Results 11 to 20 of about 11,198 (208)

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, Zhihua Zhou, Ling Zhang, Siying Meng, Shuji Li, Xuemin Wang   +5 more
doaj   +5 more sources

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, Keir Joe Menzies, Adrienne Mottis, Alessandra Piersigilli, Alessia Perino, Hiroyasu Yamamoto, Kristina Schoonjans, Johan Auwerx   +7 more
doaj   +5 more sources

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, Christine Chevalier, Thibault Chaze, Quentin Gianetto, Francis Impens, Mariette Matondo, Pascale Cossart, Mélanie A. Hamon   +7 more
doaj   +3 more sources

[SIRT2, a multi-talented deacetylase].

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, Junier, Marie-Pierre, Chneiweiss, Herve   +2 more
openaire   +3 more sources

A Glycoconjugated SIRT2 Inhibitor with Aqueous Solubility Allows Structure-Based Design of SIRT2 Inhibitors

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, Ian Robert Price, Jessica Jingyi Bai, Hening Lin   +3 more
openaire   +4 more sources

The histone deacetylase SIRT2 stabilizes Myc oncoproteins [PDF]

Cell Death & Differentiation, 2012
Myc oncoproteins are commonly upregulated in human cancers of different organ origins, stabilized by Aurora A, degraded through ubiquitin-proteasome pathway-mediated proteolysis, and exert oncogenic effects by modulating gene and protein expression. Histone deacetylases are emerging as targets for cancer therapy. Here we demonstrated that the class III
Liu, PY, Xu, N, Malyukova, A, Scarlett, CJ, Sun, YT, Zhang, XD, Ling, D, Su, SP, Nelson, CA, Chang, DK, Koach, J, Tee, AE, Haber, M, Norris, MD, Rooman, I, Toon, C, Xue, C, Cheung, B, Kumar, S, Marshall, GM, Biankin, AV, Liu, T, Shih-Ping Su, Jim, Toon, Christopher Chien Wei   +23 more
openaire   +5 more sources

SIRT2- and NRF2-Targeting Thiazole-Containing Compound with Therapeutic Activity in Huntington's Disease Models [PDF]

, 2016
There are currently no disease-modifying therapies for the neurodegenerative disorder Huntington's disease (HD). This study identified novel thiazole-containing inhibitors of the deacetylase sirtuin-2 (SIRT2) with neuroprotective activity in ex vivo ...
H Runne (7752554), DC Lo (7752587), TF Pais (7752536), SD Naidu (7752551), R Abagyan (7752575), RG Lim (7752548), LM Thompson (7752590), JE Landers (7752572), AG Kazantsev (7752593), L Quinti (7752527), MJ Van Kanegan (7752539), LS Kaltenbach (7752542), MM Maxwell (7752566), M Casale (7752530), L Meisel (7752557), NA Rauf (7752560), E Saiah (7752569), S Moniot (7752533), J Pallos (7752545), D Leyfer (7752563), R Luthi-Carter (7630133), AT Dinkova-Kostova (7752578), C Steegborn (7752581), JL Marsh (7752584)   +23 more
core   +8 more sources

SIRT2 knockout exacerbates insulin resistance in high fat-fed mice.

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, Ashley S Williams, Curtis C Hughey, Deanna P Bracy, Freyja D James, Muhammad A Ansari, David Gius, David H Wasserman   +7 more
doaj   +2 more sources

Sirt2 Regulates Liver Metabolism in a Sex-Specific Manner

Biomolecules
Sirtuin-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, Sivakama S. Bharathi, Keaton J. Solo, Joanna Bons, Jacob P. Rose, Birgit Schilling, Eric S. Goetzman   +6 more
doaj   +2 more sources

SIRT2 Promotes NLRP3-Mediated Microglia Pyroptosis and Neuroinflammation via FOXO3a Pathway After Subarachnoid Hemorrhage [PDF]

Journal of Inflammation Research
Jia-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, Sheng B, Gao S, Liu XZ, Cui Y, Peng Z, Chen XX, Ding PF, Zhuang Z, Wu LY, Hang CH, Li W   +11 more
doaj   +1 more source