Succinic acids as potent inhibitors of plasmid-borne IMP-1 metallo-beta-lactamase - Test2 - elhamkhani - TriplyDB

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

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

http://www.wikidata.org/entity/Q27632353

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Three decades of beta-lactamase inhibitors Probing substrate binding to metallo-beta-lactamase L1 from Stenotrophomonas maltophilia by using site-directed mutagenesis The 1.5-A structure of Chryseobacterium meningosepticum zinc beta-lactamase in complex with the inhibitor, D-captopril Asp-120 locates Zn2 for optimal metallo-beta-lactamase activity Amidation of Bioactive Peptides: The Structure of the Lyase Domain of the Amidating Enzyme Solution structures of the Bacillus cereus metallo-β-lactamase BcII and its complex with the broad spectrum inhibitor R -thiomandelic acid Iron(III) located in the dinuclear metallo-β-lactamase IMP-1 by pseudocontact shifts Evolving carbapenemases: can medicinal chemists advance one step ahead of the coming storm?The molecular structure and catalytic mechanism of a quorum-quenching N-acyl-L-homoserine lactone hydrolase.Mimicking natural evolution in metallo-beta-lactamases through second-shell ligand mutations.Inhibitors of VIM-2 by screening pharmacologically active and click-chemistry compound libraries Spectroscopic and mechanistic studies of heterodimetallic forms of metallo-β-lactamase NDM-1.Metallo-beta-lactamases: the quiet before the storm?Chromosome-encoded beta-lactamases TUS-1 and MUS-1 from Myroides odoratus and Myroides odoratimimus (formerly Flavobacterium odoratum), new members of the lineage of molecular subclass B1 metalloenzymes.Antibiotic adjuvants: diverse strategies for controlling drug-resistant pathogens.Biochemical, mechanistic, and spectroscopic characterization of metallo-β-lactamase VIM-2.Azolylthioacetamide: A Highly Promising Scaffold for the Development of Metallo-β-lactamase Inhibitors.Amino Acid Thioester Derivatives: A Highly Promising Scaffold for the Development of Metallo-β-lactamase L1 Inhibitors.Crystal Structure of DIM-1, an Acquired Subclass B1 Metallo-β-Lactamase from Pseudomonas stutzeri.Expression, purification, crystallization and preliminary X-ray analysis of Aeromonas hydrophilia metallo-beta-lactamase 2-Substituted 4,5-dihydrothiazole-4-carboxylic acids are novel inhibitors of metallo-β-lactamases B1-Metallo-β-Lactamases: Where Do We Stand?Probing substrate binding to the metal binding sites in metallo-β-lactamase L1 during catalysis Conformational changes in the metallo-beta-lactamase ImiS during the catalytic reaction: an EPR spectrokinetic study of Co(II)-spin label interactions.New β-phospholactam as a carbapenem transition state analog: Synthesis of a broad-spectrum inhibitor of metallo-β-lactamases Bisthiazolidines: A Substrate-Mimicking Scaffold as an Inhibitor of the NDM-1 Carbapenemase.New β-lactam antibiotics and β-lactamase inhibitors.An Update on the Status of Potent Inhibitors of Metallo-β-Lactamases.Targeting metallo-β-lactamase enzymes in antibiotic resistance.Fragment-based inhibitor discovery against β-lactamase A variety of roles for versatile zinc in metallo-β-lactamases.Progress toward inhibitors of metallo-β-lactamases.Catalytic role of the metal ion in the metallo-beta-lactamase GOB.N-arylsulfonyl hydrazones as inhibitors of IMP-1 metallo-beta-lactamase.The Role of Active Site Flexible Loops in Catalysis and of Zinc in Conformational Stability of Bacillus cereus 569/H/9 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.Studying the active-site loop movement of the São Paolo metallo-β-lactamase-1†Electronic supplementary information (ESI) available: Procedures for protein expression and purification, 19F-labelling, crystallisation, data collection, and structure de Thiomandelic acid, a broad spectrum inhibitor of zinc beta-lactamases: kinetic and spectroscopic studies.Molecular dynamics simulations of the dinuclear zinc-beta-lactamase from Bacteroides fragilis complexed with imipenem.

P2860

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P2860

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

http://www.wikidata.org/entity/Q27632353

description

2001 nî lūn-bûn

@nan

2001 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2001 թվականի օգոստոսին հրատարակված գիտական հոդված

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2001年の論文

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2001年論文

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2001年論文

@zh-hant

2001年論文

@zh-hk

2001年論文

@zh-mo

2001年論文

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2001年论文

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name

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

@ast

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

@en

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

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type

label

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

@ast

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

@en

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

@nl

prefLabel

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

@ast

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

@en

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

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P1433

Journal of Biological Chemistry

P1476

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

@en

P2093

G G Hammond

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

G P Rouen

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J H Toney

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J M Balkovec

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M L Greenlee

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M L Hammond

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N Sharma

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P M Fitzgerald

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S H Olson

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Y D Gao

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P2860

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

Antibiotic sensitization using biphenyl tetrazoles as potent inhibitors of Bacteroides fragilis metallo-beta-lactamase

Unanticipated inhibition of the metallo-beta-lactamase from Bacteroides fragilis by 4-morpholineethanesulfonic acid (MES): a crystallographic study at 1.85-A resolution

The crystal structure of the L1 metallo-beta-lactamase from Stenotrophomonas maltophilia at 1.7 A resolution

Carbapenemases: a problem in waiting?

Imipenem/Cilastatin

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

Inhibition studies on the metallo-beta-lactamase L1 from Stenotrophomonas maltophilia.

Comparison of knowledge-based and distance geometry approaches for generation of molecular conformations.

Metallo-beta-lactamase: structure and mechanism.

P304

31913-8

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scholarly article

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10.1074/JBC.M104742200

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P433

34

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P478

276

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2001-08-24T00:00:00Z

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11390410

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