Evidence map›Paper›PMID 33144644›Full record

ArticleScientific reports2020

Thermodynamic analysis of cooperative ligand binding by the ATP-binding DNA aptamer indicates a population-shift binding mechanism.

Sladjana Slavkovic, Yanrui Zhu, Zachary R Churcher, Aron A Shoara, Anne E Johnson, Philip E Johnson

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

13 citing papers in PubMed, 49 citations in OpenAlex.

  1. 4-Ethyl phenyl sulfate binding to human serum albumin.Protein science : a publication of the Protein Society · 2026
    Article
  2. Article
  3. Article
  4. Specific ATP Detection Using Molecule-Responsive DNA Nanopores.Small (Weinheim an der Bergstrasse, Germany) · 2025
    Article
  5. Review
  6. Mechanism of Dual-Site Recognition in a Classic DNA Aptamer.Journal of chemical information and modeling · 2024
    Article
  7. Review
  8. Article
  9. Article
  10. In vitro selection of aptamers and their applications.Nature reviews. Methods primers · 2023
    Article
  11. Review
  12. Characterizing Aptamers with Reconfigurable Chiral Plasmonic Assemblies.Langmuir : the ACS journal of surfaces and colloids · 2022
    Article
  13. 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

6 authors at 2 institutions in 1 country.

Sladjana SlavkovicDepartment of Chemistry and Centre for Research on Biomolecular Interactions, York University, Toronto, ON, M3J 1P3, Canada.
Yanrui ZhuDepartment of Chemistry and Centre for Research on Biomolecular Interactions, York University, Toronto, ON, M3J 1P3, Canada.
Zachary R ChurcherDepartment of Chemistry and Centre for Research on Biomolecular Interactions, York University, Toronto, ON, M3J 1P3, Canada.
Aron A ShoaraDepartment of Chemistry and Centre for Research on Biomolecular Interactions, York University, Toronto, ON, M3J 1P3, Canada.
Anne E JohnsonDepartment of Chemistry and Biology, Ryerson University, Toronto, ON, M5B 2K3, Canada.
Philip E JohnsonDepartment of Chemistry and Centre for Research on Biomolecular Interactions, York University, Toronto, ON, M3J 1P3, Canada. pjohnson@yorku.ca.
York University · CAToronto Metropolitan University · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ATP-binding DNA aptamer is often used as a model system for developing new aptamer-based biosensor methods. This aptamer follows a structure-switching binding mechanism and is unusual in that it binds two copies of its ligand. We have used isothermal titration calorimetry methods to study the binding of ATP, ADP, AMP and adenosine to the ATP-binding aptamer. Using both individual and global fitting methods, we show that this aptamer follows a positive cooperative binding mechanism. We have determined the binding affinity and thermodynamics for both ligand-binding sites. By separating the ligand-binding sites by an additional four base pairs, we engineered a variant of this aptamer that binds two adenosine ligands in an independent manner. Together with NMR and thermal stability experiments, these data indicate that the ATP-binding DNA aptamer follows a population-shift binding mechanism that is the source of the positive binding cooperativity by the aptamer.

Indexed as

ThermodynamicsAdenosine TriphosphateAptamers, NucleotideBinding SitesCalorimetryMagnetic Resonance SpectroscopyAdenosine TriphosphateAptamers, Nucleotide

Identifiers

PMID33144644
PMCPMC7609719
OpenAlexW3095438497

What OpenQuestion holds

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LicenceCC BY
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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.