An endogenous substrate for the insulin receptor-associated tyrosine kinase.
Open Access
- 1 April 1985
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 260 (7), 4461-4467
- https://doi.org/10.1016/s0021-9258(18)89287-0
Abstract
No abstract availableThis publication has 63 references indexed in Scilit:
- Insulin Receptor Phosphorylation May Not Be a Prerequisite for Acute Insulin ActionScience, 1984
- Insulin stimulates phosphorylation of serine residues in soluble insulin receptorsBiochemical and Biophysical Research Communications, 1983
- Evidence for phosphorylation of actin by the insulin receptor‐associated protein kinase from human placentaFEBS Letters, 1983
- Protein kinase activity of the insulin receptor in human circulating and cultured mononuclear cellsBiochemical and Biophysical Research Communications, 1983
- Stimulation of tyrosine-specific phosphorylation in vitro by insulin-like growth factor INature, 1983
- High tyrosine kinase activity in normal nonproliferating cellsNature, 1983
- Insulin binds to and promotes the phosphorylation of a M r 210 000 component of its receptor in detergent extracts of rat liver microsomesFEBS Letters, 1983
- Insulin-like effect of vanadate on adipocyte glycogen synthase and on phosphorylation of 95,000 dalton subunit of insulin receptorBiochemical and Biophysical Research Communications, 1983
- Glucocorticoid-induced Insulin ResistanceJournal of Clinical Investigation, 1982
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970