Biochemical and Structural Characterization of the Subclass B1 Metallo- -Lactamase VIM-4
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Crystal 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-lactamasesThe three-dimensional structure of VIM-31--a metallo-β-lactamase from Enterobacter cloacae in its native and oxidized formStructural basis for carbapenem-hydrolyzing mechanisms of carbapenemases conferring antibiotic resistanceA case study comparing quantitative stability-flexibility relationships across five metallo-β-lactamases highlighting differences within NDM-1.Molecular basis of NDM-1, a new antibiotic resistance determinantEvolution 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 ProfilesInteraction of Avibactam with Class B Metallo-β-Lactamases.Characterization of metallo-beta-lactamase VIM-27, an A57S mutant of VIM-1 associated with Klebsiella pneumoniae ST147.Detection and characterization of VIM-31, a new variant of VIM-2 with Tyr224His and His252Arg mutations, in a clinical isolate of Enterobacter cloacae.Carbapenemases in Klebsiella pneumoniae and other Enterobacteriaceae: an evolving crisis of global dimensionsExploring the Role of Residue 228 in Substrate and Inhibitor Recognition by VIM Metallo-β-lactamases.Inhibition of Streptococcus pneumoniae penicillin-binding protein 2x and Actinomadura R39 DD-peptidase activities by ceftaroline.B1-Metallo-β-Lactamases: Where Do We Stand?A convenient method to screen for carbapenemase-producing Pseudomonas aeruginosa.Metallo-β-lactamase structure and function.Dissemination of metallo-β-lactamase in Pseudomonas aeruginosa isolates in Egypt: mutation in blaVIM-4.The Role of Active Site Flexible Loops in Catalysis and of Zinc in Conformational Stability of Bacillus cereus 569/H/9 β-Lactamase.Allosteric inhibition of VIM metallo-β-lactamases by a camelid nanobody.1,2,4-Triazole-3-thione Compounds as Inhibitors of Dizinc Metallo-β-lactamases.Ceftazidime Is the Key Diversification and Selection Driver of VIM-Type Carbapenemases.
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Biochemical and Structural Characterization of the Subclass B1 Metallo- -Lactamase VIM-4
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2011 nî lūn-bûn
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2011 թուականի Մարտին հրատարակուած գիտական յօդուած
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2011 թվականի մարտին հրատարակված գիտական հոդված
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2011年の論文
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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
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name
Biochemical and Structural Characterization of the Subclass B1 Metallo- -Lactamase VIM-4
@ast
Biochemical and Structural Characterization of the Subclass B1 Metallo- -Lactamase VIM-4
@en
Biochemical and Structural Characterization of the Subclass B1 Metallo- -Lactamase VIM-4
@nl
type
label
Biochemical and Structural Characterization of the Subclass B1 Metallo- -Lactamase VIM-4
@ast
Biochemical and Structural Characterization of the Subclass B1 Metallo- -Lactamase VIM-4
@en
Biochemical and Structural Characterization of the Subclass B1 Metallo- -Lactamase VIM-4
@nl
prefLabel
Biochemical and Structural Characterization of the Subclass B1 Metallo- -Lactamase VIM-4
@ast
Biochemical and Structural Characterization of the Subclass B1 Metallo- -Lactamase VIM-4
@en
Biochemical and Structural Characterization of the Subclass B1 Metallo- -Lactamase VIM-4
@nl
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P3181
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P1476
Biochemical and Structural Characterization of the Subclass B1 Metallo- -Lactamase VIM-4
@en
P2093
Adrien Favier
Clémentine Laurent
Daouda A K Traoré
Elodie Loisel
Jean Sébastien Sohier
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P304
P3181
P356
10.1128/AAC.01486-09
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P577
2011-03-01T00:00:00Z