Species-dependent structural polymorphism of Y145Stop prion protein amyloid revealed by solid-state NMR spectroscopy

Prion diseases can be transmitted across species. Here the authors use solid-state NMR to study prion protein (PrP) amyloids from human, mouse and Syrian hamster and show that their structural differences are mainly governed by two residues, which helps to understand interspecies PrP propagation on...

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Autores principales:	Theint Theint, Philippe S. Nadaud, Darryl Aucoin, Jonathan J. Helmus, Simon P. Pondaven, Krystyna Surewicz, Witold K. Surewicz, Christopher P. Jaroniec
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/9856d994aae14b16b75bab5e7b839972
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spelling	oai:doaj.org-article:9856d994aae14b16b75bab5e7b8399722021-12-02T16:51:52ZSpecies-dependent structural polymorphism of Y145Stop prion protein amyloid revealed by solid-state NMR spectroscopy10.1038/s41467-017-00794-z2041-1723https://doaj.org/article/9856d994aae14b16b75bab5e7b8399722017-09-01T00:00:00Zhttps://doi.org/10.1038/s41467-017-00794-zhttps://doaj.org/toc/2041-1723Prion diseases can be transmitted across species. Here the authors use solid-state NMR to study prion protein (PrP) amyloids from human, mouse and Syrian hamster and show that their structural differences are mainly governed by two residues, which helps to understand interspecies PrP propagation on a molecular level.Theint TheintPhilippe S. NadaudDarryl AucoinJonathan J. HelmusSimon P. PondavenKrystyna SurewiczWitold K. SurewiczChristopher P. JaroniecNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-10 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Theint Theint Philippe S. Nadaud Darryl Aucoin Jonathan J. Helmus Simon P. Pondaven Krystyna Surewicz Witold K. Surewicz Christopher P. Jaroniec Species-dependent structural polymorphism of Y145Stop prion protein amyloid revealed by solid-state NMR spectroscopy
description	Prion diseases can be transmitted across species. Here the authors use solid-state NMR to study prion protein (PrP) amyloids from human, mouse and Syrian hamster and show that their structural differences are mainly governed by two residues, which helps to understand interspecies PrP propagation on a molecular level.
format	article
author	Theint Theint Philippe S. Nadaud Darryl Aucoin Jonathan J. Helmus Simon P. Pondaven Krystyna Surewicz Witold K. Surewicz Christopher P. Jaroniec
author_facet	Theint Theint Philippe S. Nadaud Darryl Aucoin Jonathan J. Helmus Simon P. Pondaven Krystyna Surewicz Witold K. Surewicz Christopher P. Jaroniec
author_sort	Theint Theint
title	Species-dependent structural polymorphism of Y145Stop prion protein amyloid revealed by solid-state NMR spectroscopy
title_short	Species-dependent structural polymorphism of Y145Stop prion protein amyloid revealed by solid-state NMR spectroscopy
title_full	Species-dependent structural polymorphism of Y145Stop prion protein amyloid revealed by solid-state NMR spectroscopy
title_fullStr	Species-dependent structural polymorphism of Y145Stop prion protein amyloid revealed by solid-state NMR spectroscopy
title_full_unstemmed	Species-dependent structural polymorphism of Y145Stop prion protein amyloid revealed by solid-state NMR spectroscopy
title_sort	species-dependent structural polymorphism of y145stop prion protein amyloid revealed by solid-state nmr spectroscopy
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/9856d994aae14b16b75bab5e7b839972
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Species-dependent structural polymorphism of Y145Stop prion protein amyloid revealed by solid-state NMR spectroscopy

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