α-Synuclein oligomers form by secondary nucleation

Autor: Catherine K. Xu, Georg Meisl, Ewa A. Andrzejewska, Georg Krainer, Alexander J. Dear, Marta Castellana-Cruz, Soma Turi, Irina A. Edu, Giorgio Vivacqua, Raphaël P. B. Jacquat, William E. Arter, Maria Grazia Spillantini, Michele Vendruscolo, Sara Linse, Tuomas P. J. Knowles

Publikováno v: Nature Communications, Vol 15, Iss 1, Pp 1-11 (2024)

Abstract Oligomeric species arising during the aggregation of α-synuclein are implicated as a major source of toxicity in Parkinson’s disease, and thus a major potential drug target. However, both their mechanism of formation and role in aggregati

Externí odkaz: https://doaj.org/article/a4d1104eb0184ade8af0b5e5b4fb8983

α-Synuclein oligomers form by secondary nucleation

Autor: Catherine K Xu, Georg Meisl, Ewa Andrzejewska, Georg Krainer, Alexander J Dear, Marta Castellana Cruz, Soma Turi, Raphael Jacquat, William E Arter, Michele Vendruscolo, Sara Linse, Tuomas PJ Knowles

Oligomeric species arising during aggregation of α-synuclein are proposed to be a major source of toxicity in Parkinson’s disease, and thus a major potential drug target. However, their mechanism of formation and role in aggregation are largely un

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::dcc4870555b44e74731ac4a281b09956
https://doi.org/10.1101/2023.05.28.542651

α-synuclein oligomers displace monomeric α-synuclein from lipid membranes

Autor: Greta Šneiderienė, Magdalena A. Czekalska, Catherine K. Xu, Akhila Jayaram, Georg Krainer, William E. Arter, Quentin Peter, Marta Castellana-Cruz, Kadi L. Saar, Aviad Levin, Thomas Mueller, Sebastian Fiedler, Sean R. A. Devenish, Heike Fiegler, Janet R. Kumita, Tuomas P. J. Knowles

Parkinson’s disease (PD) is an increasingly prevalent and currently incurable neurodegenerative disorder linked to the accumulation of α-synuclein (αS) protein aggregates in the nervous system. While αS binding to membranes in its monomeric stat

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::ddac2412d831b7a2a932f013e32dcae5
https://doi.org/10.1101/2023.03.21.533646

N-Terminal Acetylation of alpha-Synuclein Slows down Its Aggregation Process and Alters the Morphology of the Resulting Aggregates

Autor: Rosie Bell, Rebecca J. Thrush, Marta Castellana-Cruz, Marc Oeller, Roxine Staats, Aishwarya Nene, Patrick Flagmeier, Catherine K. Xu, Sandeep Satapathy, Celine Galvagnion, Mark R. Wilson, Christopher M. Dobson, Janet R. Kumita, Michele Vendruscolo

Publikováno v: Bell, R, Thrush, R J, Castellana-Cruz, M, Oeller, M, Staats, R, Nene, A, Flagmeier, P, Xu, C K, Satapathy, S, Galvagnion, C, Wilson, M R, Dobson, C M, Kumita, J R & Vendruscolo, M 2022, ' N-Terminal Acetylation of alpha-Synuclein Slows down Its Aggregation Process and Alters the Morphology of the Resulting Aggregates ', Biochemistry, vol. 61, no. 17, pp. 1743–1756 . https://doi.org/10.1021/acs.biochem.2c00104

Parkinson's disease is associated with the aberrant aggregation of alpha-synuclein. Although the causes of this process are still unclear, post-translational modifications of alpha-synuclein are likely to play a modulatory role. Since alpha-synuclein

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cb437c88f1bc125da79ff32116c790d9
https://curis.ku.dk/ws/files/319248519/acs.biochem.2c00104.pdf

The binding of the small heat-shock protein αB-crystallin to fibrils of α-synuclein is driven by entropic forces

Autor: Tuomas P. J. Knowles, Samuel Ness, Jacqueline A. Carozza, Michele Vendruscolo, Georg Meisl, Christopher M. Dobson, Quentin Peter, Marta Castellana-Cruz, Justin L. P. Benesch, Olga Tkachenko, Francesco A. Aprile, Tom Scheidt, Carl C Kolbe, Therese W. Herling, Mathias M. J. Bellaiche, Paolo Arosio

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America, 118 (38)
Proceedings of the National Academy of Sciences of the United States of America

Significance The formation of amyloid fibrils and toxic oligomeric species has been shown to be inhibited by their interactions with molecular chaperones, thus modulating monomer sequestration and toxicity in the context of neurodegenerative diseases

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cd548e5213dde477dbc1175952f16517
https://doi.org/10.1073/pnas.2108790118