ArticleFASEB journal : official publication of the Federation of American Societies for Experimental Biology2013
Changes in prion replication environment cause prion strain mutation.
Article in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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.
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.
Who cites it
35 citing papers in PubMed.
- Review
- Classical BSE emergence from Nor98/atypical scrapie: Unraveling the shift vs. selection dichotomy in the prion field.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Cases of Creutzfeldt-Jakob disease in young individuals: open questions regarding aetiology.Frontiers in cellular neuroscience · 2025Article
- Reactive Microglia and Astrocytes as Therapeutic Targets in Prion Diseases.Sub-cellular biochemistry · 2025Review
- Review
- Prion strains: shining new light on old concepts.Cell and tissue research · 2023Review
- Conformational diversity in purified prions produced in vitro.PLoS pathogens · 2023Article
- Melatonin: Regulation of Prion Protein Phase Separation in Cancer Multidrug Resistance.Molecules (Basel, Switzerland) · 2022Review
- Cervid Prion Protein Polymorphisms: Role in Chronic Wasting Disease Pathogenesis.International journal of molecular sciences · 2021Review
- Synthetic Prion Selection and Adaptation.Molecular neurobiology · 2019Article
- Prion and Prion-Like Protein Strains: Deciphering the Molecular Basis of Heterogeneity in Neurodegeneration.Viruses · 2019Review
- Cellular and Molecular Mechanisms of Prion Disease.Annual review of pathology · 2019Review
- Generation of novel neuroinvasive prions following intravenous challenge.Brain pathology (Zurich, Switzerland) · 2018Article
- Preserving prion strain identity upon replication of prions in vitro using recombinant prion protein.Acta neuropathologica communications · 2018Article
- Prion replication environment defines the fate of prion strain adaptation.PLoS pathogens · 2018Article
- Prion Strains and Transmission Barrier Phenomena.Pathogens (Basel, Switzerland) · 2018Review
- Methods of Protein Misfolding Cyclic Amplification.Methods in molecular biology (Clifton, N.J.) · 2017Article
- Prion Strain Diversity.Cold Spring Harbor perspectives in medicine · 2016Review
- Isolation of a Defective Prion Mutant from Natural Scrapie.PLoS pathogens · 2016Article
- Incongruity between Prion Conversion and Incubation Period following Coinfection.Journal of virology · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
Abstract
Interspecies prion transmission often leads to stable changes in physical and biological features of prion strains, a phenomenon referred to as a strain mutation. It remains unknown whether changes in the replication environment in the absence of changes in PrP primary structure can be a source of strain mutations. To approach this question, RNA content was altered in the course of amplification of hamster strains in serial protein misfolding cyclic amplification (sPMCAb). On adaptation to an RNA-depleted environment and then readaptation to an environment containing RNA, strain 263K gave rise to a novel PrP(Sc) conformation referred to as 263K(R+), which is characterized by very low conformational stability, high sensitivity to proteolytic digestion, and a replication rate of 10(6)-fold/PMCAb round, which exceeded that of 263K by almost 10(4)-fold. A series of PMCAb experiments revealed that 263K(R+) was lacking in brain-derived 263K material, but emerged de novo as a result of changes in RNA content. A similar transformation was also observed for strain Hyper, suggesting that this phenomenon was not limited to 263K. The current work demonstrates that dramatic PrP(Sc) transformations can be induced by changes in the prion replication environment and without changes in PrP primary structure.
Indexed as
Identifiers
What OpenQuestion holds
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.