Crystal structure and activity studies of the Mycobacterium tuberculosis beta-lactamase reveal its critical role in resistance to beta-lactam antibiotics - Test2 - elhamkhani - TriplyDB

Crystal structure and activity studies of the Mycobacterium tuberculosis beta-lactamase reveal its critical role in resistance to beta-lactam antibiotics

Crystal structure and activity studies of the Mycobacterium tuberculosis beta-lactamase reveal its critical role in resistance to beta-lactam antibiotics

http://www.wikidata.org/entity/Q28487411

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Optical imaging of bacterial infections Rising to the challenge: new therapies for tuberculosis Meropenem-Clavulanate Is Effective Against Extensively Drug-Resistant Mycobacterium tuberculosis Directed evolution of Mycobacterium tuberculosis β-lactamase reveals gatekeeper residue that regulates antibiotic resistance and catalytic efficiency Can Inhibitor-Resistant Substitutions in the Mycobacterium tuberculosis -Lactamase BlaC Lead to Clavulanate Resistance?: a Biochemical Rationale for the Use of -Lactam- -Lactamase Inhibitor Combinations Structural basis for carbapenem-hydrolyzing mechanisms of carbapenemases conferring antibiotic resistance Kinetic and Structural Characterization of the Interaction of 6-Methylidene Penem 2 with the β-Lactamase from Mycobacterium tuberculosis Morphological features and signature gene response elicited by inactivation of FtsI in Mycobacterium tuberculosis Saturation mutagenesis of Asn152 reveals a substrate selectivity switch in P99 cephalosporinase New Insights in to the Intrinsic and Acquired Drug Resistance Mechanisms in Mycobacteria Imaging tuberculosis with endogenous beta-lactamase reporter enzyme fluorescence in live mice.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 probe Bacterial growth and cell division: a mycobacterial perspective.Reporter enzyme fluorescence (REF) imaging and quantification of tuberculosis in live animals Combinatorial active-site variants confer sustained clavulanate resistance in BlaC β-lactamase from Mycobacterium tuberculosis.Fluorogenic probes with substitutions at the 2 and 7 positions of cephalosporin are highly BlaC-specific for rapid Mycobacterium tuberculosis detection.Combinations of β-Lactam Antibiotics Currently in Clinical Trials Are Efficacious in a DHP-I-Deficient Mouse Model of Tuberculosis Infection Hydrolysis of clavulanate by Mycobacterium tuberculosis β-lactamase BlaC harboring a canonical SDN motif.Meropenem-clavulanic acid shows activity against Mycobacterium tuberculosis in vivo.Structural enzymology using X-ray free electron lasers.A Structure-Based Classification of Class A β-Lactamases, a Broadly Diverse Family of Enzymes.Mutagenesis in the alpha3alpha4 GyrA helix and in the Toprim domain of GyrB refines the contribution of Mycobacterium tuberculosis DNA gyrase to intrinsic resistance to quinolones.World Health Organization group 5 drugs for the treatment of drug-resistant tuberculosis: unclear efficacy or untapped potential?Synthesis, pH-dependent, and plasma stability of meropenem prodrugs for potential use against drug-resistant tuberculosis Kinetic characterization of hydrolysis of nitrocefin, cefoxitin, and meropenem by β-lactamase from Mycobacterium tuberculosis.Paradoxical Hypersusceptibility of Drug-resistant Mycobacteriumtuberculosis to β-lactam Antibiotics.High tolerance to simultaneous active-site mutations in TEM-1 beta-lactamase: Distinct mutational paths provide more generalized beta-lactam recognition In vitro cross-linking of Mycobacterium tuberculosis peptidoglycan by L,D-transpeptidases and inactivation of these enzymes by carbapenems.Role of glycans and glycoproteins in disease development by Mycobacterium tuberculosis.Reappraising the use of β-lactams to treat tuberculosis.Molecular biology of drug resistance in Mycobacterium tuberculosis Antibiotic resistance mechanisms in M. tuberculosis: an update.β-Lactamase inhibition by avibactam in Mycobacterium abscessus.Antimicrobial resistance in Mycobacterium tuberculosis: mechanistic and evolutionary perspectives.Involvement of efflux pumps in the resistance to peptidoglycan synthesis inhibitors in Mycobacterium tuberculosis Ceftazidime-avibactam has potent sterilizing activity against highly drug-resistant tuberculosis.In vitro and in vivo activity of biapenem against drug-susceptible and rifampicin-resistant Mycobacterium tuberculosis.Recognizing drug targets using evolutionary information: implications for repurposing FDA-approved drugs against Mycobacterium tuberculosis H37Rv.New directions using reporter enzyme fluorescence (REF) as a tuberculosis diagnostic platform.

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Crystal structure and activity studies of the Mycobacterium tuberculosis beta-lactamase reveal its critical role in resistance to beta-lactam antibiotics

http://www.wikidata.org/entity/Q28487411

description

2006 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

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2006 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

artículu científicu espublizáu en 2006

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im August 2006 veröffentlichter wissenschaftlicher Artikel

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scientific journal article

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vedecký článok (publikovaný 2006/08/01)

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vědecký článek publikovaný v roce 2006

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wetenschappelijk artikel (gepubliceerd op 2006/08/01)

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наукова стаття, опублікована в серпні 2006

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مقالة علمية (نشرت في أغسطس 2006)

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name

Crystal structure and activity ...... nce to beta-lactam antibiotics

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Crystal structure and activity ...... nce to beta-lactam antibiotics

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Crystal structure and activity ...... nce to beta-lactam antibiotics

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type

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Crystal structure and activity ...... nce to beta-lactam antibiotics

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Crystal structure and activity ...... nce to beta-lactam antibiotics

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Crystal structure and activity ...... nce to beta-lactam antibiotics

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Crystal structure and activity ...... nce to beta-lactam antibiotics

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Crystal structure and activity ...... nce to beta-lactam antibiotics

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Crystal structure and activity ...... nce to beta-lactam antibiotics

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Antimicrobial Agents and Chemotherapy

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Crystal structure and activity ...... nce to beta-lactam antibiotics

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Craig Cassidy

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James C. Sacchettini

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P2860

A functional classification scheme for beta-lactamases and its correlation with molecular structure

Insights into the molecular basis for the carbenicillinase activity of PSE-4 beta-lactamase from crystallographic and kinetic studies

Inhibition of the SHV-1 beta-lactamase by sulfones: crystallographic observation of two reaction intermediates with tazobactam

Crystal structures of the Bacillus licheniformis BS3 class A beta-lactamase and of the acyl-enzyme adduct formed with cefoxitin

Structure of an extended-spectrum class A beta-lactamase from Proteus vulgaris K1

An ultrahigh resolution structure of TEM-1 beta-lactamase suggests a role for Glu166 as the general base in acylation

Acyl-intermediate structures of the extended-spectrum class A beta-lactamase, Toho-1, in complex with cefotaxime, cephalothin, and benzylpenicillin

Ultrahigh resolution structure of a class A beta-lactamase: on the mechanism and specificity of the extended-spectrum SHV-2 enzyme

Crystal structure of extended-spectrum beta-lactamase Toho-1: insights into the molecular mechanism for catalytic reaction and substrate specificity expansion

Molecular structure of the acyl-enzyme intermediate in beta-lactam hydrolysis at 1.7 A resolution

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10.1128/AAC.00320-06

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Akafuba bulwadde

Mycobacterium tuberculosis

antibiotic resistance

crystal structure

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1538687

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