Cargando…
The Role of Post-Translational Modifications on Prion-Like Aggregation and Liquid-Phase Separation of FUS
Subcellular mislocalization and aggregation of the human FUS protein occurs in neurons of patients with subtypes of amyotrophic lateral sclerosis and frontotemporal dementia. FUS is one of several RNA-binding proteins that can functionally self-associate into distinct liquid-phase droplet structures...
Autores principales: | Rhoads, Shannon N., Monahan, Zachary T., Yee, Debra S., Shewmaker, Frank P. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2018
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5877747/ https://www.ncbi.nlm.nih.gov/pubmed/29547565 http://dx.doi.org/10.3390/ijms19030886 |
Ejemplares similares
-
Phosphorylation of the FUS low‐complexity domain disrupts phase separation, aggregation, and toxicity
por: Monahan, Zachary, et al.
Publicado: (2017) -
Yeast Models of Prion-Like Proteins That Cause Amyotrophic Lateral Sclerosis Reveal Pathogenic Mechanisms
por: Monahan, Zachary T., et al.
Publicado: (2018) -
The prion-like domain of Fused in Sarcoma is phosphorylated by multiple kinases affecting liquid- and solid-phase transitions
por: Owen, Izzy, et al.
Publicado: (2020) -
The prionlike domain of FUS is multiphosphorylated following DNA damage without altering nuclear localization
por: Rhoads, Shannon N., et al.
Publicado: (2018) -
Post-translational modifications in liquid-liquid phase separation: a comprehensive review
por: Li, Jingxian, et al.
Publicado: (2022)