Two alternative mechanisms control the interconversion of functional states of the epidermal growth factor receptor.
Open Access
- 31 March 1988
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 263 (11) , 5373-5379
- https://doi.org/10.1016/s0021-9258(18)60726-4
Abstract
No abstract availableThis publication has 44 references indexed in Scilit:
- Epidermal growth factor induces rapid, reversible aggregation of the purified epidermal growth factor receptorBiochemistry, 1987
- Self-phosphorylation of epidermal growth factor receptor: evidence for a model of intermolecular allosteric activationBiochemistry, 1987
- Allosteric regulation of the epidermal growth factor receptor kinase.The Journal of cell biology, 1986
- Novel Interleukin-2 Receptor Subunit Detected by Cross-Linking Under High-Affinity ConditionsScience, 1986
- Protein kinase C phosphorylation at Thr 654 of the unoccupied EGF receptor and EGF binding regulate functional receptor loss by independent mechanismsCell, 1986
- Gangliosides stimulate astroglial cell proliferation in the absence of serumJournal of Cellular Physiology, 1986
- Protein kinase C phosphorylation of the EGF receptor at a threonine residue close to the cytoplasmic face of the plasma membraneNature, 1984
- Characterization of serine palmitoyltransferase activity in Chinese hamster ovary cellsBiochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1983
- Role of membrane gangliosides in the binding and action of bacterial toxinsThe Journal of Membrane Biology, 1982
- Biologically active phorbol esters specifically alter affinity of epidermal growth factor membrane receptorsNature, 1979