Ontology highlight
ABSTRACT:
SUBMITTER: Myeku N
PROVIDER: S-EPMC5905406 | biostudies-literature | 2018 Jan
REPOSITORIES: biostudies-literature
Myeku Natura N Duff Karen E KE
Trends in molecular medicine 20171209 1
Aggregates of misfolded proteins can compromise the function of the 26S proteasome complex, leaving neurons susceptible to accelerated and impaired protein homeostasis, thereby contributing to the pathogenesis of neurodegeneration. Strategies aimed at enhancing the function of the 26S proteasome via phosphorylation of key subunit epitopes have been effective in reducing protein aggregates in mouse models of disease. We discuss how phosphodiesterase (PDE) inhibitors and G protein-coupled receptor ...[more]