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Novel Role of Phosphatidylinositol 3-Kinase in CD28-mediated Costimulation

Data up to Jan 2025

Published2001
Citations51
References43

Total Citations Per Year

Abstract

References (43)

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The cytoplasmic domain of CD28 is both necessary and sufficient for costimulation of interleukin-2 secretion and association with phosphatidylinositol 3'-kinase.

1994 • 145 citations

Superantigen responses and co-stimulation: CD28 and CTLA-4 have opposing effects on T cell expansion in vitro and in vivo

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Microinjection of activated phosphatidylinositol-3 kinase induces process outgrowth in rat PC12 cells through the Rac-JNK signal transduction pathway

1998 • 128 citations

Growth Factor Receptor-bound Protein 2 SH2/SH3 Domain Binding to CD28 and Its Role in Co-signaling

1998 • 127 citations

Distinct signal transduction in mouse CD4+ and CD8+ splenic T cells after CD28 receptor ligation.

1995 • 125 citations

Selective CD28pYMNM mutations implicate phosphatidylinositol 3-kinase in CD86-CD28-mediated costimulation

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CD28-mediated up-regulation of beta 1-integrin adhesion involves phosphatidylinositol 3-kinase.

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Both CD28 ligands CD80 (B7-1) and CD86 (B7-2) activate phosphatidylinositol 3-kinase, and wortmannin reveals heterogeneity in the regulation of T cell IL-2 secretion

1995 • 74 citations

Grb2 Forms an Inducible Protein Complex with CD28 through a Src Homology 3 Domain-Proline Interaction

1998 • 69 citations

CD28 delivers costimulatory signals independently of its association with phosphatidylinositol 3-kinase.

1995 • 66 citations

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2000 • 44 citations

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1996 • 40 citations

Phorbol ester treatment inhibits phosphatidylinositol 3-kinase activation by, and association with, CD28, a T-lymphocyte surface receptor.

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Novel Role of Phosphatidylinositol 3-Kinase in CD28-mediated Costimulation (2001) – Journal of Biological Chemistry | Metascience Observatory Explorer