Independent mechanisms account for the regulation by protein kinase C of the epidermal growth factor receptor affinity and tyrosine-protein kinase activity.
Open Access
- 1 July 1988
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 263 (19) , 9462-9469
- https://doi.org/10.1016/s0021-9258(19)76563-6
Abstract
No abstract availableThis publication has 31 references indexed in Scilit:
- Synthesis of epidermal growth factor (EGF) receptor in vitro using SP6 RNA polymerase-transcribed template mRNABiochimica et Biophysica Acta (BBA) - Gene Structure and Expression, 1986
- Protein kinase C phosphorylation at Thr 654 of the unoccupied EGF receptor and EGF binding regulate functional receptor loss by independent mechanismsCell, 1986
- Phorbol esters induce transient internalization without degradation of unoccupied epidermal growth factor receptors.Proceedings of the National Academy of Sciences, 1985
- EGF receptor affinity is regulated by intracellular calcium and protein kinase CCell, 1985
- Protein kinase C phosphorylation of the EGF receptor at a threonine residue close to the cytoplasmic face of the plasma membraneNature, 1984
- Construction and applications of a highly transmissible murine retrovirus shuttle vectorCell, 1984
- Tumor promoters block tyrosine-specific phosphorylation of the epidermal growth factor receptor.Proceedings of the National Academy of Sciences, 1984
- Further purification of epidermal growth factor by high-performance liquid chromatographyAnalytical Biochemistry, 1982
- LIGAND: A versatile computerized approach for characterization of ligand-binding systemsAnalytical Biochemistry, 1980
- Biologically active phorbol esters specifically alter affinity of epidermal growth factor membrane receptorsNature, 1979