Results 41 to 50 of about 11,198 (208)

SIRT2 is involved in the modulation of depressive behaviors [PDF]

open access: yesScientific Reports, 2015
Abstract Exposure to chronic stress produces negative effects on mood and hippocampus-dependent memory formation. SIRT2 alteration has been reported in mood disorders; however, the role of SIRT2 in depression remains unclear. Therefore, we aimed to determine whether SIRT2 can restore stress-induced suppression of neurogenesis in a rat
Rui Liu   +5 more
openaire   +2 more sources

Sirtuin 2 Deficiency Increases Bacterial Phagocytosis by Macrophages and Protects from Chronic Staphylococcal Infection

open access: yesFrontiers in Immunology, 2017
Sirtuin 2 (SIRT2) is one of the seven members of the family of NAD+-dependent histone deacetylases. Sirtuins target histones and non-histone proteins according to their subcellular localization, influencing various biological processes.
Eleonora Ciarlo   +12 more
doaj   +1 more source

Quantitative proteomic analysis of the lysine acetylome reveals diverse SIRT2 substrates

open access: yesScientific Reports, 2022
Sirtuin 2 (SIRT2) is a NAD+-dependent deacetylase, which regulates multiple biological processes, including genome maintenance, aging, tumor suppression, and metabolism.
Hui Zhang   +5 more
doaj   +1 more source

SIRT2 inhibition protects against cardiac hypertrophy and ischemic injury

open access: yeseLife, 2023
Sirtuins (SIRT) exhibit deacetylation or ADP-ribosyltransferase activity and regulate a wide range of cellular processes in the nucleus, mitochondria, and cytoplasm. The role of the only sirtuin that resides in the cytoplasm, SIRT2, in the development of
Xiaoyan Yang   +10 more
doaj   +1 more source

SIRT2 controls the pentose phosphate switch [PDF]

open access: yesThe EMBO Journal, 2014
The most common enzyme defect in humans is glucose-6-phosphate dehydrogenase (G6PD) deficiency, which affects more than 400 million people. G6PD shunts glucose into the pentose phosphate pathway (PPP) to generate nucleotides and reducing potential in the form of NADPH.
Lindsay E, Wu, David A, Sinclair
openaire   +2 more sources

SIRT2-mediated deacetylation and deubiquitination of C/EBPβ prevents ethanol-induced liver injury

open access: yesCell Discovery, 2021
Protein acetylation has emerged to play pivotal roles in alcoholic liver disease (ALD). Sirutin 2 (SIRT2) is a nicotinamide adenine dinucleotide (NAD+)-dependent deacetylase involved in the regulation of aging, metabolism, and stress.
Yingting Zhang   +13 more
doaj   +1 more source

Expression and clinical significance of SIRT2 in urothelial bladder cancer and its impact on cancer cell proliferation, invasion and migration [PDF]

open access: yesJichu yixue yu linchuang, 2023
Objective To investigate the expression and clinical significance of silent information regulator 2 (SIRT2) form tissue of urothelial bladder cancer(UBC) and the effects of down-regulation of SIRT2 on the proliferation, invasion and migration of bladder ...
JIN Xiaoxia, LU Xiaoyun, LIU Yushan, LIANG Lina
doaj   +1 more source

Downregulation of SIRT2 Inhibits Invasion of Hepatocellular Carcinoma by Inhibiting Energy Metabolism

open access: yesTranslational Oncology, 2017
Hepatocellular carcinoma (HCC) is one of the most common neoplasms, and metastasis is the most important feature for HCC-related deaths. Mounting evidence implies the dynamic regulatory role of SIRT2, a histone deacetylase, in cancer cells. Unfortunately,
Shan Huang   +11 more
doaj   +1 more source

Regulation of Hypoxic Signaling and Oxidative Stress via the MicroRNA–SIRT2 Axis and Its Relationship with Aging-Related Diseases

open access: yesCells, 2021
The sirtuin family of nicotinamide adenine dinucleotide-dependent deacetylase and ADP-ribosyl transferases plays key roles in aging, metabolism, stress response, and aging-related diseases.
Taku Kaitsuka   +2 more
doaj   +1 more source

The SIRT2 Deacetylase Regulates Autoacetylation of p300 [PDF]

open access: yesMolecular Cell, 2008
Autoacetylation of the p300 histone acetyltransferase controls the transition between VP16-mediated chromatin acetylation and preinitiation complex (PIC) assembly. Currently, it is unknown if and how autoacetylated p300 is deacetylated. We found that the NAD(+)-dependent histone deacetylase SIRT2 deacetylates p300 in vitro and in cells.
Black, Joshua C.   +4 more
openaire   +2 more sources

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