ArticleStructure (London, England : 1993)2013
Cofactor molecules induce structural transformation during infectious prion formation.
Article in Structure (London, England : 1993), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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Who cites it
48 citing papers in PubMed, 66 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
- Spontaneous generation of diverse recombinant prion strains: sulfated glycan cofactors facilitate strain emergence but do not determine specific strain properties.Acta neuropathologica communications · 2025Article
- Review
- Review
- Structural biology of ex vivo mammalian prions.The Journal of biological chemistry · 2022Review
- What is the role of lipids in prion conversion and disease?Frontiers in molecular neuroscience · 2022Review
- Structure of prion β-oligomers as determined by short-distance crosslinking constraint-guided discrete molecular dynamics simulations.Proteomics · 2021Article
- Brain Somatic Mutation in Aging and Alzheimer's Disease.Annual review of genomics and human genetics · 2021Review
- Evidence of distinct α-synuclein strains underlying disease heterogeneity.Acta neuropathologica · 2021Review
- Rabbit PrP Is Partially Resistant toFrontiers in neuroscience · 2021Article
- Comparative analysis of heparin affecting the biochemical properties of chicken and murine prion proteins.PloS one · 2021Article
- The Role of Vesicle Trafficking Defects in the Pathogenesis of Prion and Prion-Like Disorders.International journal of molecular sciences · 2020Review
- PrPSc Oligomerization Appears Dynamic, Quickly Engendering Inherent M1000 Acute Synaptotoxicity.Biophysical journal · 2020Article
- Cofactor and glycosylation preferences for in vitro prion conversion are predominantly determined by strain conformation.PLoS pathogens · 2020Article
- Unique Structural Features of Mule Deer Prion Protein Provide Insights into Chronic Wasting Disease.ACS omega · 2019Article
- Enhancement of binding avidity by bivalent binding enables PrPSc-specific detection by anti-PrP monoclonal antibody 132.PloS one · 2019Article
- Prion replication environment defines the fate of prion strain adaptation.PLoS pathogens · 2018Article
- Recombinant PrP and Its Contribution to Research on Transmissible Spongiform Encephalopathies.Pathogens (Basel, Switzerland) · 2017Review
- Role of the central lysine cluster and scrapie templating in the transmissibility of synthetic prion protein aggregates.PLoS pathogens · 2017Article
- Aβ seeds and prions: How close the fit?Prion · 2017Article
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
The spread of misfolded proteins may occur in many neurodegenerative diseases. Mammalian prions are currently the only misfolded proteins in which high specific biological infectivity can be produced in vitro. Using a system that generates infectious prions de novo from purified recombinant PrP and conversion cofactors palmitoyl-oleoyl-phosphatidylglycerol (POPG) and RNA, we examined by deuterium exchange mass spectrometry (DXMS) the stepwise protein conformational changes that occur during prion formation. We found that initial incubation with POPG causes major structural changes in PrP involving all three α helices and one β strand, with subsequent addition of RNA rendering the N terminus highly exposed. Final conversion into the infectious PrP(Sc) form was accompanied by globally decreased solvent exposure, with persistence of the major cofactor-induced conformational features. Thus, we report that cofactor molecules appear to induce major structural rearrangements during prion formation, initiating a dynamic sequence of conformational changes resulting in biologically active prions.
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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.