NDM-1, the ultimate promiscuous enzyme: substrate recognition and catalytic mechanism
about
Solution structures of the Bacillus cereus metallo-β-lactamase BcII and its complex with the broad spectrum inhibitor R -thiomandelic acidDiscovery of novel new Delhi metallo-β-lactamases-1 inhibitors by multistep virtual screeningA case study comparing quantitative stability-flexibility relationships across five metallo-β-lactamases highlighting differences within NDM-1.Evolution of Metallo-β-lactamases: Trends Revealed by Natural Diversity and in vitro EvolutionMetal limitation and toxicity at the interface between host and pathogenProbing 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.Crystal Structure of DIM-1, an Acquired Subclass B1 Metallo-β-Lactamase from Pseudomonas stutzeri.Role of Non-Active-Site Residue Trp-93 in the Function and Stability of New Delhi Metallo-β-Lactamase 1.B1-Metallo-β-Lactamases: Where Do We Stand?Investigating the position of the hairpin loop in New Delhi metallo-β-lactamase, NDM-1, during catalysis and inhibitor bindingManaging transmission of carbapenem-resistant enterobacteriaceae in healthcare settings: a view from the trenches.A variety of roles for versatile zinc in metallo-β-lactamases.New Delhi metallo-β-lactamase-1: structure, inhibitors and detection of producers.Zinc Homeostasis at the Bacteria/Host Interface-From Coordination Chemistry to Nutritional Immunity.Carbapenem-resistant Enterobacteriaceae in the community: a scoping review.Kinetic Study of Laboratory Mutants of NDM-1 Metallo-β-Lactamase and the Importance of an Isoleucine at Position 35.The Role of Active Site Flexible Loops in Catalysis and of Zinc in Conformational Stability of Bacillus cereus 569/H/9 β-Lactamase.A general reaction mechanism for carbapenem hydrolysis by mononuclear and binuclear metallo-β-lactamases.Conserved residues of the Pro103-Arg115 loop are involved in triggering the allosteric response of the Escherichia coli ADP-glucose pyrophosphorylase.Monitoring conformational changes in the NDM-1 metallo-β-lactamase by 19F NMR spectroscopy.Covalent inhibition of New Delhi metallo-β-lactamase-1 (NDM-1) by cefaclor.Evaluation of different pretreatment protocols to detect accurately clinical carbapenemase-producing Enterobacteriaceae by MALDI-TOF.The mechanism of NDM-1-catalyzed carbapenem hydrolysis is distinct from that of penicillin or cephalosporin hydrolysis.Structural and functional insight of New Delhi Metallo β-lactamase-1 variants.Active Site Crowding of Cytochrome P450 3A4 as a Strategy To Alter Its Selectivity.Zinc ion-induced conformational changes in new Delphi metallo-β-lactamase 1 probed by molecular dynamics simulations and umbrella sampling.Hydrolysis of cephalexin and meropenem by New Delhi metallo-β-lactamase: the substrate protonation mechanism is drug dependent.
P2860
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P2860
NDM-1, the ultimate promiscuous enzyme: substrate recognition and catalytic mechanism
description
2013 nî lūn-bûn
@nan
2013 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
name
NDM-1, the ultimate promiscuous enzyme: substrate recognition and catalytic mechanism
@ast
NDM-1, the ultimate promiscuous enzyme: substrate recognition and catalytic mechanism
@en
type
label
NDM-1, the ultimate promiscuous enzyme: substrate recognition and catalytic mechanism
@ast
NDM-1, the ultimate promiscuous enzyme: substrate recognition and catalytic mechanism
@en
prefLabel
NDM-1, the ultimate promiscuous enzyme: substrate recognition and catalytic mechanism
@ast
NDM-1, the ultimate promiscuous enzyme: substrate recognition and catalytic mechanism
@en
P2093
P2860
P356
P1433
P1476
NDM-1, the ultimate promiscuous enzyme: substrate recognition and catalytic mechanism
@en
P2093
Christine Tesar
James Sacchettini
Joseph Mire
Mark A Cunningham
Youngchang Kim
P2860
P304
P356
10.1096/FJ.12-224014
P407
P577
2013-01-30T00:00:00Z