Insulin receptors with defective tyrosine kinase inhibit normal receptor function at the level of substrate phosphorylation.
Open Access
- 1 September 1988
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 263 (25), 12629-12637
- https://doi.org/10.1016/s0021-9258(18)37800-1
Abstract
No abstract availableThis publication has 21 references indexed in Scilit:
- Insulin-activated tyrosine phosphorylation of a 15-kilodalton protein in intact 3T3-L1 adipocytes.Proceedings of the National Academy of Sciences, 1987
- Decreased kinase activity of insulin receptors from adipocytes of non-insulin-dependent diabetic subjects.JCI Insight, 1987
- Linking functional domains of the human insulin receptor with the bacterial aspartate receptor.Proceedings of the National Academy of Sciences, 1986
- Replacement of insulin receptor tyrosine residues 1162 and 1163 compromises insulin-stimulated kinase activity and uptake of 2-deoxyglucoseCell, 1986
- (Thr-59)-insulin-like growth factor I stimulates 2-deoxyglucose transport in BC3H1 myocytes through the insulin-like growth factor receptor, not the insulin receptorBiochimica et Biophysica Acta (BBA) - Molecular Cell Research, 1986
- Expression of a functional human insulin receptor from a cloned cDNA in Chinese hamster ovary cells.Proceedings of the National Academy of Sciences, 1985
- The human insulin receptor cDNA: The structural basis for hormone-activated transmembrane signallingCell, 1985
- Human insulin receptor and its relationship to the tyrosine kinase family of oncogenesNature, 1985
- The Molecular Mechanism of Insulin ActionAnnual Review of Medicine, 1985
- Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.Proceedings of the National Academy of Sciences, 1979