Huntingtin fibrils with different toxicity, structure, and seeding potential can be interconverted

Huntingtin exon-1 (HTTex1) consists of a N-terminal N17 domain, the disease causing polyQ domain and a C-terminal proline-rich domain (PRD). Here, the authors combine electron paramagnetic resonance (EPR), solid-state NMR with other biophysical method to characterise the structural differences of va...

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Autores principales:	J. Mario Isas, Nitin K. Pandey, Hui Xu, Kazuki Teranishi, Alan K. Okada, Ellisa K. Fultz, Anoop Rawat, Anise Applebaum, Franziska Meier, Jeannie Chen, Ralf Langen, Ansgar B. Siemer
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/a3ad6629dcdc4912b80f4ba73af97d8a
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spelling	oai:doaj.org-article:a3ad6629dcdc4912b80f4ba73af97d8a2021-12-02T15:33:05ZHuntingtin fibrils with different toxicity, structure, and seeding potential can be interconverted10.1038/s41467-021-24411-22041-1723https://doaj.org/article/a3ad6629dcdc4912b80f4ba73af97d8a2021-07-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-24411-2https://doaj.org/toc/2041-1723Huntingtin exon-1 (HTTex1) consists of a N-terminal N17 domain, the disease causing polyQ domain and a C-terminal proline-rich domain (PRD). Here, the authors combine electron paramagnetic resonance (EPR), solid-state NMR with other biophysical method to characterise the structural differences of various HTTex1 fibril types with different toxicity and find that the dynamics and entanglement of the PRD domain differs among them and that the HTTex1 fibrils can be interconverted.J. Mario IsasNitin K. PandeyHui XuKazuki TeranishiAlan K. OkadaEllisa K. FultzAnoop RawatAnise ApplebaumFranziska MeierJeannie ChenRalf LangenAnsgar B. SiemerNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-11 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q J. Mario Isas Nitin K. Pandey Hui Xu Kazuki Teranishi Alan K. Okada Ellisa K. Fultz Anoop Rawat Anise Applebaum Franziska Meier Jeannie Chen Ralf Langen Ansgar B. Siemer Huntingtin fibrils with different toxicity, structure, and seeding potential can be interconverted
description	Huntingtin exon-1 (HTTex1) consists of a N-terminal N17 domain, the disease causing polyQ domain and a C-terminal proline-rich domain (PRD). Here, the authors combine electron paramagnetic resonance (EPR), solid-state NMR with other biophysical method to characterise the structural differences of various HTTex1 fibril types with different toxicity and find that the dynamics and entanglement of the PRD domain differs among them and that the HTTex1 fibrils can be interconverted.
format	article
author	J. Mario Isas Nitin K. Pandey Hui Xu Kazuki Teranishi Alan K. Okada Ellisa K. Fultz Anoop Rawat Anise Applebaum Franziska Meier Jeannie Chen Ralf Langen Ansgar B. Siemer
author_facet	J. Mario Isas Nitin K. Pandey Hui Xu Kazuki Teranishi Alan K. Okada Ellisa K. Fultz Anoop Rawat Anise Applebaum Franziska Meier Jeannie Chen Ralf Langen Ansgar B. Siemer
author_sort	J. Mario Isas
title	Huntingtin fibrils with different toxicity, structure, and seeding potential can be interconverted
title_short	Huntingtin fibrils with different toxicity, structure, and seeding potential can be interconverted
title_full	Huntingtin fibrils with different toxicity, structure, and seeding potential can be interconverted
title_fullStr	Huntingtin fibrils with different toxicity, structure, and seeding potential can be interconverted
title_full_unstemmed	Huntingtin fibrils with different toxicity, structure, and seeding potential can be interconverted
title_sort	huntingtin fibrils with different toxicity, structure, and seeding potential can be interconverted
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/a3ad6629dcdc4912b80f4ba73af97d8a
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Huntingtin fibrils with different toxicity, structure, and seeding potential can be interconverted

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