MurAA, catalysing the first committed step in peptidoglycan biosynthesis, is a target of Clp-dependent proteolysis in Bacillus subtilis
about
The Bacillus subtilis ywjI (glpX) gene encodes a class II fructose-1,6-bisphosphatase, functionally equivalent to the class III Fbp enzymeAdaptor protein controlled oligomerization activates the AAA+ protein ClpCComprehensive analysis of temporal alterations in cellular proteome of Bacillus subtilis under curcumin treatmentInvestigations to the Antibacterial Mechanism of Action of KendomycinClp-dependent proteolysis down-regulates central metabolic pathways in glucose-starved Bacillus subtilis.The ClpP protease homologue is required for the transmission traits and cell division of the pathogen Legionella pneumophilaCharacterization of the CtsR stress response regulon in Lactobacillus plantarumExposure of Staphylococcus aureus to subinhibitory concentrations of β-lactam antibiotics induces heterogeneous vancomycin-intermediate Staphylococcus aureusMurAA is required for intrinsic cephalosporin resistance of Enterococcus faecalisEvidence for the horizontal transfer of an unusual capsular polysaccharide biosynthesis locus in marine bacteriaDysregulation of bacterial proteolytic machinery by a new class of antibiotics.The antibiotic ADEP reprogrammes ClpP, switching it from a regulated to an uncontrolled protease.Proteomics analyses of Bacillus subtilis after treatment with plumbagin, a plant-derived naphthoquinone.Pharmacological inhibition of the ClpXP protease increases bacterial susceptibility to host cathelicidin antimicrobial peptides and cell envelope-active antibiotics.Clp ATPases and ClpP proteolytic complexes regulate vital biological processes in low GC, Gram-positive bacteria.The Staphylococcus aureus thiol/oxidative stress global regulator Spx controls trfA, a gene implicated in cell wall antibiotic resistance.Random mutagenesis identifies novel genes involved in the secretion of antimicrobial, cell wall-lytic enzymes by Lactococcus lactis.A cytoplasmic peptidoglycan amidase homologue controls mycobacterial cell wall synthesisIdentification by genomic and genetic analysis of two new genes playing a key role in intermediate glycopeptide resistance in Staphylococcus aureusTrapping and identification of cellular substrates of the Staphylococcus aureus ClpC chaperonePeptidoglycan biosynthesis machinery: a rich source of drug targets.Fosfomycin: Mechanism and Resistance.Suppressor Mutations Linking gpsB with the First Committed Step of Peptidoglycan Biosynthesis in Listeria monocytogenes.The ClpP peptidase is the major determinant of bulk protein turnover in Bacillus subtilis.Global regulatory impact of ClpP protease of Staphylococcus aureus on regulons involved in virulence, oxidative stress response, autolysis, and DNA repair.Involvement of Bacillus subtilis ClpE in CtsR degradation and protein quality control.Analysis of the role of Bacillus subtilis σ(M) in β-lactam resistance reveals an essential role for c-di-AMP in peptidoglycan homeostasis.Life and death of proteins: a case study of glucose-starved Staphylococcus aureus.Regulation of cyclic lipopeptide biosynthesis in Pseudomonas fluorescens by the ClpP protease.Spore cortex formation in Bacillus subtilis is regulated by accumulation of peptidoglycan precursors under the control of sigma K.Involvement of Clp protease activity in modulating the Bacillus subtilissigmaw stress response.Envelope Structures of Gram-Positive Bacteria.A metabolomics and proteomics study of the adaptation of Staphylococcus aureus to glucose starvation
P2860
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P2860
MurAA, catalysing the first committed step in peptidoglycan biosynthesis, is a target of Clp-dependent proteolysis in Bacillus subtilis
description
2004 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 2004
@ast
im Februar 2004 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2004/02/01)
@sk
vědecký článek publikovaný v roce 2004
@cs
wetenschappelijk artikel (gepubliceerd op 2004/02/01)
@nl
наукова стаття, опублікована в лютому 2004
@uk
مقالة علمية (نشرت في فبراير 2004)
@ar
name
MurAA, catalysing the first co ...... oteolysis in Bacillus subtilis
@ast
MurAA, catalysing the first co ...... oteolysis in Bacillus subtilis
@en
MurAA, catalysing the first co ...... oteolysis in Bacillus subtilis
@nl
type
label
MurAA, catalysing the first co ...... oteolysis in Bacillus subtilis
@ast
MurAA, catalysing the first co ...... oteolysis in Bacillus subtilis
@en
MurAA, catalysing the first co ...... oteolysis in Bacillus subtilis
@nl
prefLabel
MurAA, catalysing the first co ...... oteolysis in Bacillus subtilis
@ast
MurAA, catalysing the first co ...... oteolysis in Bacillus subtilis
@en
MurAA, catalysing the first co ...... oteolysis in Bacillus subtilis
@nl
P2093
P2860
P3181
P1476
MurAA, catalysing the first co ...... oteolysis in Bacillus subtilis
@en
P2093
Holger Kock
Michael Hecker
P2860
P304
P3181
P356
10.1046/J.1365-2958.2003.03875.X
P407
P577
2004-02-01T00:00:00Z