The interactome of stabilized α-synuclein oligomers and neuronal proteins

Autor: Jan J. Enghild, Arun Kumar Somavarapu, Mihaela M. Apetri, Carsten Scavenius, Femke van Diggelen, Janni Nielsen, Daniel E. Otzen, Armand W.J.W. Tepper, Signe Andrea Frank

Publikováno v: van Diggelen, F, Frank, S A, Somavarapu, A K, Scavenius, C, Apetri, M M, Nielsen, J, Tepper, A W J W, Enghild, J J & Otzen, D E 2020, ' The interactome of stabilized α-synuclein oligomers and neuronal proteins ', The FEBS Journal, vol. 287, no. 10, pp. 2037-2054 . https://doi.org/10.1111/febs.15124

While it is generally accepted that α-synuclein oligomers (αSOs) play an important role in neurodegeneration in Parkinson's disease, the basis for their cytotoxicity remains unclear. We have previously shown that docosahexaenoic acid (DHA) stabiliz

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::63d05a26ab7dd1a49de771b556d0f0f6
https://pubmed.ncbi.nlm.nih.gov/31686426

α-Synuclein Oligomers: A Study in Diversity

Autor: Femke van Diggelen, Daniel E. Otzen, Armand W.J.W. Tepper, Mihaela M. Apetri

Publikováno v: van Diggelen, F, Tepper, A, Petri, M & Otzen, D 2017, ' α-Synuclein Oligomers : A Study in Diversity ', Israel Journal of Chemistry, vol. 57, no. 7-8, pp. 699-723 . https://doi.org/10.1002/ijch.201600116

A critical step in Parkinson's disease (PD) is the formation of toxic α-synuclein oligomers (αSOs). In vitro αSOs are formed by self-assembly of α-synuclein at high concentrations, or by the addition of, for example, dopamine, lipids, ethanol, or

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2c4180cffa2cf898d8264ad2d53524c8
https://doi.org/10.1002/ijch.201600116

The effect of fluorescent labeling on α-synuclein fibril morphology

Autor: Marija Mučibabić, Gerard W. Canters, Mihaela M. Apetri, Thijs J. Aartsma

Publikováno v: Biochimica et biophysica acta. 1864(10)

The misfolding and aggregation of a small, natively unfolded protein α-synuclein (α-syn) is presumably an important factor in the development of Parkinson's disease. However, the mechanism of α-syn aggregation into amyloid fibrils and their morpho

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2b74f7a024802e5020788cc4eb2ad616
https://pubmed.ncbi.nlm.nih.gov/27475048

Secondary Structure of α-Synuclein Oligomers: Characterization by Raman and Atomic Force Microscopy

Autor: Vernon E. Anderson, Mihaela M. Apetri, Nakul C. Maiti, Michael G. Zagorski, Paul R. Carey

Publikováno v: Journal of Molecular Biology. 355:63-71

Formation of alpha-synuclein aggregates is proposed to be a crucial event in the pathogenesis of Parkinson's disease. Large soluble oligomeric species are observed as probable intermediates during fibril formation and these, or related aggregates, ma

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fc23e40936389ec6e3fc36d4c304c90f
https://doi.org/10.1016/j.jmb.2005.10.071

Two conformationally distinct α-synuclein oligomers share common epitopes and the ability to impair long-term potentiation.

Autor: van Diggelen F; Interdisciplinary Nanoscience Center (iNANO), Aarhus University, Aarhus C, Denmark.; Crossbeta Biosciences BV, Utrecht, The Netherlands., Hrle D; Klinik für Anaesthesiologie der Technischen Universität München, Klinikum Rechts der Isar, Munich, Germany., Apetri M; Crossbeta Biosciences BV, Utrecht, The Netherlands., Christiansen G; Department of Biomedicine, Aarhus University, Aarhus C, Denmark., Rammes G; Klinik für Anaesthesiologie der Technischen Universität München, Klinikum Rechts der Isar, Munich, Germany., Tepper A; Crossbeta Biosciences BV, Utrecht, The Netherlands., Otzen DE; Interdisciplinary Nanoscience Center (iNANO), Aarhus University, Aarhus C, Denmark.

Publikováno v: PloS one [PLoS One] 2019 Mar 22; Vol. 14 (3), pp. e0213663. Date of Electronic Publication: 2019 Mar 22 (Print Publication: 2019).