L. A. Joachimiak

This study shows that tau aggregation can be reduced by modifying sequences near the PGGG β-turn motif, while maintaining microtubule binding, offering therapeutic insights for neurodegenerative diseases.

This study identifies acetylation patterns that drive tau fibril formation and shows their structural and functional role in tauopathies.

This study uses crosslinking mass spectrometry to analyze conformational changes and substrate interactions in Hsp104, revealing ATP-dependent asymmetry and substrate binding sites.

This study investigates how the FTD-tau S320F mutation stabilizes local structure and promotes amyloid motif-dependent aggregation through allosteric effects.

The paper develops a new destabilizing domain (C12) with reduced basal levels and improved dynamic range, demonstrating its utility in regulating stress-responsive proteins.

This study identifies how SARS-CoV-2 PLpro selectively binds human ISG15 and K48-linked di-ubiquitin through dual domain recognition, revealing potential drug targets.

This study characterizes the biophysical properties of tau seeds, showing they are monomeric and can nucleate tau aggregation in vitro and in cells.

This study identifies DnaJC7's interaction with tau's beta-turn element to inhibit amyloid formation, suggesting a mechanism for tau aggregation regulation.

This study identifies an auto-regulatory J-domain interaction in DnaJB8 that controls Hsp70 recruitment by sequestering the J-domain surface.