Tumor Necrosis Factor-α Induces Bax-Bak Interaction and Apoptosis, Which Is Inhibited by Adenovirus E1B 19K

This publication has 38 references indexed in Scilit:

• E1B 19K Blocks Bax Oligomerization and Tumor Necrosis Factor Alpha-Mediated Apoptosis
  Journal of Virology, 2001
• Proapoptotic BAX and BAK: A Requisite Gateway to Mitochondrial Dysfunction and Death
  Science, 2001
• Insertion and Organization within Membranes of the δ-Endotoxin Pore-forming Domain, Helix 4-Loop-Helix 5, and Inhibition of Its Activity by a Mutant Helix 4 Peptide
  Journal of Biological Chemistry, 2000
• Identification of DIABLO, a Mammalian Protein that Promotes Apoptosis by Binding to and Antagonizing IAP Proteins
  Cell, 2000
• Smac, a Mitochondrial Protein that Promotes Cytochrome c–Dependent Caspase Activation by Eliminating IAP Inhibition
  Cell, 2000
• Interaction of E1B 19K with Bax is required to block Bax-induced loss of mitochondrial membrane potential and apoptosis
  Oncogene, 1998
• Structure of Bcl-x _L -Bak Peptide Complex: Recognition Between Regulators of Apoptosis
  Science, 1997
• Apoptosis by Death Factor
  Cell, 1997
• The E1B 19K protein blocks apoptosis by interacting with and inhibiting the p53-inducible and death-promoting Bax protein.
  Genes & Development, 1996
• Contenders in FasL/TNF death signaling
  Cell, 1995