Crystallographic investigation of the inhibition mode of a VIM-2 metallo-beta-lactamase from Pseudomonas aeruginosa by a mercaptocarboxylate inhibitor - Wikidata - awgldk - TriplyDB

Crystallographic investigation of the inhibition mode of a VIM-2 metallo-beta-lactamase from Pseudomonas aeruginosa by a mercaptocarboxylate inhibitor

Crystallographic investigation of the inhibition mode of a VIM-2 metallo-beta-lactamase from Pseudomonas aeruginosa by a mercaptocarboxylate inhibitor

http://www.wikidata.org/entity/Q27649184

about

Three decades of beta-lactamase inhibitors High-Resolution Crystal Structure of the Subclass B3 Metallo- -Lactamase BJP-1: Rational Basis for Substrate Specificity and Interaction with Sulfonamides Biochemical and Structural Characterization of the Subclass B1 Metallo- -Lactamase VIM-4 Structure of Apo- and Monometalated Forms of NDM-1—A Highly Potent Carbapenem-Hydrolyzing Metallo-β-Lactamase Structural Insights into the Subclass B3 Metallo- -Lactamase SMB-1 and the Mode of Inhibition by the Common Metallo- -Lactamase Inhibitor Mercaptoacetate Crystal Structure of the Mobile Metallo- -Lactamase AIM-1 from Pseudomonas aeruginosa: Insights into Antibiotic Binding and the Role of Gln157 Solution structures of the Bacillus cereus metallo-β-lactamase BcII and its complex with the broad spectrum inhibitor R -thiomandelic acid 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 Evolving carbapenemases: can medicinal chemists advance one step ahead of the coming storm?Inhibitors of VIM-2 by screening pharmacologically active and click-chemistry compound libraries Molecular basis of NDM-1, a new antibiotic resistance determinant Mutational analysis of VIM-2 reveals an essential determinant for metallo-beta-lactamase stability and folding.Molecular mechanisms of substrate recognition and specificity of New Delhi metallo-β-lactamase 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 Biochemical, mechanistic, and spectroscopic characterization of metallo-β-lactamase VIM-2.Crystal Structure of DIM-1, an Acquired Subclass B1 Metallo-β-Lactamase from Pseudomonas stutzeri.Crystallization and preliminary X-ray analysis of the subclass B3 metallo-β-lactamase SMB-1 that confers carbapenem resistance.Elucidating the Role of Residue 67 in IMP-Type Metallo-β-Lactamase Evolution.Carbapenemases in Klebsiella pneumoniae and other Enterobacteriaceae: an evolving crisis of global dimensions Crystallization and preliminary diffraction studies of GIM-1, a class B carbapenem-hydrolyzing β-lactamase.Exploring the Role of Residue 228 in Substrate and Inhibitor Recognition by VIM Metallo-β-lactamases.Role of Residues W228 and Y233 in the Structure and Activity of Metallo-β-Lactamase GIM-1.Structural Insights into Recognition of Hydrolyzed Carbapenems and Inhibitors by Subclass B3 Metallo-β-Lactamase SMB-1.Metallo-β-lactamase structure and function.An Update on the Status of Potent Inhibitors of Metallo-β-Lactamases.Targeting metallo-β-lactamase enzymes in antibiotic resistance.Thiol-Containing Metallo-β-Lactamase Inhibitors Resensitize Resistant Gram-Negative Bacteria to Meropenem.Structural Insights into TMB-1 and the Role of Residues 119 and 228 in Substrate and Inhibitor Binding.The structure of the metallo-β-lactamase VIM-2 in complex with a triazolylthioacetamide inhibitor.Systematic analysis of metallo-β-lactamases using an automated database.A potential substrate binding conformation of β-lactams and insight into the broad spectrum of NDM-1 activity Structural studies on New Delhi Metallo-β-lactamase (NDM-2) suggest old β-lactam, penicillin to be better antibiotic for NDM-2-harbouring Acinetobacter baumanni.Structural and Kinetic Studies of the Potent Inhibition of Metallo-β-lactamases by 6-Phosphonomethylpyridine-2-carboxylates.Targeting clinically-relevant metallo-β-lactamases: from high-throughput docking to broad-spectrum inhibitors.Automatic phylogenetic classification of bacterial beta-lactamase sequences including structural and antibiotic substrate preference information.Binding site residues in β-lactamases: role in non-classical interactions and metal binding

P2860

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P2860

Crystallographic investigation of the inhibition mode of a VIM-2 metallo-beta-lactamase from Pseudomonas aeruginosa by a mercaptocarboxylate inhibitor

http://www.wikidata.org/entity/Q27649184

description

2007 nî lūn-bûn

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2007 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

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2007 թվականի դեկտեմբերին հրատարակված գիտական հոդված

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2007年の論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年论文

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name

Crystallographic investigation ...... mercaptocarboxylate inhibitor

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Crystallographic investigation ...... mercaptocarboxylate inhibitor

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Crystallographic investigation ...... mercaptocarboxylate inhibitor

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Crystallographic investigation ...... mercaptocarboxylate inhibitor

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Crystallographic investigation ...... mercaptocarboxylate inhibitor

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Crystallographic investigation ...... mercaptocarboxylate inhibitor

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Crystallographic investigation ...... mercaptocarboxylate inhibitor

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Crystallographic investigation ...... mercaptocarboxylate inhibitor

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Crystallographic investigation ...... mercaptocarboxylate inhibitor

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Journal of Medicinal Chemistry

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Crystallographic investigation ...... mercaptocarboxylate inhibitor

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Hiromasa Kurosaki

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Jun-ichi Wachino

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Kazuyo Matsunaga

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Naohiro Shibata

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Shinnji Ikemizu

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Wanchun Jin

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Yoshichika Arakawa

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Yoshihiro Yamaguchi

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Yuriko Yamagata

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6647-53

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scholarly article

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10.1021/JM701031N

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26

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50

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2007-12-27T00:00:00Z

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18052313

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Pseudomonas aeruginosa