The structure of a β2-microglobulin fibril suggests a molecular basis for its amyloid polymorphism

Impaired kidney function can lead to an increase of β2-microglobulin (β2m) serum levels, which can cause β2m aggregation and amyloid fibril formation. Here the authors combine cryo-EM and magic angle spinning NMR measurements to determine the structure of a β2m fibril and they also present the low r...

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Autores principales:	Matthew G. Iadanza, Robert Silvers, Joshua Boardman, Hugh I. Smith, Theodoros K. Karamanos, Galia T. Debelouchina, Yongchao Su, Robert G. Griffin, Neil A. Ranson, Sheena E. Radford
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/c2131f4762074ff88b7f948f11bb5fd7
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spelling	oai:doaj.org-article:c2131f4762074ff88b7f948f11bb5fd72021-12-02T17:31:30ZThe structure of a β2-microglobulin fibril suggests a molecular basis for its amyloid polymorphism10.1038/s41467-018-06761-62041-1723https://doaj.org/article/c2131f4762074ff88b7f948f11bb5fd72018-10-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-06761-6https://doaj.org/toc/2041-1723Impaired kidney function can lead to an increase of β2-microglobulin (β2m) serum levels, which can cause β2m aggregation and amyloid fibril formation. Here the authors combine cryo-EM and magic angle spinning NMR measurements to determine the structure of a β2m fibril and they also present the low resolution model of a β2m fibril with a different morphology.Matthew G. IadanzaRobert SilversJoshua BoardmanHugh I. SmithTheodoros K. KaramanosGalia T. DebelouchinaYongchao SuRobert G. GriffinNeil A. RansonSheena E. RadfordNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-10 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Matthew G. Iadanza Robert Silvers Joshua Boardman Hugh I. Smith Theodoros K. Karamanos Galia T. Debelouchina Yongchao Su Robert G. Griffin Neil A. Ranson Sheena E. Radford The structure of a β2-microglobulin fibril suggests a molecular basis for its amyloid polymorphism
description	Impaired kidney function can lead to an increase of β2-microglobulin (β2m) serum levels, which can cause β2m aggregation and amyloid fibril formation. Here the authors combine cryo-EM and magic angle spinning NMR measurements to determine the structure of a β2m fibril and they also present the low resolution model of a β2m fibril with a different morphology.
format	article
author	Matthew G. Iadanza Robert Silvers Joshua Boardman Hugh I. Smith Theodoros K. Karamanos Galia T. Debelouchina Yongchao Su Robert G. Griffin Neil A. Ranson Sheena E. Radford
author_facet	Matthew G. Iadanza Robert Silvers Joshua Boardman Hugh I. Smith Theodoros K. Karamanos Galia T. Debelouchina Yongchao Su Robert G. Griffin Neil A. Ranson Sheena E. Radford
author_sort	Matthew G. Iadanza
title	The structure of a β2-microglobulin fibril suggests a molecular basis for its amyloid polymorphism
title_short	The structure of a β2-microglobulin fibril suggests a molecular basis for its amyloid polymorphism
title_full	The structure of a β2-microglobulin fibril suggests a molecular basis for its amyloid polymorphism
title_fullStr	The structure of a β2-microglobulin fibril suggests a molecular basis for its amyloid polymorphism
title_full_unstemmed	The structure of a β2-microglobulin fibril suggests a molecular basis for its amyloid polymorphism
title_sort	structure of a β2-microglobulin fibril suggests a molecular basis for its amyloid polymorphism
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/c2131f4762074ff88b7f948f11bb5fd7
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The structure of a β2-microglobulin fibril suggests a molecular basis for its amyloid polymorphism

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