The cooperative binding of TDP-43 to GU-rich RNA repeats antagonizes TDP-43 aggregation
TDP-43 is a nuclear RNA-binding protein that forms neuronal cytoplasmic inclusions in two major neurodegenerative diseases, ALS and FTLD. While the self-assembly of TDP-43 by its structured N-terminal and intrinsically disordered C-terminal domains has been widely studied, the mechanism by which mRN...
Enregistré dans:
Auteurs principaux: | Juan Carlos Rengifo-Gonzalez, Krystel El Hage, Marie-Jeanne Clément, Emilie Steiner, Vandana Joshi, Pierrick Craveur, Dominique Durand, David Pastré, Ahmed Bouhss |
---|---|
Format: | article |
Langue: | EN |
Publié: |
eLife Sciences Publications Ltd
2021
|
Sujets: | |
Accès en ligne: | https://doaj.org/article/de0ec8831ecd4f1da1a28a35d038e526 |
Tags: |
Ajouter un tag
Pas de tags, Soyez le premier à ajouter un tag!
|
Documents similaires
-
Metals in ALS TDP-43 Pathology
par: Lassi Koski, et autres
Publié: (2021) -
Tau-tubulin kinase 1 phosphorylates TDP-43 at disease-relevant sites and exacerbates TDP-43 pathology
par: Yuan Tian, et autres
Publié: (2021) -
Endocytosis regulates TDP-43 toxicity and turnover
par: Guangbo Liu, et autres
Publié: (2017) -
Functional and dynamic polymerization of the ALS-linked protein TDP-43 antagonizes its pathologic aggregation
par: Tariq Afroz, et autres
Publié: (2017) -
TDP-43 stabilises the processing intermediates of mitochondrial transcripts
par: Keiichi Izumikawa, et autres
Publié: (2017)