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Endosulfine-alpha inhibits membrane-induced α-synuclein aggregation and protects against α-synuclein neurotoxicity

Overview of attention for article published in Acta Neuropathologica Communications, January 2017
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About this Attention Score

  • In the top 25% of all research outputs scored by Altmetric
  • High Attention Score compared to outputs of the same age (83rd percentile)
  • Average Attention Score compared to outputs of the same age and source

Mentioned by

news
1 news outlet
twitter
1 tweeter

Citations

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21 Dimensions

Readers on

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43 Mendeley
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Title
Endosulfine-alpha inhibits membrane-induced α-synuclein aggregation and protects against α-synuclein neurotoxicity
Published in
Acta Neuropathologica Communications, January 2017
DOI 10.1186/s40478-016-0403-7
Pubmed ID
Authors

Daniel Ysselstein, Benjamin Dehay, Isabel M. Costantino, George P. McCabe, Matthew P. Frosch, Julia M. George, Erwan Bezard, Jean-Christophe Rochet

Abstract

Neuropathological and genetic findings suggest that the presynaptic protein α-synuclein (aSyn) is involved in the pathogenesis of synucleinopathy disorders, including Parkinson's disease (PD), dementia with Lewy bodies (DLB) and multiple system atrophy. Evidence suggests that the self-assembly of aSyn conformers bound to phospholipid membranes in an aggregation-prone state plays a key role in aSyn neurotoxicity. Accordingly, we hypothesized that protein binding partners of lipid-associated aSyn could inhibit the formation of toxic aSyn oligomers at membrane surfaces. To address this hypothesis, we characterized the protein endosulfine-alpha (ENSA), previously shown to interact selectively with membrane-bound aSyn, in terms of its effects on the membrane-induced aggregation and neurotoxicity of two familial aSyn mutants, A30P and G51D. We found that wild-type ENSA, but not the non-aSyn-binding S109E variant, interfered with membrane-induced aSyn self-assembly, aSyn-mediated vesicle disruption and aSyn neurotoxicity. Immunoblotting analyses revealed that ENSA was down-regulated in the brains of synucleinopathy patients versus non-diseased individuals. Collectively, these results suggest that ENSA can alleviate neurotoxic effects of membrane-bound aSyn via an apparent chaperone-like activity at the membrane surface, and a decrease in ENSA expression may contribute to aSyn neuropathology in synucleinopathy disorders. More generally, our findings suggest that promoting interactions between lipid-bound, amyloidogenic proteins and their binding partners is a viable strategy to alleviate cytotoxicity in a range of protein misfolding disorders.

Twitter Demographics

The data shown below were collected from the profile of 1 tweeter who shared this research output. Click here to find out more about how the information was compiled.

Mendeley readers

The data shown below were compiled from readership statistics for 43 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 43 100%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 12 28%
Student > Master 7 16%
Researcher 6 14%
Student > Doctoral Student 4 9%
Student > Bachelor 2 5%
Other 4 9%
Unknown 8 19%
Readers by discipline Count As %
Neuroscience 10 23%
Biochemistry, Genetics and Molecular Biology 7 16%
Agricultural and Biological Sciences 7 16%
Pharmacology, Toxicology and Pharmaceutical Science 2 5%
Chemistry 2 5%
Other 5 12%
Unknown 10 23%

Attention Score in Context

This research output has an Altmetric Attention Score of 10. 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 27 October 2017.
All research outputs
#1,312,630
of 12,059,719 outputs
Outputs from Acta Neuropathologica Communications
#145
of 522 outputs
Outputs of similar age
#53,176
of 326,021 outputs
Outputs of similar age from Acta Neuropathologica Communications
#9
of 20 outputs
Altmetric has tracked 12,059,719 research outputs across all sources so far. Compared to these this one has done well and is in the 88th percentile: it's in the top 25% of all research outputs ever tracked by Altmetric.
So far Altmetric has tracked 522 research outputs from this source. They typically receive more attention than average, with a mean Attention Score of 7.7. This one has gotten more attention than average, scoring higher than 69% 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 326,021 tracked outputs that were published within six weeks on either side of this one in any source. This one has done well, scoring higher than 83% of its contemporaries.
We're also able to compare this research output to 20 others from the same source and published within six weeks on either side of this one. This one has gotten more attention than average, scoring higher than 50% of its contemporaries.