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Sirtuin inhibitors

Expert Opinion on Therapeutic Patents, 2009
The sirtuin family of deacetylase enzymes comprises seven proteins (SIRT1-7) that are dependent on NAD(+) for their activity. Three proteins are located in the nucleus, three in the mitochondria and only one is predominantly cytoplasmic. Caloric restriction and oxidative stress generally up-regulate their expression. SIRT1, the orthologue of yeast Sir2,
Francisco J, Alcaín, José M, Villalba
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Sirtuins

2021
Sirtuins are involved in numerous biological processes such as cell survival and metabolism, aging, and DNA repair; thus they modulate crucial metabolic pathways. The seven members of the Sirtuin family are more and more seen as potential targets for the treatment of cancer, metabolic, neurodegenerative, and cardiovascular diseases.
Zwergel, Clemens   +2 more
openaire   +1 more source

Mitochondrial sirtuins

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2010
Sirtuins have emerged as important proteins in aging, stress resistance and metabolic regulation. Three sirtuins, SIRT3, 4 and 5, are located within the mitochondrial matrix. SIRT3 and SIRT5 are NAD(+)-dependent deacetylases that remove acetyl groups from acetyllysine-modified proteins and yield 2'-O-acetyl-ADP-ribose and nicotinamide.
Jing-Yi, Huang   +4 more
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Sirtuin activators

Expert Opinion on Therapeutic Patents, 2009
Sirtuin 1-7 (SIRT1-7) are deacetylases that are dependent on NAD(+) for their activity. SIRT1 down-regulates p53 activity, increasing lifespan, cell survival, and neuroprotection; it also deacetylates peroxisome proliferator-activated receptor-gamma and its coactivator 1alpha, promoting fat mobilization, increasing mitochondrial size and number, and ...
Francisco J, Alcaín, José M, Villalba
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C. elegans Sirtuins

2013
The nematode Caenorhabditis elegans (C. elegans) has four Sir2 paralogs, sir-2.1, sir-2.2, sir-2.3, and sir-2.4. Thus far, most of the research tools to study worm sirtuins have been developed for sir-2.1, due to its homology to yeast SIR2 and human SIRT1.
Viswanathan, Mohan, Tissenbaum, Heidi A.
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Flavonoids as Sirtuin Modulators

Current Topics in Medicinal Chemistry, 2022
Abstract: Sirtuins (SIRTs) are described as NAD+-dependent deacetylases, also known as class III histone deacetylases. So far, seven sirtuin genes (SIRTS 1–7) have been identified and characterized in mammals and also known to occur in bacteria and eukaryotes.
Deniz, FATMA SEZER   +2 more
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Sirtuins: Multifaceted Drug Targets

Current Molecular Medicine, 2011
Sirtuin (Sir2) proteins being key regulators of numerous cellular processes have been, over the recent past, the subject of intense study. Sirs have been implicated in diverse physiological processes ranging from aging and cancer to neurological dysfunctions.
Chakrabarty, SP   +2 more
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Epigenetics, sirtuins and osteoarthritis

Joint Bone Spine, 2012
Epigenetics, modifications of the DNA other than changes on the DNA sequences, is frequently studied in cancer research and aging. DNA methylation, mi-RNA, and histones deacetylation are investigated in different pathologies, including inflammatory diseases and age-related diseases such as osteoarthritis (OA).
Gabay, Odile, Sanchez, Christelle
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The Biochemistry of Sirtuins

Annual Review of Biochemistry, 2006
Sirtuins are a family of NAD+-dependent protein deacetylases widely distributed in all phyla of life. Accumulating evidence indicates that sirtuins are important regulators of organism life span. In yeast, these unique enzymes regulate gene silencing by histone deacetylation and via formation of the novel compound 2′-O-acetyl-ADP-ribose.
Anthony A, Sauve   +3 more
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Resveratrol, sirtuins, and viruses

Reviews in Medical Virology, 2015
SummaryResveratrol is a natural phenolic product found in some plants in response to stress and has been linked to the many health benefits of red wine. Over the past several decades, a great deal of research has identified diverse biological roles associated with resveratrol, including anti‐oxidant, anti‐proliferation, anti‐inflammation, anti‐cancer ...
Tao, Yang   +5 more
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