Crystal structure of NDM-1 reveals a common β-lactam hydrolysis mechanism
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"Stormy waters ahead": global emergence of carbapenemasesResistance to antibiotics targeted to the bacterial cell wallCrystal structure of New Delhi metallo-β-lactamase reveals molecular basis for antibiotic resistanceStructure of Apo- and Monometalated Forms of NDM-1—A Highly Potent Carbapenem-Hydrolyzing Metallo-β-LactamaseStructure of New Delhi metallo-β-lactamase 1 (NDM-1)His224 Alters the R2 Drug Binding Site and Phe218 Influences the Catalytic Efficiency of the Metallo- -Lactamase VIM-7Structural and biochemical characterization of VIM-26 shows that Leu224 has implications for the substrate specificity of VIM metallo-β-lactamasesOvercoming differences: The catalytic mechanism of metallo-β-lactamasesStructural basis for carbapenem-hydrolyzing mechanisms of carbapenemases conferring antibiotic resistanceBiochemical characteristics of New Delhi metallo-β-lactamase-1 show unexpected difference to other MBLsDiscovery of novel new Delhi metallo-β-lactamases-1 inhibitors by multistep virtual screeningNDM-1, the ultimate promiscuous enzyme: substrate recognition and catalytic mechanismSpectroscopic and mechanistic studies of heterodimetallic forms of metallo-β-lactamase NDM-1.Biochemical analysis of metallo-β-lactamase NDM-3 from a multidrug-resistant Escherichia coli strain isolated in Japan.Molecular basis of NDM-1, a new antibiotic resistance determinantMolecular 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.NDM-12, a novel New Delhi metallo-β-lactamase variant from a carbapenem-resistant Escherichia coli clinical isolate in Nepal.Structural Basis of Metallo-β-Lactamase Inhibition by Captopril StereoisomersComparison of Verona Integron-Borne Metallo-β-Lactamase (VIM) Variants Reveals Differences in Stability and Inhibition ProfilesBiochemical, mechanistic, and spectroscopic characterization of metallo-β-lactamase VIM-2.Probing the effect of the non-active-site mutation Y229W in New Delhi metallo-β-lactamase-1 by site-directed mutagenesis, kinetic studies, and molecular dynamics simulations.A novel New Delhi metallo-β-lactamase variant, NDM-14, isolated in a Chinese Hospital possesses increased enzymatic activity against carbapenems.Crystal Structure of DIM-1, an Acquired Subclass B1 Metallo-β-Lactamase from Pseudomonas stutzeri.Identification of a novel NDM variant, NDM-13, from a multidrug-resistant Escherichia coli clinical isolate in NepalOligopeptides as full-length New Delhi metallo-β-lactamase-1 (NDM-1) inhibitors.Exploring the Role of Residue 228 in Substrate and Inhibitor Recognition by VIM Metallo-β-lactamases.Role of Non-Active-Site Residue Trp-93 in the Function and Stability of New Delhi Metallo-β-Lactamase 1.Role of Residues W228 and Y233 in the Structure and Activity of Metallo-β-Lactamase GIM-1.Probing the role of Met221 in the unusual metallo-β-lactamase GOB-18.B1-Metallo-β-Lactamases: Where Do We Stand?NDM-8 metallo-β-lactamase in a multidrug-resistant Escherichia coli strain isolated in NepalInvestigating the position of the hairpin loop in New Delhi metallo-β-lactamase, NDM-1, during catalysis and inhibitor bindingCross-class metallo-β-lactamase inhibition by bisthiazolidines reveals multiple binding modes.New β-phospholactam as a carbapenem transition state analog: Synthesis of a broad-spectrum inhibitor of metallo-β-lactamasesBisthiazolidines: A Substrate-Mimicking Scaffold as an Inhibitor of the NDM-1 Carbapenemase.Metallo-β-lactamase structure and function.Targeting metallo-β-lactamase enzymes in antibiotic resistance.Fragment-based inhibitor discovery against β-lactamaseA variety of roles for versatile zinc in metallo-β-lactamases.
P2860
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P2860
Crystal structure of NDM-1 reveals a common β-lactam hydrolysis mechanism
description
2011 nî lūn-bûn
@nan
2011 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Crystal structure of NDM-1 reveals a common β-lactam hydrolysis mechanism
@ast
Crystal structure of NDM-1 reveals a common β-lactam hydrolysis mechanism
@en
Crystal structure of NDM-1 reveals a common β-lactam hydrolysis mechanism
@nl
type
label
Crystal structure of NDM-1 reveals a common β-lactam hydrolysis mechanism
@ast
Crystal structure of NDM-1 reveals a common β-lactam hydrolysis mechanism
@en
Crystal structure of NDM-1 reveals a common β-lactam hydrolysis mechanism
@nl
prefLabel
Crystal structure of NDM-1 reveals a common β-lactam hydrolysis mechanism
@ast
Crystal structure of NDM-1 reveals a common β-lactam hydrolysis mechanism
@en
Crystal structure of NDM-1 reveals a common β-lactam hydrolysis mechanism
@nl
P356
P1433
P1476
Crystal structure of NDM-1 reveals a common β-lactam hydrolysis mechanism
@en
P2093
HongMin Zhang
P304
P356
10.1096/FJ.11-184036
P407
P577
2011-08-01T00:00:00Z