The Human Mutation K237_V238del in a Putative Lipid Binding Motif within the V-ATPase a2 Isoform Suggests a Molecular Mechanism Underlying Cutis Laxa.

Anh Chu, Yeqi Yao, Miroslawa Glibowicka, Charles M Deber, Morris F Manolson

Open access · goldAbstract read

In one paragraph

Article in International journal of molecular sciences, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it

0cells of the map it votes in

1citing papers in PubMed

0.5field-weighted citation impact, top 39% 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

1 citing paper in PubMed, 2 citations in OpenAlex.

Control of Golgi- V-ATPase through Sac1-dependent co-regulation of PI(4)P and cholesterol.Nature communications · 2025
Article

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

5 authors at 2 institutions in 1 country.

Anh ChuFaculty of Dentistry, University of Toronto, Toronto M5G 1G6, ON, Canada.

Yeqi YaoFaculty of Dentistry, University of Toronto, Toronto M5G 1G6, ON, Canada.

Miroslawa GlibowickaDivision of Molecular Medicine, Research Institute, Hospital for Sick Children, Toronto M5G 0A4, ON, Canada.

Charles M DeberDivision of Molecular Medicine, Research Institute, Hospital for Sick Children, Toronto M5G 0A4, ON, Canada.

Morris F ManolsonFaculty of Dentistry, University of Toronto, Toronto M5G 1G6, ON, Canada.ORCID 0000-0001-8755-5460

University of Toronto · CAHospital for Sick Children · CA

Funding

CIHR 376666CIHR PJT-14850

6 · The paper itself

Abstract

Vacuolar ATPases (V-ATPases), proton pumps composed of 16 subunits, are necessary for a variety of cellular functions. Subunit "a" has four isoforms, a1-a4, each with a distinct cellular location. We identified a phosphoinositide (PIP) interaction motif, KX

Indexed as

Cutis LaxaVacuolar Proton-Translocating ATPasesHEK293 CellsHumansMutationProtein IsoformsProtein IsoformsVacuolar Proton-Translocating ATPasescutis laxaphosphoinositidesPI(4)Pprotein–lipid interactionV-ATPase a2 isoformsV-ATPases

Identifiers

PMID38396846

DOI10.3390/ijms25042170

PMCPMC10889665

OpenAlexW4391752588

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.