ArticleBiochemistry2015
Requirements for mutant and wild-type prion protein misfolding in vitro.
Article in Biochemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 26 citations in OpenAlex.
- Phosphatidic Acid Vesicles Convert the Prion Protein into β-Sheet Fibrils with a Thermostable Structure but Temperature-Sensitive Packing.International journal of molecular sciences · 2026Article
- Fluorescent non-canonical amino acid as a site-specific conformational probe of prion formation.bioRxiv : the preprint server for biology · 2026Article
- D178N prion protein mutation endows RML prions with new strain properties that do not mimic human genetic prion diseases.Acta neuropathologica · 2026Article
- Mutant knock-in mice display enhanced susceptibility to pure prion protein fibrils.The Journal of general virology · 2026Article
- Diagnosis of Prion Diseases.Sub-cellular biochemistry · 2025Review
- Anti-prion drugs do not improve survival in novel knock-in models of inherited prion disease.PLoS pathogens · 2024Article
- Creutzfeldt-Jakob disease and other prion diseases.Nature reviews. Disease primers · 2024Review
- Conformational diversity in purified prions produced in vitro.PLoS pathogens · 2023Article
- What is the role of lipids in prion conversion and disease?Frontiers in molecular neuroscience · 2022Review
- Identification of a homology-independent linchpin domain controlling mouse and bank vole prion protein conversion.PLoS pathogens · 2020Article
- Cofactor molecules: Essential partners for infectious prions.Progress in molecular biology and translational science · 2020Review
- In Vitro Seeding Activity of Glycoform-Deficient Prions from Variably Protease-Sensitive Prionopathy and Familial CJD Associated with PrPMolecular neurobiology · 2019Article
- Mutations in Prion Protein Gene: Pathogenic Mechanisms in C-Terminal vs. N-Terminal Domain, a Review.International journal of molecular sciences · 2019Review
- Full restoration of specific infectivity and strain properties from pure mammalian prion protein.PLoS pathogens · 2019Article
- Artificial strain of human prions created in vitro.Nature communications · 2018Article
- PrP P102L and Nearby Lysine Mutations Promote SpontaneousJournal of virology · 2017Article
- Generation of a new infectious recombinant prion: a model to understand Gerstmann-Sträussler-Scheinker syndrome.Scientific reports · 2017Article
- Pre-amyloid oligomers of the proteotoxic RepA-WH1 prionoid assemble at the bacterial nucleoid.Scientific reports · 2015Article
- Expanding the prion disease repertoire.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- PrP charge structure encodes interdomain interactions.Scientific reports · 2015Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Misfolding of the prion protein (PrP) plays a central role in the pathogenesis of infectious, sporadic, and inherited prion diseases. Here we use a chemically defined prion propagation system to study misfolding of the pathogenic PrP mutant D177N in vitro. This mutation causes PrP to misfold spontaneously in the absence of cofactor molecules in a process dependent on time, temperature, pH, and intermittent sonication. Spontaneously misfolded mutant PrP is able to template its unique conformation onto wild-type PrP substrate in a process that requires a phospholipid activity distinct from that required for the propagation of infectious prions. Similar results were obtained with a second pathogenic PrP mutant, E199K, but not with the polymorphic substitution M128V. Moreover, wild-type PrP inhibits mutant PrP misfolding in a dose-dependent manner, and cofactor molecules can antagonize this effect. These studies suggest that interactions between mutant PrP, wild-type PrP, and other cellular factors may control the rate of PrP misfolding in inherited prion diseases.
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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.