Cargando…
N-Terminal Ubiquitination of Amyloidogenic Proteins Triggers Removal of Their Oligomers by the Proteasome Holoenzyme
Aggregation of amyloidogenic proteins is an abnormal biological process implicated in neurodegenerative disorders. Whereas the aggregation process of amyloid-forming proteins has been studied extensively, the mechanism of aggregate removal is poorly understood. We recently demonstrated that proteaso...
Autores principales: | Ye, Yu, Klenerman, David, Finley, Daniel |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2020
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6990400/ https://www.ncbi.nlm.nih.gov/pubmed/31518613 http://dx.doi.org/10.1016/j.jmb.2019.08.021 |
Ejemplares similares
-
Filamentous Aggregates Are Fragmented by the Proteasome Holoenzyme
por: Cliffe, Rachel, et al.
Publicado: (2019) -
Toxic oligomers of the amyloidogenic HypF-N protein form pores in mitochondrial membranes
por: Farrugia, Maria Ylenia, et al.
Publicado: (2020) -
Oxidative and salt stresses alter the 26S proteasome holoenzyme and associated protein profiles in Arabidopsis thaliana
por: Bonea, Diana, et al.
Publicado: (2021) -
SOBA: Development and testing of a soluble oligomer binding assay for detection of amyloidogenic toxic oligomers
por: Shea, Dylan, et al.
Publicado: (2022) -
HIV-1 promotes ubiquitination of the amyloidogenic C-terminal fragment of APP to support viral replication
por: Gu, Feng, et al.
Publicado: (2023)