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Biophysical properties and cellular toxicity of covalent crosslinked oligomers of α-synuclein formed by photoinduced side-chain tyrosyl radicals
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SYSNO ASEP 0381273 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Biophysical properties and cellular toxicity of covalent crosslinked oligomers of α-synuclein formed by photoinduced side-chain tyrosyl radicals Author(s) Borsarelli, C.D. (AR)
Falomir-Lockhart, L.J. (DE)
Ostatná, Veronika (BFU-R) RID, ORCID
Fauerbach, J.A. (AR)
Hsiao, H.-H. (DE)
Urlaub, H. (DE)
Paleček, Emil (BFU-R) RID, ORCID
Jares-Erijman, E.A. (AR)
Jovin, T.M. (DE)Number of authors 9 Source Title Free Radical Biology and Medicine. - : Elsevier - ISSN 0891-5849
Roč. 53, č. 4 (2012), s. 1004-1015Number of pages 12 s. Language eng - English Country US - United States Keywords Parkinson's disease ; neurodegeneration ; oxidative stress Subject RIV BO - Biophysics R&D Projects KJB100040901 GA AV ČR - Academy of Sciences of the Czech Republic (AV ČR) CEZ AV0Z50040702 - BFU-R (2007-2013) UT WOS 000307920100035 DOI 10.1016/j.freeradbiomed.2012.06.035 Annotation In this work, we describe the preparation and characterization of low molecular weight covalently bound oligomeric species of alpha-synuclein (aS) obtained by crosslinking via tyrosyl radicals. Numerous analytical techniques were used to characterize the aS oligomers. The diverse oligomeric species exhibited a direct effect on the in vitro aggregation behavior of wild-type monomeric aS.Compared to the unmodified monomer, the photoinduced covalent oligomeric species demonstrated increased toxic effects on differentiated neuronal-like SH-SY5Y cells. The results highlight the importance of protein modification induced by oxidative stress in the initial molecular events leading to Parkinson’s disease. Workplace Institute of Biophysics Contact Jana Poláková, polakova@ibp.cz, Tel.: 541 517 244 Year of Publishing 2013
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