Evidence map›Paper›PMID 38743607›Full record

ArticleACS chemical neuroscience2024

Sigma Receptor Ligands Are Potent Antiprion Compounds that Act Independently of Sigma Receptor Binding.

Robert C C Mercer, Nhat T T Le, Douglas G Fraser, Mei C Q Houser, Aaron B Beeler, David A Harris

Abstract read
In one paragraph

Article in ACS chemical neuroscience, 2024. 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
–field-weighted citation impact
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.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Enhanced lysosomal activity prevents infection with PrPThe Journal of biological chemistry · 2026
    Article
  6. Article
  7. Review
  8. Review
  9. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors.

Robert C C MercerDepartment of Biochemistry & Cell Biology, Boston University Chobanian & Avedisian School of Medicine, Boston, Massachusetts 02118, United States.ORCID 0000-0001-6029-511X
Nhat T T LeDepartment of Biochemistry & Cell Biology, Boston University Chobanian & Avedisian School of Medicine, Boston, Massachusetts 02118, United States.
Douglas G FraserDepartment of Chemistry, Boston University, Boston, Massachusetts 02215, United States.
Mei C Q HouserDepartment of Biochemistry & Cell Biology, Boston University Chobanian & Avedisian School of Medicine, Boston, Massachusetts 02118, United States.
Aaron B BeelerDepartment of Chemistry, Boston University, Boston, Massachusetts 02215, United States.ORCID 0000-0002-2447-0651
David A HarrisDepartment of Biochemistry & Cell Biology, Boston University Chobanian & Avedisian School of Medicine, Boston, Massachusetts 02118, United States.

Funding

Mechanisms of Prion Protein ToxicityR01NS065244 · NINDS · BOSTON UNIVERSITY MEDICAL CAMPUS · PI HARRIS, DAVID A · 2010 to 2025
$8.9M
NINDS NIH HHS R01 NS065244
6 · The paper itself

Abstract

Prion diseases are invariably fatal neurodegenerative diseases of humans and other animals for which there are no effective treatment options. Previous work from our laboratory identified phenethylpiperidines as a novel class of anti-prion compounds. While working to identify the molecular target(s) of these molecules, we unexpectedly discovered ten novel antiprion compounds based on their known ability to bind to the sigma receptors, σ

Indexed as

Prion DiseasesReceptors, sigmaAnimalsCell Line, TumorHumansLigandsMicePrionsSigma-1 ReceptorLigandsPrionsReceptors, sigmaSigma-1 Receptorsigma-2 receptorantiprion compoundCRISPRneurodegenerationPDSPprionRT-QuICsigma receptors

Identifiers

PMID38743607
PMCPMC12172621

What OpenQuestion holds

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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.