Evidence map›Paper›PMID 42030949›Full record

ArticleCell reports methods2026

Single-molecule detection methods to study alpha-synuclein aggregation in postmortem Parkinson's disease brains.

Emre Fertan, John S H Danial, Stephen Neame, Jeff Y L Lam, Matthew W Cotton, Melanie Burke, Zengjie Xia, Yunzhao Wu, Ben Powney, Yoichi Imaizumi and 4 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Cell reports methods, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

14 authors.

Emre FertanYusuf Hamied Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, UK; UK Dementia Research Institute at University of Cambridge, Cambridge CB2 0XY, UK. Electronic address: ef417@cam.ac.uk.
John S H DanialYusuf Hamied Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, UK; UK Dementia Research Institute at University of Cambridge, Cambridge CB2 0XY, UK.
Stephen NeameEisai Ltd., EMEA Knowledge Centre, Mosquito Way, Hatfield AL10 9SN, UK.
Jeff Y L LamYusuf Hamied Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, UK; UK Dementia Research Institute at University of Cambridge, Cambridge CB2 0XY, UK.
Matthew W CottonYusuf Hamied Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, UK; UK Dementia Research Institute at University of Cambridge, Cambridge CB2 0XY, UK.
Melanie BurkeYusuf Hamied Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, UK; UK Dementia Research Institute at University of Cambridge, Cambridge CB2 0XY, UK.
Zengjie XiaYusuf Hamied Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, UK; UK Dementia Research Institute at University of Cambridge, Cambridge CB2 0XY, UK.
Yunzhao WuYusuf Hamied Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, UK; UK Dementia Research Institute at University of Cambridge, Cambridge CB2 0XY, UK.
Ben PowneyEisai Ltd., EMEA Knowledge Centre, Mosquito Way, Hatfield AL10 9SN, UK.
Yoichi ImaizumiEisai Ltd., EMEA Knowledge Centre, Mosquito Way, Hatfield AL10 9SN, UK.
Annelies QuaegebeurDepartment of Clinical Neurosciences, University of Cambridge, Cambridge CB2 0XY, UK.
Georg MeislYusuf Hamied Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, UK; UK Dementia Research Institute at University of Cambridge, Cambridge CB2 0XY, UK.
James StaddonEisai Ltd., EMEA Knowledge Centre, Mosquito Way, Hatfield AL10 9SN, UK.
David KlenermanYusuf Hamied Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, UK; UK Dementia Research Institute at University of Cambridge, Cambridge CB2 0XY, UK. Electronic address: dk10012@cam.ac.uk.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nanoscopic aggregates of alpha-synuclein (ɑSyn) have been observed in Parkinson's disease (PD). However, the processes that occur in vivo leading to the formation of these small aggregates are not well understood. We used ultra-sensitive single-molecule methods, including single molecule array (SIMOA), and super-resolution microscopy to quantify and characterize ɑSyn aggregates harvested from human brain samples, alongside a mouse model of synucleinopathy, using different tissue processing methods. While aggregate numbers did not differ between PD and control samples, larger aggregates were detected in PD brain samples. Moreover, different sub-populations of aggregates were obtained by different extraction methods, with diffusible and membrane-bound aggregates producing a more pronounced difference between disease and control samples. Our data suggest that ɑSyn aggregates slowly in the brain, leading to formation of larger aggregates in a sub-set of cells.

Indexed as

alpha-SynucleinBrainParkinson DiseaseProtein AggregatesProtein Aggregation, PathologicalSingle Molecule ImagingAnimalsDisease Models, AnimalFemaleHumansMaleMicealpha-SynucleinProtein AggregatesCP: imagingCP: neurosciencedata modelingdiffusible aggregateDNA-PAINTextractionmouse modelsarkosylSIMOAsingle-molecule detectionsoluble aggregateTriton X-100

Identifiers

PMID42030949
PMCPMC13282648

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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.