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Tyrosine Phosphorylation of Protein Kinase C-Delta in Response to the Activation of the High-Affinity Receptor for Immunoglobulin E Modifies Its Substrate Recognition.

Proceedings of the National Academy of Sciences of the United States of America - United States

doi 10.1073/pnas.92.20.9112

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September 26, 1995

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Proceedings of the National Academy of Sciences

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Tyrosine Phosphorylation of Protein Kinase C-Delta in Response to the Activation of the High-Affinity Receptor for Immunoglobulin E Modifies Its Substrate Recognition.

Proceedings of the National Academy of Sciences of the United States of America - United States

doi 10.1073/pnas.92.20.9112

Full Text

Abstract

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Date

Authors

Publisher

Related search

Activation of the Epidermal Growth Factor Receptor Signal Transduction Pathway Stimulates Tyrosine Phosphorylation of Protein Kinase C

Activation of MEK Kinase 1 by the C-Abl Protein Tyrosine Kinase in Response to DNA Damage

Phosphorylation and Activation of Β-Adrenergic Receptor Kinase by Protein Kinase C

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

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

Aggregation of the High Affinity IgE Receptor Results in the Tyrosine Phosphorylation of the Surface Adhesion Protein PECAM-1 (CD31)

Interaction Between Protein Kinase C Δ and the C-Abl Tyrosine Kinase in the Cellular Response to Oxidative Stress

Identification of Elf-1 and B61 as High Affinity Ligands for the Receptor Tyrosine Kinase MDK1

Detergent-Resistant Membrane Domains Are Required for Mast Cell Activation but Dispensable for Tyrosine Phosphorylation Upon Aggregation of the High Affinity Receptor for IgE