ArticleThe Journal of biological chemistry2009
Conformational switching within individual amyloid fibrils.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 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.
The trial behind it
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
45 citing papers in PubMed, 67 citations in OpenAlex.
- Hidden faces of alpha-synuclein: Cryo-EM revelation of fibril polymorphs driven by disease, mutations, and PTMs.BBA advances · 2026Review
- Multiple aspects of amyloid dynamicsFrontiers in molecular neuroscience · 2024Article
- Polymorphism of Alpha-Synuclein Amyloid Fibrils Depends on Ionic Strength and Protein Concentration.International journal of molecular sciences · 2021Article
- Temperature-Dependent Structural Variability of Prion Protein Amyloid Fibrils.International journal of molecular sciences · 2021Article
- Cryo-EM reveals structural breaks in a patient-derived amyloid fibril from systemic AL amyloidosis.Nature communications · 2021Article
- Multistep Changes in Amyloid Structure Induced by Cross-Seeding on a Rugged Energy Landscape.Biophysical journal · 2021Article
- Self-Replication of Prion Protein Fragment 89-230 Amyloid Fibrils Accelerated by Prion Protein Fragment 107-143 Aggregates.International journal of molecular sciences · 2020Article
- Amyloid Evolution: Antiparallel Replaced by Parallel.Biophysical journal · 2020Article
- Direct observation of prion protein oligomer formation reveals an aggregation mechanism with multiple conformationally distinct species.Chemical science · 2019Article
- Seeding and cross-seeding fibrillation of N-terminal prion protein peptides PrP(120-144).Protein science : a publication of the Protein Society · 2018Article
- Formation and properties of amyloid fibrils of prion protein.Biophysical reviews · 2018Review
- Amyloidogenic cross-seeding of Tau protein: Transient emergence of structural variants of fibrils.PloS one · 2018Article
- Source genotype influence on cross species transmission of transmissible spongiform encephalopathies evaluated by RT-QuIC.PloS one · 2018Article
- Prion Strains and Transmission Barrier Phenomena.Pathogens (Basel, Switzerland) · 2018Review
- Amyloidogenesis of Tau protein.Protein science : a publication of the Protein Society · 2017Review
- Implications of peptide assemblies in amyloid diseases.Chemical Society reviews · 2017Review
- The emergence of superstructural order in insulin amyloid fibrils upon multiple rounds of self-seeding.Scientific reports · 2016Article
- New Molecular Insight into Mechanism of Evolution of Mammalian Synthetic Prions.The American journal of pathology · 2016Article
- Two alternative pathways for generating transmissible prion disease de novo.Acta neuropathologica communications · 2015Article
- The diversity and relationship of prion protein self-replicating states.Virus research · 2015Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
A key structural component of amyloid fibrils is a highly ordered, crystalline-like cross-beta-sheet core. Conformationally different amyloid structures can be formed within the same amino acid sequence. It is generally assumed that individual fibrils consist of conformationally uniform cross-beta-structures. Using mammalian recombinant prion protein (PrP), we showed that, contrary to common perception, amyloid is capable of accommodating a significant conformational switching within individual fibrils. The conformational switch occurred when the amino acid sequence of a PrP variant used as a precursor substrate in a fibrillation reaction was not compatible with the strain-specific conformation of the fibrillar template. Despite the mismatch in amino acid sequences between the substrate and template, individual fibrils recruited the heterologous PrP variant; however, the fibril elongation proceeded through a conformational adaptation, resulting in a change in amyloid strain within individual fibrils. This study illustrates the high adaptation potential of amyloid structures and suggests that conformational switching within individual fibrils may account for adaptation of amyloid strains to a heterologous substrate. This work proposes a new mechanistic explanation for the phenomenon of strain conversion and illustrates the direction in evolution of amyloid structures. This study also provides a direct illustration that catalytic activity of self-replicating amyloid structures is not ultimately coupled with their templating effect.
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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.