M. I. Diamond

Docking for molecules that bind in a symmetric stack with SymDOCK

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.

VCP increases or decreases tau seeding using specific cofactors

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

DNAJB8 oligomerization is mediated by an aromatic-rich motif that is dispensable for substrate activity

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

FTD-tau S320F mutation stabilizes local structure and allosterically promotes amyloid motif-dependent aggregation

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

Tau seeds translocate across the cell membrane to initiate aggregation

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.

The AAA+ chaperone VCP disaggregates Tau fibrils and generates aggregate seeds

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.

RNA induces unique tau strains and stabilizes Alzheimer disease seeds

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

Dual fates of exogenous tau seeds: lysosomal clearance vs. cytoplasmic amplification

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.

Tau local structure shields amyloid motif and controls aggregation propensity

The paper investigates how local structure in tau protein modulates aggregation propensity and how mutations disrupt this structure to trigger amyloid formation.

Tau monomer encodes strains

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