Keynote Address Presented by Joel Watts, PhD, Associate Professor, Department of Biochemistry, University of Toronto In Honor Of Dr. Pierluigi Gambetti | 12:00 - 1:00 pm
"Fundamental prion disease research: progress and challenges on the road to therapeutics"
Dr. Watts obtained his PhD in Laboratory Medicine and Pathobiology from the University of Toronto in 2008 as a graduate student in David Westaway’s lab at the Tanz CRND.
Following completion of his graduate studies, Dr. Watts was awarded a CIHR fellowship to pursue postdoctoral research in the lab of Nobel laureate Stanley Prusiner at the University of California San Francisco. Dr. Watts’ doctoral and postdoctoral work focused primarily on the mammalian prion diseases, which included performing the first characterization of the prion protein family member Shadoo and developing a transgenic mouse model of sporadic Creutzfeldt-Jakob disease.
More recently, his research has begun to branch off into other neurodegenerative diseases, including Alzheimer’s disease and the synucleinopathies. As a member of the Prusiner lab, Dr. Watts led a large-scale research effort to investigate the prion-like properties of the aggregation-prone proteins involved in these diseases, which has resulted in many high-impact publications that have helped to shape the emerging field of self-propagating protein aggregates.
In 2012 Dr. Watts was awarded a K99/R00 Pathway to Independence Award from the NIH, which is a prestigious career development award given only to the top postdoctoral scholars in the United States.
In 2013 Dr. Watts was recruited back to the University of Toronto and is currently a Principal Investigator at the Tanz CRND and an Associate Professor within the Department of Biochemistry. At the Tanz CRND, Dr. Watts leads the animal modeling efforts amongst a cross-disciplinary team of scientists.
His research interests include studying the role of self-propagating protein aggregates in neurodegenerative diseases as well as exploiting the unique properties of the bank vole prion protein in order to develop superior animal and cellular models of the prion diseases.