Differential Impairment of 20S and 26S Proteasome Activities in Human Hematopoietic K562 Cells during Oxidative Stress
- 1 May 2000
- journal article
- Published by Elsevier in Archives of Biochemistry and Biophysics
- Vol. 377 (1) , 65-68
- https://doi.org/10.1006/abbi.2000.1717
Abstract
No abstract availableThis publication has 15 references indexed in Scilit:
- Poly-ADP ribose polymerase activates nuclear proteasome to degrade oxidatively damaged histonesProceedings of the National Academy of Sciences, 1999
- Protection from oxidative inactivation of the 20S proteasome byheat-shock protein 90Biochemical Journal, 1998
- Methionine residues as endogenous antioxidants in proteinsProceedings of the National Academy of Sciences, 1996
- Age-Related Decline of Rat Liver Multicatalytic Proteinase Activity and Protection from Oxidative Inactivation by Heat-Shock Protein 90Archives of Biochemistry and Biophysics, 1996
- STRUCTURE AND FUNCTIONS OF THE 20S AND 26S PROTEASOMESAnnual Review of Biochemistry, 1996
- Activation of the Multicatalytic Endopeptidase by Oxidants. Effects on Enzyme StructureBiochemistry, 1996
- Proteolysis in Cultured Liver Epithelial Cells during Oxidative StressJournal of Biological Chemistry, 1995
- OXIDATION OF FREE AMINO ACIDS AND AMINO ACID RESIDUES IN PROTEINS BY RADIOLYSIS AND BY METAL-CATALYZED REACTIONSAnnual Review of Biochemistry, 1993
- Ubiquitin is a common factor in intermediate filament inclusion bodies of diverse type in man, including those of Parkinson's disease, Pick's disease, and Alzheimer's disease, as well as Rosenthal fibres in cerebellar astrocytomas, cytoplasmic bodies in muscle, and mallory bodies in alcoholic liver diseaseThe Journal of Pathology, 1988
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970