M. I. Diamond

SymDOCK is a docking method that exploits symmetry in amyloid fibrils to predict ligand stacking, successfully reproducing known structures and predicting a new one before its determination.

This study investigates how VCP and its cofactors influence tau seeding efficiency in cellular models, finding that VCP modulates this process through distinct cofactors.

This paper identifies an aromatic-rich motif in DNAJB8 that mediates oligomerization and shows that disrupting this motif affects oligomerization but not substrate activity.

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

This study identifies a novel mechanism by which tau seeds enter cells and initiate aggregation through direct translocation across the plasma membrane, independent of endocytosis.

This study shows that the AAA+ chaperone VCP disaggregates Tau fibrils and generates seeding-active Tau as a byproduct, suggesting a role in aggregate removal and spreading in tauopathies.

The paper shows RNA, specifically polyA, induces stable tau strains and may contribute to Alzheimer's disease pathology by promoting seed formation.

This study investigates how exogenous tau seeds are cleared or amplified within cells, finding they are mostly lysosomally degraded but a small fraction enters the cytosol to replicate and is cleared by the proteasome.

The paper shows that tau monomer can encode multiple stable strains, leading to distinct neuropathologies in mice.