Prions: Generation and spread versus neurotoxicity

32Citations
Citations of this article
135Readers
Mendeley users who have this article in their library.

Abstract

Neurodegenerative diseases are characterized by the aggregation of misfolded proteins in the brain. Among these disorders are the prion diseases, which are transmissible, and in which the misfolded proteins ("prions") are also the infectious agent. Increasingly, it appears that misfolded proteins in Alzheimer and Parkinson diseases and the tauopathies also propagate in a "prion-like" manner. However, the association between prion formation, spread, and neurotoxicity is not clear. Recently, we showed that in prion disease, protein misfolding leads to neurodegeneration through dysregulation of generic proteostatic mechanisms, specifically, the unfolded protein response. Geneticandpharmacological manipulation of the unfolded protein response was neuroprotective despite continuing prion replication, hence dissociating this from neurotoxicity. The data have clear implications for treatment across the spectrum of these disorders, targeting pathogenic processes downstream of protein misfolding. © 2014 by The American Society for Biochemistry and Molecular Biology, Inc.

Cite

CITATION STYLE

APA

Halliday, M., Radford, H., & Mallucci, G. R. (2014). Prions: Generation and spread versus neurotoxicity. Journal of Biological Chemistry. American Society for Biochemistry and Molecular Biology Inc. https://doi.org/10.1074/jbc.R114.568477

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free