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- W2110930216 abstract "Focal adhesion kinase (FAK) has received much attention as a transducer of integrin-mediated signals. FAK becomes autophosphorylated on tyrosine 397 (Y397) in response to cell adhesion to the extracellular matrix (ECM) and in response to certain growth factors. Src-family kinases bind to FAK Y397 and mediate the phosphorylation of several additional tyrosine residues located within FAK. This leads to an enhancement of FAK activity and the recruitment of Grb2-SOS to the FAK signalling complex with subsequent activation of the Ras/ERK growth pathway in some cell types. Other signalling molecules such as Crk-associated substrate, Crk and paxillin can physically associate with FAK in response to adhesion to the ECM. FAK also seems to mediate cell migration and cell survival. Evidence obtained from several laboratories demonstrates that FAK is overexpressed in a variety of human cancers. FAK is not a classical oncogene and its overexpression appears to be a relatively late change in tumour progression. Because..." @default.
- W2110930216 created "2016-06-24" @default.
- W2110930216 creator A5029337682 @default.
- W2110930216 date "2000-04-01" @default.
- W2110930216 modified "2023-09-27" @default.
- W2110930216 title "Focal adhesion kinase in cancer" @default.
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- W2110930216 doi "https://doi.org/10.1517/14728222.4.2.191" @default.
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