Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The c-Src tyrosine kinase associates with the catalytic domain of ErbB-2: implications for ErbB-2 mediated signaling and transformation.

Oncogene - 17 Nov 2005

Kim Harold, Chan Richard, Dankort David L, Zuo Dongmei, Najoukas Monica, Park Morag, Muller William J

Abstract excerpt

c-Src associates with and is activated by the ErbB-2 receptor tyrosine kinase, but is unable to bind the EGFR. Although c-Src has been found to interact directly and specifically with the ErbB-2 receptor, the significance of this interaction is unclear. Using both chimeric receptor and site-directed mutagenesis approaches, the region of interaction of c-Src on ErbB-2 was identified. Significantly, EGFR could be...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Catalytic Domain
Share to Cell Polarity

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

Share to CSK Tyrosine-Protein Kinase

Share to Focal Adhesions

Share to Kidney

Share to Protein-Tyrosine Kinases

Share to Receptor, ErbB-2

Share to src-Family Kinases

Source

Identifiers

PMID: 16170374
DOI: 10.1038/sj.onc.1208898

Genes

EGFR

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.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The c-Src tyrosine kinase associates with the catalytic domain of ErbB-2: implications for ErbB-2 mediated signaling and transformation.PMID 16170374Read ↗

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

Modeling Breast Cancer–Associated c-Src and EGFR Overexpression in Human MECs: c-Src and EGFR Cooperatively Promote Aberrant Three-dimensional Acinar Structure and Invasive BehaviorSemantic proximity Read ↗

Src promotes destruction of c-Cbl: Implications for oncogenic synergy between Src and growth factor receptorsSemantic proximity Read ↗

Distinct tyrosine autophosphorylation sites mediate induction of epithelial mesenchymal like transition by an activated ErbB-2/Neu receptor.Semantic proximity Read ↗

Src family kinases, adaptor proteins and the actin cytoskeleton in epithelial-to-mesenchymal transitionSemantic proximity Read ↗

The role of Src in solid and hematologic malignancies: development of new-generation Src inhibitors.Semantic proximity Read ↗

Functional dissection of transformation by c‐Src and v‐SrcSemantic proximity Read ↗

SRC: Regulation, Role in Human Carcinogenesis and Pharmacological InhibitorsSemantic proximity Read ↗

The SRC-induced mesenchymal state in late-stage colon cancer cells.Semantic proximity Read ↗

Epidermal growth factor-induced activation and translocation of c-Src to the cytoskeleton depends on the actin binding domain of the EGF-receptor.Semantic proximity Read ↗

Oncogenic Src requires a wild-type counterpart to regulate invadopodia maturationSemantic proximity Read ↗

Increased oncogenic potential of ErbB is associated with the loss of a COOH-terminal domain serine phosphorylation site.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.