Caspase Activation Inhibits Proteasome Function during Apoptosis

This publication has 45 references indexed in Scilit:

• Preservation of Caspase-3 Subunits from Degradation Contributes to Apoptosis Evoked by Lactacystin: Any Single Lysine or Lysine Pair of the Small Subunit Is Sufficient for Ubiquitination
  Molecular Pharmacology, 2003
• Proteasome-mediated Degradation of Smac during Apoptosis: XIAP Promotes Smac Ubiquitination in Vitro
  Journal of Biological Chemistry, 2002
• A cryptic protease couples deubiquitination and degradation by the proteasome
  Nature, 2002
• A proteasomal ATPase subunit recognizes the polyubiquitin degradation signal
  Nature, 2002
• Deadly encounter: ubiquitin meets apoptosis
  Nature Reviews Molecular Cell Biology, 2002
• Proteasome inhibitor-induced apoptosis of B-chronic lymphocytic leukaemia cells involves cytochrome c release and caspase activation, accompanied by formation of an ∼700 kDa Apaf-1 containing apoptosome complex
  Leukemia, 2001
• Mechanisms of Apoptosis
  The American Journal of Pathology, 2000
• Degradation of Ornithine Decarboxylase by the 26S Proteasome
  Biochemical and Biophysical Research Communications, 2000
• The role of the ubiquitin-proteasome pathway in apoptosis
  Cell Death & Differentiation, 1999
• A protein related to a proteasomal subunit binds to the intracellular domain of the p55 TNF receptor upstream to its ‘death domain’
  FEBS Letters, 1995