Targeting the SH2-Kinase Interface in Bcr-Abl Inhibits Leukemogenesis - Test2 - elhamkhani - TriplyDB

Targeting the SH2-Kinase Interface in Bcr-Abl Inhibits Leukemogenesis

Targeting the SH2-Kinase Interface in Bcr-Abl Inhibits Leukemogenesis

http://www.wikidata.org/entity/Q27675049

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Identification of protein interactions involved in cellular signaling The Philadelphia chromosome in leukemogenesis The growing arsenal of ATP-competitive and allosteric inhibitors of BCR-ABL Dissection of the BCR-ABL signaling network using highly specific monobody inhibitors to the SHP2 SH2 domains Adhiron: a stable and versatile peptide display scaffold for molecular recognition applications Crystal structure of an SH2-kinase construct of c-Abl and effect of the SH2 domain on kinase activity Nanobodies and recombinant binders in cell biology Why modules matter Role of ABL family kinases in cancer: from leukaemia to solid tumours An evolutionarily conserved synthetic lethal interaction network identifies FEN1 as a broad-spectrum target for anticancer therapeutic development The SH2 domain regulates c-Abl kinase activation by a cyclin-like mechanism and remodulation of the hinge motion ETO family protein Mtgr1 mediates Prdm14 functions in stem cell maintenance and primordial germ cell formation Directed Evolution of a Highly Specific FN3 Monobody to the SH3 Domain of Human Lyn Tyrosine Kinase.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.Two-state dynamics of the SH3-SH2 tandem of Abl kinase and the allosteric role of the N-cap Intramolecular dynamics within the N-Cap-SH3-SH2 regulatory unit of the c-Abl tyrosine kinase reveal targeting to the cellular membrane Misfolding, Aggregation, and Disordered Segments in c-Abl and p53 in Human Cancer.Monobodies and other synthetic binding proteins for expanding protein science Selective Targeting of SH2 Domain-Phosphotyrosine Interactions of Src Family Tyrosine Kinases with Monobodies.Affimer proteins are versatile and renewable affinity reagents Delivery of antibodies to the cytosol: debunking the myths.Structural insights for engineering binding proteins based on non-antibody scaffolds Streamlining the Pipeline for Generation of Recombinant Affinity Reagents by Integrating the Affinity Maturation Step.Delivery of antibody mimics into mammalian cells via anthrax toxin protective antigen Modular evolution of phosphorylation-based signalling systems.Phosphotyrosine recognition domains: the typical, the atypical and the versatile.Crk and ABI1: binary molecular switches that regulate abl tyrosine kinase and signaling to the cytoskeleton.Structure, regulation, signaling, and targeting of abl kinases in cancer.Structure and dynamic regulation of Abl kinases.Allosteric Inhibition of Bcr-Abl Kinase by High Affinity Monobody Inhibitors Directed to the Src Homology 2 (SH2)-Kinase Interface Mutations of FLT3/ITD confer resistance to multiple tyrosine kinase inhibitors.Combining biophysical methods to analyze the disulfide bond in SH2 domain of C-terminal Src kinase.Mechanisms and novel approaches in overriding tyrosine kinase inhibitor resistance in chronic myeloid leukemia.Molecular mechanisms of SH2- and PTB-domain-containing proteins in receptor tyrosine kinase signaling.Introduction: History of SH2 Domains and Their Applications.Understanding the cellular roles of Fyn-related kinase (FRK): implications in cancer biology.Systems-pharmacology dissection of a drug synergy in imatinib-resistant CML.BCR-ABL1 kinase: hunting an elusive target with new weapons The other Achilles' heel of BCR-ABL1.

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Targeting the SH2-Kinase Interface in Bcr-Abl Inhibits Leukemogenesis

http://www.wikidata.org/entity/Q27675049

description

2011 nî lūn-bûn

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2011 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի հոտեմբերին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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name

Targeting the SH2-Kinase Interface in Bcr-Abl Inhibits Leukemogenesis

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Targeting the SH2-Kinase Interface in Bcr-Abl Inhibits Leukemogenesis

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Targeting the SH2-Kinase Interface in Bcr-Abl Inhibits Leukemogenesis

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type

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Targeting the SH2-Kinase Interface in Bcr-Abl Inhibits Leukemogenesis

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Targeting the SH2-Kinase Interface in Bcr-Abl Inhibits Leukemogenesis

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Targeting the SH2-Kinase Interface in Bcr-Abl Inhibits Leukemogenesis

@nl

prefLabel

Targeting the SH2-Kinase Interface in Bcr-Abl Inhibits Leukemogenesis

@ast

Targeting the SH2-Kinase Interface in Bcr-Abl Inhibits Leukemogenesis

@en

Targeting the SH2-Kinase Interface in Bcr-Abl Inhibits Leukemogenesis

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J.CELL.2011.08.046

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Targeting the SH2-Kinase Interface in Bcr-Abl Inhibits Leukemogenesis

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Arkadiusz M Wyrzucki

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Gerald D Gish

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Hartmut Beug

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Peter Valent

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The Grb2 binding site is required for the induction of chronic myeloid leukemia-like disease in mice by the Bcr/Abl tyrosine kinase

Controlling protein association and subcellular localization with a synthetic ligand that induces heterodimerization of proteins

A noncatalytic domain conserved among cytoplasmic protein-tyrosine kinases modifies the kinase function and transforming activity of Fujinami sarcoma virus P130gag-fps

Structural coupling of SH2-kinase domains links Fes and Abl substrate recognition and kinase activation

MolProbity: all-atom contacts and structure validation for proteins and nucleic acids

Structural mechanism for STI-571 inhibition of abelson tyrosine kinase

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Oliver Hantschel

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