Evidence map›Paper›PMID 21711245›Full record

ArticleThe Biochemical journal2011

Why does mitochondrial complex I have so many subunits?

Judy Hirst

Abstract readComment
PubMed Publisher
In one paragraph

Article in The Biochemical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.5field-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

23 citing papers in PubMed, 45 citations in OpenAlex.

  1. Global conformations ofScience advances · 2025
    Article
  2. Review
  3. The coupling mechanism of mammalian mitochondrial complex I.Nature structural & molecular biology · 2022
    Article
  4. Article
  5. Article
  6. Cytonuclear integration and co-evolution.Nature reviews. Genetics · 2018
    Review
  7. Coenzyme QEssays in biochemistry · 2018
    Review
  8. Review
  9. Article
  10. Structure of subcomplex Iβ of mammalian respiratory complex I leads to new supernumerary subunit assignments.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. Review
  16. Review
  17. Article
  18. Review
  19. Assembly factors for the membrane arm of human complex I.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

1 author at 1 institution in 1 country.

Judy HirstMedical Research Council Mitochondrial Biology Unit, Wellcome Trust/MRC Building, Cambridge, UK. jh@mrc-mbu.cam.ac.uk
MRC Mitochondrial Biology Unit · GB

Funding

Medical Research Council MC_U105663141
6 · The paper itself

Abstract

The prokaryotic and eukaryotic homologues of complex I (proton-pumping NADH:quinone oxidoreductase) perform the same function in energy transduction, but the eukaryotic enzymes are twice as big as their prokaryotic cousins, and comprise three times as many subunits. Fourteen core subunits are conserved in all complexes I, and are sufficient for catalysis - so why are the eukaryotic enzymes embellished by so many supernumerary or accessory subunits? In this issue of the Biochemical Journal, Angerer et al. have provided new evidence to suggest that the supernumerary subunits are important for enzyme stability. This commentary aims to put this suggestion into context.

Indexed as

AnimalsCattleElectron Transport Complex IEnzyme StabilityEukaryotic CellsMitochondria, HeartProkaryotic CellsProtein SubunitsElectron Transport Complex IProtein Subunits

Identifiers

PMID21711245
OpenAlexW2119402541

What OpenQuestion holds

Textmetadata
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.