Mutational analysis of the two zinc-binding sites of the Bacillus cereus 569/H/9 metallo-beta-lactamase. - Wikidata - awgldk - TriplyDB

Mutational analysis of the two zinc-binding sites of the Bacillus cereus 569/H/9 metallo-beta-lactamase.

Mutational analysis of the two zinc-binding sites of the Bacillus cereus 569/H/9 metallo-beta-lactamase.

http://www.wikidata.org/entity/Q42157632

about

Asp-120 locates Zn2 for optimal metallo-beta-lactamase activity 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 Systematic mutational analysis of the putative hydrolase PqsE: toward a deeper molecular understanding of virulence acquisition in Pseudomonas aeruginosa Mimicking natural evolution in metallo-beta-lactamases through second-shell ligand mutations.Zinc ion-induced domain organization in metallo-beta-lactamases: a flexible "zinc arm" for rapid metal ion transfer?Molecular mechanisms of substrate recognition and specificity of New Delhi metallo-β-lactamase Evolution of Metallo-β-lactamases: Trends Revealed by Natural Diversity and in vitro Evolution The tRNase Z family of proteins: physiological functions, substrate specificity and structural properties.Biochemical characterization of beta-lactamases Bla1 and Bla2 from Bacillus anthracis.Differential binding of Co(II) and Zn(II) to metallo-beta-lactamase Bla2 from Bacillus anthracis.Grafting a new metal ligand in the cocatalytic site of B. cereus metallo-beta-lactamase: structural flexibility without loss of activity.Engineered mononuclear variants in Bacillus cereus metallo-beta-lactamase BcII are inactive.Metallo-β-lactamase structure and function.The mechanisms of catalysis by metallo beta-lactamases.Impact of remote mutations on metallo-beta-lactamase substrate specificity: implications for the evolution of antibiotic resistance.Assay platform for clinically relevant metallo-β-lactamases.Structural determinants of substrate binding to Bacillus cereus metallo-beta-lactamase.Identification and characterization of an unusual metallo-β-lactamase from Serratia proteamaculans.Studies on ternary metallo-beta lactamase-inhibitor complexes using electrospray ionization mass spectrometry.Chromophore-linked substrate (CLS405): probing metallo-β-lactamase activity and inhibition.Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis.

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P2860

Mutational analysis of the two zinc-binding sites of the Bacillus cereus 569/H/9 metallo-beta-lactamase.

http://www.wikidata.org/entity/Q42157632

description

2002 nî lūn-bûn

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2002年の論文

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2002年学术文章

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2002年学术文章

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2002年学术文章

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2002年学术文章

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2002年学术文章

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2002年學術文章

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2002年學術文章

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2002年學術文章

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name

Mutational analysis of the two ...... 69/H/9 metallo-beta-lactamase.

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Mutational analysis of the two ...... 69/H/9 metallo-beta-lactamase.

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type

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Mutational analysis of the two ...... 69/H/9 metallo-beta-lactamase.

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Mutational analysis of the two ...... 69/H/9 metallo-beta-lactamase.

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Mutational analysis of the two ...... 69/H/9 metallo-beta-lactamase.

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Mutational analysis of the two ...... 69/H/9 metallo-beta-lactamase.

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0264-6021:3630687

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Biochemical Journal

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Mutational analysis of the two ...... 69/H/9 metallo-beta-lactamase.

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P2093

Carine Bebrone

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Christelle Prosperi-Meys

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Dominique de Seny

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Jean-Marie Frère

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Moreno Galleni

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Philippe Noel

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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

Crystal structure of the IMP-1 metallo beta-lactamase from Pseudomonas aeruginosa and its complex with a mercaptocarboxylate inhibitor: binding determinants of a potent, broad-spectrum inhibitor

Structural effects of the active site mutation cysteine to serine inBacillus cereuszinc-β-lactamase

The structure of the Aeromonas proteolytica aminopeptidase complexed with a hydroxamate inhibitor. Involvement in catalysis of Glu151 and two zinc ions of the co-catalytic unit

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

1.85 A resolution structure of the zinc (II) beta-lactamase from Bacillus cereus

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

Structure of In31, a blaIMP-containing Pseudomonas aeruginosa integron phyletically related to In5, which carries an unusual array of gene cassettes.

Multifocal outbreaks of metallo-beta-lactamase-producing Pseudomonas aeruginosa resistant to broad-spectrum beta-lactams, including carbapenems.

Cloning and sequencing of the metallothioprotein beta-lactamase II gene of Bacillus cereus 569/H in Escherichia coli.

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687-696

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scholarly article

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10.1042/0264-6021:3630687

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P433

Pt 3

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363

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Gian Maria Rossolini

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2002-05-01T00:00:00Z

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247449677

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