@article {Mompe{\'a}n723817, author = {Miguel Mompe{\'a}n and Emanuele Buratti and Douglas V. Laurents}, title = {{\textquotedblleft}Deciphering the amyloid foldome of TDP-43{\textquotedblright}}, elocation-id = {723817}, year = {2019}, doi = {10.1101/723817}, publisher = {Cold Spring Harbor Laboratory}, 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-43{\textquoteright}s 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-43{\textquoteright}s C-terminal region4. Whereas the Cao et al.{\textquoteright}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 segment{\textquoteright}s contributions will advance our understanding of TDP-43 aggregation.}, URL = {https://www.biorxiv.org/content/early/2019/08/04/723817}, eprint = {https://www.biorxiv.org/content/early/2019/08/04/723817.full.pdf}, journal = {bioRxiv} }