Ontology highlight
ABSTRACT:
SUBMITTER: Kaniskan HU
PROVIDER: S-EPMC4400258 | biostudies-literature | 2015 Apr
REPOSITORIES: biostudies-literature
Kaniskan H Ümit HÜ Szewczyk Magdalena M MM Yu Zhengtian Z Eram Mohammad S MS Yang Xiaobao X Schmidt Keith K Luo Xiao X Dai Miao M He Feng F Zang Irene I Lin Ying Y Kennedy Steven S Li Fengling F Dobrovetsky Elena E Dong Aiping A Smil David D Min Sun-Joon SJ Landon Melissa M Lin-Jones Jennifer J Huang Xi-Ping XP Roth Bryan L BL Schapira Matthieu M Atadja Peter P Barsyte-Lovejoy Dalia D Arrowsmith Cheryl H CH Brown Peter J PJ Zhao Kehao K Jin Jian J Vedadi Masoud M
Angewandte Chemie (International ed. in English) 20150227 17
PRMT3 catalyzes the asymmetric dimethylation of arginine residues of various proteins. It is essential for maturation of ribosomes, may have a role in lipogenesis, and is implicated in several diseases. A potent, selective, and cell-active PRMT3 inhibitor would be a valuable tool for further investigating PRMT3 biology. Here we report the discovery of the first PRMT3 chemical probe, SGC707, by structure-based optimization of the allosteric PRMT3 inhibitors we reported previously, and thorough ch ...[more]