Update of the standard numbering scheme for class B beta-lactamases. - Wikidata - wikimedia - TriplyDB

Update of the standard numbering scheme for class B beta-lactamases.

Update of the standard numbering scheme for class B beta-lactamases.

http://www.wikidata.org/entity/Q40968300

about

Updated functional classification of beta-lactamases Three decades of beta-lactamase inhibitors Carbapenemases: the versatile beta-lactamases New Perspectives on the Use of Phytochemicals as an Emergent Strategy to Control Bacterial Infections Including Biofilms The Structure of the Dizinc Subclass B2 Metallo- -Lactamase CphA Reveals that the Second Inhibitory Zinc Ion Binds in the Histidine Site High-Resolution Crystal Structure of the Subclass B3 Metallo- -Lactamase BJP-1: Rational Basis for Substrate Specificity and Interaction with Sulfonamides Structural Insights into the Subclass B3 Metallo- -Lactamase SMB-1 and the Mode of Inhibition by the Common Metallo- -Lactamase Inhibitor Mercaptoacetate Crystal Structures of Pseudomonas aeruginosa GIM-1: Active-Site Plasticity in Metallo- -Lactamases Structure of New Delhi metallo-β-lactamase 1 (NDM-1)Crystal Structure of the Mobile Metallo- -Lactamase AIM-1 from Pseudomonas aeruginosa: Insights into Antibiotic Binding and the Role of Gln157 His224 Alters the R2 Drug Binding Site and Phe218 Influences the Catalytic Efficiency of the Metallo- -Lactamase VIM-7 Structural and biochemical characterization of VIM-26 shows that Leu224 has implications for the substrate specificity of VIM metallo-β-lactamases The three-dimensional structure of VIM-31--a metallo-β-lactamase from Enterobacter cloacae in its native and oxidized form Use of ferrous iron by metallo-β-lactamases Overcoming differences: The catalytic mechanism of metallo-β-lactamases Structural basis for carbapenem-hydrolyzing mechanisms of carbapenemases conferring antibiotic resistance Biapenem inactivation by B2 metallo β-lactamases: energy landscape of the post-hydrolysis reactions Evolving carbapenemases: can medicinal chemists advance one step ahead of the coming storm?Structure-based phylogeny of the metallo-beta-lactamases Complete genome sequence of a clinical Bordetella pertussis isolate from Brazil.VIM-19, a metallo-beta-lactamase with increased carbapenemase activity from Escherichia coli and Klebsiella pneumoniae.Metallo-beta-lactamases: the quiet before the storm?Molecular mechanisms of substrate recognition and specificity of New Delhi metallo-β-lactamase Novel acquired metallo-beta-lactamase gene, bla(SIM-1), in a class 1 integron from Acinetobacter baumannii clinical isolates from Korea Computational analysis of pathogen-borne metallo β-lactamases reveals discriminating structural features between B1 types.Evolution of Metallo-β-lactamases: Trends Revealed by Natural Diversity and in vitro Evolution A standard numbering scheme for thiamine diphosphate-dependent decarboxylases.Metallo-beta-lactamase production by Pseudomonas otitidis: a species-related trait.Structural Basis of Metallo-β-Lactamase Inhibition by Captopril Stereoisomers Comparison of Verona Integron-Borne Metallo-β-Lactamase (VIM) Variants Reveals Differences in Stability and Inhibition Profiles Biapenem inactivation by B2 metallo β-lactamases: energy landscape of the hydrolysis reaction.Characterization of metallo-beta-lactamase VIM-27, an A57S mutant of VIM-1 associated with Klebsiella pneumoniae ST147.Host-specific enzyme-substrate interactions in SPM-1 metallo-β-lactamase are modulated by second sphere residues.Protein variants form a system of networks: microdiversity of IMP metallo-beta-lactamases.SMB-1, a novel subclass B3 metallo-beta-lactamase, associated with ISCR1 and a class 1 integron, from a carbapenem-resistant Serratia marcescens clinical isolate Azolylthioacetamide: A Highly Promising Scaffold for the Development of Metallo-β-lactamase Inhibitors.Meropenem and chromacef intermediates observed in IMP-25 metallo-β-lactamase-catalyzed hydrolysis.Crystallization and preliminary X-ray analysis of the subclass B3 metallo-β-lactamase SMB-1 that confers carbapenem resistance.Expression, purification, crystallization and preliminary X-ray analysis of Aeromonas hydrophilia metallo-beta-lactamase Detection and characterization of VIM-31, a new variant of VIM-2 with Tyr224His and His252Arg mutations, in a clinical isolate of Enterobacter cloacae.

P2860

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P2860

Update of the standard numbering scheme for class B beta-lactamases.

http://www.wikidata.org/entity/Q40968300

description

2004 nî lūn-bûn

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2004年の論文

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2004年論文

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2004年論文

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2004年論文

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2004年論文

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2004年論文

@zh-tw

2004年论文

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2004年论文

@zh

2004年论文

@zh-cn

name

Update of the standard numbering scheme for class B beta-lactamases.

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type

label

Update of the standard numbering scheme for class B beta-lactamases.

@en

prefLabel

Update of the standard numbering scheme for class B beta-lactamases.

@en

P1433

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P356

AAC.48.7.2347-2349.2004

P1433

Antimicrobial Agents and Chemotherapy

P1476

Update of the standard numbering scheme for class B beta-lactamases.

@en

P2093

Carine Bebrone

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Christine Anne

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Gianpiero Garau

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Isabel García-Sáez

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

Jean-Marie Frère

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Moreno Galleni

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Paola Mercuri

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

P2860

The 3-D structure of a zinc metallo-beta-lactamase from Bacillus cereus reveals a new type of protein fold

Crystal structure of human glyoxalase II and its complex with a glutathione thiolester substrate analogue

Crystal structure of the IMP-1 metallo beta-lactamase from Pseudomonas aeruginosa and its complex with a mercaptocarboxylate inhibitor: binding determinants of a potent, broad-spectrum inhibitor

Structure of a dioxygen reduction enzyme from Desulfovibrio gigas

Three-dimensional structure of FEZ-1, a monomeric subclass B3 metallo-beta-lactamase from Fluoribacter gormanii, in native form and in complex with D-captopril

The 1.5-A structure of Chryseobacterium meningosepticum zinc beta-lactamase in complex with the inhibitor, D-captopril

Crystal structure of the wide-spectrum binuclear zinc beta-lactamase from Bacteroides fragilis

Crystal structure of the zinc-dependent beta-lactamase from Bacillus cereus at 1.9 A resolution: binuclear active site with features of a mononuclear enzyme

X-ray structure of the ZnII beta-lactamase from Bacteroides fragilis in an orthorhombic crystal form

1.85 A resolution structure of the zinc (II) beta-lactamase from Bacillus cereus

P304

2347-2349

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scholarly article

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10.1128/AAC.48.7.2347-2349.2004

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P433

7

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48

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P577

2004-07-01T00:00:00Z

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15215079

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P932

434215

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