Conformationally constrained analogues of diacylglycerol. 9.1 the effect of side-chain orientation on the protein kinase C (PK-C) binding affinity of σ-lactones

This publication has 14 references indexed in Scilit:

• Conformationally constrained analogues of dag .8. Changes in PK-C binding affinity produced by isosteric groups of the 3-O-acyl function in 2-deoxy-L-ribonolactones
  Bioorganic & Medicinal Chemistry Letters, 1994
• Conformationally constrained analogues of DAG.7. Interaction of a medium-size ε-lactone with protein kinase C (PK-C)_
  Bioorganic & Medicinal Chemistry Letters, 1994
• Conformationally constrained analogues of diacylglycerol (DAG)-II. Differential interaction of δ-lactones and γ-lactones with protein kinase C (PK-C)
  Bioorganic & Medicinal Chemistry, 1993
• Conformationally constrained analogues of diacylglycerol (DAG). 4. Interaction of α-alkylidene-γ-lactones with protein kinase C (PK-C)
  Bioorganic & Medicinal Chemistry Letters, 1993
• Conformationally constrained analogues of diacylglycerol (DAG). 3. Interaction of α-alkyl-γ-lactones with protein kinase C (PK-C)
  Bioorganic & Medicinal Chemistry Letters, 1993
• Tissue and cellular distribution of the extended family of protein kinase C isoenzymes
  The Journal of cell biology, 1992
• Conformationally constrained analogs of diacylglycerol. Interaction of .gamma.-lactones with the phorbol ester receptor of protein kinase C
  Journal of the American Chemical Society, 1992
• The molecular heterogeneity of protein kinase C and its implications for cellular regulation
  Nature, 1988
• Competitive inhibition by diacylglycerol of specific phorbol ester binding.
  Proceedings of the National Academy of Sciences, 1984
• Specificity of the Fatty Acyl Moieties of Diacylglycerol for the Activation of Calcium-Activated, Phospholipid-Dependent Protein Kinase1
  The Journal of Biochemistry, 1982