Evidence map›Paper›PMID 31489376›Full record

ArticleScience advances2019

Dimeric structures of quinol-dependent nitric oxide reductases (qNORs) revealed by cryo-electron microscopy.

Chai C Gopalasingam, Rachel M Johnson, George N Chiduza, Takehiko Tosha, Masaki Yamamoto, Yoshitsugu Shiro, Svetlana V Antonyuk, Stephen P Muench, S Samar Hasnain

Open access · goldAbstract read
In one paragraph

Article in Science advances, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.9field-weighted citation impact, top 25% 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

11 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Insertion of the FeFEBS letters · 2025
    Article
  5. Diversity and evolution of nitric oxide reduction in bacteria and archaea.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  6. Article
  7. Review
  8. The accuracy of protein models automatically built into cryo-EM maps with ARP/wARP.Acta crystallographica. Section D, Structural biology · 2021
    Article
  9. Article
  10. Article
  11. 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

9 authors at 4 institutions in 2 countries.

Chai C GopalasingamMolecular Biophysics Group, Institute of Integrative Biology, Faculty of Health and Life Sciences, University of Liverpool, Liverpool L69 7ZB, UK.ORCID 0000-0002-9014-9380
Rachel M JohnsonSchool of Biomedical Sciences, Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, UK.ORCID 0000-0002-5363-837X
George N ChiduzaMolecular Biophysics Group, Institute of Integrative Biology, Faculty of Health and Life Sciences, University of Liverpool, Liverpool L69 7ZB, UK.ORCID 0000-0003-1037-5749
Takehiko ToshaRIKEN SPring-8 Center, 1-1-1 Kouto, Sayo, Hyogo 679-5148, Japan.ORCID 0000-0002-8971-0759
Masaki YamamotoRIKEN SPring-8 Center, 1-1-1 Kouto, Sayo, Hyogo 679-5148, Japan.ORCID 0000-0002-1311-1768
Yoshitsugu ShiroGraduate School of Life Science, University of Hyogo, 3-2-1 Kouto, Kamigori, Ako, Hyogo 678-1297, Japan.ORCID 0000-0003-0695-8327
Svetlana V AntonyukMolecular Biophysics Group, Institute of Integrative Biology, Faculty of Health and Life Sciences, University of Liverpool, Liverpool L69 7ZB, UK.ORCID 0000-0002-2779-9946
Stephen P MuenchSchool of Biomedical Sciences, Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, UK.ORCID 0000-0001-6869-4414
S Samar HasnainMolecular Biophysics Group, Institute of Integrative Biology, Faculty of Health and Life Sciences, University of Liverpool, Liverpool L69 7ZB, UK.ORCID 0000-0002-2854-4718
University of Liverpool · GBSPring-8 · JPUniversity of Leeds · GBUniversity of Hyogo · JP

Funding

Wellcome Trust
6 · The paper itself

Abstract

Quinol-dependent nitric oxide reductases (qNORs) are membrane-integrated, iron-containing enzymes of the denitrification pathway, which catalyze the reduction of nitric oxide (NO) to the major ozone destroying gas nitrous oxide (N

Indexed as

Bacterial ProteinsCatalytic DomainCryoelectron MicroscopyCytoplasmElectron Transport Complex IVEscherichia coliHydroquinonesNitric OxideOxidation-ReductionOxidoreductasesProtonsBacterial ProteinsElectron Transport Complex IVHydroquinonesNitric Oxidenitric-oxide reductaseOxidoreductasesProtons

Identifiers

PMID31489376
PMCPMC6713497
OpenAlexW2971265346

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.