Synthetic peptides reproducing the site phosphorylated by cAMP-dependent protein kinase in protein phosphatase inhibitor-1. Effect of structural modifications on the phosphorylation efficiency
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1983.tb07695.x/fullpdf
Reference25 articles.
1. The hormonal control of glycogen metabolism: The amino acid sequence at the phosphorylation site of protein phosphatase inhibitor-1
2. 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
3. Role of multiple basic residues in determining the substrate specificity of cyclic AMP-dependent protein kinase.
4. Optimal spatial requirements for the location of basic residues in peptide substrates for the cyclic AMP-dependent protein kinase.
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