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Halogen doped graphene quantum dots modulate TDP-43 phase separation and aggregation in the nucleus
Nature Communications Open Access 06 April 2024
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References
Original articles
Arseni, D. et al. TDP-43 forms amyloid filaments with a distinct fold in type A FTLD-TDP. Nature https://doi.org/10.1038/s41586-023-06405-w (2023)
Oiwa, K. et al. Monomerization of TDP-43 is a key determinant for inducing TDP-43 pathology in amyotrophic lateral sclerosis. Sci. Adv. 9, eadf6895 (2023)
Related articles
Arseni, D. et al. Structure of pathological TDP-43 filaments from ALS with FTLD. Nature 601, 139–143 (2022)
Afroz, T. et al. Functional and dynamic polymerization of the ALS-linked protein TDP-43 antagonizes its pathologic aggregation. Nat. Commun. 8, 45 (2017)
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Wood, H. New mechanistic insights into TDP-43 pathology. Nat Rev Neurol 19, 574 (2023). https://doi.org/10.1038/s41582-023-00870-7
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DOI: https://doi.org/10.1038/s41582-023-00870-7
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Halogen doped graphene quantum dots modulate TDP-43 phase separation and aggregation in the nucleus
Nature Communications (2024)