Date of Award
1-1-2010
Document Type
Campus Access Dissertation
Department
Chemistry and Biochemistry
Sub-Department
Chemistry
First Advisor
Thompson, Paul R
Abstract
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.
Rights
© 2010, Jessica Slack
Recommended Citation
Slack, J.(2010). Unlocking thePadlock: Elucidation of Protein Arginine Deiminase 4 Function, Activity and Activation Dynamics. (Doctoral dissertation). Retrieved from https://scholarcommons.sc.edu/etd/735