Low Mr GTP-binding proteins in human platelets: Cyclic AMP-dependent protein kinase phosphorylates m22KG(I) in membrane but not c21KG in cytosol
- 1 April 1989
- journal article
- research article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 160 (1), 235-242
- https://doi.org/10.1016/0006-291x(89)91646-x
Abstract
No abstract availableKeywords
This publication has 27 references indexed in Scilit:
- Phosphorylation by cyclic AMP-dependent protein kinase of a human platelet Mr 22,000 GTP-binding protein (smg p21) having the same putative effector domain as the ras gene productsBiochemical and Biophysical Research Communications, 1988
- Identification of a platelet Mr 22,000 GTP-binding protein as the novel smg-21 gene product having the same putative effector domain as the ras gene productsBiochemical and Biophysical Research Communications, 1988
- Purification and characterization of two GTP‐binding proteins of 22 kDa from human platelet membranesFEBS Letters, 1988
- GTP‐binding proteins in human platelet membranes serving as the specific substrate of islet‐activating protein, pertussis toxinFEBS Letters, 1988
- Partial purification and characterization of thrombolamban, A 22,000 dalton cAMP-dependent protein kinase substrate in plateletsBiochemical and Biophysical Research Communications, 1987
- G PROTEINS: TRANSDUCERS OF RECEPTOR-GENERATED SIGNALSAnnual Review of Biochemistry, 1987
- Phosphorylation of ras oncogene product by protein kinase CBiochemical and Biophysical Research Communications, 1987
- Rapid purification of protein kinase C by high performance liquid chromatographyBiochemical and Biophysical Research Communications, 1986
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970