.6911.870.92Voskuil MI, et al. (2011)
MTB strain 1254 Ctrl vs 0.5 mM DETA/NO 40min rep 4Diethylenetriamine / nitric oxide adduct-0.8012.631.55Voskuil MI, et al. (2011)
MTB strain 1254 Ctrl vs 1.0 mM DETA/NO 40min rep 4Diethylenetriamine / nitric oxide adduct0.1811.920.42Voskuil MI, et al. (2011)
MTB strain 1254 Ctrl vs 5.0 mM DETA/NO 40min rep 1Diethylenetriamine / nitric oxide adduct-1.1012.461.44Voskuil MI, et al. (2003)
MTB strain1254 vs MTB strain 1254 for DETA/NO exp control rep 1Control0.0412.380.04Voskuil MI, et al. (2011)
MTB strain1254 vs MTB strain 1254 for DETA/NO exp control rep 2Control0.0212.080.05Voskuil MI, et al. (2011)
MTB strain1254 vs MTB strain 1254 for DETA/NO exp control rep 3Control-0.3511.740.79Voskuil MI, et al. (2011)
MTB strain1254 vs MTB strain 1254 for DETA/NO exp control rep 4Control-0.2311.700.55Voskuil MI, et al. (2011)
MTB strain1254 vs MTB strain 1254 for DETA/NO exp control rep 5Control0.1711.980.31Voskuil MI, et al. (2011)
MTB strain 1254 Ctrl vs 0.5 mM DETA/NO 40min rep 5Diethylenetriamine / nitric oxide adduct-1.796.771.40Voskuil MI, et al. (2011)
MTB strain 1254 Ctrl vs 0.5 mM DETA/NO 40min rep 6Diethylenetriamine / nitric oxide adduct-2.147.801.56Voskuil MI, et al. (2011)
MTB strain 1254 Ctrl vs 0.5 mM DETA/NO 40min rep 7Diethylenetriamine / nitric oxide adduct-2.347.661.62Voskuil MI, et al. (2011)
Mtm 0.2ug/mL vs ctrl 8h 1Mitomycin0.138.890.15Boshoff HI, et al. (2004)
Mtm 0.2ug/mL vs ctrl 8h 2Mitomycin-0.177.890.21Boshoff HI, et al. (2004)
H2O2 4mM vs ctrl 8h 1H2O2-0.137.990.11Boshoff HI, et al. (2004)
UV 20J vs ctrl 8h 1Ultraviolet (UV) light0.288.640.47Boshoff HI, et al. (2004)
UV 40J vs ctrl 8h 1Ultraviolet (UV) light0.669.501.03Boshoff HI, et al. (2004)
UV 40J vs 8h 2Ultraviolet (UV) light-0.068.720.04Boshoff HI, et al. (2004)
Mtm 0.2ug/mL vs ctrl 12h 1Mitomycin0.348.710.46Boshoff HI, et al. (2004)
H2O2 4mM vs ctrl 12h 1H2O2-0.138.230.13Boshoff HI, et al. (2004)
UV 60J vs ctrl 6h 1Ultraviolet (UV) light0.518.710.79Boshoff HI, et al. (2004)
UV 40J vs ctrl 12h 1Ultraviolet (UV) light-0.058.160.06Boshoff HI, et al. (2004)
EMB 10ug/mL vs DMSO 12h 1Ethambutol0.067.870.04Boshoff HI, et al. (2004)
DIPED 5ug/mL vs DMSO 12h 1Diisopropylethylenediamine0.199.920.34Boshoff HI, et al. (2004)
EMB 10ug/mL vs DMSO 12h 2Ethambutol0.289.530.48Boshoff HI, et al. (2004)
DIPED 5ug/mL vs DMSO 12h 2Diisopropylethylenediamine0.359.880.63Boshoff HI, et al. (2004)
DIPED 10ug/mL vs DMSO 12h 1Diisopropylethylenediamine0.299.470.49Boshoff HI, et al. (2004)
DIPED 10ug/mL vs DMSO 12h 2Diisopropylethylenediamine0.459.880.81Boshoff HI, et al. (2004)
10ug/ml Ethambutol vs DMSO 12hrs 3Ethambutol0.409.650.63Fu LM and Tai SC (2009)
EMB 10ug/mL vs DMSO 12h 4Ethambutol0.359.130.48Boshoff HI, et al. (2004)
DIPED 50ug/mL vs DMSO 12h 1Diisopropylethylenediamine0.049.590.14Boshoff HI, et al. (2004)
DIPED 50ug/mL vs DMSO 12h 2Diisopropylethylenediamine0.0810.090.23Boshoff HI, et al. (2004)
H37Rv ctrl vs 2hr hypoxia rep 1Hypoxia-0.749.380.84Park HD, et al. (2003)
H37Rv ctrl vs 2hr hypoxia rep 2Hypoxia-1.179.741.17Park HD, et al. (2003)
H37Rv ctrl vs 2hr hypoxia rep 3Hypoxia-0.259.310.45Park HD, et al. (2003)
H37Rv ctrl vs 2hr hypoxia rep 4Hypoxia-0.199.590.32Park HD, et al. (2003)
H37Rv ctrl vs 2hr hypoxia rep 5Hypoxia-0.289.380.45Park HD, et al. (2003)
H37Rv ctrl vs 2hr hypoxia rep 6Hypoxia-0.318.820.51Park HD, et al. (2003)
Rv3133c/DosR mutant ctrl vs 2hr hypoxia rep 1Hypoxia-0.0510.750.18Park HD, et al. (2003)
Rv3133c/DosR mutant ctrl vs 2hr hypoxia rep 2Hypoxia-1.719.181.75Park HD, et al. (2003)
Rv3133c/DosR mutant ctrl vs 2hr hypoxia rep 3Hypoxia-0.9610.211.11Park HD, et al. (2003)
Rv3133c/DosR mutant ctrl vs 2hr hypoxia rep 4Hypoxia-0.249.550.39Park HD, et al. (2003)
Rv3133c/DosR mutant ctrl vs 2hr hypoxia rep 5Hypoxia-0.369.330.56Park HD, et al. (2003)
Rv3133c/DosR mutant ctrl vs 2hr hypoxia rep 6Hypoxia-0.378.240.56Park HD, et al. (2003)
H37Rv 0.2% Oxygen (2h) 1Hypoxia-0.088.750.19Sherman DR, et al. (2001)
H37Rv 0.2% Oxygen (2h) 2Hypoxia-0.335.260.38Sherman DR, et al. (2001)
H37Rv 0.2% Oxygen (2h) 3Hypoxia-0.155.630.24Sherman DR, et al. (2001)
H37Rv 0.2% Oxygen (2h) 4Hypoxia-0.465.750.49Sherman DR, et al. (2001)
H37Rv 0.2% Oxygen (2h) 5Hypoxia-0.056.420.14Sherman DR, et al. (2001)
H37Rv 0.2% Oxygen (2h) 6Hypoxia-0.076.150.13Sherman DR, et al. (2001)
MTB1254 Day 0 vs low Oxygen Day 4 rep 1Hypoxia-0.428.780.70Voskuil MI, et al. (2003)
MTB1254 Day 0 vs low Oxygen Day 4 rep 2Hypoxia-0.5210.220.66Voskuil MI, et al. (2003)
MTB1254 Day 0 vs low Oxygen Day 4 rep 3Hypoxia-0.289.930.40Voskuil MI, et al. (2003)
MTB1254 Day 0 vs low Oxygen Day 4 rep 4Hypoxia-0.449.520.70Voskuil MI, et al. (2004)
MTB1254 Day 0 vs low Oxygen Day 4 rep 5Hypoxia0.159.800.07Voskuil MI, et al. (2004)
MTB1254 Day 0 vs low Oxygen Day 4 rep 6Hypoxia-0.169.430.23Voskuil MI, et al. (2004)
NRP Day6: 1Non-replicating persistence-0.167.370.34Voskuil MI, et al. (2004)
NRP Day6: 2Non-replicating persistence-0.219.080.29Voskuil MI, et al. (2004)
NRP Day6: 3Non-replicating persistence-0.707.220.73Voskuil MI, et al. (2004)
NRP Day8: 1Non-replicating persistence-0.237.830.44Voskuil MI, et al. (2004)
NRP Day8: 2Non-replicating persistence-0.8410.300.78Voskuil MI, et al. (2004)
NRP Day8: 3Non-replicating persistence-0.827.170.71Voskuil MI, et al. (2004)
NRP Day10: 1Non-replicating persistence-0.036.780.08Voskuil MI, et al. (2004)
NRP Day10: 2Non-replicating persistence-0.939.870.72Voskuil MI, et al. (2004)
NRP Day10: 3Non-replicating persistence-1.116.420.99Voskuil MI, et al. (2004)
NRP Day12: 1Non-replicating persistence-0.207.440.36Voskuil MI, et al. (2004)
NRP Day12: 2Non-replicating persistence-1.069.070.90Voskuil MI, et al. (2004)
NRP Day12: 3Non-replicating persistence-1.336.781.09Voskuil MI, et al. (2004)
NRP Day14: 1Non-replicating persistence-1.1210.281.03Voskuil MI, et al. (2004)
NRP Day14: 2Non-replicating persistence-0.969.940.77Voskuil MI, et al. (2004)
NRP Day14: 3Non-replicating persistence-0.189.860.28Voskuil MI, et al. (2004)
NRP Day14: 4Non-replicating persistence-1.229.600.96Voskuil MI, et al. (2004)
NRP Day14: 5Non-replicating persistence-0.2810.530.36Voskuil MI, et al. (2004)
NRP Day14: 6Non-replicating persistence-2.049.341.33Voskuil MI, et al. (2004)
NRP Day14: 7Non-replicating persistence-1.987.331.55Voskuil MI, et al. (2004)
NRP Day14: 8Non-replicating persistence-0.317.300.37Voskuil MI, et al. (2004)
NRP Day14: 9Non-replicating persistence-0.407.300.46Voskuil MI, et al. (2004)
NRP Day20: 1Non-replicating persistence-0.988.510.67Voskuil MI, et al. (2004)
NRP Day20: 2Non-replicating persistence-1.288.520.78Voskuil MI, et al. (2004)
NRP Day30: 1Non-replicating persistence0.4010.160.05Voskuil MI, et al. (2004)
NRP Day30: 2Non-replicating persistence-1.708.640.80Voskuil MI, et al. (2004)
NRP Day80: 1Non-replicating persistence-0.786.630.40Voskuil MI, et al. (2004)
NRP Day80: 2Non-replicating persistence-0.569.110.32Voskuil MI, et al. (2004)
NRP Day80: 3Non-replicating persistence-0.868.410.40Voskuil MI, et al. (2004)
NRP Day80: 4Non-replicating persistence0.487.700.03Voskuil MI, et al. (2004)
NRP Day80: 5Non-replicating persistence-0.786.630.40Voskuil MI, et al. (2004)
MTB1254 Day 0 rep 1Growth curve0.019.900.04Voskuil MI, et al. (2004)
MTB1254 Day 0 rep 2Growth curve-0.009.650.04Voskuil MI, et al. (2004)
MTB1254 Day 0 rep 3Growth curve0.4510.311.07Voskuil MI, et al. (2003)
MTB1254 Day6:1Growth curve-0.049.390.12Voskuil MI, et al. (2004)
MTB1254 Day6:2Growth curve-0.109.680.24Voskuil MI, et al. (2004)
MTB1254 Day6:3Growth curve-0.608.560.75Voskuil MI, et al. (2004)
MTB1254 Day8:1Growth curve-0.569.080.88Voskuil MI, et al. (2004)
MTB1254 Day8:2Growth curve-0.349.830.65Voskuil MI, et al. (2004)
MTB1254 Day8:3Growth curve-1.169.481.25Voskuil MI, et al. (2004)
MTB1254 Day14:1Growth curve-0.669.110.66Voskuil MI, et al. (2004)
MTB1254 Day14:2Growth curve-0.728.971.00Voskuil MI, et al. (2004)
MTB1254 Day14:3Growth curve-1.419.301.19Voskuil MI, et al. (2004)
MTB1254 Day24:1Growth curve-1.209.580.77Voskuil MI, et al. (2004)
MTB1254 Day24:2Growth curve-0.598.790.56Voskuil MI, et al. (2004)
MTB1254 Day24:3Growth curve-0.988.750.65Voskuil MI, et al. (2004)
MTB1254 Day24:4Growth curve-1.295.461.08Voskuil MI, et al. (2004)
MTB1254 Day60:1Growth curve0.6410.130.28Voskuil MI, et al. (2004)
MTB1254 Day60:2Growth curve0.339.470.14Voskuil MI, et al. (2004)
MTB1254 Day60:3Growth curve0.649.130.41Voskuil MI, et al. (2004)
H37Rv whiB7 null ethanol vs. 1.0 ug/ml Tetracyclin for 15 min rep 1Tetracycline0.528.000.80Morris RP, et al. (2005)
H37Rv whiB7 null ethanol vs. 1.0 ug/ml Tetracyclin for 15 min rep 2Tetracycline-0.098.030.22Morris RP, et al. (2005)
H37Rv whiB7 null ethanol vs. 1.0 ug/ml Tetracyclin for 2 hr rep 1Tetracycline-0.568.800.63Morris RP, et al. (2005)
H37Rv whiB7 null ethanol vs. 1.0 ug/ml Tetracyclin for 2 hr rep 2Tetracycline-0.538.480.57Morris RP, et al. (2005)
H37Rv whiB7 null ethanol vs. 1.0 ug/ml Tetracyclin for 24 hr rep 1Tetracycline-0.648.070.56Morris RP, et al. (2005)
H37Rv whiB7 null ethanol vs. 1.0 ug/ml Tetracyclin for 24 hr rep 2Tetracycline-0.027.150.05Morris RP, et al. (2005)
H37Rv whiB7 null ethanol vs. 1.0 ug/ml Tetracyclin for 24 hr rep 3Tetracycline-0.627.150.41Morris RP, et al. (2005)
H37Rv whiB7 null ethanol vs. 1.0 ug/ml Tetracyclin for 2 hr rep 3Tetracycline-0.658.170.68Morris RP, et al. (2005)
H37Rv whiB7 null ethanol vs. 1.0 ug/ml Tetracyclin for 24 hr rep 4Tetracycline-0.658.240.57Morris RP, et al. (2005)
H37Rv whiB7 null ethanol vs. 1.0 ug/ml Tetracyclin for 2 hr rep 4Tetracycline-0.547.880.65Morris RP, et al. (2005)
H37Rv whiB7 null ethanol vs. 1.0 ug/ml Tetracyclin for 15 min rep 3Tetracycline-0.328.760.65Morris RP, et al. (2005)
H37Rv whiB7 null ethanol vs. 1.0 ug/ml Tetracyclin for 15 min rep 4Tetracycline0.509.160.63Morris RP, et al. (2005)
DIPED (50ug/mL)/DMSO, 12hDiisopropylethylenediamine0.158.570.29Boshoff HI, et al. (2004)
DIPED (100ug/mL)/DMSO, 12h. 1Diisopropylethylenediamine0.128.290.28Boshoff HI, et al. (2004)
DIPED (100ug/mL)/DMSO, 12h. 2Diisopropylethylenediamine0.389.240.55Boshoff HI, et al. (2004)
DIPED (100ug/mL)/DMSO, 12h. 3Diisopropylethylenediamine0.549.400.70Boshoff HI, et al. (2004)
EMB (10ug/mL)/DMSO, 12hEthambutol0.0110.580.01Boshoff HI, et al. (2004)
#241 (0.1ug/mL)/DMSO, 12h. 1 (GEO acc=GSM28046)Drug #2410.059.840.16Boshoff HI, et al. (2004)
#241 (1ug/mL)/DMSO, 12h. 1Drug #241-0.1210.450.23Boshoff HI, et al. (2004)
#241 (10ug/mL)/DMSO, 12h. 1Drug #241-0.399.280.45Boshoff HI, et al. (2004)
#241 (10ug/mL)/DMSO, 12h. 2Drug #241-0.349.460.33Boshoff HI, et al. (2004)
#109 (0.1ug/mL) vs DMSO, 12h (GEO acc=GSM28050)Drug #1090.5310.141.12Boshoff HI, et al. (2004)
#109 (1ug/mL) vs DMSO, 12h, replicate 1 (GEO ac=GSM28051)Drug #1090.4110.110.95Boshoff HI, et al. (2004)
#109 (1ug/mL) vs DMSO, 12h, replicate 2 (GEO acc=GSM28052)Drug #1090.099.680.28Boshoff HI, et al. (2004)
#109 (10ug/mL) vs DMSO, 12h, replicate 1 (GEO acc= GSM28053)Drug #109-0.258.650.18Boshoff HI, et al. (2004)
#109 (10ug/mL)/DMSO, 12h, replicate 2 (GEO acc= GSM28054)Drug #109-0.029.620.01Boshoff HI, et al. (2004)
20ug/mL Cephalexin/Ctrl, 6h. 1Cephalexin0.0110.820.06Boshoff HI, et al. (2004)
20ug/mL Cephalexin/Ctrl, 6h. 2Cephalexin-0.0310.490.07Boshoff HI, et al. (2004)
WT t=6h/WT t=0h. 1Starvation-0.857.710.55Boshoff HI, et al. (2004)
WT t=6h/WT t=0h. 2Starvation-0.857.790.38Boshoff HI, et al. (2004)
WT t=0h/WT t=6h. 1Starvation1.519.361.24Boshoff HI, et al. (2004)
WT t=0h/WT t=6h. 2Starvation0.828.300.66Boshoff HI, et al. (2004)
1ug/mL #121940/DMSO, 12hDrug #121940-0.049.530.05Boshoff HI, et al. (2004)
1ug/mL #111891/DMSO, 12h. 1Drug #111891-0.0910.520.18Boshoff HI, et al. (2004)
1ug/mL #111891/DMSO, 12h. 2Drug #111891-0.4910.200.68Boshoff HI, et al. (2004)
10ug/mL clofazimine/DMSO, 6hClofazimine-1.049.611.20Boshoff HI, et al. (2004)
24ug/mL cltrmazole/DMS, 6h. 2Clotrimazole-0.069.520.12Boshoff HI, et al. (2004)
20ug/mL chlorprmz/DMSO, 6h. 1Chlorpromazine-1.099.790.95Boshoff HI, et al. (2004)
2.5mM Dinitrophenol/DMSO, 6hDinitrophenol-1.169.200.88Boshoff HI, et al. (2004)
50ug/mL Thioridazine/DMSO, 6hThioridazine-1.008.280.61Boshoff HI, et al. (2004)
50ug/mL Triclosan/DMSO, 6hTriclosan-3.538.641.85Boshoff HI, et al. (2004)
20ug/mL Prcp 6776/DMSO, 6h. 1Procept 6776-2.769.072.23Boshoff HI, et al. (2004)
20ug/mL Prcp 6778/DMSO, 6h. 1Procept 67780.019.630.00Boshoff HI, et al. (2004)
100ug/mL Cephalexin/Ctrl, 6hCephalexin0.1611.460.26Boshoff HI, et al. (2004)
50ug/mL Triclosan/EtOHTriclosan-2.708.901.71Boshoff HI, et al. (2004)
10ug/mL #109/DMSO, 6hDrug #109-1.059.211.14Boshoff HI, et al. (2004)
10ug/mL #59/DMSO, 6hDrug #59-0.839.370.95Boshoff HI, et al. (2004)
20ug/mL ethambutol/DMSOEthambutol-0.449.700.87Boshoff HI, et al. (2004)
10ug/mL #241/DMSO, 6hDrug #241-1.288.730.79Boshoff HI, et al. (2004)
24ug/mL Econazole/DMSO, 6h. 1Econazole-0.319.100.59Boshoff HI, et al. (2004)
24ug/mL Econazole/DMSO, 6h. 2Econazole-0.149.030.26Boshoff HI, et al. (2004)
20ug/mL Prcp 6778/DMSO, 6h. 2Procept 6778-0.3210.150.54Boshoff HI, et al. (2004)
Succinate/7H9-based medium. 1Succinate-1.807.031.58Boshoff HI, et al. (2004)
Succinate/7H9-based medium. 2Succinate-1.318.241.23Boshoff HI, et al. (2004)
13ug/mL clfzine/DMSO, 6h. 1Clofazimine-0.867.830.98Boshoff HI, et al. (2004)
13ug/mL clfzine/DMSO, 6h. 2Clofazimine-1.018.551.30Boshoff HI, et al. (2004)
24ug/mL cltrmazole/DMS, 6h. 1Clotrimazole0.269.300.40Boshoff HI, et al. (2004)
24ug/mL cltrmazole/DMS, 6h. 3Clotrimazole0.178.470.40Boshoff HI, et al. (2004)
20ug/mL chlorprmz/DMSO, 6h. 2Chlorpromazine-1.527.681.91Boshoff HI, et al. (2004)
0.4ug/ml PA-824 vs DMSO 6hrs rep 1PA 824-0.619.020.80Boshoff HI, et al. (2004)
0.4ug/ml PA-824 vs DMSO 6hrs rep 2PA 824-2.028.622.26Fu LM and Tai SC (2009)
2ug/ml PA-824 vs DMSO 6hrs rep 1PA 824-0.859.790.41Fu LM and Tai SC (2009)
2ug/ml PA-824 vs DMSO 6hrs rep 2PA 824-3.598.942.40Boshoff HI, et al. (2004)
0.2ug/ml PA-824 vs DMSO 6hrs rep 1PA 824-2.069.532.45Boshoff HI, et al. (2004)
0.4ug/ml PA-824 vs DMSO 6hrs rep 3PA 824-3.319.042.24Boshoff HI, et al. (2004)
0.2ug/ml PA-824 vs DMSO 6hrs rep 2PA 824-1.839.352.41Boshoff HI, et al. (2004)
0.4ug/ml PA-824 vs DMSO 6hrs rep 4PA 824-2.998.832.18Boshoff HI, et al. (2004)
10uM CCCP/DMSO, 6hCarbonyl cyanide chlorophenylhydrazone-0.297.400.48Boshoff HI, et al. (2004)
100ug/mL Cphx/DMSO, 6hCephalexin0.048.920.00Boshoff HI, et al. (2004)
100uM DCCD/DMSO, 6hDicyclohexylcarboxidiimide-2.506.971.20Boshoff HI, et al. (2004)
1mM DNP/DMSO, 6h. 1Dinitrophenol-2.547.181.44Boshoff HI, et al. (2004)
20ug/ml KCN vs DMSO 6hrsPotassium cyanide-2.846.941.75Boshoff HI, et al. (2004)
100ug/mL Ceph/DMSO, 6hCephalexin0.189.330.31Boshoff HI, et al. (2004)
10ug/mL TRZ/DMSO, 6h. 1Thioridazine-1.127.781.05Boshoff HI, et al. (2004)
10ug/mL Nvb/DMSO, 6h. 2Novobiocin-0.898.370.80Boshoff HI, et al. (2004)
5ug/ml KCN vs DMSO 6hrs rep 1Potassium cyanide-1.178.191.11Manjunatha U, et al. (2009)
0.5mM DNP/DMSO, 6hDinitrophenol-0.208.970.19Boshoff HI, et al. (2004)
20uM DCCD/DMSO, 6h. 1Dicyclohexylcarboxidiimide-2.696.471.39Boshoff HI, et al. (2004)
50uM CCCP/DMSO, 6h. 1Carbonyl cyanide chlorophenylhydrazone-3.067.391.87Boshoff HI, et al. (2004)
Palmitate/Glucose. 1Palmitate-0.407.830.61Boshoff HI, et al. (2004)
Palmitate/Glucose. 2Succinate0.407.470.41Boshoff HI, et al. (2004)
50uM CCCP/DMSO, 6h. 2Carbonyl cyanide chlorophenylhydrazone-2.767.782.23Boshoff HI, et al. (2004)
20uM DCCD/DMSO, 6h. 2Dicyclohexylcarboxidiimide-1.348.530.74Boshoff HI, et al. (2004)
5ug/ml KCN vs DMSO 6hrs rep 2Potassium cyanide-1.018.060.96Manjunatha U, et al. (2009)
10ug/mL Nvb/DMSO, 6h. 3Novobiocin-1.067.701.00Boshoff HI, et al. (2004)
10ug/mL TRZ/DMSO, 6h. 2Thioridazine-1.278.011.34Boshoff HI, et al. (2004)
10mM Succinate/10mM Gluc. 1Streptomycin0.276.620.21Boshoff HI, et al. (2004)
0.05mM Palmitate/10mM Gluc. 1Palmitate-0.566.920.70Boshoff HI, et al. (2004)
1mM DNP/DMSO, 6h. 2Dinitrophenol-3.456.031.87Boshoff HI, et al. (2004)
25ug/mL TRZ/DMSO, 6hThioridazine-1.716.111.28Boshoff HI, et al. (2004)
10ug/mL Nvb/DMSO, 6h. 1Novobiocin-0.918.041.09Boshoff HI, et al. (2004)
10mM Succinate/10mM Gluc. 25-chloro-pyrazinamide0.468.560.95Boshoff HI, et al. (2004)
0.05mM Palmitate/10mM Gluc. 2Palmitate0.479.080.82Boshoff HI, et al. (2004)
0.2ug/mL Mtm:ctrl (4h). 1Mitomycin1.278.251.47Boshoff HI, et al. (2004)
0.2ug/mL Mtm:ctrl (4h). 2Mitomycin0.188.190.28Boshoff HI, et al. (2004)
4mM H2O2:ctrl (2h). 1H2O2-0.313.510.11Boshoff HI, et al. (2004)
4mM H2O2:ctrl (2h). 2H2O2-0.498.260.51Boshoff HI, et al. (2004)
4mM H2O2:ctrl (4h). 1H2O2-0.538.401.01Boshoff HI, et al. (2004)
4mM H2O2:ctrl (4h). 2H2O2-0.687.830.80Boshoff HI, et al. (2004)
25J UV:ctrl (2h)Ultraviolet (UV) light-0.239.260.72Boshoff HI, et al. (2004)
60J UV:ctrl (2h)Ultraviolet (UV) light-0.049.030.20Boshoff HI, et al. (2004)
0.12mg/mL PZA:pH5.6 (2h)Pyrazinamide-0.367.920.41Boshoff HI, et al. (2004)
1.2mg/mL PZA:pH5.6 (2h).Pyrazinamide0.038.150.07Boshoff HI, et al. (2004)
0.12mg/mL PZA:pH5.6 (2.5h)Pyrazinamide-0.617.510.78Boshoff HI, et al. (2004)
0.12mg/mL PZA:pH5.6 (4h) 1Pyrazinamide-0.047.780.03Boshoff HI, et al. (2004)
0.12mg/mL PZA:pH5.6 (4h) 2Pyrazinamide-0.358.310.36Boshoff HI, et al. (2004)
1.2mg/mL PZA:pH5.6 (5h)Pyrazinamide-0.089.850.19Boshoff HI, et al. (2004)
0.12mg/mL PZA:pH5.6 (5h)Pyrazinamide-0.148.570.24Boshoff HI, et al. (2004)
0.12mg/mL Nam:pH5.6 (2h) 1Sodium azide0.038.100.01Boshoff HI, et al. (2004)
0.12mg/mL Nam:pH5.6 (2h) 2Sodium azide0.278.460.33Boshoff HI, et al. (2004)
0.12mg/mL Nam:pH5.6 (4h) 1Sodium azide-0.347.820.38Boshoff HI, et al. (2004)
0.12mg/mL Nam:pH5.6 (4h) 2Sodium azide-0.087.990.07Boshoff HI, et al. (2004)
0.12mg/mL BZA:pH5.6 (2h)Benzamide-0.027.530.02Boshoff HI, et al. (2004)
0.12mg/mL BZA:pH5.6 (4h) 1Benzamide0.367.200.46Boshoff HI, et al. (2004)
0.12mg/mL BZA:pH5.6 (4h) 2Benzamide0.488.290.45Boshoff HI, et al. (2004)
40ug/mL 5CL:pH5.6 (2h) 15-chloro-pyrazinamide-0.527.290.57Boshoff HI, et al. (2004)
80ug/mL 5CL:pH5.6 (2h)5-chloro-pyrazinamide-0.237.380.32Boshoff HI, et al. (2004)
40ug/mL 5CL:pH5.6 (2h) 25-chloro-pyrazinamide0.009.360.03Boshoff HI, et al. (2004)
40ug/mL 5CL:pH5.6 (4h) 15-chloro-pyrazinamide0.208.420.26Boshoff HI, et al. (2004)
40ug/mL 5CL:pH5.6 (4h) 25-chloro-pyrazinamide0.198.290.24Boshoff HI, et al. (2004)
40ug/mL 5CL:pH5.6 (4h) 35-chloro-pyrazinamide-0.767.750.72Boshoff HI, et al. (2004)
2mM ZnSO4/DMSO, 6hZinc sulfate0.7810.761.03Boshoff HI, et al. (2004)
5ug/mL CFZ+0.1mM GSNO/DMSO. 1Clofazimine + S-nitrosoglutathione-2.159.251.76Boshoff HI, et al. (2004)
0.1mM GSNO/DMSO, 3.5hS-nitrosoglutathione0.8410.211.00Boshoff HI, et al. (2004)
0.2mM NaN3/DMSOSodium azide0.0810.130.06Boshoff HI, et al. (2004)
25ug/mLCPZ+0.1mMGSNO/DMSO. 2S-nitrosoglutathione + Chlorpromazine-2.348.271.29Boshoff HI, et al. (2004)
10ug/mLmdn+0.1mMGSNO/DMSO. 1S-nitrosoglutathione + Menadione0.298.680.01Boshoff HI, et al. (2004)
0.4mM NaN3/DMSOSodium azide-1.149.180.75Boshoff HI, et al. (2004)
25ug/mL CPZ/DMSO, 6hChlorpromazine-4.216.851.82Boshoff HI, et al. (2004)
0.1mM GSNO/DMSO, 6hS-nitrosoglutathione5.678.563.40Boshoff HI, et al. (2004)
5ug/mL CFZ+0.1mM GSNO/DMSO. 2Clofazimine + S-nitrosoglutathione-1.247.610.78Boshoff HI, et al. (2004)
25ug/mLCPZ+0.1mMGSNO/DMSO. 3S-nitrosoglutathione + Chlorpromazine-1.868.331.06Boshoff HI, et al. (2004)
10ug/mLmdn+0.1mMGSNO/DMSO. 2S-nitrosoglutathione + Menadione0.689.140.58Boshoff HI, et al. (2004)
PBS/Tween/7H9PBS + Tween 80-2.118.681.32Boshoff HI, et al. (2004)
0.2ug/mL #111891/DMSO, 5.5h. 1Drug #1118910.399.940.80Boshoff HI, et al. (2004)
0.2ug/mL #111891/DMSO, 5.5h. 2Drug #1118910.469.530.90Boshoff HI, et al. (2004)
0.2ug/mL #111891/DMSO, 5.5h. 3Drug #111891-0.119.100.26Boshoff HI, et al. (2004)
10mM succinatevs10mM glucoseStreptomycin0.288.500.44Boshoff HI, et al. (2004)
0.05mM palmitatevs10mM glucPalmitate-0.378.050.50Boshoff HI, et al. (2004)
10ug/mLMethoxatinvsDMSO,6hMethoxatin0.078.200.17Boshoff HI, et al. (2004)
0.1mM GSNO + 5ug/ml KCN vs DMSO 6hrs rep 1S-nitrosoglutathione + Potassium cyanide-0.876.080.68Boshoff HI, et al. (2004)
0.1mM GSNOvsDMSO, 6h S-nitrosoglutathione0.199.100.35Boshoff HI, et al. (2004)
7d Dubos NRP-1vsDubos log phase ANon-replicating persistence-1.705.241.10Boshoff HI, et al. (2004)
7d Dubos NRP-1vsDubos log phaseNon-replicating persistence-1.437.091.73Boshoff HI, et al. (2004)
20ug/mL methoxatinvsDMSO, 6hMethoxatin0.5110.000.85Boshoff HI, et al. (2004)
10ug/mL methoxatinvsDMSO, 6h AMethoxatin0.538.650.98Boshoff HI, et al. (2004)
0.1mM GSNOvsDMSO, 6h AS-nitrosoglutathione0.2410.020.23Boshoff HI, et al. (2004)
0.1mM GSNO + 5ug/ml KCN vs DMSO 6hrs rep 2S-nitrosoglutathione + Potassium cyanide-0.728.200.72Boshoff HI, et al. (2004)
