1426152-49-9Relevant articles and documents
Exploiting an allosteric binding site of PRMT3 yields potent and selective inhibitors
Liu, Feng,Li, Fengling,Ma, Anqi,Dobrovetsky, Elena,Dong, Aiping,Gao, Cen,Korboukh, Ilia,Liu, Jing,Smil, David,Brown, Peter J.,Frye, Stephen V.,Arrowsmith, Cheryl H.,Schapira, Matthieu,Vedadi, Masoud,Jin, Jian
, p. 2110 - 2124 (2013/05/08)
Protein arginine methyltransferases (PRMTs) play an important role in diverse biological processes. Among the nine known human PRMTs, PRMT3 has been implicated in ribosomal biosynthesis via asymmetric dimethylation of the 40S ribosomal protein S2 and in c