Focal adhesion kinase (p125FAK): A point of convergence in the action of neuropeptides, integrins, and oncogenes
Authors:
- Enrique RozengurtEREnrique Rozengurt
Abstract
No abstract availableThis publication has 11 references indexed in Scilit:
- Integrin-dependent phosphorylation and activation of the protein tyrosine kinase pp125FAK in platelets.Journal of Cell Biology, 1992
- Tyrosine phosphorylation of paxillin and pp125FAK accompanies cell adhesion to extracellular matrix: a role in cytoskeletal assembly.Journal of Cell Biology, 1992
- Bombesin, vasopressin, and endothelin stimulation of tyrosine phosphorylation in Swiss 3T3 cells. Identification of a novel tyrosine kinase as a major substrate.Journal of Biological Chemistry, 1992
- The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factorsCell, 1992
- Regulation of focal adhesion-associated protein tyrosine kinase by both cellular adhesion and oncogenic transformationNature, 1992
- Growth factors and cell proliferationCurrent Opinion in Cell Biology, 1992
- Integrins: Versatility, modulation, and signaling in cell adhesionCell, 1992
- Fibronectin/integrin interaction induces tyrosine phosphorylation of a 120-kDa protein.Cell Regulation, 1991
- Protein tyrosine phosphorylation and the adhesive functions of plateletsCurrent Opinion in Cell Biology, 1991
- Paxillin is a major phosphotyrosine-containing protein during embryonic development.Journal of Cell Biology, 1991