Inhibition of SIRT2 by Targeting GSK3β-Mediated Phosphorylation Alleviates SIRT2 Toxicity in SH-SY5Y Cells [PDF]
Frontiers in Cellular Neuroscience, 2019 Sirtuin 2 (SIRT2) is thought to be important in the pathogenesis of Parkinson’s disease (PD), and the inhibition of SIRT2 rescues α-synuclein toxicity in a cellular model of PD.
Shuhu Liu +5 more
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SIRT2 deficiency modulates macrophage polarization and susceptibility to experimental colitis. [PDF]
PLoS ONE, 2014 BackgroundSIRT2 belongs to a highly conserved family of NAD+-dependent deacylases, consisting of seven members (SIRT1-SIRT7), which vary in subcellular localizations and have substrates ranging from histones to transcription factors and enzymes. Recently
Giuseppe Lo Sasso +7 more
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[SIRT2, a multi-talented deacetylase]. [PDF]
Medecine sciences : M/S, 2014 Sirtuin 2 (SIRT2) is an NAD(+) (nicotinamide adenine dinucleotide)-dependent deacetylase. Studies of this protein have often been divergent, highlighting the dependence of pleiotropic effects of SIRT2 on cellular context. The natural polyphenol resveratrol is known to exert opposite actions on neural cells according to their normal or cancerous status.
Sayd, Salwa +2 more
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Infection Reveals a Modification of SIRT2 Critical for Chromatin Association [PDF]
Cell Reports, 2018 Summary: Sirtuin 2 is a nicotinamide-adenine-dinucleotide-dependent deacetylase that regulates cell processes such as carcinogenesis, cell cycle, DNA damage, and infection.
Jorge M. Pereira +7 more
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A Glycoconjugated SIRT2 Inhibitor with Aqueous Solubility Allows Structure-Based Design of SIRT2 Inhibitors [PDF]
ACS Chemical Biology, 2019 Small molecule inhibitors for SIRT2, a member of the sirtuin family of nicotinamide adenine dinucleotide-dependent protein lysine deacylases, have shown promise in treating cancer and neurodegenerative diseases. Developing SIRT2-selective inhibitors with better pharmacological properties is key to further realize the therapeutic potential of targeting ...
Jun Young Hong +3 more
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Effects of Dimerization on the Deacylase Activities of Human SIRT2 [PDF]
Biochemistry, 2023 Human sirtuin isoform 2 (SIRT2) is an NAD+-dependent enzyme that functions as a lysine deacetylase and defatty-acylase. Here, we report that SIRT2 readily dimerizes in solution and in cells and that dimerization affects its ability to remove different acyl modifications from substrates.
Jie Yang +2 more
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SIRT2 inhibition protects against cardiac hypertrophy and ischemic injury [PDF]
eLife, 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
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SIRT2 knockout exacerbates insulin resistance in high fat-fed mice. [PDF]
PLoS ONE, 2018 The NAD+-dependent deacetylase SIRT2 is unique amongst sirtuins as it is effective in the cytosol, as well as the mitochondria. Defining the role of cytosolic acetylation state in specific tissues is difficult since even physiological effects at the ...
Louise Lantier +7 more
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Sirt2 Regulates Liver Metabolism in a Sex-Specific Manner [PDF]
BiomoleculesSirtuin-2 (Sirt2), an NAD+-dependent lysine deacylase enzyme, has previously been implicated as a regulator of glucose metabolism, but the specific mechanisms remain poorly defined.
Alexandra V. Schmidt +6 more
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SIRT2 Promotes NLRP3-Mediated Microglia Pyroptosis and Neuroinflammation via FOXO3a Pathway After Subarachnoid Hemorrhage [PDF]
Journal of Inflammation ResearchJia-Qing Sun,1,5,* Bin Sheng,2,5,* Sen Gao,2,5,* Xun-Zhi Liu,2,5 Yue Cui,4,5 Zheng Peng,2,5 Xiang-Xin Chen,2,5 Peng-Fei Ding,3,5 Zong Zhuang,2,5 Ling-Yun Wu,2,5 Chun-Hua Hang,1– 5 Wei Li2– 5 1Department of Neurosurgery, Nanjing Drum Tower ...
Sun JQ +11 more
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