His224 Alters the R2 Drug Binding Site and Phe218 Influences the Catalytic Efficiency of the Metallo- -Lactamase VIM-7
about
Structural and biochemical characterization of VIM-26 shows that Leu224 has implications for the substrate specificity of VIM metallo-β-lactamasesComparison of Verona Integron-Borne Metallo-β-Lactamase (VIM) Variants Reveals Differences in Stability and Inhibition ProfilesRole of Residues W228 and Y233 in the Structure and Activity of Metallo-β-Lactamase GIM-1.Structural Insights into TMB-1 and the Role of Residues 119 and 228 in Substrate and Inhibitor Binding.Ceftazidime Is the Key Diversification and Selection Driver of VIM-Type Carbapenemases.
P2860
His224 Alters the R2 Drug Binding Site and Phe218 Influences the Catalytic Efficiency of the Metallo- -Lactamase VIM-7
description
2014 nî lūn-bûn
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2014 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
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2014 թվականի օգոստոսին հրատարակված գիտական հոդված
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2014年の論文
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2014年学术文章
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2014年学术文章
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2014年学术文章
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2014年学术文章
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2014年学术文章
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2014年學術文章
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name
His224 Alters the R2 Drug Bind ...... the Metallo- -Lactamase VIM-7
@ast
His224 Alters the R2 Drug Bind ...... the Metallo- -Lactamase VIM-7
@en
His224 Alters the R2 Drug Bind ...... the Metallo- -Lactamase VIM-7
@nl
type
label
His224 Alters the R2 Drug Bind ...... the Metallo- -Lactamase VIM-7
@ast
His224 Alters the R2 Drug Bind ...... the Metallo- -Lactamase VIM-7
@en
His224 Alters the R2 Drug Bind ...... the Metallo- -Lactamase VIM-7
@nl
prefLabel
His224 Alters the R2 Drug Bind ...... the Metallo- -Lactamase VIM-7
@ast
His224 Alters the R2 Drug Bind ...... the Metallo- -Lactamase VIM-7
@en
His224 Alters the R2 Drug Bind ...... the Metallo- -Lactamase VIM-7
@nl
P2093
P2860
P356
P1476
His224 alters the R2 drug bind ...... the metallo-β-lactamase VIM-7
@en
P2093
Gro Elin Kjæreng Bjerga
Hanna-Kirsti S Leiros
Ingar Leiros
Kine Susann Waade Edvardsen
Marit Sjo Lorentzen
Susann Skagseth
P2860
P304
P356
10.1128/AAC.02735-13
P407
P577
2014-06-09T00:00:00Z