Evidence map›Paper›PMID 35589726›Full record

ArticleNature communications2022

Cryo-EM structures define ubiquinone-10 binding to mitochondrial complex I and conformational transitions accompanying Q-site occupancy.

Injae Chung, John J Wright, Hannah R Bridges, Bozhidar S Ivanov, Olivier Biner, Caroline S Pereira, Guilherme M Arantes, Judy Hirst

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
6.9field-weighted citation impact, top 2% 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

48 citing papers in PubMed, 83 citations in OpenAlex.

  1. Article
  2. Distinct ubiquinone binding at the oxidation and reduction sites of cytochrome bcProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Hydration-Controlled Proton Transport in Respiratory Complex I.Journal of the American Chemical Society · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Global conformations ofScience advances · 2025
    Article
  11. Article
  12. Flexibility and Hydration of the QJournal of chemical information and modeling · 2025
    Article
  13. Respiratory complex I-mediated NADMolecular oncology · 2025
    Article
  14. Review
  15. Redox-Activated Proton Transfer through a Redundant Network in the QJournal of chemical information and modeling · 2025
    Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. 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

8 authors at 3 institutions in 3 countries.

Injae ChungMRC Mitochondrial Biology Unit, University of Cambridge, The Keith Peters Building, Cambridge Biomedical Campus, Hills Road, Cambridge, CB2 0XY, UK.ORCID 0000-0002-2902-4677
John J Wright *MRC Mitochondrial Biology Unit, University of Cambridge, The Keith Peters Building, Cambridge Biomedical Campus, Hills Road, Cambridge, CB2 0XY, UK.ORCID 0000-0001-8987-4449
Hannah R Bridges *MRC Mitochondrial Biology Unit, University of Cambridge, The Keith Peters Building, Cambridge Biomedical Campus, Hills Road, Cambridge, CB2 0XY, UK.ORCID 0000-0001-6890-6050
Bozhidar S Ivanov *MRC Mitochondrial Biology Unit, University of Cambridge, The Keith Peters Building, Cambridge Biomedical Campus, Hills Road, Cambridge, CB2 0XY, UK.
Olivier BinerMRC Mitochondrial Biology Unit, University of Cambridge, The Keith Peters Building, Cambridge Biomedical Campus, Hills Road, Cambridge, CB2 0XY, UK.
Caroline S PereiraDepartment of Biochemistry, Instituto de Química, Universidade de São Paulo, Av. Prof. Lineu Prestes 748, São Paulo, SP, 05508-900, Brazil.ORCID 0000-0002-0248-0883
Guilherme M ArantesDepartment of Biochemistry, Instituto de Química, Universidade de São Paulo, Av. Prof. Lineu Prestes 748, São Paulo, SP, 05508-900, Brazil.ORCID 0000-0001-5356-7703
Judy HirstMRC Mitochondrial Biology Unit, University of Cambridge, The Keith Peters Building, Cambridge Biomedical Campus, Hills Road, Cambridge, CB2 0XY, UK. jh@mrc-mbu.cam.ac.uk.ORCID 0000-0001-8667-6797
University of Cambridge · GBUniversidade de São Paulo · BRUniversity of Zurich · CH

Funding

Medical Research Council MC_UU_00015/2Medical Research Council MC_UU_00028/1
6 · The paper itself

Abstract

Mitochondrial complex I is a central metabolic enzyme that uses the reducing potential of NADH to reduce ubiquinone-10 (Q

Indexed as

Electron Transport Complex IUbiquinoneAnimalsBinding SitesCryoelectron MicroscopyMammalsMitochondrial MembranesOxidation-ReductionElectron Transport Complex IUbiquinone

Identifiers

PMID35589726
PMCPMC9120487
OpenAlexW4280633713

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.