Nanopublications

Matches in Nanopublications for { ?s ?p ?o <http://www.tkuhn.ch/bel2nanopub/RAF_xfMmBY66bLtozWG38kBbLIppOBIwedG6SX1nkPrd8#provenance>. }

Showing items 1 to 11 of 11 with 100 items per page.

_9 label "Selventa" provenance.
_8 value "The expression and action of integrins are predominantly localized to the focal adhesion complex as originally demonstrated in fibroblasts. Focal adhesion complexes are the structural connection between the ECM and the cytoskeleton. Here, transmembrane signaling is mediated by integrins that cluster with dozens of cytoskeletal proteins and signaling molecules. Interestingly, integrins not only convey signals from the ECM into the cell (outside-in), but also react to cytoplasmic alterations by altering their capability to adhere to the ECM (inside-out). After collagen-activation of integrins, the incoming signal is translated into increased tyrosine phosphorylation. Unlike the DDR, which have an intrinsic catalytic activity, integrins recruit cytoplasmic tyrosine kinases, in particular focal adhesion kinase (FAK), a 125 kDa multi-domain protein. The beta1 integrin cytoplasmic tail interacts with paxillin and talin, which both complex FAK [75]. The detailed mechanism, how FAK interacts with these proteins and becomes activated in response to integrin ligation, is not fully understood. It is clear that the autophosphorylation of FAK at several tyrosine residues enables the kinase to phosphorylate a number of other, mainly cytoskeletal proteins, including paxillin, talin, alpha-actinin, tensin, zyxin, VASP and vinculin." provenance.
_8 wasQuotedFrom 11701397 provenance.
assertion hadPrimarySource 11701397 provenance.
large_corpus.bel title "BEL Framework Large Corpus Document" provenance.
large_corpus.bel description "Approximately 61,000 statements." provenance.
assertion wasDerivedFrom large_corpus.bel provenance.
assertion wasDerivedFrom _8 provenance.
large_corpus.bel authoredBy _9 provenance.
large_corpus.bel version "20131211" provenance.