D. R. Southworth

This study identifies phosphorylation at residue S416 on tauC3 as a mechanism that inhibits its degradation by CHIP, contributing to its accumulation in Alzheimer's disease.

The paper uses CRISPR screens in iPSC-derived neurons to identify factors controlling tau aggregation, finding new pathways and potential therapeutic targets for tauopathies.

This study identifies UBXD1 as a p97 ATPase inhibitor and shows how its domains induce structural remodeling and ring opening of the p97 hexamer.

The paper determines cryo-EM structures of a mtHsp60 mutant to show how apical domains coordinate client engagement and chaperonin assembly during the ATP-dependent cycle.

The paper determines the cryo-EM structure of GTP-1 bound to Alzheimer's tau filaments, revealing a stacked binding arrangement and favorable pi-pi interactions.

This study investigates how different polyanions affect tau aggregation and conformation, finding that valency and identity influence aggregation kinetics and fibril morphology.

The paper reports the structure of Skd3-substrate complex, revealing its dodecamer formation and mechanism of protein disaggregation, with implications for SCN and MGCA7.

The paper determines the cryo-EM structure of the Hsp90:FKBP51:p23 complex, revealing how cochaperones recognize Hsp90 during client maturation.

The paper identifies PIKfyve inhibition as a strategy to block α-synuclein fibril escape from lysosomes, reducing aggregation spread in a human cell model.

This study determines high-resolution structures of E. coli ClpAP complex in substrate-bound states to elucidate the mechanism of protein unfolding and proteolysis coupling.

The paper identifies ESCRT pathway components as regulators of tau aggregation propagation by enabling endolysosomal escape of tau seeds.

The paper determines the cryo-EM structure of a hyperactive ClpB variant bound to casein and ATPγS to elucidate its substrate gripping and translocation mechanism.