| Autor: |
Witalison EE, Thompson PR, Hofseth LJ; Department of Drug Discovery and Biomedical Sciences, South Carolina College of Pharmacy 770 Sumter St., Coker Life Sciences, Rm. 513C University of South Carolina Columbia, SC 29208. hofseth@cop.sc.edu. |
| Jazyk: |
angličtina |
| Zdroj: |
Current drug targets [Curr Drug Targets] 2015; Vol. 16 (7), pp. 700-10. |
| DOI: |
10.2174/1389450116666150202160954 |
| Abstrakt: |
Human proteins are subjected to more than 200 known post-translational modifications (PTMs) (e.g., phosphorylation, glycosylation, ubiquitination, S-nitrosylation, methylation, Nacetylation, and citrullination) and these PTMs can alter protein structure and function with consequent effects on the multitude of pathways necessary for maintaining the physiological homeostasis. When dysregulated, however, the enzymes that catalyze these PTMs can impact the genesis of countless diseases. In this review, we will focus on protein citrullination, a PTM catalyzed by the Protein Arginine Deiminase (PAD) family of enzymes. Specifically, we will describe the roles of the PADs in both normal human physiology and disease. The development of PAD inhibitors and their efficacy in a variety of autoimmune disorders and cancer will also be discussed. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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