Structural analysis of the Asn152Gly mutant of P99 cephalosporinase - Wikidata - awgldk - TriplyDB

Structural analysis of the Asn152Gly mutant of P99 cephalosporinase

Structural analysis of the Asn152Gly mutant of P99 cephalosporinase

http://www.wikidata.org/entity/Q27682153

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Effect of asparagine substitutions in the YXN loop of a class C β-lactamase of Acinetobacter baumannii on substrate and inhibitor kinetics.Structure-based approach for identification of novel phenylboronic acids as serine-β-lactamase inhibitors.N152G, -S, and -T substitutions in CMY-2 β-lactamase increase catalytic efficiency for cefoxitin and inactivation rates for tazobactam.

P2860

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P2860

Structural analysis of the Asn152Gly mutant of P99 cephalosporinase

http://www.wikidata.org/entity/Q27682153

description

2012 nî lūn-bûn

@nan

2012 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2012 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2012年の論文

@ja

2012年論文

@yue

2012年論文

@zh-hant

2012年論文

@zh-hk

2012年論文

@zh-mo

2012年論文

@zh-tw

2012年论文

@wuu

name

Structural analysis of the Asn152Gly mutant of P99 cephalosporinase

@ast

Structural analysis of the Asn152Gly mutant of P99 cephalosporinase

@en

Structural analysis of the Asn152Gly mutant of P99 cephalosporinase

@nl

type

label

Structural analysis of the Asn152Gly mutant of P99 cephalosporinase

@ast

Structural analysis of the Asn152Gly mutant of P99 cephalosporinase

@en

Structural analysis of the Asn152Gly mutant of P99 cephalosporinase

@nl

prefLabel

Structural analysis of the Asn152Gly mutant of P99 cephalosporinase

@ast

Structural analysis of the Asn152Gly mutant of P99 cephalosporinase

@en

Structural analysis of the Asn152Gly mutant of P99 cephalosporinase

@nl

P1433

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P2860

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P433

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P577

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P698

Q27682153-995D64C6-04C9-4403-A2E3-B1C5C77259D3

P356

S0907444912024080

P1433

Acta Crystallographica Section D: Biological Crystallography

P1476

Structural analysis of the Asn152Gly mutant of P99 cephalosporinase

@en

P2093

James F Ruble

http://www.w3.org/2001/XMLSchema#string

Rachel A Powers

http://www.w3.org/2001/XMLSchema#string

Scott T Lefurgy

http://www.w3.org/2001/XMLSchema#string

Virginia W Cornish

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P2860

MolProbity: all-atom structure validation for macromolecular crystallography

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

Processing of X-ray diffraction data collected in oscillation mode

Structure of the extended-spectrum class C beta-lactamase of Enterobacter cloacae GC1, a natural mutant with a tandem tripeptide insertion

Structures of ceftazidime and its transition-state analogue in complex with AmpC beta-lactamase: implications for resistance mutations and inhibitor design

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

Hydrolysis of third-generation cephalosporins by class C beta-lactamases. Structures of a transition state analog of cefotoxamine in wild-type and extended spectrum enzymes

Structure of AmpC β-lactamase (AmpCD) from anEscherichia coliclinical isolate with a tripeptide deletion (Gly286-Ser287-Asp288) in the H10 helix

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

P304

1189-93

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P31

scholarly article

P356

10.1107/S0907444912024080

http://www.w3.org/2001/XMLSchema#string

P433

Pt 9

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P478

68

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P577

2012-09-01T00:00:00Z

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P698

22948919

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