RSV regulates the activation of SIRT1. Cao et al. solved the crystal structure of SIRT1 complexed with three RSV molecules (denoted as RSV1 to RSV3) and a 7-amino-4-methylcoumarin (AMC)-containing p53 peptide [15]. RSV1 and RSV2 form hydrogen bonds with both the N-terminal domain (NTD) of SIRT1 and p53-AMC peptide, while RSV3 contacts the catalytic domain (CD) of SIRT1 and the peptide. Continuous enzyme-linked microplate analysis confirmed that the bindings of RSV1 and RSV2 are crucial for the elevated SIRT1 activity toward the p53-AMC peptide, while RSV3 plays an auxiliary role