Cryo-EM analysis of V/A-ATPase intermediates reveals the transition of the ground-state structure to steady-state structures by sequential ATP binding.

Atsuko Nakanishi, Jun-Ichi Kishikawa, Kaoru Mitsuoka, Ken Yokoyama

Abstract read

In one paragraph

Article in The Journal of biological chemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it

0cells of the map it votes in

3citing papers in PubMed

–field-weighted citation impact

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

3 citing papers in PubMed.

Structures of rotary ATP synthase fromScience advances · 2025
Article
Preparation of oxygen-sensitive proteins for high-resolution cryoEM structure determination using blot-free vitrification.Nature communications · 2025
Article
Rotary mechanism of the prokaryotic VNature communications · 2024
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

4 authors.

Atsuko NakanishiDepartment of Molecular Biosciences, Kyoto Sangyo University, Kamigamo-Motoyama, Kita-ku, Kyoto, Japan; Research Center for Ultra-High Voltage Electron Microscopy, Osaka University, Osaka, Japan.

Jun-Ichi KishikawaDepartment of Molecular Biosciences, Kyoto Sangyo University, Kamigamo-Motoyama, Kita-ku, Kyoto, Japan; Institute for Protein Research, Osaka University, Osaka Japan.

Kaoru MitsuokaResearch Center for Ultra-High Voltage Electron Microscopy, Osaka University, Osaka, Japan.

Ken YokoyamaDepartment of Molecular Biosciences, Kyoto Sangyo University, Kamigamo-Motoyama, Kita-ku, Kyoto, Japan. Electronic address: yokoken@cc.kyoto-su.ac.jp.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Vacuolar/archaeal-type ATPase (V/A-ATPase) is a rotary ATPase that shares a common rotary catalytic mechanism with F

Indexed as

Adenosine TriphosphateVacuolar Proton-Translocating ATPasesCatalytic DomainCryoelectron MicroscopyEnzyme ActivationProtein ConformationAdenosine TriphosphateVacuolar Proton-Translocating ATPasesATPaseATP synthasecryo-electron microscopyenzyme mechanismH(+)-ATPasemolecular motorsingle particle analysisstructure-functionvacuolar ATPase

Identifiers

PMID36626983

DOI10.1016/j.jbc.2023.102884

PMCPMC9971907

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.