Evidence map›Paper›PMID 38424082›Full record

ReviewNature reviews. Disease primers2024

Creutzfeldt-Jakob disease and other prion diseases.

Inga Zerr, Anna Ladogana, Simon Mead, Peter Hermann, Gianluigi Forloni, Brian S Appleby

Open access · greenAbstract readReview
PubMed Publisher
In one paragraph

Review in Nature reviews. Disease primers, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed, 2 pooled it
17.1field-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

57 citing papers in PubMed, 2 syntheses or guidelines pooled it, 73 citations in OpenAlex.

  1. Pooled it
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  7. Review
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  9. Depleting prion protein using splice-switching small molecules.bioRxiv : the preprint server for biology · 2026
    Article
  10. Review
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  15. Toxic mechanisms of amyloid oligomers and therapeutic strategies.Protein science : a publication of the Protein Society · 2026
    Review
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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 5 institutions in 4 countries.

Inga ZerrNational Reference Center for CJD Surveillance, Department of Neurology, University Medical Center, Georg August University, Göttingen, Germany. ingazerr@med.uni-goettingen.de.ORCID http://orcid.org/0000-0002-6722-2463
Anna LadoganaDepartment of Neuroscience, Istituto Superiore di Sanità, Rome, Italy.ORCID http://orcid.org/0000-0002-7504-6906
Simon MeadMRC Prion Unit at UCL, Institute of Prion Diseases, London, UK.ORCID http://orcid.org/0000-0002-4326-1468
Peter HermannNational Reference Center for CJD Surveillance, Department of Neurology, University Medical Center, Georg August University, Göttingen, Germany.ORCID http://orcid.org/0000-0003-1889-8325
Gianluigi ForloniDepartment of Neuroscience, Istituto di Ricerche Farmacologiche Mario Negri IRCCS, Milan, Italy.ORCID http://orcid.org/0000-0001-5374-3914
Brian S ApplebyDepartments of Neurology, Psychiatry and Pathology, Case Western Reserve University, Cleveland, OH, USA.ORCID http://orcid.org/0000-0003-2275-3292
University of Göttingen · DECase Western Reserve University · USIstituto Superiore di Sanità · ITMario Negri Institute for Pharmacological Research · ITMRC Prion Unit · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Prion diseases share common clinical and pathological characteristics such as spongiform neuronal degeneration and deposition of an abnormal form of a host-derived protein, termed prion protein. The characteristic features of prion diseases are long incubation times, short clinical courses, extreme resistance of the transmissible agent to degradation and lack of nucleic acid involvement. Sporadic and genetic forms of prion diseases occur worldwide, of which genetic forms are associated with mutations in PRNP. Human to human transmission of these diseases has occurred due to iatrogenic exposure, and zoonotic forms of prion diseases are linked to bovine disease. Significant progress has been made in the diagnosis of these disorders. Clinical tools for diagnosis comprise brain imaging and cerebrospinal fluid tests. Aggregation assays for detection of the abnormally folded prion protein have a clear potential to diagnose the disease in peripherally accessible biofluids. After decades of therapeutic nihilism, new treatment strategies and clinical trials are on the horizon. Although prion diseases are relatively rare disorders, understanding their pathogenesis and mechanisms of prion protein misfolding has significantly enhanced the field in research of neurodegenerative diseases.

Indexed as

Creutzfeldt-Jakob SyndromePrion DiseasesAnimalsBrainCattleHumansPrion ProteinsPrion Proteins

Identifiers

PMID38424082
OpenAlexW4392286414

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.