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The major focus of our group is the target-based design of novel anti-cancer and anti-rheumatoid arthritis chemotherapeutics.  Currently we are focusing our efforts on the development of potent and selective inhibitors of enzymes whose activities are involved in modulating chromatin structure.  The modulation of chromatin structure can have drastic effects on the transcription of particular genes.  Our lab uses kinetic and structural analyses to guide the design of small molecule inhibitors, which we then synthesize and evaluate as inhibitors of these enzymes. 

Protein Arginine Methyl-Transferases (PRMTs) catalyze the mono-, asymmetric di-, and symmetric di-methylation of Arginine residues in a number of proteins including the core histone proteins.  Histone methylation on Arginine is known to help activate the transcription of estrogen responsive genes.

Protein Arginine Deiminases (PADs) catalyze the deimination of Arginine residues to citrulline in a number of proteins including histones H2A, H3, and H4.  We are focused on developing inhibitors targeting these enzymes because their activity is aberrantly upregulated in numerous diseases, including cancer, colitis, and rheumatoid arthritis.

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