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The S-Nitrosylation of protein thiol groups by NO is a widely recognized protein modification. The treatment of cells with NOBF4 induces the S-nitrosylation of FE65. In this study, we present evidence showing that FE65 modified by NO (Nitric Oxide) via S-nitrosylation induces functional changes in the protein that inhibits the HAT activity of Tip60. The results of mutational analysis of FE65 demonstrated further that the cysteine residue of FE65 (Cys440) is critical to the process ofdoi:10.4236/abc.2011.13013 fatcat:qrkegvlj7rbufmpunh55ppu2zq