Misfolded proteins that form aggregates play important roles in many neurodegenerative diseases. These misfolding events occur independently from RNA sequence changes or protein expression levels. So, redirecting misfolded disease-causing proteins is a promising therapeutic strategy, and new research suggests that the plant-derived compound baicalein remodels existing aggregations of TDP-43. Misfolded TDP-43 aggregates are a feature in diseases like amyotrophic lateral sclerosis (ALS), Alzheimer’s disease (AD) and Parkinson’s Disease (PD). This new study examined baicalein in cell models of ALS and progeria (a genetic form of premature aging). Here, baicalein corrected the structure of TDP-43, which restored the bioactivity of the protein. Even in progeria cells with defective lamin A, which promotes TDP-43 aggregates, baicalein still restored the functionality of TDP-43 and mitigated nuclear shape defects in those cells. This establishes an aging-related connection between lamin A and TDP-43. Overall, the findings suggest that baicalein restores disordered peptides and aggregates to their functional units, allowing those units to reform into their nascent proteins and preventing further neurodegeneration. This study also suggests that that targeting TDP-43 folding could treat aging-associated disorders.