ArticleInternational journal of molecular sciences2021
Temperature-Dependent Structural Variability of Prion Protein Amyloid Fibrils.
Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 37 citations in OpenAlex.
- Apolipoprotein D acts as a chaperone of Aβ peptide delaying its assembly into amyloid aggregates.Cellular and molecular life sciences : CMLS · 2026Article
- Recent Advances in Amyloids Structural Studies and Thin Film Applications.Molecules (Basel, Switzerland) · 2025Review
- Broken but not beaten: Challenge of reducing the amyloids pathogenicity by degradation.Journal of advanced research · 2025Review
- Preventing Protein Self-Association Through Strategic Covalent Modification.Journal of peptide science : an official publication of the European Peptide Society · 2025Article
- Solvent induced amyloid polymorphism and the uncovering of the elusive class 3 amyloid topology.Communications biology · 2024Article
- Article
- Investigating lysozyme amyloid fibril formation and structural variability dependence on its initial folding state under different pH conditions.Protein science : a publication of the Protein Society · 2024Article
- Realization of Amyloid-like Aggregation as a Common Cause for Pathogenesis in Diseases.Life (Basel, Switzerland) · 2023Review
- Conformation-Specific Association of Prion Protein Amyloid Aggregates with Tau Protein Monomers.International journal of molecular sciences · 2023Article
- Direct Observation of Competing Prion Protein Fibril Populations with Distinct Structures and Kinetics.ACS nano · 2023Article
- Article
- Aminoquinolones and Their Benzoquinone Dimer Hybrids as Modulators of Prion Protein Conversion.Molecules (Basel, Switzerland) · 2022Article
- Lysozyme Amyloid Fibril Structural Variability Dependence on Initial Protein Folding State.International journal of molecular sciences · 2022Article
- Article
- Interplay between epigallocatechin-3-gallate and ionic strength during amyloid aggregation.PeerJ · 2021Article
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Authors and funding
5 authors at 1 institution in 1 country.
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Abstract
Prion protein aggregation into amyloid fibrils is associated with the onset and progression of prion diseases-a group of neurodegenerative amyloidoses. The process of such aggregate formation is still not fully understood, especially regarding their polymorphism, an event where the same type of protein forms multiple, conformationally and morphologically distinct structures. Considering that such structural variations can greatly complicate the search for potential antiamyloid compounds, either by having specific propagation properties or stability, it is important to better understand this aggregation event. We have recently reported the ability of prion protein fibrils to obtain at least two distinct conformations under identical conditions, which raised the question if this occurrence is tied to only certain environmental conditions. In this work, we examined a large sample size of prion protein aggregation reactions under a range of temperatures and analyzed the resulting fibril dye-binding, secondary structure and morphological properties. We show that all temperature conditions lead to the formation of more than one fibril type and that this variability may depend on the state of the initial prion protein molecules.
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