ArticleProceedings of the National Academy of Sciences of the United States of America2013
Structural plasticity of the cellular prion protein and implications in health and disease.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- Different folding mechanisms in prion proteins from mammals with different disease susceptibility observed at the single-molecule level.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Conformational dynamics as an intrinsic determinant of prion protein misfolding and neurotoxicity.Neural regeneration research · 2024Article
- Emerging roles of the cellular prion protein (PrPCellular and molecular life sciences : CMLS · 2023Review
- Intrinsic determinants of prion protein neurotoxicity inFrontiers in molecular neuroscience · 2023Review
- Harnessing the Physiological Functions of Cellular Prion Protein in the Kidneys: Applications for Treating Renal Diseases.Biomolecules · 2021Review
- 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
- Structural effects of the highly protective V127 polymorphism on human prion protein.Communications biology · 2020Article
- Transition of the prion protein from a structured cellular form (PrPProtein science : a publication of the Protein Society · 2019Review
- Biological Spectrum of Amyotrophic Lateral Sclerosis Prions.Cold Spring Harbor perspectives in medicine · 2017Review
- Prion proteinProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Protease resistance of infectious prions is suppressed by removal of a single atom in the cellular prion protein.PloS one · 2017Article
- Complex folding and misfolding effects of deer-specific amino acid substitutions in the β2-α2 loop of murine prion protein.Scientific reports · 2015Article
- Prion Protein-Antibody Complexes Characterized by Chromatography-Coupled Small-Angle X-Ray Scattering.Biophysical journal · 2015Article
- Article
- Negative purifying selection drives prion and doppel protein evolution.Journal of molecular evolution · 2014Article
- 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
- The role of Cys179-Cys214 disulfide bond in the stability and folding of prion protein: insights from molecular dynamics simulations.Journal of molecular modeling · 2014Article
- Prion transmission prevented by modifying the β2-α2 loop structure of host PrPC.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2014Article
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Two lines of transgenic mice expressing mouse/elk and mouse/horse prion protein (PrP) hybrids, which both form a well-structured β2-α2 loop in the NMR structures at 20 °C termed rigid-loop cellular prion proteins (RL-PrP(C)), presented with accumulation of the aggregated scrapie form of PrP in brain tissue, and the mouse/elk hybrid has also been shown to develop a spontaneous transmissible spongiform encephalopathy. Independently, there is in vitro evidence for correlations between the amino acid sequence in the β2-α2 loop and the propensity for conformational transitions to disease-related forms of PrP. To further contribute to the structural basis for these observations, this paper presents a detailed characterization of RL-PrP(C) conformations in solution. A dynamic local conformational polymorphism involving the β2-α2 loop was found to be evolutionarily preserved among all mammalian species, including those species for which the WT PrP forms an RL-PrP(C). The interconversion between two ensembles of PrP(C) conformers that contain, respectively, a 310-helix turn or a type I β-turn structure of the β2-α2 loop, exposes two different surface epitopes, which are analyzed for their possible roles in the still evasive function of PrP(C) in healthy organisms and/or at the onset of a transmissible spongiform encephalopathy.
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