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Comment
. 2023 Oct;19(10):574.
doi: 10.1038/s41582-023-00870-7.

New mechanistic insights into TDP-43 pathology

Heather Wood  1
Affiliations
Comment

New mechanistic insights into TDP-43 pathology

Heather Wood. Nat Rev Neurol. 2023 Oct.
No abstract available

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References

Original articles
    1. 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) - DOI - PubMed - PMC
    1. 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) - DOI - PubMed - PMC
Related articles
    1. Arseni, D. et al. Structure of pathological TDP-43 filaments from ALS with FTLD. Nature 601, 139–143 (2022) - DOI - PubMed
    1. Afroz, T. et al. Functional and dynamic polymerization of the ALS-linked protein TDP-43 antagonizes its pathologic aggregation. Nat. Commun. 8, 45 (2017) - DOI - PubMed - PMC

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