Different soluble aggregates of Aβ42 can give rise to cellular toxicity through different mechanisms-Reference-Cited by-同舟云学术

Different soluble aggregates of Aβ42 can give rise to cellular toxicity through different mechanisms

Published:2019-04-04 Issue:1 Volume:10 Page:
ISSN:2041-1723
Container-title:Nature Communications
language:en
Short-container-title:Nat Commun

Author:

De Suman,Wirthensohn David C.,Flagmeier Patrick^ORCID,Hughes Craig,Aprile Francesco A.,Ruggeri Francesco S.,Whiten Daniel R.^ORCID,Emin Derya,Xia Zengjie,Varela Juan A.^ORCID,Sormanni Pietro,Kundel Franziska,Knowles Tuomas P. J.,Dobson Christopher M.^ORCID,Bryant Clare,Vendruscolo Michele^ORCID,Klenerman David

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/s41467-019-09477-3.pdf

Reference53 articles.

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2. Soto, C. Unfolding the role of protein misfolding in neurodegenerative diseases. Nat. Rev. Neurosci. 4, 49–60 (2003).

3. Bucciantini, M. et al. Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature 416, 507–511 (2002).

4. Kayed, R. et al. Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 300, 486–489 (2003).

5. Wälti, M. A. et al. Atomic-resolution structure of a disease-relevant Aβ(1–42) amyloid fibril. Proc. Natl Acad. Sci. USA 113, E4976–E4984 (2016).

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