%0 Journal Article %A Phoebe S. Tsoi %A Kyoungjae J. Choi %A Paul G. Leonard %A Antons Sizovs %A Mahdi Muhammad Moosa %A Kevin R. MacKenzie %A Josephine C. Ferreon %A Allan Chris M. Ferreon %T The N-terminal domain of ALS-linked TDP-43 assembles without misfolding %D 2017 %R 10.1101/134072 %J bioRxiv %P 134072 %X TDP-43 forms inclusions in several neurodegenerative diseases, and both its N- and C-terminal domains are implicated in this process. We show that the folded TDP-43 N-terminal domain oligomerizes under physiological conditions and propose that, in full-length TDP-43, association between folded N-terminal domains enhances the propensity of the intrinsically unfolded C-terminal domains to drive pathological aggregation. %U https://www.biorxiv.org/content/biorxiv/early/2017/05/04/134072.full.pdf