Thi Lieu Dang

This study shows that the thermodynamic stability of alpha-synuclein fibrils affects their disaggregation by the chaperone system HSP70, DNAJB1, and Apg2, with more stable fibrils being less efficiently disaggregated.

The paper shows that different structures of alpha-synuclein fibrils affect how Hsc70 chaperones disaggregate them, influencing protein quality control and aggregation.

This study shows DNAJB1 recruits Hsc70 in two steps to amyloid fibers, forming ordered arrays that enable efficient disaggregation, while a mutant disrupts this organization.

This study identifies a unique chaperoning mechanism in class-A JDPs that recognizes and stabilizes mutant p53, promoting cancer progression by preventing its degradation.