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- W181586561 endingPage "55" @default.
- W181586561 startingPage "37" @default.
- W181586561 abstract "Cellular interactions with extracellular matrix (ECM) play important roles in many biological processes such as embryonic development and morphogenesis, wound healing, and malignant transformation. The major cell surface receptors for ECM are the integrin family cell adhesion molecules which are composed of noncovalently associated α and ß subunits (Hynes 1992). Both α and ß subunits are transmembrane proteins containing short cytoplasmic domains that can interact directly or indirectly with cytoskeletal proteins such as talin, vinculin, α-actinin, and filamin (Burridge et al. 1992; Hynes 1992). Besides serving as a linker between ECM and cytoskeleton, integrins have been shown to mediate biochemical signal transduction across the plasma membrane to regulate various cellular functions (Juliano and Haskill 1993; Clark and Brugge 1995; Schwartz et al. 1995). Integrin-mediated cell adhesion can regulate gene expression, intracellular pH and calcium, phospholipid metabolites, small GTPase, protein serine/threonine kinases, and protein tyrosine phosphorylation. Since integrins have short cytoplasmic domains with no enzymatic activities, it is believed that coupling of the integrin cytoplasmic domains with cytoplasmic tyrosine kinases, phosphatases, and adaptor molecules are critical in initiating multiple intracellular signaling pathways mediated by integrins (Clark and Brugge 1995; Juliano and Haskill 1993; Schwartz et al. 1995)." @default.
- W181586561 created "2016-06-24" @default.
- W181586561 creator A5030957947 @default.
- W181586561 creator A5042839840 @default.
- W181586561 date "2000-01-01" @default.
- W181586561 modified "2023-10-11" @default.
- W181586561 title "Role of Focal Adhesion Kinase in Signaling by the Extracellular Matrix" @default.
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