Cargando…
Does inactivation of USP14 enhance degradation of proteasomal substrates that are associated with neurodegenerative diseases?
A common pathological hallmark of age-related neurodegenerative diseases is the intracellular accumulation of protein aggregates such as α-synuclein in Parkinson’s disease, TDP-43 in ALS, and tau in Alzheimer’s disease. Enhancing intracellular clearance of aggregation-prone proteins is a plausible s...
Autores principales: | Ortuno, Daniel, Carlisle, Holly J., Miller, Silke |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
F1000Research
2016
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4792207/ https://www.ncbi.nlm.nih.gov/pubmed/26998235 http://dx.doi.org/10.12688/f1000research.7800.2 |
Ejemplares similares
-
Facilitated Tau Degradation by USP14 Aptamers via Enhanced Proteasome Activity
por: Lee, Jung Hoon, et al.
Publicado: (2015) -
USP14 deubiquitinates proteasome-bound substrates that are ubiquitinated at multiple sites
por: Lee, Byung-Hoon, et al.
Publicado: (2016) -
Enhancement of Proteasome Activity by a Small-Molecule Inhibitor of Usp14
por: Lee, Byung-Hoon, et al.
Publicado: (2010) -
TRIM11 activates the proteasome and promotes overall protein degradation by regulating USP14
por: Chen, Liang, et al.
Publicado: (2018) -
Mutant ubiquitin found in neurodegenerative disorders is a ubiquitin fusion degradation substrate that blocks proteasomal degradation
por: Lindsten, Kristina, et al.
Publicado: (2002)