Evidence map›Paper›PMID 35420219›Full record

ArticleMovement disorders : official journal of the Movement Disorder Society2022

Alpha-Synuclein is Involved in DYT1 Dystonia Striatal Synaptic Dysfunction.

Giulia Ponterio, Gaia Faustini, Ilham El Atiallah, Giuseppe Sciamanna, Maria Meringolo, Annalisa Tassone, Paola Imbriani, Silvia Cerri, Giuseppina Martella, Paola Bonsi and 2 more

Open access · hybridAbstract read
In one paragraph

Article in Movement disorders : official journal of the Movement Disorder Society, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

4 citing papers in PubMed, 8 citations in OpenAlex.

  1. Article
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  3. Review
  4. 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

12 authors at 6 institutions in 1 country.

Giulia PonterioLaboratory of Neurophysiology and Plasticity, IRCCS Fondazione Santa Lucia, Rome, Italy.
Gaia FaustiniDivision of Pharmacology, Department of Molecular and Translational Medicine, University of Brescia, Brescia, Italy.
Ilham El AtiallahLaboratory of Neurophysiology and Plasticity, IRCCS Fondazione Santa Lucia, Rome, Italy.
Giuseppe SciamannaLaboratory of Neurophysiology and Plasticity, IRCCS Fondazione Santa Lucia, Rome, Italy.
Maria MeringoloLaboratory of Neurophysiology and Plasticity, IRCCS Fondazione Santa Lucia, Rome, Italy.
Annalisa TassoneLaboratory of Neurophysiology and Plasticity, IRCCS Fondazione Santa Lucia, Rome, Italy.
Paola ImbrianiLaboratory of Neurophysiology and Plasticity, IRCCS Fondazione Santa Lucia, Rome, Italy.
Silvia CerriIRCCS Fondazione Mondino, Pavia, Italy.ORCID 0000-0002-6466-5381
Giuseppina MartellaLaboratory of Neurophysiology and Plasticity, IRCCS Fondazione Santa Lucia, Rome, Italy.
Paola BonsiLaboratory of Neurophysiology and Plasticity, IRCCS Fondazione Santa Lucia, Rome, Italy.
Arianna Bellucci *Division of Pharmacology, Department of Molecular and Translational Medicine, University of Brescia, Brescia, Italy.ORCID 0000-0002-9581-1919
Antonio Pisani *IRCCS Fondazione Mondino, Pavia, Italy.ORCID 0000-0002-8432-594X
Fondazione Santa Lucia · ITUniversity of Brescia · ITFondazione FADOI · ITSaint Camillus International University of Health and Medical Sciences · ITUniversity of Pavia · ITUniversity of Rome Tor Vergata · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundThe neuronal protein alpha-synuclein (α-Syn) is crucially involved in Parkinson's disease pathophysiology. Intriguingly, torsinA (TA), the protein causative of DYT1 dystonia, has been found to accumulate in Lewy bodies and to interact with α-Syn. Both proteins act as molecular chaperones and control synaptic machinery. Despite such evidence, the role of α-Syn in dystonia has never been investigated.

objectiveWe explored whether α-Syn and N-ethylmaleimide sensitive fusion attachment protein receptor proteins (SNAREs), that are known to be modulated by α-Syn, may be involved in DYT1 dystonia synaptic dysfunction.

methodsWe used electrophysiological and biochemical techniques to study synaptic alterations in the dorsal striatum of the Tor1a

resultsIn the Tor1a

conclusionsOur data demonstrate an unprecedented relationship between TA and α-Syn, and reveal that α-Syn and SNAREs alterations characterize the synaptic dysfunction underlying DYT1 dystonia. © 2022 The Authors. Movement Disorders published by Wiley Periodicals LLC on behalf of International Parkinson Movement Disorder Society.

Indexed as

DystoniaDystonia Musculorum DeformansDystonic Disordersalpha-SynucleinAnimalsCorpus StriatumDisease Models, AnimalHumansMiceMice, TransgenicMolecular ChaperonesSNARE Proteinsalpha-SynucleinDyt1 protein, mouseMolecular ChaperonesSNARE ProteinsSnca protein, mouseTOR1A protein, humanasynchronous glutamate releasedystoniaSNAREsstriatumsynaptic vesicle turnoverα-synuclein

Identifiers

PMID35420219
PMCPMC9323501
OpenAlexW4223965806

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.