Evidence map›Paper›PMID 24404191›Full record

ArticlePloS one2014

Exploring physical and chemical factors influencing the properties of recombinant prion protein and the real-time quaking-induced conversion (RT-QuIC) assay.

Keding Cheng, Angela Sloan, Kristen M Avery, Michael Coulthart, Michael Carpenter, J David Knox

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.0field-weighted citation impact, top 25% 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

12 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. Article
  3. Real-Time Quaking-Induced Conversion Detection of PrPFrontiers in veterinary science · 2021
    Article
  4. Article
  5. Article
  6. Million-fold sensitivity enhancement in proteopathic seed amplification assays for biospecimens by Hofmeister ion comparisons.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. A new diagnostic test for Creutzfeldt-Jakob disease: Real-time quaking-induced conversion (RT-QulC).Canada communicable disease report = Releve des maladies transmissibles au Canada · 2015
    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

6 authors at 2 institutions in 1 country.

Keding ChengNational Microbiology Laboratory, Public Health Agency of Canada, Winnipeg, Manitoba, Canada ; Department of Human Anatomy and Cell Sciences, Faculty of Medicine, University of Manitoba, Winnipeg, Manitoba, Canada.
Angela SloanNational Microbiology Laboratory, Public Health Agency of Canada, Winnipeg, Manitoba, Canada.
Kristen M AveryNational Microbiology Laboratory, Public Health Agency of Canada, Winnipeg, Manitoba, Canada.
Michael CoulthartCentre for Food-borne, Environmental and Zoonotic Infectious Diseases, Public Health Agency of Canada, Ottawa, Ontario, Canada.
Michael CarpenterNational Microbiology Laboratory, Public Health Agency of Canada, Winnipeg, Manitoba, Canada ; Department of Medical Microbiology, Faculty of Medicine, University of Manitoba, Winnipeg, Manitoba, Canada.
J David KnoxNational Microbiology Laboratory, Public Health Agency of Canada, Winnipeg, Manitoba, Canada ; Department of Medical Microbiology, Faculty of Medicine, University of Manitoba, Winnipeg, Manitoba, Canada.
Public Health Agency of Canada · CAUniversity of Manitoba · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Real-time quaking-induced conversion (RT-QuIC), a highly specific and sensitive assay able to detect low levels of the disease-inducing isoform of the prion protein (PrP(d)) in brain tissue biopsies and cerebral spinal fluid, has great potential to become a method for diagnosing prion disease ante mortem. In order to standardize the assay method for routine analysis, an understanding of how physical and chemical factors affect the stability of the recombinant prion protein (rPrP) substrate and the RT-QuIC assay's sensitivity, specificity, and reproducibility is required. In this study, using sporadic Creutzfeldt-Jakob Disease brain homogenate to seed the reactions and an in vitro-expressed recombinant prion protein, hamster rPrP, as the substrate, the following factors affecting the RT-QuIC assay were examined: salt and substrate concentrations, substrate storage, and pH. Results demonstrated that both the generation of the quality and quantities of rPrP substrate critical to the reaction, as well as the RT-QuIC reaction itself required strict adherence to specific physical and chemical conditions. Once optimized, the RT-QuIC assay was confirmed to be a very specific and sensitive assay method for sCJD detection. Findings in this study indicate that further optimization and standardization of RT-QuIC assay is required before it can be adopted as a routine diagnostic test.

Indexed as

Biological AssayCreutzfeldt-Jakob SyndromeHumansPrionsRecombinant ProteinsReproducibility of ResultsSensitivity and SpecificityPrionsRecombinant Proteins

Identifiers

PMID24404191
PMCPMC3880330
OpenAlexW2015306242

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.