Analysis of the functional contributions of Asn233 in metallo-β-lactamase IMP-1 - Wikidata - awgldk - TriplyDB

Analysis of the functional contributions of Asn233 in metallo-β-lactamase IMP-1

Analysis of the functional contributions of Asn233 in metallo-β-lactamase IMP-1

http://www.wikidata.org/entity/Q35598527

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Mutagenesis of Zinc Ligand Residue Cys221 Reveals Plasticity in the IMP-1 Metallo- -Lactamase Active Site Crystal Structures of Pseudomonas aeruginosa GIM-1: Active-Site Plasticity in Metallo- -Lactamases Crystal Structure of the Mobile Metallo- -Lactamase AIM-1 from Pseudomonas aeruginosa: Insights into Antibiotic Binding and the Role of Gln157 Structural and biochemical characterization of VIM-26 shows that Leu224 has implications for the substrate specificity of VIM metallo-β-lactamases Structural basis for carbapenem-hydrolyzing mechanisms of carbapenemases conferring antibiotic resistance 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 Probing the effect of the non-active-site mutation Y229W in New Delhi metallo-β-lactamase-1 by site-directed mutagenesis, kinetic studies, and molecular dynamics simulations.Crystal Structure of DIM-1, an Acquired Subclass B1 Metallo-β-Lactamase from Pseudomonas stutzeri.Deep Sequencing of Random Mutant Libraries Reveals the Active Site of the Narrow Specificity CphA Metallo-β-Lactamase is Fragile to Mutations.2-Substituted 4,5-dihydrothiazole-4-carboxylic acids are novel inhibitors of metallo-β-lactamases Role of Residues W228 and Y233 in the Structure and Activity of Metallo-β-Lactamase GIM-1.B1-Metallo-β-Lactamases: Where Do We Stand?Metallo-β-lactamase structure and function.Structural Insights into TMB-1 and the Role of Residues 119 and 228 in Substrate and Inhibitor Binding.The sequence-activity relationship between metallo-β-lactamases IMP-1, IMP-6, and IMP-25 suggests an evolutionary adaptation to meropenem exposure.Structural basis of metallo-β-lactamase, serine-β-lactamase and penicillin-binding protein inhibition by cyclic boronates.Understanding the determinants of substrate specificity in IMP family metallo-β-lactamases: the importance of residue 262.Differential active site requirements for NDM-1 β-lactamase hydrolysis of carbapenem versus penicillin and cephalosporin antibiotics

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P2860

Analysis of the functional contributions of Asn233 in metallo-β-lactamase IMP-1

http://www.wikidata.org/entity/Q35598527

description

2011 nî lūn-bûn

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2011年の論文

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Analysis of the functional contributions of Asn233 in metallo-β-lactamase IMP-1

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Analysis of the functional contributions of Asn233 in metallo-β-lactamase IMP-1

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Analysis of the functional contributions of Asn233 in metallo-β-lactamase IMP-1

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Analysis of the functional contributions of Asn233 in metallo-β-lactamase IMP-1

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Analysis of the functional contributions of Asn233 in metallo-β-lactamase IMP-1

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Analysis of the functional contributions of Asn233 in metallo-β-lactamase IMP-1

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Antimicrobial Agents and Chemotherapy

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Analysis of the functional contributions of Asn233 in metallo-β-lactamase IMP-1

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Lori B Horton

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Nicholas G Brown

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Sompong Vongpunsawad

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Timothy Palzkill

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Wanzhi Huang

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P2860

Updated functional classification of beta-lactamases

Three decades of beta-lactamase inhibitors

Characterization of a new metallo-beta-lactamase gene, bla(NDM-1), and a novel erythromycin esterase gene carried on a unique genetic structure in Klebsiella pneumoniae sequence type 14 from India

Multiple sequence alignment with the Clustal series of programs

A functional classification scheme for beta-lactamases and its correlation with molecular structure

Carbapenemases: the versatile beta-lactamases

Probing substrate binding to metallo-beta-lactamase L1 from Stenotrophomonas maltophilia by using site-directed mutagenesis

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

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

Site-directed mutagenesis by overlap extension using the polymerase chain reaction

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10.1128/AAC.00340-11

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3232802

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