The Protein-tyrosine Phosphatase SHP-1 Regulates the Phosphorylation of α-Actinin
Open Access
- 1 June 2004
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 279 (24) , 25755-25764
- https://doi.org/10.1074/jbc.m314175200
Abstract
No abstract availableKeywords
This publication has 59 references indexed in Scilit:
- Early molecular events in the assembly of matrix adhesions at the leading edge of migrating cellsJournal of Cell Science, 2003
- Crystal Structure of Human Protein-tyrosine Phosphatase SHP-1Journal of Biological Chemistry, 2003
- The Molecular Adapter SLP-76 Relays Signals from Platelet Integrin αIIbβ3 to the Actin CytoskeletonJournal of Biological Chemistry, 2001
- Evidence of a Role for SHP-1 in Platelet Activation by the Collagen Receptor Glycoprotein VIPublished by Elsevier ,2000
- Roles of the SHP-1 tyrosine phosphatase in the negative regulation of cell signallingSeminars in Immunology, 2000
- The major SHP-1-binding, tyrosine-phosphorylated protein in macrophages is a member of the KIR/LIR family and an SHP-1 substrateOncogene, 1998
- Integrin-mediated Tyrosine Phosphorylation of SHPS-1 and Its Association with SHP-2Published by Elsevier ,1998
- Association of the protein tyrosine phosphatase PTP1C with the protein tyrosine kinase c-Src in human plateletsFEBS Letters, 1996
- Reduced cell motility and enhanced focal adhesion contact formation in cells from FAK-deficient miceNature, 1995
- An interaction between alpha-actinin and the beta 1 integrin subunit in vitro.The Journal of cell biology, 1990