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• W2026152516 startingPage "517" @default.
• W2026152516 abstract "Reversible acetylation has emerged as a key post-translational modification of proteins. Although the number of acetylated proteins is rapidly growing, the ways in which protein acetyltransferases and deacetylases connect with extracellular stimuli remain unclear. Recently, a regulatory network has emerged that controls the expression and activity of SIRT1, a mammalian class-III protein deacetylase. SIRT1 is an important regulator of metabolism, senescence, cancer and, possibly, longevity and is connected with crucial stress-responsive signal-transduction pathways. These connections provide important clues about how protein acetylation and deacetylation mediate cellular adaptations to extrinsic stress." @default.
• W2026152516 created "2016-06-24" @default.
• W2026152516 creator A5017066937 @default.
• W2026152516 creator A5089829834 @default.
• W2026152516 date "2008-11-01" @default.
• W2026152516 modified "2023-10-16" @default.
• W2026152516 title "The ups and downs of SIRT1" @default.
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