ArticleThe Journal of biological chemistry2011
Amyloid features and neuronal toxicity of mature prion fibrils are highly sensitive to high pressure.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 23 citations in OpenAlex.
- Broken but not beaten: Challenge of reducing the amyloids pathogenicity by degradation.Journal of advanced research · 2025Review
- Neurotoxic amyloidogenic peptides in the proteome of SARS-COV2: potential implications for neurological symptoms in COVID-19.Nature communications · 2022Article
- High-Pressure Response of Amyloid Folds.Viruses · 2019Review
- Pressure Reveals Unique Conformational Features in Prion Protein Fibril Diversity.Scientific reports · 2019Article
- Low doses of bioherbicide favour prion aggregation and propagation in vivo.Scientific reports · 2018Article
- Nonequilibrium all-atom molecular dynamics simulation of the bubble cavitation and application to dissociate amyloid fibrils.The Journal of chemical physics · 2016Article
- Article
- The Volumetric Diversity of Misfolded Prion Protein Oligomers Revealed by Pressure Dissociation.The Journal of biological chemistry · 2015Article
- Interaction of prion protein with acetylcholinesterase: potential pathobiological implications in prion diseases.Acta neuropathologica communications · 2015Article
- On the heat stability of amyloid-based biological activity: insights from thermal degradation of insulin fibrils.PloS one · 2014Article
- Cell-penetrating peptide secures an efficient endosomal escape of an intact cargo upon a brief photo-induction.Cellular and molecular life sciences : CMLS · 2013Article
- High pressure, a tool to switch between soluble and fibrillar prion protein structures.Communicative & integrative biology · 2012Article
Corrections and comments
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Authors and funding
8 authors at 4 institutions in 3 countries.
Funding
Abstract
Prion proteins (PrP) can aggregate into toxic and possibly infectious amyloid fibrils. This particular macrostructure confers on them an extreme and still unexplained stability. To provide mechanistic insights into this self-assembly process, we used high pressure as a thermodynamic tool for perturbing the structure of mature amyloid fibrils that were prepared from recombinant full-length mouse PrP. Application of high pressure led to irreversible loss of several specific amyloid features, such as thioflavin T and 8-anilino-1-naphthalene sulfonate binding, alteration of the characteristic proteinase K digestion pattern, and a significant decrease in the β-sheet structure and cytotoxicity of amyloid fibrils. Partial disaggregation of the mature fibrils into monomeric soluble PrP was observed. The remaining amyloid fibrils underwent a change in secondary structure that led to morphologically different fibrils composed of a reduced number of proto-filaments. The kinetics of these reactions was studied by recording the pressure-induced dissociation of thioflavin T from the amyloid fibrils. Analysis of the pressure and temperature dependence of the relaxation rates revealed partly unstructured and hydrated kinetic transition states and highlighted the importance of collapsing and hydrating inter- and intramolecular cavities to overcome the high free energy barrier that stabilizes amyloid fibrils.
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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.