Structural and kinetic characterization of a beta-lactamase-inhibitor protein. - sprookjes - yvandenbroek - TriplyDB

Structural and kinetic characterization of a beta-lactamase-inhibitor protein.

Structural and kinetic characterization of a beta-lactamase-inhibitor protein.

http://www.wikidata.org/entity/Q34338697

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Three decades of beta-lactamase inhibitors Flexible ligand docking using conformational ensembles Structural Insight into the Kinetics and Cp of Interactions between TEM-1 -Lactamase and -Lactamase Inhibitory Protein (BLIP)Structural and Biochemical Characterization of the Interaction between KPC-2 β-Lactamase and β-Lactamase Inhibitor Protein,Specificity and cooperativity at β-lactamase position 104 in TEM-1/BLIP and SHV-1/BLIP interactions Structural Basis of Outer Membrane Protein Biogenesis in Bacteria Increased Structural Flexibility at the Active Site of a Fluorophore-conjugated -Lactamase Distinctively Impacts Its Binding toward Diverse Cephalosporin Antibiotics Molecular docking programs successfully predict the binding of a beta-lactamase inhibitory protein to TEM-1 beta-lactamase Weighted protein residue networks based on joint recurrences between residues New beta -lactamase inhibitory protein (BLIP-I) from Streptomyces exfoliatus SMF19 and its roles on the morphological differentiation.Design of potent beta-lactamase inhibitors by phage display of beta-lactamase inhibitory protein.Display of functional beta-lactamase inhibitory protein on the surface of M13 bacteriophage.Selection of peptides inhibiting a beta-lactamase-like activity.Fine mapping of the sequence requirements for binding of beta-lactamase inhibitory protein (BLIP) to TEM-1 beta-lactamase using a genetic screen for BLIP function.Identification and characterization of beta-lactamase inhibitor protein-II (BLIP-II) interactions with beta-lactamases using phage display.Rapid detection and evaluation of clinical characteristics of emerging multiple-drug-resistant gram-negative rods carrying the metallo-beta-lactamase gene blaIMP The modular architecture of protein-protein binding interfaces Identification of a β-lactamase inhibitory protein variant that is a potent inhibitor of Staphylococcus PC1 β-lactamase.Biochemical-genetic analysis and distribution of FAR-1, a class A beta-lactamase from Nocardia farcinica Beta-lactamase inhibitors derived from single-domain antibody fragments elicited in the camelidae A potent new mode of beta-lactamase inhibition revealed by the 1.7 A X-ray crystallographic structure of the TEM-1-BLIP complex.Characterization of DinR, the Bacillus subtilis SOS repressor.Systematic substitutions at BLIP position 50 result in changes in binding specificity for class A β-lactamases.Soft protein-protein docking in internal coordinates Identification of the β-lactamase inhibitor protein-II (BLIP-II) interface residues essential for binding affinity and specificity for class A β-lactamases Electrostatics in protein-protein docking.Identification of residues in beta-lactamase critical for binding beta-lactamase inhibitory protein.Contributions of aspartate 49 and phenylalanine 142 residues of a tight binding inhibitory protein of beta-lactamases.Binding properties of a peptide derived from beta-lactamase inhibitory protein.THz frequency spectrum of protein-solvent interaction energy using a recurrence plot-based Wiener-Khinchin method.Resistance to beta-lactamase inhibitor protein does not parallel resistance to clavulanic acid in TEM beta-lactamase mutants.A regulatory gene (ccaR) required for cephamycin and clavulanic acid production in Streptomyces clavuligerus: amplification results in overproduction of both beta-lactam compounds.The bla gene of the cephamycin cluster of Streptomyces clavuligerus encodes a class A beta-lactamase of low enzymatic activity.Switchable reporter enzymes based on mutually exclusive domain interactions allow antibody detection directly in solution.Engineering Specificity from Broad to Narrow: Design of a β-Lactamase Inhibitory Protein (BLIP) Variant That Exclusively Binds and Detects KPC β-Lactamase.A novel chimeric peptide with antimicrobial activity.Role of β-lactamase residues in a common interface for binding the structurally unrelated inhibitory proteins BLIP and BLIP-II.Action-at-a-distance interactions enhance protein binding affinity.Determinants of binding affinity and specificity for the interaction of TEM-1 and SME-1 beta-lactamase with beta-lactamase inhibitory protein.FRETex: a FRET-based, high-throughput technique to analyze protein-protein interactions.

P2860

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P2860

Structural and kinetic characterization of a beta-lactamase-inhibitor protein.

http://www.wikidata.org/entity/Q34338697

description

1994 nî lūn-bûn

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1994 թուականի Ապրիլին հրատարակուած գիտական յօդուած

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1994 թվականի ապրիլին հրատարակված գիտական հոդված

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1994年の論文

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1994年論文

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1994年論文

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1994年論文

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1994年論文

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1994年論文

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1994年论文

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name

Structural and kinetic characterization of a beta-lactamase-inhibitor protein.

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Structural and kinetic characterization of a beta-lactamase-inhibitor protein.

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Structural and kinetic characterization of a beta-lactamase-inhibitor protein.

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type

label

Structural and kinetic characterization of a beta-lactamase-inhibitor protein.

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Structural and kinetic characterization of a beta-lactamase-inhibitor protein.

@en

Structural and kinetic characterization of a beta-lactamase-inhibitor protein.

@nl

prefLabel

Structural and kinetic characterization of a beta-lactamase-inhibitor protein.

@ast

Structural and kinetic characterization of a beta-lactamase-inhibitor protein.

@en

Structural and kinetic characterization of a beta-lactamase-inhibitor protein.

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Blanchard H

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Frère JM

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James MN

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Matagne A

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Strynadka NC

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657-660

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10.1038/368657A0

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