Evidence map›Paper›PMID 40272121›Full record

ArticleThe FEBS journal2025

Identification of CO-binding modes in the Cu

Jiyoung Kang, Toru Matsuoka, Masaru Tateno

Abstract read
In one paragraph

Article in The FEBS journal, 2025. 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

3 authors.

Jiyoung KangDepartment of Scientific Computing, Pukyong National University, Busan, Korea.ORCID https://orcid.org/0000-0003-2893-1512
Toru MatsuokaGraduate School of Life Science, University of Hyogo, Ako-gun, Japan.
Masaru TatenoGraduate School of Life Science, University of Hyogo, Ako-gun, Japan.

Funding

Research Grant of Pukyong National University 202316080001
6 · The paper itself

Abstract

Cytochrome c oxidase (CcO) is the terminal enzyme of the electron-transfer system and reduces an oxygen molecule to two water molecules. The trigger of this reaction is the binding of an oxygen molecule to the binuclear center (BNC) comprising the Cu

Indexed as

Electron Transport Complex IVAnimalsCatalytic DomainCattleCrystallography, X-RayEnzyme StabilityModels, ChemicalThermodynamicsValineElectron Transport Complex IVValinecomputer simulationdensity functional theoryinfrared spectroscopytransition metal

Identifiers

PMID40272121
PMCPMC12326888

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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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.