Evidence map›Paper›PMID 32392751›Full record

ReviewInternational journal of molecular sciences2020

Lipids: Key Players That Modulate α-Synuclein Toxicity and Neurodegeneration in Parkinson's Disease.

Akio Mori, Yuzuru Imai, Nobutaka Hattori

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed, 1 pooled it
3.2field-weighted citation impact, top 6% 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

37 citing papers in PubMed, 1 synthesis or guideline pooled it, 60 citations in OpenAlex.

  1. Pooled it
  2. Cellular and systemic modifiers of alpha-synuclein proteostasis.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
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  18. A new metabolic model ofLife science alliance · 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

3 authors at 1 institution in 1 country.

Akio MoriDepartment of Neurology, Juntendo University Graduate School of Medicine, Tokyo 113-8421, Japan.
Yuzuru ImaiDepartment of Neurology, Juntendo University Graduate School of Medicine, Tokyo 113-8421, Japan.ORCID 0000-0003-2924-5231
Nobutaka HattoriDepartment of Neurology, Juntendo University Graduate School of Medicine, Tokyo 113-8421, Japan.ORCID 0000-0002-2034-2556
Juntendo University · JP

Funding

Japan Society for the Promotion of Science 17H04049Japan Society for the Promotion of Science 18K15376Otsuka Pharmaceutical N/A
6 · The paper itself

Abstract

Parkinson's disease (PD) is the second most common neurodegenerative disease; it is characterized by the loss of dopaminergic neurons in the midbrain and the accumulation of neuronal inclusions, mainly consisting of α-synuclein (α-syn) fibrils in the affected regions. The prion-like property of the pathological forms of α-syn transmitted via neuronal circuits has been considered inherent in the nature of PD. Thus, one of the potential targets in terms of PD prevention is the suppression of α-syn conversion from the functional form to pathological forms. Recent studies suggested that α-syn interacts with synaptic vesicle membranes and modulate the synaptic functions. A series of studies suggest that transient interaction of α-syn as multimers with synaptic vesicle membranes composed of phospholipids and other lipids is required for its physiological function, while an α-syn-lipid interaction imbalance is believed to cause α-syn aggregation and the resultant pathological α-syn conversion. Altered lipid metabolisms have also been implicated in the modulation of PD pathogenesis. This review focuses on the current literature reporting the role of lipids, especially phospholipids, and lipid metabolism in α-syn dynamics and aggregation processes.

Indexed as

Lipid Metabolismalpha-SynucleinAnimalsHumansParkinson DiseasePhospholipidsSynaptic Vesiclesalpha-SynucleinPhospholipidsLewy bodiesNBIAParkinson’s diseasephospholipidsPLA2G6

Identifiers

PMID32392751
PMCPMC7247581
OpenAlexW3021526455

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.