Evidence map›Paper›PMID 35680944›Full record

ArticleScientific reports2022

A high-content neuron imaging assay demonstrates inhibition of prion disease-associated neurotoxicity by an anti-prion protein antibody.

Madeleine Reilly, Iryna Benilova, Azadeh Khalili-Shirazi, Christian Schmidt, Parvin Ahmed, Daniel Yip, Parmjit S Jat, John Collinge

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Scientific reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.9field-weighted citation impact, top 29% 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

11 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Prion diseases: Lessons from historical outbreaks and potential emerging ones.Protein science : a publication of the Protein Society · 2025
    Review
  6. Article
  7. Therapeutic Trajectories in Human Prion Diseases.Sub-cellular biochemistry · 2025
    Review
  8. Review
  9. Article
  10. Review
  11. High throughput screening system for engineered cardiac tissues.Frontiers in bioengineering and biotechnology · 2023
    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

8 authors at 2 institutions in 1 country.

Madeleine ReillyMRC Prion Unit at UCL, UCL Institute of Prion Diseases, University College London, Courtauld Building, 33 Cleveland Street, London, W1W 7FF, UK.
Iryna BenilovaMRC Prion Unit at UCL, UCL Institute of Prion Diseases, University College London, Courtauld Building, 33 Cleveland Street, London, W1W 7FF, UK.
Azadeh Khalili-ShiraziMRC Prion Unit at UCL, UCL Institute of Prion Diseases, University College London, Courtauld Building, 33 Cleveland Street, London, W1W 7FF, UK.
Christian SchmidtMRC Prion Unit at UCL, UCL Institute of Prion Diseases, University College London, Courtauld Building, 33 Cleveland Street, London, W1W 7FF, UK.
Parvin AhmedMRC Prion Unit at UCL, UCL Institute of Prion Diseases, University College London, Courtauld Building, 33 Cleveland Street, London, W1W 7FF, UK.
Daniel YipMRC Prion Unit at UCL, UCL Institute of Prion Diseases, University College London, Courtauld Building, 33 Cleveland Street, London, W1W 7FF, UK.
Parmjit S JatMRC Prion Unit at UCL, UCL Institute of Prion Diseases, University College London, Courtauld Building, 33 Cleveland Street, London, W1W 7FF, UK.
John CollingeMRC Prion Unit at UCL, UCL Institute of Prion Diseases, University College London, Courtauld Building, 33 Cleveland Street, London, W1W 7FF, UK. jc@prion.ucl.ac.uk.
University College London · GBMRC Prion Unit · GB

Funding

Medical Research Council MC_U12266BMedical Research Council MC_U123192748Medical Research Council MC_UU_00024/2Medical Research Council MC_UU_00024/7Medical Research Council MR/M02492X/1
6 · The paper itself

Abstract

There is an urgent need to develop disease-modifying therapies to treat neurodegenerative diseases which pose increasing challenges to global healthcare systems. Prion diseases, although rare, provide a paradigm to study neurodegenerative dementias as similar disease mechanisms involving propagation and spread of multichain assemblies of misfolded protein ("prion-like" mechanisms) are increasingly recognised in the commoner conditions such as Alzheimer's disease. However, studies of prion disease pathogenesis in mouse models showed that prion propagation and neurotoxicity can be mechanistically uncoupled and in vitro assays confirmed that highly purified prions are indeed not directly neurotoxic. To aid development of prion disease therapeutics we have therefore developed a cell-based assay for the specific neurotoxicity seen in prion diseases rather than to simply assess inhibition of prion propagation. We applied this assay to examine an anti-prion protein mouse monoclonal antibody (ICSM18) known to potently cure prion-infected cells and to delay onset of prion disease in prion-infected mice. We demonstrate that whilst ICSM18 itself lacks inherent neurotoxicity in this assay, it potently blocks prion disease-associated neurotoxicity.

Indexed as

Neurotoxicity SyndromesPrion DiseasesPrionsAnimalsMiceNeuronsPrion ProteinsPrion ProteinsPrions

Identifiers

PMID35680944
PMCPMC9184462
OpenAlexW4281637692

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.