Structural basis for imipenem inhibition of class C beta-lactamases. - Wikidata - awgldk - TriplyDB

Structural basis for imipenem inhibition of class C beta-lactamases.

Structural basis for imipenem inhibition of class C beta-lactamases.

http://www.wikidata.org/entity/Q27639969

about

Carbapenems: past, present, and future Three decades of beta-lactamase inhibitors Inhibition of Class A β-Lactamases by Carbapenems: Crystallographic Observation of Two Conformations of Meropenem in SHV-1 The 1.4 Å Crystal Structure of the Class D β-Lactamase OXA-1 Complexed with Doripenem Biochemical and Structural Characterization of Mycobacterium tuberculosis β-Lactamase with the Carbapenems Ertapenem and Doripenem Crystal Structures of Covalent Complexes of β-Lactam Antibiotics with Escherichia coli Penicillin-Binding Protein 5: Toward an Understanding of Antibiotic Specificity Structures 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,Structures of the Class D Carbapenemase OXA-24 from Acinetobacter baumannii in Complex with Doripenem Structural Insight into Potent Broad-Spectrum Inhibition with Reversible Recyclization Mechanism: Avibactam in Complex with CTX-M-15 and Pseudomonas aeruginosa AmpC -Lactamases Structure of the extended-spectrum class C β-lactamase ADC-1 fromAcinetobacter baumannii Structure of ADC-68, a novel carbapenem-hydrolyzing class C extended-spectrum β-lactamase isolated from Acinetobacter baumannii Understanding the structural mechanisms of antibiotic resistance sets the platform for new discovery Trapping and characterization of a reaction intermediate in carbapenem hydrolysis by B. cereus metallo-beta-lactamase.Inhibition of the class C beta-lactamase from Acinetobacter spp.: insights into effective inhibitor design.Identification of a new allelic variant of the Acinetobacter baumannii cephalosporinase, ADC-7 beta-lactamase: defining a unique family of class C enzymes Substrate selectivity and a novel role in inhibitor discrimination by residue 237 in the KPC-2 beta-lactamase.Active site detection by spatial conformity and electrostatic analysis--unravelling a proteolytic function in shrimp alkaline phosphatase.A fluorescent carbapenem for structure function studies of penicillin-binding proteins, β-lactamases, and β-lactam sensors.Structural basis for the extended substrate spectrum of CMY-10, a plasmid-encoded class C beta-lactamase.Exploring sequence requirements for C₃/C₄ carboxylate recognition in the Pseudomonas aeruginosa cephalosporinase: Insights into plasticity of the AmpC β-lactamase.ClbP is a prototype of a peptidase subgroup involved in biosynthesis of nonribosomal peptides.Classification of Beta-lactamases and penicillin binding proteins using ligand-centric network models.Site-saturation mutagenesis of position V117 in OXA-1 β-lactamase: effect of side chain polarity on enzyme carboxylation and substrate turnover.Global dissemination of beta-lactamases mediating resistance to cephalosporins and carbapenems.Class D β-lactamases do exist in Gram-positive bacteria.Comparative Phosphoproteomics Reveals the Role of AmpC β-lactamase Phosphorylation in the Clinical Imipenem-resistant Strain Acinetobacter baumannii SK17.Extended-spectrum cephalosporinases: structure, detection and epidemiology.Antibiotic trapping by plasmid-encoded CMY-2 β-lactamase combined with reduced outer membrane permeability as a mechanism of carbapenem resistance in Escherichia coli.A kinetic analysis of the inhibition of FOX-4 β-lactamase, a plasmid-mediated AmpC cephalosporinase, by monocyclic β-lactams and carbapenems Engineering the synthetic potential of β-lactam synthetase and the importance of catalytic loop dynamics.Selection and molecular characterization of ceftazidime/avibactam-resistant mutants in Pseudomonas aeruginosa strains containing derepressed AmpC.Phenotypic and biochemical comparison of the carbapenem-hydrolyzing activities of five plasmid-borne AmpC β-lactamases.The mechanism of NDM-1-catalyzed carbapenem hydrolysis is distinct from that of penicillin or cephalosporin hydrolysis.Modified Penicillin Molecule with Carbapenem-Like Stereochemistry Specifically Inhibits Class C β-Lactamases.Automatic phylogenetic classification of bacterial beta-lactamase sequences including structural and antibiotic substrate preference information.

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P2860

Structural basis for imipenem inhibition of class C beta-lactamases.

http://www.wikidata.org/entity/Q27639969

description

2002 nî lūn-bûn

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2002 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

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2002 թվականի դեկտեմբերին հրատարակված գիտական հոդված

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2002年の論文

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2002年論文

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2002年論文

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2002年論文

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2002年論文

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2002年論文

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2002年论文

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name

Structural Basis for Imipenem Inhibition of Class C -Lactamases

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Structural basis for imipenem inhibition of class C beta-lactamases.

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Structural basis for imipenem inhibition of class C beta-lactamases.

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type

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Structural Basis for Imipenem Inhibition of Class C -Lactamases

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Structural basis for imipenem inhibition of class C beta-lactamases.

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Structural basis for imipenem inhibition of class C beta-lactamases.

@en

prefLabel

Structural Basis for Imipenem Inhibition of Class C -Lactamases

@nl

Structural basis for imipenem inhibition of class C beta-lactamases.

@ast

Structural basis for imipenem inhibition of class C beta-lactamases.

@en

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AAC.46.12.3978-3980.2002

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Antimicrobial Agents and Chemotherapy

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Structural basis for imipenem inhibition of class C beta-lactamases.

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Beth M Beadle

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Brian K Shoichet

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P2860

Improved methods for building protein models in electron density maps and the location of errors in these models

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Inhibition of class C beta-lactamases: structure of a reaction intermediate with a cephem sulfone

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

Noncovalent interaction energies in covalent complexes: TEM-1 beta-lactamase and beta-lactams

Structure-based approach for binding site identification on AmpC beta-lactamase

Refined crystal structure of beta-lactamase from Citrobacter freundii indicates a mechanism for beta-lactam hydrolysis

Crystallographic structure of a phosphonate derivative of the Enterobacter cloacae P99 cephalosporinase: mechanistic interpretation of a beta-lactamase transition-state analog

Three-dimensional structure of AmpC beta-lactamase from Escherichia coli bound to a transition-state analogue: possible implications for the oxyanion hypothesis and for inhibitor design

SETOR: hardware-lighted three-dimensional solid model representations of macromolecules

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3978-3980

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scholarly article

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10.1128/AAC.46.12.3978-3980.2002

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