Busra Ozguney

Short UG-rich RNAs bind and stabilize TDP-43 RNA-recognition motifs to allosterically destabilize its prion-like domain helical region, preventing aggregation and mitigating neurodegeneration in cells and mice.

This paper investigates how the disordered C-terminal domain of TDP-43 interacts with RNA and identifies key residues and structural features that mediate RNA recognition and binding specificity.

This study shows methionine oxidation in TDP-43's C-terminal domain disrupts structure and phase separation through region-specific mechanisms.

This study uses computational methods to analyze how Rac1 mutations affect conformational dynamics and identifies potential therapeutic targets.

This study shows that TDP-43 aggregation in stress granules requires up-concentration and oxidative stress, leading to intra-condensate demixing and pathological aggregates.

This study uses molecular dynamics simulations to show RNA-binding stabilizes TDP-43 tandem RRMs and reduces conformational plasticity, preventing pathological aggregation.