Evidence map›Paper›PMID 29665324›Full record

ArticleThe journal of pathology. Clinical research2018

Rapid amplification of prions from variant Creutzfeldt-Jakob disease cerebrospinal fluid.

Marcelo A Barria, Andrew Lee, Alison Je Green, Richard Knight, Mark W Head

Open access · goldAbstract read
In one paragraph

Article in The journal of pathology. Clinical research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.1field-weighted citation impact, top 22% 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

21 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Diagnosis of Prion Diseases.Sub-cellular biochemistry · 2025
    Review
  5. Review
  6. Article
  7. Review
  8. Article
  9. Review
  10. Review
  11. Article
  12. Variant CJD: Reflections a Quarter of a Century on.Pathogens (Basel, Switzerland) · 2021
    Review
  13. Review
  14. Article
  15. Review
  16. Review
  17. Review
  18. Review
  19. Role of prion protein glycosylation in replication of human prions by protein misfolding cyclic amplification.Laboratory investigation; a journal of technical methods and pathology · 2019
    Article
  20. Review
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

5 authors at 1 institution in 1 country.

Marcelo A BarriaNational CJD Research & Surveillance Unit, Centre for Clinical Brain Sciences, Deanery of Clinical Medicine, The University of Edinburgh, Edinburgh, UK.ORCID 0000-0003-4789-7401
Andrew LeeNational CJD Research & Surveillance Unit, Centre for Clinical Brain Sciences, Deanery of Clinical Medicine, The University of Edinburgh, Edinburgh, UK.
Alison Je GreenNational CJD Research & Surveillance Unit, Centre for Clinical Brain Sciences, Deanery of Clinical Medicine, The University of Edinburgh, Edinburgh, UK.
Richard KnightNational CJD Research & Surveillance Unit, Centre for Clinical Brain Sciences, Deanery of Clinical Medicine, The University of Edinburgh, Edinburgh, UK.
Mark W HeadNational CJD Research & Surveillance Unit, Centre for Clinical Brain Sciences, Deanery of Clinical Medicine, The University of Edinburgh, Edinburgh, UK.
University of Edinburgh · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Human prion diseases constitute a group of infectious and invariably fatal neurodegenerative disorders associated with misfolding of the prion protein. Variant Creutzfeldt-Jakob disease (vCJD) is a zoonotic prion disease linked to oral exposure to the infectious agent that causes bovine spongiform encephalopathy (BSE) in cattle. The most recent case of definite vCJD was heterozygous (MV) at polymorphic codon 129 of the prion protein gene PRNP while all of the previous 177 definite or probable vCJD cases who underwent genetic analysis were methionine homozygous (MM). Retrospective prevalence studies conducted on lympho-reticular tissue suggest that the number of asymptomatic vCJD carriers in the United Kingdom might be around 1 in 2000 people. In addition, there have been four known cases of the transmission of vCJD infection via blood transfusion. For these reasons, a sensitive, reliable, and fast diagnostic test is currently needed. We describe a rapid and highly sensitive seeding conversion assay that detects disease-associated prion protein in the brain and cerebrospinal fluid in vCJD after 48-96 h of amplification, with 100% sensitivity and specificity. This method can amplify prions from definite, probable, and possible vCJD cases from patients who are either MM or MV at PRNP-codon 129.

Indexed as

AnimalsBrainCattleCodonCreutzfeldt-Jakob SyndromeEncephalopathy, Bovine SpongiformHomozygoteHumansMethioninePrion DiseasesPrion ProteinsRetrospective StudiesSensitivity and Specificitytau ProteinsUnited KingdomZoonosesCodonMethioninePrion ProteinsPRNP protein, humantau ProteinsCreutzfeldt-Jakob diseasediagnostic testprionprotein misfolding

Identifiers

PMID29665324
PMCPMC5903693
OpenAlexW2779266651

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.