Evidence map›Paper›PMID 31265132›Full record

ReviewJournal of neurochemistry2019

Cellular models of alpha-synuclein toxicity and aggregation.

Marion Delenclos, Jeremy D Burgess, Agaristi Lamprokostopoulou, Tiago F Outeiro, Kostas Vekrellis, Pamela J McLean

Open access · greenAbstract readReview
In one paragraph

Review in Journal of neurochemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
10.0field-weighted citation impact, top 1% 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

60 citing papers in PubMed, 117 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Gangliosides in molecular interactions and cell regulation.The Journal of biological chemistry · 2026
    Review
  6. Article
  7. Article
  8. Article
  9. Article
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  11. Review
  12. Article
  13. Review
  14. Research models to study lewy body dementia.Molecular neurodegeneration · 2025
    Review
  15. Article
  16. Review
  17. Review
  18. Article
  19. Review
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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

6 authors at 3 institutions in 4 countries.

Marion DelenclosDepartment of Neuroscience, Mayo Clinic, Jacksonville, Florida, USA.
Jeremy D BurgessDepartment of Neuroscience, Mayo Clinic, Jacksonville, Florida, USA.
Agaristi LamprokostopoulouDepartment of Neuroscience, Center for Basic Research, Biomedical Research Foundation, Academy of Athens, Athens, Greece.
Tiago F OuteiroDepartment of Experimental Neurodegeneration, Center for Biostructural Imaging of Neurodegeneration, University Medical Center Göttingen, Göttingen, Germany.ORCID 0000-0003-1679-1727
Kostas VekrellisDepartment of Neuroscience, Center for Basic Research, Biomedical Research Foundation, Academy of Athens, Athens, Greece.ORCID 0000-0001-5702-9953
Pamela J McLeanDepartment of Neuroscience, Mayo Clinic, Jacksonville, Florida, USA.ORCID 0000-0003-3168-951X
Jacksonville College · USAcademy of Athens · GRUniversitätsmedizin Göttingen · DE

Funding

Utilization of proteomics and lipidomics to identify modifiers of LBDU54NS110435 · NINDS · MAYO CLINIC JACKSONVILLE · PI DICKSON, DENNIS WILLIAM · 2019 to 2023
$14.5M
Mitochondrial Sirtuin 3 in Parkinson's diseaseR01NS110085 · NINDS · MAYO CLINIC JACKSONVILLE · PI MCLEAN, PAMELA J, SPRINGER, WOLFDIETER · 2019 to 2023
$2.5M
DFG Center for Nanoscale Microscopy and Molecular Physiology of the Brain (CNMPB).NINDS NIH HHS R01 NS110085NINDS NIH HHS U54 NS110435
6 · The paper itself

Abstract

Misfolding and aggregation of alpha-synuclein (α-synuclein) with concomitant cytotoxicity is a hallmark of Lewy body related disorders such as Parkinson's disease, dementia with Lewy bodies, and multiple system atrophy. Although it plays a pivotal role in pathogenesis and disease progression, the function of α-synuclein and the molecular mechanisms underlying α-synuclein-induced neurotoxicity in these diseases are still elusive. Many in vitro and in vivo experimental models mimicking α-synuclein pathology such as oligomerization, toxicity and more recently neuronal propagation have been generated over the years. In particular, cellular models have been crucial for our comprehension of the pathogenic process of the disease and are beneficial for screening of molecules capable of modulating α-synuclein toxicity. Here, we review α-synuclein based cell culture models that reproduce some features of the neuronal populations affected in patients, from basic unicellular organisms to mammalian cell lines and primary neurons, to the cutting edge models of patient-specific cell lines. These reprogrammed cells known as induced pluripotent stem cells (iPSCs) have garnered attention because they closely reproduce the characteristics of neurons found in patients and provide a valuable tool for mechanistic studies. We also discuss how different cell models may constitute powerful tools for high-throughput screening of molecules capable of modulating α-synuclein toxicity and prevention of its propagation. This article is part of the Special Issue "Synuclein".

Indexed as

alpha-SynucleinCell Culture TechniquesCells, CulturedCellular ReprogrammingDopamineDrug Evaluation, PreclinicalHEK293 CellsHumansInduced Pluripotent Stem CellsIn Vitro TechniquesLewy BodiesModels, NeurologicalNeurodegenerative DiseasesNeuronsProtein Aggregation, PathologicalProtein Foldingalpha-SynucleinDopamineRecombinant ProteinsSaccharomyces cerevisiae Proteinscellular modeldopaminergic neuronsoligomersParkinson’s diseaseα-Synuclein

Identifiers

PMID31265132
PMCPMC8864560
OpenAlexW2955588013

What OpenQuestion holds

Textmetadata
LicenceTDM
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.