ArticleThe Journal of biological chemistry2014
Conformational stability of mammalian prion protein amyloid fibrils is dictated by a packing polymorphism within the core region.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
33 citing papers in PubMed, 54 citations in OpenAlex.
- Phosphatidic Acid Vesicles Convert the Prion Protein into β-Sheet Fibrils with a Thermostable Structure but Temperature-Sensitive Packing.International journal of molecular sciences · 2026Article
- Hidden faces of alpha-synuclein: Cryo-EM revelation of fibril polymorphs driven by disease, mutations, and PTMs.BBA advances · 2026Review
- Significance of Histidine Hydrogen-Deuterium Exchange Mass Spectrometry in Protein Structural Biology.Biology · 2024Review
- Polymorphism of Alpha-Synuclein Amyloid Fibrils Depends on Ionic Strength and Protein Concentration.International journal of molecular sciences · 2021Article
- Structure of prion β-oligomers as determined by short-distance crosslinking constraint-guided discrete molecular dynamics simulations.Proteomics · 2021Article
- Genetic prion disease-related mutation E196K displays a novel amyloid fibril structure revealed by cryo-EM.Science advances · 2021Article
- 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
- Liquid-Liquid Phase Separation and Its Mechanistic Role in Pathological Protein Aggregation.Journal of molecular biology · 2020Review
- Formation of distinct prion protein amyloid fibrils under identical experimental conditions.Scientific reports · 2020Article
- Cross-Species and Cross-Polymorph Seeding of Lysozyme Amyloid Reveals a Dominant Polymorph.Frontiers in molecular biosciences · 2020Article
- Stable Deuterium Labeling of Histidine-Rich Lysine-Based Dendrimers.Molecules (Basel, Switzerland) · 2019Article
- Article
- Article
- Structural attributes of mammalian prion infectivity: Insights from studies with synthetic prions.The Journal of biological chemistry · 2018Article
- Amyloid by Design: Intrinsic Regulation of Microbial Amyloid Assembly.Journal of molecular biology · 2018Review
- Artificial strain of human prions created in vitro.Nature communications · 2018Article
- Prion Strains and Transmission Barrier Phenomena.Pathogens (Basel, Switzerland) · 2018Review
- Production of Monoclonal Antibodies to Pathologic β-sheet Oligomeric Conformers in Neurodegenerative Diseases.Scientific reports · 2017Article
- Self-propagating, protease-resistant, recombinant prion protein conformers with or without in vivo pathogenicity.PLoS pathogens · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Mammalian prion strains are believed to arise from the propagation of distinct conformations of the misfolded prion protein PrP(Sc). One key operational parameter used to define differences between strains has been conformational stability of PrP(Sc) as defined by resistance to thermal and/or chemical denaturation. However, the structural basis of these stability differences is unknown. To bridge this gap, we have generated two strains of recombinant human prion protein amyloid fibrils that show dramatic differences in conformational stability and have characterized them by a number of biophysical methods. Backbone amide hydrogen/deuterium exchange experiments revealed that, in sharp contrast to previously studied strains of infectious amyloid formed from the yeast prion protein Sup35, differences in β-sheet core size do not underlie differences in conformational stability between strains of mammalian prion protein amyloid. Instead, these stability differences appear to be dictated by distinct packing arrangements (i.e. steric zipper interfaces) within the amyloid core, as indicated by distinct x-ray fiber diffraction patterns and large strain-dependent differences in hydrogen/deuterium exchange kinetics for histidine side chains within the core region. Although this study was limited to synthetic prion protein amyloid fibrils, a similar structural basis for strain-dependent conformational stability may apply to brain-derived PrP(Sc), especially because large strain-specific differences in PrP(Sc) stability are often observed despite a similar size of the PrP(Sc) core region.
Indexed as
Identifiers
What OpenQuestion holds
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.