Associated Papers
J-domain proteins cooperate with Hsp70 to drive multiphase separation of RNA-binding-deficient TDP-43.
Yeo KH et al.
The Journal of Biological Chemistry, 2025
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
TAR DNA-binding protein 43 oligomers in physiology and pathology.
Lye YS et al.
Iubmb Life, 2022
The cooperative binding of TDP-43 to GU-rich RNA repeats antagonizes TDP-43 aggregation.
Rengifo-Gonzalez JC et al.
Elife, 2021
In vivo Validation of Bimolecular Fluorescence Complementation (BiFC) to Investigate Aggregate Formation in Amyotrophic Lateral Sclerosis (ALS).
Don EK et al.
Molecular Neurobiology, 2021
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
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