The Abl SH2-kinase linker naturally adopts a conformation competent for SH3 domain binding.
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Analytical Aspects of Hydrogen Exchange Mass SpectrometryFluorescence Polarization Screening Assays for Small Molecule Allosteric Modulators of ABL Kinase FunctionDynamics of the Tec-family tyrosine kinase SH3 domains.Avian influenza viruses inhibit the major cellular signalling integrator c-Abl.Two-state dynamics of the SH3-SH2 tandem of Abl kinase and the allosteric role of the N-capPartial cooperative unfolding in proteins as observed by hydrogen exchange mass spectrometry.Hierarchical modeling of activation mechanisms in the ABL and EGFR kinase domains: thermodynamic and mechanistic catalysts of kinase activation by cancer mutations.Tyrosine phosphorylation in the SH3 domain disrupts negative regulatory interactions within the c-Abl kinase core.Abl N-terminal cap stabilization of SH3 domain dynamicsMisfolding, Aggregation, and Disordered Segments in c-Abl and p53 in Human Cancer.Conformational disturbance in Abl kinase upon mutation and deregulation.Differential hydrogen/deuterium exchange mass spectrometry analysis of protein-ligand interactionsOn the solution conformation and dynamics of the HIV-1 viral infectivity factorConformational transitions in the membrane scaffold protein of phospholipid bilayer nanodiscsStructure and dynamic regulation of Abl kinases.Iminoguanidines as Allosteric Inhibitors of the Iron-Regulated Heme Oxygenase (HemO) of Pseudomonas aeruginosa.What's in a loop?Protein conformation ensembles monitored by HDX reveal a structural rationale for abscisic acid signaling protein affinities and activities.Conformational analysis of processivity clamps in solution demonstrates that tertiary structure does not correlate with protein dynamics.The stress sigma factor of RNA polymerase RpoS/σS is a solvent exposed open molecule in solution.Atomic view of the energy landscape in the allosteric regulation of Abl kinase.Coupled regulation by the juxtamembrane and sterile α motif (SAM) linker is a hallmark of Ephrin tyrosine kinase evolution.
P2860
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P2860
The Abl SH2-kinase linker naturally adopts a conformation competent for SH3 domain binding.
description
2007 nî lūn-bûn
@nan
2007 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
name
The Abl SH2-kinase linker natu ...... petent for SH3 domain binding.
@ast
The Abl SH2-kinase linker natu ...... petent for SH3 domain binding.
@en
type
label
The Abl SH2-kinase linker natu ...... petent for SH3 domain binding.
@ast
The Abl SH2-kinase linker natu ...... petent for SH3 domain binding.
@en
prefLabel
The Abl SH2-kinase linker natu ...... petent for SH3 domain binding.
@ast
The Abl SH2-kinase linker natu ...... petent for SH3 domain binding.
@en
P2860
P356
P1433
P1476
The Abl SH2-kinase linker natu ...... petent for SH3 domain binding.
@en
P2093
Shugui Chen
Thomas E Smithgall
P2860
P304
P356
10.1110/PS.062631007
P577
2007-02-27T00:00:00Z