The use of synthetic peptides for defining the specificity of typrosine protein kinases

Author:

Casnellie John E.,Krebs Edwin G.

Publisher

Elsevier BV

Subject

Cancer Research,Genetics,Molecular Biology,Molecular Medicine

Reference36 articles.

1. Phosphorylation of synthetic peptides by a tyrosine protein kinase from the particulate fraction of a lymphoma cell line;Casnellie,1982

2. A lymphoma cell line expressing elevated levels of tyrosine protein kinase activity;Casnellie;J. Biol. Chem.,1983

3. The minimum substrate of cyclic AMP-stimulated protein kinase, as studied by synthetic peptides representing the phosphorylation site of pyruvate kinase (type L) of rat liver;Zetterquist;Biochem. Biophys. Res. Comm.,1976

4. Role of multiple basic residues in determining the substrate specificity of cyclic AMP-dependent protein kinase;Kemp;J. Biol. Chem.,1977

5. Synthetic hexapeptide substrates and inhibitors of 3′:5′-cyclic AMP-dependent protein kinase;Kemp,1976

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