Protein kinase C autophosphorylates by an intrapeptide reaction.
Open Access
- 1 July 1987
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 262 (21) , 10185-10188
- https://doi.org/10.1016/s0021-9258(18)61095-6
Abstract
No abstract availableThis publication has 22 references indexed in Scilit:
- Domain structure and phosphorylation of protein kinase C.Journal of Biological Chemistry, 1987
- The Metabolism of Phosphoinositide-Derived Messenger MoleculesScience, 1986
- Isozymic forms of rat brain Ca2+-activated and phospholipid-dependent protein kinase.Proceedings of the National Academy of Sciences, 1986
- Conversion of protein kinase C from a Ca2+-dependent to an independent form of phorbol ester-binding protein by digestion with trypsimBiochemical and Biophysical Research Communications, 1986
- Studies and Perspectives of Protein Kinase CScience, 1986
- Autophosphorylation reversibly regulates the Ca2+/calmodulin-dependence of Ca2+/calmodulin-dependent protein kinase II.Proceedings of the National Academy of Sciences, 1986
- Intrapeptide autophosphorylation of the epidermal growth factor receptor: regulation of kinase catalytic function by receptor dimerizationBiochemistry, 1985
- Inositol trisphosphate and diacylglycerol as second messengersBiochemical Journal, 1984
- Insulin receptor is an insulin-dependent tyrosine protein kinase: copurification of insulin-binding activity and protein kinase activity to homogeneity from human placenta.Proceedings of the National Academy of Sciences, 1984
- Three Multifunctional Protein Kinase Systems in Transmembrane ControlPublished by Springer Nature ,1980