The N-terminal domain of ALS-linked TDP-43 assembles without misfolding
Phoebe S. Tsoi,
Kyoungjae J. Choi,
Paul G Leonard,
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)
Posted 04 May 2017
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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