Results 271 to 280 of about 77,206 (307)
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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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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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Clinica Chimica Acta, 2014
Cardiovascular disease (CVD) is the leading cause of death worldwide, with aging as the key independent risk factor. Effective interventions are necessary to delay aging. Sirtuin1 (SIRT1), a NAD(+)-dependent histone deacetylase, is closely related to lifespan extension.
Xin-Yuan, Luo +10 more
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Cardiovascular disease (CVD) is the leading cause of death worldwide, with aging as the key independent risk factor. Effective interventions are necessary to delay aging. Sirtuin1 (SIRT1), a NAD(+)-dependent histone deacetylase, is closely related to lifespan extension.
Xin-Yuan, Luo +10 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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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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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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Frontiers in GeneticsAging is linked to a time-associated decline in both cellular function and repair capacity leading to malfunction on an organismal level, increased frailty, higher incidence of diseases, and death. As the population grows older, there is a need to reveal mechanisms associated with aging that could spearhead treatments to postpone the onset of age ...
Blanka Rogina, Heidi A Tissenbaum
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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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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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Current Treatment Options in Oncology
Leukemia is a type of hematological malignancy (HM) caused by uncontrolled proliferation, apoptosis, and differentiation of hematopoietic stem cells (HSCs). Leukemia cells proliferate greatly in the bone marrow (BM), infiltrate other tissues and organs, and affect the normal hematopoietic function.
Zhongqi Wu +4 more
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Leukemia is a type of hematological malignancy (HM) caused by uncontrolled proliferation, apoptosis, and differentiation of hematopoietic stem cells (HSCs). Leukemia cells proliferate greatly in the bone marrow (BM), infiltrate other tissues and organs, and affect the normal hematopoietic function.
Zhongqi Wu +4 more
openaire +2 more sources