Growth and translation inhibition through sequence-specific RNA binding by Mycobacterium tuberculosis VapC toxin. - Wikidata - wikimedia - TriplyDB

Growth and translation inhibition through sequence-specific RNA binding by Mycobacterium tuberculosis VapC toxin.

Growth and translation inhibition through sequence-specific RNA binding by Mycobacterium tuberculosis VapC toxin.

http://www.wikidata.org/entity/Q35921645

about

Emerging Roles of Toxin-Antitoxin Modules in Bacterial Pathogenesis An RNA-seq method for defining endoribonuclease cleavage specificity identifies dual rRNA substrates for toxin MazF-mt3.Induced ectopic expression of HigB toxin in Mycobacterium tuberculosis results in growth inhibition, reduced abundance of a subset of mRNAs and cleavage of tmRNA VapC20 of Mycobacterium tuberculosis cleaves the sarcin-ricin loop of 23S rRNA Analysis of non-typeable Haemophilous influenzae VapC1 mutations reveals structural features required for toxicity and flexibility in the active site Wake me when it's over - Bacterial toxin-antitoxin proteins and induced dormancy Latent tuberculosis infection: myths, models, and molecular mechanisms Regulated Expression Systems for Mycobacteria and Their Applications Transcriptional and proteolytic regulation of the toxin-antitoxin locus vapBC10 (ssr2962/slr1767) on the chromosome of Synechocystis sp. PCC 6803.Structure-function analysis of VapB4 antitoxin identifies critical features of a minimal VapC4 toxin-binding module Structural and functional studies of the Mycobacterium tuberculosis VapBC30 toxin-antitoxin system: implications for the design of novel antimicrobial peptides Growth-regulating Mycobacterium tuberculosis VapC-mt4 toxin is an isoacceptor-specific tRNase.tRNAs taking charge.tRNA is a new target for cleavage by a MazF toxin Characterization of MazF-Mediated Sequence-Specific RNA Cleavage in Pseudomonas putida Using Massive Parallel Sequencing Characterization of the Deep-Sea Streptomyces sp. SCSIO 02999 Derived VapC/VapB Toxin-Antitoxin System in Escherichia coli.Multiple toxin-antitoxin systems in Mycobacterium tuberculosis.Molecular biology of drug resistance in Mycobacterium tuberculosis Post-transcriptional regulation of gene expression in bacterial pathogens by toxin-antitoxin systems.Antibiotic resistance mechanisms in M. tuberculosis: an update.Higher-Order Structure in Bacterial VapBC Toxin-Antitoxin Complexes.Identification of a VapBC toxin-antitoxin system in a thermophilic bacterium Thermus thermophilus HB27.VapC toxins drive cellular dormancy under uranium stress for the extreme thermoacidophile Metallosphaera prunae.Type II Toxin-Antitoxin Systems in the Unicellular Cyanobacterium Synechocystis sp. PCC 6803.Co-expression network analysis of toxin-antitoxin loci in Mycobacterium tuberculosis reveals key modulators of cellular stress.The Mycobacterium tuberculosis relBE toxin:antitoxin genes are stress-responsive modules that regulate growth through translation inhibition.The VapBC1 toxin-antitoxin complex from Mycobacterium tuberculosis: purification, crystallization and X-ray diffraction analysis.Toxin-Antitoxin Systems in Bacteria and Archaea VapC proteins from Mycobacterium tuberculosis share ribonuclease sequence specificity but differ in regulation and toxicity

P2860

Q26744373-A6DEAC87-C6E5-4F79-A713-F4C2B62EBA5C Q28486509-4352F512-3CCE-4DAD-8D37-13C943FE5F1A Q28487083-DA22AA43-6100-4D1A-90ED-2820B76BE72D Q28487499-388E174D-84D9-4C84-BCC3-225EBF91F425 Q28544904-E3387F38-94AA-4028-B30E-CCDE98625DCE Q28601184-E82DBFDD-28B0-4923-BC43-08111E245D16 Q34297816-24848DF7-C415-40BC-BBC9-2828E31868FE Q34626585-7195C309-1870-43FA-9794-22E7D13CF6F0 Q35049212-D131ABE0-C1BC-4C50-8D8C-7723101E908E Q35156594-40AC0D29-ADF9-4A9A-953D-96DEADBD33A1 Q36002459-EA459BDA-C84C-4EA8-AC87-3523D43C009B Q36207778-B8A7C69C-8755-4BF5-871B-30761219A7AE Q36443829-B9E52BFB-3C5F-44BF-8FAB-1D41CDE99515 Q36588904-93E380E4-F771-4EDF-A367-378FD45DA246 Q36590715-1F82C14A-DA38-4EB4-B1DE-7FCB5FDB74B4 Q37132897-515C7FF3-417A-46E6-8958-3C03501FF1C4 Q37670036-FB7B60C9-080C-4E6A-ABE1-89D1B857A6E8 Q38062402-D3CBB3D3-2833-46DF-9E02-56F997D4D9D5 Q38187662-26DA41C9-7F71-4E5F-9540-55AF4C968AC4 Q38830420-08E60EB9-145F-48CE-ADCF-8816DAE28CF4 Q39167588-694E3252-FEDD-40BF-8D11-D8D3152ADFF1 Q39181653-20D69087-3E69-432D-A795-453144B7472B Q39190958-EA19FFA0-9AED-4339-8423-56074880C254 Q39562676-9B7E4FB7-BDCD-47A2-BA33-16162EAF9BA0 Q40127415-9D86AAC0-6C18-4F98-BE17-884AB2D27A5A Q40936733-23829FFC-35FC-4487-BC2C-A267391C1B9A Q51702108-C73EEC83-590B-4C68-BBED-F3D3D4126154 Q57987392-2DD323C3-24B9-44E6-8654-45D6FA435780 Q58782384-FF41C2DD-F2D4-4298-A44D-948F1E050910

P2860

Growth and translation inhibition through sequence-specific RNA binding by Mycobacterium tuberculosis VapC toxin.

http://www.wikidata.org/entity/Q35921645

description

2012 nî lūn-bûn

@nan

2012年の論文

@ja

2012年論文

@yue

2012年論文

@zh-hant

2012年論文

@zh-hk

2012年論文

@zh-mo

2012年論文

@zh-tw

2012年论文

@wuu

2012年论文

@zh

2012年论文

@zh-cn

name

Growth and translation inhibit ...... erium tuberculosis VapC toxin.

