Evidence map›Paper›PMID 37048156›Full record

ArticleCells2023

α-Synuclein Preformed Fibrils Bind to β-Neurexins and Impair β-Neurexin-Mediated Presynaptic Organization.

Benjamin Feller, Aurélie Fallon, Wen Luo, Phuong Trang Nguyen, Irina Shlaifer, Alfred Kihoon Lee, Nicolas Chofflet, Nayoung Yi, Husam Khaled, Samer Karkout and 3 more

Abstract read
In one paragraph

Article in Cells, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
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  5. Article
  6. Review
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  8. Article
  9. Review
  10. Article
  11. GM1 oligosaccharide efficacy against α-synuclein aggregation and toxicity in vitro.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2023
    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

13 authors.

Benjamin FellerSynapse Development and Plasticity Research Unit, Institut de Recherches Cliniques de Montréal, Montreal, QC H2W 1R7, Canada.
Aurélie FallonSynapse Development and Plasticity Research Unit, Institut de Recherches Cliniques de Montréal, Montreal, QC H2W 1R7, Canada.ORCID 0000-0002-4938-6480
Wen LuoThe Neuro's Early Drug Discovery Unit (EDDU), Department of Neurology and Neurosurgery, Montreal Neurological Institute-Hospital, McGill University, Montreal, QC H3A 2B4, Canada.
Phuong Trang NguyenDepartment of Chemistry, Quebec Network for Research on Protein Function, Engineering and Applications, PROTEO, Université du Québec à Montréal, Montreal, QC H3C 3P8, Canada.
Irina ShlaiferThe Neuro's Early Drug Discovery Unit (EDDU), Department of Neurology and Neurosurgery, Montreal Neurological Institute-Hospital, McGill University, Montreal, QC H3A 2B4, Canada.
Alfred Kihoon LeeSynapse Development and Plasticity Research Unit, Institut de Recherches Cliniques de Montréal, Montreal, QC H2W 1R7, Canada.
Nicolas ChoffletSynapse Development and Plasticity Research Unit, Institut de Recherches Cliniques de Montréal, Montreal, QC H2W 1R7, Canada.
Nayoung YiSynapse Development and Plasticity Research Unit, Institut de Recherches Cliniques de Montréal, Montreal, QC H2W 1R7, Canada.
Husam KhaledSynapse Development and Plasticity Research Unit, Institut de Recherches Cliniques de Montréal, Montreal, QC H2W 1R7, Canada.
Samer KarkoutSynapse Development and Plasticity Research Unit, Institut de Recherches Cliniques de Montréal, Montreal, QC H2W 1R7, Canada.
Steve BourgaultDepartment of Chemistry, Quebec Network for Research on Protein Function, Engineering and Applications, PROTEO, Université du Québec à Montréal, Montreal, QC H3C 3P8, Canada.ORCID 0000-0002-5563-8787
Thomas M DurcanThe Neuro's Early Drug Discovery Unit (EDDU), Department of Neurology and Neurosurgery, Montreal Neurological Institute-Hospital, McGill University, Montreal, QC H3A 2B4, Canada.ORCID 0000-0003-3942-1956
Hideto TakahashiSynapse Development and Plasticity Research Unit, Institut de Recherches Cliniques de Montréal, Montreal, QC H2W 1R7, Canada.

Funding

CIHR PTJ-159588
6 · The paper itself

Abstract

Synucleinopathies form a group of neurodegenerative diseases defined by the misfolding and aggregation of α-synuclein (α-syn). Abnormal accumulation and spreading of α-syn aggregates lead to synapse dysfunction and neuronal cell death. Yet, little is known about the synaptic mechanisms underlying the α-syn pathology. Here we identified β-isoforms of neurexins (β-NRXs) as presynaptic organizing proteins that interact with α-syn preformed fibrils (α-syn PFFs), toxic α-syn aggregates, but not α-syn monomers. Our cell surface protein binding assays and surface plasmon resonance assays reveal that α-syn PFFs bind directly to β-NRXs through their N-terminal histidine-rich domain (HRD) at the nanomolar range (K

Indexed as

Parkinson DiseaseSynucleinopathiesalpha-SynucleinHumansLewy BodiesSynapsesalpha-Synucleinneurexinprotein interactionsynapse organizationsynaptic pathologyα-synuclein

Identifiers

PMID37048156
PMCPMC10093570

What OpenQuestion holds

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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.