Evidence map›Paper›PMID 37564404›Full record

ArticleChemical science2023

The H-NOX protein structure adapts to different mechanisms in sensors interacting with nitric oxide.

Byung-Kuk Yoo, Sergei G Kruglik, Jean-Christophe Lambry, Isabelle Lamarre, C S Raman, Pierre Nioche, Michel Negrerie

Open access · diamondAbstract read
In one paragraph

Article in Chemical science, 2023. 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
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

2 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  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

7 authors at 4 institutions in 2 countries.

Byung-Kuk YooLaboratoire d'Optique et Biosciences, INSERM U-1182, Ecole Polytechnique 91120 Palaiseau France michel.negrerie@polytechnique.edu.
Sergei G KruglikLaboratoire Jean Perrin, Institut de Biologie Paris-Seine, Sorbonne Université, CNRS 75005 Paris France.ORCID https://orcid.org/0000-0002-2945-3092
Jean-Christophe LambryLaboratoire d'Optique et Biosciences, INSERM U-1182, Ecole Polytechnique 91120 Palaiseau France michel.negrerie@polytechnique.edu.
Isabelle LamarreLaboratoire d'Optique et Biosciences, INSERM U-1182, Ecole Polytechnique 91120 Palaiseau France michel.negrerie@polytechnique.edu.
C S RamanDepartment of Pharmaceutical Sciences, School of Pharmacy, University of Maryland Baltimore Maryland 21201 USA.
Pierre NiocheEnvironmental Toxicity, Therapeutic Targets, Cellular Signaling and Biomarkers, UMR S1124, Centre Universitaire des Saints-Pères, Université Paris Descartes 75006 Paris France.
Michel NegrerieLaboratoire d'Optique et Biosciences, INSERM U-1182, Ecole Polytechnique 91120 Palaiseau France michel.negrerie@polytechnique.edu.ORCID https://orcid.org/0000-0001-9918-031X
École Polytechnique · FRCentre National de la Recherche Scientifique · FRDélégation Paris 5 · FRUniversity of Maryland, Baltimore · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Some classes of bacteria within phyla possess protein sensors identified as homologous to the heme domain of soluble guanylate cyclase, the mammalian NO-receptor. Named H-NOX domain (Heme-Nitric Oxide or OXygen-binding), their heme binds nitric oxide (NO) and O

Identifiers

PMID37564404
PMCPMC10411614
OpenAlexW4384211236

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.