Evidence map›Paper›PMID 33243981›Full record

ArticleNature communications2020

Essential role of accessory subunit LYRM6 in the mechanism of mitochondrial complex I.

Etienne Galemou Yoga, Kristian Parey, Amina Djurabekova, Outi Haapanen, Karin Siegmund, Klaus Zwicker, Vivek Sharma, Volker Zickermann, Heike Angerer

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.4field-weighted citation impact, top 10% 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

30 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
  2. Molecular and energetic basis of histidine switch dynamics in respiratory complex I.Protein science : a publication of the Protein Society · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Respiratory complex IIIbioRxiv : the preprint server for biology · 2025
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Using cryo-EM to understand the assembly pathway of respiratory complex I.Acta crystallographica. Section D, Structural biology · 2024
    Article
  15. Article
  16. Article
  17. Article
  18. Review
  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

9 authors at 2 institutions in 2 countries.

Etienne Galemou YogaMedical School, Institute of Biochemistry II, Structural Bioenergetics Group, Goethe University, Max von Laue Str. 9, 60438, Frankfurt am Main, Germany.
Kristian PareyMedical School, Institute of Biochemistry II, Structural Bioenergetics Group, Goethe University, Max von Laue Str. 9, 60438, Frankfurt am Main, Germany.
Amina DjurabekovaDepartment of Physics, P.O. Box 64, University of Helsinki, FI-00014, Helsinki, Finland.
Outi HaapanenDepartment of Physics, P.O. Box 64, University of Helsinki, FI-00014, Helsinki, Finland.ORCID 0000-0002-1958-8997
Karin SiegmundMedical School, Institute of Biochemistry II, Structural Bioenergetics Group, Goethe University, Max von Laue Str. 9, 60438, Frankfurt am Main, Germany.
Klaus ZwickerMedical School, Institute of Biochemistry I, Goethe University, Theodor-Stern-Kai 7, 60590, Frankfurt am Main, Germany.ORCID 0000-0003-2155-024X
Vivek SharmaDepartment of Physics, P.O. Box 64, University of Helsinki, FI-00014, Helsinki, Finland. vivek.sharma@helsinki.fi.ORCID 0000-0002-8838-3151
Volker ZickermannMedical School, Institute of Biochemistry II, Structural Bioenergetics Group, Goethe University, Max von Laue Str. 9, 60438, Frankfurt am Main, Germany.ORCID 0000-0001-8461-8817
Heike AngererMedical School, Institute of Biochemistry II, Structural Bioenergetics Group, Goethe University, Max von Laue Str. 9, 60438, Frankfurt am Main, Germany. Angerer@em.uni-frankfurt.de.ORCID 0000-0002-8566-5882
Goethe University Frankfurt · DEUniversity of Helsinki · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Respiratory complex I catalyzes electron transfer from NADH to ubiquinone (Q) coupled to vectorial proton translocation across the inner mitochondrial membrane. Despite recent progress in structure determination of this very large membrane protein complex, the coupling mechanism is a matter of ongoing debate and the function of accessory subunits surrounding the canonical core subunits is essentially unknown. Concerted rearrangements within a cluster of conserved loops of central subunits NDUFS2 (β1-β2

Indexed as

Electron Transport Complex IFungal ProteinsMutagenesis, Site-DirectedOxidation-ReductionProtein SubunitsProtonsUbiquinoneYarrowiaElectron Transport Complex IFungal ProteinsProtein SubunitsProtonsUbiquinone

Identifiers

PMID33243981
PMCPMC7693276
OpenAlexW3108184731

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.