(PDF) Interaction of Phosphatidylinositol

Interaction of Phosphatidylinositol 3-Kinase-Associated P85 With Epidermal Growth Factor and Platelet-Derived Growth Factor Receptors.

Molecular and Cellular Biology - United States

doi 10.1128/mcb.12.3.981

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Date

March 1, 1992

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American Society for Microbiology

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Interaction of Phosphatidylinositol 3-Kinase-Associated P85 With Epidermal Growth Factor and Platelet-Derived Growth Factor Receptors.

Molecular and Cellular Biology - United States

doi 10.1128/mcb.12.3.981

Full Text

Abstract

Categories

Date

Authors

Publisher

Related search

Interactions Between the Receptors for Platelet-Derived Growth Factor and Epidermal Growth Factor

ErbB3 Is Involved in Activation of Phosphatidylinositol 3-Kinase by Epidermal Growth Factor.

Platelet Derived Growth Factor a (PDGFA; PDGF1); Platelet Derived Growth Factor Receptor (PDGFR)

Requirement for Phosphatidylinositol 3′-Kinase Activity in Platelet-Derived Growth Factor-Stimulated Tyrosine Phosphorylation of P125 Focal Adhesion Kinase and Paxillin

ERK Regulates the Hepatocyte Growth Factor-Mediated Interaction of Gab1 and the Phosphatidylinositol 3-Kinase

Platelet-Derived Growth Factor Receptors Differentially Inform Intertumoral and Intratumoral Heterogeneity

Platelet-Derived Growth Factor Mimics Phorbol Diester Action on Epidermal Growth Factor Receptor Phosphorylation at Threonine-654.

The C-Terminal SH2 Domain of P85 Accounts for the High Affinity and Specificity of the Binding of Phosphatidylinositol 3-Kinase to Phosphorylated Platelet-Derived Growth Factor Beta Receptor.

Platelet-Derived Growth Factor Activates Protein Kinase C Epsilon Through Redundant and Independent Signaling Pathways Involving Phospholipase C Gamma or Phosphatidylinositol 3-Kinase.