Associated Papers
Stress-induced TDP-43 nuclear condensation causes splicing loss of function and STMN2 depletion.
Huang WP et al.
Cell Reports, 2024
Loss of TDP-43 oligomerization or RNA binding elicits distinct aggregation patterns.
Pérez-Berlanga M et al.
The Embo Journal, 2023
37431963 (PubMed )
Supplement: EMBJ-42-e111719-s007.pdf
TDP-43 N-terminal domain dimerisation or spatial separation by RNA binding decreases its propensity to aggregate.
Miura M et al.
Febs Letters, 2023
Split GFP technologies to structurally characterize and quantify functional biomolecular interactions of FTD-related proteins.
Foglieni C et al.
Scientific Reports, 2017
Functional and dynamic polymerization of the ALS-linked protein TDP-43 antagonizes its pathologic aggregation.
Afroz T et al.
Nature Communications, 2017
28663553 (PubMed )
Supplement: 41467_2017_62_MOESM1_ESM.pdf
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