Evidence map›Paper›PMID 28513534›Full record

ReviewInternational journal of molecular sciences2017

Unraveling Prion Protein Interactions with Aptamers and Other PrP-Binding Nucleic Acids.

Bruno Macedo, Yraima Cordeiro

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

22 citing papers in PubMed, 48 citations in OpenAlex.

  1. Review
  2. New Therapeutic Modalities in Prion Diseases.Sub-cellular biochemistry · 2025
    Review
  3. Review
  4. Liquid-liquid phase separation in hepatocellular carcinoma.Frontiers in cell and developmental biology · 2024
    Review
  5. Excess PrPNature communications · 2023
    Article
  6. Review
  7. Review
  8. Review
  9. Aptamer Applications in Neuroscience.Pharmaceuticals (Basel, Switzerland) · 2021
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Review
  17. Article
  18. Review
  19. Review
  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

2 authors at 1 institution in 1 country.

Bruno MacedoFaculty of Pharmacy, Federal University of Rio de Janeiro (UFRJ), Av. Carlos Chagas Filho 373, Bloco B, Subsolo, Sala 17, Rio de Janeiro, RJ 21941-902, Brazil. brunomacedo@ufrj.br.
Yraima CordeiroFaculty of Pharmacy, Federal University of Rio de Janeiro (UFRJ), Av. Carlos Chagas Filho 373, Bloco B, Subsolo, Sala 17, Rio de Janeiro, RJ 21941-902, Brazil. yraima@pharma.ufrj.br.
Universidade Federal do Rio de Janeiro · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Transmissible spongiform encephalopathies (TSEs) are a group of neurodegenerative disorders that affect humans and other mammals. The etiologic agents common to these diseases are misfolded conformations of the prion protein (PrP). The molecular mechanisms that trigger the structural conversion of the normal cellular PrP (PrP

Indexed as

Amyloidogenic ProteinsAnimalsAptamers, NucleotideCarrier ProteinsDNA, Single-StrandedHumansNucleic AcidsPrion DiseasesPrion ProteinsProtein BindingSELEX Aptamer TechniqueAmyloidogenic ProteinsAptamers, NucleotideCarrier ProteinsDNA, Single-StrandedNucleic AcidsPrion Proteinsaptamersnucleic acidsprion proteinSELEX (Systematic Evolution of Ligands by Exponential Enrichment)

Identifiers

PMID28513534
PMCPMC5454936
OpenAlexW2614220860

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.