Dubos NRP-1vsDubos log-phaseNon-replicating persistence-1.8510.611.66Boshoff HI, et al. (2004)
1mM DTNBvsDMSO, 6hDithiobis nitrobenzoic acid0.4110.640.81Boshoff HI, et al. (2004)
2mM DTTvsDMSO, 6hDTT-1.967.281.81Boshoff HI, et al. (2004)
1uM ValinomycinvsDMSO, 6hValinomycin-0.369.690.28Boshoff HI, et al. (2004)
10uM ValinomycinvsDMSO, 6hValinomycin-0.3810.430.26Boshoff HI, et al. (2004)
2mMb-mercaptoethanolvsDMSO,6hMercaptoethanol0.3210.340.72Boshoff HI, et al. (2004)
2mM DTNBvsDMSODithiobis nitrobenzoic acid0.039.890.05Boshoff HI, et al. (2004)
2mM DTTvsDMSO, 6h ADTT-0.589.240.81Boshoff HI, et al. (2004)
50uM NigericinvsDMSO, 6hNigericin1.219.382.15Boshoff HI, et al. (2004)
1uM ValinomycinvsDMSO, 6h AValinomycin0.409.450.38Boshoff HI, et al. (2004)
50ug/mL VerapamilvsDMSO, 6hVerapamil-0.039.450.08Boshoff HI, et al. (2004)
1uM ValinomycinvsDMSO, 6h BValinomycin-0.388.680.23Boshoff HI, et al. (2004)
20ug/mL CPZvsDMSO, 6hChlorpromazine-1.258.701.49Boshoff HI, et al. (2004)
PBS/Tw/DMSOvs7H9, 6hPBS + Tween 80 + DMSO-1.628.201.77Boshoff HI, et al. (2004)
10ug/mL menadionevsDMSO, 6hMenadione-0.429.410.43Boshoff HI, et al. (2004)
0.1mMGSNO/20ug/mLCPZvsDMSO,6hS-nitrosoglutathione + Chlorpromazine-0.838.621.06Boshoff HI, et al. (2004)
0.1mMGSNO/10ug/mLmdvsDMSO,6hS-nitrosoglutathione + Menadione-0.179.450.23Boshoff HI, et al. (2004)
50uM CCCPvsDMSO, 6hCarbonyl cyanide chlorophenylhydrazone-1.398.631.36Boshoff HI, et al. (2004)
50uM NigericinvsDMSO, 6h ANigericin0.5910.360.64Boshoff HI, et al. (2004)
0.5uMValinomycinvsDMSO,6hValinomycin0.229.570.18Boshoff HI, et al. (2004)
0.5uMValinomycin/70mMKClvsDMSO,6hValinomycin-0.969.430.72Boshoff HI, et al. (2004)
0.1mMGSNO/20ug/mLCPZvsDMSO,6hAS-nitrosoglutathione + Chlorpromazine-0.529.700.43Boshoff HI, et al. (2004)
0.1mMGSNO/10ug/mLmdvsDMSO,6hAS-nitrosoglutathione + Menadione-0.089.490.09Boshoff HI, et al. (2004)
20ug/mL CPZvsDMSO, 6h AChlorpromazine-1.129.231.07Boshoff HI, et al. (2004)
10ug/mLmnd(Dubos)vsDMSO,6hMenadione-0.309.960.40Boshoff HI, et al. (2004)
4d Dubos NRP-1vsDubos aeroNon-replicating persistence-0.419.150.34Boshoff HI, et al. (2004)
0.02mM GSNOvsDMSO, 6hS-nitrosoglutathione1.078.390.64Boshoff HI, et al. (2004)
25ug/mLCPZ+0.1mMGSNOvsDMSO AS-nitrosoglutathione + Chlorpromazine-3.945.971.87Boshoff HI, et al. (2004)
5ug/mLCFZ+0.1mMGSNOvsDMSOClofazimine + S-nitrosoglutathione-2.646.411.53Boshoff HI, et al. (2004)
PBS/Tween80/DMSOvsDMSO, 6hPBS + Tween 80 + DMSO-5.035.712.22Boshoff HI, et al. (2004)
4d Dubos NRP-1vsDubos aero ANon-replicating persistence-1.869.221.29Boshoff HI, et al. (2004)
25ug/mL CPZvsDMSO, 6h AChlorpromazine-1.588.410.98Boshoff HI, et al. (2004)
0.1mM GSNOvsDMSO, 4hS-nitrosoglutathione0.5710.170.80Boshoff HI, et al. (2004)
5ug/mLCFZ+0.1mMGSNOvsDMSO AClofazimine + S-nitrosoglutathione-1.248.981.26Boshoff HI, et al. (2004)
0.4mM NaN3vsDMSO, 4h ASodium azide0.0510.020.01Boshoff HI, et al. (2004)
25ug/mL CPZvsDMSO, 6h BChlorpromazine-2.688.521.28Boshoff HI, et al. (2004)
6ug/mL MenadionevsDMSO, 6hMenadione0.6510.680.46Boshoff HI, et al. (2004)
6ug/mLMnd+0.1mMGSNOvsDMSOS-nitrosoglutathione + Menadione2.029.371.26Boshoff HI, et al. (2004)
pH4.8vspH6.8 (4h)Acidified medium0.438.710.48Boshoff HI, et al. (2004)
pH4.8vspH6.8 (4h)AAcidified medium0.398.740.38Boshoff HI, et al. (2004)
pH4.8vspH6.8 (4h)BAcidified medium0.498.460.55Boshoff HI, et al. (2004)
pH4.8vspH6.8 (5h)Acidified medium0.1910.660.15Boshoff HI, et al. (2004)
pH4.8vspH6.8 (5.5h)Acidified medium0.0310.040.01Boshoff HI, et al. (2004)
pH4.8vspH6.8 (6h)Acidified medium-0.448.250.55Boshoff HI, et al. (2004)
pH5.2vspH6.8 (5h)Acidified medium-0.5510.500.67Boshoff HI, et al. (2004)
pH5.2vspH6.8 (10.5h)Acidified medium-0.629.630.92Boshoff HI, et al. (2004)
20mJ UVvsctrl (6h)Ultraviolet (UV) light0.539.540.78Boshoff HI, et al. (2004)
40mJ UV:ctrl (6h)Ultraviolet (UV) light0.318.600.37Boshoff HI, et al. (2004)
5ug/ml Rifampicin vs DMSO 2.5hrsRifampicin-0.3910.420.42Boshoff HI, et al. (2004)
Rif(5ug/mL)vsDMSO,2.5hARifampicin-0.137.890.10Boshoff HI, et al. (2004)
Rif(0.5ug/mL)vsDMSO,2.5hRifampicin-0.5210.561.09Boshoff HI, et al. (2004)
Rif(0.5ug/mL)vsDMSO,2.5hARifampicin-0.409.860.76Boshoff HI, et al. (2004)
10ug/mL Amikacin:EtOH, 6hAmikacin-0.589.020.42Boshoff HI, et al. (2004)
5ug/ml Streptomycin vs Ethanol 6hrsStreptomycin0.3510.620.20Boshoff HI, et al. (2004)
5ug/mLStreptomycinvsEtOH,6hAStreptomycin0.2210.540.13Boshoff HI, et al. (2004)
0.2ug/ml Isoniazid vs Ethanol 6hrs rep 3Isoniazid0.6011.010.83Manjunatha U, et al. (2009)
0.2mg/ml Ampicillin vs Ethanol 6hrsAmpicillin0.2810.110.42Boshoff HI, et al. (2004)
0.2mg/mL AmpvsEtOH, 6hAAmpicillin0.3510.540.51Boshoff HI, et al. (2004)
12ug/ml Ethionamide vs Ethanol 6hrs rep 1Ethionamide0.5010.220.63Boshoff HI, et al. (2004)
12ug/ml Ethionamide vs Ethanol 6hrs rep 2Ethionamide0.449.810.62Boshoff HI, et al. (2004)
0.13mg/ml TLM vs DMSO 6hrs rep 1Thiolactomycin0.4310.020.56Manjunatha U, et al. (2009)
0.13mg/ml TLM vs DMSO 6hrs rep 2Thiolactomycin0.2810.160.39Boshoff HI, et al. (2004)
0.1mg/mLTriclosanvsEtOH,6hBTriclosan0.4910.720.71Boshoff HI, et al. (2004)
0.1mg/mLTriclosanvsEtOH,6hCTriclosan0.6210.821.08Boshoff HI, et al. (2004)
10ug/mL OfloxvsDMSO, 6hOfloxacin0.399.950.56Boshoff HI, et al. (2004)
10ug/mL OfloxvsDMSO, 6hAOfloxacin0.3710.650.34Boshoff HI, et al. (2004)
5ug/mL AmivsEtOH, 6hAmikacin-0.4210.400.54Boshoff HI, et al. (2004)
5ug/mL AmivsEtOH, 6hAAmikacin-0.5510.030.45Boshoff HI, et al. (2004)
40ug/ml Ethionamide vs Ethanol 6hrs rep 1Ethionamide0.1811.440.20Boshoff HI, et al. (2004)
40ug/ml Ethionamide vs Ethanol 6hrs rep 2Ethionamide0.1912.090.06Boshoff HI, et al. (2004)
0.2ug/ml Isoniazid vs Ethanol 6hrs rep 1Isoniazid-0.2112.110.44Boshoff HI, et al. (2004)
0.2ug/ml Isoniazid vs Ethanol 6hrs rep 2Isoniazid-0.0611.130.09Boshoff HI, et al. (2004)
5ug/mL OfloxvsEtOH, 6hOfloxacin0.0911.200.02Boshoff HI, et al. (2004)
5ug/mL OfloxvsEtOH, 6hAOfloxacin0.0810.480.05Boshoff HI, et al. (2004)
0.2ug/mL RifvsDMSO, 6hRifampicin-1.388.290.85Boshoff HI, et al. (2004)
0.2ug/mL RifvsDMSO, 6hARifampicin-0.688.520.44Boshoff HI, et al. (2004)
2ug/mL SMvsEtOH, 6hStreptomycin-0.0610.960.16Boshoff HI, et al. (2004)
2ug/mL SMvsEtOH, 6hAStreptomycin0.1310.820.20Boshoff HI, et al. (2004)
10ug/mL TetvsEtOH, 6hTetracycline-2.4210.501.70Boshoff HI, et al. (2004)
10ug/mL TetvsEtOH, 6hATetracycline-2.229.521.53Boshoff HI, et al. (2004)
130ug/ml TLM vs DMSO 6hrs rep 1Thiolactomycin-0.2011.330.34Boshoff HI, et al. (2004)
130ug/ml TLM vs DMSO 6hrs rep 2Thiolactomycin-0.2311.370.37Manjunatha U, et al. (2009)
0.2mg/mL AmpvsEtOH, 6hBAmpicillin0.3211.520.92Boshoff HI, et al. (2004)
0.2mg/mL AmpvsEtOH, 6hCAmpicillin0.1312.480.21Boshoff HI, et al. (2004)
5ug/mL TetvsEtOH, 6hTetracycline0.4810.700.64Boshoff HI, et al. (2004)
0.2mg/ml TLM vs Ethanol 6hrs rep 1Thiolactomycin0.1811.080.31Manjunatha U, et al. (2009)
0.2mg/ml TLM vs Ethanol 6hrs rep 2Thiolactomycin0.0810.980.10Manjunatha U, et al. (2009)
0.15mg/mL TricvsEtOH, 6hATriclosan-0.3411.050.37Boshoff HI, et al. (2004)
0.15mg/mL TricvsEtOH, 6hTriclosan-0.4410.450.28Boshoff HI, et al. (2004)
10ug/ml capreomycin vs Ethanol 6hrsCapreomycin-0.1411.660.19Boshoff HI, et al. (2004)
10ug/mL CapvsEtOH, 6hCapreomycin-0.379.620.27Boshoff HI, et al. (2004)
10ug/mL LevovsEtOH, 6hLevofloxacin0.0712.590.05Boshoff HI, et al. (2004)
10ug/mL LevovsEtOH, 6hALevofloxacin-0.0010.470.12Boshoff HI, et al. (2004)
0.5ug/mLRifapentinevsEtOH,6hRifapentine0.0311.390.27Boshoff HI, et al. (2004)
0.5ug/mLRifapentinevsEtOH,6hARifapentine0.1810.960.42Boshoff HI, et al. (2004)
50ug/mL RoxvsEtOH, 6hRoxithromycin-0.1010.790.09Boshoff HI, et al. (2004)
50ug/mL RoxvsEtOH, 6hARoxithromycin-0.2410.340.11Boshoff HI, et al. (2004)
0.1mg/mL TriclosanvsEtOH, 6hTriclosan0.0410.770.21Boshoff HI, et al. (2004)
0.1mg/mL TriclosanvsEtOH, 6hATriclosan-0.4311.340.46Boshoff HI, et al. (2004)
5ug/ml Capreomycin vs Ethanol 6hrs ACapreomycin0.1910.380.20Fu LM and Tai SC (2009)
5ug/mL CapvsEtOH, 6hCapreomycin0.1610.660.08Boshoff HI, et al. (2004)
0.32ug/mL Cerulenin vs Ethanol 6hrs rep 1Cerulenin0.389.780.56Manjunatha U, et al. (2009)
0.32ug/mL Cerulenin vs Ethanol 6hrs rep 2Cerulenin0.3611.390.50Boshoff HI, et al. (2004)
30ug/mL RoxvsEtOH, 6hRoxithromycin-0.2710.280.07Boshoff HI, et al. (2004)
30ug/mL RoxvsEtOH, 6hARoxithromycin-0.3110.210.01Boshoff HI, et al. (2004)
0.5ug/mL Cerulenin vs Ethanol, 6hrs rep 1Cerulenin0.2710.890.48Manjunatha U, et al. (2009)
0.5ug/mL Cerulenin vs Ethanol, 6hrs rep 2Cerulenin0.2811.280.39Manjunatha U, et al. (2009)
10ug/mL ChlorprovsEtOHChlorpromazine-0.2910.820.38Boshoff HI, et al. (2004)
10ug/mL ChlorprovsEtOH, 6hChlorpromazine-0.1910.390.26Boshoff HI, et al. (2004)
60ug/mL ChlorprovsEtOH, 6hChlorpromazine-0.799.360.49Boshoff HI, et al. (2004)
10ug/mL clotrimvsEtOH, 6hClotrimazole0.4011.220.72Boshoff HI, et al. (2004)
10ug/mL ClotrimvsEtOH, 6hAClotrimazole0.4011.180.75Boshoff HI, et al. (2004)
10ug/mL EconazolevsEtOH, 6hEconazole0.1910.340.29Boshoff HI, et al. (2004)
10ug/mL EconazolevsEtOH, 6hAEconazole0.0311.180.03Boshoff HI, et al. (2004)
0.1ug/mL RifpvsEtOH, 6hRifapentine-0.517.900.47Boshoff HI, et al. (2004)
0.1ug/mL RifpvsEtOH, 6hARifapentine-0.849.040.94Boshoff HI, et al. (2004)
10ug/mL RoxvsEtOH, 6hRoxithromycin-0.3810.940.29Boshoff HI, et al. (2004)
10ug/mL RoxvsEtOH, 6hARoxithromycin-0.7410.340.46Boshoff HI, et al. (2004)
100ug/mLCephalexinvsEtOH,6hCephalexin0.2312.380.41Boshoff HI, et al. (2004)
100ug/mLCephalexinvsEtOH,6hACephalexin0.3312.100.59Boshoff HI, et al. (2004)
50ug/mL TriclosanvsEtOH, 6hTriclosan-1.4010.431.22Boshoff HI, et al. (2004)
50ug/mL TriclosanvsEtOH, 6hATriclosan-1.1010.611.00Boshoff HI, et al. (2004)
100ug/mL TriclosanvsEtOH, 6hTriclosan-0.7010.130.59Boshoff HI, et al. (2004)
100ug/mL TriclosanvsEtOH, 6hATriclosan-1.4010.771.12Boshoff HI, et al. (2004)
10ug/mLchlorpromazinevsctrl,6hChlorpromazine0.3212.290.56Boshoff HI, et al. (2004)
10ug/mLchlorpromazinevsctrl,6hAChlorpromazine0.3812.230.68Boshoff HI, et al. (2004)
20ug/mL Procept 6776vsDMSO, 6hProcept 6776-0.2710.750.71Boshoff HI, et al. (2004)
0.5ug/mL #121940vsDMSO,6hDrug #1219400.3010.520.66Boshoff HI, et al. (2004)
0.5ug/mL #121940vsDMSO,6hADrug #1219400.2810.880.59Boshoff HI, et al. (2004)
0.5ug/mL #111891vsDMSO,6hDrug #1118910.1710.790.45Boshoff HI, et al. (2004)
0.5ug/mL #111891vsDMSO,6hADrug #1118910.1410.610.34Boshoff HI, et al. (2004)
0.5ug/mL #111895vsDMSO,6hDrug #111895-0.1010.370.18Boshoff HI, et al. (2004)
MTB strain 1254 Ctrl vs 0.5 mM DETA/NO 1hr rep 1Diethylenetriamine / nitric oxide adduct0.6011.341.15Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs 0.5 mM DETA/NO 1hr rep 2Diethylenetriamine / nitric oxide adduct-0.9812.701.19Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs 0.5 mM DETA/NO 1hr rep 3Diethylenetriamine / nitric oxide adduct-1.1212.621.68Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs 0.5 mM DETA/NO 1hr rep 4Diethylenetriamine / nitric oxide adduct-0.9812.841.06Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs 0.5 mM DETA/NO 2hrs rep 1Diethylenetriamine / nitric oxide adduct-1.1112.391.69Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs 0.5 mM DETA/NO 2hrs rep 2Diethylenetriamine / nitric oxide adduct-1.1812.861.01Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs 0.5 mM DETA/NO 2hrs rep 3Diethylenetriamine / nitric oxide adduct-0.6813.050.82Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs 0.5 mM DETA/NO 2hrs rep 4Diethylenetriamine / nitric oxide adduct-1.4513.131.29Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs 0.5 mM DETA/NO 5min rep 1Diethylenetriamine / nitric oxide adduct-0.2113.350.67Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs 0.5 mM DETA/NO 5min rep 2Diethylenetriamine / nitric oxide adduct-0.2713.450.57Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs 0.5 mM DETA/NO 5min rep 3Diethylenetriamine / nitric oxide adduct0.1813.890.17Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs 0.5 mM DETA/NO 5min rep 4Diethylenetriamine / nitric oxide adduct0.1313.380.08Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs 0.5 mM DETA/NO 8hrs rep 1Diethylenetriamine / nitric oxide adduct-1.2513.211.01Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs 0.5 mM DETA/NO 8hrs rep 2Diethylenetriamine / nitric oxide adduct-1.2212.501.29Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs 0.5 mM DETA/NO 8hrs rep 3Diethylenetriamine / nitric oxide adduct-1.4314.031.15Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs 0.5 mM DETA/NO 8hrs rep 4Diethylenetriamine / nitric oxide adduct-0.9213.150.78Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs 0.5 mM DETA/NO 16hrs rep 1Diethylenetriamine / nitric oxide adduct-1.2910.510.91Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs 0.5 mM DETA/NO 16hrs rep 2Diethylenetriamine / nitric oxide adduct-0.9311.250.71Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs 0.5 mM DETA/NO 16hrs rep 3Diethylenetriamine / nitric oxide adduct-0.5511.500.37Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs 0.5 mM DETA/NO 16hrs rep 4Diethylenetriamine / nitric oxide adduct-0.9412.850.74Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs 0.5 mM DETA/NO 20min rep 1Diethylenetriamine / nitric oxide adduct-0.6212.971.35Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs 0.5 mM DETA/NO 20min rep 2Diethylenetriamine / nitric oxide adduct-0.7513.071.18Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs 0.5 mM DETA/NO 20min rep 3Diethylenetriamine / nitric oxide adduct-0.2712.810.52Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs 0.5 mM DETA/NO 20min rep 4Diethylenetriamine / nitric oxide adduct-1.2812.911.52Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs 0.5 mM DETA/NO 24hrs rep 1Diethylenetriamine / nitric oxide adduct-1.3313.151.48Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs 0.5 mM DETA/NO 24hrs rep 2Diethylenetriamine / nitric oxide adduct-1.4314.121.29Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs 0.5 mM DETA/NO 24hrs rep 3Diethylenetriamine / nitric oxide adduct-0.9012.760.94Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs 0.5 mM DETA/NO 24hrs rep 4Diethylenetriamine / nitric oxide adduct-1.4911.791.53Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs 0.5 mM DETA/NO 24hrs + 0.5 mM DNO 40min rep 1Diethylenetriamine / nitric oxide adduct + Diethylenetriamine-nitric oxide-0.1611.930.16Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs 0.5 mM DETA/NO 24hrs + 0.5 mM DNO 40min rep 2Diethylenetriamine / nitric oxide adduct + Diethylenetriamine-nitric oxide-0.1510.430.18Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs 0.5 mM DETA/NO 24hrs + 0.5 mM DNO 40min rep 3Diethylenetriamine / nitric oxide adduct + Diethylenetriamine-nitric oxide-1.2212.940.94Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs 0.5 mM DETA/NO 24hrs + 0.5 mM DNO 40min rep 4Diethylenetriamine / nitric oxide adduct + Diethylenetriamine-nitric oxide-2.1011.651.52Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs 0.5 mM KCN 1hr rep 1Potassium cyanide-0.4113.440.49Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs 0.5 mM KCN 1hr rep 2Potassium cyanide-0.6813.220.75Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs 0.5 mM KCN 1hr rep 3Potassium cyanide-0.2512.970.28Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs 0.5 mM KCN 20min + 0.05 mM DETA/NO 40min rep 1Potassium cyanide + Diethylenetriamine / nitric oxide adduct-0.7913.180.82Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs 0.5 mM KCN 20min + 0.05 mM DETA/NO 40min rep 2Potassium cyanide + Diethylenetriamine / nitric oxide adduct-0.5013.300.65Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs 0.5 mM KCN 20min + 0.05 mM DETA/NO 40min rep 3Potassium cyanide + Diethylenetriamine / nitric oxide adduct-0.1812.200.20Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs 0.5 mM KCN + 2hr hypoxia rep 1Potassium cyanide-1.1810.410.88Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs 0.5 mM KCN + 2hr hypoxia rep 2Potassium cyanide-1.6812.841.28Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs 0.5 mM KCN + 2hr hypoxia rep 3Potassium cyanide-2.459.141.65Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs 2hr Hypoxia rep 3Hypoxia0.4113.540.25Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs high aeration + 0.001 mM DETA/NO rep 2Diethylenetriamine / nitric oxide adduct-0.049.840.28Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs high aeration + 0.001 mM DETA/NO rep 3Diethylenetriamine / nitric oxide adduct0.119.800.39Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs high aeration + 0.01 mM DETA/NO rep 2Diethylenetriamine / nitric oxide adduct0.099.010.00Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs high aeration + 0.01 mM DETA/NO rep 3Diethylenetriamine / nitric oxide adduct-0.056.740.22Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs high aeration + 0.005 mM DETA/NO rep 2Diethylenetriamine / nitric oxide adduct0.108.940.32Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs high aeration + 0.005 mM DETA/NO rep 3Diethylenetriamine / nitric oxide adduct-0.127.360.43Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs high aeration + 0.05 mM DETA/NO rep 2Diethylenetriamine / nitric oxide adduct-0.136.820.29Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs high aeration + 0.05 mM DETA/NO rep 3Diethylenetriamine / nitric oxide adduct0.0410.130.18Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs high aeration rep1 High aeration-0.2110.160.60Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs high aeration rep2High aeration-0.1510.480.38Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs high aeration rep3High aeration-0.1910.510.57Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs low aeration + 0.001 mM DETA/NO rep 2Diethylenetriamine / nitric oxide adduct-0.079.890.37Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs low aeration + 0.001 mM DETA/NO rep 3Diethylenetriamine / nitric oxide adduct0.059.890.04Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs low aeration + 0.01 mM DETA/NO rep 1Diethylenetriamine / nitric oxide adduct0.269.170.17Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs low aeration + 0.01 mM DETA/NO rep 2Diethylenetriamine / nitric oxide adduct0.1810.170.00Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs low aeration + 0.01 mM DETA/NO rep 3Diethylenetriamine / nitric oxide adduct0.5911.340.43Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs low aeration + 0.005 mM DETA/NO rep 1Diethylenetriamine / nitric oxide adduct-0.039.590.19Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs low aeration + 0.005 mM DETA/NO rep 2Diethylenetriamine / nitric oxide adduct-0.029.460.20Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs low aeration + 0.005 mM DETA/NO rep 3Diethylenetriamine / nitric oxide adduct0.4110.780.53Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs low aeration + 0.05 mM DETA/NO rep 1Diethylenetriamine / nitric oxide adduct-1.077.980.92Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs low aeration + 0.05 mM DETA/NO rep 2Diethylenetriamine / nitric oxide adduct-1.149.721.00Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs low aeration + 0.05 mM DETA/NO rep 3Diethylenetriamine / nitric oxide adduct-0.5210.800.58Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs low aeration (0.2% oxygen) 2hr rep 1Hypoxia0.1710.080.49Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs low aeration (0.2% oxygen) 2hr rep 2Hypoxia0.029.550.02Voskuil MI, et al. (2003)
MTB strain 1254 Ctrl vs low aeration (0.2% oxygen) 2hr rep 3Hypoxia0.1711.030.24Voskuil MI, et al. (2003)
CDC1551 Ctrl vs 0.05 mM DETA/NO 40 min rep 1Diethylenetriamine / nitric oxide adduct-0.0912.790.26Voskuil MI, et al. (2003)
CDC1551 Ctrl vs 0.05 mM DETA/NO 40 min rep 2Diethylenetriamine / nitric oxide adduct0.0014.240.21Voskuil MI, et al. (2003)
CDC1551 Ctrl vs 0.05 mM DETA/NO 40 min rep 3Diethylenetriamine / nitric oxide adduct-0.2111.570.50Voskuil MI, et al. (2003)
CDC1551 Ctrl vs 0.05 mM DETA/NO 40 min rep 4Diethylenetriamine / nitric oxide adduct-0.3011.620.69Voskuil MI, et al. (2003)
CDC1551 Ctrl vs 0.05 mM DETA/NO 40 min rep 5Diethylenetriamine / nitric oxide adduct-0.2110.750.37Voskuil MI, et al. (2003)
H37Rv Ctrl vs 0.05 mM DETA/NO 40min rep 4Diethylenetriamine / nitric oxide adduct-0.0211.700.21Voskuil MI, et al. (2003)
H37Rv ctrl vs Rv3132-3134 KO 0.05 mM DETA/NO 40min rep 4Diethylenetriamine / nitric oxide adduct-0.2311.080.60Voskuil MI, et al. (2003)
H37Rv ctrl vs Rv3132-34 KO (complemented) 0.05 mM DETA/NO 40min rep 4Diethylenetriamine / nitric oxide adduct-0.0711.080.30Voskuil MI, et al. (2003)
H37 Rv3132-34 KO 0 days vs Rv3132-34 KO (complemented) hypoxia 4 day rep 1Null mutant vs complemented null mutant-0.4710.000.65Voskuil MI, et al. (2003)
