ArticleThe Journal of biological chemistry2010
Prion fibrillization is mediated by a native structural element that comprises helices H2 and H3.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 77 citations in OpenAlex.
- Fluorescent non-canonical amino acid as a site-specific conformational probe of prion formation.bioRxiv : the preprint server for biology · 2026Article
- Recognition Mechanisms between a Nanobody and Disordered Epitopes of the Human Prion Protein: An Integrative Molecular Dynamics Study.Journal of chemical information and modeling · 2023Article
- Structural biology of ex vivo mammalian prions.The Journal of biological chemistry · 2022Review
- Pathogenic prion structures at high resolution.PLoS pathogens · 2022Article
- Cellular prion protein gene polymorphisms linked to differential scrapie susceptibility correlate with distinct residue connectivity between secondary structure elements.Journal of biomolecular structure & dynamics · 2021Article
- Atomic insights into the effects of pathological mutants through the disruption of hydrophobic core in the prion protein.Scientific reports · 2019Article
- Detecting early stage structural changes in wild type, pathogenic and non-pathogenic prion variants using Markov state model.RSC advances · 2019Article
- Structural Determinants of the Prion Protein N-Terminus and Its Adducts with Copper Ions.International journal of molecular sciences · 2018Review
- Formation and properties of amyloid fibrils of prion protein.Biophysical reviews · 2018Review
- Article
- Reversible unfolding of infectious prion assemblies reveals the existence of an oligomeric elementary brick.PLoS pathogens · 2017Article
- Generating Bona Fide Mammalian Prions with Internal Deletions.Journal of virology · 2016Article
- Biochemical insight into the prion protein family.Frontiers in cell and developmental biology · 2015Review
- Acid-induced molten globule state of a prion protein: crucial role of Strand 1-Helix 1-Strand 2 segment.The Journal of biological chemistry · 2014Article
- Parallel in-register intermolecular β-sheet architectures for prion-seeded prion protein (PrP) amyloids.The Journal of biological chemistry · 2014Article
- Heparin binding confers prion stability and impairs its aggregation.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2014Article
- Molecular dynamics simulations capture the misfolding of the bovine prion protein at acidic pH.Biomolecules · 2014Article
- How does domain replacement affect fibril formation of the rabbit/human prion proteins.PloS one · 2014Article
- Probing early misfolding events in prion protein mutants by NMR spectroscopy.Molecules (Basel, Switzerland) · 2013Review
- Decrypting Prion Protein Conversion into a β-Rich Conformer by Molecular Dynamics.Journal of chemical theory and computation · 2013Article
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Authors and funding
8 authors at 2 institutions in 4 countries.
Funding
Abstract
Aggregation and misfolding of the prion protein (PrP) are thought to be the cause of a family of lethal neurodegenerative diseases affecting humans and other animals. Although the structures of PrP from several species have been solved, still little is known about the mechanisms that lead to the misfolded species. Here, we show that the region of PrP comprising the hairpin formed by the helices H2 and H3 is a stable independently folded unit able to retain its secondary and tertiary structure also in the absence of the rest of the sequence. We also prove that the isolated H2H3 is highly fibrillogenic and forms amyloid fibers morphologically similar to those obtained for the full-length protein. Fibrillization of H2H3 but not of full-length PrP is concomitant with formation of aggregates. These observations suggest a "banana-peeling" mechanism for misfolding of PrP in which H2H3 is the aggregation seed that needs to be first exposed to promote conversion from a helical to a beta-rich structure.
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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.