ArticleProceedings of the National Academy of Sciences of the United States of America2017
Prion protein dynamics before aggregation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 29 citations in OpenAlex.
- Different folding mechanisms in prion proteins from mammals with different disease susceptibility observed at the single-molecule level.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- [PSI]-CIC: A Deep-Learning Pipeline for the Annotation of Sectored Saccharomyces cerevisiae Colonies.Bulletin of mathematical biology · 2024Article
- Article
- Role of conformational dynamics in pathogenic protein aggregation.Current opinion in chemical biology · 2023Review
- Decreased Water Mobility Contributes To Increased α-Synuclein Aggregation.Angewandte Chemie (International ed. in English) · 2023Article
- Decreased Water Mobility Contributes To Increased α-Synuclein Aggregation.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2023Article
- The Proteome Folding Problem and Cellular Proteostasis.Journal of molecular biology · 2021Review
- Anti-prion Drugs Targeting the Protein Folding Activity of the Ribosome Reduce PABPN1 Aggregation.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2021Article
- Zinc determines dynamical properties and aggregation kinetics of human insulin.Biophysical journal · 2021Article
- Rabbit PrP Is Partially Resistant toFrontiers in neuroscience · 2021Article
- N-Terminal Decarboxylation as a Probe for Intramolecular Contact Formation in γ-Glu-(Pro)The journal of physical chemistry. B · 2020Article
- PrPSc Oligomerization Appears Dynamic, Quickly Engendering Inherent M1000 Acute Synaptotoxicity.Biophysical journal · 2020Article
- Hijacking Endocytosis and Autophagy in Extracellular Vesicle Communication: Where the Inside Meets the Outside.Frontiers in cell and developmental biology · 2020Review
- Microsecond sub-domain motions and the folding and misfolding of the mouse prion protein.eLife · 2019Article
- Vitamin D protects dopaminergic neurons against neuroinflammation and oxidative stress in hemiparkinsonian rats.Journal of neuroinflammation · 2018Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Prion diseases, like Alzheimer's disease and Parkinson disease, are rapidly progressive neurodegenerative disorders caused by misfolding followed by aggregation and accumulation of protein deposits in neuronal cells. Here we measure intramolecular polypeptide backbone reconfiguration as a way to understand the molecular basis of prion aggregation. Our hypothesis is that when reconfiguration is either much faster or much slower than bimolecular diffusion, biomolecular association is not stable, but as the reconfiguration rate becomes similar to the rate of biomolecular diffusion, the association is more stable and subsequent aggregation is faster. Using the technique of Trp-Cys contact quenching, we investigate the effects of various conditions on reconfiguration dynamics of the Syrian hamster and rabbit prion proteins. This protein exhibits behavior in all three reconfiguration regimes. We conclude that the hamster prion is prone to aggregation at pH 4.4 because its reconfiguration rate is slow enough to expose hydrophobic residues on the same time scale that bimolecular association occurs, whereas the rabbit sequence avoids aggregation by reconfiguring 10 times faster than the hamster sequence.
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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.