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University of South Carolina
Unlocking thePadlock: Elucidation of Protein Arginine Deiminase 4 Function, Activity and Activation Dynamics
Abstract
dc:description.abstractThe 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.
Degree
thesis:*- Name thesis:degree_name
- Ph.D.
- Level thesis:degree_level
- Campus Access Dissertation
- Discipline thesis:degree_discipline
- Chemistry and Biochemistry
- Year
- 2010
Author and committee
dc:creator, dc:contributor.*- Author dc:creator
-
- Slack, Jessica
- Contributors dc:contributor
-
- Thompson, Paul R
Subjects
dc:subject × 2Rights
dc:rights- Statement dc:rights
-
- © 2010, Jessica Slack
Identifiers
dc:identifier.*- Repository record dc:identifier
- https://scholarcommons.sc.edu/etd/735
- OAI identifier oai:identifier
- oai:scholarcommons.sc.edu:etd-1736