CD81 Associates with 14-3-3 in a Redox-regulated Palmitoylation-dependent Manner
Open Access
- 1 May 2004
- journal article
- Published by Elsevier
- Vol. 279 (19) , 19401-19406
- https://doi.org/10.1074/jbc.m312626200
Abstract
No abstract availableKeywords
This publication has 38 references indexed in Scilit:
- Identification of the Hepatitis C Virus E2 Glycoprotein Binding Site on the Large Extracellular Loop of CD81Journal of Virology, 2002
- Analysis of the CD151·α3β1 Integrin and CD151·Tetraspanin Interactions by MutagenesisPublished by Elsevier ,2001
- 14‐3‐3 proteins: key regulators of cell division, signalling and apoptosisBioEssays, 2001
- Identification of Amino Acid Residues in CD81 Critical for Interaction with Hepatitis C Virus Envelope Glycoprotein E2Journal of Virology, 2000
- CD81 (TAPA-1): A MOLECULE INVOLVED IN SIGNAL TRANSDUCTION AND CELL ADHESION IN THE IMMUNE SYSTEMAnnual Review of Immunology, 1998
- The Instructive Role of Innate Immunity in the Acquired Immune ResponseScience, 1996
- A Role for CD81 in Early T Cell DevelopmentScience, 1996
- The CD19/CD21 signal transduction complex of B lymphocytesImmunology Today, 1994
- The functional cell surface glycoprotein CD9 is distinguished by being the major fatty acid acylated and a major iodinated cell-surface component of the human plateletBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1988
- The functional glycoprotein CD9 is variably acylated: localization of the variably acylated region to a membrane-associated peptide containing the binding site for the agonistic monoclonal antibody 50H.19Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1988