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

The human sirtuins are a group of NAD+-dependent protein deacylases. They “erase” acyl
modifications from lysine residues in various cellular targets including histones, transcription …

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

Sirtuins have emerged as therapeutic targets to treat age-related diseases. There are seven
human Sirtuins (SIRT1–7) that display diversity in cellular localization and function. Growing …

Sirtuins are NAD+-dependent protein deacetylases regulating metabolism, stress
responses, and aging processes. Mammalia have seven Sirtuin isoforms, Sirt1–7, which …

Sirtuins post-translationally modulate the function of many cellular proteins that undergo
reversible acetylation–deacetylation cycles, affecting physiological responses that have …

Sirtuins are an evolutionary conserved family of NAD+-dependent protein lysine deacylases.
Mammals have seven Sirtuin isoforms, Sirt1–7. They contribute to regulation of metabolism …

Sirtuins are an evolutionarily conserved family of NAD+-dependent deacylases that display
diversity in subcellular localization and function. SIRT2, the predominantly cytosolic sirtuin …

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

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 …