Cryo-EM reveals structural breaks in a patient-derived amyloid fibril from systemic AL amyloidosis

Systemic AL amyloidosis is a protein misfolding disease caused by the aggregation and fibrillation of immunoglobulin light chains (LCs). Here, the authors present the cryo-EM structures of λ3 LC-derived amyloid fibrils that were isolated from patient tissue and they observe structural breaks, where...

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Autores principales:	Lynn Radamaker, Julian Baur, Stefanie Huhn, Christian Haupt, Ute Hegenbart, Stefan Schönland, Akanksha Bansal, Matthias Schmidt, Marcus Fändrich
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/54c83fc80d47468e9d109fced8a9dd0f
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spelling	oai:doaj.org-article:54c83fc80d47468e9d109fced8a9dd0f2021-12-02T14:26:51ZCryo-EM reveals structural breaks in a patient-derived amyloid fibril from systemic AL amyloidosis10.1038/s41467-021-21126-22041-1723https://doaj.org/article/54c83fc80d47468e9d109fced8a9dd0f2021-02-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-21126-2https://doaj.org/toc/2041-1723Systemic AL amyloidosis is a protein misfolding disease caused by the aggregation and fibrillation of immunoglobulin light chains (LCs). Here, the authors present the cryo-EM structures of λ3 LC-derived amyloid fibrils that were isolated from patient tissue and they observe structural breaks, where the two different fibril structures co-exist at different z-axial positions within the same fibril.Lynn RadamakerJulian BaurStefanie HuhnChristian HauptUte HegenbartStefan SchönlandAkanksha BansalMatthias SchmidtMarcus FändrichNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-10 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Lynn Radamaker Julian Baur Stefanie Huhn Christian Haupt Ute Hegenbart Stefan Schönland Akanksha Bansal Matthias Schmidt Marcus Fändrich Cryo-EM reveals structural breaks in a patient-derived amyloid fibril from systemic AL amyloidosis
description	Systemic AL amyloidosis is a protein misfolding disease caused by the aggregation and fibrillation of immunoglobulin light chains (LCs). Here, the authors present the cryo-EM structures of λ3 LC-derived amyloid fibrils that were isolated from patient tissue and they observe structural breaks, where the two different fibril structures co-exist at different z-axial positions within the same fibril.
format	article
author	Lynn Radamaker Julian Baur Stefanie Huhn Christian Haupt Ute Hegenbart Stefan Schönland Akanksha Bansal Matthias Schmidt Marcus Fändrich
author_facet	Lynn Radamaker Julian Baur Stefanie Huhn Christian Haupt Ute Hegenbart Stefan Schönland Akanksha Bansal Matthias Schmidt Marcus Fändrich
author_sort	Lynn Radamaker
title	Cryo-EM reveals structural breaks in a patient-derived amyloid fibril from systemic AL amyloidosis
title_short	Cryo-EM reveals structural breaks in a patient-derived amyloid fibril from systemic AL amyloidosis
title_full	Cryo-EM reveals structural breaks in a patient-derived amyloid fibril from systemic AL amyloidosis
title_fullStr	Cryo-EM reveals structural breaks in a patient-derived amyloid fibril from systemic AL amyloidosis
title_full_unstemmed	Cryo-EM reveals structural breaks in a patient-derived amyloid fibril from systemic AL amyloidosis
title_sort	cryo-em reveals structural breaks in a patient-derived amyloid fibril from systemic al amyloidosis
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/54c83fc80d47468e9d109fced8a9dd0f
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Cryo-EM reveals structural breaks in a patient-derived amyloid fibril from systemic AL amyloidosis

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