The vapBC operon from Mycobacterium smegmatis is an autoregulated toxin-antitoxin module that controls growth via inhibition of translation.
about
Comprehensive functional analysis of Mycobacterium tuberculosis toxin-antitoxin systems: implications for pathogenesis, stress responses, and evolutionMetabolic engineering of cofactor F420 production in Mycobacterium smegmatisKeeping the Wolves at Bay: Antitoxins of Prokaryotic Type II Toxin-Antitoxin SystemsToxin-antitoxin systems: Biology, identification, and applicationThe crystal structure of the Rv0301-Rv0300 VapBC-3 toxin-antitoxin complex fromM. tuberculosisreveals a Mg2+ion in the active site and a putative RNA-binding siteCrystal Structure of the VapBC Toxin–Antitoxin Complex from Shigella flexneri Reveals a Hetero-Octameric DNA-Binding AssemblyStructure, Biology, and Therapeutic Application of Toxin-Antitoxin Systems in Pathogenic BacteriaCharacterization of the interaction and cross-regulation of three Mycobacterium tuberculosis RelBE modulesInduced ectopic expression of HigB toxin in Mycobacterium tuberculosis results in growth inhibition, reduced abundance of a subset of mRNAs and cleavage of tmRNAAnalyzing the regulatory role of the HigA antitoxin within Mycobacterium tuberculosisBacterial genome instabilityMqsR/MqsA Toxin/Antitoxin System Regulates Persistence and Biofilm Formation in Pseudomonas putida KT2440.VapC toxins from Mycobacterium tuberculosis are ribonucleases that differentially inhibit growth and are neutralized by cognate VapB antitoxins.The PIN-domain ribonucleases and the prokaryotic VapBC toxin-antitoxin array.Enteric virulence associated protein VapC inhibits translation by cleavage of initiator tRNARegulation of the vapBC-1 toxin-antitoxin locus in nontypeable Haemophilus influenzae.Determination of ribonuclease sequence-specificity using Pentaprobes and mass spectrometry.A VapBC toxin-antitoxin module is a posttranscriptional regulator of metabolic flux in mycobacteria.Recent advancements in toxin and antitoxin systems involved in bacterial programmed cell death.Characterization of a chromosomal type II toxin-antitoxin system mazEaFa in the Cyanobacterium Anabaena sp. PCC 7120.Regulated Expression Systems for Mycobacteria and Their ApplicationsOne cannot rule them all: Are bacterial toxins-antitoxins druggable?Structural and functional studies of the Mycobacterium tuberculosis VapBC30 toxin-antitoxin system: implications for the design of novel antimicrobial peptidesCharacterization of the Deep-Sea Streptomyces sp. SCSIO 02999 Derived VapC/VapB Toxin-Antitoxin System in Escherichia coli.Regulating toxin-antitoxin expression: controlled detonation of intracellular molecular timebombsToxins-antitoxins: diversity, evolution and function.Chromosomal bacterial type II toxin-antitoxin systems.Higher-Order Structure in Bacterial VapBC Toxin-Antitoxin Complexes.Toxins of Prokaryotic Toxin-Antitoxin Systems with Sequence-Specific Endoribonuclease Activity.VapC6, a ribonucleolytic toxin regulates thermophilicity in the crenarchaeote Sulfolobus solfataricusCo-expression network analysis of toxin-antitoxin loci in Mycobacterium tuberculosis reveals key modulators of cellular stress.The vapB-vapC Operon of Acidovorax citrulli Functions as a Bona-fide Toxin-Antitoxin ModuleThe Mycobacterium tuberculosis relBE toxin:antitoxin genes are stress-responsive modules that regulate growth through translation inhibition.Structure and Function of a Novel ATPase that Interacts with Holliday Junction Resolvase Hjc and Promotes Branch Migration.Toxin-antitoxin systems of Mycobacterium smegmatis are essential for cell survival.Cell growth inhibition upon deletion of four toxin-antitoxin loci from the megaplasmids of Sinorhizobium meliloti.Regulation of enteric vapBC transcription: induction by VapC toxin dimer-breaking.Essentiality of succinate dehydrogenase in Mycobacterium smegmatis and its role in the generation of the membrane potential under hypoxia.Three different [NiFe] hydrogenases confer metabolic flexibility in the obligate aerobe Mycobacterium smegmatis.Convergent evolution and topologically disruptive polymorphisms among multidrug-resistant tuberculosis in Peru.
P2860
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P2860
The vapBC operon from Mycobacterium smegmatis is an autoregulated toxin-antitoxin module that controls growth via inhibition of translation.
description
2009 nî lūn-bûn
@nan
2009 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
The vapBC operon from Mycobact ...... via inhibition of translation.
@ast
The vapBC operon from Mycobact ...... via inhibition of translation.
@en
The vapBC operon from Mycobact ...... via inhibition of translation.
@nl
type
label
The vapBC operon from Mycobact ...... via inhibition of translation.
@ast
The vapBC operon from Mycobact ...... via inhibition of translation.
@en
The vapBC operon from Mycobact ...... via inhibition of translation.
@nl
prefLabel
The vapBC operon from Mycobact ...... via inhibition of translation.
@ast
The vapBC operon from Mycobact ...... via inhibition of translation.
@en
The vapBC operon from Mycobact ...... via inhibition of translation.
@nl
P2093
P1476
The vapBC operon from Mycobact ...... via inhibition of translation.
@en
P2093
Gregory M Cook
Jennifer Robson
Joanna L McKenzie
Ray Cursons
Vickery L Arcus
P304
P356
10.1016/J.JMB.2009.05.006
P407
P577
2009-05-13T00:00:00Z