Evidence map›Paper›PMID 39660833›Full record

ArticleProtein science : a publication of the Protein Society2025

Effects of allosteric effectors on oxygen binding to crystals of hemoglobin in the R-quaternary structure.

Naoya Shibayama

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Review
  2. 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

1 author.

Naoya ShibayamaDivision of Biophysics, Department of Physiology, Jichi Medical University, Shimotsuke, Tochigi, Japan.ORCID 0000-0002-2208-1126

Funding

Japan Society for the Promotion of Science 19K06601
6 · The paper itself

Abstract

Much is known about how allosteric effectors influence the equilibrium between the relaxed (R) and tense (T) states of hemoglobin (Hb), but little is known about how and to what extent the effectors lower the intrinsic O

Indexed as

HemoglobinsOxygenAllosteric RegulationAnimalsCrystallography, X-RayHorsesHumansModels, MolecularProtein BindingProtein Structure, QuaternaryHemoglobinsOxygenallosteric effectorhemoglobinhemoglobin crystalsmicrospectrophotometryoxygen affinitytwo‐state model

Identifiers

PMID39660833
PMCPMC11632842

What OpenQuestion holds

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LicenceCC BY-NC
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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.