A naturally occurring mutation of insulin receptor alanine 1134 impairs tyrosine kinase function and is associated with dominantly inherited insulin resistance.-Reference-Cited by-同舟云学术

A naturally occurring mutation of insulin receptor alanine 1134 impairs tyrosine kinase function and is associated with dominantly inherited insulin resistance.

Published:1990-09 Issue:25 Volume:265 Page:14979-14985
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Moller D.E.,Yokota A.,White M.F.,Pazianos A.G.,Flier J.S.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference52 articles.

1. The insulin receptor and the molecular mechanism of insulin action.

2. Insulin rapidly stimulates tyrosine phosphorylation of a Mr-185,000 protein in intact cells

3. Insulin rapidly stimulates phosphorylation of a 46-kDa membrane protein on tyrosine residues as well as phosphorylation of several soluble proteins in intact fat cells.

4. Insulin stimulates phosphorylation of a 120-kDa glycoprotein substrate (pp120) for the receptor-associated protein kinase in intact H-35 hepatoma cells.

5. Replacement of insulin receptor tyrosine residues 1162 and 1163 compromises insulin-stimulated kinase activity and uptake of 2-deoxyglucose

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