Evidence map›Paper›PMID 36206368›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2022

Quantitative super-resolution imaging of pathological aggregates reveals distinct toxicity profiles in different synucleinopathies.

Michael J Morten, Liina Sirvio, Huzefa Rupawala, Emma Mee Hayes, Aitor Franco, Carola Radulescu, Liming Ying, Samuel J Barnes, Arturo Muga, Yu Ye

Open access · hybridAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
10.0field-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

17 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Molecular Determinants of Protein Pathogenicity at the Single-Aggregate Level.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Mechanisms and pathology of protein misfolding and aggregation.Nature reviews. Molecular cell biology · 2023
    Review
  12. Article
  13. Review
  14. Beyond DNA: new probes for PAINT super-resolution microscopy.Chemical communications (Cambridge, England) · 2023
    Review
  15. Single-Molecule Two-Color Coincidence Detection of Unlabeled alpha-Synuclein Aggregates.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2023
    Article
  16. Article
  17. Review
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

10 authors at 3 institutions in 3 countries.

Michael J MortenDepartment of Brain Sciences, Imperial College London, London W12 0NN, United Kingdom.ORCID 0000-0002-1206-6133
Liina SirvioDepartment of Brain Sciences, Imperial College London, London W12 0NN, United Kingdom.
Huzefa RupawalaDepartment of Brain Sciences, Imperial College London, London W12 0NN, United Kingdom.
Emma Mee HayesDepartment of Brain Sciences, Imperial College London, London W12 0NN, United Kingdom.
Aitor FrancoInstituto Biofisika, University of the Basque Country (Universidad del País Vasco/Euskal Herriko Unibertsitatea), Leioa, 48940 Spain.ORCID 0000-0003-3952-842X
Carola RadulescuDepartment of Brain Sciences, Imperial College London, London W12 0NN, United Kingdom.
Liming YingNational Heart and Lung Institute, Imperial College London, London W12 0BZ, United Kingdom.ORCID 0000-0001-9752-6292
Samuel J BarnesDepartment of Brain Sciences, Imperial College London, London W12 0NN, United Kingdom.ORCID 0000-0003-4030-6453
Arturo MugaInstituto Biofisika, University of the Basque Country (Universidad del País Vasco/Euskal Herriko Unibertsitatea), Leioa, 48940 Spain.ORCID 0000-0003-0345-6882
Yu YeDepartment of Brain Sciences, Imperial College London, London W12 0NN, United Kingdom.ORCID 0000-0003-0441-6399
UK Dementia Research Institute · GBUniversity of the Basque Country · ESImperial College London · GB

Funding

Medical Research CouncilWellcome TrustWellcome Trust 101585/Z/13/Z
6 · The paper itself

Abstract

Protein aggregation is a hallmark of major neurodegenerative disorders. Increasing data suggest that smaller aggregates cause higher toxic response than filamentous aggregates (fibrils). However, the size of small aggregates has challenged their detection within biologically relevant environments. Here, we report approaches to quantitatively super-resolve aggregates in live cells and ex vivo brain tissues. We show that Amytracker 630 (AT630), a commercial aggregate-activated fluorophore, has outstanding photophysical properties that enable super-resolution imaging of α-synuclein, tau, and amyloid-β aggregates, achieving ∼4 nm precision. Applying AT630 to

Indexed as

Parkinson DiseaseSynucleinopathiesalpha-SynucleinAmyloid beta-PeptidesAnimalsLewy BodiesMiceProtein Aggregatesalpha-SynucleinAmyloid beta-PeptidesProtein Aggregatesneurodegenerationproteasomeprotein aggregationsuper-solution imagingα-synuclein

Identifiers

PMID36206368
PMCPMC9573094
OpenAlexW4303453488

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.