10.1021/jm061213n.s001 Rino Ragno Rino Ragno Silvia Simeoni Silvia Simeoni Sabrina Castellano Sabrina Castellano Caterina Vicidomini Caterina Vicidomini Antonello Mai Antonello Mai Antonella Caroli Antonella Caroli Anna Tramontano Anna Tramontano Claudia Bonaccini Claudia Bonaccini Patrick Trojer Patrick Trojer Ingo Bauer Ingo Bauer Gerald Brosch Gerald Brosch Gianluca Sbardella Gianluca Sbardella Small Molecule Inhibitors of Histone Arginine Methyltransferases:  Homology Modeling, Molecular Docking, Binding Mode Analysis, and Biological Evaluations American Chemical Society 2007 binding mode analyses Aspergillus nidulans RmtA modeling Biological EvaluationsThe screening QSAR Small Molecule Inhibitors screening arginine methyltransferase inhibitors novel PRMT inhibitors PRMT 1 Binding Mode Analysis region SAM cisteinic binding site subsite 2007-03-22 00:00:00 Journal contribution https://acs.figshare.com/articles/journal_contribution/Small_Molecule_Inhibitors_of_Histone_Arginine_Methyltransferases_Homology_Modeling_Molecular_Docking_Binding_Mode_Analysis_and_Biological_Evaluations/3017209 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.