Kinetic properties of the insulin receptor tyrosine protein kinase: Activation through an insulin-stimulated tyrosine-specific, intramolecular autophosphorylation-Reference-Cited by-同舟云学术

Kinetic properties of the insulin receptor tyrosine protein kinase: Activation through an insulin-stimulated tyrosine-specific, intramolecular autophosphorylation

Published:1986-01 Issue:1 Volume:244 Page:102-113
ISSN:0003-9861
Container-title:Archives of Biochemistry and Biophysics
language:en
Short-container-title:Archives of Biochemistry and Biophysics

Author:

Kwok Yan C.,Nemenoff Raphael A.,Powers Alvin C.,Avruch Joseph

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics

Reference25 articles.

1. Insulin stimulation of phosphorylation of the beta subunit of the insulin receptor. Formation of both phosphoserine and phosphotyrosine.

2. Phosphorylation of the hepatic insulin receptor

3. Insulin stimulates tyrosine phosphorylation of the insulin receptor in a cell-free system

4. Insulin-stimulated tyrosine phosphorylation of the insulin receptor in detergent extracts of human placental membranes. Comparison to epidermal growth factor-stimulated phosphorylation.

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

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