Metallo-β-lactamases withstand low Zn(II) conditions by tuning metal-ligand interactions - Wikidata - awgldk - TriplyDB

Metallo-β-lactamases withstand low Zn(II) conditions by tuning metal-ligand interactions

Metallo-β-lactamases withstand low Zn(II) conditions by tuning metal-ligand interactions

http://www.wikidata.org/entity/Q27681358

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Crystal Structures of Pseudomonas aeruginosa GIM-1: Active-Site Plasticity in Metallo- -Lactamases His224 Alters the R2 Drug Binding Site and Phe218 Influences the Catalytic Efficiency of the Metallo- -Lactamase VIM-7 Use of ferrous iron by metallo-β-lactamases Overcoming differences: The catalytic mechanism of metallo-β-lactamases Spectroscopic and mechanistic studies of heterodimetallic forms of metallo-β-lactamase NDM-1.Evolution of Metallo-β-lactamases: Trends Revealed by Natural Diversity and in vitro Evolution Biochemical, mechanistic, and spectroscopic characterization of metallo-β-lactamase VIM-2.Host-specific enzyme-substrate interactions in SPM-1 metallo-β-lactamase are modulated by second sphere residues.Quantitative Description of a Protein Fitness Landscape Based on Molecular Features.Crystal Structure of DIM-1, an Acquired Subclass B1 Metallo-β-Lactamase from Pseudomonas stutzeri.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.Probing the role of Met221 in the unusual metallo-β-lactamase GOB-18.Membrane anchoring stabilizes and favors secretion of New Delhi metallo-β-lactamase Crystal Structure of the Metallo-β-Lactamase GOB in the Periplasmic Dizinc Form Reveals an Unusual Metal Site.A variety of roles for versatile zinc in metallo-β-lactamases.Synthetic biology for the directed evolution of protein biocatalysts: navigating sequence space intelligently.Antibiotic resistance in Zn(II)-deficient environments: metallo-β-lactamase activation in the periplasm.A general reaction mechanism for carbapenem hydrolysis by mononuclear and binuclear metallo-β-lactamases.Clinical Variants of New Delhi Metallo-β-Lactamase Are Evolving To Overcome Zinc Scarcity.Clinical Evolution of New Delhi Metallo-β-Lactamase (NDM) Optimizes Resistance under Zn(II) Deprivation.Embelin Restores Carbapenem Efficacy against NDM-1-Positive Pathogens.

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Metallo-β-lactamases withstand low Zn(II) conditions by tuning metal-ligand interactions

http://www.wikidata.org/entity/Q27681358

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2012 nî lūn-bûn

@nan

2012 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2012 թվականի օգոստոսին հրատարակված գիտական հոդված

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2012年の論文

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2012年論文

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2012年論文

@zh-hant

2012年論文

@zh-hk

2012年論文

@zh-mo

2012年論文

@zh-tw

2012年论文

@wuu

name

Metallo-β-lactamases withstand low Zn(II) conditions by tuning metal-ligand interactions

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Metallo-β-lactamases withstand low Zn(II) conditions by tuning metal-ligand interactions

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Metallo-β-lactamases withstand low Zn(II) conditions by tuning metal-ligand interactions

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type

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Metallo-β-lactamases withstand low Zn(II) conditions by tuning metal-ligand interactions

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Metallo-β-lactamases withstand low Zn(II) conditions by tuning metal-ligand interactions

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Metallo-β-lactamases withstand low Zn(II) conditions by tuning metal-ligand interactions

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Metallo-β-lactamases withstand low Zn(II) conditions by tuning metal-ligand interactions

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Metallo-β-lactamases withstand low Zn(II) conditions by tuning metal-ligand interactions

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Metallo-β-lactamases withstand low Zn(II) conditions by tuning metal-ligand interactions

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Nature Chemical Biology

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Metallo-β-lactamases withstand low Zn(II) conditions by tuning metal-ligand interactions

@en

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Alejandro J Vila

http://www.w3.org/2001/XMLSchema#string

Francisco J Medrano Martín

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Javier M González

http://www.w3.org/2001/XMLSchema#string

Julia A Cricco

http://www.w3.org/2001/XMLSchema#string

María-Rocío Meini

http://www.w3.org/2001/XMLSchema#string

Pablo E Tomatis

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P2860

The 3-D structure of a zinc metallo-beta-lactamase from Bacillus cereus reveals a new type of protein fold

Evidence of adaptability in metal coordination geometry and active-site loop conformation among B1 metallo-beta-lactamases

Crystal structure of the zinc-dependent beta-lactamase from Bacillus cereus at 1.9 A resolution: binuclear active site with features of a mononuclear enzyme

Femtomolar sensitivity of metalloregulatory proteins controlling zinc homeostasis

Trapping and characterization of a reaction intermediate in carbapenem hydrolysis by B. cereus metallo-beta-lactamase.

Bacterial resistance to beta-lactam antibiotics: compelling opportunism, compelling opportunity.

Expansion of the zinc metallo-hydrolase family of the beta-lactamase fold.

Coordination chemistry of bacterial metal transport and sensing.

Differential binding of Co(II) and Zn(II) to metallo-beta-lactamase Bla2 from Bacillus anthracis.

A place for thioether chemistry in cellular copper ion recognition and trafficking.

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698-700

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scholarly article

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4391873

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10.1038/NCHEMBIO.1005

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8

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8

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2012-08-01T00:00:00Z

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228063172

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1003226600

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22729148

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3470787

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