Cryo-EM of full-length α-synuclein reveals fibril polymorphs with a common structural kernel-Reference-Cited by-同舟云学术

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

Published:2018-09-06 Issue:1 Volume:9 Page:
ISSN:2041-1723
Container-title:Nature Communications
language:en
Short-container-title:Nat Commun

Author:

Li Binsen,Ge Peng,Murray Kevin A.,Sheth Phorum,Zhang Meng,Nair Gayatri,Sawaya Michael R.^ORCID,Shin Woo Shik,Boyer David R.^ORCID,Ye Shulin,Eisenberg David S.^ORCID,Zhou Z. Hong,Jiang Lin^ORCID

Publisher

Springer Science and Business Media LLC

Subject

General Physics and Astronomy,General Biochemistry, Genetics and Molecular Biology,General Chemistry

Link

http://www.nature.com/articles/s41467-018-05971-2.pdf

Reference37 articles.

1. Angot, E. Alpha-synuclein cell-to-cell transfer and seeding in grafted dopaminergic neurons in vivo. PLoS ONE 7, e35671 (2012).

2. Grazia Spillantini, M. et al. Filamentous α-synuclein inclusions link multiple system atrophy with Parkinson’s disease and dementia with Lewy bodies. Neurosci. Lett. 251, 205–208 (1998).

3. Spillantini, M. G., Crowther, R. A., Jakes, R., Hasegawa, M. & Goedert, M. Alpha-Synuclein in filamentous inclusions of Lewy bodies from Parkinson’s disease and dementia with lewy bodies. Proc. Natl. Acad. Sci. USA 95, 6469–6473 (1998).

4. Vilar, M. et al. The fold of alpha-synuclein fibrils. Proc. Natl Acad. Sci. USA 105, 8637–8642 (2008).

5. Bousset, L. et al. Structural and functional characterization of two alpha-synuclein strains. Nat. Commun. 4, 2575 (2013).

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