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α-synuclein oligomers interact with ATP synthase and open the permeability transition pore in Parkinson’s disease

Overview of attention for article published in Nature Communications, June 2018
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  • In the top 5% of all research outputs scored by Altmetric
  • High Attention Score compared to outputs of the same age (98th percentile)
  • High Attention Score compared to outputs of the same age and source (92nd percentile)

Mentioned by

news
12 news outlets
blogs
1 blog
twitter
106 X users

Citations

dimensions_citation
352 Dimensions

Readers on

mendeley
497 Mendeley
citeulike
1 CiteULike
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Title
α-synuclein oligomers interact with ATP synthase and open the permeability transition pore in Parkinson’s disease
Published in
Nature Communications, June 2018
DOI 10.1038/s41467-018-04422-2
Pubmed ID
Authors

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

Abstract

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 several mitochondrial proteins including ATP synthase. Oligomeric α-synuclein impairs complex I-dependent respiration. Oligomers induce selective oxidation of the ATP synthase beta subunit and mitochondrial lipid peroxidation. These oxidation events increase the probability of permeability transition pore (PTP) opening, triggering mitochondrial swelling, and ultimately cell death. Notably, inhibition of oligomer-induced oxidation prevents the pathological induction of PTP. Inducible pluripotent stem cells (iPSC)-derived neurons bearing SNCA triplication, generate α-synuclein aggregates that interact with the ATP synthase and induce PTP opening, leading to neuronal death. This study shows how the transition of α-synuclein from its monomeric to oligomeric structure alters its functional consequences in Parkinson's disease.

X Demographics

X Demographics

The data shown below were collected from the profiles of 106 X users who shared this research output. Click here to find out more about how the information was compiled.
Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 497 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 497 100%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 94 19%
Researcher 79 16%
Student > Master 61 12%
Student > Bachelor 61 12%
Student > Doctoral Student 16 3%
Other 65 13%
Unknown 121 24%
Readers by discipline Count As %
Neuroscience 114 23%
Biochemistry, Genetics and Molecular Biology 112 23%
Agricultural and Biological Sciences 47 9%
Medicine and Dentistry 23 5%
Chemistry 16 3%
Other 51 10%
Unknown 134 27%
Attention Score in Context

Attention Score in Context

This research output has an Altmetric Attention Score of 153. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 02 September 2021.
All research outputs
#246,635
of 23,968,814 outputs
Outputs from Nature Communications
#3,603
of 50,657 outputs
Outputs of similar age
#5,798
of 331,991 outputs
Outputs of similar age from Nature Communications
#93
of 1,179 outputs
Altmetric has tracked 23,968,814 research outputs across all sources so far. Compared to these this one has done particularly well and is in the 98th percentile: it's in the top 5% of all research outputs ever tracked by Altmetric.
So far Altmetric has tracked 50,657 research outputs from this source. They typically receive a lot more attention than average, with a mean Attention Score of 56.2. This one has done particularly well, scoring higher than 92% of its peers.
Older research outputs will score higher simply because they've had more time to accumulate mentions. To account for age we can compare this Altmetric Attention Score to the 331,991 tracked outputs that were published within six weeks on either side of this one in any source. This one has done particularly well, scoring higher than 98% of its contemporaries.
We're also able to compare this research output to 1,179 others from the same source and published within six weeks on either side of this one. This one has done particularly well, scoring higher than 92% of its contemporaries.