Amyloid fibril structure of α-synuclein determined by cryo-electron microscopy-Reference-Cited by-同舟云学术

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Amyloid fibril structure of α-synuclein determined by cryo-electron microscopy

Published:2018-07-31 Issue:9 Volume:28 Page:897-903
ISSN:1001-0602
Container-title:Cell Research
language:en
Short-container-title:Cell Res

Author:

Li Yaowang,Zhao Chunyu,Luo Feng,Liu Zhenying,Gui Xinrui,Luo Zhipu,Zhang Xiang,Li Dan,Liu Cong^ORCID,Li Xueming

Funder

National Natural Science Foundation of China (National Science Foundation of China)

Major State Basic Research Development Program

Publisher

Springer Science and Business Media LLC

Subject

Cell Biology,Molecular Biology

Link

http://www.nature.com/articles/s41422-018-0075-x.pdf

Reference43 articles.

1. Goedert, M., Clavaguera, F. & Tolnay, M. The propagation of prion-like protein inclusions in neurodegenerative diseases. Trends Neurosci. 33, 317–325 (2010).

2. Jucker, M. & Walker, L. C. Self-propagation of pathogenic protein aggregates in neurodegenerative diseases. Nature 501, 45–51 (2013).

3. Knowles, T. P., Vendruscolo, M. & Dobson, C. M. The amyloid state and its association with protein misfolding diseases. Nat. Rev. Mol. Cell Biol. 15, 384–396 (2014).

4. Tycko, R. Physical and structural basis for polymorphism in amyloid fibrils. Protein Sci. 23, 1528–1539 (2014).

5. Riek, R. & Eisenberg, D. S. The activities of amyloids from a structural perspective. Nature 539, 227–235 (2016).

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