A conserved protonation-dependent switch controls drug binding in the Abl kinase
about
Rational approaches to improving selectivity in drug designExploration of type II binding mode: A privileged approach for kinase inhibitor focused drug discovery?Design principles underpinning the regulatory diversity of protein kinasesStructural analysis of the catalytically inactive kinase domain of the human EGF receptor 3Equally Potent Inhibition of c-Src and Abl by Compounds that Recognize Inactive Kinase ConformationsDynamics connect substrate recognition to catalysis in protein kinase AStructural and Spectroscopic Analysis of the Kinase Inhibitor Bosutinib and an Isomer of Bosutinib Binding to the Abl Tyrosine Kinase DomainSequence Determinants of a Specific Inactive Protein Kinase ConformationSubstrate and Inhibitor Specificity of the Type II p21-Activated Kinase, PAK6A conserved water-mediated hydrogen bond network defines bosutinib's kinase selectivityThe multiple nucleotide-divalent cation binding modes of Saccharomyces cerevisiae CK2α indicate a possible co-substrate hydrolysis product (ADP/GDP) release pathwayMechanisms of drug resistance in kinases.Structural insight into selectivity and resistance profiles of ROS1 tyrosine kinase inhibitors.Hotspot mutations in KIT receptor differentially modulate its allosterically coupled conformational dynamics: impact on activation and drug sensitivityThe SH2 domain regulates c-Abl kinase activation by a cyclin-like mechanism and remodulation of the hinge motionMolecular Determinants Underlying Binding Specificities of the ABL Kinase Inhibitors: Combining Alanine Scanning of Binding Hot Spots with Network Analysis of Residue Interactions and CoevolutionTowards a Molecular Understanding of the Link between Imatinib Resistance and Kinase Conformational DynamicsDivergent modulation of Src-family kinase regulatory interactions with ATP-competitive inhibitors.Substrate-specific reorganization of the conformational ensemble of CSK implicates novel modes of kinase functionProtein kinases: evolution of dynamic regulatory proteinsHierarchical modeling of activation mechanisms in the ABL and EGFR kinase domains: thermodynamic and mechanistic catalysts of kinase activation by cancer mutations.An aggregate analysis of many predicted structures to reduce errors in protein structure comparison caused by conformational flexibilityTargeting electrostatic interactions in accelerated molecular dynamics with application to protein partial unfolding.A transition path ensemble study reveals a linchpin role for Mg(2+) during rate-limiting ADP release from protein kinase A.Computational delineation of tyrosyl-substrate recognition and catalytic landscapes by the epidermal growth factor receptor tyrosine kinase domain.Molecular basis for pseudokinase-dependent autoinhibition of JAK2 tyrosine kinase.Conformational preference of ChaK1 binding peptides: a molecular dynamics study.Computational modeling of allosteric communication reveals organizing principles of mutation-induced signaling in ABL and EGFR kinases.The energy landscape analysis of cancer mutations in protein kinasesSequence and structure signatures of cancer mutation hotspots in protein kinasesComputational insights for the discovery of non-ATP competitive inhibitors of MAP kinasesLarge conformational changes in proteins: signaling and other functions.Mechanism of the Association Pathways for a Pair of Fast and Slow Binding Ligands of HIV-1 Protease.Use of allostery to identify inhibitors of calmodulin-induced activation of Bacillus anthracis edema factor.Predicting inactive conformations of protein kinases using active structures: conformational selection of type-II inhibitors.Conformational Transition Pathways of Epidermal Growth Factor Receptor Kinase Domain from Multiple Molecular Dynamics Simulations and Bayesian Clustering.Characterization of the Src/Abl hybrid kinase SmTK6 of Schistosoma mansoni.Binding free energy calculation with QM/MM hybrid methods for Abl-Kinase inhibitorDynamic architecture of a protein kinase.Engineering of an epoxide hydrolase for efficient bioresolution of bulky pharmaco substrates.
P2860
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P2860
A conserved protonation-dependent switch controls drug binding in the Abl kinase
description
2008 nî lūn-bûn
@nan
2008 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
A conserved protonation-dependent switch controls drug binding in the Abl kinase
@ast
A conserved protonation-dependent switch controls drug binding in the Abl kinase
@en
A conserved protonation-dependent switch controls drug binding in the Abl kinase
@nl
type
label
A conserved protonation-dependent switch controls drug binding in the Abl kinase
@ast
A conserved protonation-dependent switch controls drug binding in the Abl kinase
@en
A conserved protonation-dependent switch controls drug binding in the Abl kinase
@nl
prefLabel
A conserved protonation-dependent switch controls drug binding in the Abl kinase
@ast
A conserved protonation-dependent switch controls drug binding in the Abl kinase
@en
A conserved protonation-dependent switch controls drug binding in the Abl kinase
@nl
P2093
P2860
P3181
P356
P1476
A conserved protonation-dependent switch controls drug binding in the Abl kinase
@en
P2093
David E Shaw
Filipp Frank
Huafeng Xu
Michael P Eastwood
Morten Ø Jensen
Ron O Dror
Yibing Shan
P2860
P304
P3181
P356
10.1073/PNAS.0811223106
P407
P577
2008-12-24T00:00:00Z