ArticleBiochemistry2011
Atomic structures suggest determinants of transmission barriers in mammalian prion disease.
Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 61 citations in OpenAlex.
- Cryo-EM structure of disease-related prion fibrils provides insights into seeding barriers.Nature structural & molecular biology · 2022Article
- Mapping the sequence specificity of heterotypic amyloid interactions enables the identification of aggregation modifiers.Nature communications · 2022Article
- RNA as the stone guest of protein aggregation.Nucleic acids research · 2020Review
- Cellular and Molecular Mechanisms of Prion Disease.Annual review of pathology · 2019Review
- Seeding and cross-seeding fibrillation of N-terminal prion protein peptides PrP(120-144).Protein science : a publication of the Protein Society · 2018Article
- Amyloid-Like β-Aggregates as Force-Sensitive Switches in Fungal Biofilms and Infections.Microbiology and molecular biology reviews : MMBR · 2018Review
- Towards the design of anti-amyloid short peptide helices.Bioinformation · 2018Article
- Asparagine and glutamine ladders promote cross-species prion conversion.The Journal of biological chemistry · 2017Article
- Implications of peptide assemblies in amyloid diseases.Chemical Society reviews · 2017Review
- Toward the Atomic Structure of PrPCold Spring Harbor perspectives in biology · 2017Review
- Structural Biology of PrP Prions.Cold Spring Harbor perspectives in medicine · 2017Review
- Review
- N-terminal Prion Protein Peptides (PrP(120-144)) Form Parallel In-register β-Sheets via Multiple Nucleation-dependent Pathways.The Journal of biological chemistry · 2016Article
- Human prion protein sequence elements impede cross-species chronic wasting disease transmission.The Journal of clinical investigation · 2015Article
- Structural studies of truncated forms of the prion protein PrP.Biophysical journal · 2015Article
- A proposed mechanism for the promotion of prion conversion involving a strictly conserved tyrosine residue in the β2-α2 loop of PrPC.The Journal of biological chemistry · 2014Article
- Article
- Molecular dynamics simulation of temperature induced unfolding of animal prion protein.Journal of molecular modeling · 2013Article
- The effect of β2-α2 loop mutation on amyloidogenic properties of the prion protein.FEBS letters · 2013Article
- Crystal structure of a human prion protein fragment reveals a motif for oligomer formation.Journal of the American Chemical Society · 2013Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Prion represents a unique class of pathogens devoid of nucleic acid. The deadly diseases transmitted by it between members of one species and, in certain instances, to members of other species present a public health concern. Transmissibility and the barriers to transmission between species have been suggested to arise from the degree to which a pathological protein conformation from an individual of one species can seed a pathological conformation in another species. However, this hypothesis has never been illustrated at an atomic level. Here we present three X-ray atomic structures of the same segment from human, mouse, and hamster PrP, which is critical for forming amyloid and confers species specificity in PrP seeding experiments. The structures reveal that different sequences encode different steric zippers and suggest that the degree of dissimilarity of these zipper structures gives rise to transmission barriers in prion disease, such as those that protect humans from acquiring bovine spongiform encephalopathy (BSE) and chronic wasting disease (CWD).
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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.