Evidence map›Paper›PMID 39596523›Full record

ArticleInternational journal of molecular sciences2024

In Vitro Cell Model Investigation of Alpha-Synuclein Aggregate Morphology Using Spectroscopic Imaging.

Priyanka Swaminathan, Therése Klingstedt, Vasileios Theologidis, Hjalte Gram, Johan Larsson, Lars Hagen, Nina B Liabakk, Odrun A Gederaas, Per Hammarström, K Peter R Nilsson and 2 more

Abstract read
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In one paragraph

Article in International journal of molecular sciences, 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. Article
  2. The Progress of Active Immunotherapy for Parkinson's Disease.International journal of molecular sciences · 2026
    Review
  3. Article
  4. 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

12 authors.

Priyanka SwaminathanDepartment of Physics, Faculty of Natural Sciences, Norwegian University of Science and Technology (NTNU), Gløshaugen, Realfagbygget, NO-7491 Trondheim, Norway.
Therése KlingstedtDepartment of Physics, Chemistry and Biology, Linköping University, SE-581 83 Linköping, Sweden.
Vasileios TheologidisDepartment of Clinical Medicine-Core Center for Molecular Morphology, Section for Stereology and Microscopy, Aarhus University, 8000 Aarhus, Denmark.
Hjalte GramDANDRITE, Danish Research Institute of Translational Neuroscience & Department of Biomedicine, Aarhus University, 8000 Aarhus, Denmark.
Johan LarssonDepartment of Physics, Chemistry and Biology, Linköping University, SE-581 83 Linköping, Sweden.
Lars HagenPROMEC-Proteomics and Modomics Experimental Core Facility at NTNU and the Central Norway Regional Health Authority, NO-7491 Trondheim, Norway.
Nina B LiabakkDepartment of Clinical and Molecular Medicine, NTNU Norwegian University of Science and Technology, NO-7491 Trondheim, Norway.
Odrun A GederaasDivision of Natural Sciences, University of Agder, NO-4630 Kristiansand, Norway.
Per HammarströmDepartment of Physics, Chemistry and Biology, Linköping University, SE-581 83 Linköping, Sweden.
K Peter R NilssonDepartment of Physics, Chemistry and Biology, Linköping University, SE-581 83 Linköping, Sweden.
Nathalie Van Den BergeDepartment of Clinical Medicine-Core Center for Molecular Morphology, Section for Stereology and Microscopy, Aarhus University, 8000 Aarhus, Denmark.ORCID 0000-0001-9384-1279
Mikael LindgrenDepartment of Physics, Faculty of Natural Sciences, Norwegian University of Science and Technology (NTNU), Gløshaugen, Realfagbygget, NO-7491 Trondheim, Norway.ORCID 0000-0001-6649-7871

Funding

Horizon 2020 101004806Norges forskningsråd 329397Swedish Research Council 2021-00698TNA-MOSBRI 2023-150
6 · The paper itself

Abstract

Recently, it has been hypothesized that alpha-synuclein protein strain morphology may be associated with clinical subtypes of alpha-synucleinopathies, like Parkinson's disease and multiple system atrophy. However, direct evidence is lacking due to the caveat of conformation-specific characterization of protein strain morphology. Here we present a new cell model based in vitro method to explore various alpha-synuclein (αsyn) aggregate morphotypes. We performed a spectroscopic investigation of the HEK293 cell model, transfected with human wildtype-αsyn and A53T-αsyn variants, using the amyloid fibril-specific heptameric luminescent oligomeric thiophene h-FTAA. The spectral profile of h-FTAA binding to aggregates displayed a blue-shifted spectrum with a fluorescence decay time longer than in PBS, suggesting a hydrophobic binding site. In vitro spectroscopic binding characterization of h-FTAA with αsyn pre-formed fibrils suggested a binding dissociation constant K

Indexed as

alpha-SynucleinAmyloidHEK293 CellsHumansProtein AggregatesProtein Aggregation, PathologicalSpectrometry, Fluorescencealpha-SynucleinAmyloidProtein AggregatesSNCA protein, humanFLIMHEK293 cellsh-FTAALCOαsyn aggregate morphologies

Identifiers

PMID39596523
PMCPMC11594916

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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.