A conserved protonation-dependent switch controls drug binding in the Abl kinase - Test2 - elhamkhani - TriplyDB

A conserved protonation-dependent switch controls drug binding in the Abl kinase

A conserved protonation-dependent switch controls drug binding in the Abl kinase

http://www.wikidata.org/entity/Q24657421

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Rational approaches to improving selectivity in drug design Exploration of type II binding mode: A privileged approach for kinase inhibitor focused drug discovery?Design principles underpinning the regulatory diversity of protein kinases Structural analysis of the catalytically inactive kinase domain of the human EGF receptor 3 Equally Potent Inhibition of c-Src and Abl by Compounds that Recognize Inactive Kinase Conformations Dynamics connect substrate recognition to catalysis in protein kinase A Structural and Spectroscopic Analysis of the Kinase Inhibitor Bosutinib and an Isomer of Bosutinib Binding to the Abl Tyrosine Kinase Domain Sequence Determinants of a Specific Inactive Protein Kinase Conformation Substrate and Inhibitor Specificity of the Type II p21-Activated Kinase, PAK6 A conserved water-mediated hydrogen bond network defines bosutinib's kinase selectivity The multiple nucleotide-divalent cation binding modes of Saccharomyces cerevisiae CK2α indicate a possible co-substrate hydrolysis product (ADP/GDP) release pathway Mechanisms 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 sensitivity The SH2 domain regulates c-Abl kinase activation by a cyclin-like mechanism and remodulation of the hinge motion Molecular Determinants Underlying Binding Specificities of the ABL Kinase Inhibitors: Combining Alanine Scanning of Binding Hot Spots with Network Analysis of Residue Interactions and Coevolution Towards a Molecular Understanding of the Link between Imatinib Resistance and Kinase Conformational Dynamics Divergent 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 function Protein kinases: evolution of dynamic regulatory proteins Hierarchical 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 flexibility Targeting 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 kinases Sequence and structure signatures of cancer mutation hotspots in protein kinases Computational insights for the discovery of non-ATP competitive inhibitors of MAP kinases Large 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 inhibitor Dynamic 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

http://www.wikidata.org/entity/Q24657421

description

2008 nî lūn-bûn

@nan

2008 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի դեկտեմբերին հրատարակված գիտական հոդված

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2008年の論文

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2008年論文

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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

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PNAS.0811223106

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Proceedings of the National Academy of Sciences of the United States of America

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A conserved protonation-dependent switch controls drug binding in the Abl kinase

@en

P2093

David E Shaw

http://www.w3.org/2001/XMLSchema#string

Filipp Frank

http://www.w3.org/2001/XMLSchema#string

Huafeng Xu

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Michael P Eastwood

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Morten Ø Jensen

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Ron O Dror

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Yibing Shan

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P2860

The protein kinase complement of the human genome

A census of human cancer genes

H++: a server for estimating pKas and adding missing hydrogens to macromolecules

A simple method for displaying the hydropathic character of a protein

Structural mechanism for STI-571 inhibition of abelson tyrosine kinase

Structural basis for the autoinhibition of c-Abl tyrosine kinase

Mutagenesis of p38alpha MAP kinase establishes key roles of Phe169 in function and structural dynamics and reveals a novel DFG-OUT state

Phosphotransferase and substrate binding mechanism of the cAMP-dependent protein kinase catalytic subunit from porcine heart as deduced from the 2.0 A structure of the complex with Mn2+ adenylyl imidodiphosphate and inhibitor peptide PKI(5-24)

Three-dimensional structure of the tyrosine kinase c-Src

Crystal structure of the Src family tyrosine kinase Hck

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139-144

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scholarly article

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546915

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10.1073/PNAS.0811223106

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1

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106

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Markus A Seeliger

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2008-12-24T00:00:00Z

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23699519

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19109437

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2610013

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