A. R. Ormsby

This study identifies a stress-induced trimeric protein disaggregase in human cells that collapses during replicative aging, contributing to pathophysiological consequences.

The paper uses protein painting to show how pharmacological stimuli remodel conserved proteostasis machinery across the proteome in whole cells.

The paper investigates how sequence grammars of unfolded globular proteins drive phase separation and formation of UPODs, highlighting the role of hydrophobic residues and their impact on disease-related interactions.

The paper develops a biosensor to compare protein homeostasis resilience in the nucleus and cytosol of human cells, finding the nucleus has lower chaperone activity and aggregation suppression capacity.

This study investigates how mutant Huntingtin exon 1 chains form inclusions in cells, finding that nascent chains do not stall on ribosomes but that ribosome quality control proteins are recruited into the aggregates.

This study shows that arginine valency in C9ORF72 DPRs causes promiscuous proteome binding, ribosome stalling, actin cytoskeleton disruption, and arginine hypomethylation.