Small Molecule Inhibitors of Histone Arginine Methyltransferases:  Homology Modeling, Molecular Docking, Binding Mode Analysis, and Biological Evaluations RagnoRino SimeoniSilvia CastellanoSabrina VicidominiCaterina MaiAntonello CaroliAntonella TramontanoAnna BonacciniClaudia TrojerPatrick BauerIngo BroschGerald SbardellaGianluca 2007 The screening of the inhibition capabilities of dye-like small molecules from a focused library against both human PRMT1 and <i>Aspergillus </i><i>nidulans</i> RmtA is reported as well as molecular modeling studies (homology modeling, molecular docking, and 3-D QSAR) of the catalytic domain of the PRMT1 fungal homologue RmtA. The good correlation between computational and biological results makes RmtA a reliable tool for screening arginine methyltransferase inhibitors. In addition, the binding mode analyses of tested derivatives reveal the crucial role of two regions, the pocket formed by Ile12, His13, Met16, and Thr49 and the SAM cisteinic binding site subsite. These regions should be taken into account in the design of novel PRMT inhibitors.