H37 Rv3132-34 KO 0 days vs Rv3132-34 KO (complemented) hypoxia 4 day rep 2Null mutant vs complemented null mutant-0.419.880.65Voskuil MI, et al. (2003)
H37 Rv3132-34 KO 0 days vs Rv3132-34 KO (complemented) hypoxia 4 day rep 3Null mutant vs complemented null mutant-0.539.890.80Voskuil MI, et al. (2003)
H37 Rv3132-34 KO 0 days vs Rv3132-34 KO (complemented) hypoxia 4 day rep 4Null mutant vs complemented null mutant-0.609.350.70Voskuil MI, et al. (2003)
H37Rv 0 day ctrl vs Rv3132-34 KO hypoxia 4 day rep 1Wild type vs Mutant-0.8710.091.03Voskuil MI, et al. (2003)
H37Rv 0 day ctrl vs Rv3132-34 KO hypoxia 4 day rep 2Wild type vs Mutant-1.0110.181.41Voskuil MI, et al. (2003)
H37Rv 0 day ctrl vs Rv3132-34 KO hypoxia 4 day rep 3Wild type vs Mutant-0.619.190.94Voskuil MI, et al. (2003)
H37Rv 0 day ctrl vs Rv3132-34 KO hypoxia 4 day rep 4Wild type vs Mutant-0.739.751.32Voskuil MI, et al. (2003)
30ug/mLProcept6776vsDMSO,6hProcept 6776-0.5710.230.55Boshoff HI, et al. (2004)
30ug/mLProcept6776vsDMSO,6hAProcept 6776-0.4910.390.42Boshoff HI, et al. (2004)
5ug/mLProcept 6778vsDMSO,6hProcept 6778-0.0211.120.04Boshoff HI, et al. (2004)
5ug/mLProcept 6778vsDMSO,6hAProcept 67780.0711.130.20Boshoff HI, et al. (2004)
20ug/mLProcept6778vsDMSO,6hProcept 6778-0.2411.280.63Boshoff HI, et al. (2004)
0.5ug/mL #111895vsDMSO, 6hDrug #111895-0.2010.900.37Boshoff HI, et al. (2004)
0.5ug/mL #124196vsDMSO, 6hDrug #1241960.0010.830.08Boshoff HI, et al. (2004)
0.5ug/mL #124196vsDMSO, 6hADrug #124196-0.0011.200.00Boshoff HI, et al. (2004)
2ug/mL #121940vsDMSO, 6hDrug #121940-0.439.410.37Boshoff HI, et al. (2004)
200uM Dipyridylvsctrl, 6hDipyridyl-1.189.171.06Boshoff HI, et al. (2004)
12.5ug/mL AntimycinvsDMSO, 6hAntimycin A0.4610.990.56Boshoff HI, et al. (2004)
25ug/mL AntimycinvsDMSO, 6hAntimycin A-0.019.350.16Boshoff HI, et al. (2004)
20ug/mL Procept6776vsDMSO, 6hProcept 6776-1.428.560.69Boshoff HI, et al. (2004)
20ug/mLProcept6778vsDMSO,6hAProcept 6778-0.069.260.00Boshoff HI, et al. (2004)
20ug/mLProcept6778vsDMSO,6hBProcept 6778-0.298.650.01Boshoff HI, et al. (2004)
40ug/mLProcept6778vsDMSO,6hProcept 6778-2.469.051.22Boshoff HI, et al. (2004)
40ug/mLProcept6778vsDMSO,6hAProcept 6778-1.999.501.00Boshoff HI, et al. (2004)
2ug/mL #111895vsDMSO, 6hDrug #111895-1.159.910.93Boshoff HI, et al. (2004)
2ug/mL #111895vsDMSO, 6hADrug #111895-1.309.811.13Boshoff HI, et al. (2004)
9ug/mLAscidideminNpvsDMSO,6hAscididemin-1.299.801.02Boshoff HI, et al. (2004)
50ug/mLAntimycinAvsDMSO, 6hAntimycin A0.8210.201.07Boshoff HI, et al. (2004)
50ug/mLAntimycinAvsDMSO, 6hAAntimycin A0.629.190.87Boshoff HI, et al. (2004)
10ug/mL PA-1vsDMSO, 6hPA 10.549.020.72Boshoff HI, et al. (2004)
10ug/mL PA-1vsDMSO, 6hAPA 10.418.130.44Boshoff HI, et al. (2004)
10ug/mL PA-21vsDMSO, 6hPA 210.408.920.54Boshoff HI, et al. (2004)
10ug/mL PA-21vsDMSO, 6hAPA 210.338.040.41Boshoff HI, et al. (2004)
10ug/mL TriclosanvsDMSO, 6hTriclosan-1.698.140.55Boshoff HI, et al. (2004)
10ug/mL TriclosanvsDMSO, 6hATriclosan-1.258.500.70Boshoff HI, et al. (2004)
10ug/mL PA-1vsDMSO, 6hBPA 10.208.210.47Boshoff HI, et al. (2004)
50ug/mL PA-21vsDMSO, 6hPA 210.048.680.16Boshoff HI, et al. (2004)
50ug/mL PA-1vsDMSO, 6hPA 10.209.770.40Boshoff HI, et al. (2004)
10ug/mL TriclosanvsDMSO, 6hBTriclosan0.5610.391.04Boshoff HI, et al. (2004)
50ug/mL PA-21vsDMSO, 6hAPA 210.219.840.42Boshoff HI, et al. (2004)
10ug/mL TriclosanvsDMSO, 6hCTriclosan0.148.540.28Boshoff HI, et al. (2004)
0.5ug/mL Cerulenin vs DMSO, 6hrs rep 4Cerulenin0.839.130.69Manjunatha U, et al. (2009)
0.5ug/mL Cerulenin vs DMSO, 6hrs rep 1Cerulenin0.6811.000.98Manjunatha U, et al. (2009)
0.5ug/mL Cerulenin vs DMSO, 6hrs rep 2Cerulenin0.5310.850.83Manjunatha U, et al. (2009)
150uM Deferroxaminevsctrl, 6hDeferoxamine0.7910.600.38Boshoff HI, et al. (2004)
150uM Deferroxaminevsctrl, 6hADeferoxamine0.3411.010.65Boshoff HI, et al. (2004)
150uM Deferroxaminevsctrl, 6hBDeferoxamine0.2810.760.56Boshoff HI, et al. (2004)
100uM Dipyridylvsctrl, 6hDipyridyl0.4410.480.66Boshoff HI, et al. (2004)
100uM DipyridylvsCtrl, 6hADipyridyl0.5110.700.82Boshoff HI, et al. (2004)
1 ug/mL #111891vsDMSO, 6hDrug #1118910.7611.771.41Boshoff HI, et al. (2004)
1ug/mL #111891vsDMSO, 6hDrug #1118910.449.840.68Boshoff HI, et al. (2004)
1ug/mL #111895vsDMSO, 6hDrug #1118950.3110.210.38Boshoff HI, et al. (2004)
1ug/mL #111895vsDMSO, 6hADrug #1118950.0210.350.18Boshoff HI, et al. (2004)
1ug/mL #124196vsDMSO, 6hDrug #1241960.2510.590.40Boshoff HI, et al. (2004)
1ug/mL #124196vsDMSO, 6hADrug #1241960.1910.690.40Boshoff HI, et al. (2004)
9ug/mLAscidideminNpvsDMSO,6hAAscididemin-0.349.890.20Boshoff HI, et al. (2004)
9ug/mLAscidideminNpvsDMSO,6hBAscididemin-0.369.730.50Boshoff HI, et al. (2004)
2ug/mL #121940vsDMSO, 6hADrug #1219400.1510.560.15Boshoff HI, et al. (2004)
2ug/mL #111891vsDMSO, 6hDrug #1118910.339.980.58Boshoff HI, et al. (2004)
2ug/mL #111895vsDMSO, 6hBDrug #111895-0.709.900.61Boshoff HI, et al. (2004)
50ug/mLAntimycinAvsDMSO, 6hBAntimycin A0.469.820.74Boshoff HI, et al. (2004)
0.5ug/mL Cerulenin vs DMSO, 6hrs rep 3Cerulenin0.0810.170.23Boshoff HI, et al. (2004)
250uM DeferroxaminevsDMSO, 6hDeferoxamine0.3710.340.60Boshoff HI, et al. (2004)
200uM Dipyridylvsctrl, 6hADipyridyl-0.5710.440.60Boshoff HI, et al. (2004)
9ug/mLNaturalproductvsDMSO,6hAscididemin-0.7210.460.75Boshoff HI, et al. (2004)
4ug/mLNaturalcompoundvsDMSO,6hAscididemin-0.2210.490.33Boshoff HI, et al. (2004)
1ug/mL #109vsDMSO, 6hADrug #1090.429.560.93Boshoff HI, et al. (2004)
10ug/mL #109vsDMSO, 6hDrug #109-0.338.790.22Boshoff HI, et al. (2004)
1ug/mL #109vsDMSO, 6hDrug #1090.089.600.19Boshoff HI, et al. (2004)
10ug/mL #109vsDMSO, 6hADrug #1090.0611.140.01Boshoff HI, et al. (2004)
1ug/mL #241vsDMSO, 6hDrug #2410.218.740.41Boshoff HI, et al. (2004)
1ug/mL #241vsDMSO, 6hADrug #241-0.338.990.22Boshoff HI, et al. (2004)
10ug/mL #241vsDMSO, 6hDrug #241-0.718.560.40Boshoff HI, et al. (2004)
1ug/mL #59vsDMSO, 6hDrug #590.229.500.21Boshoff HI, et al. (2004)
1ug/mL #59vsDMSO, 6hADrug #59-0.018.920.03Boshoff HI, et al. (2004)
10ug/mL #59vsDMSO, 6hDrug #59-0.369.570.50Boshoff HI, et al. (2004)
10ug/mL #59vsDMSO, 6hADrug #59-0.319.200.22Boshoff HI, et al. (2004)
10ug/mL EMBvsDMSO, 6hEthambutol0.057.790.29Boshoff HI, et al. (2004)
10ug/mL EMBvsDMSO, 6hAEthambutol-0.098.490.05Boshoff HI, et al. (2004)
0.1ug/mL Mtmvsctrl (0.33h)Mitomycin0.578.851.06Boshoff HI, et al. (2004)
0.2ug/mL Mtmvsctrl (0.33h)Mitomycin0.478.420.93Boshoff HI, et al. (2004)
0.1ug/mL Mtmvsctrl (0.75h)Mitomycin0.639.291.18Boshoff HI, et al. (2004)
0.2ug/mL Mtmvsctrl (0.75h)Mitomycin0.748.671.47Boshoff HI, et al. (2004)
0.2ug/mL Mtmvsctrl (1.5h)Mitomycin0.548.751.20Boshoff HI, et al. (2004)
0.2ug/mL Mtmvsctrl (2h)Mitomycin3.274.962.07Boshoff HI, et al. (2004)
0.2ug/mL Mtmvsctrl (2h)AMitomycin-0.138.100.07Boshoff HI, et al. (2004)
0.2ug/mL Mtmvsctrl (2h)BMitomycin0.728.850.94Boshoff HI, et al. (2004)
0.2ug/mL Mtmvsctrl (2h)CMitomycin-0.997.380.64Boshoff HI, et al. (2004)
0.2ug/mL Mtmvsctrl (4h)Mitomycin0.788.210.96Boshoff HI, et al. (2004)
0.2ug/mL Mtmvsctrl (4h)AMitomycin-0.408.840.48Boshoff HI, et al. (2004)
0.2ug/mL Mtmvsctrl (4h)BMitomycin0.919.411.19Boshoff HI, et al. (2004)
0.2ug/mL Mtmvsctrl (6h)Mitomycin0.338.380.43Boshoff HI, et al. (2004)
4mM H2O2vsctrl (1h)H2O20.238.760.21Boshoff HI, et al. (2004)
4mM H2O2vsctrl (2h)H2O20.509.700.69Boshoff HI, et al. (2004)
4mM H2O2vsctrl (2h)AH2O2-1.267.741.21Boshoff HI, et al. (2004)
4mM H2O2vsctrl (4h)H2O20.028.010.12Boshoff HI, et al. (2004)
4mM H2O2vsctrl (4h)AH2O20.149.340.24Boshoff HI, et al. (2004)
25J UVvs ctrl (6h)Ultraviolet (UV) light0.218.950.33Boshoff HI, et al. (2004)
60J UVvsctrl (6h)Ultraviolet (UV) light0.369.200.55Boshoff HI, et al. (2004)
0.12mg/mL PZAvspH5.6 (4h)Pyrazinamide0.147.830.22Boshoff HI, et al. (2004)
1.2mg/mL PZAvspH5.6 (4h)Pyrazinamide0.237.480.24Boshoff HI, et al. (2004)
0.12mg/mL PZAvspH5.6 (4h)APyrazinamide0.028.400.02Boshoff HI, et al. (2004)
1.2mg/mL PZAvspH5.6 (4h)APyrazinamide0.268.610.18Boshoff HI, et al. (2004)
1.2mg/mL PZAvspH5.6 (4h)BPyrazinamide-0.658.160.65Boshoff HI, et al. (2004)
0.12mg/mL PZAvspH5.6 (5.5h)Pyrazinamide-0.129.620.28Boshoff HI, et al. (2004)
1.2mg/mL PZAvspH5.6 (6h)Pyrazinamide-0.557.750.76Boshoff HI, et al. (2004)
1.2mg/mL PZAvspH5.6 (6h)APyrazinamide-0.328.650.41Boshoff HI, et al. (2004)
0.12mg/mL PZAvspH5.6 (6h)Pyrazinamide0.067.810.01Boshoff HI, et al. (2004)
0.12mg/mL PZAvspH5.6 (6h)APyrazinamide-0.477.520.35Boshoff HI, et al. (2004)
1.2mg/mL PZAvspH5.6 (7h)Pyrazinamide-0.148.000.14Boshoff HI, et al. (2004)
1.2mg/mL PZAvspH5.6 (7h)APyrazinamide-1.607.141.68Boshoff HI, et al. (2004)
1.2mg/mL PZAvspH5.6 (10.5h)Pyrazinamide-0.1410.210.21Boshoff HI, et al. (2004)
0.12mg/mL PZAvspH5.6 (10.5h)Pyrazinamide-0.309.150.33Boshoff HI, et al. (2004)
0.12mg/mL PZAvspH5.6 (11h)Pyrazinamide-0.219.280.35Boshoff HI, et al. (2004)
1.2mg/mL PZAvspH5.6 (16h)Pyrazinamide0.848.780.84Boshoff HI, et al. (2004)
0.12mg/mL NamvspH5.6 (4h)Sodium azide-1.676.320.92Boshoff HI, et al. (2004)
1.2mg/mL NamvspH5.6 (5h)Sodium azide-0.469.320.65Boshoff HI, et al. (2004)
0.12mg/mL NamvspH5.6 (5.5h)Sodium azide-0.169.690.30Boshoff HI, et al. (2004)
0.12mg/mL NamvspH5.6 (7h)Sodium azide-0.418.330.55Boshoff HI, et al. (2004)
1.2mg/mL NamvspH5.6 (10.5h)Sodium azide-0.3610.490.44Boshoff HI, et al. (2004)
0.12mg/mL BZAvspH5.6 (5h)Benzamide-0.888.440.80Boshoff HI, et al. (2004)
0.12mg/mL BZAvspH5.6 (7h)Benzamide-0.279.320.38Boshoff HI, et al. (2004)
0.12mg/mL BZAvspH5.6 (11h)Benzamide-0.558.980.59Boshoff HI, et al. (2004)
pH4.8vspH6.8 (2h)Acidified medium1.247.651.09Boshoff HI, et al. (2004)
pH4.8vspH6.8 (2h)AAcidified medium0.318.940.40Boshoff HI, et al. (2004)
pH4.8vspH6.8 (2h)BAcidified medium0.148.920.16Boshoff HI, et al. (2004)
pH4.8vspH6.8 (4h)CAcidified medium0.438.710.48Boshoff HI, et al. (2004)
pH4.8vspH6.8 (7h)Acidified medium-0.209.060.27Boshoff HI, et al. (2004)
pH4.8vspH6.8 (11h)Acidified medium0.1710.410.14Boshoff HI, et al. (2004)
pH5.2vspH6.8 (2h)Acidified medium1.048.101.15Boshoff HI, et al. (2004)
pH5.2vspH6.8 (5.5h)Acidified medium0.0610.210.06Boshoff HI, et al. (2004)
pH5.2vspH6.8 (11h)Acidified medium0.069.280.05Boshoff HI, et al. (2004)
pH5.2vspH6.8 (16h)Acidified medium0.4410.280.60Boshoff HI, et al. (2004)
pH5.6vspH6.8 (2h)Acidified medium0.847.721.22Boshoff HI, et al. (2004)
pH5.6vspH6.8 (2h)AAcidified medium0.368.520.64Boshoff HI, et al. (2004)
pH5.6vspH6.8 (4h)Acidified medium0.268.890.32Boshoff HI, et al. (2004)
pH5.6vspH6.8 (4h)AAcidified medium0.537.230.60Boshoff HI, et al. (2004)
pH5.6vspH6.8 (4h)BAcidified medium0.418.890.51Boshoff HI, et al. (2004)
pH5.6vspH6.8 (7h)Acidified medium0.378.590.55Boshoff HI, et al. (2004)
pH5.6vspH6.8 (5h)Acidified medium0.2610.240.31Boshoff HI, et al. (2004)
pH5.6vspH6.8 (11h)Acidified medium0.028.870.00Boshoff HI, et al. (2004)
pH5.6vspH6.8 (16h)Acidified medium0.429.200.67Boshoff HI, et al. (2004)
0.1ug/mL Mtmvsctrl (1.5h)Mitomycin0.378.880.77Boshoff HI, et al. (2004)
H37Rv hypoxia 4hr rep 1Hypoxia1.709.711.21Rustad TR, et al. (2008)
H37Rv hypoxia 4hr rep 2Hypoxia2.4810.021.96Rustad TR, et al. (2008)
H37Rv hypoxia 4hr rep 4Hypoxia-0.629.430.75Rustad TR, et al. (2008)
H37Rv hypoxia 4hr rep 5Hypoxia-0.4310.130.91Rustad TR, et al. (2008)
H37Rv hypoxia 4hr rep 6Hypoxia-1.019.601.41Rustad TR, et al. (2008)
H37Rv hypoxia 8hr rep 1Hypoxia1.748.651.08Rustad TR, et al. (2008)
H37Rv hypoxia 8hr rep 2Hypoxia4.577.562.25Rustad TR, et al. (2008)
H37Rv hypoxia 12hr rep 1Hypoxia1.498.440.85Rustad TR, et al. (2008)
H37Rv hypoxia 12hr rep 2Hypoxia2.317.671.48Rustad TR, et al. (2008)
H37Rv hypoxia 1 day rep 2Hypoxia1.068.510.48Rustad TR, et al. (2008)
H37Rv hypoxia 1 day rep 3Hypoxia2.658.701.70Rustad TR, et al. (2008)
H37Rv hypoxia 1 day rep 5Hypoxia-0.199.600.18Rustad TR, et al. (2008)
H37Rv hypoxia 1 day rep 6Hypoxia-1.758.051.07Rustad TR, et al. (2008)
H37Rv hypoxia 1 day rep 7Hypoxia0.2911.250.32Rustad TR, et al. (2008)
H37Rv hypoxia 1 day rep 9Hypoxia1.498.671.12Rustad TR, et al. (2008)
H37Rv hypoxia 4 day rep 2Hypoxia0.0411.810.03Rustad TR, et al. (2008)
H37Rv hypoxia 4 day rep 4Hypoxia-0.2210.380.13Rustad TR, et al. (2008)
H37Rv hypoxia 4 day rep 5Hypoxia-0.7610.380.44Rustad TR, et al. (2008)
H37Rv hypoxia 4 day rep 6Hypoxia-0.9810.460.73Rustad TR, et al. (2008)
H37Rv hypoxia 4 day rep 7Hypoxia2.867.171.67Rustad TR, et al. (2008)
H37Rv hypoxia 7 day rep 1Hypoxia2.866.720.91Rustad TR, et al. (2008)
H37Rv hypoxia 7 day rep 5Hypoxia-0.848.920.70Rustad TR, et al. (2008)
H37Rv hypoxia 7 day rep 6Hypoxia-3.274.821.49Rustad TR, et al. (2008)
H37Rv hypoxia 7 day rep 7Hypoxia-0.7011.260.54Rustad TR, et al. (2008)
H37dosR mutant hypoxia 4hr rep 1Hypoxia1.499.440.81Rustad TR, et al. (2008)
H37dosR mutant hypoxia 4hr rep 2Hypoxia1.679.781.41Rustad TR, et al. (2008)
H37dosR mutant hypoxia 4hr rep 4Hypoxia2.059.682.07Rustad TR, et al. (2008)
H37dosR mutant hypoxia 4hr rep 5Hypoxia2.298.631.92Rustad TR, et al. (2008)
H37dosR mutant hypoxia 8hr rep 3Hypoxia2.148.681.59Rustad TR, et al. (2008)
H37dosR mutant hypoxia 12hr rep 1Hypoxia1.419.090.94Rustad TR, et al. (2008)
H37dosR mutant hypoxia 12hr rep 4Hypoxia2.278.361.77Rustad TR, et al. (2008)
H37dosR mutant hypoxia 1 day rep 1Hypoxia-2.628.881.79Rustad TR, et al. (2008)
H37dosR mutant hypoxia 1 day rep 2Hypoxia-2.369.581.64Rustad TR, et al. (2008)
H37dosR mutant hypoxia 1 day rep 3Hypoxia-3.069.002.29Rustad TR, et al. (2008)
H37dosR mutant hypoxia 1 day rep 4Hypoxia1.506.971.10Rustad TR, et al. (2008)
H37dosR mutant hypoxia 1 day rep 6Hypoxia1.449.370.99Rustad TR, et al. (2008)
H37dosR mutant hypoxia 4 day rep 1Hypoxia0.719.360.48Rustad TR, et al. (2008)
H37dosR mutant hypoxia 7 day rep 1Hypoxia-2.298.441.16Rustad TR, et al. (2008)
H37dosR mutant hypoxia 8hr rep 2Hypoxia0.386.510.26Rustad TR, et al. (2008)
H37dosR mutant hypoxia 12hr rep 3Hypoxia2.445.380.92Rustad TR, et al. (2008)
H37dosR mutant hypoxia 1 day rep 5Hypoxia2.495.340.99Rustad TR, et al. (2008)
H37Rv hypoxia 4hr rep 3Hypoxia-0.259.580.19Rustad TR, et al. (2008)
H37Rv hypoxia 4hr rep 7Hypoxia1.086.130.70Rustad TR, et al. (2008)
H37Rv hypoxia 8hr rep 3Hypoxia1.664.560.69Rustad TR, et al. (2008)
H37Rv hypoxia 12hr rep 3Hypoxia3.015.131.02Rustad TR, et al. (2008)
H37Rv hypoxia 1 day rep 4Hypoxia-0.599.860.60Rustad TR, et al. (2008)
H37Rv hypoxia 1 day rep 10Hypoxia3.115.131.04Rustad TR, et al. (2008)
H37Rv hypoxia 4 day rep 1Hypoxia2.516.121.21Rustad TR, et al. (2008)
H37Rv hypoxia 7 day rep 4Hypoxia3.3310.971.43Rustad TR, et al. (2008)
H37Rv hypoxia 7 day rep 3Hypoxia1.946.960.90Rustad TR, et al. (2008)
H37Rv hypoxia 7 day rep 2Hypoxia1.898.090.72Rustad TR, et al. (2008)
H37Rv hypoxia 4 day rep 3Hypoxia2.119.371.02Rustad TR, et al. (2008)
Ctrl Vs sigB overexpression 12hrWild type vs overexpression-0.337.910.35Lee JH, et al. (2008)
Control Vs sigG knockoutWild type vs Mutant-0.006.240.05Lee JH, et al. (2008)
H37Rv cDNA Cy3 vs H37Rv gDNA Cy5 (DS) rep 1Control cDNA vs gDNA0.308.090.25Andreu N and Gibert I (2008)
H37Rv cDNA Cy3 vs H37Rv gDNA Cy5 (DS) rep 2Control cDNA vs gDNA0.367.320.29Andreu N and Gibert I (2008)
H37Rv cDNA Cy3 vs H37Rv gDNA Cy5 (DS) rep 3Control cDNA vs gDNA0.467.590.34Andreu N and Gibert I (2008)
H37Rv cDNA Cy5 vs H37Rv gDNA Cy3 rep 1Control cDNA vs gDNA-0.1110.610.22Andreu N and Gibert I (2008)
H37Rv cDNA Cy5 vs H37Rv gDNA Cy3 rep 2Control cDNA vs gDNA-0.4210.200.41Andreu N and Gibert I (2008)
H37Rv cDNA Cy5 vs H37Rv gDNA Cy3 rep 3Control cDNA vs gDNA-0.5910.610.43Andreu N and Gibert I (2008)
Strain 27 cDNA Cy3 vs H37Rv gDNA Cy5 (DS) rep 1Strain comparison0.177.830.22Andreu N and Gibert I (2008)
Strain 27 cDNA Cy3 vs H37Rv gDNA Cy5 (DS) rep 2Strain comparison0.378.120.22Andreu N and Gibert I (2008)
Strain 27 cDNA Cy5 vs H37Rv gDNA Cy3 rep 1Strain comparison-0.2010.830.25Andreu N and Gibert I (2008)
Strain 27 cDNA Cy5 vs H37Rv gDNA Cy3 rep 2Strain comparison-0.579.720.40Andreu N and Gibert I (2008)
Strain 32 cDNA Cy3 vs H37Rv gDNA Cy5 (DS) rep 1Strain comparison0.157.780.18Andreu N and Gibert I (2008)
Strain 32 cDNA Cy3 vs H37Rv gDNA Cy5 (DS) rep 2Strain comparison0.078.230.13Andreu N and Gibert I (2008)
Strain 32 cDNA Cy5 vs H37Rv gDNA Cy3 rep 1Strain comparison0.0010.640.21Andreu N and Gibert I (2008)
Strain 32 cDNA Cy5 vs H37Rv gDNA Cy3 rep 2Strain comparison0.3210.820.01Andreu N and Gibert I (2008)
Strain 32 cDNA Cy5 vs H37Rv gDNA Cy3 rep 3Strain comparison-0.1310.230.30Andreu N and Gibert I (2008)
Strain 49 cDNA Cy3 vs H37Rv gDNA Cy5 (DS) rep 1Strain comparison-0.007.170.11Andreu N and Gibert I (2008)
Strain 49 cDNA Cy3 vs H37Rv gDNA Cy5 (DS) rep 2Strain comparison-0.158.520.19Andreu N and Gibert I (2008)
Strain 49 cDNA Cy3 vs H37Rv gDNA Cy5 (DS) rep 3Strain comparison0.037.320.03Andreu N and Gibert I (2008)
Strain 49 cDNA Cy5 vs H37Rv gDNA Cy3 rep 1Strain comparison-0.539.880.71Andreu N and Gibert I (2008)
Strain 49 cDNA Cy5 vs H37Rv gDNA Cy3 rep 2Strain comparison-0.019.280.34Andreu N and Gibert I (2008)
Strain 49 cDNA Cy5 vs H37Rv gDNA Cy3 rep 3Strain comparison0.519.780.17Andreu N and Gibert I (2008)
H37Rv wild type Vs H37Rv wild type rep 1Control-0.419.660.63Fontan PA, et al. (2009)
H37Rv wild type Vs H37Rv wild type rep 2Control-0.079.250.29Fontan PA, et al. (2009)
H37Rv wild type Vs H37Rv wild type rep 3Control-0.278.480.37Fontan PA, et al. (2009)
H37Rv wild type Vs H37Rv wild type rep 4Control0.329.270.47Fontan PA, et al. (2009)
H37Rv wild type Vs H37Rv wild type rep 5Control0.089.440.37Fontan PA, et al. (2009)
H37Rv wild type Vs H37Rv wild type rep 6Control-0.178.170.32Fontan PA, et al. (2009)
H37Rv wild type vs H37Rv sigB null mutant rep 1Wild type vs Mutant0.179.420.34Fontan PA, et al. (2009)
H37Rv wild type vs H37Rv sigB null mutant rep 2Wild type vs Mutant0.019.240.05Fontan PA, et al. (2009)
H37Rv wild type vs H37Rv sigB null mutant rep 3Wild type vs Mutant0.008.960.08Fontan PA, et al. (2009)
H37Rv wild type vs H37Rv sigB null mutant rep 4Wild type vs Mutant-0.039.250.13Fontan PA, et al. (2009)
H37Rv wild type vs H37Rv sigB null mutant rep 5Wild type vs Mutant0.069.350.12Fontan PA, et al. (2009)
H37Rv wild type vs H37Rv sigB null mutant rep 6Wild type vs Mutant-0.049.760.12Fontan PA, et al. (2009)
H37Rv wild type control vs 0.05% SDS for 60 min rep 1SDS0.019.360.13Fontan PA, et al. (2009)
H37Rv wild type control vs 0.05% SDS for 60 min rep 2SDS-0.279.610.34Fontan PA, et al. (2009)
H37Rv wild type control vs 0.05% SDS for 60 min rep 3SDS0.319.800.08Fontan PA, et al. (2009)
H37Rv wild type control vs 0.05% SDS for 60 min rep 4SDS-0.158.870.36Fontan PA, et al. (2009)
H37Rv wild type control vs 0.05% SDS for 60 min rep 5SDS0.218.920.06Fontan PA, et al. (2009)
H37Rv wild type control vs 0.05% SDS for 60 min rep 6SDS0.129.320.11Fontan PA, et al. (2009)
H37Rv sigB null mutant control vs 0.05% SDS for 60 min rep 1SDS-0.038.480.18Fontan PA, et al. (2009)
H37Rv sigB null mutant control vs 0.05% SDS for 60 min rep 2SDS0.398.360.31Fontan PA, et al. (2009)
H37Rv sigB null mutant control vs 0.05% SDS for 60 min rep 3SDS0.028.220.02Fontan PA, et al. (2009)
H37Rv sigB null mutant control vs 0.05% SDS for 60 min rep 4SDS0.109.410.03Fontan PA, et al. (2009)
H37Rv sigB null mutant control vs 0.05% SDS for 60 min rep 5SDS0.599.980.31Fontan PA, et al. (2009)
H37Rv sigB null mutant control vs 0.05% SDS for 60 min rep 6SDS0.248.760.02Fontan PA, et al. (2009)
H37Rv wild type control vs 5mM Diamide for 60 min rep 1Diamide-0.419.410.62Fontan PA, et al. (2009)
H37Rv wild type control vs 5mM Diamide for 60 min rep 2Diamide-0.189.250.39Fontan PA, et al. (2009)
H37Rv wild type control vs 5mM Diamide for 60 min rep 3Diamide-0.518.270.69Fontan PA, et al. (2009)
H37Rv wild type control vs 5mM Diamide for 60 min rep 4Diamide-0.499.120.71Fontan PA, et al. (2009)
H37Rv wild type control vs 5mM Diamide for 60 min rep 5Diamide-0.088.570.15Fontan PA, et al. (2009)
H37Rv wild type control vs 5mM Diamide for 60 min rep 6Diamide-0.129.390.20Fontan PA, et al. (2009)
H37Rv sigB null mutant control vs 5mM Diamide for 60 min rep 1Diamide-0.438.930.75Fontan PA, et al. (2009)
H37Rv sigB null mutant control vs 5mM Diamide for 60 min rep 2Diamide-0.078.380.24Fontan PA, et al. (2009)
H37Rv sigB null mutant control vs 5mM Diamide for 60 min rep 3Diamide0.269.540.15Fontan PA, et al. (2009)
H37Rv sigB null mutant control vs 5mM Diamide for 60 min rep 4Diamide-0.089.540.32Fontan PA, et al. (2009)
H37Rv sigB null mutant control vs 5mM Diamide for 60 min rep 5Diamide-0.458.710.79Fontan PA, et al. (2009)
H37Rv sigB null mutant control vs 5mM Diamide for 60 min rep 6Diamide0.229.130.15Fontan PA, et al. (2009)
MTB strain1254 vs MTB strain 1254 for H2O2 exp control rep 1Control0.138.550.13Voskuil MI, et al. (2011)
MTB strain1254 vs MTB strain 1254 for H2O2 exp control rep 2Control0.197.300.28Voskuil MI, et al. (2011)
