Structural features determining the site specificity of a rat liver cAMP-independent protein kinase
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference20 articles.
1. Phosphorylated Sites In Substrates of Intracellular Protein Kinases: A Common Feature in Amino Acid Sequences
2. Amino acid sequences at the two sites on glycogen synthetase phosphorylated by cyclic AMP-dependent protein kinase and their dephosphorylation by protein phosphatase-III
3. 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 liver
4. Role of multiple basic residues in determining the substrate specificity of cyclic AMP-dependent protein kinase.
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