Functional and dynamic polymerization of the ALS-linked protein TDP-43 antagonizes its pathologic aggregation

TDP-43 aggregation is observed in amyotrophic lateral sclerosis. Here the authors combine X-ray crystallography, nuclear magnetic resonance and electron microscopy studies and show that physiological oligomerization of TDP-43 is mediated through its N-terminal domain, which forms functional and dyna...

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Autores principales:	Tariq Afroz, Eva-Maria Hock, Patrick Ernst, Chiara Foglieni, Melanie Jambeau, Larissa A. B. Gilhespy, Florent Laferriere, Zuzanna Maniecka, Andreas Plückthun, Peer Mittl, Paolo Paganetti, Frédéric H. T. Allain, Magdalini Polymenidou
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/19fe9db6d453476b99cb7c03271c33ca
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spelling	oai:doaj.org-article:19fe9db6d453476b99cb7c03271c33ca2021-12-02T13:57:45ZFunctional and dynamic polymerization of the ALS-linked protein TDP-43 antagonizes its pathologic aggregation10.1038/s41467-017-00062-02041-1723https://doaj.org/article/19fe9db6d453476b99cb7c03271c33ca2017-06-01T00:00:00Zhttps://doi.org/10.1038/s41467-017-00062-0https://doaj.org/toc/2041-1723TDP-43 aggregation is observed in amyotrophic lateral sclerosis. Here the authors combine X-ray crystallography, nuclear magnetic resonance and electron microscopy studies and show that physiological oligomerization of TDP-43 is mediated through its N-terminal domain, which forms functional and dynamic oligomers antagonizing pathologic aggregation.Tariq AfrozEva-Maria HockPatrick ErnstChiara FoglieniMelanie JambeauLarissa A. B. GilhespyFlorent LaferriereZuzanna ManieckaAndreas PlückthunPeer MittlPaolo PaganettiFrédéric H. T. AllainMagdalini PolymenidouNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-15 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Tariq Afroz Eva-Maria Hock Patrick Ernst Chiara Foglieni Melanie Jambeau Larissa A. B. Gilhespy Florent Laferriere Zuzanna Maniecka Andreas Plückthun Peer Mittl Paolo Paganetti Frédéric H. T. Allain Magdalini Polymenidou Functional and dynamic polymerization of the ALS-linked protein TDP-43 antagonizes its pathologic aggregation
description	TDP-43 aggregation is observed in amyotrophic lateral sclerosis. Here the authors combine X-ray crystallography, nuclear magnetic resonance and electron microscopy studies and show that physiological oligomerization of TDP-43 is mediated through its N-terminal domain, which forms functional and dynamic oligomers antagonizing pathologic aggregation.
format	article
author	Tariq Afroz Eva-Maria Hock Patrick Ernst Chiara Foglieni Melanie Jambeau Larissa A. B. Gilhespy Florent Laferriere Zuzanna Maniecka Andreas Plückthun Peer Mittl Paolo Paganetti Frédéric H. T. Allain Magdalini Polymenidou
author_facet	Tariq Afroz Eva-Maria Hock Patrick Ernst Chiara Foglieni Melanie Jambeau Larissa A. B. Gilhespy Florent Laferriere Zuzanna Maniecka Andreas Plückthun Peer Mittl Paolo Paganetti Frédéric H. T. Allain Magdalini Polymenidou
author_sort	Tariq Afroz
title	Functional and dynamic polymerization of the ALS-linked protein TDP-43 antagonizes its pathologic aggregation
title_short	Functional and dynamic polymerization of the ALS-linked protein TDP-43 antagonizes its pathologic aggregation
title_full	Functional and dynamic polymerization of the ALS-linked protein TDP-43 antagonizes its pathologic aggregation
title_fullStr	Functional and dynamic polymerization of the ALS-linked protein TDP-43 antagonizes its pathologic aggregation
title_full_unstemmed	Functional and dynamic polymerization of the ALS-linked protein TDP-43 antagonizes its pathologic aggregation
title_sort	functional and dynamic polymerization of the als-linked protein tdp-43 antagonizes its pathologic aggregation
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/19fe9db6d453476b99cb7c03271c33ca
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Functional and dynamic polymerization of the ALS-linked protein TDP-43 antagonizes its pathologic aggregation

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