Cargando…
Integrin-dependent phosphorylation and activation of the protein tyrosine kinase pp125FAK in platelets
We have investigated mechanisms involved in integrin-mediated signal transduction in platelets by examining integrin-dependent phosphorylation and activation of a newly identified protein tyrosine kinase, pp125FAK (FAK, focal adhesion kinase). This kinase was previously shown to be localized in foca...
Formato: | Texto |
---|---|
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
1992
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2289696/ https://www.ncbi.nlm.nih.gov/pubmed/1385445 |
Ejemplares similares
-
Adhesive ligand binding to integrin alpha IIb beta 3 stimulates tyrosine phosphorylation of novel protein substrates before phosphorylation of pp125FAK
Publicado: (1993) -
T cell receptor- and beta 1 integrin-mediated signals synergize to induce tyrosine phosphorylation of focal adhesion kinase (pp125FAK) in human T cells
Publicado: (1995) -
Tyrosine phosphorylation of paxillin and pp125FAK accompanies cell adhesion to extracellular matrix: a role in cytoskeletal assembly
Publicado: (1992) -
Direct association of pp125FAK with paxillin, the focal adhesion- targeting mechanism of pp125FAK
Publicado: (1995) -
Beta 2 integrin-dependent protein tyrosine phosphorylation and activation of the FGR protein tyrosine kinase in human neutrophils
Publicado: (1994)