Office: Science & Engineering (Building 50), Room 3528
Phone: (904) 620-1951
Bachelor of Science - University of South Carolina 2003
Ph.D. - University of South Carolina 2009
Postdoctural Research - The Scripps Research Institute 2010-2012
Dr. Knuckley teaches General Chemistry I Lecture and Laboratory.
Dr. Knuckley is interested in using kinetic and structural analysis to study the catalytic mechanisms of cancer-related proteins. Additionally, he is focused on the identification of novel ligands for disease related proteins and using these to develop tools for diagnosing these diseases. His interests also include the development of kinetic assays and chemical tool compounds.
Arginine Ribosyltransferases and Ribosylhydrolases – ADP-ribosylation is a reversible post-translational modification of arginine residues. This modification is catalyzed by the arginine ribosyltransferase (ART) family and can be removed by the ADP-arginine ribosylhydrolase (ARH) family. Currently, there are three ARH family members (ARH1, 2, and 3) found in mammals and more than XX ART (ART) family members. Recent studies have identified that proper control of the protein ADP-ribosylation levels is essential for cancer suppression. Experimental studies targeting the mechanism of catalysis, substrate specificity, and regulation of these enzymes will undoubtedly aid in the development of chemical tools and inhibitors.
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