Multi-Domain Interplay Controls Full-Length TDP-43 Phase Separation and Condensate Dynamics
Published in bioRxiv (preprint), 2026
Explicit-solvent, near-atomic resolution coarse-grained simulations reveal how the interplay among TDP-43 domains drives phase separation of the full-length protein, capturing the role of the conserved LCD helix, aromatic and N-terminal residues, phosphomimicking mutations, and NTD-NTD dimer formation in condensate dynamics. Read more
Recommended citation: Ping, X., Badr, R. G. M., Hutten, S., Chen, X., Baltz, L., Yadav, M., Hoeppner, J. S., Schmid, F., Dormann, D., & Stelzl, L. S. (2026). "Multi-Domain Interplay Controls Full-Length TDP-43 Phase Separation and Condensate Dynamics." bioRxiv. https://doi.org/10.64898/2026.06.03.729912 https://www.biorxiv.org/content/10.64898/2026.06.03.729912v1