Evidence map›Paper›PMID 23864498›Full record

ReviewJournal of the Royal Society, Interface2013

Functions of the hydrophilic channels in protonmotive cytochrome c oxidase.

Peter R Rich, Amandine Maréchal

Open access · bronzeAbstract readReview
In one paragraph

Review in Journal of the Royal Society, Interface, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
4.3field-weighted citation impact, top 5% 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

42 citing papers in PubMed, 94 citations in OpenAlex.

  1. Review
  2. Coupling between electrons' spin and proton transfer in chiral biological crystals.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Structural and functional mechanisms of cytochrome c oxidase.Journal of inorganic biochemistry · 2025
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Structural basis of mammalian complex IV inhibition by steroids.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  11. Structures ofScience (New York, N.Y.) · 2022
    Article
  12. Functional Dynamics of an Ancient Membrane-Bound Hydrogenase.Journal of the American Chemical Society · 2021
    Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. A common coupling mechanism for A-type heme-copper oxidases from bacteria to mitochondria.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  19. Article
  20. Snapshot of an oxygen intermediate in the catalytic reaction of cytochromeProceedings of the National Academy of Sciences of the United States of America · 2019
    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

2 authors at 1 institution in 1 country.

Peter R RichGlynn Laboratory of Bioenergetics, Institute of Structural and Molecular Biology, University College London, Gower Street, London WC1E 6BT, UK. prr@ucl.ac.uk
Amandine Maréchal
University College London · GB

Funding

Biotechnology and Biological Sciences Research Council BB/C50747X/1Biotechnology and Biological Sciences Research Council BB/K001094/1
6 · The paper itself

Abstract

The structures and functions of hydrophilic channels in electron-transferring membrane proteins are discussed. A distinction is made between proton channels that can conduct protons and dielectric channels that are non-conducting but can dielectrically polarize in response to the introduction of charge changes in buried functional centres. Functions of the K, D and H channels found in A1-type cytochrome c oxidases are reviewed in relation to these ideas. Possible control of function by dielectric channels and their evolutionary relation to proton channels is explored.

Indexed as

Evolution, MolecularAnimalsElectron Transport Complex IVHumansProton-Motive ForceElectron Transport Complex IVcharge transferdielectric propertieselectrostaticshydrophilic channelsproton transferredox proteins

Identifiers

PMID23864498
PMCPMC3730678
OpenAlexW2133179591

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.