MTB strain1254 vs MTB strain 1254 for H2O2 exp control rep 3Control0.326.600.57Voskuil MI, et al. (2011)
MTB strain 1254 Ctrl vs 0.05 mM H202 40min rep 2H2O20.048.700.03Voskuil MI, et al. (2011)
MTB strain 1254 Ctrl vs 0.5 mM H202 40min rep 1H2O2-0.187.500.42Voskuil MI, et al. (2011)
MTB strain 1254 Ctrl vs 5.0 mM H202 40min rep 4H2O2-1.138.701.29Voskuil MI, et al. (2011)
MTB strain 1254 Ctrl vs 5.0 mM H202 40min rep 6H2O2-1.447.511.72Voskuil MI, et al. (2011)
MTB strain 1254 Ctrl vs 10.0 mM H202 40min rep 6H2O2-1.778.291.41Voskuil MI, et al. (2011)
MTB strain 1254 Ctrl vs 50.0 mM H202 40min rep 4H2O2-0.017.330.01Voskuil MI, et al. (2011)
MTB strain 1254 Ctrl vs 50.0 mM H202 40min rep 6H2O20.478.720.39Voskuil MI, et al. (2011)
MTB strain 1254 Ctrl vs 200 mM H202 40min rep 2H2O21.098.091.06Voskuil MI, et al. (2011)
MTB strain 1254 Ctrl vs 0.5 mM DETA/NO 4hrs rep 1Diethylenetriamine / nitric oxide adduct-1.3812.641.64Voskuil MI, et al. (2011)
MTB strain 1254 Ctrl vs 0.5 mM DETA/NO 4hrs rep 2Diethylenetriamine / nitric oxide adduct-0.9013.090.68Voskuil MI, et al. (2011)
MTB strain 1254 Ctrl vs 0.5 mM DETA/NO 4hrs rep 3Diethylenetriamine / nitric oxide adduct-0.9311.510.69Voskuil MI, et al. (2011)
MTB strain 1254 Ctrl vs 0.5 mM DETA/NO 4hrs rep 4Diethylenetriamine / nitric oxide adduct-1.3912.640.96Voskuil MI, et al. (2011)
MTB strain TB294 Ctrl vs SigA overexpression rep1Wild type vs overexpression0.427.990.47Wu S, et al. (2009)
MTB strain TB294 SigA overexpression vs Ctrl(DS) rep1Wild type vs overexpression-0.036.220.20Wu S, et al. (2009)
MTB strain TB294 Ctrl vs SigA overexpression rep2Wild type vs overexpression0.738.150.89Wu S, et al. (2009)
MTB strain TB294 SigA overexpression vs Ctrl (DS) rep2Wild type vs overexpression-0.618.460.77Wu S, et al. (2009)
Whole Lung Surfactant 30min rep 1Whole Lung Surfactant-0.2010.690.62Schwab U, et al. (2009)
Whole Lung Surfactant 30min rep 2Whole Lung Surfactant-0.179.570.43Schwab U, et al. (2009)
Whole Lung Surfactant 30min rep 3Whole Lung Surfactant-0.459.581.02Schwab U, et al. (2009)
Whole Lung Surfactant 30min rep 4Whole Lung Surfactant-0.6710.262.40Schwab U, et al. (2009)
Whole Lung Surfactant 30min rep 5Whole Lung Surfactant-0.2010.360.67Schwab U, et al. (2009)
Whole Lung Surfactant 2hrs rep 1Whole Lung Surfactant0.039.900.04Schwab U, et al. (2009)
Whole Lung Surfactant 2hrs rep 2Whole Lung Surfactant-1.098.720.85Schwab U, et al. (2009)
Whole Lung Surfactant 2hrs rep 3Whole Lung Surfactant0.259.460.56Schwab U, et al. (2009)
Extracted Lung Surfactant 30min rep 1Extracted Lung Surfactant-0.2111.041.05Schwab U, et al. (2009)
Extracted Lung Surfactant 30min rep 2Extracted Lung Surfactant-0.319.930.76Schwab U, et al. (2009)
Extracted Lung Surfactant 30min rep 3Extracted Lung Surfactant-0.349.690.90Schwab U, et al. (2009)
Extracted Lung Surfactant 30min rep 4Extracted Lung Surfactant-0.0211.190.09Schwab U, et al. (2009)
Extracted Lung Surfactant 2hrs rep 1Extracted Lung Surfactant0.049.650.05Schwab U, et al. (2009)
Extracted Lung Surfactant 2hrs rep 2Extracted Lung Surfactant-0.188.950.31Schwab U, et al. (2009)
Purified Surfactant Lipids 30min rep 1Purified Surfactant Lipids-0.489.700.91Schwab U, et al. (2009)
Purified Surfactant Lipids 30min rep 2Purified Surfactant Lipids-0.0810.310.31Schwab U, et al. (2009)
Purified Surfactant Lipids 2hrs rep 1Purified Surfactant Lipids-1.128.870.98Schwab U, et al. (2009)
Purified Surfactant Lipids 2hrs rep 2Purified Surfactant Lipids0.189.630.44Schwab U, et al. (2009)
Purified Human SP-A Coated 2hrs rep1 Human Pulmonary Surfactant Protein A0.3310.620.86Schwab U, et al. (2009)
Purified Human SP-A Coated 2hrs rep2Human Pulmonary Surfactant Protein A0.0410.330.05Schwab U, et al. (2009)
Purified Human SP-A Uncoated 2hrs rep1 Human Pulmonary Surfactant Protein A0.1411.350.61Schwab U, et al. (2009)
Purified Human SP-A Uncoated 2hrs rep2Human Pulmonary Surfactant Protein A0.149.320.25Schwab U, et al. (2009)
Purified Human SP-A Uncoated 2hrs rep3Human Pulmonary Surfactant Protein A-0.109.220.31Schwab U, et al. (2009)
Purified Human SP-A Uncoated 2hrs rep4Human Pulmonary Surfactant Protein A-0.018.320.05Schwab U, et al. (2009)
H37Rv Ctrl vs 2 ug/ml garlic extract 6hrs rep 1Garlic Extract-8.964.614.43O'Donnell G, et al. (2009)
H37Rv Ctrl vs 2 ug/ml garlic extract 6hrs rep 2Garlic Extract-1.8410.230.92O'Donnell G, et al. (2009)
H37Rv Ctrl vs 10 ug/ml garlic extract 6hrsGarlic Extract-2.448.571.16O'Donnell G, et al. (2009)
H37Rv Ctrl vs 5 ug/ml garlic extract 6hrsGarlic Extract-0.1510.510.05O'Donnell G, et al. (2009)
H37Ra, 7H9 roll-replicate 1_clone7H9 medium rolling-0.089.330.32Gao Q, et al. (2004)
H37Ra, 7H9 roll-replicate 2_clone7H9 medium rolling-0.3310.060.59Gao Q, et al. (2004)
H37Rv, 7H9 roll-replicate 1_clone7H9 medium rolling-0.329.990.30Gao Q, et al. (2004)
H37Rv, 7H9 roll-replicate 2_clone7H9 medium rolling-0.079.880.22Gao Q, et al. (2004)
H37Rv, 7H9 roll-replicate 3_clone7H9 medium rolling-0.4510.000.54Gao Q, et al. (2004)
H37Rv, 7H9 roll-replicate 4_clone7H9 medium rolling-0.119.620.09Gao Q, et al. (2004)
H37Ra, 7H9 roll-replicate 3_clone7H9 medium rolling-0.099.870.12Gao Q, et al. (2004)
H37Rv grown in 7H9 vs H37Rv 4hrs after infection in macrophages rep 1Grown in macrophages0.7011.191.02Fontan P, et al. (2008)
H37Rv grown in 7H9 vs H37Rv 4hrs after infection in macrophages rep 2Grown in macrophages-1.4210.141.70Fontan P, et al. (2008)
H37Rv grown in 7H9 vs H37Rv 4hrs after infection in macrophages rep 3Grown in macrophages-0.2510.720.47Fontan P, et al. (2008)
H37Rv grown in 7H9 vs H37Rv 4hrs after infection in macrophages rep 4Grown in macrophages0.2210.960.21Fontan P, et al. (2008)
H37Rv grown in 7H9 vs H37Rv 4hrs after infection in macrophages rep 5Grown in macrophages-1.5610.071.67Fontan PA, et al. (2008)
H37Rv grown in 7H9 vs H37Rv 24hrs after infection in macrophages rep 1Grown in macrophages-0.8010.450.50Fontan PA, et al. (2008)
H37Rv grown in 7H9 vs H37Rv 24hrs after infection in macrophages rep 2Grown in macrophages0.5111.100.52Fontan P, et al. (2008)
H37Rv grown in 7H9 vs H37Rv 24hrs after infection in macrophages rep 3Grown in macrophages-0.3310.680.20Fontan PA, et al. (2008)
H37Rv grown in 7H9 vs H37Rv 24hrs after infection in macrophages rep 4Grown in macrophages-0.2010.741.78Fontan PA, et al. (2008)
H37Rv grown in 7H9 vs H37Rv 24hrs after infection in macrophages rep 5Grown in macrophages0.1610.931.05Fontan PA, et al. (2008)
H37Rv grown in 7H9 vs H37Rv 4hrs after infection in macrophages rep 6Grown in macrophages1.0010.760.63Fontan P, et al. (2008)
H37Rv wild type vs sigE mutant in 7H9 media (DS) rep 1Wild type vs Mutant-1.1710.261.00Fontan PA, et al. (2008)
H37Rv wild type vs sigE mutant in 7H9 media (DS) rep 2Wild type vs Mutant0.2410.970.53Fontan PA, et al. (2008)
H37Rv wild type vs sigE mutant in 7H9 media rep 1Wild type vs Mutant-0.4410.620.61Fontan PA, et al. (2008)
H37Rv wild type vs sigE mutant in 7H9 media (DS) rep 3Wild type vs Mutant-1.3410.171.68Fontan PA, et al. (2008)
H37Rv wild type vs sigE mutant in 7H9 media rep 2Wild type vs Mutant0.1710.930.64Fontan PA, et al. (2008)
H37Rv wild type vs sigE mutant in 7H9 media rep 3Wild type vs Mutant0.5411.120.51Fontan PA, et al. (2008)
H37Rv wild type vs sigE mutant in RPMI media for 2hrs (DS) rep 1Wild type vs Mutant1.3611.530.23Fontan PA, et al. (2008)
H37Rv wild type vs sigE mutant in RPMI media for 2hrs (DS) rep 2Wild type vs Mutant1.2911.490.30Fontan PA, et al. (2008)
H37Rv wild type vs sigE mutant in RPMI media for 2 hrs rep 1Wild type vs Mutant0.4311.060.25Fontan PA, et al. (2008)
H37Rv wild type vs sigE mutant in RPMI media for 2 hrs rep 2Wild type vs Mutant-0.3010.690.74Fontan PA, et al. (2008)
H37Rv wild type vs sigE mutant in RPMI media for 2 hrs (DS) rep 3Wild type vs Mutant-1.2810.201.27Fontan PA, et al. (2008)
H37Rv wild type vs sigE mutant in RPMI media for 2 hrs rep 3Wild type vs Mutant1.6011.650.69Fontan PA, et al. (2008)
H37Rv vs SigE mutant 24hrs after macrophage infection (DS) rep 1Grown in macrophages-1.2110.240.86Fontan PA, et al. (2008)
H37Rv vs SigE mutant 24hrs after macrophage infection rep 1Grown in macrophages0.6411.170.14Fontan PA, et al. (2008)
H37Rv vs SigE mutant 24hrs after macrophage infection rep 2Grown in macrophages0.9211.300.84Fontan PA, et al. (2008)
H37Rv vs SigE mutant 24hrs after macrophage infection (DS) rep 2Grown in macrophages1.5511.621.06Fontan PA, et al. (2008)
H37Rv vs SigE mutant 24hrs after macrophage infection (DS) rep 3Grown in macrophages0.2210.950.15Fontan PA, et al. (2008)
H37Rv vs SigE mutant 24hrs after macrophage infection rep 3Grown in macrophages-2.589.561.01Fontan PA, et al. (2008)
SigE mutant grown in 7H9 vs 24hrs after infection in macrophages (DS) rep 1Grown in macrophages-0.8310.430.80Fontan PA, et al. (2008)
SigE mutant grown in 7H9 vs 24hrs after infection in macrophages rep 1Grown in macrophages0.7511.220.24Fontan PA, et al. (2008)
SigE mutant grown in 7H9 vs 24hrs after infection in macrophages (DS) rep 2Grown in macrophages0.6511.170.09Fontan PA, et al. (2008)
SigE mutant grown in 7H9 vs 24hrs after infection in macrophages (DS) rep 3Grown in macrophages-0.5210.580.41Fontan PA, et al. (2008)
SigE mutant grown in 7H9 vs 24hrs after infection in macrophages rep 2Grown in macrophages0.5611.130.11Fontan PA, et al. (2008)
H37Rv wild type Cy3 vs Rv0485 Tn mutant Cy5 rep 1Wild type vs Mutant0.469.020.53Goldstone RM, et al. (2009)
H37Rv wild type Cy3 vs Rv0485 Tn mutant Cy5 rep 2Wild type vs Mutant0.1710.010.14Goldstone RM, et al. (2009)
H37Rv wild type Cy3 vs Rv0485 Tn mutant Cy5 rep 3Wild type vs Mutant-0.887.740.46Goldstone RM, et al. (2009)
H37Rv wild type Cy5 vs Rv0485 Tn mutant Cy3 (DS) rep 1Wild type vs Mutant0.089.670.19Goldstone RM, et al. (2009)
H37Rv wild type Cy5 vs Rv0485 Tn mutant Cy3 (DS) rep 2Wild type vs Mutant-0.529.270.39Goldstone RM, et al. (2009)
H37Rv wild type Cy5 vs Rv0485 Tn mutant Cy3 (DS) rep 3Wild type vs Mutant-0.158.520.04Goldstone RM, et al. (2009)
H37Rv control vs 1mg/ml cholesterol for 3 hrs rep 1Cholesterol-0.399.960.55Nesbitt NM, et al. (2010)
H37Rv control vs 1mg/ml cholesterol for 3 hrs rep 2Cholesterol0.379.080.50Nesbitt NM, et al. (2010)
H37Rv control vs 1mg/ml cholesterol for 3 hrs rep 3Cholesterol0.228.620.32Nesbitt NM, et al. (2010)
H37Rv control vs 1mg/ml cholesterol for 24 hrs rep 1Cholesterol0.357.750.35Nesbitt NM, et al. (2010)
H37Rv control vs 1mg/ml cholesterol for 24 hrs rep 2Cholesterol0.907.580.82Nesbitt NM, et al. (2010)
H37Rv control vs 1mg/ml cholesterol for 24 hrs rep 3Cholesterol0.348.250.25Nesbitt NM, et al. (2010)
CDC1551 wild type vs kstR null rep 1Wild type vs Mutant1.095.930.67Nesbitt NM, et al. (2010)
CDC1551 wild type vs kstR null rep 2Wild type vs Mutant-1.135.780.86Nesbitt NM, et al. (2010)
CDC1551 wild type vs kstR null rep 3Wild type vs Mutant0.316.360.20Nesbitt NM, et al. (2010)
CDC1551 wild type vs kstR null in 1mg/ml cholesterol for 24 hrs rep 1Cholesterol-0.315.960.26Nesbitt NM, et al. (2010)
CDC1551 wild type vs kstR null in 1mg/ml cholesterol for 24 hrs rep 2Cholesterol0.047.870.27Nesbitt NM, et al. (2010)
CDC1551 wild type vs kstR null in 1mg/ml cholesterol for 24 hrs rep 3Cholesterol-0.316.610.31Nesbitt NM, et al. (2010)
H37Rv wt vs dosS null rapid anaerobic dormancy day 6 rep 1Wild type vs Mutant0.335.530.26Honaker RW, et al. (2009)
H37Rv wt vs dosS null rapid anaerobic dormancy day 6 rep 2Wild type vs Mutant0.096.210.08Honaker RW, et al. (2009)
H37Rv wt vs dosS null rapid anaerobic dormancy day 6 rep 3Wild type vs Mutant0.133.640.12Honaker RW, et al. (2009)
H37Rv wt vs dosT null rapid anaerobic dormancy day 6 rep 1Wild type vs Mutant0.315.510.19Honaker RW, et al. (2009)
H37Rv wt vs dosT null rapid anaerobic dormancy day 6 rep 2Wild type vs Mutant0.305.580.34Honaker RW, et al. (2009)
H37Rv wt vs dosT null rapid anaerobic dormancy day 6 rep 3Wild type vs Mutant0.446.170.32Honaker RW, et al. (2009)
H37Rv wt vs dosS/dosT null rapid anaerobic dormancy day 6 rep 2Wild type vs Mutant-0.715.970.46Honaker RW, et al. (2009)
H37Rv wt vs dosS/dosT null rapid anaerobic dormancy day 6 rep 3Wild type vs Mutant-2.554.761.48Honaker RW, et al. (2009)
H37Rv wt vs dosS/dosT null dosT complemented rapid anaerobic dormancy day 6 rep 1Wild type vs Mutant0.295.920.17Honaker RW, et al. (2009)
H37Rv wt vs dosS/dosT null dosT complemented rapid anaerobic dormancy day 6 rep 2Wild type vs Mutant-1.614.291.66Honaker RW, et al. (2009)
H37Rv wt vs dosS/dosT null dosT complemented rapid anaerobic dormancy day 6 rep 3Wild type vs Mutant-1.584.701.20Honaker RW, et al. (2009)
H37Rv wt vs dosT null anaerobic Gaspak 4hr rep 1Wild type vs Mutant-0.047.410.14Honaker RW, et al. (2009)
H37Rv wt vs dosT null anaerobic Gaspak 4hr rep 2Wild type vs Mutant0.418.050.57Honaker RW, et al. (2009)
H37Rv wt vs dosT null anaerobic Gaspak 4hr rep 3Wild type vs Mutant0.285.500.14Honaker RW, et al. (2009)
H37Rv wt vs dosS null anaerobic Gaspak 4hr rep 1Wild type vs Mutant-0.538.280.84Honaker RW, et al. (2009)
H37Rv wt vs dosS null anaerobic Gaspak 4hr rep 2Wild type vs Mutant-0.327.940.36Honaker RW, et al. (2009)
H37Rv wt vs dosS/dosT null anaerobic Gaspak 4hr rep 1Wild type vs Mutant0.897.160.50Honaker RW, et al. (2009)
H37Rv wt vs dosS/dosT null anaerobic Gaspak 4hr rep 2Wild type vs Mutant1.056.900.76Honaker RW, et al. (2009)
H37Rv wt vs dosS/dosT null anaerobic Gaspak 4hr rep 3Wild type vs Mutant1.646.750.75Honaker RW, et al. (2009)
H37Rv wt vs dosT null anaerobic Gaspak24hr rep 1Wild type vs Mutant-0.065.580.13Honaker RW, et al. (2009)
H37Rv wt vs dosT null anaerobic Gaspak24hr rep 2Wild type vs Mutant-0.736.690.73Honaker RW, et al. (2009)
H37Rv wt vs dosT null anaerobic Gaspak24hr rep 3Wild type vs Mutant-0.254.390.36Honaker RW, et al. (2009)
H37Rv wt vs dosS null anaerobic Gaspak 24hr rep 2Wild type vs Mutant0.717.380.53Honaker RW, et al. (2009)
H37Rv wt vs dosS null anaerobic Gaspak 24hr rep 3Wild type vs Mutant-3.982.792.21Honaker RW, et al. (2009)
H37Rv wt vs dosS/dosT null anaerobic Gaspak24hr rep 1Wild type vs Mutant-1.566.660.84Honaker RW, et al. (2009)
H37Rv wt vs dosS/dosT null anaerobic Gaspak24hr rep 2Wild type vs Mutant-0.826.370.74Honaker RW, et al. (2009)
H37Rv wt vs dosS/dosT null anaerobic Gaspak24hr rep 3Wild type vs Mutant0.376.470.21Honaker RW, et al. (2009)
H37Rv wt vs dosS null nitric oxide treatment 1hr rep 1Wild type vs Mutant0.257.040.07Honaker RW, et al. (2009)
H37Rv wt vs dosS null nitric oxide treatment 1hr rep 2Wild type vs Mutant-0.237.880.46Honaker RW, et al. (2009)
H37Rv wt vs dosS null nitric oxide treatment 1hr rep 3Wild type vs Mutant-0.096.830.08Honaker RW, et al. (2009)
H37Rv wt vs dosS null nitric oxide treatment 1hr rep 4Wild type vs Mutant-0.467.870.82Honaker RW, et al. (2009)
H37Rv wt vs dosT null nitric oxide treatment 1hr rep 1Wild type vs Mutant-0.048.010.22Honaker RW, et al. (2009)
H37Rv wt vs dosT null nitric oxide treatment 1hr rep 2Wild type vs Mutant0.607.660.37Honaker RW, et al. (2009)
H37Rv wt vs dosT null nitric oxide treatment 1hr rep 3Wild type vs Mutant0.068.700.14Honaker RW, et al. (2009)
CDC1551 Ctrl vs clinical isolate 10514-01_Afri2 rep 1Strain comparison0.119.170.21Homolka S, et al. (2010)
CDC1551 Ctrl vs clinical isolate 10514-01_Afri2 rep 2Strain comparison-0.329.240.91Homolka S, et al. (2010)
CDC1551 Ctrl vs clinical isolate 10514-01_Afri2 rep 3Strain comparison-0.118.190.17Homolka S, et al. (2010)
CDC1551 Ctrl vs clinical isolate 10517-01_Afri2 rep 1Strain comparison0.118.760.34Homolka S, et al. (2010)
CDC1551 Ctrl vs clinical isolate 10517-01_Afri2 rep 2Strain comparison-0.129.560.32Homolka S, et al. (2010)
CDC1551 Ctrl vs clinical isolate 10517-01_Afri2 rep 3Strain comparison-0.128.020.09Homolka S, et al. (2010)
CDC1551 Ctrl vs clinical isolate 12954-03_Beijing rep 1Strain comparison-0.247.930.40Homolka S, et al. (2010)
CDC1551 Ctrl vs clinical isolate 12954-03_Beijing rep 2Strain comparison-0.419.311.04Homolka S, et al. (2010)
CDC1551 Ctrl vs clinical isolate 12954-03_Beijing rep 3Strain comparison0.058.140.13Homolka S, et al. (2010)
CDC1551 Ctrl vs clinical isolate 1500-03_Beijing rep 1Strain comparison-0.278.470.54Homolka S, et al. (2010)
CDC1551 Ctrl vs clinical isolate 1500-03_Beijing rep 2Strain comparison-0.239.270.71Homolka S, et al. (2010)
CDC1551 Ctrl vs clinical isolate 1500-03_Beijing rep 3Strain comparison-0.138.390.10Homolka S, et al. (2010)
CDC1551 Ctrl vs clinical isolate 1797-03_EAI rep 1Strain comparison0.199.310.36Homolka S, et al. (2010)
CDC1551 Ctrl vs clinical isolate 1797-03_EAI rep 2Strain comparison0.0110.090.03Homolka S, et al. (2010)
CDC1551 Ctrl vs clinical isolate 1797-03_EAI rep 3Strain comparison0.138.710.30Homolka S, et al. (2010)
CDC1551 Ctrl vs clinical isolate 1934-03_Beijing rep 1Strain comparison0.108.370.06Homolka S, et al. (2010)
CDC1551 Ctrl vs clinical isolate 1934-03_Beijing rep 2Strain comparison-0.449.800.92Homolka S, et al. (2010)
CDC1551 Ctrl vs clinical isolate 1934-03_Beijing rep 3Strain comparison0.278.090.44Homolka S, et al. (2010)
CDC1551 Ctrl vs clinical isolate 2169-99_Uganda rep 1Strain comparison0.219.220.44Homolka S, et al. (2010)
CDC1551 Ctrl vs clinical isolate 2169-99_Uganda rep 2Strain comparison-0.079.690.21Homolka S, et al. (2010)
CDC1551 Ctrl vs clinical isolate 2169-99_Uganda rep 3Strain comparison0.188.760.39Homolka S, et al. (2010)
CDC1551 Ctrl vs clinical isolate 2199-99_Uganda rep 1Strain comparison0.568.650.74Homolka S, et al. (2010)
CDC1551 Ctrl vs clinical isolate 2199-99_Uganda rep 2Strain comparison-0.329.600.96Homolka S, et al. (2010)
CDC1551 Ctrl vs clinical isolate 2199-99_Uganda rep 3Strain comparison-0.168.020.15Homolka S, et al. (2010)
CDC1551 Ctrl vs clinical isolate 2333-99_Uganda rep 1Strain comparison0.049.040.04Homolka S, et al. (2010)
CDC1551 Ctrl vs clinical isolate 2333-99_Uganda rep 2Strain comparison-0.688.881.12Homolka S, et al. (2010)
CDC1551 Ctrl vs clinical isolate 2333-99_Uganda rep 3Strain comparison0.098.840.27Homolka S, et al. (2010)
CDC1551 Ctrl vs clinical isolate 2336-02_Haarlem rep 1Strain comparison-0.148.250.30Homolka S, et al. (2010)
CDC1551 Ctrl vs clinical isolate 2336-02_Haarlem rep 2Strain comparison-0.329.870.80Homolka S, et al. (2010)
CDC1551 Ctrl vs clinical isolate 2336-02_Haarlem rep 3Strain comparison0.747.860.83Homolka S, et al. (2010)
CDC1551 Ctrl vs clinical isolate 4130-02_Haarlem rep 1Strain comparison0.118.740.13Homolka S, et al. (2010)
CDC1551 Ctrl vs clinical isolate 4130-02_Haarlem rep 2Strain comparison-0.249.960.64Homolka S, et al. (2010)
CDC1551 Ctrl vs clinical isolate 4130-02_Haarlem rep 3Strain comparison0.128.410.20Homolka S, et al. (2010)
CDC1551 Ctrl vs clinical isolate 4850-03_EAI rep 1Strain comparison0.298.990.64Homolka S, et al. (2010)
CDC1551 Ctrl vs clinical isolate 4850-03_EAI rep 2Strain comparison-0.289.170.55Homolka S, et al. (2010)
CDC1551 Ctrl vs clinical isolate 4850-03_EAI rep 3Strain comparison0.198.490.39Homolka S, et al. (2010)
CDC1551 Ctrl vs clinical isolate 5468-02_Afri2 rep 1Strain comparison-0.508.040.55Homolka S, et al. (2010)
CDC1551 Ctrl vs clinical isolate 5468-02_Afri2 rep 2Strain comparison-0.409.610.79Homolka S, et al. (2010)
CDC1551 Ctrl vs clinical isolate 5468-02_Afri2 rep 3Strain comparison0.058.290.17Homolka S, et al. (2010)
CDC1551 Ctrl vs clinical isolate 947-01_EAI rep 1Strain comparison0.078.960.12Homolka S, et al. (2010)
CDC1551 Ctrl vs clinical isolate 947-01_EAI rep 2Strain comparison-0.439.581.13Homolka S, et al. (2010)
CDC1551 Ctrl vs clinical isolate 947-01_EAI rep 3Strain comparison0.338.710.66Homolka S, et al. (2010)
CDC1551 Ctrl vs clinical isolate 9532-03_Haarlem rep 1Strain comparison0.098.950.17Homolka S, et al. (2010)
CDC1551 Ctrl vs clinical isolate 9532-03_Haarlem rep 2Strain comparison-0.429.681.22Homolka S, et al. (2010)
CDC1551 Ctrl vs clinical isolate 9532-03_Haarlem rep 3Strain comparison0.148.970.35Homolka S, et al. (2010)
CDC1551 Ctrl vs H37Rv rep 1Strain comparison-0.018.790.03Homolka S, et al. (2010)
CDC1551 Ctrl vs H37Rv rep 2Strain comparison-0.389.651.14Homolka S, et al. (2010)
CDC1551 Ctrl vs H37Rv rep 3Strain comparison0.158.650.30Homolka S, et al. (2010)
CDC1551 extra vs intracellular in resting macrophages rep 1Grown in macrophages0.3310.320.48Homolka S, et al. (2010)
CDC1551 extra vs intracellular in resting macrophages rep 2Grown in macrophages-0.248.670.16Homolka S, et al. (2010)
Clinical isolate 10514-01_Afri2 extra vs intracellular in resting macrophages rep 1Grown in macrophages1.059.321.28Homolka S, et al. (2010)
Clinical isolate 10514-01_Afri2 extra vs intracellular in resting macrophages rep 2Grown in macrophages-0.039.610.10Homolka S, et al. (2010)
