Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein-Reference-Cited by-同舟云学术

Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein

Published:2016-03-28 Issue:5 Volume:23 Page:409-415
ISSN:1545-9993
Container-title:Nature Structural & Molecular Biology
language:en
Short-container-title:Nat Struct Mol Biol

Author:

Tuttle Marcus D,Comellas Gemma,Nieuwkoop Andrew J,Covell Dustin J,Berthold Deborah A,Kloepper Kathryn D,Courtney Joseph M,Kim Jae K,Barclay Alexander M,Kendall Amy,Wan William,Stubbs Gerald,Schwieters Charles D,Lee Virginia M Y,George Julia M,Rienstra Chad M

Publisher

Springer Science and Business Media LLC

Subject

Molecular Biology,Structural Biology

Link

http://www.nature.com/articles/nsmb.3194.pdf

Reference74 articles.

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2. Luk, K.C. et al. Exogenous α-synuclein fibrils seed the formation of Lewy body-like intracellular inclusions in cultured cells. Proc. Natl. Acad. Sci. USA 106, 20051–20056 (2009).

3. Volpicelli-Daley, L.A. et al. Exogenous α-synuclein fibrils induce Lewy body pathology leading to synaptic dysfunction and neuron death. Neuron 72, 57–71 (2011).

4. Desplats, P. et al. Inclusion formation and neuronal cell death through neuron-to-neuron transmission of α-synuclein. Proc. Natl. Acad. Sci. USA 106, 13010–13015 (2009).

5. Luk, K.C. et al. Pathological α-synuclein transmission initiates Parkinson-like neurodegeneration in nontransgenic mice. Science 338, 949–953 (2012).

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