ReviewAnnual review of microbiology2013
Prions and the potential transmissibility of protein misfolding diseases.
Review in Annual review of microbiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.
What it found
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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.
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.
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Who cites it
59 citing papers in PubMed, 104 citations in OpenAlex.
- Ring trial of 2nd generation RT-QuIC diagnostic tests for sporadic CJD.Annals of clinical and translational neurology · 2020Trial
- Life at the interface: Byron Caughey's search for prion disease inhibitors through chemistry, structure, and cell physiology.Acta neuropathologica · 2026Review
- Transcriptomic analysis of Rnq1 loss and prionization reveals alterations in translation pathways and energy metabolism.Scientific reports · 2026Article
- Prions and protein aggregates as pathogens, self-propagating structures, biomarkers, and therapeutic targets.Microbiology and molecular biology reviews : MMBR · 2025Review
- Contrasting roles of autophagy in cellular prion infection.Autophagy · 2025Article
- A same day α-synuclein RT-QuIC seed amplification assay for synucleinopathy biospecimens.Npj biosensing · 2025Article
- Aggregating amyloid resources: A comprehensive review of databases on amyloid-like aggregation.Computational and structural biotechnology journal · 2024Review
- Degradation and/or Dissociation of Neurodegenerative Disease-Related Factor Amyloid-β by a Suspension Containing Calcium Hydrogen Carbonate Mesoscopic Crystals.International journal of molecular sciences · 2024Article
- Cryo-EM structure of a natural prion: chronic wasting disease fibrils from deer.Acta neuropathologica · 2024Article
- Lack of Transmission of Chronic Wasting Disease Prions to Human Cerebral Organoids.Emerging infectious diseases · 2024Article
- Sensitive detection of pathological seeds of α-synuclein, tau and prion protein on solid surfaces.PLoS pathogens · 2024Article
- Intrinsic determinants of prion protein neurotoxicity inFrontiers in molecular neuroscience · 2023Review
- Cryo-EM of prion strains from the same genotype of host identifies conformational determinants.PLoS pathogens · 2022Article
- Structural biology of ex vivo mammalian prions.The Journal of biological chemistry · 2022Review
- Pathogenic prion structures at high resolution.PLoS pathogens · 2022Article
- Microglia have limited influence on early prion pathogenesis, clearance, or replication.PloS one · 2022Article
- Is Multiple System Atrophy a Prion-like Disorder?International journal of molecular sciences · 2021Review
- RNA-seq and network analysis reveal unique glial gene expression signatures during prion infection.Molecular brain · 2020Article
- Challenges and Advances in Antemortem Diagnosis of Human Transmissible Spongiform Encephalopathies.Frontiers in bioengineering and biotechnology · 2020Review
- Insight From Animals Resistant to Prion Diseases: Deciphering the Genotype - Morphotype - Phenotype Code for the Prion Protein.Frontiers in cellular neuroscience · 2020Review
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Prions, or infectious proteins, represent a major frontier in the study of infectious agents. The prions responsible for mammalian transmissible spongiform encephalopathies (TSEs) are due primarily to infectious self-propagation of misfolded prion proteins. TSE prion structures remain ill-defined, other than being highly structured, self-propagating, and often fibrillar protein multimers with the capacity to seed, or template, the conversion of their normal monomeric precursors into a pathogenic form. Purified TSE prions usually take the form of amyloid fibrils, which are self-seeding ultrastructures common to many serious protein misfolding diseases such as Alzheimer's, Parkinson's, Huntington's and Lou Gehrig's (amytrophic lateral sclerosis). Indeed, recent reports have now provided evidence of prion-like propagation of several misfolded proteins from cell to cell, if not from tissue to tissue or individual to individual. These findings raise concerns that various protein misfolding diseases might have spreading, prion-like etiologies that contribute to pathogenesis or prevalence.
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Registered trials
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.