ArticleProtein science : a publication of the Protein Society2017
Molecular dynamics simulations of early steps in RNA-mediated conversion of prions.
Article in Protein science : a publication of the Protein Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 12 citations in OpenAlex.
- Origin of life: β-sheet amyloid conformers as the primordial functional polymers on the early Earth and their role in the emergence of complex dynamic networks.FEBS letters · 2025Review
- Roles of Nucleic Acids in Protein Folding, Aggregation, and Disease.ACS chemical biology · 2024Review
- Early Stages of RNA-Mediated Conversion of Human Prions.The journal of physical chemistry. B · 2022Article
- The Way forward for the Origin of Life: Prions and Prion-Like Molecules First Hypothesis.Life (Basel, Switzerland) · 2021Article
- Prion protein PrP nucleic acid binding and mobilization implicates retroelements as the replicative component of transmissible spongiform encephalopathy.Archives of virology · 2020Review
- Amyloid and the origin of life: self-replicating catalytic amyloids as prebiotic informational and protometabolic entities.Cellular and molecular life sciences : CMLS · 2018Article
- Mutations Alter RNA-Mediated Conversion of Human Prions.ACS omega · 2018Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The rate-limiting step in prion diseases is the initial transition of a prion protein from its native form into a mis-folded state in which the protein not only forms cell-toxic aggregates but also becomes infectious. Recent experiments implicate polyadenosine RNA as a possible agent for generating the initial seed. In order to understand the mechanism of RNA-mediated mis-folding and aggregation of prions, we dock polyadenosine RNA to mouse and human prion models. Changes in stability and secondary structure of the prions upon binding to polyadenosine RNA are evaluated by comparing molecular dynamics simulations of these complexes with that of the unbound prions.
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