Evidence for a Regulatory Binding Site for Arginine-Rich Peptides on Protein Kinase C
- 1 August 1998
- journal article
- Published by Elsevier in Archives of Biochemistry and Biophysics
- Vol. 356 (2) , 258-264
- https://doi.org/10.1006/abbi.1998.0766
Abstract
No abstract availableKeywords
This publication has 9 references indexed in Scilit:
- Covalent Modification of Protein Kinase C Isozymes by the Inactivating Peptide Substrate Analog N-Biotinyl-Arg-Arg-Arg-Cys-Leu-Arg-Arg-LeuPublished by Elsevier ,1996
- Substrate-Induced Translocation of PKC-? to the MembraneArchives of Biochemistry and Biophysics, 1995
- Irreversible Inactivation of Protein Kinase C by a Peptide-Substrate AnalogPublished by Elsevier ,1995
- Kinetic analysis of protein kinase C: product and dead-end inhibition studies using ADP, poly(L-lysine), nonhydrolyzable ATP analogs, and diadenosine oligophosphatesBiochemistry, 1991
- Lipid dependence of surface conformations of protein kinase CBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1990
- Protein kinase C penetration into lipid bilayersArchives of Biochemistry and Biophysics, 1990
- Role of substrate in determining the phospholipid specificity of protein kinase C activationBiochemistry, 1987
- Role of substrate in imparting calcium and phospholipid requirements to protein kinase C activationBiochemistry, 1987
- Ca2+ phospholipid-dependent and independent phosphorylation of synthetic peptide substrates by protein kinase CEuropean Journal of Biochemistry, 1987