Results 11 to 20 of about 17,907 (258)

Sirtuins, Metabolism and Cancer [PDF]

open access: yesFrontiers in Pharmacology, 2012
More than a decade ago, sirtuins were discovered as a highly conserved family of NAD+-dependent enzymes that extend lifespan in lower organisms. In mammals, sirtuins are key regulators of stress responses and metabolism, influencing a range of diseases ...
Barbara eMartinez-Pastor   +1 more
doaj   +5 more sources

Sirtuins and Insulin Resistance [PDF]

open access: yesFrontiers in Endocrinology, 2018
The mammalian Sirtuins (SIRT1-7) are an evolutionarily conserved family of NAD+-dependent deacylase and mono-ADP-ribosyltransferase. Sirtuins display distinct subcellular localizations and functions and are involved in cell survival, senescence ...
Shuang Zhou   +2 more
doaj   +3 more sources

Sirtuins, Bioageing, and Cancer [PDF]

open access: yesJournal of Aging Research, 2011
The Sirtuins are a family of orthologues of yeast Sir2 found in a wide range of organisms from bacteria to man. They display a high degree of conservation between species, in both sequence and function, indicative of their key biochemical roles. Sirtuins
D. McGuinness   +3 more
doaj   +4 more sources

Mitochondrial Sirtuins in Reproduction [PDF]

open access: yesAntioxidants, 2021
Mitochondria act as hubs of numerous metabolic pathways. Mitochondrial dysfunctions contribute to altering the redox balance and predispose to aging and metabolic alterations. The sirtuin family is composed of seven members and three of them, SIRT3-5, are housed in mitochondria.
Di Emidio, Giovanna   +5 more
openaire   +5 more sources

Sirtuin 1 and Sirtuin 3 in Granulosa Cell Tumors [PDF]

open access: yesInternational Journal of Molecular Sciences, 2021
Sirtuins (SIRTs) are NAD+-dependent deacetylases that regulate proliferation and cell death. In the human ovary, granulosa cells express sirtuin 1 (SIRT1), which has also been detected in human tumors derived from granulosa cells, i.e., granulosa cell tumors (GCTs), and in KGN cells.
Nina Schmid   +7 more
openaire   +2 more sources

Sirtuins and cognition: implications for learning and memory in neurological disorders

open access: yesFrontiers in Physiology, 2022
Sirtuins are an evolutionarily conserved family of regulatory proteins that function in an NAD+ -dependent manner. The mammalian family of sirtuins is composed of seven histone deacetylase and ADP-ribosyltransferase proteins (SIRT1-SIRT7) that are found ...
Eric Fagerli   +5 more
doaj   +1 more source

Sirtuins as a potential molecular target of cosmetic ingredients [PDF]

open access: yesFarmacja Polska, 2022
Sirtuins are a group of enzymes belonging to histone deacetylases. However, they can also catalyze other deacylation reactions (including, for example, demallonylation, desuccinylation or deglutarylation), as well as ADP-ribosylation reactions.
Katarzyna Brezdeń   +2 more
doaj   +1 more source

Sirtuin Modulators [PDF]

open access: yes, 2011
Members of the sirtuin family including the founding protein Sir2 in Saccharomyces cerevisiae have been linked to lifespan extension in simple organisms. This finding prompted evaluation of the role of Sir2 orthologues in many aging-associated conditions including neurodegeneration, type II diabetes and cancer.
Sumit S, Mahajan   +3 more
openaire   +2 more sources

Roles of sirtuins in asthma

open access: yesRespiratory Research, 2022
Sirtuins are nicotinamide adenine dinucleotide (NAD+)-dependent lysine deacylases and deacetylases that participate in a variety of cellular processes, including transcriptional activity, energy metabolism, DNA damage response, inflammation, apoptosis ...
Yahui Liu, Guochao Shi
doaj   +1 more source

Alterations of sirtuins in mitochondrial cytochrome c-oxidase deficiency. [PDF]

open access: yesPLoS ONE, 2017
Sirtuins are NAD+ dependent deacetylases, which regulate mitochondrial energy metabolism as well as cellular response to stress. The NAD/NADH-system plays a crucial role in oxidative phosphorylation linking sirtuins and the mitochondrial respiratory ...
Arne Björn Potthast   +3 more
doaj   +1 more source

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