ArticleJournal of molecular biology2008
Conformational stability of PrP amyloid fibrils controls their smallest possible fragment size.
Article in Journal of molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
40 citing papers in PubMed, 69 citations in OpenAlex.
- Amyloids and prions in the light of evolution.Current genetics · 2023Review
- Prion strains: shining new light on old concepts.Cell and tissue research · 2023Review
- Role of sialylation of N-linked glycans in prion pathogenesis.Cell and tissue research · 2023Review
- Nucleation seed size determines amyloid clearance and establishes a barrier to prion appearance in yeast.Nature structural & molecular biology · 2020Article
- Thermostability as a highly dependent prion strain feature.Scientific reports · 2019Article
- Amyloid found in human cataracts with two-dimensional infrared spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Article
- Pathologic and biochemical characterization of PrPBMC veterinary research · 2018Article
- Enhanced neuroinvasion by smaller, soluble prions.Acta neuropathologica communications · 2017Article
- Purification and Fibrillation of Full-Length Recombinant PrP.Methods in molecular biology (Clifton, N.J.) · 2017Article
- Multifaceted Role of Sialylation in Prion Diseases.Frontiers in neuroscience · 2016Review
- Synthetic prions with novel strain-specified properties.PLoS pathogens · 2015Article
- Sialylation of the prion protein glycans controls prion replication rate and glycoform ratio.Scientific reports · 2015Article
- The diversity and relationship of prion protein self-replicating states.Virus research · 2015Review
- A human CCT5 gene mutation causing distal neuropathy impairs hexadecamer assembly in an archaeal model.Scientific reports · 2014Article
- Is supramolecular filament chirality the underlying cause of major morphology differences in amyloid fibrils?Journal of the American Chemical Society · 2014Article
- The effect of β2-α2 loop mutation on amyloidogenic properties of the prion protein.FEBS letters · 2013Article
- Different anti-aggregation and pro-degradative functions of the members of the mammalian sHSP family in neurological disorders.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2013Review
- Selective molecular recognition in amyloid growth and transmission and cross-species barriers.Journal of molecular biology · 2012Review
- Dissociation of recombinant prion protein fibrils into short protofilaments: implications for the endocytic pathway and involvement of the N-terminal domain.Biochemistry · 2012Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Fibril fragmentation is considered to be an essential step in prion replication. Recent studies have revealed a strong correlation between the incubation period to prion disease and conformational stability of synthetic prions. To gain insight into the molecular mechanism that accounts for this correlation, we proposed that the conformational stability of prion fibrils controls their intrinsic fragility or the size of the smallest possible fibrillar fragments. Using amyloid fibrils produced from full-length mammalian prion protein under three growth conditions, we found a correlation between conformational stability and the smallest possible fragment sizes. Specifically, the fibrils that were conformationally less stable were found to produce shorter pieces upon fragmentation. Site-specific denaturation experiments revealed that the fibril conformational stability was controlled by the region that acquires a cross-beta-sheet structure. Using atomic force microscopy imaging, we found that fibril fragmentation occurred in both directions--perpendicular to and along the fibrillar axis. Two mechanisms of fibril fragmentation were identified: (i) fragmentation caused by small heat shock proteins, including alpha B-crystallin, and (ii) fragmentation due to mechanical stress arising from adhesion of the fibril to a surface. This study provides new mechanistic insight into the prion replication mechanism and offers a plausible explanation for the correlation between conformational stability of synthetic prions and incubation time to prion disease.
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Registered trials
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.