Evidence map›Paper›PMID 22016521›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2011

Oligomeric-induced activity by thienyl pyrimidine compounds traps prion infectivity.

Adeline Ayrolles-Torro, Thibaut Imberdis, Joan Torrent, Karine Toupet, Ilia V Baskakov, Guillaume Poncet-Montange, Catherine Grégoire, Françoise Roquet-Baneres, Sylvain Lehmann, Didier Rognan and 3 more

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.3field-weighted citation impact, top 41% 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

9 citing papers in PubMed, 18 citations in OpenAlex.

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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

13 authors at 4 institutions in 2 countries.

Adeline Ayrolles-TorroUniversité Montpellier 2, Montpellier, F-34095 France.
Thibaut Imberdis
Joan Torrent
Karine Toupet
Ilia V Baskakov
Guillaume Poncet-Montange
Catherine Grégoire
Françoise Roquet-Baneres
Sylvain Lehmann
Didier Rognan
Martine Pugnière
Jean-Michel Verdier
Véronique Perrier
Inserm · FRCentre National de la Recherche Scientifique · FRUniversité de Montpellier · FRUniversity of Maryland, Baltimore · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Accumulation of PrP(Sc), an abnormal form of cellular prion protein (PrP), in the brain of animals and humans leads to fatal neurodegenerative disorders known as prion diseases. Limited protease digestion of PrP(Sc) produces a truncated form called PrP(27-30) that retains prion infectivity and is the main marker of disease targeted in most diagnostic tests. In the search for new anti-prion molecules, drug-screening assays on prion-infected murine cells have been oriented toward decreasing levels of PrP(27-30). In contrast, we screened for drugs promoting multimers of PrP(27-30), illustrating a possible stabilization of mouse PrP(Sc) species, because recent studies aiming to characterize the conformational stability of various prion strains showed that stable recombinant amyloids produced more stable prion strain, leading to longest incubation time. We identified a family of thienyl pyrimidine derivatives that induce SDS-resistant dimers and trimers of PrP(27-30). Bioassays performed on mice brain homogenates treated with these compounds showed that these thienyl pyrimidine derivatives diminished prion infectivity in vivo. Oligomeric-induced activity by thienyl pyrimidine compounds is a promising approach not only to understanding the pathogenesis of prions but also for prion diagnostics. This approach could be extended to other neurodegenerative "prionopathies," such as Alzheimer's, Huntington, or Parkinson's diseases.

Indexed as

AnilidesAnimalsBrainCell Line, TumorDisease Models, AnimalDose-Response Relationship, DrugDrug Evaluation, PreclinicalEndopeptidase KGlial Fibrillary Acidic ProteinHumansMiceModels, MolecularNeuroblastomaPeptide FragmentsPeptide HydrolasesPrion Diseases2-(methylthio)benzanilideAnilidesEndopeptidase KGlial Fibrillary Acidic ProteinPeptide FragmentsPeptide HydrolasesPrPC ProteinsPyrimidinesSilicon

Identifiers

PMID22016521
PMCPMC6623559
OpenAlexW2113891785

What OpenQuestion holds

Textmetadata
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.