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Sirtuin 1 protein is a highly conserved NAD+-dependent class III histone deacetylase belonging to the sirtuin family. It is homologous to yeast Sir2 and plays a central role in regulating diverse biological processes including gene expression through epigenetic modification by deacetylating both histone and non-histone proteins. Its functions extend across cell proliferation, differentiation, stress response adaptation, energy balance maintenance, aging processes, cancer development/progression prevention or promotion depending on context; it also regulates apoptosis by targeting key factors like p53. SIRT1 is ubiquitously expressed across tissues with subcellular localization varying according to physiological state. Due to its broad regulatory roles—especially its anti-inflammatory and antioxidant properties—SIRT1 has become an important therapeutic target under investigation for cancer therapy as well as treatment of metabolic syndrome-related diseases and neurodegenerative conditions.
Activation or inhibition of NAD+-dependent deacetylase activity to modulate acetylation status of target proteins such as p53 and NF-kappaB; this can affect apoptosis, inflammation, metabolism, and cell survival pathways.
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