TDP‐43 Aggregation: The Healthy‐Toxic Balance of the Prion‐Like Domain
Luca Zangrando, Emanuele Buratti, Francesca Paron · 2026
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Description
Luca Zangrando, Emanuele Buratti, and Francesca Paron review the double life of the protein TDP-43 in a 2026 article. TDP-43 normally manages RNA tasks from splicing to transport, and its clumps mark diseases such as ALS and much frontotemporal degeneration. Newer work shows its self-gathering is not always harmful.
Reversible assemblies and liquid droplets help TDP-43 do its normal jobs. Mutations, altered RNA binding, chemical tags, or cutting can tip that balance into permanent toxic aggregates, much like prion proteins. The review maps the structural switches in its prion-like domain and surveys strategies to clear aggregates or steer its phase behavior. Keeping the healthy side of the balance is the therapeutic goal.
Catalog record
| CREATOR | Luca Zangrando, Emanuele Buratti, Francesca Paron |
|---|---|
| YEAR | 2026 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 110653 |
| LICENSE | https://creativecommons.org/licenses/by/4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |