Allosteric inhibitors of Bcr-abl-dependent cell proliferation. - Wikidata - awgldk - TriplyDB

Allosteric inhibitors of Bcr-abl-dependent cell proliferation.

Allosteric inhibitors of Bcr-abl-dependent cell proliferation.

http://www.wikidata.org/entity/Q33231742

about

Quantitative analysis of HSP90-client interactions reveals principles of substrate recognition ABL tyrosine kinases: evolution of function, regulation, and specificity c-Abl phosphorylates α-synuclein and regulates its degradation: implication for α-synuclein clearance and contribution to the pathogenesis of Parkinson's disease Allosteric inhibition of the nonMyristoylated c-Abl tyrosine kinase by phosphopeptides derived from Abi1/Hssh3bp1 Highly specific, bisubstrate-competitive Src inhibitors from DNA-templated macrocycles Molecular mechanisms for survival regulation of chronic myeloid leukemia stem cells Ten things you should know about protein kinases: IUPHAR Review 14 Targeting cancer with kinase inhibitors The growing arsenal of ATP-competitive and allosteric inhibitors of BCR-ABL Current concepts in pediatric Philadelphia chromosome-positive acute lymphoblastic leukemia Abl Kinases Regulate HGF/Met Signaling Required for Epithelial Cell Scattering, Tubulogenesis and Motility Targeting Bcr–Abl by combining allosteric with ATP-binding-site inhibitors Crystal Structures of ABL-Related Gene (ABL2) in Complex with Imatinib, Tozasertib (VX-680), and a Type I Inhibitor of the Triazole Carbothioamide Class Mechanisms of drug resistance in kinases.The function of phosphatidylinositol 5-phosphate 4-kinase γ (PI5P4Kγ) explored using a specific inhibitor that targets the PI5P-binding site Role of ABL family kinases in cancer: from leukaemia to solid tumours Allosteric interactions between the myristate- and ATP-site of the Abl kinase Identification of small molecules that disrupt signaling between ABL and its positive regulator RIN1 Fluorescence Polarization Screening Assays for Small Molecule Allosteric Modulators of ABL Kinase Function Defying c-Abl signaling circuits through small allosteric compounds.NMR reveals the allosteric opening and closing of Abelson tyrosine kinase by ATP-site and myristoyl pocket inhibitors.Enhanced SH3/linker interaction overcomes Abl kinase activation by gatekeeper and myristic acid binding pocket mutations and increases sensitivity to small molecule inhibitors The Abl SH2-kinase linker naturally adopts a conformation competent for SH3 domain binding.Activation state-selective kinase inhibitor assay based on ion mobility-mass spectrometry Misfolding, Aggregation, and Disordered Segments in c-Abl and p53 in Human Cancer.Insights into protein kinase regulation and inhibition by large scale structural comparison Detection of secondary binding sites in proteins using fragment screening 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 Emerging drugs for chronic myeloid leukemia.Assay development and high-throughput screening of small molecular c-Abl kinase activators.Small molecule probes of cellular pathways and networks.Seven transmembrane receptors as shapeshifting proteins: the impact of allosteric modulation and functional selectivity on new drug discovery.A type-II kinase inhibitor capable of inhibiting the T315I "gatekeeper" mutant of Bcr-Abl.A Non-ATP-Competitive Dual Inhibitor of JAK2 and BCR-ABL Kinases: Elucidation of a Novel Therapeutic Spectrum Based on Substrate Competitive Inhibition.Myristoylation and membrane binding regulate c-Src stability and kinase activity Imaging the intracellular distribution of tyrosine kinase inhibitors in living cells with quantitative hyperspectral stimulated Raman scattering Allosteric inhibition enhances the efficacy of ABL kinase inhibitors to target unmutated BCR-ABL and BCR-ABL-T315I Overcoming Chemical, Biological, and Computational Challenges in the Development of Inhibitors Targeting Protein-Protein Interactions.Overcoming Bcr-Abl T315I mutation by combination of GNF-2 and ATP competitors in an Abl-independent mechanism.

P2860

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P2860

Allosteric inhibitors of Bcr-abl-dependent cell proliferation.

http://www.wikidata.org/entity/Q33231742

description

2006 nî lūn-bûn

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2006 թուականի Յունուարին հրատարակուած գիտական յօդուած

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2006 թվականի հունվարին հրատարակված գիտական հոդված

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2006年の論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年论文

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name

Allosteric inhibitors of Bcr-abl-dependent cell proliferation.

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Allosteric inhibitors of Bcr-abl-dependent cell proliferation.

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type

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Allosteric inhibitors of Bcr-abl-dependent cell proliferation.

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Allosteric inhibitors of Bcr-abl-dependent cell proliferation.

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prefLabel

Allosteric inhibitors of Bcr-abl-dependent cell proliferation.

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Allosteric inhibitors of Bcr-abl-dependent cell proliferation.

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Nature Chemical Biology

P1476

Allosteric inhibitors of Bcr-abl-dependent cell proliferation.

@en

P2093

Anastasia Velentza

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

Christine Sloan

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Doriano Fabbro

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

Francisco J Adrián

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

Guobao Zhang

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

Jürgen Mestan

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

Nathanael S Gray

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

Paul Manley

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

Qiang Ding

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

Sheng Ding

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P2888

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95-102

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scholarly article

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10.1038/NCHEMBIO760

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2

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2

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2006-01-15T00:00:00Z

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7356263

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16415863

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allosteric inhibitor