Evidence map›Paper›PMID 22009743›Full record

ArticleThe Journal of biological chemistry2011

The composition of plant mitochondrial supercomplexes changes with oxygen availability.

Santiago J Ramírez-Aguilar, Mandy Keuthe, Marcio Rocha, Vadim V Fedyaev, Katharina Kramp, Kapuganti J Gupta, Allan G Rasmusson, Waltraud X Schulze, Joost T van Dongen

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

39 citing papers in PubMed, 93 citations in OpenAlex.

  1. Article
  2. Review
  3. Comparative mitogenomics ofFrontiers in plant science · 2026
    Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Research journey of respirasome.Protein & cell · 2020
    Review
  15. Review
  16. Review
  17. Article
  18. Oxidative stress is tightly regulated by cytochromeProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  19. Respiratory chain supercomplexes: Structures, function and biogenesis.Seminars in cell & developmental biology · 2018
    Review
  20. Review
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 3 institutions in 3 countries.

Santiago J Ramírez-AguilarMax Planck Institute of Molecular Plant Physiology, Energy Metabolism Research Group, Am Mühlenberg 1, D-14476, Potsdam, Germany.
Mandy Keuthe
Marcio Rocha
Vadim V Fedyaev
Katharina Kramp
Kapuganti J Gupta
Allan G Rasmusson
Waltraud X Schulze
Joost T van Dongen
Max Planck Institute of Molecular Plant Physiology · DEBashkir State University · RULund University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Respiratory supercomplexes are large protein structures formed by various enzyme complexes of the mitochondrial electron transport chain. Using native gel electrophoresis and activity staining, differential regulation of complex activity within the supercomplexes was investigated. During prolonged hypoxia, complex I activity within supercomplexes diminished, whereas the activity of the individual complex I-monomer increased. Concomitantly, an increased activity was observed during hypoxia for complex IV in the smaller supercomplexes that do not contain complex I. These changes in complex activity within supercomplexes reverted again during recovery from the hypoxic treatment. Acidification of the mitochondrial matrix induced similar changes in complex activity within the supercomplexes. It is suggested that the increased activity of the small supercomplex III(2)+IV can be explained by the dissociation of complex I from the large supercomplexes. This is discussed to be part of a mechanism regulating the involvement of the alternative NADH dehydrogenases, known to be activated by low pH, and complex I, which is inhibited by low pH. It is concluded that the activity of complexes within supercomplexes can be regulated depending on the oxygen status and the pH of the mitochondrial matrix.

Indexed as

Cell HypoxiaElectron Transport Complex IElectron Transport Complex IVHydrogen-Ion ConcentrationMembrane Potential, MitochondrialMitochondriaMultienzyme ComplexesPlant ProteinsPlantsSolanum tuberosumTandem Mass SpectrometryElectron Transport Complex IElectron Transport Complex IVMultienzyme ComplexesPlant Proteins

Identifiers

PMID22009743
PMCPMC3234806
OpenAlexW2047695085

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.