Direct observation of the three regions in α-synuclein that determine its membrane-bound behaviour-Reference-Cited by-同舟云学术

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Direct observation of the three regions in α-synuclein that determine its membrane-bound behaviour

Published:2014-05-29 Issue:1 Volume:5 Page:
ISSN:2041-1723
Container-title:Nature Communications
language:en
Short-container-title:Nat Commun

Author:

Fusco Giuliana,De Simone Alfonso,Gopinath Tata,Vostrikov Vitaly,Vendruscolo Michele,Dobson Christopher M.,Veglia Gianluigi

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/ncomms4827.pdf

Reference54 articles.

1. Lee, H. J., Choi, C. & Lee, S. J. Membrane-bound alpha-synuclein has a high aggregation propensity and the ability to seed the aggregation of the cytosolic form. J. Biol. Chem. 277, 671–678 (2002).

2. Bodner, C. R., Maltsev, A. S., Dobson, C. M. & Bax, A. Differential phospholipid binding of alpha-synuclein variants implicated in Parkinson's disease revealed by solution NMR spectroscopy. Biochemistry 49, 862–871 (2010).

3. Perrin, R. J., Woods, W. S., Clayton, D. F. & George, J. M. Interaction of human alpha-Synuclein and Parkinson's disease variants with phospholipids. Structural analysis using site-directed mutagenesis. J Biol. Chem. 275, 34393–34398 (2000).

4. Comellas, G., Lemkau, L. R., Zhou, D. H., George, J. M. & Rienstra, C. M. Structural intermediates during alpha-synuclein fibrillogenesis on phospholipid vesicles. J. Am. Chem. Soc. 134, 5090–5099 (2012).

5. Breydo, L., Wu, J. W. & Uversky, V. N. Alpha-synuclein misfolding and Parkinson's disease. Biochem. Biophys. Acta 1822, 261–285 (2012).

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