Andrew P. Longhini

This paper identifies I-PDBs as BAG2-driven organelles that link proteostasis to CD8+ T cell surveillance by processing pathological tau into antigenic peptides.

The paper designs synthetic tau fibrils that mimic AD and CTE structures, showing strong seeding ability and catalytic effects in vitro and in cells.

This paper identifies a tau peptide fragment that forms seeding-competent fibrils and shows how the P301L mutation facilitates its aggregation into 4R tauopathy-like structures.

This paper develops a protein-like polymer that inhibits tau fibril propagation in human-derived models of neurodegeneration by targeting a specific structural motif of 4R tau isoforms.

The paper designs a 19-residue peptide that selectively induces aggregation of 4R tau over 3R tau, revealing structural and amino acid determinants of tauopathy propagation.