Regarding other arginine methyltransferases, the best characterized cell-active allosteric inhibitor of PRMT3-SGC707—was proven to inhibit the methylation of both endogenous and exogenous H4R3 and bind to overexpressed PRMT3 in the embryonic kidney cell line HEK293 and lung cancer cell line A549, with a Kd at 85 nM (using an isothermal titration calorimetry assay) [153,154]. This evidence concerns the gene PRMT3 and lung carcinoma.