Interaction of protein kinase C with membranes is regulated by Ca2+, phorbol esters, and ATP.

This publication has 25 references indexed in Scilit:

• A model for intracellular translocation of protein kinase C involving synergism between Ca2+ and phorbol esters
  Nature, 1985
• Interleukin-2 stimulates association of protein kinase C with plasma membrane
  Nature, 1985
• Protein kinase C translocates from cytosol to membrane upon hormone activation: Effects of thyrotropin-releasing hormone in GH3 cells
  Biochemical and Biophysical Research Communications, 1985
• Autophosphorylation of Calmodulin‐Kinase II in Synaptic Junctions Modulates Endogenous Kinase Activity
  Journal of Neurochemistry, 1984
• Turnover of Inositol Phospholipids and Signal Transduction
  Science, 1984
• Protein kinase C: Rapid enzyme purification and substrate-dependence of the diacylglycerol effect
  Biochemical and Biophysical Research Communications, 1984
• Modulation of Ca2+-activated, phospholipid-dependent protein kinase in platelets treated with a tumor-promoting phorbol ester
  Biochemical and Biophysical Research Communications, 1984
• Inositol phospholipids in membrane function
  Trends in Biochemical Sciences, 1979
• A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
  Analytical Biochemistry, 1976
• Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
  Nature, 1970