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The N-terminal domain of ALS-linked TDP-43 assembles without misfolding

By Phoebe S. Tsoi, Kyoungjae J. Choi, Paul G Leonard, Antons Sizovs, Mahdi Muhammad Moosa, Kevin R. MacKenzie, Josephine C. Ferreon, Allan Chris M. Ferreon

Posted 04 May 2017
bioRxiv DOI: 10.1101/134072 (published DOI: 10.1002/anie.201706769)

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.

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