Insulin binds to and promotes the phosphorylation of a M r 210 000 component of its receptor in detergent extracts of rat liver microsomes
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(83)80587-0/fullpdf
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1. Insulin Stimulates the Phosphorylation of the 95,000-Dalton Subunit of Its Own Receptor
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3. Purification and characterization of epidermal growth factor receptor/protein kinase from normal mouse liver.
4. Insulin Receptor: Evidence That It Is a Protein Kinase
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1. Cleavage site mutants of the subtype B insulin receptor are uncleaved and fully functional;Molecular and Cellular Endocrinology;1997-04
2. Increased hepatic insulin proreceptor-to-receptor ratio in diabetes: a possible processing defect;American Journal of Physiology-Endocrinology and Metabolism;1991-11-01
3. Insulin Receptor Structure;Insulin;1990
4. Cytoplasmic domains determine signal specificity, cellular routing characteristics and influence ligand binding of epidermal growth factor and insulin receptors.;The EMBO Journal;1989-10
5. Evidence for exogenous substrate phosphorylation and dimer formation by the activated 190 kDa insulin proreceptor in vitro;Biochemical and Biophysical Research Communications;1989-04
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