ArticleBiochemistry2012
Dissociation of recombinant prion protein fibrils into short protofilaments: implications for the endocytic pathway and involvement of the N-terminal domain.
Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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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
6 citing papers in PubMed.
- Direct Observation of Murine Prion Protein Replication in Vitro.Journal of the American Chemical Society · 2018Article
- PrP charge structure encodes interdomain interactions.Scientific reports · 2015Article
- Charge neutralization of the central lysine cluster in prion protein (PrP) promotes PrP(Sc)-like folding of recombinant PrP amyloids.The Journal of biological chemistry · 2015Article
- Live imaging of prions reveals nascent PrPSc in cell-surface, raft-associated amyloid strings and webs.The Journal of cell biology · 2014Article
- Novel insights into amylin aggregation.Biotechnology, biotechnological equipment · 2014Article
- Mouse prion protein polymorphism Phe-108/Val-189 affects the kinetics of fibril formation and the response to seeding: evidence for a two-step nucleation polymerization mechanism.The Journal of biological chemistry · 2013Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Fibril dissociation is necessary for efficient conversion of normal prion protein to its misfolded state and continued propagation into amyloid. Recent studies have revealed that conversion occurs along the endocytic pathway. To improve our understanding of the dissociation process, we have investigated the effect of low pH on the stability of recombinant prion fibrils. We show that under conditions that mimic the endocytic environment, amyloid fibrils made from full-length prion protein dissociate both laterally and axially to form protofilaments. Approximately 5% of the protofilaments are short enough to be considered soluble and contain ~100-300 monomers per structure; these also retain the biophysical characteristics of the filaments. We propose that protonation of His residues and charge repulsion in the N-terminal domain trigger fibril dissociation. Our data suggest that lysosomes and late endosomes are competent milieus for propagating the misfolded state not only by destabilizing the normal prion protein but also by accelerating the dissociation of fibrils into smaller structures that may act as seeds.
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Registered trials
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