Yuna M. Ayala

The paper shows that SRSF1 and TDP-43 form microphases through protein interactions, and MALAT1 enhances this process by binding to SRSF1 microphases.

This study investigates the structural basis of TDP-43 C-terminal domain multimerization using biophysical experiments, AlphaFold2-Multimer, and simulations, revealing helical oligomerization and the role of specific residues in phase separation and disease.

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 shows that 5-ethynyluridine (5EU) causes nuclear accumulation of TDP-43 and other RNA-binding proteins by altering RNA metabolism and splicing.

This study shows that TDP-43 aggregation through prion-like seeding impairs its autoregulation, leading to dysfunction and loss of function in cells.

This study shows that TDP-43 aggregate seeds persist in both mouse and human skeletal muscle even after the removal of large TDP-43 inclusions.

This study identifies VCP as a suppressor of proteopathic seeding and shows that VCP dysfunction increases seeding of multiple aggregates, contributing to neurodegeneration.

This study identifies TDP-43 oligomers as early intermediates in aggregation, showing ALS-linked mutations accelerate this process and enhance aggregate propagation.