Sirtuins (SIRTs) are nicotine adenine dinucleotide (+)-dependent histone deacetylases
regulating critical signaling pathways in prokaryotes and eukaryotes, and are involved in …

The NAD+-dependent protein lysine deacylases of the Sirtuin family regulate various
physiological functions, from energy metabolism to stress responses. The human Sirtuin …

Sirtuins are NAD+-dependent histone deacetylases regulating important metabolic
pathways in prokaryotes and eukaryotes and are involved in many biological processes …

Abstract BACKGROUND Sirtuins (SIRT1-7) are a family of NAD+-dependent deacetylases
that catalyze post-translational modifications of proteins. Together, they respond to …

Sirtiun 5 (SIRT5) is a NAD+-dependent protein lysine deacylase primarily located in
mitochondria. SIRT5 displays an affinity for negatively charged acyl groups and mainly …

Sirtuins are NAD+-dependent protein deacylases involved in metabolic regulation and
aging-related diseases. Specific activators for seven human Sirtuin isoforms would be …

The mitochondrial SIRT3 modulates several biological pathways such as cancer,
metabolism, and hypoxia-related diseases. Recently, we discovered new 1, 4 …

Sirtuins are NAD+‐dependent protein deacylases that cleave off acetyl, as well as other acyl
groups, from the ε‐amino group of lysines in histones and other substrate proteins. Seven …

Abstract Sirtuin-1 (SIRT1), the mammalian ortholog of yeast Sir2p, is well known to be a
highly conserved NAD+-dependent protein deacetylase that has been emerging as a key …

Sirtuins catalyze deacetylation of lysine residues with a NAD+-dependent mechanism. In
mammals, the sirtuin family is composed of seven members, divided into four subclasses …