ArticlePeerJ2015
Polymorphism of amyloid-like fibrils can be defined by the concentration of seeds.
Article in PeerJ, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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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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Who cites it
12 citing papers in PubMed, 29 citations in OpenAlex.
- On the reversibility of amyloid fibril formation.Biophysics reviews · 2025Review
- Quaternary structure of patient-homogenate amplified α-synuclein fibrils modulates seeding of endogenous α-synuclein.Communications biology · 2022Article
- Stability matters, too - the thermodynamics of amyloid fibril formation.Chemical science · 2022Review
- Article
- Aggregation Condition-Structure Relationship of Mouse Prion Protein Fibrils.International journal of molecular sciences · 2021Article
- Temperature-Dependent Structural Variability of Prion Protein Amyloid Fibrils.International journal of molecular sciences · 2021Article
- Secondary Nucleation and the Conservation of Structural Characteristics of Amyloid Fibril Strains.Frontiers in molecular biosciences · 2021Review
- Self-Replication of Prion Protein Fragment 89-230 Amyloid Fibrils Accelerated by Prion Protein Fragment 107-143 Aggregates.International journal of molecular sciences · 2020Article
- Formation of distinct prion protein amyloid fibrils under identical experimental conditions.Scientific reports · 2020Article
- The Environment Is a Key Factor in Determining the Anti-Amyloid Efficacy of EGCG.Biomolecules · 2019Article
- Article
- Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Prions are infectious proteins where the same protein may express distinct strains. The strains are enciphered by different misfolded conformations. Strain-like phenomena have also been reported in a number of other amyloid-forming proteins. One of the features of amyloid strains is the ability to self-propagate, maintaining a constant set of physical properties despite being propagated under conditions different from those that allowed initial formation of the strain. Here we report a cross-seeding experiment using strains formed under different conditions. Using high concentrations of seeds results in rapid elongation and new fibrils preserve the properties of the seeding fibrils. At low seed concentrations, secondary nucleation plays the major role and new fibrils gain properties predicted by the environment rather than the structure of the seeds. Our findings could explain conformational switching between amyloid strains observed in a wide variety of in vivo and in vitro experiments.
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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.