Phosphorylation of synthetic insulin receptor peptides by the insulin receptor kinase and evidence that the preferred sequence containing Tyr-1150 is phosphorylated in vivo.-Reference-Cited by-同舟云学术

Phosphorylation of synthetic insulin receptor peptides by the insulin receptor kinase and evidence that the preferred sequence containing Tyr-1150 is phosphorylated in vivo.

Published:1986-07 Issue:21 Volume:261 Page:10000-10005
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Stadtmauer L,Rosen O M

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference23 articles.

1. Tyrosine-specific protein kinase activity is associated with the purified insulin receptor.

2. Insulin receptor is an insulin-dependent tyrosine protein kinase: copurification of insulin-binding activity and protein kinase activity to homogeneity from human placenta.

3. Phosphorylation activates the insulin receptor tyrosine protein kinase.

4. Tyrosine phosphorylation of the insulin receptor beta subunit activates the receptor-associated tyrosine kinase activity.

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

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1. Resin immobilized synthetic peptides used to characterize phosphorylation and antigenic properties of insulin receptor autophosphorylation domains;International Journal of Peptide and Protein Research;2009-01-12

2. Insulin Receptor Tyrosine Kinase;Comprehensive Physiology;2001-12

3. Identification of Ser1275 and Ser1309 as Autophosphorylation Sites of the Human Insulin Receptor in Intact Cells;Biochemical and Biophysical Research Communications;2001-03

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

5. A Cellular Reporter Assay to Monitor Insulin Receptor Kinase Activity Based on STAT 5-Dependent Luciferase Gene Expression;Analytical Biochemistry;1999-12