Evidence map›Paper›PMID 36939875›Full record

ArticleActa neuropathologica2023

Phosphatidylinositol-3,4,5-trisphosphate interacts with alpha-synuclein and initiates its aggregation and formation of Parkinson's disease-related fibril polymorphism.

Chi-Jing Choong, César Aguirre, Keita Kakuda, Goichi Beck, Hiroki Nakanishi, Yasuyoshi Kimura, Shuichi Shimma, Kei Nabekura, Makoto Hideshima, Junko Doi and 15 more

Open access · hybridAbstract read
In one paragraph

Article in Acta neuropathologica, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
4.9field-weighted citation impact, top 4% 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

15 citing papers in PubMed, 25 citations in OpenAlex.

  1. Nanoscale CabioRxiv : the preprint server for biology · 2026
    Article
  2. Review
  3. Article
  4. Genetic Sketch of Parkinson's Disease in India.Annals of Indian Academy of Neurology · 2025
    Article
  5. Article
  6. Review
  7. Article
  8. Role of Lipids in the Pathogenesis of Parkinson's Disease.International journal of molecular sciences · 2024
    Review
  9. Review
  10. Article
  11. Article
  12. Review
  13. Mechanisms and pathology of protein misfolding and aggregation.Nature reviews. Molecular cell biology · 2023
    Review
  14. Article
  15. 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

25 authors at 3 institutions in 2 countries.

Chi-Jing Choong *Department of Neurology, Osaka University Graduate School of Medicine, 2-2 Yamadaoka, Suita, Osaka, 565-0871, Japan.
César Aguirre *Department of Neurology, Osaka University Graduate School of Medicine, 2-2 Yamadaoka, Suita, Osaka, 565-0871, Japan.
Keita Kakuda *Department of Neurology, Osaka University Graduate School of Medicine, 2-2 Yamadaoka, Suita, Osaka, 565-0871, Japan.
Goichi BeckDepartment of Neurology, Osaka University Graduate School of Medicine, 2-2 Yamadaoka, Suita, Osaka, 565-0871, Japan.
Hiroki NakanishiLipidome Lab Co., Ltd, Akita-City, Akita, 010-0825, Japan.
Yasuyoshi KimuraDepartment of Neurology, Osaka University Graduate School of Medicine, 2-2 Yamadaoka, Suita, Osaka, 565-0871, Japan.
Shuichi ShimmaDepartment of Biotechnology, Graduate School of Engineering, Osaka University, 2-1 Yamadaoka, Suita, Osaka, 565-0871, Japan.
Kei NabekuraDepartment of Neurology, Osaka University Graduate School of Medicine, 2-2 Yamadaoka, Suita, Osaka, 565-0871, Japan.
Makoto HideshimaDepartment of Neurology, Osaka University Graduate School of Medicine, 2-2 Yamadaoka, Suita, Osaka, 565-0871, Japan.
Junko DoiDepartment of Neurology, Osaka University Graduate School of Medicine, 2-2 Yamadaoka, Suita, Osaka, 565-0871, Japan.
Keiichi YamaguchiGlobal Center for Medical Engineering and Informatics, Osaka University, 2-1 Yamadaoka, Suita, Osaka, 565-0871, Japan.
Kichitaro NakajimaGlobal Center for Medical Engineering and Informatics, Osaka University, 2-1 Yamadaoka, Suita, Osaka, 565-0871, Japan.
Tomoya WadayamaDepartment of Neurology, Osaka University Graduate School of Medicine, 2-2 Yamadaoka, Suita, Osaka, 565-0871, Japan.
Hideki HayakawaDepartment of Neurology, Osaka University Graduate School of Medicine, 2-2 Yamadaoka, Suita, Osaka, 565-0871, Japan.
Kousuke BabaDepartment of Neurology, Osaka University Graduate School of Medicine, 2-2 Yamadaoka, Suita, Osaka, 565-0871, Japan.
Kotaro OgawaDepartment of Neurology, Osaka University Graduate School of Medicine, 2-2 Yamadaoka, Suita, Osaka, 565-0871, Japan.
Toshihide TakeuchiDepartment of Neurology, Kindai University, 3-4-1 Kowakae, Higashiosaka City, Osaka, 577-8502, Japan.
Shaymaa Mohamed Mohamed BadawyDepartment of Neurology, Osaka University Graduate School of Medicine, 2-2 Yamadaoka, Suita, Osaka, 565-0871, Japan.
Shigeo MurayamaBrain Bank for Neurodevelopmental, Neurological and Psychiatric Disorders, United Graduate School of Child Development, Osaka University, 2-2 Yamadaoka, Suita, Osaka, 565-0871, Japan.
Seiichi NaganoDepartment of Neurology, Osaka University Graduate School of Medicine, 2-2 Yamadaoka, Suita, Osaka, 565-0871, Japan.
Yuji GotoGlobal Center for Medical Engineering and Informatics, Osaka University, 2-1 Yamadaoka, Suita, Osaka, 565-0871, Japan.
Yohei MiyanoiriInstitute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka, 565-0871, Japan.
Yoshitaka NagaiDepartment of Neurology, Kindai University, 3-4-1 Kowakae, Higashiosaka City, Osaka, 577-8502, Japan.
Hideki Mochizuki *Department of Neurology, Osaka University Graduate School of Medicine, 2-2 Yamadaoka, Suita, Osaka, 565-0871, Japan. hmochizuki@neurol.med.osaka-u.ac.jp.
Kensuke Ikenaka *Department of Neurology, Osaka University Graduate School of Medicine, 2-2 Yamadaoka, Suita, Osaka, 565-0871, Japan. ikenaka@neurol.med.osaka-u.ac.jp.ORCID 0000-0002-5559-1966
The University of Osaka · JPKindai University · JPZagazig University · EG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lipid interaction with α-synuclein (αSyn) has been long implicated in the pathogenesis of Parkinson's disease (PD). However, it has not been fully determined which lipids are involved in the initiation of αSyn aggregation in PD. Here exploiting genetic understanding associating the loss-of-function mutation in Synaptojanin 1 (SYNJ1), a phosphoinositide phosphatase, with familial PD and analysis of postmortem PD brains, we identified a novel lipid molecule involved in the toxic conversion of αSyn and its relation to PD. We first established a SYNJ1 knockout cell model and found SYNJ1 depletion increases the accumulation of pathological αSyn. Lipidomic analysis revealed SYNJ1 depletion elevates the level of its substrate phosphatidylinositol-3,4,5-trisphosphate (PIP

Indexed as

Parkinson Diseasealpha-SynucleinBrainHumansLipidsNeuronsPhosphatidylinositol Phosphatesalpha-SynucleinLipidsPhosphatidylinositol PhosphatesAlpha-synucleinParkinson’s diseasePhosphatidylinositol-3,4,5-trisphosphateSynaptojanin 1

Identifiers

PMID36939875
PMCPMC10119223
OpenAlexW4327900048

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.