Company: West Virginia University
Job title: Associate Professor
I am interested in understanding how proteins are degraded by the ubiquitin proteasome system (UPS). The process of protein degradation is exquisitely regulated and absolutely essential for life and is exploited in many diseases, including neurodegenerative diseases and cancer. More specifically, we strive to uncover the underpinning molecular mechanisms that govern how different regulatory complexes that bind to the 20S proteasome (proteolytic particle) recognize and catalyze the degradation of different classes of proteins. In the long-term, we hope to shed light on the question of why the cell needs such a diverse array of proteasome regulatory complexes to regulate protein degradation. Our ultimate purpose is to discover new mechanisms to modulate these pathways that promise therapeutic utility to treat these diseases. This has been the foremost driving force behind my entire career.
Targeting the Proteasome to Prevent Impairment by Pathological Oligomers with a Common Morphology 2:45 pm
A common soluble oligomer morphology, can be found across the spectrum of neurodegenerative disease These soluble oligomers are potent allosteric inhibitors of proteasome function Understanding the mechanisms of impairment is leading to small molecules that can rescue oligomer impairment and restore proteasome function, which is lost in neurodegenerative diseaseRead more
day: Day Two