Ontology highlight
ABSTRACT:
SUBMITTER: Morimoto D
PROVIDER: S-EPMC6414897 | biostudies-literature | 2018 Feb
REPOSITORIES: biostudies-literature
Morimoto Daichi D Nishizawa Ryo R Walinda Erik E Takashima Shingo S Sugase Kenji K Shirakawa Masahiro M
Polymers 20180227 3
Ubiquitin and its polymeric forms are conjugated to intracellular proteins to regulate diverse intracellular processes. Intriguingly, polyubiquitin has also been identified as a component of pathological protein aggregates associated with Alzheimer's disease and other neurodegenerative disorders. We recently found that polyubiquitin can form amyloid-like fibrils, and that these fibrillar aggregates can be degraded by macroautophagy. Although the structural properties appear to function in recogn ...[more]