{"id":{"repo_id":"south-carolina","oai_identifier":"oai:scholarcommons.sc.edu:etd-1736"},"canonical_url":"https://search.dev.ndltd.org/etd/south-carolina/oai:scholarcommons.sc.edu:etd-1736","repository":{"repo_id":"south-carolina","name":"University of South Carolina","base_url":"https://scholarcommons.sc.edu/do/oai/"},"display":{"title":"Unlocking thePadlock: Elucidation of Protein Arginine Deiminase 4 Function, Activity and Activation Dynamics","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.","abstract_html":"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.","abstract_has_math":false,"creators":["Slack, Jessica"],"institution":null,"degree_name":"Ph.D.","degree_level":"Campus Access Dissertation","degree_discipline":"Chemistry and Biochemistry","degree_department":null,"school":null,"contributors":["Thompson, Paul R"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2010,"date_issued":"2010-01-01T08:00:00Z","date_published":"2010-01-01T08:00:00Z","updated_at":"2026-07-24T04:37:08Z","subjects":["Chemistry","Physical Sciences and Mathematics"],"languages":[],"rights":["© 2010, Jessica Slack"],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"https://scholarcommons.sc.edu/etd/735","outbound_label":"Repository record","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Thompson, Paul R"]},{"key":"dc:creator","label":"Author","values":["Slack, Jessica"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"thesis:degree_discipline","label":"Discipline","values":["Chemistry and Biochemistry"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Campus Access Dissertation"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Ph.D."]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Chemistry","Physical Sciences and Mathematics"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:rights","label":"Dc Rights","values":["© 2010, Jessica Slack"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["https://scholarcommons.sc.edu/etd/735"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["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."]},{"key":"dc:title","label":"Title","values":["Unlocking thePadlock: Elucidation of Protein Arginine Deiminase 4 Function, Activity and Activation Dynamics"]}]}],"canonical_facts":{"dc:contributor":["Thompson, Paul R"],"dc:creator":["Slack, Jessica"],"dc:description.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."],"dc:identifier":["https://scholarcommons.sc.edu/etd/735"],"dc:rights":["© 2010, Jessica Slack"],"dc:subject":["Chemistry","Physical Sciences and Mathematics"],"dc:title":["Unlocking thePadlock: Elucidation of Protein Arginine Deiminase 4 Function, Activity and Activation Dynamics"],"thesis:degree_discipline":["Chemistry and Biochemistry"],"thesis:degree_level":["Campus Access Dissertation"],"thesis:degree_name":["Ph.D."]},"updated_at":"2026-07-24T04:37:08Z"}