Our research focuses on elucidating the structural and functional diversity of amyloidogenic conformers involved in protein misfolding diseases. We aim to uncover how distinct misfolded conformers emerge along the amyloidogenic pathway and investigate their ability to crosstalk with other amyloid-prone proteins within the cellular environment. 

Our goal is to combine structural biology, protein engineering, and in vivo models, to understand how these pathogenic interactions between various misfolded protein conformers contribute to disease progression and identify structure-specific residues for diagnostic and therapeutic targeting.

Our research groups also focus on elucidating the structures of pathogenic proteins found in Clubroot disease caused by the intracellular pathogen Plasmodiophora brassicae, a soil-borne protist that affects Brassicaceae plants, including Canola. 

Currently, high-resolution structures of pathogenic proteins associated with Clubroot are not yet resolved, hindering intervention and prevention strategies. Our lab employs a combination of "omics" approaches to identify protein biomarkers associated with clubroot disease.