Tuite, M.F. and Koloteva-Levine, N. (2004) Propagating prions in fungi and mammals. Molecular Cell, 14 (5). pp. 541-552. ISSN 1097-2765.
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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.
|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:||Faculties > Science Technology and Medical Studies > School of Biosciences > Protein Science Group|
|Depositing User:||Mick Tuite|
|Date Deposited:||02 Oct 2008 16:37|
|Last Modified:||31 Jul 2012 07:58|
|Resource URI:||http://kar.kent.ac.uk/id/eprint/11315 (The current URI for this page, for reference purposes)|
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