Cargando…
Oxidative regulation of TDP-43 self-association by a β-to-α conformational switch
An evolutionarily conserved region of the TDP-43 low complexity domain twenty residues in length can adopt either an α-helical or β-strand conformation. When in the latter conformation, TDP-43 self-associates via the formation of a labile, cross-β structure. Self-association can be monitored via the...
Autores principales: | Gu, Jinge, Zhou, Xiaoming, Sutherland, Lillian, Kato, Masato, Jaczynska, Klaudia, Rizo, Josep, McKnight, Steven L. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Cold Spring Harbor Laboratory
2023
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10491227/ https://www.ncbi.nlm.nih.gov/pubmed/37693418 http://dx.doi.org/10.1101/2023.08.29.555361 |
Ejemplares similares
-
Oxidative regulation of TDP-43 self-association by a β-to-α conformational switch
por: Gu, Jinge, et al.
Publicado: (2023) -
Redox-mediated regulation of an evolutionarily conserved cross-β structure formed by the TDP43 low complexity domain
por: Lin, Yi, et al.
Publicado: (2020) -
Ca(2+)-dependent release of synaptotagmin-1 from the SNARE complex on phosphatidylinositol 4,5-bisphosphate-containing membranes
por: Voleti, Rashmi, et al.
Publicado: (2020) -
Antibody against TDP-43 phosphorylated at serine 375 suggests conformational differences of TDP-43 aggregates among FTLD–TDP subtypes
por: Neumann, Manuela, et al.
Publicado: (2020) -
Molecular machinery turns full circle
por: Rizo, Josep, et al.
Publicado: (2021)