Anne S. Wentink

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

This study shows that the Hsp70 disaggregation machinery disassembles Tau fibrils, generating small seeding-competent Tau species that can drive aggregation.