The Cellular Protein PRA1 Modulates the Anti-apoptotic Activity of Epstein-Barr Virus BHRF1, a Homologue of Bcl-2, through Direct Interaction

This publication has 52 references indexed in Scilit:

• A novel protein, RTN-xS, interacts with both Bcl-xL and Bcl-2 on endoplasmic reticulum and reduces their anti-apoptotic activity
  Oncogene, 2000
• PRA1 Inhibits the Extraction of Membrane-bound Rab GTPase by GDI1
  Published by Elsevier ,2000
• Bis, a Bcl-2-binding protein that synergizes with Bcl-2 in preventing cell death
  Oncogene, 1999
• Interaction Cloning and Characterization of the cDNA Encoding the Human Prenylated Rab Acceptor (PRA1)
  Biochemical and Biophysical Research Communications, 1999
• Characterization of monoclonal antibodies to the Zta and DNase proteins of epstein-barr virus
  Journal of Biomedical Science, 1997
• The Release of Cytochrome c from Mitochondria: A Primary Site for Bcl-2 Regulation of Apoptosis
  Science, 1997
• Apoptosis in the Pathogenesis and Treatment of Disease
  Science, 1995
• Dissection of functional domains in Bcl-2α by site-directed mutagenesis
  Biochemistry and Cell Biology, 1994
• The protein bcl-2 alpha does not require membrane attachment, but two conserved domains to suppress apoptosis.
  The Journal of cell biology, 1994
• Characteristics of a Human Cell Line Transformed by DNA from Human Adenovirus Type 5
  Journal of General Virology, 1977