Clinical isolate 10517-01_Afri2 extra vs intracellular in resting macrophages rep 1Grown in macrophages1.079.601.19Homolka S, et al. (2010)
Clinical isolate 10517-01_Afri2 extra vs intracellular in resting macrophages rep 2Grown in macrophages-0.309.080.32Homolka S, et al. (2010)
Clinical isolate 12954-03_Beijing extra vs intracellular in resting macrophages rep 1Grown in macrophages0.669.800.79Homolka S, et al. (2010)
Clinical isolate 12954-03_Beijing extra vs intracellular in resting macrophages rep 2Grown in macrophages-0.349.030.24Homolka S, et al. (2010)
Clinical isolate 1500-03_Beijing extra vs intracellular in resting macrophages rep 1Grown in macrophages0.2710.120.36Homolka S, et al. (2010)
Clinical isolate 1500-03_Beijing extra vs intracellular in resting macrophages rep 2Grown in macrophages-0.538.920.59Homolka S, et al. (2010)
Clinical isolate 1797-03_EAI extra vs intracellular in resting macrophages rep 1Grown in macrophages-0.0210.390.14Homolka S, et al. (2010)
Clinical isolate 1797-03_EAI extra vs intracellular in resting macrophages rep 2Grown in macrophages-0.508.760.58Homolka S, et al. (2010)
Clinical isolate 1934-03_Beijing extra vs intracellular in resting macrophages rep 1Grown in macrophages0.159.510.11Homolka S, et al. (2010)
Clinical isolate 1934-03_Beijing extra vs intracellular in resting macrophages rep 2Grown in macrophages0.389.500.57Homolka S, et al. (2010)
Clinical isolate 2169-99_Uganda extra vs intracellular in resting macrophages rep 1Grown in macrophages0.259.750.18Homolka S, et al. (2010)
Clinical isolate 2169-99_Uganda extra vs intracellular in resting macrophages rep 2Grown in macrophages-0.898.720.64Homolka S, et al. (2010)
Clinical isolate 2191-99_Uganda extra vs intracellular in resting macrophages rep 1Grown in macrophages0.248.420.41Homolka S, et al. (2010)
Clinical isolate 2191-99_Uganda extra vs intracellular in resting macrophages rep 2Grown in macrophages-0.249.220.14Homolka S, et al. (2010)
Clinical isolate 2333-99_Uganda extra vs intracellular in resting macrophages rep 1Grown in macrophages0.759.630.87Homolka S, et al. (2010)
Clinical isolate 2333-99_Uganda extra vs intracellular in resting macrophages rep 2Grown in macrophages-0.728.700.46Homolka S, et al. (2010)
Clinical isolate 2336-02_Haarlem extra vs intracellular in resting macrophages rep 1Grown in macrophages0.3410.320.56Homolka S, et al. (2010)
Clinical isolate 2336-02_Haarlem extra vs intracellular in resting macrophages rep 2Grown in macrophages0.368.840.48Homolka S, et al. (2010)
Clinical isolate 4130-02_Haarlem extra vs intracellular in resting macrophages rep 1Grown in macrophages0.3610.070.67Homolka S, et al. (2010)
Clinical isolate 4130-02_Haarlem extra vs intracellular in resting macrophages rep 2Grown in macrophages-0.049.340.08Homolka S, et al. (2010)
Clinical isolate 4850-03_EAI extra vs intracellular in resting macrophages rep 1Grown in macrophages0.159.760.20Homolka S, et al. (2010)
Clinical isolate 4850-03_EAI extra vs intracellular in resting macrophages rep 2Grown in macrophages0.019.100.03Homolka S, et al. (2010)
Clinical isolate 5468-02_Afri2 extra vs intracellular in resting macrophages rep 1Grown in macrophages0.639.350.53Homolka S, et al. (2010)
Clinical isolate 5468-02_Afri2 extra vs intracellular in resting macrophages rep 2Grown in macrophages-0.349.000.29Homolka S, et al. (2010)
Clinical isolate 947-01_EAI extra vs intracellular in resting macrophages rep 1Grown in macrophages0.069.810.00Homolka S, et al. (2010)
Clinical isolate 947-01_EAI extra vs intracellular in resting macrophages rep 2Grown in macrophages-0.608.750.69Homolka S, et al. (2010)
Clinical isolate 9532-03_Haarlem extra vs intracellular in resting macrophages rep 1Grown in macrophages0.7310.101.20Homolka S, et al. (2010)
Clinical isolate 9532-03_Haarlem extra vs intracellular in resting macrophages rep 2Grown in macrophages0.669.240.81Homolka S, et al. (2010)
H37Rv extra vs intracellular in resting macrophages rep 1Grown in macrophages0.1510.340.20Homolka S, et al. (2010)
H37Rv extra vs intracellular in resting macrophages rep 2Grown in macrophages-0.449.610.67Homolka S, et al. (2010)
Clinical isolate 10514-01_Afri2 extra vs intracellular in activated macrophages rep 1Grown in macrophages-0.776.690.71Homolka S, et al. (2010)
Clinical isolate 10514-01_Afri2 extra vs intracellular in activated macrophages rep 2Grown in macrophages0.739.351.14Homolka S, et al. (2010)
Clinical isolate 10517-01_Afri2 extra vs intracellular in activated macrophages rep 1Grown in macrophages-0.607.831.05Homolka S, et al. (2010)
Clinical isolate 10517-01_Afri2 extra vs intracellular in activated macrophages rep 2Grown in macrophages-0.668.380.92Homolka S, et al. (2010)
Clinical isolate 12954-03_Beijing extra vs intracellular in activated macrophages rep 1Grown in macrophages0.709.090.82Homolka S, et al. (2010)
Clinical isolate 12954-03_Beijing extra vs intracellular in activated macrophages rep 2Grown in macrophages0.678.530.97Homolka S, et al. (2010)
Clinical isolate 1500-03_Beijing extra vs intracellular in activated macrophages rep 1Grown in macrophages1.278.701.32Homolka S, et al. (2010)
Clinical isolate 1500-03_Beijing extra vs intracellular in activated macrophages rep 2Grown in macrophages0.569.410.68Homolka S, et al. (2010)
Clinical isolate 1797-03_EAI extra vs intracellular in activated macrophages rep 1Grown in macrophages-0.429.310.35Homolka S, et al. (2010)
Clinical isolate 1797-03_EAI extra vs intracellular in activated macrophages rep 2Grown in macrophages-0.298.660.46Homolka S, et al. (2010)
Clinical isolate 1934-03_Beijing extra vs intracellular in activated macrophages rep 1Grown in macrophages0.409.520.56Homolka S, et al. (2010)
Clinical isolate 1934-03_Beijing extra vs intracellular in activated macrophages rep 2Grown in macrophages0.527.840.65Homolka S, et al. (2010)
Clinical isolate 2169-99_Uganda extra vs intracellular in activated macrophages rep 1Grown in macrophages-0.548.280.84Homolka S, et al. (2010)
Clinical isolate 2169-99_Uganda extra vs intracellular in activated macrophages rep 2Grown in macrophages-0.398.510.82Homolka S, et al. (2010)
Clinical isolate 2191-99_Uganda extra vs intracellular in activated macrophages rep 1Grown in macrophages-0.218.440.34Homolka S, et al. (2010)
Clinical isolate 2191-99_Uganda extra vs intracellular in activated macrophages rep 2Grown in macrophages-0.329.220.55Homolka S, et al. (2010)
Clinical isolate 2333-99_Uganda extra vs intracellular in activated macrophages rep 1Grown in macrophages0.288.090.45Homolka S, et al. (2010)
Clinical isolate 2333-99_Uganda extra vs intracellular in activated macrophages rep 2Grown in macrophages0.078.460.06Homolka S, et al. (2010)
Clinical isolate 2336-02_Haarlem extra vs intracellular in activated macrophages rep 1Grown in macrophages0.519.210.77Homolka S, et al. (2010)
Clinical isolate 2336-02_Haarlem extra vs intracellular in activated macrophages rep 2Grown in macrophages0.508.870.80Homolka S, et al. (2010)
Clinical isolate 4130-02_Haarlem extra vs intracellular in activated macrophages rep 1Grown in macrophages1.168.891.32Homolka S, et al. (2010)
Clinical isolate 4130-02_Haarlem extra vs intracellular in activated macrophages rep 2Grown in macrophages-0.257.510.30Homolka S, et al. (2010)
Clinical isolate 4850-03_EAI extra vs intracellular in activated macrophages rep 1Grown in macrophages0.069.020.23Homolka S, et al. (2010)
Clinical isolate 4850-03_EAI extra vs intracellular in activated macrophages rep 2Grown in macrophages0.198.540.22Homolka S, et al. (2010)
Clinical isolate 5468-02_Afri2 extra vs intracellular in activated macrophages rep 1Grown in macrophages0.278.160.27Homolka S, et al. (2010)
Clinical isolate 5468-02_Afri2 extra vs intracellular in activated macrophages rep 2Grown in macrophages-0.318.310.54Homolka S, et al. (2010)
Clinical isolate 947-01_EAI extra vs intracellular in activated macrophages rep 1Grown in macrophages-1.547.111.46Homolka S, et al. (2010)
Clinical isolate 947-01_EAI extra vs intracellular in activated macrophages rep 2Grown in macrophages-0.438.330.62Homolka S, et al. (2010)
Clinical isolate 9532-03_Haarlem extra vs intracellular in activated macrophages rep 1Grown in macrophages0.499.040.66Homolka S, et al. (2010)
Clinical isolate 9532-03_Haarlem extra vs intracellular in activated macrophages rep 2Grown in macrophages-0.218.070.26Homolka S, et al. (2010)
H37Rv extra vs intracellular in activated macrophages rep 1Grown in macrophages-0.498.400.12Homolka S, et al. (2010)
H37Rv extra vs intracellular in activated macrophages rep 2Grown in macrophages-0.178.020.29Homolka S, et al. (2010)
CDC1551 extra vs intracellular in activated macrophages rep 1Grown in macrophages-0.118.560.07Homolka S, et al. (2010)
CDC1551 extra vs intracellular in activated macrophages rep 2Grown in macrophages-0.779.060.82Homolka S, et al. (2010)
H37Rv wild type vs PepD null mutant rep 1Wild type vs Mutant0.669.341.00White MJ, et al. (2010)
H37Rv wild type vs PepD null mutant (DS) rep 1Wild type vs Mutant-0.358.780.61White MJ, et al. (2010)
H37Rv wild type vs PepD null mutant rep 2Wild type vs Mutant0.649.530.99White MJ, et al. (2010)
H37Rv wild type vs PepD null mutant (DS) rep 2Wild type vs Mutant-0.408.210.72White MJ, et al. (2010)
H37Rv wild type vs PepD null mutant rep 3Wild type vs Mutant0.3110.320.47White MJ, et al. (2010)
CDC1551 wild type vs aprABC null mutant rep 1Wild type vs Mutant0.0110.990.12Abramovitch RB, et al. (2011)
CDC1551 wild type vs aprABC null mutant rep 2Wild type vs Mutant0.0910.720.07Abramovitch RB, et al. (2011)
CDC1551 wild type vs aprABC null mutant rep 3Wild type vs Mutant0.3710.520.71Abramovitch RB, et al. (2011)
CDC1551 wild type vs aprBC null mutant rep 1Wild type vs Mutant-0.0711.990.39Abramovitch RB, et al. (2011)
CDC1551 wild type vs aprBC null mutant rep 2Wild type vs Mutant0.0410.630.02Abramovitch RB, et al. (2011)
CDC1551 wild type vs aprBC null mutant rep 3Wild type vs Mutant0.1411.190.34Abramovitch RB, et al. (2011)
CDC1551 wild type vs aprC null mutant rep 1Wild type vs Mutant-0.1011.130.50Abramovitch RB, et al. (2011)
CDC1551 wild type vs aprC null mutant rep 2Wild type vs Mutant-0.0710.760.43Abramovitch RB, et al. (2011)
CDC1551 wild type vs aprC null mutant rep 3Wild type vs Mutant0.4510.890.98Abramovitch RB, et al. (2011)
CDC1551 wild type vs phoP Tn mutant rep 1Wild type vs Mutant-0.1511.430.51Abramovitch RB, et al. (2011)
CDC1551 wild type vs phoP Tn mutant rep 2Wild type vs Mutant0.0610.760.01Abramovitch RB, et al. (2011)
CDC1551 wild type vs phoP Tn mutant rep 3Wild type vs Mutant0.1810.760.22Abramovitch RB, et al. (2011)
CDC1551 ctrl vs ctrl at 0 hr rep 1Control0.4010.260.93Dutta NK, et al. (2010)
CDC1551 ctrl vs ctrl at 0 hr rep 2Control-0.339.471.17Dutta NK, et al. (2010)
CDC1551 ctrl vs 10 ug/ml Thioridazine 1hr rep 1Thioridazine-0.866.580.81Dutta NK, et al. (2010)
CDC1551 ctrl vs 10 ug/ml Thioridazine 1hr rep 2Thioridazine-1.515.751.17Dutta NK, et al. (2010)
CDC1551 ctrl vs 40 ug/ml Thioridazine 1hr rep 1Thioridazine-0.906.910.96Dutta NK, et al. (2010)
CDC1551 ctrl vs 40 ug/ml Thioridazine 1hr rep 2Thioridazine-0.913.890.55Dutta NK, et al. (2010)
CDC1551 ctrl vs 10 ug/ml Thioridazine 2hr rep 1Thioridazine-1.789.101.28Dutta NK, et al. (2010)
CDC1551 ctrl vs 10 ug/ml Thioridazine 2hr rep 2Thioridazine-0.4210.990.79Dutta NK, et al. (2010)
CDC1551 ctrl vs 40 ug/ml Thioridazine 2hr rep 1Thioridazine-0.8510.241.50Dutta NK, et al. (2010)
CDC1551 ctrl vs 40 ug/ml Thioridazine 2hr rep 2Thioridazine-1.709.521.31Dutta NK, et al. (2010)
CDC1551 ctrl vs 10 ug/ml Thioridazine 4hr rep 1Thioridazine-1.708.061.36Dutta NK, et al. (2010)
CDC1551 ctrl vs 10 ug/ml Thioridazine 4hr rep 2Thioridazine-0.589.660.45Dutta NK, et al. (2010)
CDC1551 ctrl vs 40 ug/ml Thioridazine 4hr rep 1Thioridazine-0.919.980.84Dutta NK, et al. (2010)
CDC1551 ctrl vs 40 ug/ml Thioridazine 4hr rep 2Thioridazine-0.7210.380.65Dutta NK, et al. (2010)
CDC1551 ctrl vs 10 ug/ml Thioridazine 6hr rep 1Thioridazine-1.775.411.00Dutta NK, et al. (2010)
CDC1551 ctrl vs 10 ug/ml Thioridazine 6hr rep 2Thioridazine-1.167.210.88Dutta NK, et al. (2010)
CDC1551 ctrl vs 40 ug/ml Thioridazine 6hr rep 1Thioridazine-0.2710.790.31Dutta NK, et al. (2010)
CDC1551 ctrl vs 40 ug/ml Thioridazine 6hr rep 2Thioridazine0.886.720.87Dutta NK, et al. (2010)
H37Rv ctrl vs 1ug/ml Isoniazid for 2hrs rep 1Isoniazid0.359.510.61Karakousis PC, et al. (2008)
H37Rv ctrl vs 1ug/ml Isoniazid for 2hrs rep 2Isoniazid-0.399.710.92Karakousis PC, et al. (2008)
H37Rv ctrl vs 1ug/ml Isoniazid for 2hrs rep 3Isoniazid0.0310.630.01Karakousis PC, et al. (2008)
H37Rv ctrl vs 1ug/ml Isoniazid for 6hrs rep 1Isoniazid0.499.561.29Karakousis PC, et al. (2008)
H37Rv ctrl vs 1ug/ml Isoniazid for 6hrs rep 2Isoniazid-0.098.860.13Karakousis PC, et al. (2008)
H37Rv ctrl vs 1ug/ml Isoniazid for 6hrs rep 3Isoniazid0.5410.490.80Karakousis PC, et al. (2008)
H37Rv KatG null, ctrl vs 1ug/ml Isoniazid for 2hrs rep 1Isoniazid-0.5610.490.78Karakousis PC, et al. (2008)
H37Rv KatG null, ctrl vs 1ug/ml Isoniazid for 2hrs rep 2Isoniazid-0.3910.081.34Karakousis PC, et al. (2008)
H37Rv KatG null, ctrl vs 1ug/ml Isoniazid for 2hrs rep 3Isoniazid-0.539.010.56Karakousis PC, et al. (2008)
H37Rv nutrient starved, ctrl vs 1ug/ml Isoniazid for 2hrs rep 1Isoniazid-0.255.650.29Karakousis PC, et al. (2008)
H37Rv nutrient starved, ctrl vs 1ug/ml Isoniazid for 2hrs rep 2Isoniazid-0.174.900.28Karakousis PC, et al. (2008)
H37Rv O2 depleted, ctrl vs 1ug/ml Isoniazid for 2hrs rep 1Isoniazid-0.045.410.11Karakousis PC, et al. (2008)
H37Rv O2 depleted, ctrl vs 1ug/ml Isoniazid for 2hrs rep 3Isoniazid-0.446.370.45Karakousis PC, et al. (2008)
H37Rv mouse hallow fiber, ctrl vs 25mg/kg Isoniazid 3rd dose 6hrs rep 1Isoniazid0.175.700.10Karakousis PC, et al. (2008)
H37Rv mouse hallow fiber, ctrl vs 25mg/kg Isoniazid 3rd dose 6hrs rep 2Isoniazid0.339.350.31Karakousis PC, et al. (2008)
H37Rv ctrl vs relE1 overexpression 6 hr rep 1Wild type vs overexpression0.348.760.32Singh R, et al. (2010)
H37Rv ctrl vs relE1 overexpression 6 hr rep 2Wild type vs overexpression0.157.350.21Singh R, et al. (2010)
H37Rv ctrl vs relE1 overexpression 6 hr rep 3Wild type vs overexpression0.1210.510.25Singh R, et al. (2010)
H37Rv ctrl vs relE1 overexpression 6 hr rep 4Wild type vs overexpression0.657.590.03Singh R, et al. (2010)
H37Rv ctrl vs relE1 overexpression 24 hr rep 1Wild type vs overexpression-1.617.800.80Singh R, et al. (2010)
H37Rv ctrl vs relE1 overexpression 24 hr rep 2Wild type vs overexpression0.2910.900.44Singh R, et al. (2010)
H37Rv ctrl vs relE1 overexpression 72 hr rep 1Wild type vs overexpression0.544.970.23Singh R, et al. (2010)
H37Rv ctrl vs relE1 overexpression 72 hr rep 2Wild type vs overexpression-1.307.010.62Singh R, et al. (2010)
H37Rv ctrl vs relE1 overexpression 72 hr rep 3Wild type vs overexpression-0.399.950.61Singh R, et al. (2010)
H37Rv ctrl vs relE1 overexpression 72 hr rep 4Wild type vs overexpression-0.409.950.63Singh R, et al. (2010)
H37Rv ctrl vs relE2 overexpression 6 hr rep 1Wild type vs overexpression0.577.580.89Singh R, et al. (2010)
H37Rv ctrl vs relE2 overexpression 6 hr rep 2Wild type vs overexpression0.238.420.10Singh R, et al. (2010)
H37Rv ctrl vs relE2 overexpression 6 hr rep 3Wild type vs overexpression0.4410.950.99Singh R, et al. (2010)
H37Rv ctrl vs relE2 overexpression 24 hr rep 1Wild type vs overexpression1.504.920.38Singh R, et al. (2010)
H37Rv ctrl vs relE2 overexpression 24 hr rep 2Wild type vs overexpression-0.228.240.40Singh R, et al. (2010)
H37Rv ctrl vs relE2 overexpression 24 hr rep 3Wild type vs overexpression0.3010.720.60Singh R, et al. (2010)
H37Rv ctrl vs relE2 overexpression 72 hr rep 1Wild type vs overexpression0.718.360.10Singh R, et al. (2010)
H37Rv ctrl vs relE2 overexpression 72 hr rep 2Wild type vs overexpression0.877.490.74Singh R, et al. (2010)
H37Rv ctrl vs relE2 overexpression 72 hr rep 3Wild type vs overexpression0.578.281.29Singh R, et al. (2010)
H37Rv ctrl vs relE2 overexpression 72 hr rep 4Wild type vs overexpression-0.019.640.04Singh R, et al. (2010)
H37Rv ctrl vs relE2 overexpression 72 hr rep 5Wild type vs overexpression-0.009.640.03Singh R, et al. (2010)
H37Rv ctrl vs relE3 overexpression 6 hr rep 1Wild type vs overexpression0.236.870.35Singh R, et al. (2010)
H37Rv ctrl vs relE3 overexpression 6 hr rep 2Wild type vs overexpression0.258.920.01Singh R, et al. (2010)
H37Rv ctrl vs relE3 overexpression 6 hr rep 3Wild type vs overexpression-0.3411.040.72Singh R, et al. (2010)
H37Rv ctrl vs relE3 overexpression 6 hr rep 4Wild type vs overexpression0.835.370.22Singh R, et al. (2010)
H37Rv ctrl vs relE3 overexpression 24 hr rep 1Wild type vs overexpression-0.0210.190.14Singh R, et al. (2010)
H37Rv ctrl vs relE3 overexpression 24 hr rep 2Wild type vs overexpression0.247.550.22Singh R, et al. (2010)
H37Rv ctrl vs relE3 overexpression 72 hr rep 1Wild type vs overexpression0.807.950.23Singh R, et al. (2010)
H37Rv ctrl vs relE3 overexpression 72 hr rep 2Wild type vs overexpression0.898.851.72Singh R, et al. (2010)
H37Rv ctrl vs relE3 overexpression 72 hr rep 3Wild type vs overexpression1.738.211.23Singh R, et al. (2010)
H37Rv ctrl vs relE3 overexpression 72 hr rep 4Wild type vs overexpression-0.148.950.28Singh R, et al. (2010)
H37Rv ctrl vs relE3 overexpression 72 hr rep 5Wild type vs overexpression-0.138.950.27Singh R, et al. (2010)
H37Rv reaeration for 1hrs rep 1Reaeration-0.297.280.42Sherrid AM, et al. (2010)
H37Rv reaeration for 1hrs rep 2Reaeration-0.796.470.78Sherrid AM, et al. (2010)
H37Rv reaeration for 1hrs rep 3Reaeration-0.776.491.05Sherrid AM, et al. (2010)
H37Rv reaeration for 1hrs rep 4Reaeration-0.896.920.86Sherrid AM, et al. (2010)
H37Rv reaeration for 4hrs rep 1Reaeration-0.477.160.45Sherrid AM, et al. (2010)
H37Rv reaeration for 4hrs rep 2Reaeration-0.576.880.62Sherrid AM, et al. (2010)
H37Rv reaeration for 4hrs rep 3Reaeration-0.537.270.66Sherrid AM, et al. (2010)
H37Rv reaeration for 4hrs rep 4Reaeration0.326.860.50Sherrid AM, et al. (2010)
H37Rv reaeration for 1hrs rep 5Reaeration-0.097.560.12Sherrid AM, et al. (2010)
H37Rv reaeration for 1hrs rep 6Reaeration-2.165.131.14Sherrid AM, et al. (2010)
H37Rv reaeration for 1hrs rep 7Reaeration-1.683.270.40Sherrid AM, et al. (2010)
H37Rv reaeration for 1hrs rep 8Reaeration0.956.830.69Sherrid AM, et al. (2010)
H37Rv reaeration for 4hrs rep 5Reaeration0.646.310.16Sherrid AM, et al. (2010)
H37Rv reaeration for 4hrs rep 6Reaeration-1.876.451.22Sherrid AM, et al. (2010)
H37Rv reaeration for 4hrs rep 7Reaeration0.006.570.19Sherrid AM, et al. (2010)
H37Rv reaeration for 4hrs rep 8Reaeration1.437.291.01Sherrid AM, et al. (2010)
H37Rv reaeration for 24hrs rep 5Reaeration-2.238.641.72Sherrid AM, et al. (2010)
H37Rv reaeration for 24hrs rep 6Reaeration-1.988.441.91Sherrid AM, et al. (2010)
H37Rv reaeration for 6hrs rep 2Reaeration-0.131.200.65Sherrid AM, et al. (2010)
H37Rv reaeration for 6hrs rep 3Reaeration-0.191.360.34Sherrid AM, et al. (2010)
H37Rv reaeration for 6hrs rep 4Reaeration-1.082.200.32Sherrid AM, et al. (2010)
H37Rv reaeration for 6hrs rep 5Reaeration1.675.020.91Sherrid AM, et al. (2010)
H37Rv reaeration for 12hrs rep 1Reaeration-0.927.700.64Sherrid AM, et al. (2010)
H37Rv reaeration for 12hrs rep 2Reaeration-1.157.101.09Sherrid AM, et al. (2010)
H37Rv reaeration for 12hrs rep 5Reaeration0.103.880.21Sherrid AM, et al. (2010)
H37Rv reaeration for 12hrs rep 6Reaeration5.003.901.92Sherrid AM, et al. (2010)
H37Rv reaeration for 24hrs rep 1Reaeration-2.0111.221.80Sherrid AM, et al. (2010)
H37Rv reaeration for 24hrs rep 2Reaeration-1.5011.011.01Sherrid AM, et al. (2010)
H37Rv reaeration for 24hrs rep 4Reaeration-1.570.790.09Sherrid AM, et al. (2010)
H37Rv maltose-1-phosphate stress stimulon rep 2Null mutant vs complemented null mutant1.9010.341.31Kalscheuer R, et al. (2010)
H37Rv maltose-1-phosphate stress stimulon rep 3Null mutant vs complemented null mutant1.478.360.63Kalscheuer R, et al. (2010)
H37Rv maltose-1-phosphate stress stimulon rep 1Null mutant vs complemented null mutant1.019.650.60Kalscheuer R, et al. (2010)
CDC1551 nadABC null nicotinamide starvation rep 3Nicotinamide-0.988.560.51Vilcheze C, et al. (2010)
M. bovis nadABC null nicotinamide starvation rep 2Nicotinamide-1.927.780.52Vilcheze C, et al. (2010)
M. bovis nadABC null nicotinamide starvation rep 3Nicotinamide-2.986.890.85Vilcheze C, et al. (2010)
CDC1551 nadABC null nicotinamide starvation rep 2Nicotinamide-0.209.350.14Vilcheze C, et al. (2010)
CDC1551 nadABC null nicotinamide starvation rep 1Nicotinamide-1.178.160.56Vilcheze C, et al. (2010)
M. bovis nadABC null nicotinamide starvation rep 1Nicotinamide-3.247.990.97Vilcheze C, et al. (2010)
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Folder International day for biodiversity 2013
