Cryo-EM structure of a transthyretin-derived amyloid fibril from a patient with hereditary ATTR amyloidosis

Systemic amyloidosis of the ATTR is one of the most abundant forms of systemic amyloidosis and caused by misfolding of the circulating blood protein transthyretin (TTR). Here the authors present the cryo-EM structure of patient-derived Val30Met ATTR amyloid fibrils which reveals that the protofilame...

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Autores principales:	Matthias Schmidt, Sebastian Wiese, Volkan Adak, Jonas Engler, Shubhangi Agarwal, Günter Fritz, Per Westermark, Martin Zacharias, Marcus Fändrich
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/1cfd6f8b528f4738ac103cd51fd0beb4
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spelling	oai:doaj.org-article:1cfd6f8b528f4738ac103cd51fd0beb42021-12-02T16:58:04ZCryo-EM structure of a transthyretin-derived amyloid fibril from a patient with hereditary ATTR amyloidosis10.1038/s41467-019-13038-z2041-1723https://doaj.org/article/1cfd6f8b528f4738ac103cd51fd0beb42019-11-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-13038-zhttps://doaj.org/toc/2041-1723Systemic amyloidosis of the ATTR is one of the most abundant forms of systemic amyloidosis and caused by misfolding of the circulating blood protein transthyretin (TTR). Here the authors present the cryo-EM structure of patient-derived Val30Met ATTR amyloid fibrils which reveals that the protofilament consists of an N-terminal and a C-terminal TTR fragment and discuss implications for the mechanism of misfolding.Matthias SchmidtSebastian WieseVolkan AdakJonas EnglerShubhangi AgarwalGünter FritzPer WestermarkMartin ZachariasMarcus FändrichNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-9 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Matthias Schmidt Sebastian Wiese Volkan Adak Jonas Engler Shubhangi Agarwal Günter Fritz Per Westermark Martin Zacharias Marcus Fändrich Cryo-EM structure of a transthyretin-derived amyloid fibril from a patient with hereditary ATTR amyloidosis
description	Systemic amyloidosis of the ATTR is one of the most abundant forms of systemic amyloidosis and caused by misfolding of the circulating blood protein transthyretin (TTR). Here the authors present the cryo-EM structure of patient-derived Val30Met ATTR amyloid fibrils which reveals that the protofilament consists of an N-terminal and a C-terminal TTR fragment and discuss implications for the mechanism of misfolding.
format	article
author	Matthias Schmidt Sebastian Wiese Volkan Adak Jonas Engler Shubhangi Agarwal Günter Fritz Per Westermark Martin Zacharias Marcus Fändrich
author_facet	Matthias Schmidt Sebastian Wiese Volkan Adak Jonas Engler Shubhangi Agarwal Günter Fritz Per Westermark Martin Zacharias Marcus Fändrich
author_sort	Matthias Schmidt
title	Cryo-EM structure of a transthyretin-derived amyloid fibril from a patient with hereditary ATTR amyloidosis
title_short	Cryo-EM structure of a transthyretin-derived amyloid fibril from a patient with hereditary ATTR amyloidosis
title_full	Cryo-EM structure of a transthyretin-derived amyloid fibril from a patient with hereditary ATTR amyloidosis
title_fullStr	Cryo-EM structure of a transthyretin-derived amyloid fibril from a patient with hereditary ATTR amyloidosis
title_full_unstemmed	Cryo-EM structure of a transthyretin-derived amyloid fibril from a patient with hereditary ATTR amyloidosis
title_sort	cryo-em structure of a transthyretin-derived amyloid fibril from a patient with hereditary attr amyloidosis
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/1cfd6f8b528f4738ac103cd51fd0beb4
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Cryo-EM structure of a transthyretin-derived amyloid fibril from a patient with hereditary ATTR amyloidosis

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