Cryo-EM fibril structures from systemic AA amyloidosis reveal the species complementarity of pathological amyloids

Systemic AA amyloidosis is caused by misfolding of the acute phase protein serum amyloid A1. Here the authors present the cryo-EM structures of murine and human AA amyloid fibrils that were isolated from tissue samples and describe how the fibrils differ in their fundamental structural properties.

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Autores principales:	Falk Liberta, Sarah Loerch, Matthies Rennegarbe, Angelika Schierhorn, Per Westermark, Gunilla T. Westermark, Bouke P. C. Hazenberg, Nikolaus Grigorieff, Marcus Fändrich, Matthias Schmidt
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/a47ab7cd22cf43a58ce79e21f975d4b7
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spelling	oai:doaj.org-article:a47ab7cd22cf43a58ce79e21f975d4b72021-12-02T16:50:59ZCryo-EM fibril structures from systemic AA amyloidosis reveal the species complementarity of pathological amyloids10.1038/s41467-019-09033-z2041-1723https://doaj.org/article/a47ab7cd22cf43a58ce79e21f975d4b72019-03-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-09033-zhttps://doaj.org/toc/2041-1723Systemic AA amyloidosis is caused by misfolding of the acute phase protein serum amyloid A1. Here the authors present the cryo-EM structures of murine and human AA amyloid fibrils that were isolated from tissue samples and describe how the fibrils differ in their fundamental structural properties.Falk LibertaSarah LoerchMatthies RennegarbeAngelika SchierhornPer WestermarkGunilla T. WestermarkBouke P. C. HazenbergNikolaus GrigorieffMarcus FändrichMatthias SchmidtNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-10 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Falk Liberta Sarah Loerch Matthies Rennegarbe Angelika Schierhorn Per Westermark Gunilla T. Westermark Bouke P. C. Hazenberg Nikolaus Grigorieff Marcus Fändrich Matthias Schmidt Cryo-EM fibril structures from systemic AA amyloidosis reveal the species complementarity of pathological amyloids
description	Systemic AA amyloidosis is caused by misfolding of the acute phase protein serum amyloid A1. Here the authors present the cryo-EM structures of murine and human AA amyloid fibrils that were isolated from tissue samples and describe how the fibrils differ in their fundamental structural properties.
format	article
author	Falk Liberta Sarah Loerch Matthies Rennegarbe Angelika Schierhorn Per Westermark Gunilla T. Westermark Bouke P. C. Hazenberg Nikolaus Grigorieff Marcus Fändrich Matthias Schmidt
author_facet	Falk Liberta Sarah Loerch Matthies Rennegarbe Angelika Schierhorn Per Westermark Gunilla T. Westermark Bouke P. C. Hazenberg Nikolaus Grigorieff Marcus Fändrich Matthias Schmidt
author_sort	Falk Liberta
title	Cryo-EM fibril structures from systemic AA amyloidosis reveal the species complementarity of pathological amyloids
title_short	Cryo-EM fibril structures from systemic AA amyloidosis reveal the species complementarity of pathological amyloids
title_full	Cryo-EM fibril structures from systemic AA amyloidosis reveal the species complementarity of pathological amyloids
title_fullStr	Cryo-EM fibril structures from systemic AA amyloidosis reveal the species complementarity of pathological amyloids
title_full_unstemmed	Cryo-EM fibril structures from systemic AA amyloidosis reveal the species complementarity of pathological amyloids
title_sort	cryo-em fibril structures from systemic aa amyloidosis reveal the species complementarity of pathological amyloids
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/a47ab7cd22cf43a58ce79e21f975d4b7
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Cryo-EM fibril structures from systemic AA amyloidosis reveal the species complementarity of pathological amyloids

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