Results 271 to 280 of about 72,220 (305)
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Metabolic benefits from Sirt1 and Sirt1 activators
Current Opinion in Clinical Nutrition and Metabolic Care, 2009To evaluate the role of mammalian Sirt1 and Sirt1 activators in the protection from metabolic disorders such as diet-induced obesity, diabetes type 2, or nonalcoholic fatty liver disease.Sirtuins are highly conserved nicotinamide adenine dinucleotide (NAD+)-dependent deacetylases that are activated by NAD+ and inhibited by NAD in its reduced form (NADH)
Nilika, Chaudhary, Paul T, Pfluger
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Journal of Diabetes and its Complications, 2016
Sirtuin 1 (SIRT1) is a prototype mammalian NAD(+)-dependent protein deacetylase that has emerged as a key metabolic sensor in various metabolic tissues. Growing evidence suggests that SIRT1 regulates glucose and lipid metabolism through its deacetylase activity.
Yue, Cao +5 more
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Sirtuin 1 (SIRT1) is a prototype mammalian NAD(+)-dependent protein deacetylase that has emerged as a key metabolic sensor in various metabolic tissues. Growing evidence suggests that SIRT1 regulates glucose and lipid metabolism through its deacetylase activity.
Yue, Cao +5 more
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Molecular Aspects of Medicine, 2008
SIRT1 is the mammalian homologue of yeast silent information regulator (Sir)-2, a member of the sirtuin family of protein deacetylases which have gained much attention as mediators of lifespan extension in several model organisms. Induction of SIRT1 expression also attenuates neuronal degeneration and death in animal models of Alzheimer's disease and ...
Bor Luen, Tang, Christelle En Lin, Chua
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SIRT1 is the mammalian homologue of yeast silent information regulator (Sir)-2, a member of the sirtuin family of protein deacetylases which have gained much attention as mediators of lifespan extension in several model organisms. Induction of SIRT1 expression also attenuates neuronal degeneration and death in animal models of Alzheimer's disease and ...
Bor Luen, Tang, Christelle En Lin, Chua
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Bioorganic & Medicinal Chemistry Letters, 2017
In the current study, bivalent compounds 1-17 constructed by covalently linking the ɛ-amino group of lysine in a tripeptidic scaffold to a functionality via a linker were prepared and examined for their inhibitory potencies against SIRT1, a prototypical member of the β-nicotinamide adenine dinucleotide (β-NAD+)-dependent sirtuin family of protein Nε ...
Juan, Wang +3 more
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In the current study, bivalent compounds 1-17 constructed by covalently linking the ɛ-amino group of lysine in a tripeptidic scaffold to a functionality via a linker were prepared and examined for their inhibitory potencies against SIRT1, a prototypical member of the β-nicotinamide adenine dinucleotide (β-NAD+)-dependent sirtuin family of protein Nε ...
Juan, Wang +3 more
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Function of SIRT1 in physiology
Biochemistry (Moscow), 2009Sirtuins were originally defined as a family of oxidized nicotinamide adenine nucleotide (NAD+)-dependent enzymes that deacetylate lysine residues on various proteins. The sirtuins are remarkably conserved throughout evolution from archae to eukaryotes.
Xing-Xing, Kong +6 more
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Nature Reviews Endocrinology, 2009
Sirtuin 1 (SIRT1), the mammalian homolog of SIR2, was originally identified as a NAD-dependent histone deacetylase, the activity of which is closely associated with lifespan under calorie restriction. Growing evidence suggests that SIRT1 regulates glucose or lipid metabolism through its deacetylase activity for over two dozen known substrates, and has ...
Fengxia, Liang +2 more
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Sirtuin 1 (SIRT1), the mammalian homolog of SIR2, was originally identified as a NAD-dependent histone deacetylase, the activity of which is closely associated with lifespan under calorie restriction. Growing evidence suggests that SIRT1 regulates glucose or lipid metabolism through its deacetylase activity for over two dozen known substrates, and has ...
Fengxia, Liang +2 more
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A Review of Sirt1 and Sirt1 Modulators in Cardiovascular and Metabolic Diseases
Recent Patents on Cardiovascular Drug Discovery, 2008Sirt1 (member of the sirtuin family) is a nicotinamide adenosine dinucleotide (NAD)-dependent deacetylase that removes acetyl groups from various proteins. A wide variety of proteins are Sirt1 substrates; the list includes many transcription factors and cofactors. Deacetylation of these factors may lead to activation or inactivation of the factor, thus
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Trends in Endocrinology & Metabolism, 2006
Sirtuins (Sir2-related enzymes) are a recently discovered class of NAD(+)-dependent protein deacetylases that regulate gene expression in a variety of organisms by deacetylation of modified lysine residues on histones, transcription factors and other proteins.
Tianle, Yang +3 more
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Sirtuins (Sir2-related enzymes) are a recently discovered class of NAD(+)-dependent protein deacetylases that regulate gene expression in a variety of organisms by deacetylation of modified lysine residues on histones, transcription factors and other proteins.
Tianle, Yang +3 more
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Trends in Biochemical Sciences, 2008
Reversible acetylation has emerged as a key post-translational modification of proteins. Although the number of acetylated proteins is rapidly growing, the ways in which protein acetyltransferases and deacetylases connect with extracellular stimuli remain unclear.
Hye-Sook, Kwon, Melanie, Ott
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Reversible acetylation has emerged as a key post-translational modification of proteins. Although the number of acetylated proteins is rapidly growing, the ways in which protein acetyltransferases and deacetylases connect with extracellular stimuli remain unclear.
Hye-Sook, Kwon, Melanie, Ott
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Journal of Cellular Biochemistry
ABSTRACT Sirtuin 1 (SIRT1) is a NAD + ‐dependent deacetylase belonging to the sirtuin family, which regulates a broad spectrum of cellular processes through deacetylation of both histones in the nucleus and non‐histone proteins in the cytosol. Accumulating evidence indicates
Altaf A. Abdulkhaliq +11 more
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ABSTRACT Sirtuin 1 (SIRT1) is a NAD + ‐dependent deacetylase belonging to the sirtuin family, which regulates a broad spectrum of cellular processes through deacetylation of both histones in the nucleus and non‐histone proteins in the cytosol. Accumulating evidence indicates
Altaf A. Abdulkhaliq +11 more
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