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 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 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.