Membrane protein-lipid hydrogen bonding: evidence from protein kinase C, diglyceride, and tumor promotors
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(86)80559-2/fullpdf
Reference35 articles.
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4. Activation of calcium and phospholipid-dependent protein kinase by diacylglycerol, its possible relation to phosphatidylinositol turnover.
5. Exogenous sn-1,2-diacylglycerols containing saturated fatty acids function as bioregulators of protein kinase C in human platelets.
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1. Reorientational properties of fluorescent analogues of the protein kinase C cofactors diacylglycerol and phorbol ester;Biophysical Chemistry;1996-02
2. Protein kinase C and its substrates;Molecular and Cellular Endocrinology;1996-01
3. The phorbol ester TPA markedly enhances the binding of calcium to the regulatory domain of protein kinase C β1 in the presence of phosphatidylserine;Carcinogenesis;1995
4. The Interaction between Protein Kinase C and Lipid Cofactors Studied by Simultaneous Observation of Lipid and Protein Fluorescence;Journal of Biological Chemistry;1995-01
5. The Discovery of Novel, Structurally Diverse Protein Kinase C Agonists through Computer 3D-Database Pharmacophore Search. Molecular Modeling Studies;Journal of Medicinal Chemistry;1994-12
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