Evidence map›Paper›PMID 29565978›Full record

ArticlePloS one2018

Exogenous α-synuclein hinders synaptic communication in cultured cortical primary rat neurons.

G C Hassink, C C Raiss, I M J Segers-Nolten, R J A van Wezel, V Subramaniam, J le Feber, M M A E Claessens

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.7field-weighted citation impact, top 11% 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

16 citing papers in PubMed, 29 citations in OpenAlex.

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  11. Metal ions shape α-synuclein.Scientific reports · 2020
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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

7 authors at 2 institutions in 1 country.

G C HassinkClinical Neurophysiology, MIRA Institute for Biomedical Technology and Technical Medicine, University of Twente, Postbus, Enschede, the Netherlands.
C C RaissNanobiophysics Group, MESA+ Institute for Nanotechnology, University of Twente, Postbus, Enschede, the Netherlands.
I M J Segers-NoltenNanobiophysics Group, MESA+ Institute for Nanotechnology, University of Twente, Postbus, Enschede, the Netherlands.
R J A van WezelBiomedical Signal and Systems, MIRA Institute for Biomedical Technology and Technical Medicine, University of Twente, Postbus, Enschede, the Netherlands.
V SubramaniamNanobiophysics Group, MESA+ Institute for Nanotechnology, University of Twente, Postbus, Enschede, the Netherlands.
J le FeberClinical Neurophysiology, MIRA Institute for Biomedical Technology and Technical Medicine, University of Twente, Postbus, Enschede, the Netherlands.ORCID 0000-0002-0605-1437
M M A E ClaessensClinical Neurophysiology, MIRA Institute for Biomedical Technology and Technical Medicine, University of Twente, Postbus, Enschede, the Netherlands.
University of Twente · NLRadboud University Nijmegen · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Amyloid aggregates of the protein α-synuclein (αS) called Lewy Bodies (LB) and Lewy Neurites (LN) are the pathological hallmark of Parkinson's disease (PD) and other synucleinopathies. We have previously shown that high extracellular αS concentrations can be toxic to cells and that neurons take up αS. Here we aimed to get more insight into the toxicity mechanism associated with high extracellular αS concentrations (50-100 μM). High extracellular αS concentrations resulted in a reduction of the firing rate of the neuronal network by disrupting synaptic transmission, while the neuronal ability to fire action potentials was still intact. Furthermore, many cells developed αS deposits larger than 500 nm within five days, but otherwise appeared healthy. Synaptic dysfunction clearly occurred before the establishment of large intracellular deposits and neuronal death, suggesting that an excessive extracellular αS concentration caused synaptic failure and which later possibly contributed to neuronal death.

Indexed as

Action Potentialsalpha-SynucleinAnimalsCells, CulturedCell SurvivalCerebral CortexExtracellular SpaceHumansIntracellular SpaceNeuronsProtein Aggregation, PathologicalRats, WistarRecombinant ProteinsSynapsesSynaptic Transmissionalpha-SynucleinRecombinant ProteinsSNCA protein, humanSnca protein, rat

Identifiers

PMID29565978
PMCPMC5863964
OpenAlexW2791045308

What OpenQuestion holds

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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.