Decreased proteolysis caused by protein aggregates, inclusion bodies, plaques, lipofuscin, ceroid, and ‘aggresomes’ during oxidative stress, aging, and disease
Top Cited Papers
- 1 December 2004
- journal article
- review article
- Published by Elsevier in The International Journal of Biochemistry & Cell Biology
- Vol. 36 (12) , 2519-2530
- https://doi.org/10.1016/j.biocel.2004.04.020
Abstract
No abstract availableKeywords
This publication has 105 references indexed in Scilit:
- Proteasome inhibition by lipofuscin/ceroid during postmitotic aging of fibroblastsThe FASEB Journal, 2000
- Posttranslational Quality Control: Folding, Refolding, and Degrading ProteinsScience, 1999
- The Hydrophobic Effect Contributes to Polyubiquitin Chain RecognitionBiochemistry, 1998
- Biochemical basis of lipofuscin, ceroid, and age pigment-like fluorophoresFree Radical Biology & Medicine, 1996
- EXTRACTION AND PURIFICATION OF YELLOW-FLUORESCENT LIPOFUSCIN IN RAT KIDNEYGerontology, 1995
- OXIDATION OF FREE AMINO ACIDS AND AMINO ACID RESIDUES IN PROTEINS BY RADIOLYSIS AND BY METAL-CATALYZED REACTIONSAnnual Review of Biochemistry, 1993
- 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 processesMechanisms of Ageing and Development, 1992
- Macroxyproteinase (M.O.P.): A 670 kDa Proteinase complex that degrades oxidatively denatured proteins in red blood cellsFree Radical Biology & Medicine, 1989
- Influence of environmental stress on lipofuscin productionArchives of Gerontology and Geriatrics, 1986
- Intracellular proteolytic systems may function as secondary antioxidant defenses: An hypothesisJournal of Free Radicals in Biology & Medicine, 1986