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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Nature Portfolio
2018
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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) |
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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 |
work_keys_str_mv |
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