Molecular structure and interactions within amyloid-like fibrils formed by a low-complexity protein sequence from FUS
The low-complexity (LC) domain mediates liquid-liquid phase separation and fibril formation of the RNA-binding protein FUS (FUsed in Sarcoma). Here, the authors combine cryo-EM, solid-state NMR measurements and MD simulations to structurally characterise the fibrils formed by the C-terminal half of...
Guardado en:
Autores principales: | Myungwoon Lee, Ujjayini Ghosh, Kent R. Thurber, Masato Kato, Robert Tycko |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2020
|
Materias: | |
Acceso en línea: | https://doaj.org/article/8142805573524157b65818c9f357da0e |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
Cryo-EM structure of amyloid fibrils formed by the entire low complexity domain of TDP-43
por: Qiuye Li, et al.
Publicado: (2021) -
RRM domain of ALS/FTD-causing FUS characteristic of irreversible unfolding spontaneously self-assembles into amyloid fibrils
por: Yimei Lu, et al.
Publicado: (2017) -
Mycobacterium tuberculosis CarD, an essential global transcriptional regulator forms amyloid-like fibrils
por: Gundeep Kaur, et al.
Publicado: (2018) -
Unlocked concanavalin A forms amyloid-like fibrils from coagulation of long-lived "crinkled" intermediates.
por: Valeria Vetri, et al.
Publicado: (2013) -
AA amyloid fibrils from diseased tissue are structurally different from in vitro formed SAA fibrils
por: Akanksha Bansal, et al.
Publicado: (2021)