Evidence map›Paper›PMID 32393395›Full record

ReviewTranslational neurodegeneration2020

The emerging roles of vacuolar-type ATPase-dependent Lysosomal acidification in neurodegenerative diseases.

Qiaoyun Song, Bo Meng, Haidong Xu, Zixu Mao

Open access · goldAbstract readReview
In one paragraph

Review in Translational neurodegeneration, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 116 papers, 3 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
116citing papers in PubMed, 3 pooled it
10.6field-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

116 citing papers in PubMed, 3 syntheses or guidelines pooled it, 220 citations in OpenAlex.

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56 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

4 authors at 1 institution in 2 countries.

Qiaoyun SongDepartment of Pharmacology and Chemical Biology, Emory University School of Medicine, Atlanta, GA, 30322, USA.
Bo MengDepartment of Pharmacology and Chemical Biology, Emory University School of Medicine, Atlanta, GA, 30322, USA.
Haidong XuDepartment of Pharmacology and Chemical Biology, Emory University School of Medicine, Atlanta, GA, 30322, USA.
Zixu MaoDepartment of Pharmacology and Chemical Biology, Emory University School of Medicine, Atlanta, GA, 30322, USA. zmao@emory.edu.ORCID 0000-0001-9883-9231
Emory University · US

Funding

Chaperone-mediated Autophagy and Synaptic Dysfunction in Parkinson's DiseaseR01NS107505 · NINDS · EMORY UNIVERSITY · PI MAO, ZIXU, WEN, ZHEXING · 2018 to 2022
$2.5M
The Role of Drosha in the Pathogenesis of Alzheimer's DiseaseR01NS095269 · NINDS · EMORY UNIVERSITY · PI MAO, ZIXU · 2016 to 2020
$2.4M
NIH HHS R01NS095269NIH HHS R01NS107505
6 · The paper itself

Abstract

backgroundLysosomes digest extracellular material from the endocytic pathway and intracellular material from the autophagic pathway. This process is performed by the resident hydrolytic enzymes activated by the highly acidic pH within the lysosomal lumen. Lysosome pH gradients are mainly maintained by the vacuolar (H MAIN BODY: As a large multi-subunit complex, the V-ATPase is composed of an integral membrane V0 domain involved in proton translocation and a peripheral V1 domain catalyzing ATP hydrolysis. The canonical functions of V-ATPase rely on its H

conclusionV-ATPase complex is a universal proton pump and plays an important role in lysosome acidification in all types of cells. Since V-ATPase dysfunction contributes to the pathogenesis of multiple neurodegenerative diseases, further understanding the mechanisms that regulate the canonical and non-canonical functions of V-ATPase will reveal molecular details of disease process and help assess V-ATPase or molecules related to its regulation as therapeutic targets.

Indexed as

HumansHydrogen-Ion ConcentrationLysosomal Storage DiseasesLysosomesNeurodegenerative DiseasesVacuolar Proton-Translocating ATPasesVacuolesVacuolar Proton-Translocating ATPasesAutophagyLysosomal acidificationNeurodegenerationVacuolar-type ATPase

Identifiers

PMID32393395
PMCPMC7212675
OpenAlexW3027286818

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.