Impairment of the ubiquitin-proteasome system by protein aggregation.
By Neil F. Bence, Roopal M. Sampat, R. Kopito. Science, 2001
2,082 citations recorded by the source corpus.
View Paper: https://www.semanticscholar.org/paper/2125d5e10080ef250cbabd30641e8f774534db8c
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Citations in the corpus
- A role for ubiquitin in selective autophagy. (2009, background): “Alternatively, they may inactivate the proteasome and mediate cytotoxicity (Bence et al., 2001).”
- Principles of protein folding, misfolding and aggregation. (2004, background): “Degradation pathways, such as those of the ubiquitin–proteasome system, are therefore highly regulated in order to avoid such events [80,81].”
- What is the role of protein aggregation in neurodegeneration? (2005, background): “One interesting hypothesis is that abnormal proteins might inhibit the proteasom”
- Pathogenesis of parkinson's disease: dopamine, vesicles and α-synuclein (2002, background): “gov/htbin-post/Omim/dispmim?219700">cystic fibrosis proteins can inhibit proteasomal function in vitro”
- Molecular chaperones and protein quality control. (2006, unknown): “Yet evidence of the last few years indicates that these modified proteins present a particular challenge to proteasomes, possibly leading to their inhibition (Bence et al., 2001; Bennett et al., 2005).”
- ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats. (2002, background): “…fragments with pathogenic repeat lengths are colocalized with various molecular chaperons and proteasome components (e.g., HSP70, HSP40, 20S, and 19S) (Waelter et al. 2001) and impair the function of the ubiquitine–proteasome systems (UPS) (Bence et al. 2001; Jana et al. 2001; Waelter et al. 2001).”
- ER stress and neurodegenerative diseases (2006, background): “It is generally thought that the activity of UPS is mitigated in these diseases either by the protein aggregates or by enhanced oxidative stress and other toxic products.(7,8) Dysfunctional UPS in turn cause more accumula-”
- In and out of the ER: protein folding, quality control, degradation, and related human diseases. (2007, unknown): “actually cause their inactivation (20).”
- Degradation of misfolded proteins prevents ER-derived oxidative stress and cell death. (2004, background): “process leading to ROS accumulation derives from the subsequent proteasome inhibition (Bence et al., 2001).”
- The roles of intracellular protein-degradation pathways in neurodegeneration (2006, background): “Decreased proteasome-pathway activity seems to be a feature of many cell models in which intracellular aggregates are forme”
- From endoplasmic-reticulum stress to the inflammatory response (2008, background): “Recent studies suggest that the protein aggregates associated with these diseases might inhibit the proteasome, thereby preventing ER-associated protein degradation (ERAD) and leading to the accumulation of unfolded proteins in the E”
- Amyloid-like aggregates sequester numerous metastable proteins with essential cellular functions. (2011, background): “In another model, misfolding proteins, by engaging the chaperone machinery, are thought to interfere with central protein quality control and clearance mechanisms, possibly resulting in a propagation of folding defects (Balch et al., 2008; Bence et al., 2001; Gidalevitz et al., 2006).”
- Sequestosome 1/p62 Is a Polyubiquitin Chain Binding Protein Involved in Ubiquitin Proteasome Degradation (2004, background): “Aggregation may impair the proteasome or, alternatively, impaired proteasome activity may seed aggregates (2).”
- Endoplasmic Reticulum Stress and the Unfolded Protein Response in Cellular Models of Parkinson's Disease (2002, background): “These affect protein folding in the cytoplasm and may lead to ER stress by impacting the process of ER-associated protein degradation (Bence et al., 2001; Nishtoh et al., 2002).”