The three-dimensional structure of VIM-2, a Zn-beta-lactamase from Pseudomonas aeruginosa in its reduced and oxidised form
about
Characterization of a new metallo-beta-lactamase gene, bla(NDM-1), and a novel erythromycin esterase gene carried on a unique genetic structure in Klebsiella pneumoniae sequence type 14 from IndiaResistance to antibiotics targeted to the bacterial cell wallThe Structure of the Dizinc Subclass B2 Metallo- -Lactamase CphA Reveals that the Second Inhibitory Zinc Ion Binds in the Histidine SiteA structural view of the antibiotic degradation enzyme NDM-1 from a superbugBiochemical and Structural Characterization of the Subclass B1 Metallo- -Lactamase VIM-4Crystal 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-LactamaseCrystal Structures of Pseudomonas aeruginosa GIM-1: Active-Site Plasticity in Metallo- -LactamasesStructure 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-lactamasesThe three-dimensional structure of VIM-31--a metallo-β-lactamase from Enterobacter cloacae in its native and oxidized formUse of ferrous iron by metallo-β-lactamasesOvercoming differences: The catalytic mechanism of metallo-β-lactamasesStructural basis for carbapenem-hydrolyzing mechanisms of carbapenemases conferring antibiotic resistanceInsights from modeling the 3D structure of New Delhi metallo-β-lactamse and its binding interactions with antibiotic drugsBiochemical characteristics of New Delhi metallo-β-lactamase-1 show unexpected difference to other MBLsEvolving carbapenemases: can medicinal chemists advance one step ahead of the coming storm?Inhibitors of VIM-2 by screening pharmacologically active and click-chemistry compound librariesNovel VIM metallo-beta-lactamase variant from clinical isolates of Enterobacteriaceae from AlgeriaVIM-19, a metallo-beta-lactamase with increased carbapenemase activity from Escherichia coli and Klebsiella pneumoniae.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-lactamaseEvolution of Metallo-β-lactamases: Trends Revealed by Natural Diversity and in vitro EvolutionStructural 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.Crystal Structure of DIM-1, an Acquired Subclass B1 Metallo-β-Lactamase from Pseudomonas stutzeri.Differential binding of Co(II) and Zn(II) to metallo-beta-lactamase Bla2 from Bacillus anthracis.Detection and characterization of VIM-31, a new variant of VIM-2 with Tyr224His and His252Arg mutations, in a clinical isolate of Enterobacter cloacae.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.Biochemical characterization of metallo-beta-lactamase VIM-11 from a Pseudomonas aeruginosa clinical strain.B1-Metallo-β-Lactamases: Where Do We Stand?Crystal Structure of the Metallo-β-Lactamase GOB in the Periplasmic Dizinc Form Reveals an Unusual Metal Site.Metallo-β-lactamase structure and function.Targeting metallo-β-lactamase enzymes in antibiotic resistance.A variety of roles for versatile zinc in metallo-β-lactamases.The structure of the metallo-β-lactamase VIM-2 in complex with a triazolylthioacetamide inhibitor.Bulgecin A as a β-lactam enhancer for carbapenem-resistant Pseudomonas aeruginosa and carbapenem-resistant Acinetobacter baumannii clinical isolates containing various resistance mechanisms.
P2860
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P2860
The three-dimensional structure of VIM-2, a Zn-beta-lactamase from Pseudomonas aeruginosa in its reduced and oxidised form
description
2008 nî lūn-bûn
@nan
2008 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
The three-dimensional structur ...... its reduced and oxidised form
@ast
The three-dimensional structur ...... its reduced and oxidised form
@en
The three-dimensional structur ...... its reduced and oxidised form
@nl
type
label
The three-dimensional structur ...... its reduced and oxidised form
@ast
The three-dimensional structur ...... its reduced and oxidised form
@en
The three-dimensional structur ...... its reduced and oxidised form
@nl
prefLabel
The three-dimensional structur ...... its reduced and oxidised form
@ast
The three-dimensional structur ...... its reduced and oxidised form
@en
The three-dimensional structur ...... its reduced and oxidised form
@nl
P2093
P3181
P1476
The three-dimensional structur ...... its reduced and oxidised form
@en
P2093
G M Rossolini
I Garcia-Saez
J-D Docquier
O Dideberg
P304
P3181
P356
10.1016/J.JMB.2007.11.012
P407
P577
2008-01-18T00:00:00Z