Evidence map›Paper›PMID 30357392›Full record

ArticleNucleic acids research2018

Several structural motifs cooperate in determining the highly effective anti-thrombin activity of NU172 aptamer.

Romualdo Troisi, Valeria Napolitano, Vera Spiridonova, Irene Russo Krauss, Filomena Sica

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
2.9field-weighted citation impact, top 8% 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

35 citing papers in PubMed, 72 citations in OpenAlex.

  1. Article
  2. Folding and unfolding dynamics of a DNA aptamer studied by heteronuclearJournal of magnetic resonance (San Diego, Calif. : 1997) · 2026
    Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Aptamer-Based DNA Allosteric Switch for Regulation of Protein Activity.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. 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

5 authors at 3 institutions in 2 countries.

Romualdo TroisiDepartment of Chemical Sciences, University of Naples 'Federico II', Naples 80126, Italy.
Valeria NapolitanoDepartment of Chemical Sciences, University of Naples 'Federico II', Naples 80126, Italy.
Vera SpiridonovaA.N. Belozersky Institute of Physico-Chemical Biology, M.V. Lomonosov Moscow State University, Moscow 119992, Russia.
Irene Russo KraussDepartment of Chemical Sciences, University of Naples 'Federico II', Naples 80126, Italy.
Filomena SicaDepartment of Chemical Sciences, University of Naples 'Federico II', Naples 80126, Italy.
University of Naples Federico II · ITConsorzio Interuniversitario per lo Sviluppo dei Sistemi a Grande Interfase · ITLomonosov Moscow State University · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Despite aptamers are very promising alternative to antibodies, very few of them are under clinical trials or are used as drugs. Among them, NU172 is currently in Phase II as anticoagulant in heart disease treatments. It inhibits thrombin activity much more effectively than TBA, the best-known thrombin binding aptamer. The crystal structure of thrombin-NU172 complex reveals a bimodular duplex/quadruplex architecture for the aptamer, which binds thrombin exosite I through a highly complementary surface involving all three loops of the G-quadruplex module. Although the duplex domain does not interact directly with thrombin, the features of the duplex/quadruplex junction and the solution data on two newly designed NU172 mutants indicate that the duplex moiety is important for the optimization of the protein-ligand interaction and for the inhibition of the enzyme activity. Our work discloses the structural features determining the inhibition of thrombin by NU172 and put the basis for the design of mutants with improved properties.

Indexed as

Amino Acid MotifsAnticoagulantsAptamers, NucleotideCircular DichroismCrystallography, X-RayFibrinogenFibrinolytic AgentsG-QuadruplexesHumansLigandsModels, MolecularMutationOligonucleotidesProtein BindingProtein ConformationThrombinAnticoagulantsAptamers, NucleotideFibrinogenFibrinolytic AgentsLigandsNU172OligonucleotidesThrombinthrombin aptamer

Identifiers

PMID30357392
PMCPMC6294562
OpenAlexW2896789896

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.