Impairment of the ubiquitin-proteasome system by protein aggregation.
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Summary
It is reported that protein aggregation directly impaired the function of the ubiquitin-proteasome system, suggesting a potential mechanism linking protein aggregation to cellular disregulation and cell death.
- Type
- article
- Published
- 2001-05-25
- Cited by
- 2,084
- References
- 14
- OpenAlex
- https://openalex.org/W1997369314
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:46466882
Keywords
Proteasome, Ubiquitin, Cell biology, Proteolysis, Protein aggregation
References
- Ubiquitin‐mediated proteolysis: biological regulation via destruction
- Intermediate filaments and ubiquitin: a new thread in the understanding of chronic neurodegenerative diseases.
- Abortive oncogeny and cell cycle-mediated events in Alzheimer disease.
- In vivo inhibition of cyclin B degradation and induction of cell-cycle arrest in mammalian cells by the neutral cysteine protease inhibitor N-acetylleucylleucylnorleucinal.
- Degradation signals for ubiquitin system proteolysis in Saccharomyces cerevisiae
- Thermolability of ubiquitin-activating enzyme from the mammalian cell cycle mutant ts85.
- Multicatalytic proteinase is present in Lewy bodies and neurofibrillary tangles in diffuse Lewy body disease brains.
- Glutamine repeats as polar zippers: their possible role in inherited neurodegenerative diseases.
- Processive Degradation of Proteins and Other Catalytic Properties of the Proteasome from Thermoplasma acidophilum*
- Glutamine repeats and neurodegeneration.
- Aggresomes: A Cellular Response to Misfolded Proteins
- Characterization and Dynamics of Aggresome Formation by a Cytosolic Gfp-Chimera✪
- Molecular pathogenesis of movement disorders: are protein aggregates a common link in neuronal degeneration?
- An inhibitor of the chymotrypsin-like activity of the multicatalytic proteinase complex (20S proteasome) induces arrest in G2-phase and metaphase in HeLa cells.
Cited by
- Endoplasmic reticulum stress in brain damage.
- Trinucleotide repeat disease. The androgen receptor in spinal and bulbar muscular atrophy.
- A NOVEL CLASS OF IMMUNOPROTEASOME CATALYTIC SUBUNIT LMP2 INHIBITOR AND ITS THERAPEUTIC POTENTIALS IN CANCER
- Identification of novel factors that promote trinucleotide repeat instability
- Current understanding on the pathogenesis of polyglutamine diseases
- Loss of Uch-L1 and Uch-L3 leads to neurodegeneration, posterior paralysis and dysphagia.
- Expansion explosion: new clues to the pathogenesis of repeat expansion neurodegenerative diseases.
- Huntington's disease: a synaptopathy?
- Toxic RNA in the nucleus: unstable microsatellite expression in neuromuscular disease.
- Molecular genetics approaches in yeast to study amyloid diseases
- Oxidative stress, induced by 6-hydroxydopamine, reduces proteasome activities in PC12 cells
- Cutting Edge: Microbial Products Elicit Formation of Dendritic Cell Aggresome-Like Induced Structures in Macrophages1
- A surfactant protein C precursor protein BRICHOS domain mutation causes endoplasmic reticulum stress, proteasome dysfunction, and caspase 3 activation.
- p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death
- The ubiquitin-proteasome system: focus on the heart.
- Stochastic kinetics of intracellular huntingtin aggregate formation
- Glutathione protects cells against arsenite-induced toxicity.
- Mechanisms of disease II: cellular protein quality control.
- Protein quality control: the who’s who, the where’s and therapeutic escapes
- Proteomic and oxidative stress analysis in human brain samples of Huntington disease.
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