Evidence map›Paper›PMID 33386842›Full record

ArticleJournal of molecular cell biology2021

Observation of an α-synuclein liquid droplet state and its maturation into Lewy body-like assemblies.

Maarten C Hardenberg, Tessa Sinnige, Sam Casford, Samuel T Dada, Chetan Poudel, Elizabeth A Robinson, Monika Fuxreiter, Clemens F Kaminksi, Gabriele S Kaminski Schierle, Ellen A A Nollen and 2 more

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of molecular cell biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 98 papers.

0numbers the graph read from it
0cells of the map it votes in
98citing papers in PubMed
5.5field-weighted citation impact, top 3% 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

98 citing papers in PubMed, 101 citations in OpenAlex.

  1. Cellular and systemic modifiers of alpha-synuclein proteostasis.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
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  18. A Novel α-Synuclein K58N Missense Variant in a Patient with Parkinson's Disease.Movement disorders : official journal of the Movement Disorder Society · 2025
    Article
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38 more citing papers are in PubMed but not listed here.

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

12 authors at 3 institutions in 3 countries.

Maarten C HardenbergCentre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, UK.
Tessa SinnigeCentre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, UK.
Sam CasfordCentre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, UK.
Samuel T DadaCentre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, UK.
Chetan PoudelDepartment of Chemical Engineering and Biotechnology, University of Cambridge, Cambridge CB3 0AS, UK.
Elizabeth A RobinsonCentre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, UK.
Monika FuxreiterMTA-DE Laboratory of Protein Dynamics, Department of Biochemistry and Molecular Biology, University of Debrecen, Hungary.
Clemens F KaminksiDepartment of Chemical Engineering and Biotechnology, University of Cambridge, Cambridge CB3 0AS, UK.
Gabriele S Kaminski SchierleDepartment of Chemical Engineering and Biotechnology, University of Cambridge, Cambridge CB3 0AS, UK.
Ellen A A NollenEuropean Research Institute for the Biology of Aging, University Medical Center Groningen, University of Groningen, Groningen 9713 AV, The Netherlands.
Christopher M DobsonCentre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, UK.
Michele VendruscoloCentre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, UK.ORCID 0000-0002-3616-1610
University of Cambridge · GBUniversity of Debrecen · HUUniversity of Groningen · NL

Funding

Biotechnology and Biological Sciences Research Council BB/M011194/1Medical Research Council G0902243Medical Research Council MR/K02292X/1Wellcome TrustWellcome Trust 065807/Z/01/ZWellcome Trust 203249/Z/16/Z
6 · The paper itself

Abstract

Misfolded α-synuclein is a major component of Lewy bodies, which are a hallmark of Parkinson's disease (PD). A large body of evidence shows that α-synuclein can aggregate into amyloid fibrils, but the relationship between α-synuclein self-assembly and Lewy body formation remains unclear. Here, we show, both in vitro and in a Caenorhabditis elegans model of PD, that α-synuclein undergoes liquid‒liquid phase separation by forming a liquid droplet state, which converts into an amyloid-rich hydrogel with Lewy-body-like properties. This maturation process towards the amyloid state is delayed in the presence of model synaptic vesicles in vitro. Taken together, these results suggest that the formation of Lewy bodies may be linked to the arrested maturation of α-synuclein condensates in the presence of lipids and other cellular components.

Indexed as

alpha-SynucleinAnimalsAnimals, Genetically ModifiedCaenorhabditis elegansCaenorhabditis elegans ProteinsDisease Models, AnimalHumansLewy BodiesParkinson Diseasealpha-SynucleinCaenorhabditis elegans Proteinsliquid‒liquid phase separationParkinson's diseaseα-synuclein

Identifiers

PMID33386842
PMCPMC8339365
OpenAlexW3113629859

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.