α-synuclein oligomers interact with ATP synthase and open the permeability transition pore in Parkin...
α-synuclein oligomers interact with ATP synthase and open the permeability transition pore in Parkinson’s disease
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Full title
Author / Creator
Ludtmann, Marthe H. R. , Angelova, Plamena R. , Horrocks, Mathew H. , Choi, Minee L. , Rodrigues, Margarida , Baev, Artyom Y. , Berezhnov, Alexey V. , Yao, Zhi , Little, Daniel , Banushi, Blerida , Al-Menhali, Afnan Saleh , Ranasinghe, Rohan T. , Whiten, Daniel R. , Yapom, Ratsuda , Dolt, Karamjit Singh , Devine, Michael J. , Gissen, Paul , Kunath, Tilo , Jaganjac, Morana , Pavlov, Evgeny V. , Klenerman, David , Abramov, Andrey Y. and Gandhi, Sonia
Publisher
London: Nature Publishing Group UK
Journal title
Language
English
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Publication information
Publisher
London: Nature Publishing Group UK
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More information
Scope and Contents
Contents
Protein aggregation causes α-synuclein to switch from its physiological role to a pathological toxic gain of function. Under physiological conditions, monomeric α-synuclein improves ATP synthase efficiency. Here, we report that aggregation of monomers generates beta sheet-rich oligomers that localise to the mitochondria in close proximity to severa...
Alternative Titles
Full title
α-synuclein oligomers interact with ATP synthase and open the permeability transition pore in Parkinson’s disease
Authors, Artists and Contributors
Author / Creator
Angelova, Plamena R.
Horrocks, Mathew H.
Choi, Minee L.
Rodrigues, Margarida
Baev, Artyom Y.
Berezhnov, Alexey V.
Yao, Zhi
Little, Daniel
Banushi, Blerida
Al-Menhali, Afnan Saleh
Ranasinghe, Rohan T.
Whiten, Daniel R.
Yapom, Ratsuda
Dolt, Karamjit Singh
Devine, Michael J.
Gissen, Paul
Kunath, Tilo
Jaganjac, Morana
Pavlov, Evgeny V.
Klenerman, David
Abramov, Andrey Y.
Gandhi, Sonia
Identifiers
Primary Identifiers
Record Identifier
TN_cdi_doaj_primary_oai_doaj_org_article_66a1b1816bc747869ab5c60b308732ab
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_66a1b1816bc747869ab5c60b308732ab
Other Identifiers
ISSN
2041-1723
E-ISSN
2041-1723
DOI
10.1038/s41467-018-04422-2
