The AAA + ATPase TorsinA polymerizes into hollow helical tubes with 8.5 subunits per turn

Torsins are unusual AAA + ATPases of unknown function that reside in the endoplasmic reticulum of all animals. Here the authors report that TorsinA forms tubular helical filaments with an unusual periodicity and that filamentous TorsinA directly interacts with membranes to form tubular protrusions....

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Autores principales:	F. Esra Demircioglu, Weili Zheng, Alexander J. McQuown, Nolan K. Maier, Nicki Watson, Iain M. Cheeseman, Vladimir Denic, Edward H. Egelman, Thomas U. Schwartz
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/c1401ed5770944979beff084b9fa8646
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spelling	oai:doaj.org-article:c1401ed5770944979beff084b9fa86462021-12-02T15:35:14ZThe AAA + ATPase TorsinA polymerizes into hollow helical tubes with 8.5 subunits per turn10.1038/s41467-019-11194-w2041-1723https://doaj.org/article/c1401ed5770944979beff084b9fa86462019-07-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-11194-whttps://doaj.org/toc/2041-1723Torsins are unusual AAA + ATPases of unknown function that reside in the endoplasmic reticulum of all animals. Here the authors report that TorsinA forms tubular helical filaments with an unusual periodicity and that filamentous TorsinA directly interacts with membranes to form tubular protrusions.F. Esra DemirciogluWeili ZhengAlexander J. McQuownNolan K. MaierNicki WatsonIain M. CheesemanVladimir DenicEdward H. EgelmanThomas U. SchwartzNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-12 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q F. Esra Demircioglu Weili Zheng Alexander J. McQuown Nolan K. Maier Nicki Watson Iain M. Cheeseman Vladimir Denic Edward H. Egelman Thomas U. Schwartz The AAA + ATPase TorsinA polymerizes into hollow helical tubes with 8.5 subunits per turn
description	Torsins are unusual AAA + ATPases of unknown function that reside in the endoplasmic reticulum of all animals. Here the authors report that TorsinA forms tubular helical filaments with an unusual periodicity and that filamentous TorsinA directly interacts with membranes to form tubular protrusions.
format	article
author	F. Esra Demircioglu Weili Zheng Alexander J. McQuown Nolan K. Maier Nicki Watson Iain M. Cheeseman Vladimir Denic Edward H. Egelman Thomas U. Schwartz
author_facet	F. Esra Demircioglu Weili Zheng Alexander J. McQuown Nolan K. Maier Nicki Watson Iain M. Cheeseman Vladimir Denic Edward H. Egelman Thomas U. Schwartz
author_sort	F. Esra Demircioglu
title	The AAA + ATPase TorsinA polymerizes into hollow helical tubes with 8.5 subunits per turn
title_short	The AAA + ATPase TorsinA polymerizes into hollow helical tubes with 8.5 subunits per turn
title_full	The AAA + ATPase TorsinA polymerizes into hollow helical tubes with 8.5 subunits per turn
title_fullStr	The AAA + ATPase TorsinA polymerizes into hollow helical tubes with 8.5 subunits per turn
title_full_unstemmed	The AAA + ATPase TorsinA polymerizes into hollow helical tubes with 8.5 subunits per turn
title_sort	aaa + atpase torsina polymerizes into hollow helical tubes with 8.5 subunits per turn
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/c1401ed5770944979beff084b9fa8646
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The AAA + ATPase TorsinA polymerizes into hollow helical tubes with 8.5 subunits per turn

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