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Article

Grb2 and Shc adapter proteins play distinct roles in Neu (ErbB-2)-induced mammary tumorigenesis: implications for human breast cancer.

Molecular and cellular biology - 1 Mar 2001

Dankort D, Maslikowski B, Warner N, Kanno N, Kim H, Wang Z, Moran M F, Oshima R G, Cardiff R D, Muller W J

Abstract excerpt

Amplification of the Neu (ErbB-2 or HER-2) receptor tyrosine kinase occurs in 20 to 30% of human mammary carcinomas, correlating with a poor clinical prognosis. We have previously demonstrated that four (Y1144 Y1201, Y1227 and Y1253) of the five known Neu autophosphorylation sites can independently mediate transforming signals. The transforming potential of two of these mutants correlates with their capacity to...

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

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Identifiers

PMID: 11238891
DOI: 10.1128/MCB.21.5.1540-1551.2001
PMCID: PMC86700

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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.

Related research

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Research trail→

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Grb2 and Shc adapter proteins play distinct roles in Neu (ErbB-2)-induced mammary tumorigenesis: implications for human breast cancer.PMID 11238891Read ↗

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Multiple ErbB-2/Neu Phosphorylation Sites Mediate Transformation through Distinct Effector Proteins.Semantic proximity Read ↗

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Grb7, a Critical Mediator of EGFR/ErbB Signaling, in Cancer Development and as a Potential Therapeutic TargetSemantic proximity Read ↗

Amplification of the <i>neu/erbB-2</i> oncogene in a mouse model of mammary tumorigenesisSemantic proximity Read ↗

A role for the scaffolding adapter GAB2 in breast cancer.Semantic proximity Read ↗

c-Src associates with ErbB2 through an interaction between catalytic domains and confers enhanced transforming potential.Semantic proximity Read ↗

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