Insights into positive and negative requirements for protein-protein interactions by crystallographic analysis of the beta-lactamase inhibitory proteins BLIP, BLIP-I, and BLP
about
Structural and Biochemical Characterization of the Interaction between KPC-2 β-Lactamase and β-Lactamase Inhibitor Protein,Molecular Rearrangements Involved in the Capsid Shell Maturation of Bacteriophage T7Structural Basis of Outer Membrane Protein Biogenesis in BacteriaAnalysis of the Binding Forces Driving the Tight Interactions between -Lactamase Inhibitory Protein-II (BLIP-II) and Class A -LactamasesNMR approaches in structure-based lead discovery: recent developments and new frontiers for targeting multi-protein complexesWeighted protein residue networks based on joint recurrences between residuesThree steps to gold: mechanism of protein adsorption revealed by Brownian and molecular dynamics simulations.Designing specific protein-protein interactions using computation, experimental library screening, or integrated methodsIdentification and characterization of beta-lactamase inhibitor protein-II (BLIP-II) interactions with beta-lactamases using phage display.Protein binding specificity versus promiscuity.Low-stringency selection of TEM1 for BLIP shows interface plasticity and selection for faster binders.Systematic substitutions at BLIP position 50 result in changes in binding specificity for class A β-lactamases.Identification of the β-lactamase inhibitor protein-II (BLIP-II) interface residues essential for binding affinity and specificity for class A β-lactamasesTHz frequency spectrum of protein-solvent interaction energy using a recurrence plot-based Wiener-Khinchin method.BLIP-II is a highly potent inhibitor of Klebsiella pneumoniae carbapenemase (KPC-2).BLIP-II Employs Differential Hotspot Residues To Bind Structurally Similar Staphylococcus aureus PBP2a and Class A β-Lactamases.Role of β-lactamase residues in a common interface for binding the structurally unrelated inhibitory proteins BLIP and BLIP-II.Detecting transitions in protein dynamics using a recurrence quantification analysis based bootstrap method.The adaptive nature of protein residue networks.Tackling the Antibiotic Resistance Caused by Class A -Lactamases through the Use of -Lactamase Inhibitory Protein
P2860
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P2860
Insights into positive and negative requirements for protein-protein interactions by crystallographic analysis of the beta-lactamase inhibitory proteins BLIP, BLIP-I, and BLP
description
2009 nî lūn-bûn
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2009 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Insights into positive and neg ...... proteins BLIP, BLIP-I, and BLP
@ast
Insights into positive and neg ...... proteins BLIP, BLIP-I, and BLP
@en
Insights into positive and neg ...... proteins BLIP, BLIP-I, and BLP
@nl
type
label
Insights into positive and neg ...... proteins BLIP, BLIP-I, and BLP
@ast
Insights into positive and neg ...... proteins BLIP, BLIP-I, and BLP
@en
Insights into positive and neg ...... proteins BLIP, BLIP-I, and BLP
@nl
prefLabel
Insights into positive and neg ...... proteins BLIP, BLIP-I, and BLP
@ast
Insights into positive and neg ...... proteins BLIP, BLIP-I, and BLP
@en
Insights into positive and neg ...... proteins BLIP, BLIP-I, and BLP
@nl
P2093
P1476
Insights into positive and neg ...... proteins BLIP, BLIP-I, and BLP
@en
P2093
Daniel C Lim
Kye Joon Lee
Liza de Castro
Michael Gretes
Natalie C J Strynadka
Sung Gyun Kang
P304
P356
10.1016/J.JMB.2009.03.058
P407
P577
2009-03-28T00:00:00Z