Łukasz A. Joachimiak

This paper describes a novel AAV9 variant, AAV9fyhr, that improves CNS gene delivery while minimizing peripheral tissue tropism through targeted amino acid modifications.

The paper identifies sequence changes that bias tau aggregation toward CTE-like structures using mutagenesis and structural analysis.

This study identifies CTE-like tau seeds in ALS/PDC brain and spinal cord using alanine mutational scanning, suggesting ALS/PDC is a CTE-like tauopathy.

This study uses generative protein design to explore how sequences encode amyloid fibril structures, showing a continuous compatibility between sequences and a common amyloid fold.

This study identifies cysteine residues as critical for tau aggregation and propagation in cells, both spontaneously and when seeded.

This study identifies a hybrid inflammasome formed by NLRP1 and NLRP3 in human cells, associated with inflammation in inflammasomopathies and transplant patients.

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 shows DnaJB1 inhibits tau aggregation by binding its N-terminus in vitro and in cellular models, with interactions enhanced by polyanionic factors.

This paper identifies specific azo compounds that enhance HTRA1 abundance but have varying effects on its activity, suggesting potential therapeutic applications for diseases like AMD.

The paper identifies amino acids critical for tau strain propagation by analyzing their role in amyloid templating across different tauopathies.

The paper develops anti-tau antibodies that selectively bind pathological tau seeds in neurodegenerative diseases, supporting a model of conformational change at P301.

This study identifies DnaJC7 as a specific regulator of tau seeding through its interaction with Hsp70, showing that its protective activity depends on the J domain and substrate binding site.

The paper uses an in silico alanine scan method to identify energetically important interactions in tau amyloid fibrils and classifies structures using machine learning.

The paper shows that seed-competent tau monomer (Ms) forms before insoluble fibrils in PS19 tauopathy mice, initiating pathology in a phosphorylation-independent manner.

The paper identifies inert and seed-competent tau monomers, showing structural differences that influence aggregation potential.