ArticleFEBS letters2009
The role of glycophosphatidylinositol anchor in the amplification of the scrapie isoform of prion protein in vitro.
Article in FEBS letters, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
What it found
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Who cites it
26 citing papers in PubMed.
- Conservation of strain properties of bank vole-adapted chronic wasting disease in the absence of glycosylation and membrane anchoring.Neurobiology of disease · 2025Article
- Synthesis of a Bifunctionalized Glycosylphosphatidylinositol (GPI) Anchor Useful for the Study of GPI Biology.Chemistry (Weinheim an der Bergstrasse, Germany) · 2023Article
- Ligands binding to the prion protein induce its proteolytic release with therapeutic potential in neurodegenerative proteinopathies.Science advances · 2021Article
- Prion protein-Semisynthetic prion protein (PrP) variants with posttranslational modifications.Journal of peptide science : an official publication of the European Peptide Society · 2019Review
- Full restoration of specific infectivity and strain properties from pure mammalian prion protein.PLoS pathogens · 2019Article
- Molecular and Clinical Aspects of Protein Aggregation Assays in Neurodegenerative Diseases.Molecular neurobiology · 2018Review
- Article
- Recombinant PrP and Its Contribution to Research on Transmissible Spongiform Encephalopathies.Pathogens (Basel, Switzerland) · 2017Review
- A Structural and Functional Comparison Between Infectious and Non-Infectious Autocatalytic Recombinant PrP Conformers.PLoS pathogens · 2015Article
- Article
- Shedding light on prion disease.Prion · 2015Article
- Article
- A C-terminal membrane anchor affects the interactions of prion proteins with lipid membranes.The Journal of biological chemistry · 2014Article
- Article
- Recombinant human prion protein inhibits prion propagation in vitro.Scientific reports · 2013Article
- Detection of the GPI-anchorless prion protein fragment PrP226* in human brain.BMC neurology · 2013Article
- High-resolution structure of infectious prion protein: the final frontier.Nature structural & molecular biology · 2012Review
- Article
- Article
- Cyclic amplification of prion protein misfolding.Methods in molecular biology (Clifton, N.J.) · 2012Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Transmissible spongiform encephalopathies are associated with an autocatalytic conversion of normal prion protein, PrP(C), to a protease-resistant form, PrPres. This autocatalytic reaction can be reproduced in vitro using a procedure called protein misfolding cyclic amplification (PMCA). Here we show that, unlike brain-derived PrP(C), bacterially-expressed recombinant prion protein (rPrP) is a poor substrate for PrPres amplification in a standard PMCA reaction. The differences between PrP(C) and rPrP appear to be due to the lack of the glycophosphatidylinositol anchor in the recombinant protein. These findings shed a new light on prion protein conversion process and have important implications for the efforts to generate synthetic prions for structural and biophysical studies.
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