WW- and SH3-Domain Interactions with Epstein-Barr Virus LMP2A
- 1 June 2000
- journal article
- Published by Elsevier in Experimental Cell Research
- Vol. 257 (2) , 332-340
- https://doi.org/10.1006/excr.2000.4900
Abstract
No abstract availableKeywords
This publication has 52 references indexed in Scilit:
- Signal transduction from the B cell antigen-receptorCurrent Opinion in Immunology, 1999
- Sequence polymorphisms between latent membrane proteins LMP1 and LMP2A do not correlate in EBV-associated reactive and malignant lympho-proliferationsInternational Journal of Cancer, 1999
- B cell development: signal transduction by antigen receptors and their surrogatesCurrent Opinion in Immunology, 1999
- From Src Homology domains to other signaling modules: proposal of the `protein recognition code'Oncogene, 1998
- The Immunoreceptor Tyrosine-Based Activation Motif of Epstein–Barr Virus LMP2A Is Essential for Blocking BCR-Mediated Signal TransductionVirology, 1997
- FBP WW domains and the Abl SH3 domain bind to a specific class of proline-rich ligandsThe EMBO Journal, 1997
- Integral membrane protein 2 of Epstein—barr virus regulates reactivation from latency through dominant negative effects on protein-tyrosine kinasesImmunity, 1995
- Sequence polymorphism in the Epstein--Barr virus latent membrane protein (LMP)-2 geneJournal of General Virology, 1995
- Proteins with SH2 and SH3 domains couple receptor tyrosine kinases to intracellular signalling pathwaysPhilosophical Transactions Of The Royal Society B-Biological Sciences, 1993
- The Terminal Protein Gene 2 of Epstein-Barr Virus Is Transcribed from a Bidirectional Latent Promoter RegionJournal of General Virology, 1989