The role of COOH-terminal and acidic domains in the activity and stability of human insulin receptor protein tyrosine kinase studied by purified deletion mutants of the beta subunit domain.-Reference-Cited by-同舟云学术

The role of COOH-terminal and acidic domains in the activity and stability of human insulin receptor protein tyrosine kinase studied by purified deletion mutants of the beta subunit domain.

Published:1993-10 Issue:30 Volume:268 Page:22444-22449
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Yan P.F.,Li S.L.,Liang S.J.,Giannini S,Fujita-Yamaguchi Y

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference27 articles.

1. Oncogenes and signal transduction

2. SH2 and SH3 domains: elements that control interactions of cytoplasmic signaling proteins

3. Growth factor signaling by receptor tyrosine kinases

4. Structure of the insulin receptor substrate IRS-1 defines a unique signal transduction protein

5. Phosphatidylinositol 3′-kinase is activated by association with IRS-1 during insulin stimulation.

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1. Autophosphorylation of the two C-terminal tyrosine residues Tyr1316and Tyr1322modulates the activity of the insulin receptor kinase in vitro;FEBS Letters;2000-08-07

2. The carboxyl-terminal domain of insulin-like growth factor-I receptor interacts with the insulin receptor and activates its protein tyrosine kinase;FEBS Letters;1998-01-02

3. Regulation of Insulin Action by Protein Tyrosine Phosphatases;Vitamins & Hormones;1998

4. Regulation of the insulin signalling pathway by cellular protein-tyrosine phosphatases;Insulin Action;1998

5. A Synthetic Peptide Derived from a COOH-terminal Domain of the Insulin Receptor Specifically Enhances Insulin Receptor Signaling;Journal of Biological Chemistry;1996-12