Evidence map›Paper›PMID 31097622›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2019

Increased Lysosomal Exocytosis Induced by Lysosomal Ca

Taiji Tsunemi, Tamara Perez-Rosello, Yuta Ishiguro, Asako Yoroisaka, Sohee Jeon, Kana Hamada, Malini Rammonhan, Yvette C Wong, Zhong Xie, Wado Akamatsu and 4 more

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 105 papers.

0numbers the graph read from it
0cells of the map it votes in
105citing papers in PubMed
11.9field-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

105 citing papers in PubMed, 157 citations in OpenAlex.

  1. Article
  2. Biological psychiatry global open science · 2026
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  20. Rab27b Promotes Lysosomal Function and Alpha-Synuclein Clearance in Neurons.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2025
    Article

45 more citing papers are in PubMed but not listed here.

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

14 authors at 2 institutions in 2 countries.

Taiji TsunemiKen and Ruth Davee Department of Neurology, t-tsunemi@juntendo.ac.jp dkrainc@nm.org.
Tamara Perez-RoselloDepartment of Physiology, Northwestern University Feinberg School of Medicine, Chicago, Illinois 60611.
Yuta IshiguroDepartment of Neurology, and.
Asako YoroisakaDepartment of Neurology, and.
Sohee JeonKen and Ruth Davee Department of Neurology.
Kana HamadaKen and Ruth Davee Department of Neurology.
Malini RammonhanKen and Ruth Davee Department of Neurology.
Yvette C WongKen and Ruth Davee Department of Neurology.
Zhong XieDepartment of Physiology, Northwestern University Feinberg School of Medicine, Chicago, Illinois 60611.
Wado AkamatsuCenter for Genomic and Regenerative Medicine, Juntendo University School of Medicine, Tokyo 113-8421, Japan.
Joseph R MazzulliKen and Ruth Davee Department of Neurology.
D James SurmeierDepartment of Physiology, Northwestern University Feinberg School of Medicine, Chicago, Illinois 60611.
Nobutaka HattoriDepartment of Neurology, and.ORCID 0000-0002-2034-2556
Dimitri KraincKen and Ruth Davee Department of Neurology, t-tsunemi@juntendo.ac.jp dkrainc@nm.org.
Juntendo University · JPNorthwestern University · US

Funding

The role of ATP13A2/PARK9 in secretion of exosomes and alpha synucleinR37NS096241 · NINDS · NORTHWESTERN UNIVERSITY AT CHICAGO · PI KRAINC, DIMITRI · 2016 to 2020
$3.1M
NINDS NIH HHS R37 NS096241
6 · The paper itself

Abstract

The accumulation of misfolded proteins is a common pathological feature of many neurodegenerative disorders, including synucleinopathies such as Parkinson's disease (PD), which is characterized by the presence of α-synuclein (α-syn)-containing Lewy bodies. However, although recent studies have investigated α-syn accumulation and propagation in neurons, the molecular mechanisms underlying α-syn transmission have been largely unexplored. Here, we examined a monogenic form of synucleinopathy caused by loss-of-function mutations in lysosomal ATP13A2/PARK9. These studies revealed that lysosomal exocytosis regulates intracellular levels of α-syn in human neurons. Loss of PARK9 function in patient-derived dopaminergic neurons disrupted lysosomal Ca

Indexed as

alpha-SynucleinCalcium Channel AgonistsCell Line, TumorCells, CulturedDopaminergic NeuronsExocytosisHumansInduced Pluripotent Stem CellsLysosomesProton-Translocating ATPasesalpha-SynucleinATP13A2 protein, humanCalcium Channel AgonistsProton-Translocating ATPasesalpha synucleindopaminergic neuronKufor–Rakeb syndromelysosomal exocytosisParkinson's diseaseTRPML1

Identifiers

PMID31097622
PMCPMC6636071
OpenAlexW2944833260

What OpenQuestion holds

Textmetadata
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.