Evidence map›Paper›PMID 37585526›Full record

ArticleScience advances2023

α-Synuclein liquid condensates fuel fibrillar α-synuclein growth.

Leonard Piroska, Alexis Fenyi, Scott Thomas, Marie-Aude Plamont, Virginie Redeker, Ronald Melki, Zoher Gueroui

Open access · goldAbstract read
In one paragraph

Article in Science advances, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
8.6field-weighted citation impact, top 2% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

26 citing papers in PubMed, 42 citations in OpenAlex.

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  13. Amyloid-β modulates the phase separation and aggregation of α-synuclein.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
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  15. Micropipette aspiration reveals differential RNA-dependent viscoelasticity of nucleolar subcompartments.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 1 institution in 1 country.

Leonard PiroskaPASTEUR, Department of Chemistry, École Normale Supérieure, PSL University, Sorbonne Université, CNRS, 75005 Paris, France.ORCID 0009-0000-7142-0027
Alexis FenyiInstitut Francois Jacob (MIRCen), CEA, CNRS, Fontenay-aux-Roses, France.ORCID 0000-0003-3270-2085
Scott ThomasPASTEUR, Department of Chemistry, École Normale Supérieure, PSL University, Sorbonne Université, CNRS, 75005 Paris, France.
Marie-Aude PlamontPASTEUR, Department of Chemistry, École Normale Supérieure, PSL University, Sorbonne Université, CNRS, 75005 Paris, France.ORCID 0000-0003-2112-3555
Virginie RedekerInstitut Francois Jacob (MIRCen), CEA, CNRS, Fontenay-aux-Roses, France.ORCID 0000-0003-2694-8388
Ronald MelkiInstitut Francois Jacob (MIRCen), CEA, CNRS, Fontenay-aux-Roses, France.
Zoher GuerouiPASTEUR, Department of Chemistry, École Normale Supérieure, PSL University, Sorbonne Université, CNRS, 75005 Paris, France.ORCID 0000-0003-1819-5427
Centre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

α-Synuclein (α-Syn) aggregation into fibrils with prion-like features is intimately associated with Lewy pathology and various synucleinopathies. Emerging studies suggest that α-Syn could form liquid condensates through phase separation. The role of these condensates in aggregation and disease remains elusive and the interplay between α-Syn fibrils and α-Syn condensates remains unexplored, possibly due to difficulties in triggering the formation of α-Syn condensates in cells. To address this gap, we developed an assay allowing the controlled assembly/disassembly of α-Syn condensates in cells and studied them upon exposure to preformed α-Syn fibrillar polymorphs. Fibrils triggered the evolution of liquid α-Syn condensates into solid-like structures displaying growing needle-like extensions and exhibiting pathological amyloid hallmarks. No such changes were elicited on α-Syn that did not undergo phase separation. We, therefore, propose a model where α-Syn within condensates fuels exogenous fibrillar seeds growth, thus speeding up the prion-like propagation of pathogenic aggregates.

Indexed as

alpha-SynucleinPrionsAmyloidalpha-SynucleinAmyloidPrions

Identifiers

PMID37585526
PMCPMC10431715
OpenAlexW4385860690

What OpenQuestion holds

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LicenceCC BY
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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.