Replacement of insulin receptor tyrosine residues 1162 and 1163 compromises insulin-stimulated kinase activity and uptake of 2-deoxyglucose

Leland Ellis; Éric Clauser; David O. Morgan; Marc Edery; Richard A. Roth; William J. Rutter

doi:10.1016/0092-8674(86)90786-5

Keywords

AutophosphorylationInsulin receptorBiologyInsulin receptor substrateInsulinTyrosineBiochemistryIRS2Tyrosine kinaseCell biologyKinaseProtein kinase ASignal transductionEndocrinologyInsulin resistance

Affiliated Institutions

Related Publications

Characterization of selective resistance to insulin signaling in the vasculature of obese Zucker (fa/fa) rats

Zhen Jiang , You-Wei Lin , Allen Clemont +6 more

Both insulin resistance and hyperinsulinemia have been reported to be independent risk factors for cardiovascular diseases. However, little is known regarding insulin signaling ...

1999 Journal of Clinical Investigation 601 citations

Tumor necrosis factor alpha inhibits signaling from the insulin receptor.

Gökhan S. Hotamışlıgil , David Murray , Lisa Choy +1 more

Insulin resistance is a common problem associated with infections and cancer and, most importantly, is the central component of non-insulin-dependent diabetes mellitus. We have ...

1994 Proceedings of the National Academy o... 1189 citations

Insect cell-expressed p180erbB3 possesses an impaired tyrosine kinase activity.

Pamela M. Guy , Jill Platko , Lewis C. Cantley +2 more

Protein kinases share a number of highly conserved or invariant amino acid residues in their catalytic domains, suggesting that these residues are necessary for kinase activity....

1994 Proceedings of the National Academy o... 690 citations

Deceiving appearances: signaling by “dead” and “fractured” receptor protein-tyrosine kinases

Michael Kroiher , Michael A. Miller , Robert E. Steele

The mechanisms by which most receptor protein-tyrosine kinases (RTKs) transmit signals are now well established. Binding of ligand results in the dimerization of receptor monome...

2000 BioEssays 90 citations

Structure and autoregulation of the insulin-like growth factor 1 receptor kinase.

Svetlana Favelyukis , Jeffrey H. Till , Stevan R. Hubbard +1 more

2001 Nature Structural Biology 331 citations

Publication Info

Year: 1986
Type: article
Volume: 45
Issue: 5
Pages: 721-732
Citations: 1093
Access: Closed

External Links

View on DOI.org

Social Impact

Altmetric

Replacement of insulin receptor tyrosine residues 1162 and 1163 compromises insulin-stimulated kinase activity and uptake of 2-deoxyglucose

PlumX Metrics

Social media, news, blog, policy document mentions

Citation Metrics

1093

OpenAlex

Cite This

APA Style

                            
                                
                                    Leland Ellis, 
                                
                                    Éric Clauser, 
                                
                                    David O. Morgan
                                
                                et al.
                            
                            (1986). 
                            Replacement of insulin receptor tyrosine residues 1162 and 1163 compromises insulin-stimulated kinase activity and uptake of 2-deoxyglucose. 
                            Cell
                            , 45
                            (5)
                            , 721-732.
                            https://doi.org/10.1016/0092-8674(86)90786-5
                        

Identifiers

DOI: 10.1016/0092-8674(86)90786-5