Evidence map›Paper›PMID 33182593›Full record

ReviewMolecules (Basel, Switzerland)2020

Dimeric and Multimeric DNA Aptamers for Highly Effective Protein Recognition.

Claudia Riccardi, Ettore Napolitano, Domenica Musumeci, Daniela Montesarchio

Open access · goldAbstract readReview
In one paragraph

Review in Molecules (Basel, Switzerland), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing 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

21 citing papers in PubMed, 51 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Determining the Optimal Heparin Binding Domain Distance in VEGFInternational journal of molecular sciences · 2026
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
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 at 3 institutions in 1 country.

Claudia RiccardiDepartment of Chemical Sciences, University of Naples Federico II, via Cintia 21, I-80126 Naples, Italy.ORCID 0000-0002-7182-0757
Ettore NapolitanoDepartment of Chemical Sciences, University of Naples Federico II, via Cintia 21, I-80126 Naples, Italy.ORCID 0000-0001-6160-1860
Domenica MusumeciDepartment of Chemical Sciences, University of Naples Federico II, via Cintia 21, I-80126 Naples, Italy.ORCID 0000-0001-7624-1933
Daniela MontesarchioDepartment of Chemical Sciences, University of Naples Federico II, via Cintia 21, I-80126 Naples, Italy.ORCID 0000-0001-6295-6911
University of Naples Federico II · ITInstitute of Biostructure and Bioimaging · ITUniversity of Campania "Luigi Vanvitelli" · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Multivalent interactions frequently occur in biological systems and typically provide higher binding affinity and selectivity in target recognition than when only monovalent interactions are operative. Thus, taking inspiration by nature, bivalent or multivalent nucleic acid aptamers recognizing a specific biological target have been extensively studied in the last decades. Indeed, oligonucleotide-based aptamers are suitable building blocks for the development of highly efficient multivalent systems since they can be easily modified and assembled exploiting proper connecting linkers of different nature. Thus, substantial research efforts have been put in the construction of dimeric/multimeric versions of effective aptamers with various degrees of success in target binding affinity or therapeutic activity enhancement. The present review summarizes recent advances in the design and development of dimeric and multimeric DNA-based aptamers, including those forming G-quadruplex (G4) structures, recognizing different key proteins in relevant pathological processes. Most of the designed constructs have shown improved performance in terms of binding affinity or therapeutic activity as anti-inflammatory, antiviral, anticoagulant, and anticancer agents and their number is certainly bound to grow in the next future.

Indexed as

G-QuadruplexesAnticoagulantsAnti-Inflammatory AgentsAntineoplastic AgentsAntiviral AgentsAptamers, NucleotideCD3 ComplexCell Adhesion MoleculesDimerizationDNAHumansImmunoglobulin MNucleolinPhosphoproteinsProtein Structure, SecondaryProto-Oncogene Proteins c-metAnticoagulantsAnti-Inflammatory AgentsAntineoplastic AgentsAntiviral AgentsAptamers, NucleotideCD3 ComplexCell Adhesion MoleculesDNAImmunoglobulin MNucleolinPhosphoproteinsProto-Oncogene Proteins c-metPTK7 protein, humanpyrrolidin-3-yl-methanesulfonic acidPyrrolidinesReceptor Protein-Tyrosine KinasesReceptors, Antigen, T-CellRNA-Binding ProteinsVascular Endothelial Growth Factor AVitronectinaptamerdesigndimerizationG-quadruplexmolecular recognitionmultivalencyprotein targettherapy

Identifiers

PMID33182593
PMCPMC7698228
OpenAlexW3100524168

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.