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Mutations Alter RNA-Mediated Conversion of Human Prions
[Image: see text] Prion diseases are connected with self-replication and self-propagation of misfolded proteins. The rate-limiting factor is the formation of the initial seed. We have recently studied the early stages in the conversion between functional PrP(C) and the infectious scrapie PrP(SC) for...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical Society
2018
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5928492/ https://www.ncbi.nlm.nih.gov/pubmed/29732450 http://dx.doi.org/10.1021/acsomega.7b02007 |
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author | Alred, Erik J. Lodangco, Izra Gallaher, Jennifer Hansmann, Ulrich H.E. |
author_facet | Alred, Erik J. Lodangco, Izra Gallaher, Jennifer Hansmann, Ulrich H.E. |
author_sort | Alred, Erik J. |
collection | PubMed |
description | [Image: see text] Prion diseases are connected with self-replication and self-propagation of misfolded proteins. The rate-limiting factor is the formation of the initial seed. We have recently studied the early stages in the conversion between functional PrP(C) and the infectious scrapie PrP(SC) form, triggered by the binding of RNA. Here, we study how this process is modulated by the prion sequence. We focus on residues 129 and 178, which are connected to the hereditary neurodegenerative disease fatal familial insomnia. |
format | Online Article Text |
id | pubmed-5928492 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | American Chemical Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-59284922018-05-02 Mutations Alter RNA-Mediated Conversion of Human Prions Alred, Erik J. Lodangco, Izra Gallaher, Jennifer Hansmann, Ulrich H.E. ACS Omega [Image: see text] Prion diseases are connected with self-replication and self-propagation of misfolded proteins. The rate-limiting factor is the formation of the initial seed. We have recently studied the early stages in the conversion between functional PrP(C) and the infectious scrapie PrP(SC) form, triggered by the binding of RNA. Here, we study how this process is modulated by the prion sequence. We focus on residues 129 and 178, which are connected to the hereditary neurodegenerative disease fatal familial insomnia. American Chemical Society 2018-04-09 /pmc/articles/PMC5928492/ /pubmed/29732450 http://dx.doi.org/10.1021/acsomega.7b02007 Text en Copyright © 2018 American Chemical Society This is an open access article published under an ACS AuthorChoice License (http://pubs.acs.org/page/policy/authorchoice_termsofuse.html) , which permits copying and redistribution of the article or any adaptations for non-commercial purposes. |
spellingShingle | Alred, Erik J. Lodangco, Izra Gallaher, Jennifer Hansmann, Ulrich H.E. Mutations Alter RNA-Mediated Conversion of Human Prions |
title | Mutations Alter RNA-Mediated Conversion of Human Prions |
title_full | Mutations Alter RNA-Mediated Conversion of Human Prions |
title_fullStr | Mutations Alter RNA-Mediated Conversion of Human Prions |
title_full_unstemmed | Mutations Alter RNA-Mediated Conversion of Human Prions |
title_short | Mutations Alter RNA-Mediated Conversion of Human Prions |
title_sort | mutations alter rna-mediated conversion of human prions |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5928492/ https://www.ncbi.nlm.nih.gov/pubmed/29732450 http://dx.doi.org/10.1021/acsomega.7b02007 |
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