L. A. Joachimiak

Amyloid-motif-dependent tau self-assembly is modulated by isoform sequence context

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.

Disease-associated patterns of acetylation stabilize tau fibril formation

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

Mapping Hsp104 structure and substrate interactions using crosslinking mass spectrometry

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

FTD-tau S320F mutation stabilizes local structure and allosterically promotes amyloid motif-dependent aggregation

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

Development of a new DHFR-based destabilizing domain with enhanced basal turnover and applicability in mammalian systems

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

Dual domain recognition determines SARS-CoV-2 PLpro selectivity for human ISG15 and K48-linked di-ubiquitin

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.

Biophysical properties of a tau seed

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

DnaJC7 binds natively folded structural elements in tau to inhibit amyloid formation

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

Auto-regulatory J-domain interactions control Hsp70 recruitment to the DnaJB8 chaperone

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

Tau local structure shields amyloid motif and controls aggregation propensity

The paper investigates how local structure in tau protein modulates aggregation propensity and how mutations disrupt this structure to trigger amyloid formation.