@ast

Growth and translation inhibit ...... erium tuberculosis VapC toxin.

@en

type

label

Growth and translation inhibit ...... erium tuberculosis VapC toxin.

@ast

Growth and translation inhibit ...... erium tuberculosis VapC toxin.

@en

prefLabel

Growth and translation inhibit ...... erium tuberculosis VapC toxin.

@ast

Growth and translation inhibit ...... erium tuberculosis VapC toxin.

@en

P1433

Q35921645-A22AEA23-7975-4E80-B12C-C96609CFAB18

P1476

Q35921645-EA15E613-AE57-4BB0-A8C8-D04D4103926E

P2093

Q35921645-1EDA7EA4-6ADA-41D3-9A14-45845A7B51A9

Q35921645-50719FDB-ED2E-42FE-A23E-D0CEE2425BBB

Q35921645-62838B5B-7BF5-4C4B-A844-D0F300427B17

Q35921645-90241AA1-7A43-4F93-9F3D-163812A4A458

Q35921645-E79E71DF-13B4-4367-ABBB-BA7A8B6429C1

Q35921645-FD51793E-59B7-484A-BF65-E9F089D9FB39

P2860

Q35921645-07242188-FE35-4597-9D6F-938AC56369B0

Q35921645-0A6433CB-6E78-4536-B159-EC6ED0DC0756

Q35921645-1196EA4F-7D7D-4718-B352-1C61D02EF655

Q35921645-1A26484E-6DEE-464B-8077-1E42E92ECA4A

Q35921645-1BE9583A-B5AA-4878-9291-5B4ECAFDA427

Q35921645-1D2413E2-DFF3-4736-82DB-54A6274C8DA8

Q35921645-1D990ED0-B1D5-4FC2-A6C3-3922B7851DA0

Q35921645-2FABC8E7-4DC4-4F57-AD6F-577C347D969F

Q35921645-2FB580A6-8707-4603-B688-0FF16F2B1894

Q35921645-3C06B923-F1BD-49A0-AAEE-43715C4F5551

P304

Q35921645-665E6DF2-2569-4470-903B-CE5BF4E4DDCC

P31

Q35921645-26DEFD50-66EF-43CC-A0A4-1825CCC292DA

P356

Q35921645-0186E909-BDA7-4B95-BDE3-7117D06A825D

P407

Q35921645-1E94EDAD-E960-48FC-9F0A-CD9E1C2BD2A3

P433

Q35921645-DC1BC630-A8F5-474C-98FC-C23D19941436

P478

Q35921645-97403231-D688-48AE-B86E-2D04C3E5E3A7

P577

Q35921645-4D67F6C5-5617-46D3-8FE6-7B35E5E58AB6

P698

Q35921645-3B0D691B-E42C-440E-82A0-47BC713E576B

P921

Q35921645-9F63AE9C-8207-45D8-BDB0-8F7EBE8BA9EC

P932

Q35921645-9484D3FD-C5D4-409F-A521-A16EDF2203A6

P356

JBC.M112.340109

P1433

Journal of Biological Chemistry

P1476

Growth and translation inhibit ...... erium tuberculosis VapC toxin.

@en

P2093

Jared D Sharp

http://www.w3.org/2001/XMLSchema#string

Jonathan W Cruz

http://www.w3.org/2001/XMLSchema#string

Masayori Inouye

http://www.w3.org/2001/XMLSchema#string

Nancy A Woychik

http://www.w3.org/2001/XMLSchema#string

Robert N Husson

http://www.w3.org/2001/XMLSchema#string

Sahadevan Raman

http://www.w3.org/2001/XMLSchema#string

P2860

Comprehensive functional analysis of Mycobacterium tuberculosis toxin-antitoxin systems: implications for pathogenesis, stress responses, and evolution

RelE, a global inhibitor of translation, is activated during nutritional stress

Toxin-antitoxin loci are highly abundant in free-living but lost from host-associated prokaryotes

Crystallization and preliminary X-ray analysis of the PIN domain of human EST1A

An SOS-regulated type 2 toxin-antitoxin system

Structure and proposed activity of a member of the VapBC family of toxin-antitoxin systems. VapBC-5 from Mycobacterium tuberculosis

Structures of the PIN domains of SMG6 and SMG5 reveal a nuclease within the mRNA surveillance complex

Controlling gene expression in mycobacteria with anhydrotetracycline and Tet repressor

Distant structural homology leads to the functional characterization of an archaeal PIN domain as an exonuclease

The Structural Basis for mRNA Recognition and Cleavage by the Ribosome-Dependent Endonuclease RelE

P304

12835-12847

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1074/JBC.M112.340109

http://www.w3.org/2001/XMLSchema#string

P407

P433

16

http://www.w3.org/2001/XMLSchema#string

P478

287

http://www.w3.org/2001/XMLSchema#string

P577

2012-02-21T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

22354968

http://www.w3.org/2001/XMLSchema#string

P921

Mycobacterium tuberculosis

P932

3339977

http://www.w3.org/2001/XMLSchema#string