Oncogenic activation of p185neu stimulates tyrosine phosphorylation in vivo
about
Heregulin-dependent regulation of HER2/neu oncogenic signaling by heterodimerization with HER3Constitutive activation of fibroblast growth factor receptor 3 by the transmembrane domain point mutation found in achondroplasiaThe erbB-2 mitogenic signaling pathway: tyrosine phosphorylation of phospholipase C-gamma and GTPase-activating protein does not correlate with erbB-2 mitogenic potencySpk1, a new kinase from Saccharomyces cerevisiae, phosphorylates proteins on serine, threonine, and tyrosine.Inhibition of eIF2alpha dephosphorylation inhibits ErbB2-induced deregulation of mammary acinar morphogenesisA chimeric EGF-R-neu proto-oncogene allows EGF to regulate neu tyrosine kinase and cell transformation.The epidermal growth factor receptor and the product of the neu protooncogene are members of a receptor tyrosine phosphorylation cascade.Activation of Neu (ErbB-2) mediated by disulfide bond-induced dimerization reveals a receptor tyrosine kinase dimer interface.Role of HER2 gene overexpression in breast carcinoma.Elevated expression of activated forms of Neu/ErbB-2 and ErbB-3 are involved in the induction of mammary tumors in transgenic mice: implications for human breast cancerA subdomain in the transmembrane domain is necessary for p185neu* activation.ErbB2 activation and signal transduction in normal and malignant mammary cells.Overexpression of the p185erB-2 tyrosine kinase growth factor receptor: control or chaos.Ligand-independent dimerization of oncogenic v-erbB products involves covalent interactions.Intrinsic signaling function of APP as a novel target of three V642 mutations linked to familial Alzheimer's disease.Functional assay for HER-2/neu demonstrates active signalling in a minority of HER-2/neu-overexpressing invasive human breast tumours.Transmembrane domain sequence requirements for activation of the p185c-neu receptor tyrosine kinase.ErbB2 is necessary for induction of carcinoma cell invasion by ErbB family receptor tyrosine kinases.PML suppresses oncogenic transformation of NIH/3T3 cells by activated neu.Oligomerization of epidermal growth factor receptors on A431 cells studied by time-resolved fluorescence imaging microscopy. A stereochemical model for tyrosine kinase receptor activation17 beta-estradiol mimics ligand activity of the c-erbB2 protooncogene product.Identification and characterization of a novel enhancer for the rat neu promoter.The juxtamembrane regions of the epidermal growth factor receptor and gp185erbB-2 determine the specificity of signal transduction.The carboxy-terminal domains of erbB-2 and epidermal growth factor receptor exert different regulatory effects on intrinsic receptor tyrosine kinase function and transforming activityTransformation of NIH 3T3 cells by overexpression of the normal coding sequence of the rat neu gene.Tyrosine phosphorylation is an early and specific event involved in primary keratinocyte differentiationMultiple cis- and trans-acting elements involved in regulation of the neu gene.Negative autoregulation of the neu gene is mediated by a novel enhancer.Adenovirus type 5 E1A gene products act as transformation suppressors of the neu oncogeneCarboxyl-terminal deletion and point mutations decrease the transforming potential of the activated rat neu oncogene product.Non-Ligand-Induced Dimerization is Sufficient to Initiate the Signalling and Endocytosis of EGF ReceptorThe role of HER2 in early breast cancer metastasis and the origins of resistance to HER2-targeted therapies.Antiserum raised against a synthetic phosphotyrosine-containing peptide selectively recognizes p185neu/erbB-2 and the epidermal growth factor receptor.Mutations affecting conserved cysteine residues within the extracellular domain of Neu promote receptor dimerization and activation.Characterization of a neu/c-erbB-2 protein-specific activating factorAgonistic antibodies stimulate the kinase encoded by the neu protooncogene in living cells but the oncogenic mutant is constitutively activeHER2-family signalling mechanisms, clinical implications and targeting in breast cancer.The transforming potential of the c-erbB-2 protein is regulated by its autophosphorylation at the carboxyl-terminal domain.Endocytosis deficiency of epidermal growth factor (EGF) receptor-ErbB2 heterodimers in response to EGF stimulation.Macrophage inhibitory cytokine-1 activates AKT and ERK-1/2 via the transactivation of ErbB2 in human breast and gastric cancer cells.
P2860
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P2860
Oncogenic activation of p185neu stimulates tyrosine phosphorylation in vivo
description
1988 nî lūn-bûn
@nan
1988年の論文
@ja
1988年論文
@yue
1988年論文
@zh-hant
1988年論文
@zh-hk
1988年論文
@zh-mo
1988年論文
@zh-tw
1988年论文
@wuu
1988年论文
@zh
1988年论文
@zh-cn
name
Oncogenic activation of p185neu stimulates tyrosine phosphorylation in vivo
@en
type
label
Oncogenic activation of p185neu stimulates tyrosine phosphorylation in vivo
@en
prefLabel
Oncogenic activation of p185neu stimulates tyrosine phosphorylation in vivo
@en
P2093
P2860
P356
P1476
Oncogenic activation of p185neu stimulates tyrosine phosphorylation in vivo
@en
P2093
P2860
P304
P356
10.1128/MCB.8.9.3969
P407
P577
1988-09-01T00:00:00Z