HER4-mediated biological and biochemical properties in NIH 3T3 cells. Evidence for HER1-HER4 heterodimers (Q24336345)

positive regulation of cell population proliferation

GOA release 2020-03-11

1 reference

GOA release 2020-03-11

author name string

B D Cohen

1

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J M Green

2

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L Foy

3

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H P Fell

Journal of Biological Chemistry

4

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publication date

1 March 1996

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language of work or name

English

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published in

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volume

271

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issue

9

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page(s)

4813-8

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cites work

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The bovine papillomavirus E5 transforming protein can stimulate the transforming activity of EGF and CSF-1 receptors

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Intermolecular association of the p185neu protein and EGF receptor modulates EGF receptor function

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A novel transforming protein (SHC) with an SH2 domain is implicated in mitogenic signal transduction

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SH2 domains recognize specific phosphopeptide sequences

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ARIA, a protein that stimulates acetylcholine receptor synthesis, is a member of the neu ligand family

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Dimerization of cell surface receptors in signal transduction

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Heterodimerization of the erbB-1 and erbB-2 receptors in human breast carcinoma cells: a mechanism for receptor transregulation

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Increased expression of the putative growth factor receptor p185HER2 causes transformation and tumorigenesis of NIH 3T3 cells

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Isolation and characterization of ERBB3, a third member of the ERBB/epidermal growth factor receptor family: evidence for overexpression in a subset of human mammary tumors

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HER4 expression correlates with cytotoxicity directed by a heregulin-toxin fusion protein

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erbB-2 is a potent oncogene when overexpressed in NIH/3T3 cells

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ErbB3 is involved in activation of phosphatidylinositol 3-kinase by epidermal growth factor

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Tumor promoter and epidermal growth factor stimulate phosphorylation of the c-erbB-2 gene product in MKN-7 human adenocarcinoma cells

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Epidermal Growth Factor

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