Michael P. Vigers

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 study uses NMR to show phosphoryl groups in tau fibrils form ordered 1D wires that stabilize pathological aggregation.

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.

The paper shows that cell-passaged tau fibrils from CBD and PSP patients generate heterogeneous fibrils with a subpopulation resembling the original disease fold.

The paper identifies the proline-rich domain (PRD) of tau as a driver of liquid-liquid phase separation (LLPS) in cells, showing its phosphorylation-dependent behavior and interaction with microtubules.