Phosphorylation of the 165-kDa dihydropyridine/phenylalkylamine receptor from skeletal muscle by protein kinase C.
Open Access
- 1 November 1988
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 263 (33) , 17342-17349
- https://doi.org/10.1016/s0021-9258(19)77841-7
Abstract
No abstract availableThis publication has 46 references indexed in Scilit:
- Phosphorylation of the purified receptor for calcium channel blockers by cAMP kinase and protein kinase CEuropean Journal of Biochemistry, 1987
- Photoaffinity labelling and phosphorylation of a 165 kilodalton peptide associated with dihydropyridine and phenylalkylamine-sensitive calcium channelsBiochemical and Biophysical Research Communications, 1987
- The 165‐KDa peptide of the purified skeletal muscle dihydropyridine receptor contains the known regulatory sites of the calcium channelEuropean Journal of Biochemistry, 1987
- Regulation of the cardiac calcium channel by protein phosphatasesEuropean Journal of Biochemistry, 1987
- Photoaffinity labelling of the phenylalkylamine receptor of the skeletal muscle transverse‐tubule calcium channelFEBS Letters, 1987
- Mechanisms of calcium channel modulation by β-adrenergic agents and dihydropyridine calcium agonistsJournal of Molecular and Cellular Cardiology, 1986
- Properties of receptors for the Ca2+‐channel blocker verapamil in transverse‐tubule membranes of skeletal muscleEuropean Journal of Biochemistry, 1984
- Purification of the dihydropyridine receptor of the voltage-dependent Ca2+ channel from skeletal muscle transverse tubules using (+) [3H]PN 200-110Biochemical and Biophysical Research Communications, 1984
- Solubilization of the nitrendipine receptor from skeletal muscle transverse tubule membranes Interactions with specific inhibitors of the voltage‐dependent Ca2+ channelEuropean Journal of Biochemistry, 1984
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970