The protein acetylation of either the α-amino groups of amino-terminal residues or of internal
lysine or cysteine residues is one of the major posttranslational protein modifications that …

Sirtuins comprise a unique class of nicotinamide adenine dinucleotide (NAD+)-dependent
deacetylases that target multiple protein substrates to execute diverse biological functions …

The sirtuin family of enzymes are able to catalyze the Nε-acyl-lysine deacylation reaction on
histone and non-histone protein substrates. Over the past years since the discovery of its …

Sirtuins are Class III protein deacetylases with seven conserved isoforms. In general,
Sirtuins are highly activated under cellular stress conditions in which NAD+ levels are …

Sirtuins are NAD+-dependent enzymes universally present in all organisms, where they play
central roles in regulating numerous biological processes. Although early studies showed …

The sirtuin family of proteins is categorised as class III histone deacetylases that play
complex and important roles in ageing-related pathological conditions such as cancer and …

Lysine propionylation is a recently identified post‐translational modification that has been
observed in proteins such as p53 and histones and is thought to play a role similar to …

Sirtuins are NAD+-dependent deacetylases involved in chemical reversal of acetyllysine
modifications of cellular proteins. Deacetylation catalyzed by sirtuins is implicated in …

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

Sirtuins are critical regulators of many cellular processes, including insulin secretion, the cell
cycle, and apoptosis. Sirtuins are associated with a variety of age-associated diseases such …