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Communication
A Chloroacetamidine-Based Inactivator of Protein Arginine Methyltransferase 1: Design, Synthesis, and In Vitro and In Vivo Evaluation
Article first published online: 17 MAY 2010
DOI: 10.1002/cbic.201000209
Copyright © 2010 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Additional Information
How to Cite
Obianyo, O., Causey, C. P., Osborne, T. C., Jones, J. E., Lee, Y.-H., Stallcup, M. R. and Thompson, P. R. (2010), A Chloroacetamidine-Based Inactivator of Protein Arginine Methyltransferase 1: Design, Synthesis, and In Vitro and In Vivo Evaluation. ChemBioChem, 11: 1219–1223. doi: 10.1002/cbic.201000209
Publication History
- Issue published online: 7 JUN 2010
- Article first published online: 17 MAY 2010
- Manuscript Received: 5 APR 2010
Funded by
- University of South Carolina
- NIH. Grant Numbers: GM079357, DK055274
Keywords:
- Cl-amidine;
- enzymes;
- inhibitors;
- protein arginine methyltransferase;
- transcription
Protein arginine methyltransferases (PRMTs) catalyze the post-translational methylation of arginine residues. PRMT1 is the predominant mammalian isozyme and is responsible for generating the majority of the asymmetrically dimethylated arginine found in vivo. Herein, we describe the most potent PRMT1 inhibitor, C21, described to date.