Evidence map›Paper›PMID 26717487›Full record

ArticlePloS one2015

Cooperativity in Binding Processes: New Insights from Phenomenological Modeling.

Diego I Cattoni, Osvaldo Chara, Sergio B Kaufman, F Luis González Flecha

Abstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing 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

26 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Quantification and potential functional relevance of binding cooperativity of adjacent transcription factors on DNA.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. Article
  7. Article
  8. Biophysical Characterization of the MMethods in molecular biology (Clifton, N.J.) · 2025
    Article
  9. Review
  10. Article
  11. Salvianolic acid B inhibits thrombosis and directly blocks the thrombin catalytic site.Research and practice in thrombosis and haemostasis · 2024
    Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. A Novel and Functionally Diverse Class of Acetylcholine-Gated Ion Channels.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2023
    Article
  17. Article
  18. Cooperativity between the orthosteric and allosteric ligand binding sites of RORγt.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  19. International journal of molecular sciences · 2021
    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

4 authors.

Diego I CattoniLaboratorio de Biofísica Molecular, Instituto de Química y Fisicoquímica Biológicas, Universidad de Buenos Aires - CONICET, Buenos Aires, Argentina.
Osvaldo CharaInstitute of Physics of Liquids and Biological Systems (IFLYSIB), University of La Plata - CONICET, La Plata, Argentina.
Sergio B KaufmanLaboratorio de Biofísica Molecular, Instituto de Química y Fisicoquímica Biológicas, Universidad de Buenos Aires - CONICET, Buenos Aires, Argentina.
F Luis González FlechaLaboratorio de Biofísica Molecular, Instituto de Química y Fisicoquímica Biológicas, Universidad de Buenos Aires - CONICET, Buenos Aires, Argentina.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cooperative binding is one of the most interesting and not fully understood phenomena involved in control and regulation of biological processes. Here we analyze the simplest phenomenological model that can account for cooperativity (i.e. ligand binding to a macromolecule with two binding sites) by generating equilibrium binding isotherms from deterministically simulated binding time courses. We show that the Hill coefficients determined for cooperative binding, provide a good measure of the Gibbs free energy of interaction among binding sites, and that their values are independent of the free energy of association for empty sites. We also conclude that although negative cooperativity and different classes of binding sites cannot be distinguished at equilibrium, they can be kinetically differentiated. This feature highlights the usefulness of pre-equilibrium time-resolved strategies to explore binding models as a key complement of equilibrium experiments. Furthermore, our analysis shows that under conditions of strong negative cooperativity, the existence of some binding sites can be overlooked, and experiments at very high ligand concentrations can be a valuable tool to unmask such sites.

Indexed as

Models, BiologicalProtein BindingBinding SitesEnergy MetabolismKineticsLigandsMacromolecular SubstancesTime FactorsLigandsMacromolecular Substances

Identifiers

PMID26717487
PMCPMC4696654

What OpenQuestion holds

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Registered trials

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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.