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A Chloroacetamidine‐Based Inactivator of Protein Arginine Methyltransferase 1: Design, Synthesis, and In Vitro and In Vivo Evaluation
Author(s) -
Obianyo Obiamaka,
Causey Corey P.,
Osborne Tanesha C.,
Jones Justin E.,
Lee YoungHo,
Stallcup Michael R.,
Thompson Paul R.
Publication year - 2010
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201000209
Subject(s) - methylation , methyltransferase , protein arginine methyltransferase 5 , arginine , in vivo , biochemistry , in vitro , readability , transferase , computational biology , biology , chemistry , enzyme , computer science , genetics , amino acid , gene , programming language
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.