Evidence map›Paper›PMID 41759743›Full record

ArticleThe Journal of biological chemistry2026

Structure of Acinetobacter baumannii cytochrome bo

Quan Li, Rui Hao, Jiapeng Zhu, Jiao Li

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Quan LiSchool of Medicine, Nanjing University of Chinese Medicine, Nanjing, China.
Rui HaoSchool of Medicine, Nanjing University of Chinese Medicine, Nanjing, China.
Jiapeng ZhuSchool of Medicine, Nanjing University of Chinese Medicine, Nanjing, China. Electronic address: zhujiapeng@hotmail.com.
Jiao LiSchool of Medicine, Nanjing University of Chinese Medicine, Nanjing, China. Electronic address: jiao.li@njucm.edu.cn.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Heme-copper oxidases (heme-copper oxidoreductases) are terminal oxidases that couple oxygen reduction to proton pumping for ATP synthesis. Although our previous work has elucidated the structure and proton transfer mechanism of the Escherichia coli cytochrome bo

Indexed as

Acinetobacter baumanniiCytochromesElectron Transport Complex IVCytochrome b GroupEscherichia coli ProteinsModels, MolecularOxidoreductasesProtein ConformationUbiquinoneCytochrome b Groupcytochrome bo3, E coliCytochromesElectron Transport Complex IVEscherichia coli ProteinsOxidoreductasesubiquinol oxidaseUbiquinoneAcinetobacter baumanniicryo-EMelectron transportheme–copper oxidoreductaseproton pumpubiquinone

Identifiers

PMID41759743
PMCPMC13022660

What OpenQuestion holds

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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.