ATP biphasically modulates LLPS of TDP-43 PLD by specifically binding arginine residues
Dang Mei et al. use NMR and microscopy approaches to examine how ATP impacts the liquid-liquid phase separation (LLPS) of prion-like domains in TDP-43, a RNA-binding protein that is implicated in ALS and other neurological disorders. Their results suggest that ATP specifically binds to a subset of T...
Guardado en:
Autores principales: | Mei Dang, Liangzhong Lim, Jian Kang, Jianxing Song |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2021
|
Materias: | |
Acceso en línea: | https://doaj.org/article/f4adf49a14ff4b13b8c5014276353840 |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
The cooperative binding of TDP-43 to GU-rich RNA repeats antagonizes TDP-43 aggregation
por: Juan Carlos Rengifo-Gonzalez, et al.
Publicado: (2021) -
Metals in ALS TDP-43 Pathology
por: Lassi Koski, et al.
Publicado: (2021) -
Tau-tubulin kinase 1 phosphorylates TDP-43 at disease-relevant sites and exacerbates TDP-43 pathology
por: Yuan Tian, et al.
Publicado: (2021) -
Endocytosis regulates TDP-43 toxicity and turnover
por: Guangbo Liu, et al.
Publicado: (2017) -
Zinc binding to RNA recognition motif of TDP-43 induces the formation of amyloid-like aggregates
por: Cyrille Garnier, et al.
Publicado: (2017)