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...

Descripción completa

Guardado en:
Detalles Bibliográficos
Autores principales: 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
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2018
Materias:
Q
Acceso en línea:https://doaj.org/article/66a1b1816bc747869ab5c60b308732ab
Etiquetas: Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
id oai:doaj.org-article:66a1b1816bc747869ab5c60b308732ab
record_format dspace
spelling 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)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle 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 AT marthehrludtmann asynucleinoligomersinteractwithatpsynthaseandopenthepermeabilitytransitionporeinparkinsonsdisease
AT plamenarangelova asynucleinoligomersinteractwithatpsynthaseandopenthepermeabilitytransitionporeinparkinsonsdisease
AT mathewhhorrocks asynucleinoligomersinteractwithatpsynthaseandopenthepermeabilitytransitionporeinparkinsonsdisease
AT mineelchoi asynucleinoligomersinteractwithatpsynthaseandopenthepermeabilitytransitionporeinparkinsonsdisease
AT margaridarodrigues asynucleinoligomersinteractwithatpsynthaseandopenthepermeabilitytransitionporeinparkinsonsdisease
AT artyomybaev asynucleinoligomersinteractwithatpsynthaseandopenthepermeabilitytransitionporeinparkinsonsdisease
AT alexeyvberezhnov asynucleinoligomersinteractwithatpsynthaseandopenthepermeabilitytransitionporeinparkinsonsdisease
AT zhiyao asynucleinoligomersinteractwithatpsynthaseandopenthepermeabilitytransitionporeinparkinsonsdisease
AT daniellittle asynucleinoligomersinteractwithatpsynthaseandopenthepermeabilitytransitionporeinparkinsonsdisease
AT bleridabanushi asynucleinoligomersinteractwithatpsynthaseandopenthepermeabilitytransitionporeinparkinsonsdisease
AT afnansalehalmenhali asynucleinoligomersinteractwithatpsynthaseandopenthepermeabilitytransitionporeinparkinsonsdisease
AT rohantranasinghe asynucleinoligomersinteractwithatpsynthaseandopenthepermeabilitytransitionporeinparkinsonsdisease
AT danielrwhiten asynucleinoligomersinteractwithatpsynthaseandopenthepermeabilitytransitionporeinparkinsonsdisease
AT ratsudayapom asynucleinoligomersinteractwithatpsynthaseandopenthepermeabilitytransitionporeinparkinsonsdisease
AT karamjitsinghdolt asynucleinoligomersinteractwithatpsynthaseandopenthepermeabilitytransitionporeinparkinsonsdisease
AT michaeljdevine asynucleinoligomersinteractwithatpsynthaseandopenthepermeabilitytransitionporeinparkinsonsdisease
AT paulgissen asynucleinoligomersinteractwithatpsynthaseandopenthepermeabilitytransitionporeinparkinsonsdisease
AT tilokunath asynucleinoligomersinteractwithatpsynthaseandopenthepermeabilitytransitionporeinparkinsonsdisease
AT moranajaganjac asynucleinoligomersinteractwithatpsynthaseandopenthepermeabilitytransitionporeinparkinsonsdisease
AT evgenyvpavlov asynucleinoligomersinteractwithatpsynthaseandopenthepermeabilitytransitionporeinparkinsonsdisease
AT davidklenerman asynucleinoligomersinteractwithatpsynthaseandopenthepermeabilitytransitionporeinparkinsonsdisease
AT andreyyabramov asynucleinoligomersinteractwithatpsynthaseandopenthepermeabilitytransitionporeinparkinsonsdisease
AT soniagandhi asynucleinoligomersinteractwithatpsynthaseandopenthepermeabilitytransitionporeinparkinsonsdisease
_version_ 1718383218366873600