Methionine oxidation within the prion protein.

ABSTRACT: Prion diseases are characterized by the self-templated misfolding of the cellular prion protein (PrP^C) into infectious aggregates (PrP^Sc). The detailed molecular basis of the misfolding and aggregation of PrP^C remains incompletely understood. It is believed that the transient misfolding of PrP^C into partially structured intermediates precedes the formation of insoluble protein aggregates and is a critical component of the prion misfolding pathway. A number of environmental factors have been shown to induce the destabilization of PrP^C and promote its initial misfolding. Recently, oxidative stress and reactive oxygen species (ROS) have emerged as one possible mechanism by which the destabilization of PrP^C can be induced under

SUBMITTER: Bettinger J 

PROVIDER: S-EPMC7518762 | biostudies-literature | 2020 Dec

REPOSITORIES: biostudies-literature