Associated Papers
From Evasion to Collapse: The Kinetic Cascade of TDP-43 and the Failure of Proteostasis.
Jamerlan A et al.
International Journal of Molecular Sciences, 2026
Structural details of helix-mediated multimerization of the conserved region of TDP-43 C-terminal domain.
Rizuan A et al.
Nature Communications, 2025
TDP-43 loss induces cryptic polyadenylation in ALS/FTD.
Bryce-Smith S et al.
Nature Neuroscience, 2025
De novo design of protein binders to stabilize monomeric TDP-43 and inhibit its pathological aggregation.
Sun G et al.
Proceedings of the National Academy of Sciences of the United States of America, 2025
Pathological C-terminal phosphomimetic substitutions alter the mechanism of liquid-liquid phase separation of TDP-43 low complexity domain.
Haider R et al.
Protein Science : a Publication of the Protein Society, 2024
Decoding Missense Variants by Incorporating Phase Separation via Machine Learning.
Feng M et al.
Nature Communications, 2024
Polystyrene nanoparticles trigger aberrant condensation of TDP-43 and amyotrophic lateral sclerosis-like symptoms.
Sun H et al.
Nature Nanotechnology, 2024
Structural details of helix-mediated TDP-43 C-terminal domain multimerization.
Rizuan A et al.
Biorxiv : the Preprint Server for Biology, 2024
Pathological C-terminal phosphomimetic substitutions alter the mechanism of liquid-liquid phase separation of TDP-43 low complexity domain.
Haider R et al.
Biorxiv : the Preprint Server for Biology, 2024
Phosphomimetic substitutions in TDP-43's transiently α-helical region suppress phase separation.
Haider R et al.
Biophysical Journal, 2024
RNA-mediated ribonucleoprotein assembly controls TDP-43 nuclear retention.
Dos Passos PM et al.
Plos Biology, 2024
TDP-43 loss induces extensive cryptic polyadenylation in ALS/FTD.
Bryce-Smith S et al.
Biorxiv : the Preprint Server for Biology, 2024
A synergy between site-specific and transient interactions drives the phase separation of a disordered, low-complexity domain.
Mohanty P et al.
Proceedings of the National Academy of Sciences of the United States of America, 2023
RNA-mediated ribonucleoprotein assembly controls TDP-43 nuclear retention.
Dos Passos PM et al.
Biorxiv : the Preprint Server for Biology, 2023
Dissecting the Effect of ALS Mutation G335D on the Early Aggregation of the TDP-43 Amyloidogenic Core Peptide: Helix-to-β-Sheet Transition and Conformational Shift.
Li F et al.
Journal of Chemical Information and Modeling, 2023
Heat-shock chaperone HSPB1 regulates cytoplasmic TDP-43 phase separation and liquid-to-gel transition.
Lu S et al.
Nature Cell Biology, 2022
TDP-43 condensation properties specify its RNA-binding and regulatory repertoire.
Hallegger M et al.
Cell, 2021
TDP-43 α-helical structure tunes liquid-liquid phase separation and function.
Conicella AE et al.
Proceedings of the National Academy of Sciences of the United States of America, 2020
ALS Mutations Disrupt Phase Separation Mediated by α-Helical Structure in the TDP-43 Low-Complexity C-Terminal Domain.
Conicella AE et al.
Structure (london, England : 1993), 2016
A New Phase in ALS Research.
Chong PA et al.
Structure (london, England : 1993), 2016