Ontology highlight
ABSTRACT:
SUBMITTER: Bolognesi B
PROVIDER: S-EPMC6744496 | biostudies-literature | 2019 Sep
REPOSITORIES: biostudies-literature
Bolognesi Benedetta B Faure Andre J AJ Seuma Mireia M Schmiedel Jörn M JM Tartaglia Gian Gaetano GG Lehner Ben B
Nature communications 20190913 1
Insoluble protein aggregates are the hallmarks of many neurodegenerative diseases. For example, aggregates of TDP-43 occur in nearly all cases of amyotrophic lateral sclerosis (ALS). However, whether aggregates cause cellular toxicity is still not clear, even in simpler cellular systems. We reasoned that deep mutagenesis might be a powerful approach to disentangle the relationship between aggregation and toxicity. We generated >50,000 mutations in the prion-like domain (PRD) of TDP-43 and quanti ...[more]