Synthetic segments of the mammalian βAR are preferentially recognized by cAMP-dependent protein kinase and protein kinase C
- 31 July 1987
- journal article
- research article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 147 (1) , 168-173
- https://doi.org/10.1016/s0006-291x(87)80102-x
Abstract
No abstract availableThis publication has 15 references indexed in Scilit:
- Phosphorylation by protein kinase C of a synthetic heptapeptide bearing a lysine residue on the C terminal side of serineBiochemical and Biophysical Research Communications, 1987
- Substrate specificity of protein kinase CEuropean Journal of Biochemistry, 1986
- Cloning of the gene and cDNA for mammalian β-adrenergic receptor and homology with rhodopsinNature, 1986
- Phorbol diester treatment promotes enhanced adenylate cyclase activity in frog erythrocytesArchives of Biochemistry and Biophysics, 1986
- Synthetic myelin basic protein peptide analogs are specific inhibitors of phospholipid/calcium-dependent protein kinase (protein kinase C)Biochemical and Biophysical Research Communications, 1986
- Molecular mechanisms of receptor desensitization using the β-adrenergic receptor-coupled adenylate cyclase system as a modelNature, 1985
- Desensitization of the Response of Adenylate Cyclase to CatecholaminesPublished by Elsevier ,1983
- Phosphorylation-Dephosphorylation of EnzymesAnnual Review of Biochemistry, 1979
- Solid Phase Peptide Synthesis. I. The Synthesis of a TetrapeptideJournal of the American Chemical Society, 1963