Protein kinase C: Rapid enzyme purification and substrate-dependence of the diacylglycerol effect
- 1 August 1984
- journal article
- research article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 122 (3) , 1268-1275
- https://doi.org/10.1016/0006-291x(84)91229-4
Abstract
No abstract availableThis publication has 32 references indexed in Scilit:
- A New View of Receptor ActionScience, 1984
- Ca2+-Activated, phospholipid-dependent protein kinase catalyzes the phosphorylation of actin-binding proteinsBiochemical and Biophysical Research Communications, 1984
- Phorbol ester-induced activation of human platelets is associated with protein kinase C phosphorylation of myosin light chainsNature, 1983
- Histones H3 and H4 inhibit protein kinase C specificallyBiochemical and Biophysical Research Communications, 1983
- Phospholipid degradation and signal translation for protein phosphorylationTrends in Biochemical Sciences, 1983
- Phosphorylation of calf thymus H1 histone by calcium-activated, phospholipid-dependent protein kinaseBiochemical and Biophysical Research Communications, 1980
- Unsaturated diacylglycerol as a possible messenger for the activation of calcium-activated, phospholipid-dependent protein kinase systemBiochemical and Biophysical Research Communications, 1979
- Inositol phospholipids in membrane functionTrends in Biochemical Sciences, 1979
- 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