Evidence map›Paper›PMID 32926337›Full record

ArticleNeurotoxicity research2021

Alpha-Synuclein Aggregates Associated with Mitochondria in Tunnelling Nanotubes.

Dario Valdinocci, Jaromira Kovarova, Jiri Neuzil, Dean L Pountney

Open access · greenAbstract read
PubMed Publisher
In one paragraph

Article in Neurotoxicity research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed, 1 pooled it
1.6field-weighted citation impact, top 13% 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

24 citing papers in PubMed, 1 synthesis or guideline pooled it, 32 citations in OpenAlex.

  1. Pooled it
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  12. Tunneling Nanotubes in the Brain.Results and problems in cell differentiation · 2024
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  14. Nascent mitochondrial proteins initiate the localized condensation of cytosolic protein aggregates on the mitochondrial surface.Proceedings of the National Academy of Sciences of the United States of America · 2023
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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

4 authors at 2 institutions in 2 countries.

Dario ValdinocciSchool of Medical Science, Griffith University, Gold Coast, Queensland, 4222, Australia.
Jaromira KovarovaInstitute of Biotechnology (BIOCEV), Czech Academy of Sciences, Prague-West, Czech Republic.
Jiri NeuzilSchool of Medical Science, Griffith University, Gold Coast, Queensland, 4222, Australia.
Dean L PountneySchool of Medical Science, Griffith University, Gold Coast, Queensland, 4222, Australia. d.pountney@griffith.edu.au.ORCID http://orcid.org/0000-0002-0653-7832
Griffith University · AUCzech Academy of Sciences, Institute of Biotechnology · CZ

Funding

Grantová Agentura České Republiky 20-05942SGriffith University N/A
6 · The paper itself

Abstract

The interaction of α-synuclein with mitochondria in both typical and atypical Parkinson's disease is a critical component of degeneration. The mechanism of cell-to-cell propagation of pathological α-synuclein in synucleinopathies is unclear. Intercellular exchange of mitochondria along tunnelling nanotubes has been described in other diseases, such as cancer; however, its role in synucleinopathies is unknown. Pathological α-synuclein species have been demonstrated previously to move from cell to cell via tunnelling nanotubes. This process was further explored using co-culture and monoculture systems to determine if α-synuclein binds to migrating mitochondria within tunnelling nanotubes. Super-resolution analysis via stimulated emission depletion microscopy showed interaction between α-synuclein with the mitochondrial outer membrane and the presence of alpha-synuclein associated with mitochondria in tunnelling nanotubes between 1321N1, differentiated THP-1 and SH-SY5Y cell types. siRNA knockdown of Miro1, a critical protein-bridging mitochondria to the motor adaptor complex, had no effect on mitochondrial density or α-synuclein association with mitochondria in tunnelling nanotubes. The results show that α-synuclein aggregates associate with mitochondria in intercellular tunnelling nanotubes, suggesting that mitochondria-mediated α-synuclein transfer between cells may contribute to cell-to-cell spread of α-synuclein aggregates and disease propagation.

Indexed as

Nanotubesalpha-SynucleinCell Line, TumorCoculture TechniquesHumansMitochondriaProtein Aggregation, Pathologicalalpha-SynucleinAlpha-synucleinMiro1MitochondriaParkinson’s diseaseTunnelling nanotube

Identifiers

PMID32926337
OpenAlexW3085917723

What OpenQuestion holds

Textmetadata
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.