Evidence map›Paper›PMID 31333408›Full record

ReviewFrontiers in neuroscience2019

Lipids as

Kensuke Ikenaka, Mari Suzuki, Hideki Mochizuki, Yoshitaka Nagai

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in neuroscience, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

14 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Article
  3. Lysophagy protects against propagation of α-synuclein aggregation through ruptured lysosomal vesicles.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  4. Article
  5. Transcranial photobiomodulation ameliorates midbrain and striatum neurochemical impairments and behavioral deficits in reserpine-induced parkinsonism in rats.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2023
    Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Synergistic Effects of Milk-Derived Exosomes and Galactose onInternational journal of molecular sciences · 2021
    Review
  11. Therapeutic Potential ofParkinson's disease · 2021
    Review
  12. Review
  13. The Role of Lipids in the Initiation of α-Synuclein Misfolding.Frontiers in cell and developmental biology · 2020
    Review
  14. 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

4 authors at 2 institutions in 1 country.

Kensuke IkenakaDepartment of Neurology, Graduate School of Medicine, Osaka University, Osaka, Japan.
Mari SuzukiDepartment of Neurotherapeutics, Graduate School of Medicine, Osaka University, Osaka, Japan.
Hideki MochizukiDepartment of Neurology, Graduate School of Medicine, Osaka University, Osaka, Japan.
Yoshitaka NagaiDepartment of Neurology, Graduate School of Medicine, Osaka University, Osaka, Japan.
Osaka University · JPTokyo Metropolitan Institute of Medical Science · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Aggregation of α-synuclein (αSyn) plays a central role in the pathogenesis of Parkinson's disease (PD) and dementia with Lewy bodies (DLB). Lewy bodies (LBs) and Lewy neurites, which consist mainly of aggregated αSyn, are widely observed in the affected regions of patient brains. Except for some familial forms of PD/DLB, most sporadic PD/DLB patients express the wild-type (WT) αSyn protein without any mutations, and the mechanisms as to how WT αSyn gains the propensity to pathologically aggregate still remains unclear. Furthermore, the mechanisms by which the same αSyn protein can cause different synucleinopathies with distinct phenotypes and pathologies, such as PD, DLB, and multiple system atrophy (MSA), still remain largely unknown. Recently, mutations in the

Indexed as

fibrillipidParkinson’s diseasesynucleinopathyα-synuclein

Identifiers

PMID31333408
PMCPMC6619337
OpenAlexW2949242126

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.