ArticleThe American journal of pathology2016
New Molecular Insight into Mechanism of Evolution of Mammalian Synthetic Prions.
Article in The American journal of pathology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 30 citations in OpenAlex.
- 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
- Reactive Microglia and Astrocytes as Therapeutic Targets in Prion Diseases.Sub-cellular biochemistry · 2025Review
- Prion assemblies: structural heterogeneity, mechanisms of formation, and role in species barrier.Cell and tissue research · 2023Review
- Prion strains: shining new light on old concepts.Cell and tissue research · 2023Review
- Role of sialylation of N-linked glycans in prion pathogenesis.Cell and tissue research · 2023Review
- From Posttranslational Modifications to Disease Phenotype: A Substrate Selection Hypothesis in Neurodegenerative Diseases.International journal of molecular sciences · 2021Review
- Posttranslational modifications define course of prion strain adaptation and disease phenotype.The Journal of clinical investigation · 2020Article
- Modeling PrPFrontiers in bioengineering and biotechnology · 2020Article
- Variable Protease-Sensitive Prionopathy Transmission to Bank Voles.Emerging infectious diseases · 2019Article
- Prion Strain-Specific Structure and Pathology: A View from the Perspective of Glycobiology.Viruses · 2018Review
- 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
- Iatrogenic Creutzfeldt-Jakob disease with Amyloid-β pathology: an international study.Acta neuropathologica communications · 2018Article
- Prion Strains and Transmission Barrier Phenomena.Pathogens (Basel, Switzerland) · 2018Review
- Strains of Pathological Protein Aggregates in Neurodegenerative Diseases.Discoveries (Craiova, Romania) · 2017Review
- Molecular dynamics simulations of early steps in RNA-mediated conversion of prions.Protein science : a publication of the Protein Society · 2017Article
- Cross-seeding of prions by aggregated α-synuclein leads to transmissible spongiform encephalopathy.PLoS pathogens · 2017Article
- Novel strain properties distinguishing sporadic prion diseases sharing prion protein genotype and prion type.Scientific reports · 2017Article
- Infectious prions and proteinopathies.Prion · 2017Article
- Looking at the recent advances in understanding α-synuclein and its aggregation through the proteoform prism.F1000Research · 2017Review
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5 authors at 1 institution in 1 country.
Funding
Abstract
Previous studies established that transmissible prion diseases could be induced by in vitro-produced recombinant prion protein (PrP) fibrils with structures that are fundamentally different from that of authentic PrP scrapie isoform (PrP(Sc)). To explain evolution of synthetic prions, a new mechanism referred to as deformed templating was introduced. Here, we asked whether an increase in expression level of the cellular form of PrP (PrP(C)) speeds up the evolution of synthetic strains in vivo. We found that in transgenic mice that overexpress hamster PrP(C), PrP(C) overexpression accelerated recombinant PrP fibril-induced conversion of PrP(C) to the abnormal proteinase K-resistant state, referred to as atypical PrPres, which was the first product of PrP(C) misfolding in vivo. However, overexpression of PrP(C) did not facilitate the second step of synthetic strain evolution-transition from atypical PrPres to PrP(Sc), which is attributed to the stochastic nature of rare deformed templating events. In addition, the potential of atypical PrPres to interfere with replication of a short-incubation time prion strain was investigated. Atypical PrPres was found to interfere strongly with replication of 263K in vitro; however, it did not delay prion disease in animals. The rate of deformed templating does not depend on the concentration of substrate and is hence more likely to be controlled by the intrinsic rate of conformational errors in templating alternative self-propagating states.
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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.