Evidence map›Paper›PMID 39078560›Full record

ArticleTheory in biosciences = Theorie in den Biowissenschaften2024

2-Site versus 3-site models of ATP hydrolysis by F

Sunil Nath

Abstract read
PubMed Publisher
In one paragraph

Article in Theory in biosciences = Theorie in den Biowissenschaften, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

1 citing paper in PubMed.

  1. Symmetry breaking and mismatch in the torsional mechanism of ATP synthesis by FTheory in biosciences = Theorie in den Biowissenschaften · 2025
    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

1 author.

Sunil NathDepartment of Biochemical Engineering and Biotechnology, Indian Institute of Technology Delhi, Hauz Khas, New Delhi, 110016, India. sunath@iitd.ac.in.ORCID http://orcid.org/0000-0002-0362-069X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The F

Indexed as

Adenosine TriphosphateProton-Translocating ATPasesAlgorithmsBinding SitesCatalysisCatalytic DomainHydrolysisKineticsModels, MolecularRotationAdenosine TriphosphateProton-Translocating ATPases2-Site or bi-Site catalysis3-site or tri-site catalysisADP‒ATP exchangeATP synthesis and ATP hydrolysisBovine mitochondrial bMF1Boyer’s binding change mechanism of ATP synthesis/hydrolysisCombinatorial proofCombinatoricsConservation equationsConservation law/principleF1-ATPaseHuman mitochondrial hMF1Ligand displacement/substitutionMathematical constraintsMolecular mechanismNath’s torsional mechanism of ATP synthesis/hydrolysisRotationThermophilic bacterial TF1

Identifiers

PMID39078560

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.