Evidence map›Paper›PMID 23977222›Full record

ArticlePloS one2013

The toll-like receptor agonist imiquimod is active against prions.

Nassima Oumata, Phu Hai Nguyen, Vincent Beringue, Flavie Soubigou, Yanhong Pang, Nathalie Desban, Catherine Massacrier, Yannis Morel, Carine Paturel, Marie-Astrid Contesse and 5 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2013. 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
1.5field-weighted citation impact, top 18% 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, 27 citations in OpenAlex.

  1. Article
  2. Review
  3. Anti-prion Drugs Targeting the Protein Folding Activity of the Ribosome Reduce PABPN1 Aggregation.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2021
    Article
  4. Neural regeneration research · 2021
    Review
  5. Review
  6. Ribosomal RNA Modulates Aggregation of theInternational journal of molecular sciences · 2020
    Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  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

15 authors at 9 institutions in 4 countries.

Nassima OumataLaboratoire de Chimie Organique 2, INSERM U1022, Université Paris Descartes, Paris, France.
Phu Hai Nguyen
Vincent Beringue
Flavie Soubigou
Yanhong Pang
Nathalie Desban
Catherine Massacrier
Yannis Morel
Carine Paturel
Marie-Astrid Contesse
Serge Bouaziz
Suparna Sanyal
Hervé Galons
Marc Blondel
Cécile Voisset
Innate Pharma (France) · FRCentre Hospitalier Régional Universitaire de Brest · FRUniversité de Bretagne Occidentale · FRUniversité Paris Cité · FRUppsala University · SECentre National de la Recherche Scientifique · FRDélégation Paris 5 · FRÉtablissement Français du Sang · FRInstitut National de la Recherche Agronomique · MA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Using a yeast-based assay, a previously unsuspected antiprion activity was found for imiquimod (IQ), a potent Toll-like receptor 7 (TLR7) agonist already used for clinical applications. The antiprion activity of IQ was first detected against yeast prions [PSI (+) ] and [URE3], and then against mammalian prion both ex vivo in a cell-based assay and in vivo in a transgenic mouse model for prion diseases. In order to facilitate structure-activity relationship studies, we conducted a new synthetic pathway which provides a more efficient means of producing new IQ chemical derivatives, the activity of which was tested against both yeast and mammalian prions. The comparable antiprion activity of IQ and its chemical derivatives in the above life forms further emphasizes the conservation of prion controlling mechanisms throughout evolution. Interestingly, this study also demonstrated that the antiprion activity of IQ and IQ-derived compounds is independent from their ability to stimulate TLRs. Furthermore, we found that IQ and its active chemical derivatives inhibit the protein folding activity of the ribosome (PFAR) in vitro.

Indexed as

AminoquinolinesAnimalsCell LineDrug Evaluation, PreclinicalGlutathione PeroxidaseGuanosineHumansImidazolesImiquimodMembrane GlycoproteinsMicePeptide Termination FactorsPrion DiseasesPrionsProtein FoldingPrPSc ProteinsAminoquinolinesgardiquimodGlutathione PeroxidaseGuanosineImidazolesImiquimodloxoribineMembrane GlycoproteinsPeptide Termination FactorsPrionsPrPSc ProteinsresiquimodSaccharomyces cerevisiae ProteinsSUP35 protein, S cerevisiaeTlr7 protein, mouseTLR8 protein, mouseToll-Like Receptor 7Toll-Like Receptor 8URE2 protein, S cerevisiae

Identifiers

PMID23977222
PMCPMC3745460
OpenAlexW2124471271

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.