The theme Water and Biodiversity was chosen to coincide with the United Nations designation of 2013 as the International Year of Water Cooperation.
Water and Biodiversity is the theme for International Day for Biological Diversity (IDB) in 2013. Designation of IDB 2013 on the theme of water provides Parties to the Convention on Biological Diversity (CBD) and the public at large the opportunity to raise awareness about this vital issue, and to increase positive action.
DOC Press release - celebration of 22 May 2013 in Belgium (French) Download
DOC Press release - celebration of 22 May 2013 in Belgium (Dutch) Download
PDF Flyer of activities organised by the Royal Belgian Institute of Natural Sciences for the IDB 2013 Download
URL International day for biodiversity 2013 at the CBD Secretariat
URL Booklet provided by the CBD Secretariat on Natural Solutions for water security
logo CBD logo NFP Belgium logo RBINS
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People & Places
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BEST SANCTUARY FROM THE FAST TRACK Minneapolis 1998 -
Established more than 90 years ago by a schoolteacher and naturalist who foresaw the urban sprawl that has made many Minnesota birds and wildflowers rare sights, these 14 acres are a sliver of lovingly tended paradise. All the environments we've paved over are represented: woodland, wetland, prairie, oak savannah. The garden is a living museum of native plants and wildflowers, and one of the few places to see endangered species such as the Mountain Dwarf Trout Lily. Raptors, owls, and songbirds are often spotted along the quiet walking paths where signs mark plants for your edification. Hours: 7:30 a.m. to dusk.
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Ecosystem diversity
From MarineBiotech Infopages
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This defintion is one of four of the components that are described as making up marine biodiversity.
[2]Ecosystem diversity is a term that incorporates both habitat and community diversity. A habitat is the environment in which an organism or species lives and includes the physical characteristics (e.g. climate or the availability of suitable food and shelter) that make it especially well suited to meet the life cycle needs of that species. A community consists of the assemblage of populations of plants and animals that occupy an area and their interactions with each other and their environment. An ecosystem is a unique combination of plant, animal and microorganism communities and their non-living physical characteristics interacting as a functional unit. Inherent in ecosystem diversity are thus both biotic (living) and abiotic (non-living) components, which makes it different from both genetic and species diversity.
References
The main author of this article is Sohier, Charlotte
Please note that others may also have edited the contents of this article.
Citation: Sohier, Charlotte (2019): Ecosystem diversity. Available from http://www.coastalwiki.org/wiki/Ecosystem_diversity [accessed on 3-06-2020]
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World Database of Nematodes
Linked to the Marine Biology Section, UGent
Nemys source details
Taheri, M.; Braeckman, U.; Vincx, M.; Vanaverbeke, J. (2014). Effect of short-term hypoxia on marine nematode community structure and vertical distribution pattern in three different sediment types of the North Sea. Marine Environmental Research. 99: 149-159.
196178
10.1016/j.marenvres.2014.04.010 [view]
Taheri, M.; Braeckman, U.; Vincx, M.; Vanaverbeke, J.
2014
Effect of short-term hypoxia on marine nematode community structure and vertical distribution pattern in three different sediment types of the North Sea
Marine Environmental Research
99: 149-159
Publication
Available for editors PDF available [request]
North Sea (and Channel)
Ecology
RIS (EndNote, Reference Manager, ProCite, RefWorks)
BibTex (BibDesk, LaTeX)
Date
action
by
2015-02-25 08:10:33Z
created
This service is powered by LifeWatch Belgium
Learn more»
Web interface and database structure initially created by Tim Deprez; now hosted and maintained by VLIZ
Page generated 2019-11-15 · contact: Tânia Nara Bezerra or [email protected]
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WorldCat Identities
Nurse, Paul 1949-
Overview
Works: 57 works in 82 publications in 2 languages and 855 library holdings
Genres: History Conference proceedings Biography
Roles: Author, Narrator, Author of introduction, Interviewee
Classifications: QR73.7, 576.13
Publication Timeline
.
Most widely held works about Paul Nurse
Most widely held works by Paul Nurse
The Microbial cell cycle by P Nurse( Book )
8 editions published in 1984 in English and held by 290 WorldCat member libraries worldwide
Genius of Britain the scientists who changed the world ( Visual )
2 editions published between 2010 and 2011 in English and held by 137 WorldCat member libraries worldwide
Britain's great inventors and scientists have taken mankind to places and into worlds that we only dreamed possible. This essential book presents a compelling overview of those achievements and the fascinating stories of the people who did it
The great ideas of biology : the Romanes lecture for 2003 delivered before the University of Oxford on 30 October 2003 by Paul Nurse( Book )
5 editions published between 2003 and 2004 in English and held by 81 WorldCat member libraries worldwide
Creation by Jill Marshall( Visual )
1 edition published in 2002 in English and held by 63 WorldCat member libraries worldwide
Presents the latest advances in cloning, stem cell development, and genetic science. Includes an overview of the cloning research of José Cibelli, and comments by noted scientists Lee Silver and Paul Nurse on how these developments have changed human life
Science under attack ( Visual )
5 editions published in 2011 in English and held by 44 WorldCat member libraries worldwide
The consensus of the world's science academies, reached after a series of annual conferences, is that climate change is real, and that it's caused by human activity. Why, then, do so many people doubt these findings? In this program Nobel Prize winner Paul Nurse seeks to understand what may be the greatest amount of suspicion of the scientific community since the Dark Ages. Nurse goes head to head with climate change skeptic Fred Singer, and takes on the misinterpreted "Climategate" emails that ignited a firestorm of denier outrage. Nurse also talks to a man with HIV who does not believe the virus causes AIDS, and examines wariness of genetically modified foods. The role of the media in politicizing research and evidence is also considered
Eukaryotic chromosome replication : proceedings of a Royal Society discussion meeting held on 10 and 11 December 1986 by Royal Society discussion meeting( Book )
3 editions published in 1987 in English and held by 40 WorldCat member libraries worldwide
Predictor ( Visual )
1 edition published in 2003 in English and held by 24 WorldCat member libraries worldwide
One of a four-part series presenting research and breakthroughs in the field of human genetics. This segment looks at the extent to which genes determine human behavior and destiny. A woman discovers that a single letter change in the genome has been responsible for her family's generations-old "curse" of deformed hands. Dr. Hugh Montgomery of University College Hospital, London, screens the DNA of army recruits for the ACE or endurance gene which may affect their longevity as well as their basic training. Dr. Dean Hammer of the National Institutes of Health explains his search for a thrill-seeker gene, D4DR. Attorney Daniel Summer argues for leniency for his death-row client because his DNA predisposed him to a life of crime. Professor Lee Silver of Princeton University and Nobel Laureate Sir Paul Nurse also provide commentary
The great ideas of biology : the Romanes lecture for 2003 by Paul Nurse( Book )
3 editions published in 2004 in English and held by 18 WorldCat member libraries worldwide
Eukaryotic chromosome replication : a discussion by R. A Laskey( Book )
3 editions published between 1987 and 1989 in English and held by 15 WorldCat member libraries worldwide
Abstracts of papers presented at the 1993 meeting on yeast cell biology : August 17-August 22, 1993 ( Book )
1 edition published in 1993 in English and held by 15 WorldCat member libraries worldwide
Genius of Britain. the scientists who changed the world ( Visual )
1 edition published in 2011 in English and held by 14 WorldCat member libraries worldwide
Charismatic men of action and reclusive eccentrics. Eureka moments and serendipitous strokes of luck. Discoveries born of crisis and insatiable curiosity. The history of scientific progress in Britain offers an astonishing breadth of personalities and has had an awe-inspiring effect on civilization. Each episode brings an era of scientific thought to life, with modern-day geniuses examining the legacies of their heroes
Genius of Britain. the scientists who changed the world ( Visual )
1 edition published in 2011 in English and held by 13 WorldCat member libraries worldwide
Charismatic men of action and reclusive eccentrics. Eureka moments and serendipitous strokes of luck. Discoveries born of crisis and insatiable curiosity. The history of scientific progress in Britain offers an astonishing breadth of personalities and has had an awe-inspiring effect on civilization. Each episode brings an era of scientific thought to life, with modern-day geniuses examining the legacies of their heroes
Abstracts of papers presented at the 1987 meeting on yeast cell biology : August 11-August 16, 1987 ( Book )
2 editions published in 1987 in English and held by 13 WorldCat member libraries worldwide
How to build a human ( Visual )
3 editions published between 2002 and 2003 in English and held by 13 WorldCat member libraries worldwide
One of a four-part series presenting research and breakthroughs in the field of human genetics. In this segment, pioneering methods of human cloning give a paralyzed Texas doctor hope that he will walk again. Meanwhile in England, a couple prepares for the result of cloning the natural way: triplets. Shows the latest advances in stem cell development and genetic science. The efforts of Dr. José Cibelli, head of research at Advanced Cell Technology, which led to the first artificially cloned embroyo, are paralleled with genetic replication as it occurs naturally in the womb. Professor Lee Silver, molecular biologist at Princeton University, and Nobel Prize-winning cell biologist Sir Paul Nurse comment on how these innovations have changed human life
How to build a human ( Visual )
1 edition published in 2002 in English and held by 12 WorldCat member libraries worldwide
One of a four-part series presenting research and breakthroughs in the field of human genetics. This segment looks at the extent to which genes determine human behavior and destiny. A woman discovers that a single letter change in the genome has been responsible for her family's generations-old "curse" of deformed hands. Dr. Hugh Montgomery of University College Hospital, London, screens the DNA of army recruits for the ACE or endurance gene which may affect their longevity as well as their basic training. Dr. Dean Hammer of the National Institutes of Health explains his search for a thrill-seeker gene, D4DR. Attorney Daniel Summer argues for leniency for his death-row client because his DNA predisposed him to a life of crime. Professor Lee Silver of Princeton University and Nobel Laureate Sir Paul Nurse also provide commentary
Hevreka! : veliki izumitelji in njihove genialne domislice by Richard Platt( Book )
1 edition published in 2003 in Slovenian and held by 5 WorldCat member libraries worldwide
The great ideas of biology : the Harveian oration delivered before the Fellows of the Royal College of Physicians of London on Thursday 16 October 2003 by Paul Nurse( Book )
1 edition published in 2003 in English and held by 5 WorldCat member libraries worldwide
Charlie Rose ( Visual )
1 edition published in 2007 in English and held by 4 WorldCat member libraries worldwide
(Producer) Panel discusses the rise in obesity in the U.S., along with its accompanying health concerns, such as type 2 diabetes. A number of obesity experts voice their opinions on the best measures to prevent further weight increases and to treat the existing health concerns
Charlie Rose ( Visual )
1 edition published in 2007 in English and held by 4 WorldCat member libraries worldwide
(Producer) Discusses existing successes in the use of stem cells, such as bone marrow transplants, and the hopes for future applications of both adult and embryonic stem cells, both as a way to model and study disease and a possible treatment for a variety of conditions, such as heart and blood disease, diabetes, Parkinson's, Lou Gehrig's disease, Alzheimer's, spinal cord injuries, and cancer. The uses of federal and private funding for the research are also considered
KNAW Heineken lectures : 1996 ( Book )
1 edition published in 1997 in English and held by 3 WorldCat member libraries worldwide
moreShow More Titles
fewerShow Fewer Titles
Audience Level
0
Audience Level
1
Kids General Special
Audience level: 0.61 (from 0.00 for Sir Paul N ... to 1.00 for Charlie Ro ...)
Alternative Names
Nurse, P. M.
Nurse, Paul M.
Nurse, Paul Maxime.
Languages
English (45)
Slovenian (1)
Covers
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57
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cf5cd1df0ee2161e1684bdc019357275
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-8,945,299,369,401,574,000
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Overview
• Product name
Anti-CD69 antibody [FN50], prediluted (PerCP)
See all CD69 primary antibodies
• Description
Mouse monoclonal [FN50] to CD69, prediluted (PerCP)
• Host species
Mouse
• Conjugation
PerCP. Ex: 482nm, Em: 675nm
• Tested applications
Suitable for: Flow Cytmore details
• Species reactivity
Reacts with: Human, Cynomolgus monkey
• Immunogen
Anti-µ-stimulated Human B lymphocytes.
• Positive control
• Human whole blood
• General notes
The antibody is conjugated with Peridinin-chlorophyll-protein complex (PerCP) under optimum conditions.
Properties
Applications
Our Abpromise guarantee covers the use of ab135933 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Application Abreviews Notes
Flow Cyt Use 20µl for 106 cells.
(In 100 µl of whole blood).
ab118658 - Mouse monoclonal IgG1, is suitable for use as an isotype control with this antibody.
Target
• Function
Involved in lymphocyte proliferation and functions as a signal transmitting receptor in lymphocytes, natural killer (NK) cells, and platelets.
• Tissue specificity
Expressed on the surface of activated T-cells, B-cells, natural killer cells, neutrophils, eosinophils, epidermal Langerhans cells and platelets.
• Sequence similarities
Contains 1 C-type lectin domain.
• Developmental stage
Earliest inducible cell surface glycoprotein acquired during lymphoid activation.
• Post-translational
modifications
Constitutive Ser/Thr phosphorylation in both mature thymocytes and activated T-lymphocytes.
• Cellular localization
Membrane.
• Information by UniProt
• Database links
• Alternative names
• Activation inducer molecule (AIM/CD69) antibody
• Activation inducer molecule antibody
• AIM antibody
• BL-AC/P26 antibody
• BLAC/P26 antibody
• C-type lectin domain family 2 member C antibody
• CD69 antibody
• CD69 antigen (p60, early T-cell activation antigen) antibody
• CD69 antigen antibody
• CD69 molecule antibody
• CD69_HUMAN antibody
• CLEC2C antibody
• EA1 antibody
• Early activation antigen CD69 antibody
• Early lymphocyte activation antigen antibody
• Early T cell activation antigen p60 antibody
• Early T-cell activation antigen p60 antibody
• GP32/28 antibody
• Leu23 antibody
• Leukocyte surface antigen Leu-23 antibody
• MLR-3 antibody
• MLR3 antibody
• VEA antibody
• Very Early Activation Antigen antibody
see all
Images
• Flow cytometry analysis of Human whole blood from buffy coat, staining CD69 with ab135933. Cells were stimulated with anti-CD3/CD28 overnight before isolation by a Ficoll density gradient. The sample was incubated with the primary antibody (1/100 in 1% BSA in PBS) for 1 hour at 4°C.
Gating Strategy: Live lymphocytes
See Abreview
• Flow cytometry analysis of Cynomolgus monkey whole blood after red blod cell lysis, staining CD69 with ab135933. Cells were stimulated with PMA overnight and fixed with paraformaldehyde. The sample was incubated with the primary antibody (1/100 in 1% BSA in PBS) for 1 hour at 4°C.
Gating Strategy: Live lymphocytes
See Abreview
References
This product has been referenced in:
• Ramos-Martínez E et al. Reduction of respiratory infections in asthma patients supplemented with vitamin D is related to increased serum IL-10 and IFN? levels and cathelicidin expression. Cytokine 108:239-246 (2018). Flow Cyt ; Human . Read more (PubMed: 29402723) »
See 1 Publication for this product
Customer reviews and Q&As
Filter by Application
Filter by Species
Filter by Ratings
1-4 of 4 Abreviews
Application
Flow Cytometry
Sample
Rat Cell (Splenocytes)
Specification
Splenocytes
Preparation
Cell harvesting/tissue preparation method: isolated from spleen of immunized rat
Sample buffer: PBS/BSA 1%
Permeabilization
No
Gating Strategy
alive lymphocytes
Abcam user community
Verified customer
Submitted Jan 09 2013
Application
Flow Cytometry
Sample
Mouse Cell (Splenocytes)
Specification
Splenocytes
Preparation
Cell harvesting/tissue preparation method: isolated from spleen cells and stimulated with anti-CD3/CD28
Sample buffer: PBS/BSA 1%
Permeabilization
No
Gating Strategy
alive lymphocytes
Abcam user community
Verified customer
Submitted Jan 03 2013
Application
Flow Cytometry
Sample
Human Cell (from buffy coat)
Specification
from buffy coat
Preparation
Cell harvesting/tissue preparation method: after ficoll purification
Sample buffer: PBS/BSA 1%
Permeabilization
No
Gating Strategy
alive lymphocytes
Abcam user community
Verified customer
Submitted Jan 02 2013
Application
Flow Cytometry
Sample
Cynomolgus Monkey Cell (from whole blood)
Specification
from whole blood
Preparation
Cell harvesting/tissue preparation method: after red blood cell lysis
Sample buffer: PBS/BSA 1%
Fixation
Paraformaldehyde
Permeabilization
No
Gating Strategy
alive lymphocytes
Abcam user community
Verified customer
Submitted Jan 02 2013
Please note: All products are "FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC PROCEDURES"
For licensing inquiries, please contact [email protected]
Sign up
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57
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cf5cd1df0ee2161e1684bdc019357275
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-7,736,184,630,415,816,000
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Principles of RNA and protein quality control at the eukaryotic ribosome
Principles of RNA and protein quality control at the eukaryotic ribosome
Not available
Not available
Hassemer, Timm
2017
English
Universitätsbibliothek der Ludwig-Maximilians-Universität München
Hassemer, Timm (2017): Principles of RNA and protein quality control at the eukaryotic ribosome. Dissertation, LMU München: Faculty of Chemistry and Pharmacy
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Alfa Aesar™ Tris-Glycine Large Precast Gel, 2D, 10-20%, 20x20cm, 22.3x20cm (back), low fluor., 1 well, for Bio-Rad™ systems
Specifications
Product Type Tris-Glycine Large Precast Gel
View More Specs
Products ${productFamilyLength}
Catalog Number Mfr. No. Quantity Price Quantity
Catalog Number Mfr. No. Quantity Price Quantity
AAJ67620KZ Alfa Aesar™
J67620KZ
6 Each N/A N/A
Please call Customer Service at 1-800-234-7437 or send an email to [email protected] for assistance.
AAJ67620SA Alfa Aesar™
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Specifications Description & Specifications
Specifications
Tris-Glycine Large Precast Gel
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Home | Contact
PROSITE documentation PDOC00970 [for PROSITE entry PS01262]
Eukaryotic initiation factor 1A signature
Description
Eukaryotic translation initiation factor 1A (eIF-1A) [1] (formerly known as eiF-4C) is a protein that seems to be required for maximal rate of protein biosynthesis. It enhances ribosome dissociation into subunits and stabilizes the binding of the initiator Met-tRNA to 40S ribosomal subunits.
eIF-1A is a hydrophilic protein of about 15 to 17 Kd. Archaebacteria also seem to possess a eIF-1A homolog.
