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dc.contributor.authorAbbi, S.es
dc.contributor.authorGuan, J.L.es
dc.date.accessioned2011-05-11T10:59:00Z-
dc.date.available2011-05-11T10:59:00Z-
dc.date.issued2002-
dc.identifier.issn0213-3911es
dc.identifier.urihttp://hdl.handle.net/10201/20844-
dc.description.abstractIntegrin-mediated cell adhesion to extracellular matrix (ECM) plays important roles in a variety of biological processes. Recent studies suggested that integrins mediate signal transduction across the plasma membrane via activating several intracellular signaling pathways. Focal adhesion kinase (FAK) is a non-receptor tyrosine kinase that has been shown to be a major mediator of integrin signal transduction pathways. Upon activation by integrins, FAK undergoes autophosphorylation as well as associations with several other intracellular signaling molecules. These interactions in the signaling pathways have been shown to regulation a variety of cellular functions such as cell spreading, migration, cell proliferation, apoptosis and cell survival. Recent progress in the understanding of FAK interactions with other proteins in the regulation of these cellular functions will be discussed in this reviewes
dc.formatapplication/pdfes
dc.format.extent9es
dc.languageenges
dc.publisherMurcia : F. Hernándezes
dc.relation.ispartofHistology and histopathologyes
dc.rightsinfo:eu-repo/semantics/openAccesses
dc.subjectIntegrinses
dc.subjectFocal adhesion kinase (FAK)es
dc.subject.otherCDU::6 - Ciencias aplicadas::61 - Medicinaes
dc.titleFocal adhesion kinase: Protein interactions and cellular functionses
dc.typeinfo:eu-repo/semantics/articlees
Aparece en las colecciones:Vol.17, nº 4 (2002)

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