Evidence map›Paper›PMID 28790319›Full record

ArticleScientific reports2017

Novel animal model defines genetic contributions for neuron-to-neuron transfer of α-synuclein.

Trevor Tyson, Megan Senchuk, Jason F Cooper, Sonia George, Jeremy M Van Raamsdonk, Patrik Brundin

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

28 citing papers in PubMed, 40 citations in OpenAlex.

  1. Review
  2. Article
  3. Unraveling Molecular Targets for Neurodegenerative Diseases ThroughInternational journal of molecular sciences · 2025
    Review
  4. Article
  5. Article
  6. Invertebrate genetic models of amyotrophic lateral sclerosis.Frontiers in molecular neuroscience · 2024
    Review
  7. Review
  8. Review
  9. Monitoring α-synuclein aggregation.Neurobiology of disease · 2023
    Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. Review
  15. "Janus-Faced" α-Synuclein: Role in Parkinson's Disease.Frontiers in cell and developmental biology · 2021
    Review
  16. Article
  17. Biomolecules · 2020
    Review
  18. Article
  19. Article
  20. 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

6 authors at 1 institution in 1 country.

Trevor TysonCenter for Neurodegenerative Science, Van Andel Research Institute, Grand Rapids, Michigan, USA. trevor.tyson@vai.org.
Megan SenchukCenter for Neurodegenerative Science, Van Andel Research Institute, Grand Rapids, Michigan, USA.
Jason F CooperCenter for Neurodegenerative Science, Van Andel Research Institute, Grand Rapids, Michigan, USA.
Sonia GeorgeCenter for Neurodegenerative Science, Van Andel Research Institute, Grand Rapids, Michigan, USA.
Jeremy M Van RaamsdonkCenter for Neurodegenerative Science, Van Andel Research Institute, Grand Rapids, Michigan, USA.ORCID 0000-0001-8376-9605
Patrik BrundinCenter for Neurodegenerative Science, Van Andel Research Institute, Grand Rapids, Michigan, USA.
Van Andel Institute · US

Funding

European Research Council 269064
6 · The paper itself

Abstract

Cell-to-cell spreading of misfolded α-synuclein (α-syn) is suggested to contribute to the progression of neuropathology in Parkinson's disease (PD). Compelling evidence supports the hypothesis that misfolded α-syn transmits from neuron-to-neuron and seeds aggregation of the protein in the recipient cells. Furthermore, α-syn frequently appears to propagate in the brains of PD patients following a stereotypic pattern consistent with progressive spreading along anatomical pathways. We have generated a C. elegans model that mirrors this progression and allows us to monitor α-syn neuron-to-neuron transmission in a live animal over its lifespan. We found that modulation of autophagy or exo/endocytosis, affects α-syn transfer. Furthermore, we demonstrate that silencing C. elegans orthologs of PD-related genes also increases the accumulation of α-syn. This novel worm model is ideal for screening molecules and genes to identify those that modulate prion-like spreading of α-syn in order to target novel strategies for disease modification in PD and other synucleinopathies.

Indexed as

Disease Models, AnimalAdenosine TriphosphatasesAldehyde Oxidoreductasesalpha-SynucleinAnimalsAutophagyBrainCaenorhabditis elegansCaenorhabditis elegans ProteinsCell CommunicationDiscoidin Domain Receptor 2EndocytosisExocytosisGene Expression RegulationGenes, ReporterGreen Fluorescent ProteinsAdenosine TriphosphatasesAldehyde Oxidoreductasesalpha-SynucleinCaenorhabditis elegans ProteinsCATP-6 protein, C elegansDiscoidin Domain Receptor 2DJR-1.2 protein, C elegansenhanced green fluorescent proteinGreen Fluorescent ProteinsLRK-1 protein, C elegansparkin proteinProtein AggregatesProtein Serine-Threonine KinasesRNA, Small InterferingSirolimusTryptophan HydroxylaseUbiquitin-Protein Ligases

Identifiers

PMID28790319
PMCPMC5548897
OpenAlexW2741293755

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.