Interaction of cyclic adenosine 3':5'-monophosphate with protein kinase. Equilibrium binding models.

This publication has 13 references indexed in Scilit:

• Comparison of adenosine 3':5'-monophosphate-dependent protein kinases from rabbit skeletal and bovine heart muscle.
  Journal of Biological Chemistry, 1975
• L-Threonine Dehydrase as a Model of Allosteric Control Involving Ligand-lnduced Oligomerization
  Current Topics in Cellular Regulation, 1975
• Heterogeneity and Unusually High Affinity in the Interactions of Adenosine 3′:5′-Monophosphate with Specific Binding Proteins from Liver and Hepatoma Cells
  Journal of Biological Chemistry, 1974
• Activation of Protein Kinase by Physiological Concentrations of Cyclic AMP
  Proceedings of the National Academy of Sciences, 1974
• Kinetics of Allosteric Enzymes
  Annual Review of Biophysics and Bioengineering, 1974
• Ligand-induced dimer-to-tetramer transformation in cytosine triphosphate synthetase
  Biochemistry, 1972
• Protein Kinases* *Support of the National Institutes of Arthritis and Metabolic Diseases, NIH, U. S. Public Health Service (AM 12842), the Muscular Dystrophy Association of America, and the American Heart Association is acknowledged.
  Current Topics in Cellular Regulation, 1972
• Protein-Protein Interaction and Enzymatic Activity
  Annual Review of Biochemistry, 1971
• Cooperative interactions and determination of protein association-dissociation equilibria. Hemerythrin
  Biochemistry, 1968
• A Theoretical Study of the Binding of Small Molecules to a Polymerizing Protein System. A Model for Allosteric Effects^*
  Biochemistry, 1967