Augmented Mitogenesis and Impaired Metabolic Signaling Mediated by a Truncated Insulin Receptor
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference29 articles.
1. Insulin Stimulates the Phosphorylation of the 95,000-Dalton Subunit of Its Own Receptor
2. Phosphorylation activates the insulin receptor tyrosine protein kinase.
3. Acute insulin action requires insulin receptor kinase activity: introduction of an inhibitory monoclonal antibody into mammalian cells blocks the rapid effects of insulin.
4. Replacement of insulin receptor tyrosine residues 1162 and 1163 compromises insulin-stimulated kinase activity and uptake of 2-deoxyglucose
5. Human insulin receptors mutated at the ATP-binding site lack protein tyrosine kinase activity and fail to mediate postreceptor effects of insulin.
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