Binding or bending: distinction of allosteric Abl kinase agonists from antagonists by an NMR-based conformational assay
about
Ten things you should know about protein kinases: IUPHAR Review 14Crystal Structures of ABL-Related Gene (ABL2) in Complex with Imatinib, Tozasertib (VX-680), and a Type I Inhibitor of the Triazole Carbothioamide ClassHydrophobic Core Variations Provide a Structural Framework for Tyrosine Kinase Evolution and Functional SpecializationNMR reveals the allosteric opening and closing of Abelson tyrosine kinase by ATP-site and myristoyl pocket inhibitors.Detection of secondary binding sites in proteins using fragment screeningAssay development and high-throughput screening of small molecular c-Abl kinase activators.Structure-guided optimization of small molecule c-Abl activatorsTwenty years on: the impact of fragments on drug discovery.SPLINTS: small-molecule protein ligand interface stabilizers.Moving Beyond Active-Site Detection: MixMD Applied to Allosteric Systems.Biophysics: for HTS hit validation, chemical lead optimization, and beyond.The impact of structural biology in medicine illustrated with four case studies.Novel approaches for targeting kinases: allosteric inhibition, allosteric activation and pseudokinases.Isotope labeling in insect cells.(E)-(2-Chloro-benzyl-idene)amino 2-amino-4-chloro-benzoate.Allosteric BCR-ABL inhibitors in Philadelphia chromosome-positive acute lymphoblastic leukemia: novel opportunities for drug combinations to overcome resistance.Synthesis, kinetic studies and molecular modeling of novel tacrine dimers as cholinesterase inhibitors.Current NMR Techniques for Structure-Based Drug Discovery.Acceleration of protein backbone NMR assignment by combinatorial labeling: Application to a small molecule binding study.The allosteric inhibitor ABL001 enables dual targeting of BCR-ABL1.Biosensor-based approach to the identification of protein kinase ligands with dual-site modes of action.19F-NMR-Based Dual-Site Reporter Assay for the Discovery and Distinction of Catalytic and Allosteric Kinase Inhibitors.Allosterische Kinaseinhibitoren
P2860
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P2860
Binding or bending: distinction of allosteric Abl kinase agonists from antagonists by an NMR-based conformational assay
description
2010 nî lūn-bûn
@nan
2010 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Binding or bending: distinctio ...... NMR-based conformational assay
@ast
Binding or bending: distinctio ...... NMR-based conformational assay
@en
Binding or bending: distinctio ...... NMR-based conformational assay
@nl
type
label
Binding or bending: distinctio ...... NMR-based conformational assay
@ast
Binding or bending: distinctio ...... NMR-based conformational assay
@en
Binding or bending: distinctio ...... NMR-based conformational assay
@nl
prefLabel
Binding or bending: distinctio ...... NMR-based conformational assay
@ast
Binding or bending: distinctio ...... NMR-based conformational assay
@en
Binding or bending: distinctio ...... NMR-based conformational assay
@nl
P2093
P356
P1476
Binding or bending: distinctio ...... NMR-based conformational assay
@en
P2093
Andreas L Marzinzik
André Strauss
Doriano Fabbro
Gabriele Fendrich
Jürgen Mestan
Pascal Furet
Robert M Grotzfeld
Sandra W Cowan-Jacob
Simona Cotesta
Wolfgang Jahnke
P304
P356
10.1021/JA101837N
P407
P577
2010-05-26T00:00:00Z