Results 1 to 10 of about 1,011 (109)

VapC proteins from Mycobacterium tuberculosis share ribonuclease sequence specificity but differ in regulation and toxicity. [PDF]

open access: goldPLoS ONE, 2018
The chromosome of Mycobacterium tuberculosis (Mtb) contains a large number of Type II toxin-antitoxin (TA) systems. The majority of these belong to the VapBC TA family, characterised by the VapC protein consisting of a PIN domain with four conserved ...
Abigail Sharrock   +4 more
doaj   +4 more sources

Characterization of the Deep-Sea Streptomyces sp. SCSIO 02999 Derived VapC/VapB Toxin-Antitoxin System in Escherichia coli [PDF]

open access: goldToxins, 2016
Toxin-antitoxin (TA) systems are small genetic elements that are ubiquitous in prokaryotes. Most studies on TA systems have focused on commensal and pathogenic bacteria; yet very few studies have focused on TAs in marine bacteria, especially those ...
Yunxue Guo   +4 more
doaj   +3 more sources

In Silico Analysis of Genetic VapC Profiles from the Toxin-Antitoxin Type II VapBC Modules among Pathogenic, Intermediate, and Non-Pathogenic Leptospira [PDF]

open access: goldMicroorganisms, 2019
Pathogenic Leptospira spp. is the etiological agent of leptospirosis. The high diversity among Leptospira species provides an array to look for important mediators involved in pathogenesis.
Alexandre P. Y. Lopes   +5 more
doaj   +3 more sources

Toxins VapC and PasB from Prokaryotic TA Modules Remain Active in Mammalian Cancer Cells [PDF]

open access: goldToxins, 2014
Among the great number of addictive modules which have been discovered, only a few have been characterized. However, research concerning the adoption of toxins from these systems shows their great potential as a tool for molecular biology and medicine.
Łukasz Wieteska   +3 more
doaj   +3 more sources

The vapB-vapC operon of Acidovorax citrulli functions as a bona-fide toxin-antitoxin module [PDF]

open access: goldFrontiers in Microbiology, 2016
Toxin–antitoxin systems are commonly found on plasmids and chromosomes of bacteria and archaea. These systems appear as biscystronic genes encoding a stable toxin and a labile antitoxin, which protects the cells from the toxin’s activity. Under specific,
Reut eShavit   +4 more
doaj   +3 more sources

VAPC, an human endogenous inhibitor for hepatitis C virus (HCV) infection, is intrinsically unstructured but forms a "fuzzy complex" with HCV NS5B. [PDF]

open access: goldPLoS ONE, 2012
Nearly 200 million people are infected by hepatitis C virus (HCV) worldwide. For replicating the HCV genome, the membrane-associated machinery needs to be formed by both HCV non-structural proteins (including NS5B) and human host factors such as VAPB ...
Shaveta Goyal   +6 more
doaj   +4 more sources

VapC toxins from Mycobacterium tuberculosis are ribonucleases that differentially inhibit growth and are neutralized by cognate VapB antitoxins. [PDF]

open access: goldPLoS ONE, 2011
The chromosome of Mycobacterium tuberculosis (Mtb) encodes forty seven toxin-antitoxin modules belonging to the VapBC family. The role of these modules in the physiology of Mtb and the function(s) served by their expansion are unknown.
Bintou Ahmadou Ahidjo   +7 more
doaj   +4 more sources

VapC from the leptospiral VapBC toxin-antitoxin module displays ribonuclease activity on the initiator tRNA.

open access: goldPLoS ONE, 2014
The prokaryotic ubiquitous Toxin-Antitoxin (TA) operons encode a stable toxin and an unstable antitoxin. The most accepted hypothesis of the physiological function of the TA system is the reversible cessation of cellular growth under stress conditions ...
Alexandre P Y Lopes   +8 more
doaj   +4 more sources

Effect of rickettsial toxin VapC on its eukaryotic host.

open access: goldPLoS ONE, 2011
Rickettsia are intracellular bacteria typically associated with arthropods that can be transmitted to humans by infected vectors. Rickettsia spp. can cause mild to severe human disease with a possible protection effect of corticosteroids when antibiotic ...
Gilles Audoly   +9 more
doaj   +4 more sources

Phosphorylation of VapB antitoxins affects intermolecular interactions to regulate VapC toxin activity in <i>Mycobacterium tuberculosis</i>. [PDF]

open access: closedJ Bacteriol
Toxin–antitoxin modules are present in many bacterial pathogens. The VapBC family is particularly abundant in members of the Mycobacterium tuberculosis complex, with 50 modules present in the M. tuberculosis genome.
Malakar B   +4 more
europepmc   +3 more sources

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