Cryo-EM of full-length α-synuclein reveals fibril polymorphs with a common structural kernel

The intrinsically disordered protein alpha-synuclein (aSyn) forms polymorphic fibrils. Here the authors provide molecular insights into aSyn fibril polymorphism and present the cryo-EM structures of the two predominant species, a rod and a twister both determined at 3.7 Å resolution.

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Autores principales: Binsen Li, Peng Ge, Kevin A. Murray, Phorum Sheth, Meng Zhang, Gayatri Nair, Michael R. Sawaya, Woo Shik Shin, David R. Boyer, Shulin Ye, David S. Eisenberg, Z. Hong Zhou, Lin Jiang
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Lenguaje:EN
Publicado: Nature Portfolio 2018
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Acceso en línea:https://doaj.org/article/7d6d7834f70b4294ba675d175de06cd2
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spelling oai:doaj.org-article:7d6d7834f70b4294ba675d175de06cd22021-12-02T16:49:49ZCryo-EM of full-length α-synuclein reveals fibril polymorphs with a common structural kernel10.1038/s41467-018-05971-22041-1723https://doaj.org/article/7d6d7834f70b4294ba675d175de06cd22018-09-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-05971-2https://doaj.org/toc/2041-1723The intrinsically disordered protein alpha-synuclein (aSyn) forms polymorphic fibrils. Here the authors provide molecular insights into aSyn fibril polymorphism and present the cryo-EM structures of the two predominant species, a rod and a twister both determined at 3.7 Å resolution.Binsen LiPeng GeKevin A. MurrayPhorum ShethMeng ZhangGayatri NairMichael R. SawayaWoo Shik ShinDavid R. BoyerShulin YeDavid S. EisenbergZ. Hong ZhouLin JiangNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-10 (2018)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Binsen Li
Peng Ge
Kevin A. Murray
Phorum Sheth
Meng Zhang
Gayatri Nair
Michael R. Sawaya
Woo Shik Shin
David R. Boyer
Shulin Ye
David S. Eisenberg
Z. Hong Zhou
Lin Jiang
Cryo-EM of full-length α-synuclein reveals fibril polymorphs with a common structural kernel
description The intrinsically disordered protein alpha-synuclein (aSyn) forms polymorphic fibrils. Here the authors provide molecular insights into aSyn fibril polymorphism and present the cryo-EM structures of the two predominant species, a rod and a twister both determined at 3.7 Å resolution.
format article
author Binsen Li
Peng Ge
Kevin A. Murray
Phorum Sheth
Meng Zhang
Gayatri Nair
Michael R. Sawaya
Woo Shik Shin
David R. Boyer
Shulin Ye
David S. Eisenberg
Z. Hong Zhou
Lin Jiang
author_facet Binsen Li
Peng Ge
Kevin A. Murray
Phorum Sheth
Meng Zhang
Gayatri Nair
Michael R. Sawaya
Woo Shik Shin
David R. Boyer
Shulin Ye
David S. Eisenberg
Z. Hong Zhou
Lin Jiang
author_sort Binsen Li
title Cryo-EM of full-length α-synuclein reveals fibril polymorphs with a common structural kernel
title_short Cryo-EM of full-length α-synuclein reveals fibril polymorphs with a common structural kernel
title_full Cryo-EM of full-length α-synuclein reveals fibril polymorphs with a common structural kernel
title_fullStr Cryo-EM of full-length α-synuclein reveals fibril polymorphs with a common structural kernel
title_full_unstemmed Cryo-EM of full-length α-synuclein reveals fibril polymorphs with a common structural kernel
title_sort cryo-em of full-length α-synuclein reveals fibril polymorphs with a common structural kernel
publisher Nature Portfolio
publishDate 2018
url https://doaj.org/article/7d6d7834f70b4294ba675d175de06cd2
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