Transmembrane signalling by insulin via an insulin receptor mutated at tyrosines 1158, 1162, and 1163
- 16 September 1991
- journal article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 179 (2) , 912-918
- https://doi.org/10.1016/0006-291x(91)91905-r
Abstract
No abstract availableKeywords
This publication has 11 references indexed in Scilit:
- Substrates for Insulin-Receptor KinaseDiabetes Care, 1990
- Monoclonal Antibodies Mimic Insulin Activation of Ribosomal Protein S6 Kinase without Activation of Insulin Receptor Tyrosine KinaseJournal of Biological Chemistry, 1989
- Monoclonal antibodies to the human insulin receptor mimic a spectrum of biological effects in transfected fibroblasts without activating receptor kinaseBiochemical and Biophysical Research Communications, 1989
- Participation of Ca currents in colonic electrical activityAmerican Journal of Physiology-Cell Physiology, 1989
- Cascade of autophosphorylation in the β‐subunit of the insulin receptorJournal of Cellular Biochemistry, 1989
- Receptor cross-linking restores an insulin metabolic effect altered by mutation on tyrosine 1162 and tyrosine 1163Biochemistry, 1989
- The Insulin Receptor: Molecular Biology and Transmembrane Signaling*Endocrine Reviews, 1987
- Replacement of insulin receptor tyrosine residues 1162 and 1163 compromises insulin-stimulated kinase activity and uptake of 2-deoxyglucoseCell, 1986
- Mapping surface structures of the human insulin receptor with monoclonal antibodies: localization of main immunogenic regions to the receptor kinase domainBiochemistry, 1986
- The human insulin receptor cDNA: The structural basis for hormone-activated transmembrane signallingCell, 1985