Evolving carbapenemases: can medicinal chemists advance one step ahead of the coming storm? - Wikidata - wikimedia - TriplyDB

Evolving carbapenemases: can medicinal chemists advance one step ahead of the coming storm?

Evolving carbapenemases: can medicinal chemists advance one step ahead of the coming storm?

http://www.wikidata.org/entity/Q28752557

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New β-lactamase inhibitors: a therapeutic renaissance in an MDR world.QM/MM studies of monozinc β-lactamase CphA suggest that the crystal structure of an enzyme-intermediate complex represents a minor pathway.Biapenem inactivation by B2 metallo β-lactamases: energy landscape of the hydrolysis reaction.An altered zinc-binding site confers resistance to a covalent inactivator of New Delhi metallo-beta-lactamase-1 (NDM-1) discovered by high-throughput screening Protein variants form a system of networks: microdiversity of IMP metallo-beta-lactamases.Meropenem and chromacef intermediates observed in IMP-25 metallo-β-lactamase-catalyzed hydrolysis.Prevalence and Fate of Carbapenemase Genes in a Wastewater Treatment Plant in Northern China.Elucidating the Role of Residue 67 in IMP-Type Metallo-β-Lactamase Evolution.B1-Metallo-β-Lactamases: Where Do We Stand?New Delhi metallo-β-lactamase-1: structure, inhibitors and detection of producers.The Role of Active Site Flexible Loops in Catalysis and of Zinc in Conformational Stability of Bacillus cereus 569/H/9 β-Lactamase.Elucidating the role of Trp105 in the KPC-2 β-lactamase.The sequence-activity relationship between metallo-β-lactamases IMP-1, IMP-6, and IMP-25 suggests an evolutionary adaptation to meropenem exposure.Assay platform for clinically relevant metallo-β-lactamases.Systematic analysis of metallo-β-lactamases using an automated database.Biochemical characterization of IMP-30, a metallo-β-lactamase with enhanced activity toward ceftazidime Understanding the determinants of substrate specificity in IMP family metallo-β-lactamases: the importance of residue 262.Exploring the conformational and reactive dynamics of biomolecules in solution using an extended version of the glycine reactive force field.Carbamylmethyl Mercaptoacetate Thioether: A Novel Scaffold for the Development of L1 Metallo-β-lactamase Inhibitors.Engineering the stereochemistry of cephalosporin for specific detection of pathogenic carbapenemase-expressing bacteria.1,2,4-Triazole-3-thione Compounds as Inhibitors of Dizinc Metallo-β-lactamases.Inhibition of a cold-active alkaline phosphatase by imipenem revealed by in silico modeling of metallo-β-lactamase active sites.Defining the architecture of KPC-2 Carbapenemase: identifying allosteric networks to fight antibiotics resistance Diversity and Proliferation of Metallo-β-Lactamases: a Clarion Call for Clinically Effective Metallo-β-Lactamase Inhibitors

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P2860

Evolving carbapenemases: can medicinal chemists advance one step ahead of the coming storm?

http://www.wikidata.org/entity/Q28752557

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2010 nî lūn-bûn

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2010 թուականի Ապրիլին հրատարակուած գիտական յօդուած

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2010 թվականի ապրիլին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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Evolving carbapenemases: can m ...... tep ahead of the coming storm?

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Evolving carbapenemases: can m ...... tep ahead of the coming storm?

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Evolving carbapenemases: can m ...... tep ahead of the coming storm?

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Evolving carbapenemases: can m ...... tep ahead of the coming storm?

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Evolving carbapenemases: can m ...... tep ahead of the coming storm?

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Journal of Medicinal Chemistry

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Evolving carbapenemases: can m ...... tep ahead of the coming storm?

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Jeffrey H Toney

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Kevin T Duprez

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Ni Ai

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Peter Oelschlaeger

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William J Welsh

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P2860

Novel carbapenem-hydrolyzing beta-lactamase, KPC-1, from a carbapenem-resistant strain of Klebsiella pneumoniae

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

Carbapenemases: the versatile beta-lactamases

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

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.

Competitive Inhibitors of the CphA Metallo- -Lactamase from Aeromonas hydrophila

Crystallographic investigation of the inhibition mode of a VIM-2 metallo-beta-lactamase from Pseudomonas aeruginosa by a mercaptocarboxylate inhibitor

The three-dimensional structure of VIM-2, a Zn-beta-lactamase from Pseudomonas aeruginosa in its reduced and oxidised form

Structural basis for the broad-spectrum inhibition of metallo-beta-lactamases by thiols

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3013-3027

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10.1021/JM9012938

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8

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20121112

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