Evidence map›Paper›PMID 37080960›Full record

ArticleNature communications2023

Parkinson's disease-associated ATP13A2/PARK9 functions as a lysosomal H

Takuto Fujii, Shushi Nagamori, Pattama Wiriyasermkul, Shizhou Zheng, Asaka Yago, Takahiro Shimizu, Yoshiaki Tabuchi, Tomoyuki Okumura, Tsutomu Fujii, Hiroshi Takeshima and 1 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
14.7field-weighted citation impact, top 1% 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

45 citing papers in PubMed, 57 citations in OpenAlex.

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  11. ATP13A2 restrains macrophage NLRP3 inflammasome activation to repress neurodegeneration via modulating mitochondrial homeostasis.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  15. Wild-typemedRxiv : the preprint server for health sciences · 2026
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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

11 authors at 3 institutions in 1 country.

Takuto FujiiDepartment of Pharmaceutical Physiology, Faculty of Pharmaceutical Sciences, University of Toyama, Toyama, 930-0194, Japan. fujiitk@pha.u-toyama.ac.jp.ORCID 0000-0002-0547-1691
Shushi NagamoriCenter for SI Medical Research and Department of Laboratory Medicine, The Jikei University School of Medicine, Tokyo, 105-8461, Japan.ORCID 0000-0003-0203-2754
Pattama WiriyasermkulCenter for SI Medical Research and Department of Laboratory Medicine, The Jikei University School of Medicine, Tokyo, 105-8461, Japan.ORCID 0000-0001-7068-7969
Shizhou ZhengDepartment of Pharmaceutical Physiology, Faculty of Pharmaceutical Sciences, University of Toyama, Toyama, 930-0194, Japan.
Asaka YagoDepartment of Pharmaceutical Physiology, Faculty of Pharmaceutical Sciences, University of Toyama, Toyama, 930-0194, Japan.
Takahiro ShimizuDepartment of Pharmaceutical Physiology, Faculty of Pharmaceutical Sciences, University of Toyama, Toyama, 930-0194, Japan.
Yoshiaki TabuchiDivision of Molecular Genetics Research, Life Science Research Center, University of Toyama, Toyama, 930-0194, Japan.ORCID 0000-0002-6007-6176
Tomoyuki OkumuraDepartment of Surgery and Science, Faculty of Medicine, University of Toyama, Toyama, 930-0194, Japan.
Tsutomu FujiiDepartment of Surgery and Science, Faculty of Medicine, University of Toyama, Toyama, 930-0194, Japan.ORCID 0000-0003-0625-1911
Hiroshi TakeshimaDepartment of Biological Chemistry, Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto, 606-8501, Japan.ORCID 0000-0003-4525-3725
Hideki SakaiDepartment of Pharmaceutical Physiology, Faculty of Pharmaceutical Sciences, University of Toyama, Toyama, 930-0194, Japan. sakaih@pha.u-toyama.ac.jp.ORCID 0000-0002-9753-7941
University of Toyama · JPJikei University School of Medicine · JPKyoto University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mutations in the human ATP13A2 (PARK9), a lysosomal ATPase, cause Kufor-Rakeb Syndrome, an early-onset form of Parkinson's disease (PD). Here, we demonstrate that ATP13A2 functions as a lysosomal H

Indexed as

Parkinson Diseasealpha-SynucleinH(+)-K(+)-Exchanging ATPaseHumansLysosomesMutationParkinsonian DisordersProton-Translocating ATPasesalpha-SynucleinATP13A2 protein, humanH(+)-K(+)-Exchanging ATPaseProton-Translocating ATPases

Identifiers

PMID37080960
PMCPMC10119128
OpenAlexW4366549724

What Socratic 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 Socratic graph.