α-synuclein oligomers interact with ATP synthase and open the permeability transition pore in Parkinson’s disease
How toxic aggregated forms of α-synuclein lead to neurodegeneration is unclear. Here authors use biophysical and cellular imaging methods to show that specific oligomers of α-synuclein exert effects on mitochondria to induce opening of the permeability transition pore, leading to cell death in Parki...
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Nature Portfolio
2018
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oai:doaj.org-article:66a1b1816bc747869ab5c60b308732ab2021-12-02T16:49:49Zα-synuclein oligomers interact with ATP synthase and open the permeability transition pore in Parkinson’s disease10.1038/s41467-018-04422-22041-1723https://doaj.org/article/66a1b1816bc747869ab5c60b308732ab2018-06-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-04422-2https://doaj.org/toc/2041-1723How toxic aggregated forms of α-synuclein lead to neurodegeneration is unclear. Here authors use biophysical and cellular imaging methods to show that specific oligomers of α-synuclein exert effects on mitochondria to induce opening of the permeability transition pore, leading to cell death in Parkinson’s disease.Marthe H. R. LudtmannPlamena R. AngelovaMathew H. HorrocksMinee L. ChoiMargarida RodriguesArtyom Y. BaevAlexey V. BerezhnovZhi YaoDaniel LittleBlerida BanushiAfnan Saleh Al-MenhaliRohan T. RanasingheDaniel R. WhitenRatsuda YapomKaramjit Singh DoltMichael J. DevinePaul GissenTilo KunathMorana JaganjacEvgeny V. PavlovDavid KlenermanAndrey Y. AbramovSonia GandhiNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-16 (2018) |
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Science Q Marthe H. R. Ludtmann Plamena R. Angelova Mathew H. Horrocks Minee L. Choi Margarida Rodrigues Artyom Y. Baev Alexey V. Berezhnov Zhi Yao Daniel Little Blerida Banushi Afnan Saleh Al-Menhali Rohan T. Ranasinghe Daniel R. Whiten Ratsuda Yapom Karamjit Singh Dolt Michael J. Devine Paul Gissen Tilo Kunath Morana Jaganjac Evgeny V. Pavlov David Klenerman Andrey Y. Abramov Sonia Gandhi α-synuclein oligomers interact with ATP synthase and open the permeability transition pore in Parkinson’s disease |
description |
How toxic aggregated forms of α-synuclein lead to neurodegeneration is unclear. Here authors use biophysical and cellular imaging methods to show that specific oligomers of α-synuclein exert effects on mitochondria to induce opening of the permeability transition pore, leading to cell death in Parkinson’s disease. |
format |
article |
author |
Marthe H. R. Ludtmann Plamena R. Angelova Mathew H. Horrocks Minee L. Choi Margarida Rodrigues Artyom Y. Baev Alexey V. Berezhnov Zhi Yao Daniel Little Blerida Banushi Afnan Saleh Al-Menhali Rohan T. Ranasinghe Daniel R. Whiten Ratsuda Yapom Karamjit Singh Dolt Michael J. Devine Paul Gissen Tilo Kunath Morana Jaganjac Evgeny V. Pavlov David Klenerman Andrey Y. Abramov Sonia Gandhi |
author_facet |
Marthe H. R. Ludtmann Plamena R. Angelova Mathew H. Horrocks Minee L. Choi Margarida Rodrigues Artyom Y. Baev Alexey V. Berezhnov Zhi Yao Daniel Little Blerida Banushi Afnan Saleh Al-Menhali Rohan T. Ranasinghe Daniel R. Whiten Ratsuda Yapom Karamjit Singh Dolt Michael J. Devine Paul Gissen Tilo Kunath Morana Jaganjac Evgeny V. Pavlov David Klenerman Andrey Y. Abramov Sonia Gandhi |
author_sort |
Marthe H. R. Ludtmann |
title |
α-synuclein oligomers interact with ATP synthase and open the permeability transition pore in Parkinson’s disease |
title_short |
α-synuclein oligomers interact with ATP synthase and open the permeability transition pore in Parkinson’s disease |
title_full |
α-synuclein oligomers interact with ATP synthase and open the permeability transition pore in Parkinson’s disease |
title_fullStr |
α-synuclein oligomers interact with ATP synthase and open the permeability transition pore in Parkinson’s disease |
title_full_unstemmed |
α-synuclein oligomers interact with ATP synthase and open the permeability transition pore in Parkinson’s disease |
title_sort |
α-synuclein oligomers interact with atp synthase and open the permeability transition pore in parkinson’s disease |
publisher |
Nature Portfolio |
publishDate |
2018 |
url |
https://doaj.org/article/66a1b1816bc747869ab5c60b308732ab |
work_keys_str_mv |
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