Structure-activity relationships in the inhibition of serine beta-lactamases by phosphonic acid derivatives.

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Structure-activity relationships in the inhibition of serine beta-lactamases by phosphonic acid derivatives.

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http://www.wikidata.org/entity/Q42831747

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1993 nî lūn-bûn

@nan

1993年の論文

@ja

1993年論文

@yue

1993年論文

@zh-hant

1993年論文

@zh-hk

1993年論文

@zh-mo

1993年論文

@zh-tw

1993年论文

@wuu

1993年论文

@zh

1993年论文

@zh-cn

name

Structure-activity relationshi ...... y phosphonic acid derivatives.

@en

Structure-activity relationshi ...... y phosphonic acid derivatives.

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Item

label

Structure-activity relationshi ...... y phosphonic acid derivatives.

@en

Structure-activity relationshi ...... y phosphonic acid derivatives.

@nl

prefLabel

Structure-activity relationshi ...... y phosphonic acid derivatives.

@en

Structure-activity relationshi ...... y phosphonic acid derivatives.

@nl

P1476

Structure-activity relationshi ...... y phosphonic acid derivatives.

@en

P2093

Pratt RF

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Rahil J

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P2860

Inactivation of the RTEM-1 cysteine beta-lactamase by iodoacetate. The nature of active-site functional groups and comparisons with the native enzyme

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

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

Secondary 18O isotope effects as a tool for studying reactions of phosphate mono-, di-, and triesters.

Mechanism of acyl transfer by the class A serine beta-lactamase of Streptomyces albus G.

Inhibition of a class C beta-lactamase by a specific phosphonate monoester.

Kinetics and mechanism of the serine beta-lactamase catalyzed hydrolysis of depsipeptides.

Evidence for an oxyanion hole in serine beta-lactamases and DD-peptidases.

Phosphonate monoester inhibitors of class A beta-lactamases.

Mechanism of inhibition of the class C beta-lactamase of Enterobacter cloacae P99 by phosphonate monoesters.

P304

389-393

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P31

scholarly article

P356

10.1042/BJ2960389

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P407

English

P478

296 ( Pt 2)

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P577

1993-12-01T00:00:00Z

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P5875

14942722

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P698

8257429

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P932

1137708

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