Evidence map›Paper›PMID 30630857›Full record

ArticleThe EMBO journal2019

Clustering of Tau fibrils impairs the synaptic composition of α3-Na

Amulya Nidhi Shrivastava, Virginie Redeker, Laura Pieri, Luc Bousset, Marianne Renner, Karine Madiona, Caroline Mailhes-Hamon, Audrey Coens, Luc Buée, Philippe Hantraye and 2 more

Open access · hybridAbstract read
In one paragraph

Article in The EMBO journal, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
5.1field-weighted citation impact, top 4% 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

32 citing papers in PubMed, 56 citations in OpenAlex.

  1. Differential proteostasis imbalance and the molecular basis of distinct synucleinopathies and tauopathies.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
    Review
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  9. Tau and Amyloid β Protein in Patient-Derived Aqueous Brain Extracts Act Concomitantly to Disrupt Long-Term PotentiationThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2023
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  17. Mitochondrial ROS control neuronal excitability and cell fate in frontotemporal dementia.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2022
    Article
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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

12 authors at 2 institutions in 1 country.

Amulya Nidhi ShrivastavaCEA, Institut François Jacob (MIRcen) and CNRS Laboratory of Neurodegenerative Diseases (UMR9199), Fontenay-aux-Roses, France.ORCID 0000-0002-1322-8018
Virginie RedekerCEA, Institut François Jacob (MIRcen) and CNRS Laboratory of Neurodegenerative Diseases (UMR9199), Fontenay-aux-Roses, France.ORCID 0000-0003-2694-8388
Laura PieriCEA, Institut François Jacob (MIRcen) and CNRS Laboratory of Neurodegenerative Diseases (UMR9199), Fontenay-aux-Roses, France.
Luc BoussetCEA, Institut François Jacob (MIRcen) and CNRS Laboratory of Neurodegenerative Diseases (UMR9199), Fontenay-aux-Roses, France.
Marianne RennerINSERM, UMR - S 839 Institut du Fer à Moulin (IFM), Sorbonne Université, Paris, France.
Karine MadionaCEA, Institut François Jacob (MIRcen) and CNRS Laboratory of Neurodegenerative Diseases (UMR9199), Fontenay-aux-Roses, France.
Caroline Mailhes-HamonInstitut de Biologie de l'ENS (IBENS), École Normale Supérieure, INSERM, CNRS, PSL Research University, Paris, France.
Audrey CoensCEA, Institut François Jacob (MIRcen) and CNRS Laboratory of Neurodegenerative Diseases (UMR9199), Fontenay-aux-Roses, France.
Luc BuéeCHU Lille, INSERM UMR-S 1172 JPArc "Alzheimer & Tauopathies" Universite Lille, Lille, France.
Philippe HantrayeCEA, Institut François Jacob (MIRcen) and CNRS Laboratory of Neurodegenerative Diseases (UMR9199), Fontenay-aux-Roses, France.
Antoine TrillerInstitut de Biologie de l'ENS (IBENS), École Normale Supérieure, INSERM, CNRS, PSL Research University, Paris, France triller@biologie.ens.fr ronald.melki@cnrs.fr.ORCID 0000-0002-7530-1233
Ronald MelkiCEA, Institut François Jacob (MIRcen) and CNRS Laboratory of Neurodegenerative Diseases (UMR9199), Fontenay-aux-Roses, France triller@biologie.ens.fr ronald.melki@cnrs.fr.ORCID 0000-0003-0000-7096
Centre National de la Recherche Scientifique · FRInserm · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tau assemblies have prion-like properties: they propagate from one neuron to another and amplify by seeding the aggregation of endogenous Tau. Although key in prion-like propagation, the binding of exogenous Tau assemblies to the plasma membrane of naïve neurons is not understood. We report that fibrillar Tau forms clusters at the plasma membrane following lateral diffusion. We found that the fibrils interact with the Na

Indexed as

alpha-SynucleinAmyloidAnimalsCA1 Region, HippocampalCell MembraneHumansMiceMice, Inbred C57BLNeuronsReceptors, AMPASodium-Potassium-Exchanging ATPaseSynapsestau Proteinsalpha-SynucleinAmyloidATP1A3 protein, humanReceptors, AMPASodium-Potassium-Exchanging ATPasetau Proteinscross‐talk of pathogenic proteinsmisfolding diseaseprotein aggregation and clusteringsingle‐particle trackingtauopathies

Identifiers

PMID30630857
PMCPMC6356061
OpenAlexW2909771213

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.