Evidence map›Paper›PMID 39197832›Full record

ArticleACS chemical neuroscience2024

Single-Molecule Fingerprinting Reveals Different Growth Mechanisms in Seed Amplification Assays for Different Polymorphs of α-Synuclein Fibrils.

Derrick Lau, Yuan Tang, Vijaya Kenche, Thomas Copie, Daryan Kempe, Eve Jary, Noah J Graves, Maté Biro, Colin L Masters, Nicolas Dzamko and 2 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in ACS chemical neuroscience, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. 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

12 authors.

Derrick LauEMBL Australia Node for Single Molecule Science and School of Biomedical Sciences, Faculty of Medicine, The University of New South Wales, Sydney, NSW 2052, Australia.ORCID 0000-0002-9311-647X
Yuan TangBrain and Mind Centre and Faculty of Medicine and Health, School of Medical Sciences, University of Sydney, Camperdown, NSW 2050, Australia.
Vijaya KencheFlorey Institute of Neuroscience and Mental Health, The University of Melbourne, Parkville, VIC 3010, Australia.
Thomas CopieEMBL Australia Node for Single Molecule Science and School of Biomedical Sciences, Faculty of Medicine, The University of New South Wales, Sydney, NSW 2052, Australia.ORCID 0000-0001-6766-0116
Daryan KempeEMBL Australia Node for Single Molecule Science and School of Biomedical Sciences, Faculty of Medicine, The University of New South Wales, Sydney, NSW 2052, Australia.
Eve JaryEMBL Australia Node for Single Molecule Science and School of Biomedical Sciences, Faculty of Medicine, The University of New South Wales, Sydney, NSW 2052, Australia.
Noah J GravesEMBL Australia Node for Single Molecule Science and School of Biomedical Sciences, Faculty of Medicine, The University of New South Wales, Sydney, NSW 2052, Australia.
Maté BiroEMBL Australia Node for Single Molecule Science and School of Biomedical Sciences, Faculty of Medicine, The University of New South Wales, Sydney, NSW 2052, Australia.
Colin L MastersFlorey Institute of Neuroscience and Mental Health, The University of Melbourne, Parkville, VIC 3010, Australia.
Nicolas DzamkoBrain and Mind Centre and Faculty of Medicine and Health, School of Medical Sciences, University of Sydney, Camperdown, NSW 2050, Australia.
Yann GambinEMBL Australia Node for Single Molecule Science and School of Biomedical Sciences, Faculty of Medicine, The University of New South Wales, Sydney, NSW 2052, Australia.
Emma SiereckiEMBL Australia Node for Single Molecule Science and School of Biomedical Sciences, Faculty of Medicine, The University of New South Wales, Sydney, NSW 2052, Australia.ORCID 0000-0001-9970-868X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

α-Synuclein (αSyn) aggregates, detected in the biofluids of patients with Parkinson's disease (PD), have the ability to catalyze their own aggregation, leading to an increase in the number and size of aggregates. This self-templated amplification is used by newly developed assays to diagnose Parkinson's disease and turns the presence of αSyn aggregates into a biomarker of the disease. It has become evident that αSyn can form fibrils with slightly different structures, called "strains" or polymorphs, but little is known about their differential reactivity in diagnostic assays. Here, we compared the properties of two well-described αSyn polymorphs. Using single-molecule techniques, we observed that one of the polymorphs had an increased tendency to undergo secondary nucleation and we showed that this could explain the differences in reactivity observed in

Indexed as

alpha-SynucleinParkinson DiseaseHumansProtein AggregatesProtein Aggregation, PathologicalSingle Molecule Imagingalpha-SynucleinProtein AggregatesSNCA protein, humanParkinson’s diseasePMCApreformed fibrilsRT-QuICseed amplification assaysingle-molecule detectionstrainsα-synuclein

Identifiers

PMID39197832
PMCPMC11413846

What OpenQuestion holds

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LicenceCC BY-NC-ND
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.