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Glutathione transferase-P1-1 binding with naturally occurring ligands: assessment by docking simulations
2011
Journal of Biophysical Chemistry
Glutathione transferase-P1-1 (hGSTP1-1), which is associated with acquired drug resistance in some tumour cells, requires two identical subunits for full activity. Naturally occurring inhibitors for GSTP1-1 quaternary structure could be interesting therapeutic agents. The aim of this study was to investigate potential binding sites for hGSTP1-1 interaction with ligands many of which occur naturally. Simulations were performed with commercial docking software and with GST monomer or dimer as
doi:10.4236/jbpc.2011.24046
fatcat:zkx5saobv5a3xedosso3a3kduy