Her4 and Her2/neu tyrosine kinase domains dimerize and activate in a reconstituted in vitro system
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Orchestration of ErbB3 signaling through heterointeractions and homointeractions.Structural Analysis of the Mechanism of Inhibition and Allosteric Activation of the Kinase Domain of HER2 ProteinActivating HER2 mutations in HER2 gene amplification negative breast cancerHER2 activating mutations are targets for colorectal cancer treatmentErbB polymorphisms: insights and implications for response to targeted cancer therapeuticsPhosphoproteomics of collagen receptor networks reveals SHP-2 phosphorylation downstream of wild-type DDR2 and its lung cancer mutantsEvidence for intermolecular interactions between the intracellular domains of the arabidopsis receptor-like kinase ACR4, its homologs and the Wox5 transcription factorComputational modeling of allosteric communication reveals organizing principles of mutation-induced signaling in ABL and EGFR kinases.A highly efficient peptide substrate for EGFR activates the kinase by inducing aggregationActivation of human VPS4A by ESCRT-III proteins reveals ability of substrates to relieve enzyme autoinhibition.Carboxyl-group footprinting maps the dimerization interface and phosphorylation-induced conformational changes of a membrane-associated tyrosine kinase.Catalytic control in the EGF receptor and its connection to general kinase regulatory mechanisms.Regulation of the catalytic activity of the EGF receptor.Mechanics of EGF receptor/ErbB2 kinase activation revealed by luciferase fragment complementation imaging.Structural analysis of the EGFR/HER3 heterodimer reveals the molecular basis for activating HER3 mutationsNeuregulin-4 is a survival factor for colon epithelial cells both in culture and in vivoStructural Basis for the Non-catalytic Functions of Protein Kinases.HER2 stabilizes EGFR and itself by altering autophosphorylation patterns in a manner that overcomes regulatory mechanisms and promotes proliferative and transformation signaling.Synergistic activation of p21-activated kinase 1 by phosphatidylinositol 4,5-bisphosphate and Rho GTPasesHER family kinase domain mutations promote tumor progression and can predict response to treatment in human breast cancer.Carboxyl group footprinting mass spectrometry and molecular dynamics identify key interactions in the HER2-HER3 receptor tyrosine kinase interface.Expression of HER2 in Breast Cancer Promotes a Massive Reorganization of Gene Activity and Suggests a Role for Epigenetic RegulationDestabilization of the epidermal growth factor receptor (EGFR) by a peptide that inhibits EGFR binding to heat shock protein 90 and receptor dimerization.Phosphoproteomic analysis identifies activated MET-axis PI3K/AKT and MAPK/ERK in lapatinib-resistant cancer cell line.Evaluation of the antitumor activity of dacomitinib in models of human bladder cancerTargeting of preexisting and induced breast cancer stem cells with trastuzumab and trastuzumab emtansine (T-DM1).Molecular dynamics simulations of transitions for ECD epidermal growth factor receptors show key differences between human and drosophila forms of the receptors.Activating ERBB4 mutations in non-small cell lung cancer.EGF and NRG induce phosphorylation of HER3/ERBB3 by EGFR using distinct oligomeric mechanisms.A comprehensive review of heregulins, HER3, and HER4 as potential therapeutic targets in cancer.Biophysical Evidence for Intrinsic Disorder in the C-terminal Tails of the Epidermal Growth Factor Receptor (EGFR) and HER3 Receptor Tyrosine Kinases.
P2860
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P2860
Her4 and Her2/neu tyrosine kinase domains dimerize and activate in a reconstituted in vitro system
description
2009 nî lūn-bûn
@nan
2009 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Her4 and Her2/neu tyrosine kin ...... reconstituted in vitro system
@ast
Her4 and Her2/neu tyrosine kin ...... reconstituted in vitro system
@en
type
label
Her4 and Her2/neu tyrosine kin ...... reconstituted in vitro system
@ast
Her4 and Her2/neu tyrosine kin ...... reconstituted in vitro system
@en
prefLabel
Her4 and Her2/neu tyrosine kin ...... reconstituted in vitro system
@ast
Her4 and Her2/neu tyrosine kin ...... reconstituted in vitro system
@en
P2093
P2860
P356
P1476
Her4 and Her2/neu tyrosine kin ...... reconstituted in vitro system
@en
P2093
John Monsey
Paul Schlesinger
P2860
P304
P356
10.1074/JBC.M109.096032
P407
P577
2009-12-18T00:00:00Z