Fibril polymorphism affects immobilized non-amyloid flanking domains of huntingtin exon1 rather than its polyglutamine core

Huntington's disease is caused by a polyglutamine stretch expansion in the first exon of huntingtin. Here, the authors use infrared spectroscopy and solid-state NMR and show that polymorphic huntingtin exon1 fibres differ in their flanking regions but not their core polyglutamine amyloid struct...

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Autores principales:	Hsiang-Kai Lin, Jennifer C. Boatz, Inge E. Krabbendam, Ravindra Kodali, Zhipeng Hou, Ronald Wetzel, Amalia M. Dolga, Michelle A. Poirier, Patrick C. A. van der Wel
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/6d1f8de6f3eb481d8704dc203117b49c
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spelling	oai:doaj.org-article:6d1f8de6f3eb481d8704dc203117b49c2021-12-02T14:42:20ZFibril polymorphism affects immobilized non-amyloid flanking domains of huntingtin exon1 rather than its polyglutamine core10.1038/ncomms154622041-1723https://doaj.org/article/6d1f8de6f3eb481d8704dc203117b49c2017-05-01T00:00:00Zhttps://doi.org/10.1038/ncomms15462https://doaj.org/toc/2041-1723Huntington's disease is caused by a polyglutamine stretch expansion in the first exon of huntingtin. Here, the authors use infrared spectroscopy and solid-state NMR and show that polymorphic huntingtin exon1 fibres differ in their flanking regions but not their core polyglutamine amyloid structures.Hsiang-Kai LinJennifer C. BoatzInge E. KrabbendamRavindra KodaliZhipeng HouRonald WetzelAmalia M. DolgaMichelle A. PoirierPatrick C. A. van der WelNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-12 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Hsiang-Kai Lin Jennifer C. Boatz Inge E. Krabbendam Ravindra Kodali Zhipeng Hou Ronald Wetzel Amalia M. Dolga Michelle A. Poirier Patrick C. A. van der Wel Fibril polymorphism affects immobilized non-amyloid flanking domains of huntingtin exon1 rather than its polyglutamine core
description	Huntington's disease is caused by a polyglutamine stretch expansion in the first exon of huntingtin. Here, the authors use infrared spectroscopy and solid-state NMR and show that polymorphic huntingtin exon1 fibres differ in their flanking regions but not their core polyglutamine amyloid structures.
format	article
author	Hsiang-Kai Lin Jennifer C. Boatz Inge E. Krabbendam Ravindra Kodali Zhipeng Hou Ronald Wetzel Amalia M. Dolga Michelle A. Poirier Patrick C. A. van der Wel
author_facet	Hsiang-Kai Lin Jennifer C. Boatz Inge E. Krabbendam Ravindra Kodali Zhipeng Hou Ronald Wetzel Amalia M. Dolga Michelle A. Poirier Patrick C. A. van der Wel
author_sort	Hsiang-Kai Lin
title	Fibril polymorphism affects immobilized non-amyloid flanking domains of huntingtin exon1 rather than its polyglutamine core
title_short	Fibril polymorphism affects immobilized non-amyloid flanking domains of huntingtin exon1 rather than its polyglutamine core
title_full	Fibril polymorphism affects immobilized non-amyloid flanking domains of huntingtin exon1 rather than its polyglutamine core
title_fullStr	Fibril polymorphism affects immobilized non-amyloid flanking domains of huntingtin exon1 rather than its polyglutamine core
title_full_unstemmed	Fibril polymorphism affects immobilized non-amyloid flanking domains of huntingtin exon1 rather than its polyglutamine core
title_sort	fibril polymorphism affects immobilized non-amyloid flanking domains of huntingtin exon1 rather than its polyglutamine core
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/6d1f8de6f3eb481d8704dc203117b49c
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Fibril polymorphism affects immobilized non-amyloid flanking domains of huntingtin exon1 rather than its polyglutamine core

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