Mechanism of Activation of Protein Kinase I from Rabbit Skeletal Muscle. The Equilibrium Parameters of Ligand Interaction and Protein Dissociation
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1978.tb12639.x/fullpdf
Reference27 articles.
1. Comparison of adenosine 3':5'-monophosphate-dependent protein kinases from rabbit skeletal and bovine heart muscle.
2. Reversible autophosphorylation of a cyclic 3':5'-AMP-dependent protein kinase from bovine cardiac muscle.
3. Dissociation and reassociation of the phosphorylated and nonphosphorylated forms of adenosine 3':5' -monophosphate-dependent protein kinase from bovine cardiac muscle.
4. ATP (Mg2+) induced inhibition of cyclic AMP reactivity with a skeletal muscle protein kinase
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1. Limited proteolysis alters the photoaffinity labeling of adenosine 3',5'-monophosphate dependent protein kinase II with 8-azidoadenosine 3',5'-monophosphate;Biochemistry;1987-09-22
2. Correlation of photolabeling with occupancy of cAMP binding sites in the regulatory subunit of cAMP-dependent protein kinase I;Biochemistry;1987-06-16
3. Inhibitory action of certain cyclophosphate derivatives of cAMP on cAMP-dependent protein kinases;European Journal of Biochemistry;1984-07
4. ATP and other nucleoside triphosphates inhibit the binding of insulin to its receptor;Metabolism;1984-06
5. Characterization of the interchain and intrachain interactions between the binding sites of the free regulatory moiety of protein kinase I.;Journal of Biological Chemistry;1984-02
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