Biosynthesis and Posttranslational Modifications of Protein Kinase C in Human Breast Cancer Cells
Open Access
- 1 August 1989
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 264 (23) , 13902-13909
- https://doi.org/10.1016/s0021-9258(18)80085-0
Abstract
No abstract availableThis publication has 55 references indexed in Scilit:
- Protein Kinase C Contains a Pseudosubstrate Prototope in Its Regulatory DomainScience, 1987
- Immunological quantitation of phospholipid/CA2+‐dependent protein kinase of human mammary carcinoma cells: Inverse relationship to estrogen receptorsInternational Journal of Cancer, 1987
- Enzymatically inactive p60c-src mutant with altered ATP-binding site is fully phosphorylated in its carboxy-terminal regulatory regionCell, 1987
- Conversion of protein kinase C from a Ca2+-dependent to an independent form of phorbol ester-binding protein by digestion with trypsimBiochemical and Biophysical Research Communications, 1986
- Cloning and expression of multiple protein kinase C cDNAsCell, 1986
- Protein kinase C negatively modulated by phorbol esterFEBS Letters, 1986
- Protein kinase C desensitization by phorbol esters and its impact on growth of human breast cancer cellsBiochemical and Biophysical Research Communications, 1986
- Inositol trisphosphate, a novel second messenger in cellular signal transductionNature, 1984
- Cyclic Adenosine Monophosphate-Dependent Protein Kinases of Human Seminal Plasma: Origin and Characteristics of Multiple FormsBiology of Reproduction, 1982
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976