Evidence map›Paper›PMID 33398328›Full record

ArticleNucleic acids research2021

Terminal deoxynucleotidyl transferase-mediated formation of protein binding polynucleotides.

Jon Ashley, Anna-Lisa Schaap-Johansen, Mohsen Mohammadniaei, Maryam Naseri, Paolo Marcatili, Marta Prado, Yi Sun

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.0field-weighted citation impact, top 24% 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

12 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. SegDesign: A modular framework for controllable protein segment engineering.Protein science : a publication of the Protein Society · 2026
    Article
  3. Advances in aptamer technology for target-based drug discovery.Journal of pharmaceutical analysis · 2026
    Review
  4. Article
  5. Review
  6. Article
  7. A Massively ParallelACS synthetic biology · 2024
    Article
  8. Article
  9. Review
  10. The Protein-Templated Synthesis of Enzyme-Generated Aptamers.Angewandte Chemie (International ed. in English) · 2022
    Article
  11. Review
  12. 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

7 authors at 2 institutions in 2 countries.

Jon AshleyTechnical University of Denmark, Department of Health Technology, Kgs. Lyngby 2800, Denmark.
Anna-Lisa Schaap-JohansenTechnical University of Denmark, Department of Health Technology, Kgs. Lyngby 2800, Denmark.
Mohsen MohammadniaeiTechnical University of Denmark, Department of Health Technology, Kgs. Lyngby 2800, Denmark.
Maryam NaseriTechnical University of Denmark, Department of Health Technology, Kgs. Lyngby 2800, Denmark.
Paolo MarcatiliTechnical University of Denmark, Department of Health Technology, Kgs. Lyngby 2800, Denmark.
Marta PradoInternational Iberian Nanotechnology Laboratory (INL), Av. Mestre José Veiga Braga 4715-330, Portugal.
Yi SunTechnical University of Denmark, Department of Health Technology, Kgs. Lyngby 2800, Denmark.
Technical University of Denmark · DKInternational Iberian Nanotechnology Laboratory · PT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Terminal deoxynucleotidyl transferase (TdT) enzyme plays an integral part in the V(D)J recombination, allowing for the huge diversity in expression of immunoglobulins and T-cell receptors within lymphocytes, through their unique ability to incorporate single nucleotides into oligonucleotides without the need of a template. The role played by TdT in lymphocytes precursors found in early vertebrates is not known. In this paper, we demonstrated a new screening method that utilises TdT to form libraries of variable sized (vsDNA) libraries of polynucleotides that displayed binding towards protein targets. The extent of binding and size distribution of each vsDNA library towards their respective protein target can be controlled through the alteration of different reaction conditions such as time of reaction, nucleotide ratio and initiator concentration raising the possibility for the rational design of aptamers prior to screening. The new approach, allows for the screening of aptamers based on size as well as sequence in a single round, which minimises PCR bias. We converted the protein bound sequences to dsDNA using rapid amplification of variable ends assays (RAVE) and sequenced them using next generation sequencing. The resultant aptamers demonstrated low nanomolar binding and high selectivity towards their respective targets.

Indexed as

Aptamers, NucleotideBinding SitesDNADNA NucleotidylexotransferaseDNA, Single-StrandedDrug Evaluation, PreclinicalElectrophoretic Mobility Shift AssayGene LibraryHigh-Throughput Nucleotide SequencingLactoferrinNucleic Acid Amplification TechniquesProtein BindingSubstrate SpecificityThrombinV(D)J RecombinationAptamers, NucleotideDNADNA NucleotidylexotransferaseDNA, Single-StrandedLactoferrinLTF protein, humanThrombinthrombin aptamer

Identifiers

PMID33398328
PMCPMC7826267
OpenAlexW3120278075

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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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.