As a signature pattern, we selected a conserved region in the central section of these proteins.
Last update:
December 2004 / Pattern and text revised.
Technical section
PROSITE method (with tools and information) covered by this documentation:
IF1A, PS01262; Eukaryotic initiation factor 1A signature (PATTERN)
Reference
1AuthorsWei C.-L. Kainuma M. Hershey J.W.B.
TitleCharacterization of yeast translation initiation factor 1A and cloning of its essential gene.
SourceJ. Biol. Chem. 270:22788-22794(1995).
PubMed ID7559407
PROSITE is copyright. It is produced by the SIB Swiss Institute Bioinformatics. There are no restrictions on its use by non-profit institutions as long as its content is in no way modified. Usage by and for commercial entities requires a license agreement. For information about the licensing scheme send an email to
Prosite License or see: prosite_license.html.
Miscellaneous
View entry in original PROSITE document format
View entry in raw text format (no links)
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User:Tamarabrenner
From OpenWetWare
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I work as the Assistant Director of Life Sciences Education, helping with various programs for undergraduate education in the life sciences.
You can find me in the BioLabs, Room 1087. email: tamara_brenner AT harvard.edu
I did my doctoral work in Christine Guthrie's lab at the University of California, San Francisco, where I studied pre-mRNA splicing in budding yeast.
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1887
Abstract
Suppression of the CpG dinucleotide is widespread in RNA viruses infecting vertebrates and plants, and in the genomes of retroviruses and small mammalian DNA viruses. The functional basis for CpG suppression in the latter was investigated through the construction of mutants of the parvovirus, minute virus of mice (MVM) with increased CpG or TpA dinucleotides in the VP gene. CpG-high mutants displayed extraordinary attenuation in A9 cells compared to wild-type MVM (>six logs), while TpA elevation showed no replication effect. Attenuation was independent of Toll-like receptor 9 and STING-mediated DNA recognition pathways and unrelated to effects on translation efficiency. While translation from codon-optimized VP RNA was enhanced in a cell-free assay, MVM containing this sequence was highly attenuated. Further mutational analysis indicated that this arose through its increased numbers of CpG dinucleotides (7→70) and separately from its increased G+C content (42.3→57.4 %), which independently attenuated replication. CpG-high viruses showed impaired NS mRNA expression by qPCR and reduced NS and particularly VP protein expression detected by immunofluorescence and replication in A549 cells, effects reversed in zinc antiviral protein (ZAP) knockout cells, even though nuclear relocalization of VP remained defective. The demonstrated functional basis for CpG suppression in MVM and potentially other small DNA viruses and the observed intolerance of CpGs in coding sequences, even after codon optimization, has implications for the use of small DNA virus vectors in gene therapy and immunization.
Funding
This study was supported by the:
• Peter Simmonds , Wellcome Trust , (Award WT103767MA)
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57
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cf5cd1df0ee2161e1684bdc019357275
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-1,655,603,697,673,013,000
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Browse by Person
Up a level
Export as [feed] Atom [feed] RSS 1.0 [feed] RSS 2.0
Group by: Item Type | No Grouping
Jump to: Article
Number of items: 2.
Article
Ward, TA orcid.org/0000-0003-0937-4554, McHugh, PJ and Durant, ST (2017) Small molecule inhibitors uncover synthetic genetic interactions of human flap endonuclease 1 (FEN1) with DNA damage response genes. PLoS ONE, 12 (6). e0179278. ISSN 1932-6203
Exell, JC, Thompson, MJ, Finger, LD et al. (11 more authors) (2016) Cellularly active N-hydroxyurea FEN1 inhibitors block substrate entry to the active site. Nature Chemical Biology, 12 (10). pp. 815-821. ISSN 1552-4450
This list was generated on Sun Oct 13 16:39:23 2019 BST.
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57
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cf5cd1df0ee2161e1684bdc019357275
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-5,526,638,580,043,573,000
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EST details — SGN-E392590
Search information
Request: 392590Match: SGN-E392590
Request From: SGN database generated linkMatch Type: EST sequence internal identifier
Clone information
SGN ID: SGN-C180725Clone name: TUS-35-B19
cartOrder Clone
Library Name: TUSOrganism: Solanum lycopersicum (formerly Lycopersicon esculentum)
Tissue: Rearrayed collection of L. esculentum cDNA clones
Development Stage:
Microarray: SGN-C180725 is on microarray TOM1 spot ID 1-1-6.2.17.18 [Order] [Tomato Microarray Database]
There is no map position defined on SGN for this EST or others in the same unigene.
Additional sequencing
Clone: SGN-C68999 [cLEN-8-J23] Trace: SGN-T88746 EST: SGN-E274050 Direction: 5' Facility: TIGR
Clone: SGN-C180725 [TUS-35-B19] Trace: SGN-T193917 EST: SGN-E392591 Direction: 5' Facility: INRA
[Show information hierarchy]
Sequence
Sequence Id: SGN-E392590Length: 344 bp (866 bp untrimmed)
Status: Current VersionDirection: 3' [See links to 5' reads above]
>SGN-E392590 [] (trimmed) GACAGACAAGGAAGTAAATACAATGACACCAGCTTACTAGTAAATAAAATAACATTTCATATTTTTAGCTTACTGATTTATTTCAGTCCACTAAA
AATAAATAAAAATACAATTTCATGTAATACTGGGCTGCTTAATGGAGTTTGAACTCATTCACCATCTCCAACATGACTTACATCTCGATCGGGGC
TATGAAACAAACAATCTGGATAAACAACAAGTCTTTGTTCTAATCAGTATGGCAAAGATTCCATAACAAGGCAGATGGAAAATACCAACAGCAAA
GTACCAAAGGGGAACATATTGAGATGACAAGTCCAAAAAGGGATACCGCCACCTCAACC
[BLAST] [AA Translate]
Unigenes
Current Unigene builds
[SGN-E392590] SGN-U585544 Tomato 200607 Build 2 11 ESTs assembled
Follow SGN-U# link for detailed information and annotations
Chromatogram
SGN-ID: SGN-T193916 [Download][View] Facility Assigned ID: FA0AAD23CA10FM1
Submitter: Koni Sequencing Facility: INRA
Funding Organization: Funding for 5' and 3' resequencing of TOM1 microarray clones was provided by INRA. Sequencing was performed by Genoscope, Evry cedex, France. \ \ \
Quality processing
Processed By: SGN Basecalling Software: phred
Vector Signature: 3' sequence read, incomplete (flanking vector not found)
Passed all screens and filters
Sequence Entropy: 0.910 Expected Error Rate: 0.0029 Quality Trim Threshold: 14.5
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cf5cd1df0ee2161e1684bdc019357275
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6,879,960,750,196,224,000
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Biotechnology of Aquatic Animals
Biotechnology of Aquatic Animals
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57
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cf5cd1df0ee2161e1684bdc019357275
|
-6,401,584,486,939,137,000
|
Author
Khue Nguyen
Publication Date
2008
Document Type
Honors Thesis
Department
Biological Sciences
Abstract
Stress activates a series of metabolic changes in skeletal muscle which include the expression of various heat shock proteins and the activation of common intracellular signaling cascades such as the MAPK cascades. The role of the MAPK cascades in mitigating damage from stressors such as exercise and heat shock is not well understood. Our lab has previously shown that the MAPK cascades are regulated differentially by gender in mice that endured a single bout of eccentrically-biased, non-damaging downhill running (Cwaline et al., 2005). Because exercise induces elevated body temperatures, the current study aimed to look at changes in activation of the MAPKs in vitro, using mouse C2C12 skeletal muscle cells, during the course of normal development and after heat shock (2 hours at 42°C) at the myoblast, early myotube, and the late myotube stages of development. The results of this study suggest that during myogenesis in vitro, differentiation or growth are concurrent with the differential activation of ERK1/2 and JNK1/2. Heat shock also seems to have differential effects during myogensis. In myoblasts, heat shock either inhibits cell division or decreases cell viability and increases ERK1/2,p38, and JNK1/2 activation. In early myotubes, heat shock increases ERK1/2 and p38 activation. And in late myotubes, heat shock activates JNK1/2 while ERK1/2 and p38 activation is inhibited. In addition, ERK1/2 may have a protective role in helping cells cope with heat stress.
Language
English
Comments
iv, 110 leaves : col. ill. Thesis (Honors)--Smith College, Northampton, Mass., 2008. Includes bibliographical references (leaves 101-110)
Share
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57
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cf5cd1df0ee2161e1684bdc019357275
|
1,290,647,324,174,148,400
|
About
Kay About the author: My name is Kay. I am a rather unremarkable physical chemist-turned biochemist-turned bioinformatician, who is currently using computers to answer the most fundamental questions in life science: where does all stuff come from, what does it all mean, and how can I possibly get a high-impact journal to accept one of my manuscripts.
Is this blog anonymous? Not really. It is true that you won’t find my full name written anywhere. The reason for this is not that I want to stay in the dark – if you want to known my name, just write an e-mail to suicyte at gmx. net. The reason for not printing my name here is that I don’t want to see Google (and the rest of crowd) having automatic links between my name (and employer) and this blog. I am not totally sure why I don’t like the idea, but it is connected to the fact that getting indexed is kind of irreversible – once you’re in, you can’t get out again.
About this blog: This blog deals with matters arising in the molecular biosciences, particular in those areas I find exciting (apoptosis, regulated proteolysis, protein functional prediction, evolution, etc.)
About the title image: This is a snapshot I have taken 2003 somewhere in Tuscany. I think it was close to Monte Oliveto.
Legal stuff: Everything I write here is my own opinion, not that of my employer. Unless stated otherwise, you may use all material found here (text and images) under a CC attribution license. Obvious exceptions include material authored by others – this fact will be indicated.
Some more information on the purpose of this blog can be gathered from, my first post ever.
Responses
1. Hi Kay,
I found your thoughts on scotin interesting. I work with a protein called WWOX that I found to interact with scotin via the WWOX WW domains. I am interested in your “scotin-like family of receptors” and wonder if you would share your analysis with me?
2. Dear Kay,
It’s not a response really – just a quick question…
do you think that we ought to call the ubiquitinated proteome the “ubiquitinome” or the “ubiquitome”?
I did a quick Pubmed search, don’t know whether something was wrong with it, but I only found one vote for each.
Best wishes,
Paula Row.
3. Dear Paula,
according to many, the world already has enough ‘omes’ and ‘omics’ words. Personally, I don’t care that much. Both words have been used before, but only rarely so.
Just don’t call the set of all proteases the ‘proteasome’ 🙂
Best Wishes, Kay
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TRNAR-UCU Gene
RNA gene GIFtS: 6
GCID: GC00U922339
Transfer RNA Arginine (Anticodon UCU)
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(According to 1HGNC, 2Entrez Gene,
3UniProtKB/Swiss-Prot, 4UniProtKB/TrEMBL, 5OMIM, 6GeneLoc, 7Ensembl, 8DME, 9miRBase, 10fRNAdb, 12H-InvDB, 13NCBI, 14NONCODE, and/or 15RNAdb)
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Subcategory (RNA class): tRNA
Quality score for this RNA gene is 0
Aliases
Transfer RNA Arginine (Anticodon UCU)2
External Ids: Entrez Gene: 1001265262
Export aliases for TRNAR-UCU gene to outside databases
Previous GC identifiers: GC09U901023 GC09M130142 GC09M131102
(According to Entrez Gene, GeneCards, Tocris Bioscience, Wikipedia's Gene Wiki, PharmGKB,
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Entrez Gene summary for TRNAR-UCU Gene:
This record serves to anchor the annotations of this class of tRNAs at multiple locations on the human genome. The
placements are predicted using tRNAscan-SE (Lowe, T.M. and Eddy, S.R. 1997. Nucleic Acids Res. 25:955-964, PubMed
9023104).
GeneCards Summary for TRNAR-UCU Gene:
TRNAR-UCU is an RNA gene, and is affiliated with the tRNA class.
(According to GeneLoc and/or HGNC, and/or
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(SuperPaths according to PathCards, Pathways according to R&D Systems, Cell Signaling Technology, KEGG, PharmGKB, BioSystems, Sino Biological, Reactome, Tocris Bioscience, GeneGo (Thomson Reuters), QIAGEN, and/or UniProtKB, Sets of similar genes according to GenesLikeMe, Interaction Networks according to QIAGEN, and/or STRING, Interactions according to 1UniProtKB, 2MINT, 3I2D, and/or 4STRING, with links to IntAct and Ensembl, Ontologies according to Gene Ontology Consortium 01 Apr 2014 via Entrez Gene, Sets of similar genes according to GenesLikeMe)
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(Secondary structures according to fRNAdb,
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DOTS (version 10), and/or AceView, transcript ids from Ensembl with links to UCSC,
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(RNA expression data according to H-InvDB, NONCODE, miRBase, and RNAdb, Expression images according to data from BioGPS, Illumina Human BodyMap, and CGAP SAGE, Sets of similar genes according to GenesLikeMe, in vivo and in vitro expression data from LifeMap Discovery™, Protein expression images according to data from SPIRE 1MOPED, 2PaxDb, and 3MaxQB, plus additional links to SOURCE, and/or BioGPS, and/or UniProtKB,
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Expression evidence for TRNAR-UCU:none
See probesets specificity/sensitivity at GeneAnnot
CGAP TAG: --
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(Orthologs according to 1,2HomoloGene (2older version, for species not in 1newer version), 3euGenes, 4SGD , 5MGI Mar 06 2013, with possible further links to Flybase and/or WormBase, and/or 6Ensembl pan taxonomic compara , Gene Trees according to Ensembl and TreeFam)
About This Section
--
(Paralogs according to 1HomoloGene,
2Ensembl, and 3SIMAP, Pseudogenes according to 4Pseudogene.org Build 68,Sets of similar genes according to GenesLikeMe)
About This Section
--
(SNPs/Variants according to the 1NCBI SNP Database, 2Ensembl, 3PupaSUITE, and 4UniProtKB, Linkage Disequilibrium by HapMap, Structural Variations(CNVs/InDels/Inversions) from the Database of Genomic Variants, Mutations from the Human Gene Mutation Database (HGMD), the Human Cytochrome P450 Allele Nomenclature Database, and the Locus Specific Mutation Databases (LSDB), Blood group antigen gene mutations by BGMUT, Resequencing Primers, Cancer Mutation PCR Arrays and Assays, and Copy Number PCR Arrays from QIAGEN)
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Site Specific Mutation Identification with PCR Assays
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(in which this Gene is Involved, According to MalaCards, OMIM, UniProtKB, the University of Copenhagen DISEASES database, Genatlas, GeneTests, GAD, HuGE Navigator, and/or TGDB, Sets of similar genes according to GenesLikeMe)
About This Section
--
(in PubMed. Associations of this gene to articles via 1Entrez Gene, 2UniProtKB/Swiss-Prot, 3HGNC, 4GAD, 5PharmGKB, 6HMDB, 7DrugBank, 8UniProtKB/TrEMBL, 9 Novoseek, and/or 10fRNAdb)
About This Section
--
(in PubMed, OMIM, and NCBI Bookshelf)
About This Section
ANDOR
Aliases
Free Text
Query String
PubMed
OMIM
NCBI Bookshelf
(Note: In FireFox, select the above section and copy using Ctrl-C)
(According to Entrez Gene, HGNC, AceView, euGenes, Ensembl, miRBase, ECgene, Kegg, and/or H-InvDB)
About This Section
Entrez Gene: 100126526 euGenes: HUgn100126526
(According to HUGE)
About This Section
--
(According to PharmGKB, ATLAS, HORDE, IMGT, LEIDEN, UniProtKB/Swiss-Prot, UniProtKB/TrEMBL, and/or others, e.g. Wikipedia and GeneReviews, via UniProtKB/Swiss-Prot)
About This Section
--
(Patent information from GeneIP,
Licensable technologies from WIS Yeda, Salk, Tufts,
IP news from LifeMap Sciences, Inc.)
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Patent Information for TRNAR-UCU gene:
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GeneCards and IP:
Japan Patent Office Licenses GeneCards European Patent Office Licenses GeneCards Improving the IP Search
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Hot genes Disease genes TRNAR-UCU gene at Home site.
Version: 3.12.384 19 Apr 2015
hostname: 356977-web1.xennexinc.com index build: 128 solr: 1.4
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Media, PA News: Everybody's Home Page
Radical Mycology To Present Workshops About The Uses And Benefits Of Mushrooms
Sep 07
RELEASE – On September 7, Transition Town Media will be hosting two mushroom related workshops: “Mushroom ID for a Healthy Planet”and “Putting the FUN in Fungi.”
These workshops will be taught by members of Radical Mycology, an international volunteer organization that educates the public about the uses and benefits of fungi.
What: Mycology Workshops: “Mushroom ID for a Healthy Planet” and “Putting the FUN in Fungi”
When: Sunday, September 7 from 2pm – 5:30pm
Where: Providence Friends Meeting (105 N Providence Rd, Media, PA 19063)
Who: Open to the public; “Putting the FUN in Fungi” is designed for children ages 7 and older
Cost: donation is encouraged ($10 suggested)
Workshop 1: “Mushroom ID for a Healthy Planet”
• This workshop will introduce participants to the core skills for mushroom identification and how to use this knowledge to increase personal and community resilience.
• The workshop will begin with a lecture component and end with a mushroom foray in a nearby park where participants will get to utilize the knowledge that they’ve learned.
• To help make the event accessible to all members of the larger Media community, workshop will be donation-based.
Workshop 2: “Putting the FUN in Fungi”
• This special workshop is designed for children ages 7 and up.
• Through games and activities, children will learn how to answer questions like, “What do mushrooms eat,” “What does it mean to be a decomposer,” and “How can we work with mushrooms to clean water and soil?”
• After the games and activities, children will be able to go on the mushroom foray with the adults.
2014-09-07 RadicalMycology copy
Radical Mycology North American Tour
The collaborative event between Transition Town Media and the Radical Mycology Collective is part of Radical Mycology’s 3-month tour across North America. Radical Mycology, a volunteer-based organization and grassroots movement, is dedicated to educating the world on the positive benefits of the fungal kingdom for personal, societal, and ecological health.
The 2014 tour will promote their upcoming book, Radical Mycology and the third annual Radical Mycology Convergence, an organizational conference. The tour will teach the skills and theories behind the Radical Mycology movement.
“Our goal is to build a grassroots movement and network of people that work with fungi as allies in their efforts for a more sustainable and ecologically just future,” says Radical Mycology co-founder Peter McCoy.
Radical Mycology co-founder Maya Elson notes that, “Our past educational events, such as the Radical Mycology Convergences, have been very well attended and supported. People are ready for powerful solutions for personal, societal and ecological health that they can practice in their backyards, with or without the support of big institutions. We’re very excited to be taking the next step towards making these solutions a reality all over the US and the world.”
As part of the 2014 Radical Mycology tour, the Media workshops will further empower people with the skills and information they need to work with the fungi to create positive and lasting change.
About Transition Town Media
Transition Town Media is a group of residents aiming to find community-based (vs. government or corporate driven) solutions to the world’s most pressing problems – to build community resilience in response to climate change, peak oil, and economic instability.
To learn more visit www.transitiontownmedia.org.
About Radical Mycology
Radical Mycology is a movement and social philosophy based on the belief that the life cycles of fungi and their interactions in nature serve as powerful learning tools for how humans can best relate to each other and steward the world they live in. The Radical Mycology Collective organizes educational events and disseminates free literature and other media on the many uses of fungi for personal, societal, and ecological health.
To learn more visit www.radicalmycology.com, or call us at 360.561.5612.
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Shuguang Zhang
MIT
Shuguang Zhang pursues on membrane protein engineering at Center for Bits & Atoms, Massachusetts Institute of Technology. He received his B.S from Sichuan University, China and Ph.D. in biochemistry & molecular biology from University of California at Santa Barbara, USA. He was an American Cancer Society Postdoctoral Fellow and a Whitaker Foundation Investigator at MIT. He was a John Simon Guggenheim Fellow and the winner of the 2006 Wilhelm Exner Medal of Austria. He is a Fellow of American Institute of Medical and Biological Engineering and Fellow of US National Academy of Inventors. He is a Foreign Corresponding Member of Austrian Academy of Sciences. He has so far published over 160 scientific papers relevant to proteins and self-assembling peptides that have been cited over 21,000 times, with h-index 70. He has 18 issued patents and 20 pending patent applications. He is also a co-founder and board member of Molecular Frontiers Foundation that encourages young people to ask big and good questions in order to win Molecular Frontiers Inquiry Prize and to stimulate scientists to explore new knowledge frontiers.
http://cba.mit.edu/people/shuguang/
http://www.gf.org/fellows/all-fellows/shuguang-zhang/
Our Sponsors
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Scripps scientists describe protein used by bacteria and cancer cells to resist drugs
05/11/05
Scientists at The Scripps Research Institute have solved the structure of a protein called MsbA that is involved in resisting antibiotics and chemotherapy.
The structure of this membrane transporter protein is described in the current issue of the journal Science. Bacteria use these transporters to nullify antibiotics, and human cancer cells have similar membrane transporters on their surfaces that undermine the potency of chemotherapy drugs.
"We actually have very good drugs to fight cancer and to kill bacteria," says Assistant Professor Geoffrey Chang, Ph.D., of the Department of Molecular Biology. "[But] they can't always get in the cells to work."
The structures Chang and Research Associate Christopher Reyes solved using high-resolution x-ray crystallography reveal molecular details that could be useful for improving cancer therapy and fighting antibiotic-resistant bacteria.
Wonder Drugs and Super Bugs
At the dawn of the 20th century, bacterial infections accounted for several of the leading causes of death in the United States. Then came the antibiotic revolution. Antibiotic "wonder drugs" toppled tuberculosis (TB) and typhoid fever, controlled cholera and gonorrhea, reduced staphylococcal dysentery, and lowered the incidence of many other pandemic bacterial infections. These antibiotics are basically natural chemicals (or derivatives of natural chemicals) produced by other bacteria or fungi in the environment to kill off the competition. Scientists in the last century have discovered a number of these natural "antibiotic" products that have been used as the basis for treating bacterial infections.
By the middle of the century, the threat posed by many types of bacteria seemed to be waning. Bacterial infections that once topped the list as leading causes of death in the United States were no longer among the top ten. The average life expectancy in the United States soared from 47.3 years in 1900 to almost 80 years today, and antibiotics are partly to thank for this.
But in the last few decades, mutant strains of several types of bacteria with the ability to resist antibiotics have emerged, including those that cause TB, pneumonia, cholera, typhoid, salmonella, and staphylococcal dysentery. The bacteria that were once contained by drugs are now outstripping the ability of drugs to contain them, and as a result, says Chang, "What's happening today is that a lot of these diseases are coming back."
These diseases are coming back resistant to the antibiotics that have been used to treat them, and people infected with these resistant strains must be treated with alternative antibiotics.
Now some super bugs -- multiple drug-resistant bacteria -- are emerging as an even greater threat. Multiple drug-resistant TB is no longer susceptible to broad categories of antibiotics, such as rifampicin, isoniazid, and streptomycin. Some strains of the common hospital infection-causing bacteria Staphylococcus aureus are resistant to all antibiotics except vancomycin, which is a drug of last resort, and some strains of Streptococcus pneumoniae are even resistant to vancomycin. Certain strains of Shigella dysenteriae, the cause of epidemic dysentery, have even become resistant to all but a single drug -- the quinolone ciprofloxacin -- and may soon become completely untreatable. This is a major concern for public health because, according to the World Health Organization (WHO), large-scale epidemics of dysentery driven by this pathogen have been known to cause tens of thousands of deaths in Central America, South Asia, and central and southern Africa.
Treating multiple drug-resistant bacterial infections can be a hundred times more expensive than treating normal infections, and the WHO estimates the total cost of treating all hospital-borne antibiotic resistant bacterial infections is around $10 billion a year. Worse, with modern rapid transit and world travel, multiple drug-resistant bacteria could potentially spread beyond the isolated confines of a hospital and into the general population.
Resistance to Antibiotics and Chemotherapy
Bacteria resist antibiotic drugs in a number of ways. Classical antibiotics target essential machinery in bacterial cells, such as protein synthesis, nucleic acid replication, and cell wall synthesis. Bacteria acquire antibiotic resistance by doing things like encoding enzymes that degrade antibiotics or sequester antibiotics by binding to them, undergoing small point mutations in the molecular targets that lower a drug's affinity, and overproducing a drug's substrate in the cell.
However, another way that bacteria resist antibiotic drugs is by using membrane transporters -- large proteins that sit in the cell membrane and move other molecules in and out of the cell.
One of these transporters, the structure of which is the subject of Chang and Reyes' recent Science paper, is called MsbA. It belongs to the ATP Binding Cassette (ABC) transporter molecule family. ABC transporters are ubiquitous on the cell surfaces of almost all organisms. This is one of the largest superfamilies of transporter molecules. They transfer drugs, sugars, and peptides in organisms from bacteria to humans.
MsbA molecules play an essential role for bacteria because they help them build their cell walls by flipping molecules like "lipopolysaccharide" (LPS) and "lipid A" from the inner membrane to the outer membrane. These molecules are components of bacterial cell walls, and flipping them from the inner to the outer membrane of bacteria is necessary for bacterial cell growth.
The structure is important for a number of reasons. One is that solving the structure helped Chang and Reyes to propose a mechanism by which it works. The structure of MsbA is a dimer with two identical subunits. These subunits stretch across the cell membrane, coming together at the top (outside of the cell) and opening up like two outstretched arms on the inside of the cell.
Significantly, the structure is trapped in what they call a "post-hydrolysis" state -- basically caught in the act of flipping an LPS molecule. "You get to see the molecule half-cocked in action, just before the lipid is flipped outside," says Chang.
When the arms encounter LPS or lipid A, they close around the polar part of the amphipathic molecule, flip it over, and send it through the top to the other side of the membrane. This is most likely the same thing that happens when other drug pumps transport antibiotics out of the cell, and the structure of MsbA may help scientists design compounds to block its action. Coming up with a way to block this transporter would potentially make antibiotics more potent.
Any potential MsbA blocker might also have the dual effect of weakening the bacteria since many different bacteria use the same transporters for flipping LPS out of the cell and erecting a major barrier that blocks antibiotics from entering. Blocking MsbA could prevent this.
"It's an Achilles heel," says Chang. "Without being able to flip LPS outside, a bacteria cannot build its outer membrane."
The solved structure may also lead to ways of improving cancer chemotherapy. Humans have proteins called multidrug resistance transporters that are orthologous to MsbA (similar function and the same evolutionary ancestor). In human cells, these transporters play an essential protective role by removing harmful toxins, and transporter proteins are often found in the human gut, colon, and urinary tract. They are also found in mammary tissue, where they are involved in transporting lipids into milk ducts during lactation.
Unfortunately, this protective role can reduce the efficacy of certain cancer treatments, says Chang, since the drugs are perceived as toxins.
Having a high resolution structure such as the one Chang and Reyes solved could open the door for scientists to design a new class of drugs that patients would take in conjunction with antibiotic or chemotherapeutic agents to keep those drugs in the cells and increase their efficacy.
Finally, this structure is significant because it belongs to a class of proteins -- the membrane proteins -- that have been among the most difficult structures to study because they are notoriously hard to solve. Less than one half of one percent of the structures contained in the Brookhaven National Laboratory Protein Data Bank are of integral membrane proteins, despite the fact that over a third of all proteins in the body are in the membrane.
Source: Eurekalert & others
Last reviewed: By John M. Grohol, Psy.D. on 21 Feb 2009
Published on PsychCentral.com. All rights reserved.
