Insulin-sensitive phosphorylation of serine 1293/1294 on the human insulin receptor by a tightly associated serine kinase.
Open Access
- 4 January 1990
- journal article
- abstracts
- Published by Elsevier
- Vol. 265 (2) , 947-954
- https://doi.org/10.1016/s0021-9258(19)40141-5
Abstract
No abstract availableKeywords
This publication has 18 references indexed in Scilit:
- Direct activation of the serine/threonine kinase activity of raf-1 through tyrosine phosphorylation by the PDGF β-receptorCell, 1989
- Presence of an insulin-stimulated serine kinase in cell extracts from IM-9 cellsBiochemical and Biophysical Research Communications, 1986
- Replacement of insulin receptor tyrosine residues 1162 and 1163 compromises insulin-stimulated kinase activity and uptake of 2-deoxyglucoseCell, 1986
- 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
- Autophosphorylation sites on the epidermal growth factor receptorNature, 1984
- Insulin stimulates phosphorylation of serine residues in soluble insulin receptorsBiochemical and Biophysical Research Communications, 1983
- The isolation of peptides by high-performance liquid chromatography using predicted elution positionsAnalytical Biochemistry, 1982
- Empirical Predictions of Protein ConformationAnnual Review of Biochemistry, 1978
- Occurrence of phosphorylated residues in predicted β-turns: Implications for β-turn participation in control mechanismsBiochemical and Biophysical Research Communications, 1977