Evidence that insulin plus ATP may induce a conformational change in the beta subunit of the insulin receptor without inducing receptor autophosphorylation.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference41 articles.
1. Human insulin receptors mutated at the ATP-binding site lack protein tyrosine kinase activity and fail to mediate postreceptor effects of insulin.
2. The Nature and Regulation of the Insulin Receptor: Structure and Function
3. Replacement of insulin receptor tyrosine residues 1162 and 1163 does not alter the mitogenic effect of the hormone.
4. Receptor cross-linking restores an insulin metabolic effect altered by mutation on tyrosine 1162 and tyrosine 1163
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2. Phosphorylation of the insulin receptor by AMP-activated protein kinase (AMPK) promotes ligand-independent activation of the insulin signalling pathway in rodent muscle;Diabetologia;2011-12-30
3. Interdependent Regulation of Insulin Receptor Kinase Activity by ADP and Hydrogen Peroxide;Journal of Biological Chemistry;2005-02
4. Platelet‐derived growth factor activates production of reactive oxygen species by NAD(P)H‐oxidase in smooth muscle cells through Gi1,2;The FASEB Journal;2002-11
5. Intrasteric Inhibition of ATP Binding Is Not Required To Prevent Unregulated Autophosphorylation or Signaling by the Insulin Receptor;Molecular and Cellular Biology;2001-07
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