Deciphering the Amyloid Foldome of TDP-43
Mompean, M.; Buratti, E.; Laurents, D.
Show abstract
TDP-43 is an essential regulator of RNA splicing and metabolism and its aggregates play key roles in devastating diseases, including Amyotrophic Lateral Sclerosis (ALS)1, Frontotemporal Dementia (FTD) and Limbic-Predominant Age-Related TDP-43 Encephalopathy (LATE)2. Besides this pathological aggregation, TDP-43s oligomerization also serves vital functions3, which adds urgency to determine pathological conformations of TDP-43. The recently published cryo-EM study by Cao, Eisenberg and coworkers now reveals amyloid structures of putative pathological aggregates from TDP-43s C-terminal region4. Whereas the Cao et al.s cryo-EM structures contain both the hydrophobic and Q/N-rich segments, the data were interpreted mainly through the lens of hydrophobic contacts. However, the Q/N-rich region can form amyloid on its own5,6 and therefore additional considerations of the Q/N-rich segments contributions will advance our understanding of TDP-43 aggregation.
Matching journals
The top 5 journals account for 50% of the predicted probability mass.
Similar papers in this journal
Similar papers in this journal
- Structures of plasmepsin X from P. falciparum reveal a novel inactivation mechanism of the zymogen and molecular basis for binding of inhibitors in mature enzyme 92%
- Polyglutamine expansion induced dynamic misfolding of Androgen Receptor 91%
- The Urfold: Structural Similarity Just above the Superfold Level? 91%
Similar papers in this journal
"Similar papers" are the closest papers from that journal in the model's embedding space. They show what the match is built on, but the ranking comes mostly from a classifier over the whole training set, not from these examples alone.