Cargando…
Conserved Acidic Amino Acid Residues in a Second RNA Recognition Motif Regulate Assembly and Function of TDP-43
Accumulating evidence suggests that pathogenic TAR DNA-binding protein (TDP)-43 fragments contain a partial RNA-recognition motif domain 2 (RRM2) in amyotrophic lateral sclerosis (ALS)/frontotemporal lobar degeneration. However, the molecular basis for how this domain links to the conformation and f...
Autores principales: | Shodai, Akemi, Ido, Akemi, Fujiwara, Noriko, Ayaki, Takashi, Morimura, Toshifumi, Oono, Miki, Uchida, Tsukasa, Takahashi, Ryosuke, Ito, Hidefumi, Urushitani, Makoto |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2012
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3530536/ https://www.ncbi.nlm.nih.gov/pubmed/23300771 http://dx.doi.org/10.1371/journal.pone.0052776 |
Ejemplares similares
-
CUL2-mediated clearance of misfolded TDP-43 is paradoxically affected by VHL in oligodendrocytes in ALS
por: Uchida, Tsukasa, et al.
Publicado: (2016) -
Elimination of TDP-43 inclusions linked to amyotrophic lateral sclerosis by a misfolding-specific intrabody with dual proteolytic signals
por: Tamaki, Yoshitaka, et al.
Publicado: (2018) -
Failure of DNA double-strand break repair by tau mediates Alzheimer’s disease pathology in vitro
por: Asada-Utsugi, Megumi, et al.
Publicado: (2022) -
Conformational change of RNA-helicase DHX30 by ALS/FTD-linked FUS induces mitochondrial dysfunction and cytosolic aggregates
por: Hikiami, Ryota, et al.
Publicado: (2022) -
Molecular Dissection of TDP-43 as a Leading Cause of ALS/FTLD
por: Tamaki, Yoshitaka, et al.
Publicado: (2022)