Structural and biochemical evaluation of bisubstrate inhibitors of protein arginine N-methyltransferases PRMT1 and CARM1 (PRMT4)
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DOI: 10.1042/bcj20190826
Abstract: Attenuating the function of protein arginine methyltransferases (PRMTs) is an objective for the investigation and treatment of several diseases including cardiovascular disease and cancer. Bisubstrate inhibitors that simultaneously target binding sites for arginine substrate and… read more here.
Keywords: protein arginine; evaluation bisubstrate; bisubstrate; arginine methyltransferases ... See more keywords
Structural and biochemical evaluation of bisubstrate inhibitors of protein arginine N-methyltransferases PRMT1 and CARM1 (PRMT4).
Sign Up to like & getrecommendations! Published in 2020 at "Biochemical Journal"
DOI: 10.2210/pdb6s7c/pdb
Abstract: Attenuating the function of protein arginine methyltransferases (PRMTs) is an objective for the investigation and treatment of several diseases including cardiovascular disease and cancer. Bisubstrate inhibitors that simultaneously target binding sites for arginine substrate and… read more here.
Keywords: protein arginine; evaluation bisubstrate; bisubstrate; arginine methyltransferases ... See more keywords