Cargando…
Molecular structure of an amyloid fibril formed by FUS low-complexity domain
FUS is a multifunctional nuclear protein which undergoes liquid–liquid phase separation in response to stress and DNA damage. Dysregulation of FUS dynamic phase separation leads to formation of pathological fibril closely associated with neurodegenerative diseases such as amyotrophic lateral scleros...
Autores principales: | Sun, Yunpeng, Zhang, Shenqing, Hu, Jiaojiao, Tao, Youqi, Xia, Wencheng, Gu, Jinge, Li, Yichen, Cao, Qin, Li, Dan, Liu, Cong |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2021
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8749265/ https://www.ncbi.nlm.nih.gov/pubmed/35036880 http://dx.doi.org/10.1016/j.isci.2021.103701 |
Ejemplares similares
-
Hsp70 exhibits a liquid-liquid phase separation ability and chaperones condensed FUS against amyloid aggregation
por: Li, Yichen, et al.
Publicado: (2022) -
Subtle change of fibrillation condition leads to substantial alteration of recombinant Tau fibril structure
por: Li, Xiang, et al.
Publicado: (2022) -
Generic amyloid fibrillation of TMEM106B in patient with Parkinson’s disease dementia and normal elders
por: Fan, Yun, et al.
Publicado: (2022) -
SARS-CoV-2 impairs the disassembly of stress granules and promotes ALS-associated amyloid aggregation
por: Li, Yichen, et al.
Publicado: (2022) -
Heparin induces α-synuclein to form new fibril polymorphs with attenuated neuropathology
por: Tao, Youqi, et al.
Publicado: (2022)