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Article

Domain-specific interactions between the p185(neu) and epidermal growth factor receptor kinases determine differential signaling outcomes.

The Journal of biological chemistry - 8 Jan 1999

Qian X, O'Rourke D M, Fei Z, Zhang H T, Kao C C, Greene M I

Abstract excerpt

We expressed the epidermal growth factor receptor (EGFR) along with mutant p185(neu) proteins containing the rat transmembrane point mutation. The work concerned the study of the contributions made by various p185(neu) subdomains to signaling induced by a heterodimeric ErbB complex. Co-expression of full-length EGFR and oncogenic p185(neu) receptors resulted in an increased EGF-induced phosphotyrosine content of...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 9872991
DOI: 10.1074/jbc.274.2.574

Genes

EGFR
EGF

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Domain-specific interactions between the p185(neu) and epidermal growth factor receptor kinases determine differential signaling outcomes.PMID 9872991Read ↗

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Identification of p185neu sequences required for monoclonal antibody- or ligand-mediated receptor signal attenuation.Semantic proximity Read ↗

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GM3 content modulates the EGF-activated p185c-neu levels, but not those of the constitutively activated oncoprotein p185neu.Semantic proximity Read ↗

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Activity and cellular localization of an oncogenic glioblastoma multiforme-associated EGF receptor mutant possessing a duplicated kinase domain.Semantic proximity Read ↗

EGFR phosphorylates tumor-derived EGFRvIII driving STAT3/5 and progression in glioblastoma.Semantic proximity Read ↗

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Analysis of deletions of the carboxyl terminus of the epidermal growth factor receptor reveals self-phosphorylation at tyrosine 992 and enhanced in vivo tyrosine phosphorylation of cell substrates.Semantic proximity Read ↗

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