Calcium mobilisation controls tyrosine protein phosphorylation independently of the activation of protein kinase C in human platelets
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(94)00414-5/fullpdf
Reference30 articles.
1. Platelet tyrosine-specific protein phosphorylation is regulated by thrombin.
2. Thrombin treatment induces rapid changes in tyrosine phosphorylation in platelets.
3. Thrombin and collagen induce rapid phosphorylation of a common set of cellular proteins on tyrosine in human platelets
4. Ionophore A23187-induced protein-tyrosine phosphorylation of human platelets: Possible synergism between Ca2+ mobilization and protein kinase C activation
5. Cytosolic and stored calcium antagonistically control tyrosine phosphorylation of specific platelet proteins.
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