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|
57
|
cf5cd1df0ee2161e1684bdc019357275
|
-3,373,189,566,893,023,700
|
PCR inhibition by U.V.
txpljfg at UABCVSR.cvsr.uab.edu txpljfg at UABCVSR.cvsr.uab.edu
Fri Feb 4 14:15:56 EST 1994
UV irradiation of DNA causes the formation of thymine dimers. I would
not recommend irradiation of the primers or the dNTPs. It seems likely
that you are damaging your oligo's
>
> In order to eliminate contamination in my
> PCR reactions, I have treated most reagents
> with uv (except the oligos) including the
> wax, and am now getting poor yields where
> I used to get better yields using the same
> temperatures/times. THE question:: does uv
> create some chemical products that inhibit
> pcr????
>
> Also I have heard that just storing oligo's for
> long periods in water at -20 C. will result in
> the oligo's being less efficient for PCR..
>
> ANY COMENTS?
> Rich
> rocket1 at bu.edu
>
>
==============================================================================
James F. George, Ph.D. "Back off man, I'm a scientist"
Department of Surgery --Bill Murray
University of Alabama at Birmingham
205-934-4261 voice
txpljfg at uabcvsr.cvsr.uab.edu
===============================================================================
More information about the Methods mailing list
|
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57
|
cf5cd1df0ee2161e1684bdc019357275
|
-7,603,422,736,223,242,000
|
About Help FAQ
Cdkn2atm4Rdp
Targeted Allele Detail
Nomenclature
Symbol: Cdkn2atm4Rdp
Name: cyclin-dependent kinase inhibitor 2A; targeted mutation 4, Ronald DePinho
MGI ID: MGI:2687203
Synonyms: Ink4a/ARFF2-3, Ink4a/Arflox, Ink4a/Arf Lox, Ink4a-p19ARF-
Gene: Cdkn2a Location: Chr4:89274471-89294653 bp, - strand Genetic Position: Chr4, 42.15 cM, cytoband C3-C6
Mutation
origin
Germline Transmission: Earliest citation of germline transmission: J:87196
Parent Cell Line: Not Specified (ES Cell)
Strain of Origin: Not Specified
Mutation
description
Allele Type: Targeted (Conditional ready, No functional change)
Mutation: Insertion
Mutation detailsExons 2 and 3 were left flanked by single loxP sites after an frt-flanked neo cassette was excised from intron 3 via FLP-mediated recombination. (J:87196)
Phenotypes
Loading...
View phenotypes for all genotypes (concatenated display).
Disease models
Loading...
Find Mice (IMSR)
Mouse strains and cell lines available from the International Mouse Strain Resource (IMSR)
Carrying this Mutation: Mouse Strains: 0 strains available Cell Lines: 0 lines available
Carrying any Cdkn2a Mutation: 26 strains or lines available
Notes
Phenotypic Similarity to Human Syndrome: Soft Tissue Sarcoma J:125101 in double Kras and Cdkn2a mutants.
References
Original: J:87196 Aguirre AJ, et al., Activated Kras and Ink4a/Arf deficiency cooperate to produce metastatic pancreatic ductal adenocarcinoma. Genes Dev. 2003 Dec 15;17(24):3112-26
All: 44 reference(s)
Contributing Projects:
Mouse Genome Database (MGD), Gene Expression Database (GXD), Mouse Tumor Biology (MTB), Gene Ontology (GO), MouseCyc
Citing These Resources
Funding Information
Warranty Disclaimer & Copyright Notice
Send questions and comments to User Support.
last database update
11/17/2015
MGI 6.01
The Jackson Laboratory
|
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|
cf5cd1df0ee2161e1684bdc019357275
|
5,401,231,540,969,381,000
|
We are seeking a motivated PhD student to join our research team working
on eco-evolutionary dynamics at the Max Planck Institute for Evolutionary
Biology in Plön, Germany.
We are looking for a highly motivated ecologist or evolutionary biologist
to join our group Community Dynamics at the Max Planck institute for
Evolutionary Biology (http://web.evolbio.mpg.de/comdyn) and the Kiel
Evolution Center (http://www.kec.uni-kiel.de). The ideal candidate is
fascinated by evolutionary and ecological questions, independent and
creative. She/he has a background in evolutionary biology, population
or community ecology. A MSc (or equivalent) in Biology is required.
There is a continuing interest to identify the interactions and feedback
dynamics between ecological and evolutionary changes at the same time
scale. This interest in eco-evolutionary dynamics is fuelled by the
need to understand how populations and communities could adapt to rapid
environmental change such as warming, invasion and pollution. Despite
this pressing need to understand eco-evolutionary dynamics, they are
not well understood in complex systems. In the project we aim to (1)
identify rapid adaptive changes in coevolving host-virus populations in
different food webs that differ in the types of species interactions and
complexity and to (2) comprehend how the dynamics of adaptive changes
alter the ecological dynamics and potential feedbacks. We will combine
controlled laboratory experiments, whole genome sequencing of populations
across different time points and modeling to characterize and compare
the adaptive dynamics and their consequences within the different food
webs. For more information on potential the project contact Lutz Becks
([email protected]).
The institute offers a stimulating international environment and
an excellent infrastructure with access to state‐of‐the-art
techniques. The town of Plön is in the middle of the Schleswig-Holstein
lake-district within a very attractive and touristic environment near the
Baltic Sea, close to the university towns of Lübeck and Kiel. Hamburg
and Lübeck are the closest airports.
The position is funded for three years. We ask applicants to send
a PDF file containing their CV and letter of motivation as well
as contact information of two references by e-mail to Lutz Becks
(mailto:[email protected]). We will begin reviewing applications
starting March 22th until the position is filled.
The Max Planck Society is an equal opportunity employer.
Dr. Lutz Becks
Community Dynamics Group
Max Planck Institute for Evolutionary Biology
August Thienemann Str. 2
24306 Plön
Germany
Telephone: +49 4522 763 230
Lutz Becks <[email protected]>
Share with your networks
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|
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57
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cf5cd1df0ee2161e1684bdc019357275
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-2,026,323,145,203,721,700
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• MUKESH CHOUDHARY
Articles written in Journal of Genetics
• Skim sequencing: an advanced NGS technology for crop improvement
PARDEEP KUMAR MUKESH CHOUDHARY B. S. JAT BHUPENDER KUMAR VISHAL SINGH VIRENDER KUMAR DEEPAK SINGLA SUJAY RAKSHIT
More Details Abstract Fulltext PDF
High-throughput genotyping has become more convenient and cost-effective due to recent advancements in next-generation sequencing (NGS) techniques. Numerous approaches exploring sequencing advances for genotyping have been developed over the past decade, which includes different variants of genotyping-by-sequencing (GBS), and restriction-site associated DNA sequencing (RAD-seq). Most of these methods are based on the reduced representation of the genome, which ultimately reduces the cost of sequencing by many folds. However, continuously lowering the cost of sequencing makes it more convenient to use whole genome-based approaches. In this regard, skim sequencing, where low coverage whole-genome sequencing is used for the identification of large numbers of polymorphic markers cost-effectively. In the present review, we have discussed recent technological advancements, applicability, and challenges of skim sequencing-based genotypic approaches for crop improvement programmes. Skim sequencing is being extensively used for genotyping indiverse plant species and has a wide range of applications, particularly in quantitative trait loci (QTL) mapping, genomewide association studies (GWAS), fine genetic map construction, and identification of recombination and gene conversion events in various breeding programmes. The cost-effectiveness, simplicity, and genomewide coverage will increase the application of skims sequencing-based genotyping. The article summarizes the protocol, uses, bioinformatics tools, its application, and future prospects of skim sequencing in crop improvement.
• Journal of Genetics | News
• Editorial Note on Continuous Article Publication
Posted on July 25, 2019
Click here for Editorial Note on CAP Mode
© 2022-2023 Indian Academy of Sciences, Bengaluru.
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cf5cd1df0ee2161e1684bdc019357275
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-762,437,079,223,003,000
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Interleukin-1 Receptor-Associated Kinase 1 (IRAK1) (C-Term), (AA 683-712) antibody
Details for Product No. ABIN392233
Request Want additional data for this product?
The Independent Validation Initiative strives to provide you with high quality data. Find out more
Antigen
Synonyms IRAK1, IRAK, pelle, AA408924, IRAK-1, IRAK1-S, Il1rak, Plpk, mPLK, RGD1563841
Epitope
C-Term, AA 683-712
(33), (33), (29), (24), (14), (8), (8), (8), (7), (6), (6), (4), (3), (3), (2), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1)
Reactivity
Human
(208), (101), (79), (36), (24), (24), (12)
Host
Rabbit
(198), (40), (1)
Clonality (Clone)
Polyclonal ()
Conjugate
Un-conjugated
(12), (10), (10), (5), (5), (5), (5), (5), (5), (5), (5), (5), (5), (5)
Application
Western Blotting (WB), Immunohistochemistry (IHC)
(159), (116), (57), (50), (41), (37), (23), (22), (19), (7), (3), (2), (1)
Pubmed 3 references available
Quantity 400 µL
Options
Shipping to United States (Change)
Availability Will be delivered in 2 to 3 Business Days
Request Want additional data for this product?
The Independent Validation Initiative strives to provide you with high quality data. Find out more
Catalog No. ABIN392233
291.50 $
Plus shipping costs $45.00
Order hotline:
• +1 404 474 4654
• +1 888 205 9894 (TF)
Immunogen This IRAK antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 683-712 AA from the C-terminal region of human IRAK.
Clone RB02337
Isotype Ig
Specificity This IRAK antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 683~712 amino acids from the C-terminal region of human IRAK1.
Purification This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.
Alternative Name IRAK
Background Protein kinases are enzymes that transfer a phosphate group from a phosphate donor, generally the g phosphate of ATP, onto an acceptor amino acid in a substrate protein. By this basic mechanism, protein kinases mediate most of the signal transduction in eukaryotic cells, regulating cellular metabolism, transcription, cell cycle progression, cytoskeletal rearrangement and cell movement, apoptosis, and differentiation. With more than 500 gene products, the protein kinase family is one of the largest families of proteins in eukaryotes. The family has been classified in 8 major groups based on sequence comparison of their tyrosine (PTK) or serine/threonine (STK) kinase catalytic domains. The tyrosine-like kinase (TLK) group consists of 40 tyrosine and serine-threonine kinases such as MLK (mixed-lineage kinase), LISK (LIMK/TESK), IRAK (interleukin-1 receptor-associated kinase), Raf, RIPK (receptor-interacting protein kinase), and STRK (activin and TGF-beta receptors) families.
Synonyms: interleukin-1 receptor-associated kinase 1
Molecular Weight 76536 DA
Gene ID 3654
UniProt P51617
Research Area Phospho-specific antibodies, Cell Signaling, Protein Modifications, Cell Cycle, Transcription Factors, Signaling, Metabolism, Cell Structure
Application Notes WB = 1:1000, IHC = 1:50-100
Restrictions For Research Use only
Format Liquid
Concentration 2 mg/mL
Buffer PBS with 0.09 % (W/V) sodium azide
Preservative Sodium azide
Precaution of Use This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage 4 °C/-20 °C
Storage Comment Maintain refrigerated at 2-8 °C for up to 6 months. For long term storage store at -20 °C in small aliquots to prevent freeze-thaw cycles.
Expiry Date 6 months
Supplier Images
anti-Interleukin-1 Receptor-Associated Kinase 1 (IRAK1) (C-Term), (AA 683-712) antibody Western blot analysis of anti-IRAK1 Pab (ABIN392233) in Jurkat cell lysate. IRAK1 (Arrow) was detected using purified polyclonal antibody. Secondary HRP-anti-rabbit was used for signal visualization with chemiluminescence.
anti-Interleukin-1 Receptor-Associated Kinase 1 (IRAK1) (C-Term), (AA 683-712) antibody (2) Western blot analysis of IRAK1 (arrow) using rabbit polyclonal IRAK Antibody (C-term) (ABIN392233). 293 cell lysates (2 µg/lane) either nontransfected (Lane 1) or transiently transfected with the IRAK1 gene (Lane 2) (Origene Technologies).
anti-Interleukin-1 Receptor-Associated Kinase 1 (IRAK1) (C-Term), (AA 683-712) antibody (3) Formalin-fixed and paraffin-embedded human cancer tissue reacted with the primary antibody, which was peroxidase-conjugated to the secondary antibody, followed by AEC staining. BC = breast carcinoma. HC = hepatocarcinoma
Background publications Cao, Henzel, Gao: "IRAK: a kinase associated with the interleukin-1 receptor." in: Science (New York, N.Y.), Vol. 271, Issue 5252, pp. 1128-31, 1996 (PubMed).
Jiang, Johnson, Nie et al.: "Pellino 1 is required for interleukin-1 (IL-1)-mediated signaling through its interaction with the IL-1 receptor-associated kinase 4 (IRAK4)-IRAK-tumor necrosis factor receptor-associated factor 6 (TRAF6) complex." in: The Journal of biological chemistry, Vol. 278, Issue 13, pp. 10952-6, 2003 (PubMed).
Jensen, Whitehead: "Pellino3, a novel member of the Pellino protein family, promotes activation of c-Jun and Elk-1 and may act as a scaffolding protein." in: Journal of immunology (Baltimore, Md. : 1950), Vol. 171, Issue 3, pp. 1500-6, 2003 (PubMed).
Validation Images
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57
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cf5cd1df0ee2161e1684bdc019357275
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-2,873,956,954,008,765,400
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Co-factor demand and regeneration in the enzymatic one-step reduction of carboxylates to aldehydes in cell-free systems
Gernot Strohmeier*, Anna Schwarz, Jennifer N. Andexer, Margit Winkler
*Korrespondierende/r Autor/-in für diese Arbeit
Publikation: Beitrag in einer FachzeitschriftArtikelBegutachtung
Abstract
Addressing the challenges associated with the development of in vitro biocatalytic carboxylate reductions for potential applications, important aspects of the co-factor regeneration systems and strategies for minimizing over-reduction were investigated. The ATP recycling can be performed with similarly high efficiency exploiting the polyphosphate source by combining Meiothermus ruber polyphosphate kinase and adenylate kinase or with Sinorhizobium meliloti polyphosphate kinase instead of the latter. Carboxylate reductions with the enzyme candidates used in this work allow operating at co-factor concentrations of adenosine 5'-triphosphate and β-nicotinamide adenine dinucleotide 2'-phosphate of 100 µM and, thereby, reducing the amounts of alcohols formed by side activities in the enzyme preparations. This study confirmed the expected benefits of carboxylic acid reductases in chemoselectively reducing the carboxylates to the corresponding aldehydes while leaving reductively-sensitive nitro, ester and cyano groups intact.
Originalspracheenglisch
Seiten (von - bis)202-207
Seitenumfang6
FachzeitschriftJournal of Biotechnology
Jahrgang307
DOIs
PublikationsstatusVeröffentlicht - 10 Jan. 2020
ASJC Scopus subject areas
• Angewandte Mikrobiologie und Biotechnologie
• Bioengineering
• Biotechnology
Fields of Expertise
• Human- & Biotechnology
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57
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cf5cd1df0ee2161e1684bdc019357275
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-367,957,830,254,816,260
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The United States Environmental Protection Agency’s Center for Computational Toxicology and Exposure
Browse
Presentation.pdf (3.55 MB)
The Influence of Turbidity, Light Intensity, and Temperature Stress on Microcystin-Production by Toxic Cyanobacteria in Oligotrophic Systems and Batch Experiments
Download (3.55 MB)
presentation
posted on 2023-11-21, 20:26 authored by Kansas Keeton, Terri Jicha, Aabir Banerji, Kasey Benesh, Anna Peterson, Brent Gilbertson, Matthew Lambert
Presentation to St. Louis River Estuary on March 8-10, 2023 in Duluth, MN
Science Inventory, CCTE products: https://cfpub.epa.gov/si/si_public_search_results.cfm?advSearch=true&showCriteria=2&keyword=CCTE&TIMSType=&TIMSSubTypeID=&epaNumber=&ombCat=Any&dateBeginPublishedPresented=07/01/2017&dateEndPublishedPresented=&dateBeginUpdated=&dateEndUpdated=&DEID=&personName=&personID=&role=Any&journalName=&journalID=&publisherName=&publisherID=&sortBy=pubDate&count=25
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57
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cf5cd1df0ee2161e1684bdc019357275
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-8,058,682,018,925,321,000
|
MexAM1_META1p3072 6827978 Gamma-glutamyl phosphate reductase (GPR) (Glutamate-5- semialdehyde dehydrogenase) (Glutamyl-gamma-semialdehyde dehydrogenase) (GSA dehydrogenase) (RefSeq)
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Residual Expression Plot
mex_bicluster_0138 0.38
mex_bicluster_0464 0.35
Title Insert TAG Module
NA
Orthologues Paralogues
COG EC Description TIGR Roles
(E) COG14 | Gamma-glutamyl phosphate reductase (1.2.1.41) Glutamate-5-semialdehyde dehydrogenase. Amino acid biosynthesis, Glutamate family
Product (LegacyBRC) Product (RefSeq)
GI Number Accession Blast Conserved Domains
240139621 YP_002964097.1 Run
Link to STRINGS STRINGS Network
MexAM1_META1p3072
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|
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Publications by: Madhavi Agrawal
Also publishes as (Madhavi A. Agrawal, Madhavi S. Agrawal)
Up a level
Export as [feed] Atom [feed] RSS 1.0 [feed] RSS 2.0
Number of items: 3.
Agrawal, Madhavi S., and Bowden, Bruce F. (2007) Noordehydrocyclodercitin, a hexacyclic pyridoacridine alkaloid from the marine ascidian, Aplidium sp. Natural Product Research, 21 (9). pp. 782-786.
Agrawal, Madhavi (2007) Isolation and structural elucidation of cytotoxic agents from marine invertebrates and plants sourced from the Great Barrier Reef, Australia. PhD thesis, James Cook University.
Agrawal, Madhavi A., and Bowden, Bruce F. (2005) Marine sponge Dysidea heracea revisited: another brominated diphenyl ether. Marine Drugs, 3 (1). pp. 9-14.
This list was generated on Fri Nov 24 14:05:56 2017 AEST.
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choanosomal
adjective
cho·a·no·som·al | \ ¦kōə(ˌ)nō¦sōməl, kō¦anə¦s- \
Definition of choanosomal
: of or relating to a choanosome
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Cite this Entry
“Choanosomal.” Merriam-Webster.com Dictionary, Merriam-Webster, https://www.merriam-webster.com/dictionary/choanosomal. Accessed 26 Sep. 2020.
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You are here:Home » Molecular Biology » MB-Growth Factors » Neuregulin 1 (NRG1) Recombinant, Human
Neuregulin 1 (NRG1) Recombinant, Human
Pricing
For pricing information, USA customers sign in.
Outside USA? Please contact your distributor for pricing.
Specifications
Catalog #156053
SourceRecombinant Human from E. coli
Purity 95%
Endotoxin1.0EU per 1ug (determined by the LAL method)
Accession NoE7EX30
FragmentGlu20~His242 (Accession No: E7EX30)
SequenceMGHHHHHHSGSEF- E MKSQESAAGS KLVLRCETSS EYSSLRFKWF KNGNELNRKN KPQNIKIQKK PGKSELRINK ASLADSGEYM CKVISKLGND SASANITIVE SNEIITGMPA STEGAYVSSA TSTSTTGTSH LVKCAEKEKT FCVNGGECFM VKDLSNPSRY LCKCPNEFTG DRCQNYVMAS FYKHLGIEFM EAEELYQKRV LTITGICIAL LVVGIMCVVA YCKTKKQRKK LH
Epitope TagN-terminal His-Tag
Molecular Weight26.3kD
ApplicationsSuitable for use in ELISA, Western Blot, Immunoprecipitation, SDS-PAGE.
Other applications not tested.
Recommended DilutionOptimal dilutions to be determined by the researcher.
Storage and StabilityMay be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -80°C. Aliquots are stable for at least 12 months from date of shipment. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
NoteThermal stability is described by the loss rate of the target protein. The loss rate was determined by accelerated thermal degradation by incubating the protein at 37°C for 48h, with no obvious degradation or precipitation observed. Protein loss is <5% within the expiration date under appropriate storage conditions.
Molecular Weight26.3kD
Important NoteThis product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications without the expressed written authorization of United States Biological.
External Links
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产品中心您的位置：网站首页 > 产品中心 > ASONE亚速旺 > 生命科学相关耗材 > AS2311日本ASONE亚速旺PCR管
日本ASONE亚速旺PCR管
日本ASONE亚速旺PCR管
更新时间：2022-05-20
访问量：410
厂商性质：代理商
生产地址：
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日本ASONE亚速旺PCR管AS2311
PCR管 PCRチューブ PCR TUBE
品牌：AS ONE/亚速旺
日本ASONE亚速旺PCR管AS2311特点：
● 管壁厚度极度均一，确保反应体系受热均匀，显著降低蒸发率。
● 管体V型倾角设计，可以贴合大多数品牌PCR仪的加热模块。
● 平盖和凸盖两种适用于不同PCR仪。
● 密封性好，开关轻松自如，减少手指磨损。
● 低蒸发率，低吸附，高热传导性。
● 无DNase，无Rnase.无热源。
规格：
● 材质：PP（聚丙烯）
● 颜色：透明
● 耐热温度：－40～121℃（可高温高压灭菌）
日本ASONE亚速旺PCR管AS2311
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6. 福建力得干式变压器温度控制器LD-B10系列。
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57
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cf5cd1df0ee2161e1684bdc019357275
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-5,733,012,784,869,632,000
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Skip to search formSkip to main content
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3,12-dihydroroquefortine
Known as: 2H-Pyrazino(1',2':1,5)pyrrolo(2,3-b)indole-1,4(3H,5aH)-dione, 10b-(1,1-dimethyl-2-propenyl)-6,10b,11,11a-tetrahydro-3-(1H-imidazol-4-ylmethyl)-
National Institutes of Health
Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
2018
2018
Abstract —Secondary metabolites of 25 Penicillium strains isolated from high-latitude ecosystems (upper layer of Antarctic soils… Expand
• table 1
• table 1
• table 3
• table 3
Is this relevant?
2007
2007
Mutants of a Penicillium roquefortii strain were obtained by ultraviolet irradiation (UV) and ethylmethansulfonate (EMS). Based… Expand
Is this relevant?
2007
2007
Mycotoxins produced by seven strains ofPenicillium vulpinum (formerlyPenicillium claviforme) isolated from different sources were… Expand
• table 1
• table 2
Is this relevant?
2005
2005
A new culturePenicillium farinosum synthesizing roquefortine and 3, 12-dihydroroquefortine was found. UnlikeP. roqueforti, a… Expand
• figure I
• figure 2
Is this relevant?
2004
2004
Secondary metabolites of three strains of Penicillium aurantiogriseumisolated from permafrost sediments were identified. It was… Expand
• figure 1
• figure 2
Is this relevant?
2004
2004
The ability to produce alkaloids has been studied in 13 strains belonging to ten species of the genus Penicillium. Most of these… Expand
• figure 2
• figure 1
• figure 3
Is this relevant?
2004
2004
New isomers of clavine alkaloids with distinctively low chromatographic mobilities were isolated from the collection and mutant… Expand
• figure 1
• figure 2
• table 1
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• figure 3
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2002
2002
The analysis of the absorption spectra of the low-molecular-weight nitrogen-containing secondary metabolites—alkaloids—of four… Expand
• table 1
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Is this relevant?
2000
2000
Fungi of the species Penicillium piscarium produced diketopiperazine alkaloids (isorugulosuvine, puberuline, verrucosine… Expand
Is this relevant?
1979
1979
The alkaloid composition of mycelium and culture liquid filtrate of the fungus Penicillium roqueforti IBPM-F-141 was studied. The… Expand
Is this relevant?
|
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Tag Genetics
Sussman to lead Genome Center of Wisconsin
Mike Sussman, longtime director of the UW–Madison Biotechnology Center, has announced that he is stepping down from that position to serve as director of the genome center. Chris Bradfield has been named interim Biotechnology Center director.
An Achilles heel discovered in viruses could fuel new antiviral approaches
Scientists at the Morgridge Institute for Research have discovered a promising new target to fight a class of viruses responsible for health threats such as Zika, polio, dengue, SARS and hepatitis C.
Study advances gene therapy for glaucoma
A new study shows an improved tactic for delivering new genes into the eye's drain, called the trabecular meshwork, offering a promising treatment for glaucoma.
Designer molecule points to treatment for diseases caused by DNA repeats
“Most young people with Friedreich’s ataxia develop severe heart problems and are wheelchair-bound," says researcher Aseem Ansari, "but the disease is so rare that few drug companies invest in it."
Course explores new field at intersection of genomics and society
Jason Fletcher is researching how public policy intersects with genetic data, what our genes can predict about how society functions, and how we should use this data responsibly — an area of study dubbed "social genomics."
Reflective art installation displays beauty, intrigue of genetics
Pictures obtained from Ahna Skop’s exploration of the cell — as well as striking images from other UW–Madison research projects — will serve as a basis for a traveling art exhibit, “Genetic Reflections.”
Genetics and stress interact to shape human health and well-being
Scientists at the University of Wisconsin–Madison’s Waisman Center have shown one way in which human genetics and chronic stress interact to shape health and well-being later in life.
Bacterial supermachine reveals streamlined protein assembly line
Biochemists from the University of Wisconsin–Madison and the Max Planck Institute (MPI) for Biophysical Chemistry in Germany have revealed the defined architecture of what is called the “expressome.”
Fred Blattner: genetics pioneer, entrepreneurial success, and all that jazz
Fred Blattner has been doing DNA research for more than 50 years, and he founded or co-founded three successful companies all focused on DNA: DNASTAR, Nimblegen and Scarab Genomics.
Fast Plants Program’s new varieties are tailored for classroom use
A UW–Madison program built around plants that mature quickly enough to engage the scientific curiosity of elementary through college students is releasing two new varieties that make the popular plants even better suited to classrooms.
Food scientist aiding fuel ethanol with new engineered bacteria
James Steele’s new company, Lactic Solutions, is advancing a judo-like remedy: using genetic engineering to transform enemy into friend.
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Kevin
Kevin is a lifelong learner and continues to advance his knowledge deeper in biology and also in programming, computer networking, and design. Kevin is a Postdoctoral Research Fellow in the Department of Integrative Biology and Pharmacology at the University of Texas Medical School at Houston in the Levental Lab. His work has contributed to the understanding of the dynamic nature of lipids and proteins in cellular membranes and how dynamic changes in sections of the cell membrane regulate cellular activity and contribute to disease states.
Prior to joining the Levental Lab, Kevin received his Ph.D. at the University of Houston (UH) in Biology. His research focused on genome evolution, population genetics of copy number variation, and eukaryotic parasitism. His work involved bench laboratory work as well as programming computer simulations and advanced statistical analysis of large data sets. He was involved with many student activities at UH, including acting treasurer and sports coordinator for the BioScience Graduate Society, founding member and treasurer of Students for Personal Safety, and mentoring undergraduate students in independent research. Kevin also worked at UH as a teacher in microbiology for science major students.
Kevin received his Bachelor’s in Science from the University of Houston – Downtown, where he started his research experience under Lisa Morano, Ph.D. and Jeff Flosi, Ph.D. He made the Dean’s list and was awarded a research scholarship for his work on testing the effectiveness of agriculture disease assays. During his undergraduate education, Kevin supported himself through school by working at the law firm Vinson & Elkins.
0
answers
1
question
~1k
people reached
• Houston, TX
• Member for 5 years, 4 months
• 3 profile views
• Last seen Aug 14 '16 at 22:32
Top tags (1)
Score 0
Posts 1
Posts % 100
Top posts (1) All Questions Answers | Votes Newest
Badges (4)
Gold
Silver
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4
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