Crystallographic investigation of the inhibition mode of a VIM-2 metallo-beta-lactamase from Pseudomonas aeruginosa by a mercaptocarboxylate inhibitor
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Three decades of beta-lactamase inhibitorsHigh-Resolution Crystal Structure of the Subclass B3 Metallo- -Lactamase BJP-1: Rational Basis for Substrate Specificity and Interaction with SulfonamidesBiochemical and Structural Characterization of the Subclass B1 Metallo- -Lactamase VIM-4Structure of Apo- and Monometalated Forms of NDM-1—A Highly Potent Carbapenem-Hydrolyzing Metallo-β-LactamaseStructural Insights into the Subclass B3 Metallo- -Lactamase SMB-1 and the Mode of Inhibition by the Common Metallo- -Lactamase Inhibitor MercaptoacetateCrystal Structure of the Mobile Metallo- -Lactamase AIM-1 from Pseudomonas aeruginosa: Insights into Antibiotic Binding and the Role of Gln157Solution structures of the Bacillus cereus metallo-β-lactamase BcII and its complex with the broad spectrum inhibitor R -thiomandelic acidStructural and biochemical characterization of VIM-26 shows that Leu224 has implications for the substrate specificity of VIM metallo-β-lactamasesThe three-dimensional structure of VIM-31--a metallo-β-lactamase from Enterobacter cloacae in its native and oxidized formEvolving carbapenemases: can medicinal chemists advance one step ahead of the coming storm?Inhibitors of VIM-2 by screening pharmacologically active and click-chemistry compound librariesMolecular basis of NDM-1, a new antibiotic resistance determinantMutational 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-lactamaseComputational 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 EvolutionBiochemical, 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 dimensionsCrystallization 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 activityStructural 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
description
2007 nî lūn-bûn
@nan
2007 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
name
Crystallographic investigation ...... mercaptocarboxylate inhibitor
@ast
Crystallographic investigation ...... mercaptocarboxylate inhibitor
@en
Crystallographic investigation ...... mercaptocarboxylate inhibitor
@nl
type
label
Crystallographic investigation ...... mercaptocarboxylate inhibitor
@ast
Crystallographic investigation ...... mercaptocarboxylate inhibitor
@en
Crystallographic investigation ...... mercaptocarboxylate inhibitor
@nl
prefLabel
Crystallographic investigation ...... mercaptocarboxylate inhibitor
@ast
Crystallographic investigation ...... mercaptocarboxylate inhibitor
@en
Crystallographic investigation ...... mercaptocarboxylate inhibitor
@nl
P2093
P356
P1476
Crystallographic investigation ...... mercaptocarboxylate inhibitor
@en
P2093
Hiromasa Kurosaki
Jun-ichi Wachino
Kazuyo Matsunaga
Naohiro Shibata
Shinnji Ikemizu
Wanchun Jin
Yoshichika Arakawa
Yoshihiro Yamaguchi
Yuriko Yamagata
P304
P356
10.1021/JM701031N
P407
P577
2007-12-27T00:00:00Z