Associated Papers
The AAA + ATPase TorsinA polymerizes into hollow helical tubes with 8.5 subunits per turn.
Demircioglu FE et al.
Nature Communications, 2019
DYT1 Dystonia Patient-Derived Fibroblasts Have Increased Deformability and Susceptibility to Damage by Mechanical Forces.
Gill NK et al.
Frontiers in Cell and Developmental Biology, 2019
Dynamic functional assembly of the Torsin AAA+ ATPase and its modulation by LAP1.
Chase AR et al.
Molecular Biology of the Cell, 2017
Human TorsinA can function in the yeast cytosol as a molecular chaperone.
Adam I et al.
The Biochemical Journal, 2017
Structures of TorsinA and its disease-mutant complexed with an activator reveal the molecular basis for primary dystonia.
Demircioglu FE et al.
Elife, 2016
Torsin ATPases: structural insights and functional perspectives.
Laudermilch E et al.
Current Opinion in Cell Biology, 2016
LINCing defective nuclear-cytoskeletal coupling and DYT1 dystonia.
Saunders CA et al.
Cellular and Molecular Bioengineering, 2016
Torsins: not your typical AAA+ ATPases.
Rose AE et al.
Critical Reviews in Biochemistry and Molecular Biology, 2015
How lamina-associated polypeptide 1 (LAP1) activates Torsin.
Sosa BA et al.
Elife, 2014
The BiP molecular chaperone plays multiple roles during the biogenesis of torsinA, an AAA+ ATPase associated with the neurological disease early-onset torsion dystonia.
Zacchi LF et al.
The Journal of Biological Chemistry, 2014
Regulation of Torsin ATPases by LAP1 and LULL1.
Zhao C et al.
Proceedings of the National Academy of Sciences of the United States of America, 2013
Untethering the nuclear envelope and cytoskeleton: biologically distinct dystonias arising from a common cellular dysfunction.
Atai NA et al.
International Journal of Cell Biology, 2012
Static retention of the lumenal monotopic membrane protein torsinA in the endoplasmic reticulum.
Vander Heyden AB et al.
The Embo Journal, 2011
The nuclear envelope localization of DYT1 dystonia torsinA-ΔE requires the SUN1 LINC complex component.
Jungwirth MT et al.
Bmc Cell Biology, 2011
TorsinA and the torsinA-interacting protein printor have no impact on endoplasmic reticulum stress or protein trafficking in yeast.
Valastyan JS et al.
Plos One, 2011
A unique redox-sensing sensor II motif in TorsinA plays a critical role in nucleotide and partner binding.
Zhu L et al.
The Journal of Biological Chemistry, 2010
The early-onset torsion dystonia-associated protein, torsinA, is a homeostatic regulator of endoplasmic reticulum stress response.
Chen P et al.
Human Molecular Genetics, 2010
The early-onset torsion dystonia-associated protein, torsinA, displays molecular chaperone activity in vitro.
Burdette AJ et al.
Cell Stress & Chaperones, 2010
Interaction of torsinA with its major binding partners is impaired by the dystonia-associated DeltaGAG deletion.
Naismith TV et al.
The Journal of Biological Chemistry, 2009
Printor, a novel torsinA-interacting protein implicated in dystonia pathogenesis.
Giles LM et al.
The Journal of Biological Chemistry, 2009
LULL1 retargets TorsinA to the nuclear envelope revealing an activity that is impaired by the DYT1 dystonia mutation.
Vander Heyden AB et al.
Molecular Biology of the Cell, 2009
Consequences of the DYT1 mutation on torsinA oligomerization and degradation.
Gordon KL et al.
Neuroscience, 2008
TorsinA binds the KASH domain of nesprins and participates in linkage between nuclear envelope and cytoskeleton.
Nery FC et al.
Journal of Cell Science, 2008
Effects of genetic variations in the dystonia protein torsinA: identification of polymorphism at residue 216 as protein modifier.
Kock N et al.
Human Molecular Genetics, 2006
Dystonia-causing mutant torsinA inhibits cell adhesion and neurite extension through interference with cytoskeletal dynamics.
Hewett JW et al.
Neurobiology of Disease, 2006
TorsinA in the nuclear envelope.
Naismith TV et al.
Proceedings of the National Academy of Sciences of the United States of America, 2004
Abstracts of the 4th International Dystonia Symposium. Atlanta, Georgia, USA. June 13-15, 2002.
Unknown Author
Movement Disorders : Official Journal of the Movement Disorder Society, 2002