Cyclic AMP-dependent protein kinase phosphorylates serine378 in vitronectin
- 1 August 1991
- journal article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 179 (1) , 655-660
- https://doi.org/10.1016/0006-291x(91)91422-9
Abstract
No abstract availableKeywords
This publication has 20 references indexed in Scilit:
- Endogenous cleavage of the Arg-379-Ala-380 bond in vitronectin results in a distinct conformational change which ‘buries’ Ser-378, its site of phosphorylation by protein kinase ABiochemical Journal, 1991
- The phosphorylation of the two‐chain form of vitronectin by protein kinase A is heparin dependentFEBS Letters, 1990
- Polymorphism of the human vitronectin gene causes vitronectin blood typeBiochemical and Biophysical Research Communications, 1990
- SC5b‐7, SC5b‐8 and SC5b‐9 complexes of complement: ultrastructure and localization of the S‐protein (vitronectin) within the macromoleculesEuropean Journal of Immunology, 1989
- Vitronectin is phosphorylated by a cAMP-dependent protein kinase released by activation of human platelets with thrombinBiochemical and Biophysical Research Communications, 1988
- A potent synthetic peptide inhibitor of the cAMP-dependent protein kinase.Journal of Biological Chemistry, 1986
- Physicochemical characterization of human S-protein and its function in the blood coagulation systemBiochemical Journal, 1985
- Characterization of human S protein, an inhibitor of the membrane attack complex of complement. Demonstration of a free reactive thiol groupBiochemistry, 1985
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- [10] Assay of inorganic phosphate, total phosphate and phosphatasesPublished by Elsevier ,1966