Evidence map›Paper›PMID 15254384›Full record

ReviewJournal of bioenergetics and biomembranes2000

Stoichiometry of energy coupling by proton-translocating ATPases: a history of variability.

J J Tomashek, W S Brusilow

Abstract readHistorical ArticleReview
PubMed Publisher
In one paragraph

Review in Journal of bioenergetics and biomembranes, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.0field-weighted citation impact, top 26% 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

21 citing papers in PubMed, 69 citations in OpenAlex.

  1. Article
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  3. Review
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  11. Comparison of the H+/ATP ratios of the H+-ATP synthases from yeast and from chloroplast.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  12. Article
  13. Review
  14. Forward operation of adenine nucleotide translocase during F0F1-ATPase reversal: critical role of matrix substrate-level phosphorylation.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2010
    Article
  15. Article
  16. Article
  17. The thermodynamic H+/ATP ratios of the H+-ATPsynthases from chloroplasts and Escherichia coli.Proceedings of the National Academy of Sciences of the United States of America · 2008
    Article
  18. Article
  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

2 authors at 1 institution in 1 country.

J J TomashekWayne State University School of Medicine, Department of Biochemistry and Molecular Biology, Detroit, Michigan 48201, USA.
W S Brusilow
Wayne State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

One of the central energy-coupling reactions in living systems is the intraconversion of ATP with a transmembrane proton gradient, carried out by proton-translocating F- and V-type ATPases/synthases. These reversible enzymes can hydrolyze ATP and pump protons, or can use the energy of a transmembrane proton gradient to synthesize ATP from ADP and inorganic phosphate. The stoichiometry of these processes (H(+)/ATP, or coupling ratio) has been studied in many systems for many years, with no universally agreed upon solution. Recent discoveries concerning the structure of the ATPases, their assembly and the stoichiometry of their numerous subunits, particularly the proton-carrying proteolipid (subunit c) of the F(O) and V(0) sectors, have shed new light on this question and raise the possibility of variable coupling ratios modulated by variable proteolipid stoichiometries.

Indexed as

History, 20th CenturyOsmosisProtein SubunitsProton-Translocating ATPasesThermodynamicsProtein SubunitsProton-Translocating ATPases

Identifiers

PMID15254384
OpenAlexW154894623

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.