Date of Award
Campus Access Dissertation
Chemistry and Biochemistry
Thompson, Paul R
The Protein Arginine Deiminase (PAD) family contains five known mammalian isozoymes (PADs 1, 2, 3, 4, and 6) that catalyze the post-translational modification of peptidyl-arginine to form peptidyl-citrulline in a variety of protein substrates. Over the past decade the importance of this post translational modification has become increasingly apparent as its putative roles in diseases becomes more evident. Enormous effort has been made towards understanding the physiological roles of these protein modifying enzymes, in particular, PAD4, due to the increasing evidence linking dysregulated PAD activity to the incidence and severity of Rheumatiod Arthritis (RA) and other human diseases, such as cancer and colitis.
Slack, J.(2010). Unlocking thePadlock: Elucidation of Protein Arginine Deiminase 4 Function, Activity and Activation Dynamics. (Doctoral dissertation). Retrieved from http://scholarcommons.sc.edu/etd/735