Tuite, Mick F., Koloteva-Levine, Nadejda (2004) Propagating prions in fungi and mammals. Molecular Cell, 14 (5). pp. 541-552. ISSN 1097-2765. (doi:10.1016/j.molcel.2004.05.012) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided) (KAR id:11315)
The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided. | |
Official URL: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=... |
Abstract
Prions constitute a rare class of protein, which can switch to a robust amyloid form and then propagate that form in the absence of a nucleic acid determinant, thereby creating a unique, protein-only infectious agent. Details of the mechanism that drives conversion to the prion form and then subsequent propagation of that form are beginning to emerge using a range of in vivo and in vitro approaches. Recent studies on both mammalian and fungal prions are providing a greater understanding of the structural features that distinguish prions from non-transmissible amyloids.
Item Type: | Article |
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DOI/Identification number: | 10.1016/j.molcel.2004.05.012 |
Additional information: | 1097-2765 (Print) Journal Article Research Support, Non-U.S. Gov't Review |
Uncontrolled keywords: | Amyloid/metabolism Animals Cell-Free System Fungal Proteins/*metabolism Humans Mammals/*metabolism Models, Biological Prion Diseases/*metabolism/transmission Prions/chemistry/*metabolism Protein Folding Protein Structure, Tertiary/physiology |
Subjects: | Q Science > QR Microbiology |
Divisions: | Divisions > Division of Natural Sciences > Biosciences |
Depositing User: | Michael Tuite |
Date Deposited: | 02 Oct 2008 16:37 UTC |
Last Modified: | 05 Nov 2024 09:44 UTC |
Resource URI: | https://kar.kent.ac.uk/id/eprint/11315 (The current URI for this page, for reference purposes) |
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