Selective degradation of oxidatively modified protein substrates by the proteasome

This publication has 92 references indexed in Scilit:

• Recent developments in the intracellular degradation of oxidized proteins 1,2 1Guest Editor: Earl Stadtman 2This article is part of a series of reviews on “Oxidatively Modified Proteins in Aging and Disease.” The full list of papers may be found on the homepage of the journal.
  Free Radical Biology & Medicine, 2002
• Ezrin turnover and cell shape changes catalyzed by proteasome in oxidatively stressed cells
  The FASEB Journal, 2002
• Oxidative Stress-Associated Impairment of Proteasome Activity during Ischemia–Reperfusion Injury
  Journal of Cerebral Blood Flow & Metabolism, 2000
• Structure of 20S proteasome from yeast at 2.4Å resolution
  Nature, 1997
• Biochemical basis of lipofuscin, ceroid, and age pigment-like fluorophores
  Free Radical Biology & Medicine, 1996
• OH• treatment of tetanus toxin reduces its susceptibility to limited proteolysis with more efficient presentation to specific T cells
  Molecular Immunology, 1993
• The intracellular storage and turnover of apolipoprotein B of oxidized LDL in macrophages
  Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1992
• Lipofuscin-like fluorophores can result from reactions between oxidized ascorbic acid and glutamine. Carbonyl-protein cross-linking may represent a common reaction in oxygen radical and glycosylation-related ageing processes
  Mechanisms of Ageing and Development, 1992
• Macroxyproteinase (M.O.P.): A 670 kDa Proteinase complex that degrades oxidatively denatured proteins in red blood cells
  Free Radical Biology & Medicine, 1989
• Intracellular proteolytic systems may function as secondary antioxidant defenses: An hypothesis
  Journal of Free Radicals in Biology & Medicine, 1986