Evidence map›Paper›PMID 15250827›Full record

ArticleThe Biochemical journal2004

Structural organization of mitochondrial human complex I: role of the ND4 and ND5 mitochondria-encoded subunits and interaction with prohibitin.

Ingrid Bourges, Claire Ramus, Bénédicte Mousson de Camaret, Réjane Beugnot, Claire Remacle, Pierre Cardol, Götz Hofhaus, Jean-Paul Issartel

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

65 citing papers in PubMed, 133 citations in OpenAlex.

  1. Article
  2. Article
  3. Mitochondrial RNA in Inflammation.International journal of biological sciences · 2025
    Review
  4. Colonocyte keratins stabilize mitochondria and contribute to mitochondrial energy metabolism.American journal of physiology. Gastrointestinal and liver physiology · 2024
    Article
  5. Review
  6. Exploring Intrinsic Disorder in Human Synucleins and Associated Proteins.International journal of molecular sciences · 2024
    Article
  7. Article
  8. Article
  9. Prohibitions in the meta-inflammatory response: a review.Frontiers in molecular biosciences · 2024
    Review
  10. PRKAG2.2 is essential for FoxA1Science advances · 2023
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Prohibitin S-Nitrosylation Is Required for the Neuroprotective Effect of Nitric Oxide in Neuronal Cultures.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2020
    Article

5 more citing papers are in PubMed but not listed here.

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 5 institutions in 3 countries.

Ingrid BourgesUMR 5090 CNRS-DRDC, CEA Grenoble, 38054 Grenoble cedex 9, France.
Claire Ramus
Bénédicte Mousson de Camaret
Réjane Beugnot
Claire Remacle
Pierre Cardol
Götz Hofhaus
Jean-Paul Issartel
Commissariat à l'Énergie Atomique et aux Énergies Alternatives · FRUniversity of Liège · BECEA Grenoble · FRHeinrich Heine University Düsseldorf · DEHôpital Debrousse · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mitochondria-encoded ND (NADH dehydrogenase) subunits, as components of the hydrophobic part of complex I, are essential for NADH:ubiquinone oxidoreductase activity. Mutations or lack of expression of these subunits have significant pathogenic consequences in humans. However, the way these events affect complex I assembly is poorly documented. To understand the effects of particular mutations in ND subunits on complex I assembly, we studied four human cell lines: ND4 non-expressing cells, ND5 non-expressing cells, and rho degrees cells that do not express any ND subunits, in comparison with normal complex I control cells. In control cells, all the seven analysed nuclear-encoded complex I subunits were found to be attached to the mitochondrial inner membrane, except for the 24 kDa subunit, which was nearly equally partitioned between the membranes and the matrix. Absence of a single ND subunit, or even all the seven ND subunits, caused no major changes in the nuclear-encoded complex I subunit content of mitochondria. However, in cells lacking ND4 or ND5, very low amounts of 24 kDa subunit were found associated with the membranes, whereas most of the other nuclear-encoded subunits remained attached. In contrast, membrane association of most of the nuclear subunits was significantly reduced in the absence of all seven ND proteins. Immunopurification detected several subcomplexes. One of these, containing the 23, 30 and 49 kDa subunits, also contained prohibitin. This is the first description of prohibitin interaction with complex I subunits and suggests that this protein might play a role in the assembly or degradation of mitochondrial complex I.

Indexed as

Bone NeoplasmsCell Line, TumorChromatography, LiquidDNA, NeoplasmElectron Transport Complex IGenotypeHumansMass SpectrometryMitochondriaMitochondrial ProteinsNADH DehydrogenaseOsteosarcomaOxidative PhosphorylationProhibitinsProtein SubunitsRepressor ProteinsDNA, NeoplasmElectron Transport Complex IMitochondrial ProteinsMT-ND5 protein, humanNADH DehydrogenaseNADH dehydrogenase subunit 4ProhibitinsProtein SubunitsRepressor Proteins

Identifiers

PMID15250827
PMCPMC1133742
OpenAlexW2023026614

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.