Evidence map›Paper›PMID 41368826›Full record

ArticleProteomics2026

Probing Early α-Synuclein Oligomers: Insights Into Aggregation Pathways of NACore and preNAC Segments Probed by Trapped Ion-Mobility Mass Spectrometry and Fluorescence Spectroscopy.

Agathe Depraz Depland, Stephanie Mikromanolis, Iuliia Stroganova, Anouk M Rijs

Abstract read
In one paragraph

Article in Proteomics, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
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

4 authors.

Agathe Depraz DeplandDepartment of Chemistry and Pharmaceutical Sciences, Division of Bioanalytical Chemistry, Amsterdam Institute of Molecular and Life Sciences, Vrije Universiteit Amsterdam, Amsterdam, the Netherlands.
Stephanie MikromanolisDepartment of Chemistry and Pharmaceutical Sciences, Division of Bioanalytical Chemistry, Amsterdam Institute of Molecular and Life Sciences, Vrije Universiteit Amsterdam, Amsterdam, the Netherlands.
Iuliia StroganovaDepartment of Chemistry and Pharmaceutical Sciences, Division of Bioanalytical Chemistry, Amsterdam Institute of Molecular and Life Sciences, Vrije Universiteit Amsterdam, Amsterdam, the Netherlands.
Anouk M RijsDepartment of Chemistry and Pharmaceutical Sciences, Division of Bioanalytical Chemistry, Amsterdam Institute of Molecular and Life Sciences, Vrije Universiteit Amsterdam, Amsterdam, the Netherlands.ORCID 0000-0002-7446-9907

Funding

The Dutch Research Council (NWO) Aspasia - 015.015.009The Dutch Research Council (NWO) VICI - VI.C.192.024
6 · The paper itself

Abstract

Misfolding and aggregation of α-Synuclein (α-Syn) play a central role in Parkinson's disease (PD), with oligomeric intermediates implicated as key toxic species. Here, we investigate the aggregation of two α-Syn segments, the NACore (

Indexed as

alpha-SynucleinIon Mobility SpectrometryAmino Acid SequenceHumansMass SpectrometryParkinson DiseaseProtein AggregatesProtein MultimerizationSpectrometry, Fluorescencealpha-SynucleinProtein Aggregatesearly‐stage oligomersNACoreParkinson's diseasepeptide aggregationThT fluorescencetrapped ion‐mobility mass spectrometry

Identifiers

PMID41368826
PMCPMC13048457

What OpenQuestion holds

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Registered trials

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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.