Evidence map›Paper›PMID 28049716›Full record

ArticleJournal of cell science2017

Sideroflexin 3 is an α-synuclein-dependent mitochondrial protein that regulates synaptic morphology.

Inês S Amorim, Laura C Graham, Roderick N Carter, Nicholas M Morton, Fella Hammachi, Tilo Kunath, Giuseppa Pennetta, Sarah M Carpanini, Jean C Manson, Douglas J Lamont and 2 more

Open access · hybridAbstract read
In one paragraph

Article in Journal of cell science, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

25 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Genetic ablation ofiScience · 2026
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  16. Non-coding RNA-mediated high expression ofFrontiers in immunology · 2022
    Article
  17. Review
  18. Article
  19. Forward genetic analysis using OCT screening identifiesProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  20. 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

12 authors at 5 institutions in 1 country.

Inês S AmorimCentre for Integrative Physiology, University of Edinburgh, Hugh Robson Building, Edinburgh, EH8 9XD, UK.
Laura C GrahamEuan MacDonald Centre for Motor Neurone Disease Research, Chancellor's Building, University of Edinburgh, Edinburgh, EH16 4SB, UK.
Roderick N CarterMolecular Metabolism Group, University/BHF Centre for Cardiovascular Science, Queen's Medical Research Institute, University of Edinburgh, Edinburg, EH16 4TJ, UK.
Nicholas M MortonMolecular Metabolism Group, University/BHF Centre for Cardiovascular Science, Queen's Medical Research Institute, University of Edinburgh, Edinburg, EH16 4TJ, UK.
Fella HammachiMRC Centre for Regenerative Medicine, Institute for Stem Cell Research, The University of Edinburgh, Edinburgh, EH16 4UU, UK.
Tilo KunathMRC Centre for Regenerative Medicine, Institute for Stem Cell Research, The University of Edinburgh, Edinburgh, EH16 4UU, UK.
Giuseppa PennettaCentre for Integrative Physiology, University of Edinburgh, Hugh Robson Building, Edinburgh, EH8 9XD, UK.
Sarah M CarpaniniDivision of Neurobiology, The Roslin Institute and Royal (Dick) School of Veterinary Studies, University of Edinburgh, Edinburgh, EH25 9RG, UK.
Jean C MansonDivision of Neurobiology, The Roslin Institute and Royal (Dick) School of Veterinary Studies, University of Edinburgh, Edinburgh, EH25 9RG, UK.
Douglas J LamontFingerPrints Proteomics Facility, College of Life Sciences, University of Dundee, Dundee, DD1 5EH, UK.
Thomas M WishartEuan MacDonald Centre for Motor Neurone Disease Research, Chancellor's Building, University of Edinburgh, Edinburgh, EH16 4SB, UK.
Thomas H GillingwaterCentre for Integrative Physiology, University of Edinburgh, Hugh Robson Building, Edinburgh, EH8 9XD, UK T.Gillingwater@ed.ac.uk.ORCID 0000-0002-0306-5577
Roslin Institute · GBMott MacDonald (United Kingdom) · GBMRC Centre for Regenerative Medicine · GBThe Queen's Medical Research Institute · GBUniversity of Dundee · GB

Funding

Biotechnology and Biological Sciences Research Council BB/J004332/1Biotechnology and Biological Sciences Research Council BBS/E/D/20251969Medical Research Council MR/J012831/1Medical Research Council MR/K017047/1Medical Research Council MR/M010341/1Parkinson's UK F-0902Parkinson's UK K-1205Wellcome TrustWellcome Trust 100981/Z/13/Z
6 · The paper itself

Abstract

α-Synuclein plays a central role in Parkinson's disease, where it contributes to the vulnerability of synapses to degeneration. However, the downstream mechanisms through which α-synuclein controls synaptic stability and degeneration are not fully understood. Here, comparative proteomics on synapses isolated from α-synuclein

Indexed as

alpha-SynucleinAnimalsCation Transport ProteinsDrosophila melanogasterDrosophila ProteinsEnergy MetabolismGene OntologyHumansMembrane ProteinsMice, Inbred C57BLMice, KnockoutMitochondrial MembranesMitochondrial ProteinsNeuromuscular JunctionSynapsesalpha-SynucleinCation Transport ProteinsDrosophila ProteinsMembrane ProteinsMitochondrial ProteinsSfxn2 protein, DrosophilaSfxn3 protein, mouseAlpha-synucleinMitochondriaNeurodegenerationSideroflexin 3Synapse

Identifiers

PMID28049716
PMCPMC5278670
OpenAlexW2563028246

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.