HDAC inhibition and acetylation‐driven disulfide‐linked aggregation of TDP43: implications for TDP43 proteinopathies
Our findings highlight the critical role of acetylation-mediated disulfide-linked aggregation in TDP43 pathology and suggest that HDAC inhibition contributes to TDP43 mislocalization and stable oligomer formation. Targeting this pathway may provide a novel therapeutic strategy for TDP43 proteinopathies, including ALS and FTLD.
Authors
- Ae Nim Pae (ORCID: https://orcid.org/0000-0002-3678-8253)
- Yun Kyung Kim (ORCID: https://orcid.org/0000-0002-8682-120X)
- Sungsu Lim
Institutions
- The Seoul Institute (KR)
- Korea Institute of Science and Technology (KR)
Publication Details
- Journal
- Alzheimer s & Dementia
- Published
- 2025-12-01
- DOI
- https://doi.org/10.1002/alz70855_100815
- Primary Topic
- Amyotrophic Lateral Sclerosis Research
- Type
- article
- Field-Weighted Citation Impact
- 0.00