Cargando…
The AAA + ATPase TorsinA polymerizes into hollow helical tubes with 8.5 subunits per turn
TorsinA is an ER-resident AAA + ATPase, whose deletion of glutamate E303 results in the genetic neuromuscular disease primary dystonia. TorsinA is an unusual AAA + ATPase that needs an external activator. Also, it likely does not thread a peptide substrate through a narrow central channel, in contra...
Autores principales: | Demircioglu, F. Esra, Zheng, Weili, McQuown, Alexander J., Maier, Nolan K., Watson, Nicki, Cheeseman, Iain M., Denic, Vladimir, Egelman, Edward H., Schwartz, Thomas U. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2019
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6646356/ https://www.ncbi.nlm.nih.gov/pubmed/31332180 http://dx.doi.org/10.1038/s41467-019-11194-w |
Ejemplares similares
-
Intracellular complexes of the early-onset torsion dystonia-associated AAA+ ATPase TorsinA
por: Li, Hui, et al.
Publicado: (2014) -
TorsinA and the TorsinA-Interacting Protein Printor Have No Impact on Endoplasmic Reticulum Stress or Protein Trafficking in Yeast
por: Valastyan, Julie S., et al.
Publicado: (2011) -
TorsinA: a therapeutic target for ALS?
Publicado: (2014) -
TorsinA regulates the LINC to moving nuclei
por: Starr, Daniel A., et al.
Publicado: (2017) -
TorsinA controls TAN line assembly and the retrograde flow of dorsal perinuclear actin cables during rearward nuclear movement
por: Saunders, Cosmo A., et al.
Publicado: (2017)