Irreversible inhibition of the Mycobacterium tuberculosis beta-lactamase by clavulanate.
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Carbapenems to Treat Multidrug and Extensively Drug-Resistant Tuberculosis: A Systematic ReviewRising to the challenge: new therapies for tuberculosisMeropenem-Clavulanate Is Effective Against Extensively Drug-Resistant Mycobacterium tuberculosisBiochemical and Structural Characterization of Mycobacterium tuberculosis β-Lactamase with the Carbapenems Ertapenem and DoripenemStructures of the Michaelis Complex (1.2 Å) and the Covalent Acyl Intermediate (2.0 Å) of Cefamandole Bound in the Active Sites of the Mycobacterium tuberculosis β-Lactamase K73A and E166A Mutants,Targeting the Cell Wall of Mycobacterium tuberculosis: Structure and Mechanism of L,D-Transpeptidase 2Structure of LdtMt2, anL,D-transpeptidase fromMycobacterium tuberculosisNXL104 Irreversibly Inhibits the β-Lactamase from Mycobacterium tuberculosisDirected evolution of Mycobacterium tuberculosis β-lactamase reveals gatekeeper residue that regulates antibiotic resistance and catalytic efficiencyCan Inhibitor-Resistant Substitutions in the Mycobacterium tuberculosis -Lactamase BlaC Lead to Clavulanate Resistance?: a Biochemical Rationale for the Use of -Lactam- -Lactamase Inhibitor CombinationsTebipenem, a New Carbapenem Antibiotic, Is a Slow Substrate That Inhibits the β-Lactamase from Mycobacterium tuberculosisStructures of free and inhibited forms of the L,D-transpeptidase LdtMt1 from Mycobacterium tuberculosisKinetic and Structural Characterization of the Interaction of 6-Methylidene Penem 2 with the β-Lactamase from Mycobacterium tuberculosisThe peptidoglycan of stationary-phase Mycobacterium tuberculosis predominantly contains cross-links generated by L,D-transpeptidationKinetic 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.Rapid cytolysis of Mycobacterium tuberculosis by faropenem, an orally bioavailable β-lactam antibiotic.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.The Mycobacterium tuberculosis protein LdtMt2 is a nonclassical transpeptidase required for virulence and resistance to amoxicillin.Exploring the inhibition of CTX-M-9 by beta-lactamase inhibitors and carbapenems.Strategies for discovering and derisking covalent, irreversible enzyme inhibitors.The chemical biology of new drugs in the development for tuberculosis.Rapid point-of-care detection of the tuberculosis pathogen using a BlaC-specific fluorogenic probeActivity of carbapenems combined with clavulanate against murine tuberculosis.Inactivation kinetics of a new target of beta-lactam antibiotics.Combinatorial active-site variants confer sustained clavulanate resistance in BlaC β-lactamase from Mycobacterium tuberculosis.Impact of β-lactamase inhibition on the activity of ceftaroline against Mycobacterium tuberculosis and Mycobacterium abscessus.Current development and future prospects in chemotherapy of tuberculosisHydrolysis of clavulanate by Mycobacterium tuberculosis β-lactamase BlaC harboring a canonical SDN motif.Mutation landscape of acquired cross-resistance to glycopeptide and β-lactam antibiotics in Enterococcus faeciumMeropenem-clavulanic acid shows activity against Mycobacterium tuberculosis in vivo.Carbapenems and Rifampin Exhibit Synergy against Mycobacterium tuberculosis and Mycobacterium abscessus.Antimicrobial susceptibility testing, drug resistance mechanisms, and therapy of infections with nontuberculous mycobacteria.Inactivation of Mycobacterium tuberculosis l,d-transpeptidase LdtMt₁ by carbapenems and cephalosporinsStructural enzymology using X-ray free electron lasers.Loss of a Functionally and Structurally Distinct ld-Transpeptidase, LdtMt5, Compromises Cell Wall Integrity in Mycobacterium tuberculosis.In Vitro Activity of β-Lactams in Combination with β-Lactamase Inhibitors against Multidrug-Resistant Mycobacterium tuberculosis Isolates.New drugs and regimens for treatment of TB.World Health Organization group 5 drugs for the treatment of drug-resistant tuberculosis: unclear efficacy or untapped potential?
P2860
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P2860
Irreversible inhibition of the Mycobacterium tuberculosis beta-lactamase by clavulanate.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年学术文章
@wuu
2007年学术文章
@zh-cn
2007年学术文章
@zh-hans
2007年学术文章
@zh-my
2007年学术文章
@zh-sg
2007年學術文章
@yue
2007年學術文章
@zh
2007年學術文章
@zh-hant
name
Irreversible inhibition of the Mycobacterium tuberculosis beta-lactamase by clavulanate.
@en
type
label
Irreversible inhibition of the Mycobacterium tuberculosis beta-lactamase by clavulanate.
@en
prefLabel
Irreversible inhibition of the Mycobacterium tuberculosis beta-lactamase by clavulanate.
@en
P2860
P356
P1433
P1476
Irreversible inhibition of the Mycobacterium tuberculosis beta-lactamase by clavulanate.
@en
P2093
Jean-Emmanuel Hugonnet
John S Blanchard
P2860
P304
11998-12004
P356
10.1021/BI701506H
P407
P577
2007-10-04T00:00:00Z