Structural features determining the site specificity of a rat liver cAMP-independent protein kinase
- 15 March 1979
- journal article
- Published by Elsevier BV in Biochemical and Biophysical Research Communications
- Vol. 87 (1), 114-120
- https://doi.org/10.1016/0006-291x(79)91654-1
Abstract
No abstract availableKeywords
This publication has 15 references indexed in Scilit:
- Phosphorylation of αs2-casein by two rat liver ‘casein kinases’FEBS Letters, 1978
- Empirical Predictions of Protein ConformationAnnual Review of Biochemistry, 1978
- Occurrence of phosphorylated residues in predicted β-turns: Implications for β-turn participation in control mechanismsBiochemical and Biophysical Research Communications, 1977
- Bovine alphaso Casein; a Phosphorylated Homologue of alphas1 CaseinEuropean Journal of Biochemistry, 1977
- Amino acid sequences at the two sites on glycogen synthetase phosphorylated by cyclic AMP‐dependent protein kinase and their dephosphorylation by protein phosphatase‐IIIFEBS Letters, 1977
- Complete amino acid sequence of bovine αS2‐caseinFEBS Letters, 1977
- Phosphorylation of casein fractions by rat liver ‘phosvitin kinase’FEBS Letters, 1977
- The minimum substrate of cyclic AMP-stimulated protein kinase, as studied by synthetic peptides representing the phosphorylatable site of pyruvate kinase (type L) of rat liverBiochemical and Biophysical Research Communications, 1976
- Phosphorylated Sites In Substrates of Intracellular Protein Kinases: A Common Feature in Amino Acid SequencesScience, 1976
- Prediction of protein conformationBiochemistry, 1974