Probing the role of Asp-120(81) of metallo-beta-lactamase (IMP-1) by site-directed mutagenesis, kinetic studies, and X-ray crystallography. - Wikidata - wikimedia - TriplyDB

Probing the role of Asp-120(81) of metallo-beta-lactamase (IMP-1) by site-directed mutagenesis, kinetic studies, and X-ray crystallography.

Probing the role of Asp-120(81) of metallo-beta-lactamase (IMP-1) by site-directed mutagenesis, kinetic studies, and X-ray crystallography.

http://www.wikidata.org/entity/Q46402244

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Mechanism of the quorum-quenching lactonase (AiiA) from Bacillus thuringiensis. 2. Substrate modeling and active site mutations Asp-120 locates Zn2 for optimal metallo-beta-lactamase activity Structural Insights into the Subclass B3 Metallo- -Lactamase SMB-1 and the Mode of Inhibition by the Common Metallo- -Lactamase Inhibitor Mercaptoacetate His224 Alters the R2 Drug Binding Site and Phe218 Influences the Catalytic Efficiency of the Metallo- -Lactamase VIM-7 Overcoming differences: The catalytic mechanism of metallo-β-lactamases Evolving carbapenemases: can medicinal chemists advance one step ahead of the coming storm?Characteristics and function of sulfur dioxygenase in Echiuran worm Urechis unicinctus NDM-12, a novel New Delhi metallo-β-lactamase variant from a carbapenem-resistant Escherichia coli clinical isolate in Nepal.Biochemical, mechanistic, and spectroscopic characterization of metallo-β-lactamase VIM-2.Meropenem and chromacef intermediates observed in IMP-25 metallo-β-lactamase-catalyzed hydrolysis.A Carbapenem-Resistant Pseudomonas aeruginosa Isolate Harboring Two Copies of blaIMP-34 Encoding a Metallo-β-Lactamase.B1-Metallo-β-Lactamases: Where Do We Stand?Metallo-β-lactamase structure and function.Structural and Mutagenic Analysis of Metallo-β-Lactamase IMP-18.Role of zinc content on the catalytic efficiency of B1 metallo beta-lactamases.Purification, crystallization and preliminary X-ray analysis of IMP-18, a class B carbapenemase from Pseudomonas aeruginosa.Pneumococcal phosphorylcholine esterase, Pce, contains a metal binuclear center that is essential for substrate binding and catalysis Exploring the conformational and reactive dynamics of biomolecules in solution using an extended version of the glycine reactive force field.Probing the Interaction of Aspergillomarasmine A with Metallo-β-lactamases NDM-1, VIM-2, and IMP-7.Hydrolysis of cephalexin and meropenem by New Delhi metallo-β-lactamase: the substrate protonation mechanism is drug dependent.Binding site residues in β-lactamases: role in non-classical interactions and metal binding

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P2860

Probing the role of Asp-120(81) of metallo-beta-lactamase (IMP-1) by site-directed mutagenesis, kinetic studies, and X-ray crystallography.

http://www.wikidata.org/entity/Q46402244

description

2005 nî lūn-bûn

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2005年の論文

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2005年学术文章

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2005年学术文章

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2005年学术文章

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2005年学术文章

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2005年学术文章

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2005年学术文章

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2005年學術文章

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2005年學術文章

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name

Probing the role of Asp-120(81 ...... es, and X-ray crystallography.

@en

Probing the role of Asp-120(81 ...... es, and X-ray crystallography.

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type

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Probing the role of Asp-120(81 ...... es, and X-ray crystallography.

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Probing the role of Asp-120(81 ...... es, and X-ray crystallography.

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Probing the role of Asp-120(81 ...... es, and X-ray crystallography.

@en

Probing the role of Asp-120(81 ...... es, and X-ray crystallography.

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Journal of Biological Chemistry

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Probing the role of Asp-120(81 ...... es, and X-ray crystallography.

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P2093

Akiko Kawanami

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Hiromasa Kurosaki

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Hisami Yasuzawa

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Masafumi Goto

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Takahiro Kuroki

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Toshihiro Higashi

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Wanchun Jin

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Yoshichika Arakawa

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Yoshihiro Yamaguchi

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Yuriko Yamagata

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P2860

Improved methods for building protein models in electron density maps and the location of errors in these models

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Processing of X-ray diffraction data collected in oscillation mode

Succinic acids as potent inhibitors of plasmid-borne IMP-1 metallo-beta-lactamase

Identification of a series of tricyclic natural products as potent broad-spectrum inhibitors of metallo-beta-lactamases.

Crystal structure of the wide-spectrum binuclear zinc beta-lactamase from Bacteroides fragilis

AMoRe: an automated package for molecular replacement

On the mechanism of the metallo-beta-lactamase from Bacteroides fragilis.

Metallo-beta-lactamase producers in environmental microbiota: new molecular class B enzyme in Janthinobacterium lividum.

The Aeromonas hydrophila cphA gene: molecular heterogeneity among class B metallo-beta-lactamases.

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20824-20832

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10.1074/JBC.M414314200

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21

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X-ray crystallography