Evidence map›Paper›PMID 27174240›Full record

ReviewNature reviews. Neurology2016

Advanced tests for early and accurate diagnosis of Creutzfeldt-Jakob disease.

Gianluigi Zanusso, Salvatore Monaco, Maurizio Pocchiari, Byron Caughey

Erratum issuedAbstract readReview
PubMed Publisher
In one paragraph

Review in Nature reviews. Neurology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
11.3field-weighted citation impact, top 1% 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

56 citing papers in PubMed, 125 citations in OpenAlex.

  1. Suspected encephalitis in adults.Practical neurology · 2026
    Review
  2. Article
  3. Article
  4. Review
  5. Review
  6. Diagnosis of Prion Diseases.Sub-cellular biochemistry · 2025
    Review
  7. Review
  8. Article
  9. Review
  10. PRNP expression predicts imaging findings in sporadic Creutzfeldt-Jakob disease.Annals of clinical and translational neurology · 2023
    Article
  11. Review
  12. Article
  13. Article
  14. Probing the origin of prion protein misfolding via reconstruction of ancestral proteins.Protein science : a publication of the Protein Society · 2022
    Article
  15. Review
  16. Article
  17. Review
  18. Article
  19. Review
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 3 institutions in 2 countries.

Gianluigi ZanussoDepartment of Neurosciences, Biomedicine and Movement Sciences, Policlinico G.B. Rossi, University of Verona, Piazzale L.A. Scuro 10, 37134 Verona, Italy.
Salvatore MonacoDepartment of Neurosciences, Biomedicine and Movement Sciences, Policlinico G.B. Rossi, University of Verona, Piazzale L.A. Scuro 10, 37134 Verona, Italy.
Maurizio PocchiariDepartment of Cell Biology and Neurosciences, Istituto Superiore di Sanità, Viale Regina Elena, 299, 00161 Rome, Italy.
Byron CaugheyLaboratory of Persistent Viral Diseases, Rocky Mountain Laboratories, National Institute for Allergy and Infectious Diseases, National Institutes of Health, 903 4th Street, Hamilton, 59840 Montana, USA.
University of Verona · ITIstituto Superiore di Sanità · ITNational Institutes of Health · US

Funding

Detection of PrionsZIAAI001086 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI CAUGHEY, BYRON · 2009 to 2025
$18.1M
6 · The paper itself

Abstract

Early and accurate diagnosis of Creutzfeldt-Jakob disease (CJD) is a necessary to distinguish this untreatable disease from treatable rapidly progressive dementias, and to prevent iatrogenic transmission. Currently, definitive diagnosis of CJD requires detection of the abnormally folded, CJD-specific form of protease-resistant prion protein (PrP(CJD)) in brain tissue obtained postmortem or via biopsy; therefore, diagnosis of sporadic CJD in clinical practice is often challenging. Supporting investigations, including MRI, EEG and conventional analyses of cerebrospinal fluid (CSF) biomarkers, are helpful in the diagnostic work-up, but do not allow definitive diagnosis. Recently, novel ultrasensitive seeding assays, based on the amplified detection of PrP(CJD), have improved the diagnostic process; for example, real-time quaking-induced conversion (RT-QuIC) is a sensitive method to detect prion-seeding activity in brain homogenate from humans with any subtype of sporadic CJD. RT-QuIC can also be used for in vivo diagnosis of CJD: its diagnostic sensitivity in detecting PrP(CJD) in CSF samples is 96%, and its specificity is 100%. Recently, we provided evidence that RT-QuIC of olfactory mucosa brushings is a 97% sensitive and 100% specific for sporadic CJD. These assays provide a basis for definitive antemortem diagnosis of prion diseases and, in doing so, improve prospects for reducing the risk of prion transmission. Moreover, they can be used to evaluate outcome measures in therapeutic trials for these as yet untreatable infections.

Indexed as

Creutzfeldt-Jakob SyndromeEarly DiagnosisHumansMolecular Diagnostic Techniques

Identifiers

PMID27174240
OpenAlexW2374024322

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.