Properties of a human insulin receptor with a COOH-terminal truncation. I. Insulin binding, autophosphorylation, and endocytosis.
Open Access
- 1 June 1988
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 263 (18) , 8904-8911
- https://doi.org/10.1016/s0021-9258(18)68393-0
Abstract
No abstract availableThis publication has 28 references indexed in Scilit:
- Separate domains of the insulin receptor contain sites of autophosphorylation and tyrosine kinase activityBiochemistry, 1987
- Large deletions in the cytoplasmic kinase domain of the epidermal growth factor receptor do not affect its laternal mobility.The Journal of cell biology, 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
- Human epidermal growth factor receptor cDNA sequence and aberrant expression of the amplified gene in A431 epidermoid carcinoma cellsNature, 1984
- In VitroDeletional Mutagenesis for Bacterial Production of the 20,000-Dalton Form of Human Pituitary Growth Hormone.DNA, 1983
- Phosphorylation activates the insulin receptor tyrosine protein kinase.Proceedings of the National Academy of Sciences, 1983
- Insulin Stimulates the Phosphorylation of the 95,000-Dalton Subunit of Its Own ReceptorScience, 1982
- A new technique for the assay of infectivity of human adenovirus 5 DNAVirology, 1973