Effect of insulin receptor autophosphorylation on insulin receptor binding.
Explore this paper's citation graph
Summary
The absence of any feedback mechanism by which insulin receptor activation by phosphorylation affects binding affinity of insulin receptor itself is demonstrated.
- Type
- article
- Published
- 1986-05-01
- Cited by
- 9
- References
- 16
- OpenAlex
- https://openalex.org/W2043502953
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:34799854
Keywords
Autophosphorylation, Insulin receptor, Insulin receptor substrate, Insulin-like growth factor 1 receptor, IRS2
References
- Insulin receptor kinase activity in rat liver. Regulation by fasting and high carbohydrate feeding.
- Phosphorylation of the hepatic insulin receptor
- Tyrosine phosphorylation of the insulin receptor beta subunit activates the receptor-associated tyrosine kinase activity.
- Differences in the sites of phosphorylation of the insulin receptor in vivo and in vitro.
- Tumor-promoting phorbol diesters mediate phosphorylation of the epidermal growth factor receptor.
- Role of disulfides in the subunit structure of the insulin receptor. Reduction of class I disulfides does not impair transmembrane signalling.
- Phosphorylation of exogenous substrates by the insulin receptor-associated protein kinase.
- Substrate specificities of insulin and epidermal growth factor receptor kinases.
- THE ATTRACTIONS OF PROTEINS FOR SMALL MOLECULES AND IONS
- Inhibition of insulin and epidermal growth factor (EGF) receptor autophosphorylation by a human polyclonal IgG.
- Binding of insulin receptors to lectins: evidence for common carbohydrate determinants on several membrane receptors.
- ATP and other nucleoside triphosphates inhibit the binding of insulin to its receptor.
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
- Inhibition of insulin receptor binding by phorbol esters.
- Probes of membrane structure.
- Two different protein kinase activities are associated with the insulin receptor.
Cited by
- Mathematical Modeling of Biochemical Signal Transduction Pathways in Mammalian Cells – A Domain-Oriented Approach to Reduce Combinatorial Complexity
- Reduced Order Modeling and Analysis of Cellular Signal Transduction
- Direct modulation of insulin receptor protein tyrosine kinase by vanadate and anti-insulin receptor monoclonal antibodies.
- Species specificity of insulin binding and insulin receptor protein tyrosine kinase activity.
- Regulation of insulin receptor-associated tyrosine kinase by a polyclonal IgG.
- Exact model reduction of combinatorial reaction networks
- Mathematical modeling and analysis of insulin clearance in vivo
- An evaluation of the cross-linking model for the interaction of insulin with its receptor.
- The Insulin Receptor: An Important Target for the Development of Novel Medicines and Pesticides
Related papers
- Insulin stimulates association of a 41kDa G-protein (GIR41) with the insulin receptor.
- The long acting human insulin analog HOE 901: characteristics of insulin signalling in comparison to Asp(B10) and regular insulin.
- Insulin-receptor autophosphorylation and kinase activity are constitutively increased in fibroblasts cultured from a patient with heritable insulin-resistance.
- Glucose-induced insulin secretion is impaired and insulin-induced phosphorylation of the insulin receptor and insulin receptor substrate-1 are increased in protein-deficient rats.
- Insulin-like growth factor I signalling through heterodimers of insulin and insulin-like growth factor I receptors.
- Quantitative dissociation of glucose transport stimulation and insulin receptor tyrosine kinase activation in isolated adipocytes with a covalent insulin dimer (B29,B29'-suberoyl-insulin).
- Alteration of Insulin-Receptor Kinase Activity by High-Fat Feeding
- Sustained signalling from the insulin receptor after stimulation with insulin analogues exhibiting increased mitogenic potency.
- Stimulation of glycogen synthesis by insulin in human erythroleukemia cells requires the synthesis of glycosyl-phosphatidylinositol.