Sirtuin
Silent information regulator 2 (Sir2) proteins, also known as sirtuins, are a family of nicotine adenine dinucleotide (NAD) dependent protein deacetylases in organisms ranging from bacteria to humans that are characterized by the presence of a unique and highly conserved catalytic domain of approximately 260 amino acids. Sirtuins are divided into 5 classes, including Class I (subclasses Ia, Ib and Ic), Class II, Class III, Class IV (subclasses IVa and IVb) and Class U (Gram-positive bacteria specific). The catalytic domain of sirtuins is comprised of two bilobed globular domains, the large domain containing the NAD-binding pocket and the small domain binding the acetyl-lysine substrate.
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Summary: cell-permeable, selective inhibitor of SIRT2 -
Summary: inhibitor of SIRT2 -
Summary: SIRT1 inhibitor -
1 CitationSummary: Sirt1 and Sirt3 inhibitor -
Summary: SIRT1 and SIRT2 inhibitor -
Summary: Cell-permeable resveratrol prodrug -
Summary: SIRT1 and SIRT2 inhibitor -
Summary: SIRT2 inhibitor, potent and selective -
Summary: selective and brain-permeable SIRT2 inhibitor -
Target: Sir2-like Family Deacetylases (Sirtuins)Summary: SIRT1 inhibitor