ArticleBiophysical journal2011
Fibril formation of the rabbit/human/bovine prion proteins.
Article in Biophysical journal, 2011. 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, 55 citations in OpenAlex.
- Underestimated role of macromolecular crowding in bioengineeredMaterials today. Bio · 2025Article
- Excess PrPNature communications · 2023Article
- Genetic prion disease-related mutation E196K displays a novel amyloid fibril structure revealed by cryo-EM.Science advances · 2021Article
- Cryo-EM structure of an amyloid fibril formed by full-length human prion protein.Nature structural & molecular biology · 2020Article
- Glycosylation Significantly Inhibits the Aggregation of Human Prion Protein and Decreases Its Cytotoxicity.Scientific reports · 2018Article
- Discovery of small molecules binding to the normal conformation of prion by combining virtual screening and multiple biological activity evaluation methods.Journal of computer-aided molecular design · 2017Article
- Prion protein dynamics before aggregation.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Unique Properties of the Rabbit Prion Protein Oligomer.PloS one · 2016Article
- The Unexposed Secrets of Prion Protein Oligomers.Journal of molecular neuroscience : MN · 2015Review
- pH responsiveness of fibrous assemblies of repeat-sequence amphipathic α-helix polypeptides.Protein science : a publication of the Protein Society · 2015Article
- Progress on low susceptibility mechanisms of transmissible spongiform encephalopathies.Dong wu xue yan jiu = Zoological research · 2014Review
- How does domain replacement affect fibril formation of the rabbit/human prion proteins.PloS one · 2014Article
- The role of crowded physiological environments in prion and prion-like protein aggregation.International journal of molecular sciences · 2013Review
- Cupric ions induce the oxidation and trigger the aggregation of human superoxide dismutase 1.PloS one · 2013Article
- Protein disulfide isomerase interacts with tau protein and inhibits its fibrillization.PloS one · 2013Article
- Fibril-forming motifs are essential and sufficient for the fibrillization of human Tau.PloS one · 2012Article
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Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Prion diseases are infectious fatal neurodegenerative diseases including Creutzfeldt-Jakob disease in humans and bovine spongiform encephalopathy in cattle. The misfolding and conversion of cellular PrP in such mammals into pathogenic PrP is believed to be the key procedure. Rabbits are among the few mammalian species that exhibit resistance to prion diseases, but little is known about the molecular mechanism underlying such resistance. Here, we report that the crowding agents Ficoll 70 and dextran 70 have different effects on fibrillization of the recombinant full-length PrPs from different species: although these agents dramatically promote fibril formation of the proteins from human and cow, they significantly inhibit fibrillization of the rabbit protein by stabilizing its native state. We also find that fibrils formed by the rabbit protein contain less β-sheet structure and more α-helix structure than those formed by the proteins from human and cow. In addition, amyloid fibrils formed by the rabbit protein do not generate a proteinase K-resistant fragment of 15-16-kDa, but those formed by the proteins from human and cow generate such proteinase K-resistant fragments. Together, these results suggest that the strong inhibition of fibrillization of the rabbit PrP by the crowded physiological environment and the absence of such a protease-resistant fragment for the rabbit protein could be two of the reasons why rabbits are resistant to prion diseases.
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