[HTML][HTML] Interaction with polyglutamine aggregates reveals a Q/N-rich domain in TDP-43

RA Fuentealba, M Udan, S Bell, I Wegorzewska… - Journal of Biological …, 2010 - ASBMB
The identification of pathologic TDP-43 aggregates in amyotrophic lateral sclerosis (ALS)
and frontotemporal lobar degeneration, followed by the discovery of dominantly inherited
point mutations in TDP-43 in familial ALS, have been critical insights into the mechanism of
these untreatable neurodegenerative diseases. However, the biochemical basis of TDP-43
aggregation and the mechanism of how mutations in TDP-43 lead to disease remain
enigmatic. In efforts to understand how TDP-43 alters its cellular localization in response to …