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Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
TLDR
The analysis of two SIR2 mutations supports the idea that this deacetylase activity accounts for silencing, recombination suppression and extension of life span in vivo, and provides a molecular framework of NAD-dependent histone de acetylation that connects metabolism, genomic silencing and ageing in yeast and, perhaps, in higher eukaryotes.
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hSIR2SIRT1 Functions as an NAD-Dependent p53 Deacetylase
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Negative control of p53 by Sir2alpha promotes cell survival under stress.
TLDR
It is shown that mammalian Sir2alpha physically interacts with p53 and attenuates p53-mediated functions, and Nicotinamide inhibits an NAD-dependent p53 deacetylation induced by Sir2 alpha, and also enhances the p53 acetylation levels in vivo.
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The NAD Biosynthesis Pathway Mediated by Nicotinamide Phosphoribosyltransferase Regulates Sir2 Activity in Mammalian Cells*
TLDR
It is found that Nampt was the ratelimiting component in this mammalian NAD biosynthesis pathway and regulates the function of Sir2α and thereby plays an important role in controlling various biological events in mammals.
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Nicotinamide mononucleotide, a key NAD(+) intermediate, treats the pathophysiology of diet- and age-induced diabetes in mice.
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Nampt/PBEF/Visfatin regulates insulin secretion in beta cells as a systemic NAD biosynthetic enzyme.
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Negative Control of p53 by Sir2α Promotes Cell Survival under Stress
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Circadian Clock Feedback Cycle Through NAMPT-Mediated NAD+ Biosynthesis
TLDR
It is reported that both the rate-limiting enzyme in mammalian Nicotinamide adenine dinucleotide (NAD+) biosynthesis, nicotinamide phosphoribosyltransferase (NAMPT), and levels of NAD+ display circadian oscillations that are regulated by the core clock machinery in mice.
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NAD+ and sirtuins in aging and disease.
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Increased dosage of mammalian Sir2 in pancreatic beta cells enhances glucose-stimulated insulin secretion in mice.
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