A potent new mode of beta-lactamase inhibition revealed by the 1.7 A X-ray crystallographic structure of the TEM-1-BLIP complex.
about
The structure of BVU2987 from Bacteroides vulgatus reveals a superfamily of bacterial periplasmic proteins with possible inhibitory functionGenetic and Structural Insights into the Dissemination Potential of the Extremely Broad-Spectrum Class A -Lactamase KPC-2 Identified in an Escherichia coli Strain and an Enterobacter cloacae Strain Isolated from the Same Patient in FranceComputational Redesign of the SHV-1 β-Lactamase/β-Lactamase Inhibitor Protein InterfaceStructural 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,Analysis of the Binding Forces Driving the Tight Interactions between -Lactamase Inhibitory Protein-II (BLIP-II) and Class A -LactamasesTargeting Class A and C Serine β-Lactamases with a Broad-Spectrum Boronic Acid DerivativeSolving structures of protein complexes by molecular replacement with PhaserWeighted protein residue networks based on joint recurrences between residuesDesign of generic biosensors based on green fluorescent proteins with allosteric sites by directed evolution.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.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.The modular architecture of protein-protein binding interfacesIdentification of a β-lactamase inhibitory protein variant that is a potent inhibitor of Staphylococcus PC1 β-lactamase.Beta-lactamase inhibitors derived from single-domain antibody fragments elicited in the camelidaeUse of periplasmic target protein capture for phage display engineering of tight-binding protein-protein interactions.Ankyrin-mediated self-protection during cell invasion by the bacterial predator Bdellovibrio bacteriovorusProtein binding specificity versus promiscuity.Exploring the potential impact of an expanded genetic code on protein functionSystematic substitutions at BLIP position 50 result in changes in binding specificity for class A β-lactamases.Soft protein-protein docking in internal coordinatesIdentification of the β-lactamase inhibitor protein-II (BLIP-II) interface residues essential for binding affinity and specificity for class A β-lactamasesThe structure of Toho1 β-lactamase in complex with penicillin reveals the role of Tyr105 in substrate recognition.Electrostatics in protein-protein docking.Protein-protein docking with multiple residue conformations and residue substitutions.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.Engineering Specificity from Broad to Narrow: Design of a β-Lactamase Inhibitory Protein (BLIP) Variant That Exclusively Binds and Detects KPC β-Lactamase.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.Docking molecules by families to increase the diversity of hits in database screens: computational strategy and experimental evaluation.Determinants of binding affinity and specificity for the interaction of TEM-1 and SME-1 beta-lactamase with beta-lactamase inhibitory protein.Dissecting the protein-protein interface between beta-lactamase inhibitory protein and class A beta-lactamases.Site-saturation mutagenesis of Tyr-105 reveals its importance in substrate stabilization and discrimination in TEM-1 beta-lactamase.
P2860
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P2860
A potent new mode of beta-lactamase inhibition revealed by the 1.7 A X-ray crystallographic structure of the TEM-1-BLIP complex.
description
1996 nî lūn-bûn
@nan
1996 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի մարտին հրատարակված գիտական հոդված
@hy
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
name
A potent new mode of beta-lact ...... ure of the TEM-1-BLIP complex.
@ast
A potent new mode of beta-lact ...... ure of the TEM-1-BLIP complex.
@en
A potent new mode of beta-lact ...... ure of the TEM-1-BLIP complex.
@nl
type
label
A potent new mode of beta-lact ...... ure of the TEM-1-BLIP complex.
@ast
A potent new mode of beta-lact ...... ure of the TEM-1-BLIP complex.
@en
A potent new mode of beta-lact ...... ure of the TEM-1-BLIP complex.
@nl
prefLabel
A potent new mode of beta-lact ...... ure of the TEM-1-BLIP complex.
@ast
A potent new mode of beta-lact ...... ure of the TEM-1-BLIP complex.
@en
A potent new mode of beta-lact ...... ure of the TEM-1-BLIP complex.
@nl
P2093
P2860
P356
P1476
A potent new mode of beta-lact ...... ture of the TEM-1-BLIP complex
@en
P2093
P2860
P304
P356
10.1038/NSB0396-290
P577
1996-03-01T00:00:00Z