Studies on the phosphorylation of myelin basic protein by protein kinase C and adenosine 3‘:5‘-monophosphate-dependent protein kinase.
Open Access
- 1 October 1985
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 260 (23) , 12492-12499
- https://doi.org/10.1016/s0021-9258(17)38898-1
Abstract
No abstract availableThis publication has 37 references indexed in Scilit:
- Inositol trisphosphate, a novel second messenger in cellular signal transductionNature, 1984
- Protein kinase C phosphorylates the synthetic peptide Arg-Arg-Lys-Ala-Ser-Gly-Pro-Pro-Val in the presence of phospholipid plus either Ca2+ or a phorbol ester tumor promoterBiochemical and Biophysical Research Communications, 1984
- Protein kinase C phosphorylation of the EGF receptor at a threonine residue close to the cytoplasmic face of the plasma membraneNature, 1984
- Turnover of Inositol Phospholipids and Signal TransductionScience, 1984
- Calcium ion stimulated endogenous protein kinase catalyzed phosphorylation of basic proteins in myelin subfractions and myelin-like membrane fraction from rat brainBiochemistry, 1980
- Phosphorylation-Dephosphorylation of EnzymesAnnual Review of Biochemistry, 1979
- N-terminal amino acid sequences of variant-specific surface antigens from Trypanosoma bruceiNature, 1976
- Inositol phospholipids and cell surface receptor functionBiochimica et Biophysica Acta (BBA) - Reviews on Biomembranes, 1975
- Phosphorylation of selected serine and threonine residues in myelin basic protein by endogenous and exogenous protein kinasesNature, 1974
- Solid‐phase Edman degradation of a protein: N‐terminal sequence of cytochromec fromCandida kruseiFEBS Letters, 1973