Deletion of C-terminal 113 amino acids impairs processing and internalization of human insulin receptor: Comparison of receptors expressed in CHO and NIH-3T3 cells
- 1 December 1993
- journal article
- research article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
- Vol. 1220 (1) , 1-14
- https://doi.org/10.1016/0167-4889(93)90090-c
Abstract
No abstract availableKeywords
This publication has 36 references indexed in Scilit:
- Insulin receptors internalize by a rapid, saturable pathway requiring receptor autophosphorylation and an intact juxtamembrane region.The Journal of cell biology, 1991
- The Protein Kinase Family: Conserved Features and Deduced Phylogeny of the Catalytic DomainsScience, 1988
- After Insulin BindsScience, 1987
- Antibody-induced down-regulation of a mutated insulin receptor lacking an intact cytoplasmic domainBiochemistry, 1987
- Replacement of insulin receptor tyrosine residues 1162 and 1163 compromises insulin-stimulated kinase activity and uptake of 2-deoxyglucoseCell, 1986
- Insulin receptor biosynthesis in cultured lymphocytes from insulin-resistant patients.Journal of Clinical Investigation, 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
- Insulin stimulates tyrosine phosphorylation of the insulin receptor in a cell-free systemNature, 1982
- Insulin Stimulates the Phosphorylation of the 95,000-Dalton Subunit of Its Own ReceptorScience, 1982