Ligand and p185c-neu density govern receptor interactions and tyrosine kinase activation.
about
The tumor suppressor RECK interferes with HER-2/Neu dimerization and attenuates its oncogenic signalingErk5 participates in neuregulin signal transduction and is constitutively active in breast cancer cells overexpressing ErbB2Trastuzumab, an appropriate first-line single-agent therapy for HER2-overexpressing metastatic breast cancerDominant-negative mutants of Grb2 induced reversal of the transformed phenotypes caused by the point mutation-activated rat HER-2/NeuConversion of a radioresistant phenotype to a more sensitive one by disabling erbB receptor signaling in human cancer cellsSignal transduction in mammary tumorigenesis: a transgenic perspective.Bivalence of EGF-like ligands drives the ErbB signaling networkOverexpression of ErbB2 in cancer and ErbB2-targeting strategies.Engagement of overexpressed Her2 with GEP100 induces autonomous invasive activities and provides a biomarker for metastases of lung adenocarcinoma.HER2/neu: mechanisms of dimerization/oligomerization.A kinase associated with chromatin that can be activated by ligand-p185c-Neu or epidermal growth factor-receptor interactions.ErbB2, but not ErbB1, reinitiates proliferation and induces luminal repopulation in epithelial aciniErbB2/Neu-induced, cyclin D1-dependent transformation is accelerated in p27-haploinsufficient mammary epithelial cells but impaired in p27-null cellsBiochemical evidence for the autophosphorylation and transphosphorylation of transforming growth factor beta receptor kinases.Growth factor-induced resistance to tamoxifen is associated with a mutation of estrogen receptor alpha and its phosphorylation at serine 305.Cooperation of the ErbB2 receptor and transforming growth factor beta in induction of migration and invasion in mammary epithelial cells.Laminin activates the p185HER2 oncoprotein and mediates growth inhibition of breast carcinoma cellsMolecular Mechanisms of Trastuzumab-Based Treatment in HER2-Overexpressing Breast CancerErbB2 and bone sialoprotein as markers for metastatic osteosarcoma cells.Mutations affecting conserved cysteine residues within the extracellular domain of Neu promote receptor dimerization and activation.Trastuzumab and doxorubicin-related cardiotoxicity and the cardioprotective role of exercise.Structural analysis of p185c-neu and epidermal growth factor receptor tyrosine kinases: oligomerization of kinase domainsPnck overexpression in HER-2 gene-amplified breast cancer causes Trastuzumab resistance through a paradoxical PTEN-mediated process.Comparison of the biochemical and kinetic properties of the type 1 receptor tyrosine kinase intracellular domains. Demonstration of differential sensitivity to kinase inhibitors.ErbB-2 amplification inhibits down-regulation and induces constitutive activation of both ErbB-2 and epidermal growth factor receptors.Mitosis-specific negative regulation of epidermal growth factor receptor, triggered by a decrease in ligand binding and dimerization, can be overcome by overexpression of receptor.ErbB-2 signaling is involved in regulating PSA secretion in androgen-independent human prostate cancer LNCaP C-81 cells.Heterogeneity of ERBB2 in gastric carcinomas: a study of tissue microarray and matched primary and metastatic carcinomas.Collagen-homology domain 1 deletion mutant of Shc suppresses transformation mediated by neu through a MAPK-independent pathway.
P2860
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P2860
Ligand and p185c-neu density govern receptor interactions and tyrosine kinase activation.
description
1994 nî lūn-bûn
@nan
1994 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի մարտին հրատարակված գիտական հոդված
@hy
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
name
Ligand and p185c-neu density govern receptor interactions and tyrosine kinase activation.
@ast
Ligand and p185c-neu density govern receptor interactions and tyrosine kinase activation.
@en
type
label
Ligand and p185c-neu density govern receptor interactions and tyrosine kinase activation.
@ast
Ligand and p185c-neu density govern receptor interactions and tyrosine kinase activation.
@en
prefLabel
Ligand and p185c-neu density govern receptor interactions and tyrosine kinase activation.
@ast
Ligand and p185c-neu density govern receptor interactions and tyrosine kinase activation.
@en
P2093
P2860
P356
P1476
Ligand and p185c-neu density govern receptor interactions and tyrosine kinase activation.
@en
P2093
P2860
P304
P356
10.1073/PNAS.91.5.1711
P407
P577
1994-03-01T00:00:00Z