The Mycobacterium tuberculosis protein LdtMt2 is a nonclassical transpeptidase required for virulence and resistance to amoxicillin.
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Resistance to antibiotics targeted to the bacterial cell wallProtein complexes and proteolytic activation of the cell wall hydrolase RipA regulate septal resolution in mycobacteriaTargeting the Cell Wall of Mycobacterium tuberculosis: Structure and Mechanism of L,D-Transpeptidase 2Structural basis for the inhibition ofMycobacterium tuberculosisL,D-transpeptidase by meropenem, a drug effective against extensively drug-resistant strainsStructure of LdtMt2, anL,D-transpeptidase fromMycobacterium tuberculosisCrystal structure of L,D-transpeptidase LdtMt2 in complex with meropenem reveals the mechanism of carbapenem against Mycobacterium tuberculosisStructures of free and inhibited forms of the L,D-transpeptidase LdtMt1 from Mycobacterium tuberculosisComparative genomic analysis of Mycobacterium tuberculosis drug resistant strains from RussiaKinetic features of L,D-transpeptidase inactivation critical for β-lactam antibacterial activityBinding and processing of β-lactam antibiotics by the transpeptidase LdtMt2 from Mycobacterium tuberculosis.New Insights in to the Intrinsic and Acquired Drug Resistance Mechanisms in MycobacteriaStructural insight into the inactivation of Mycobacterium tuberculosis non-classical transpeptidase LdtMt2 by biapenem and tebipenem.Protective efficacy of BCG overexpressing an L,D-transpeptidase against M. tuberculosis infection.Non-classical transpeptidases yield insight into new antibacterialsGenetic characterization of mycobacterial L,D-transpeptidases.Cell wall structure and function in lactic acid bacteria.Mycobacteriophage endolysins: diverse and modular enzymes with multiple catalytic activities.Synthetic lethality reveals mechanisms of Mycobacterium tuberculosis resistance to β-lactamsThe cell envelope glycoconjugates of Mycobacterium tuberculosisQuantitative mass spectrometry reveals plasticity of metabolic networks in Mycobacterium smegmatis.The peptidoglycan of Mycobacterium abscessus is predominantly cross-linked by L,D-transpeptidasesGenetics of Capsular Polysaccharides and Cell Envelope (Glyco)lipids.Activity of carbapenems combined with clavulanate against murine tuberculosis.Inactivation kinetics of a new target of beta-lactam antibiotics.Comparative genomics for mycobacterial peptidoglycan remodelling enzymes reveals extensive genetic multiplicityClostridium difficile has an original peptidoglycan structure with a high level of N-acetylglucosamine deacetylation and mainly 3-3 cross-links.Diaminopimelic Acid Amidation in Corynebacteriales: NEW INSIGHTS INTO THE ROLE OF LtsA IN PEPTIDOGLYCAN MODIFICATIONChiZ levels modulate cell division process in mycobacteria.Transcriptional Profiling of Coxiella burnetii Reveals Extensive Cell Wall Remodeling in the Small Cell Variant Developmental Form.Messenger functions of the bacterial cell wall-derived muropeptides.Kinetic analysis of Enterococcus faecium L,D-transpeptidase inactivation by carbapenemsInactivation of Mycobacterium tuberculosis l,d-transpeptidase LdtMt₁ by carbapenems and cephalosporinsPeptidoglycan synthesis in Mycobacterium tuberculosis is organized into networks with varying drug susceptibility.Loss of a Functionally and Structurally Distinct ld-Transpeptidase, LdtMt5, Compromises Cell Wall Integrity in Mycobacterium tuberculosis.Meropenem inhibits D,D-carboxypeptidase activity in Mycobacterium tuberculosis.Crystal structure of FadD32, an enzyme essential for mycolic acid biosynthesis in mycobacteria.Identification of Mycobacterial Genes Involved in Antibiotic Sensitivity: Implications for the Treatment of Tuberculosis with β-Lactam-Containing Regimens.Acyl acceptor recognition by Enterococcus faecium L,D-transpeptidase Ldtfm.Toward antituberculosis drugs: in silico screening of synthetic compounds against Mycobacterium tuberculosisl,d-transpeptidase 2Rv1894c is a novel hypoxia-induced nitronate monooxygenase required for Mycobacterium tuberculosis virulence.
P2860
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P2860
The Mycobacterium tuberculosis protein LdtMt2 is a nonclassical transpeptidase required for virulence and resistance to amoxicillin.
description
2010 nî lūn-bûn
@nan
2010 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի մարտին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年学术文章
@wuu
2010年学术文章
@zh-cn
2010年学术文章
@zh-hans
2010年学术文章
@zh-my
2010年学术文章
@zh-sg
2010年學術文章
@yue
name
The Mycobacterium tuberculosis ...... and resistance to amoxicillin.
@ast
The Mycobacterium tuberculosis ...... and resistance to amoxicillin.
@en
type
label
The Mycobacterium tuberculosis ...... and resistance to amoxicillin.
@ast
The Mycobacterium tuberculosis ...... and resistance to amoxicillin.
@en
prefLabel
The Mycobacterium tuberculosis ...... and resistance to amoxicillin.
@ast
The Mycobacterium tuberculosis ...... and resistance to amoxicillin.
@en
P2860
P50
P356
P1433
P1476
The Mycobacterium tuberculosis ...... and resistance to amoxicillin
@en
P2093
Radhika Gupta
William R Bishai
P2860
P2888
P304
P356
10.1038/NM.2120
P407
P577
2010-03-21T00:00:00Z