ArticleJournal of chemical theory and computation2013
Decrypting Prion Protein Conversion into a β-Rich Conformer by Molecular Dynamics.
Article in Journal of chemical theory and computation, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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Who cites it
11 citing papers in PubMed.
- Conversion of Helix 1 into a Loop in Prion Protein Misfolding.ACS omega · 2023Article
- Synthetic Sulfated Polymers Control Amyloid Aggregation of Ovine Prion Protein and Decrease Its Toxicity.Polymers · 2022Article
- Identification of Two Early Folding Stage Prion Non-Local Contacts Suggested to Serve as Key Steps in Directing the Final Fold to Be Either Native or Pathogenic.International journal of molecular sciences · 2021Article
- Cellular prion protein gene polymorphisms linked to differential scrapie susceptibility correlate with distinct residue connectivity between secondary structure elements.Journal of biomolecular structure & dynamics · 2021Article
- Natural and Synthetic Derivatives of Hydroxycinnamic Acid Modulating the Pathological Transformation of Amyloidogenic Proteins.Molecules (Basel, Switzerland) · 2020Review
- Insights into the Bidirectional Properties of the Sheep-Deer Prion Transmission Barrier.Molecular neurobiology · 2019Review
- Structural basis for the complete resistance of the human prion protein mutant G127V to prion disease.Scientific reports · 2018Article
- Effects of pH and aggregation in the human prion conversion into scrapie form: a study using molecular dynamics with excited normal modes.European biophysics journal : EBJ · 2018Article
- Monitoring Conformational Landscape of Ovine Prion Protein Monomer Using Ion Mobility Coupled to Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2017Article
- Generating Bona Fide Mammalian Prions with Internal Deletions.Journal of virology · 2016Article
- Urea-Water Solvation Forces on Prion Structures.Journal of chemical theory and computation · 2012Article
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Prion diseases are fatal neurodegenerative diseases characterized by the formation of β-rich oligomers and the accumulation of amyloid fibrillar deposits in the central nervous system. Understanding the conversion of the cellular prion protein into its β-rich polymeric conformers is fundamental to tackling the early stages of the development of prion diseases. In this paper, we have identified unfolding and refolding steps critical to the conversion into a β-rich conformer for different constructs of the ovine prion protein by molecular dynamics simulations. By combining our results with
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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.