ArticleProceedings of the National Academy of Sciences of the United States of America2016
Amyloid fibrils from the N-terminal prion protein fragment are infectious.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed, 85 citations in OpenAlex.
- Prions and protein aggregates as pathogens, self-propagating structures, biomarkers, and therapeutic targets.Microbiology and molecular biology reviews : MMBR · 2025Review
- The Glycine-Rich Region as a Flexible Molecular Glue Promoting hPrPJournal of chemical information and modeling · 2025Article
- Cofactors facilitate bona fide prion misfolding in vitro but are not necessary for the infectivity of recombinant murine prions.PLoS pathogens · 2025Article
- Article
- Understanding the key features of the spontaneous formation of bona fide prions through a novel methodology that enables their swift and consistent generation.Acta neuropathologica communications · 2023Article
- Anchorless risk or released benefit? An updated view on the ADAM10-mediated shedding of the prion protein.Cell and tissue research · 2023Review
- Prion assemblies: structural heterogeneity, mechanisms of formation, and role in species barrier.Cell and tissue research · 2023Review
- Prion strains viewed through the lens of cryo-EM.Cell and tissue research · 2023Review
- Conversion of Helix 1 into a Loop in Prion Protein Misfolding.ACS omega · 2023Article
- Cryo-EM structure of disease-related prion fibrils provides insights into seeding barriers.Nature structural & molecular biology · 2022Article
- Amyloidogenesis via interfacial shear in a containerless biochemical reactor aboard the International Space Station.NPJ microgravity · 2022Article
- Article
- Review
- Structural biology of ex vivo mammalian prions.The Journal of biological chemistry · 2022Review
- Pathogenic prion structures at high resolution.PLoS pathogens · 2022Article
- Influence of the Dynamically Disordered N-Terminal Tail Domain on the Amyloid Core Structure of Human Y145Stop Prion Protein Fibrils.Frontiers in molecular biosciences · 2022Article
- Structural consequences of sequence variation in mammalian prion β2α2 loop segments.Frontiers in neuroscience · 2022Article
- Structurally distinct external solvent-exposed domains drive replication of major human prions.PLoS pathogens · 2021Article
- Two distinct conformers of PrPActa neuropathologica communications · 2021Article
- A seven-residue deletion in PrP leads to generation of a spontaneous prion formed from C-terminal C1 fragment of PrP.The Journal of biological chemistry · 2020Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Recombinant C-terminally truncated prion protein PrP23-144 (which corresponds to the Y145Stop PrP variant associated with a Gerstmann-Sträussler-Scheinker-like prion disease) spontaneously forms amyloid fibrils with a parallel in-register β-sheet architecture and β-sheet core mapping to residues ∼112-139. Here we report that mice (both tga20 and wild type) inoculated with a murine (moPrP23-144) version of these fibrils develop clinical prion disease with a 100% attack rate. Remarkably, even though fibrils in the inoculum lack the entire C-terminal domain of PrP, brains of clinically sick mice accumulate longer proteinase K-resistant (PrP
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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.