(PDF) Protein Kinase C Isoforms Α, Δ and Θ Require Insulin

Protein Kinase C Isoforms Α, Δ and Θ Require Insulin Receptor Substrate-1 to Inhibit the Tyrosine Kinase Activity of the Insulin Receptor in Human Kidney Embryonic Cells (HEK 293 Cells)

Diabetologia - Germany

doi 10.1007/s001250050995

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June 25, 1998

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Springer Science and Business Media LLC

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Protein Kinase C Isoforms Α, Δ and Θ Require Insulin Receptor Substrate-1 to Inhibit the Tyrosine Kinase Activity of the Insulin Receptor in Human Kidney Embryonic Cells (HEK 293 Cells)

Diabetologia - Germany

doi 10.1007/s001250050995

Full Text

Abstract

Categories

Date

Authors

Publisher

Related search

Insulin Receptor Is an Insulin-Dependent Tyrosine Protein Kinase: Copurification of Insulin-Binding Activity and Protein Kinase Activity to Homogeneity From Human Placenta.

Protein Kinase C Directly Phosphorylates the Insulin Receptor in Vitro and Reduces Its Protein-Tyrosine Kinase Activity.

Protein Kinase Activity of the Insulin Receptor

Protein Kinase C-Ζ-Induced Phosphorylation of Ser318in Insulin Receptor Substrate-1 (IRS-1) Attenuates the Interaction With the Insulin Receptor and the Tyrosine Phosphorylation of IRS-1

Serine Residues 994 and 1023/25 Are Important for Insulin Receptor Kinase Inhibition by Protein Kinase C Isoforms Β2 and Θ

S-Nitrosation of the Insulin Receptor, Insulin Receptor Substrate 1, and Protein Kinase B/Akt: A Novel Mechanism of Insulin Resistance

Protein Kinase C in Insulin Releasing Cells

Human Insulin Receptor Substrate-1 (IRS-1) Polymorphism G972R Causes IRS-1 to Associate With the Insulin Receptor and Inhibit Receptor Autophosphorylation

Insulin Receptor Substrate-2 Mediated Insulin-Like Growth Factor-I Receptor Overexpression in Pancreatic Adenocarcinoma Through Protein Kinase C