ArticleBiophysical journal2012
Degradation of fungal prion HET-s(218-289) induces formation of a generic amyloid fold.
Article in Biophysical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 25 citations in OpenAlex.
- A model-based prion vaccine protects a transgenic mouse line carrying a Gerstmann-Sträussler-Scheinker disease mutation.Acta neuropathologica · 2026Article
- Rational design of structure-based vaccines targeting misfolded alpha-synuclein conformers of Parkinson's disease and related disorders.Bioengineering & translational medicine · 2024Article
- Amyloids: The History of Toxicity and Functionality.Biology · 2021Review
- Comparing the Folds of Prions and Other Pathogenic Amyloids.Pathogens (Basel, Switzerland) · 2018Review
- The Structure of PrPPathogens (Basel, Switzerland) · 2018Review
- Recombinant PrPSc shares structural features with brain-derived PrPSc: Insights from limited proteolysis.PLoS pathogens · 2018Article
- A 31-residue peptide induces aggregation of tau's microtubule-binding region in cells.Nature chemistry · 2017Article
- Structural Biology of PrP Prions.Cold Spring Harbor perspectives in medicine · 2017Review
- Protein folding, misfolding and aggregation: The importance of two-electron stabilizing interactions.PloS one · 2017Article
- Rapid Filament Supramolecular Chirality Reversal of HET-s (218-289) Prion Fibrils Driven by pH Elevation.The journal of physical chemistry. B · 2015Article
- Structural studies of truncated forms of the prion protein PrP.Biophysical journal · 2015Article
- Truncated forms of the prion protein PrP demonstrate the need for complexity in prion structure.Prion · 2015Article
- Contribution of specific residues of the β-solenoid fold to HET-s prion function, amyloid structure and stability.PLoS pathogens · 2014Article
- Fiber diffraction of the prion-forming domain HET-s(218-289) shows dehydration-induced deformation of a complex amyloid structure.Biochemistry · 2014Article
- Fungal prion HET-s as a model for structural complexity and self-propagation in prions.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Heterogeneous seeding of a prion structure by a generic amyloid form of the fungal prion-forming domain HET-s(218-289).The Journal of biological chemistry · 2013Article
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6 authors at 3 institutions in 1 country.
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Abstract
The prion-forming domain of the fungal prion protein HET-s, HET-s(218-289), is known from solid-state NMR studies to have a β-solenoidal structure; the β-solenoid has the cross-β structure characteristic of all amyloids, but is inherently more complex than the generic stacked β-sheets found in studies of small synthetic peptides. At low pH HET-s(218-289) has also been reported to form an alternative structure, which has not been characterized. We have confirmed by x-ray fiber diffraction that HET-s(218-289) adopts a β-solenoidal structure at neutral pH, and shown that at low pH, it forms either a β-solenoid or a stacked β-sheet structure, depending on the integrity of the protein and the conditions of fibrillization. The low pH stacked-sheet structure is usually formed only by proteolyzed HET-s(218-289), but intact HET-s(218-289) can form stacked sheets when seeded with proteolyzed stacked-sheet HET-s(218-289). The polymorphism of HET-s parallels the structural differences between the infectious brain-derived and the much less infectious recombinant mammalian prion protein PrP. Taken together, these observations suggest that the functional or pathological forms of amyloid proteins are more complex than the simple generic stacked-sheet amyloids commonly formed by short peptides.
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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.