TDP-43 self-interaction is modulated by redox-active compounds Auranofin, Chelerythrine and Riluzole.

ABSTRACT: Amyotrophic lateral sclerosis (ALS) represents a fatal neurodegenerative disease, which is characterized by a rapid loss of lower and upper motor neurons. As a major neuropathological hallmark, protein aggregates containing the Transactivating Response Region (TAR) DNA Binding Protein (TDP-43) are detectable in about 95% of sporadic ALS patients. TDP-43 interacts with itself physiologically to form liquid droplets, which may progress to pathological aggregates. In this study, we established the NanoBit luciferase complementation assay to measure TDP-43 self-interaction and found the fusion of the split luciferase subunits to the N-terminus of the protein as the strongest interacting partners. A screen of pharmacologically active compounds from the LOPAC^®1280 library identified a

SUBMITTER: Oberstadt M 

PROVIDER: S-EPMC5797228 | biostudies-literature | 2018 Feb

REPOSITORIES: biostudies-literature