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Cited by 469

The DOI matches its Crossref record; 70 of the 70 references it cites were found in a registry or an index.

Signaling through focal adhesion kinase

Hanks, Steven K., Polte, Thomas R.·1997·BioEssays
DOI 10.1002/bies.950190208
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Abstract

Focal adhesion kinase (FAK) is a nonreceptor protein‐tyrosine kinase implicated in controlling cellular responses to the engagement of cell‐surface integrins, including cell spreading and migration, survival and proliferation. Aberrant FAK signaling may contribute to the process of cell transformation by certain oncoproteins, including v‐Src. Progress toward elucidating the events leading to FAK activation following integrin‐mediated cell adhesion, as well as events downstream of FAK, has come through the identification of FAK phosphorylation sites and interacting proteins. A signaling partnership is formed between FAK and Src‐family kinases, leading to tyrosine phosphorylation of FAK and associated ‘docking’ proteins Cas and paxillin. Subsequent recruitment of proteins containing Src homology 2 domains, including Grb2 and c‐Crk, to the complex is likely to trigger adhesion‐induced cellular responses, including changes to the actin cytoskeleton and activation of the Ras‐MAP kinase pathway.

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Crossref · 10.1002/bies.950190208

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Metadata

Authors
Hanks, S. K., & Polte, T. R.
Venue
BioEssays
Publisher
Wiley
Published
1997-02
Volume
19
Issue
2
Pages
137-145
ISSN
  • 0265-9247 (ISSN-L)
  • 1521-1878
DOI
10.1002/bies.950190208
OpenAlex
W2160839395
Cited by
469
References
70
FWCI
3.44
Type
journal article
Language
en
Open access
closed

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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.