A mathematical model of the dynamics of prion aggregates with chaperone-mediated fragmentation.

ABSTRACT: Prions are proteins most commonly associated with fatal neurodegenerative diseases in mammals but are also responsible for a number of harmless heritable phenotypes in yeast. These states arise when a misfolded form of a protein appears and, rather than be removed by cellular quality control mechanisms, persists. The misfolded prion protein forms aggregates and is capable of converting normally folded protein to the misfolded state through direct interaction between the two forms. The dominant mathematical model for prion aggregate dynamics has been the nucleated polymerization model (NPM) which considers the dynamics of only the normal protein and the aggregates. However, for yeast prions the molecular chaperone Hsp104 is essential for prion propagation. Further, although mammals do not e

SUBMITTER: Davis JK 

PROVIDER: S-EPMC4823377 | biostudies-literature | 2016 May

REPOSITORIES: biostudies-literature