Evidence map›Paper›PMID 36598799›Full record

ArticleMolecular biology of the cell2023

Chimeric a-subunit isoforms generate functional yeast V-ATPases with altered regulatory properties in vitro and in vivo.

Farzana Tuli, Patricia M Kane

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

4 citing papers in PubMed, 5 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. 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

2 authors at 1 institution in 1 country.

Farzana TuliDepartment of Biochemistry and Molecular Biology, SUNY Upstate Medical University, Syracuse, NY 13210.
Patricia M KaneDepartment of Biochemistry and Molecular Biology, SUNY Upstate Medical University, Syracuse, NY 13210.
SUNY Upstate Medical University · US

Funding

Regulation and Cellular Functions of V-ATPasesR35GM145256 · NIGMS · UPSTATE MEDICAL UNIVERSITY · PI PATRICIA M KANE · 2022 to 2026
$2.9M
Regulation of V-ATPases by PhosphoinositidesR01GM126020 · NIGMS · UPSTATE MEDICAL UNIVERSITY · PI KANE, PATRICIA M · 2018 to 2021
$1.1M
NIGMS NIH HHS R01 GM126020NIGMS NIH HHS R35 GM145256
6 · The paper itself

Abstract

V-ATPases are highly regulated proton pumps that acidify organelles. The V-ATPase a-subunit is a two-domain protein containing a C-terminal transmembrane domain responsible for proton transport and an N-terminal cytosolic domain (aNT) that is a regulatory hub, integrating environmental inputs to regulate assembly, localization, and V-ATPase activity. The yeast

Indexed as

Saccharomyces cerevisiae ProteinsVacuolar Proton-Translocating ATPasesProtein IsoformsSaccharomyces cerevisiaeVacuolesProtein IsoformsSaccharomyces cerevisiae ProteinsVacuolar Proton-Translocating ATPases

Identifiers

PMID36598799
PMCPMC10011726
OpenAlexW4313482836

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.