Species specificity of insulin binding and insulin receptor protein tyrosine kinase activity.
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Summary
Data suggest that MA 10 is directed against a region of the insulin receptor that is in between the insulin-binding domain and the beta-subunit and that in human, but not rat, tissues, this region is involved in insulin binding.
- Type
- article
- Published
- 1987-12-01
- Cited by
- 6
- References
- 26
- OpenAlex
- https://openalex.org/W2048689184
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:21373112
Keywords
Autophosphorylation, Insulin receptor, IRS2, Internal medicine, GRB10
References
- Insulin receptors, receptor antibodies, and the mechanism of insulin action.
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- Insulin receptor kinase activity in rat liver. Regulation by fasting and high carbohydrate feeding.
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- Human insulin receptors mutated at the ATP-binding site lack protein tyrosine kinase activity and fail to mediate postreceptor effects of insulin.
- Protein kinase activity of the insulin receptor.
- Effect of monoclonal antibodies on human insulin receptor autophosphorylation, negative cooperativity, and down-regulation.
- Purification of the insulin receptor from human placenta by chromatography on immobilized wheat germ lectin and receptor antibody.
- An antipeptide antibody that specifically inhibits insulin receptor autophosphorylation and protein kinase activity.
- Dual regulation of glycogen metabolism by insulin and insulin-like growth factors in human hepatoma cells (HEP-G2). Analysis with an anti-receptor monoclonal antibody.
- Insulin receptor phosphorylation may not be a prerequisite for acute insulin action.
- Insulin receptor: evidence that it is a protein kinase.
- A monoclonal antibody to human insulin receptor.
- Replacement of lysine residue 1030 in the putative ATP-binding region of the insulin receptor abolishes insulin- and antibody-stimulated glucose uptake and receptor kinase activity.
- Monoclonal antibodies to the human insulin receptor block insulin binding and inhibit insulin action.
- Effect of insulin receptor autophosphorylation on insulin receptor binding.
- Isolation of a Drosophila genomic sequence homologous to the kinase domain of the human insulin receptor and detection of the phosphorylated Drosophila receptor with an anti-peptide antibody.
- The insulin receptor and tyrosine protein kinase activity.
- Phosphorylation activates the insulin receptor tyrosine protein kinase.
- Human autoantibodies directed against the human, but not the rat, insulin receptor.
Cited by
- Direct modulation of insulin receptor protein tyrosine kinase by vanadate and anti-insulin receptor monoclonal antibodies.
- Antipeptide antibodies toward the extracellular domain of insulin receptor beta-subunit.
- Kinetics of insulin binding and kinase activity of the partially purified insulin receptor from human skeletal muscle.
- Antibodies directed to the insulin receptor. Clinical aspects and applications to the study of insulin action
- Evidence that human and porcine insulin differently affect the human insulin receptor: studies with monoclonal anti-insulin receptor antibodies
- Evidence That Two Naturally Occurring Human Insulin Receptor α-Subunit Variants Are Immunologically Distinct
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