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nuclear complex formed by the phosphatases PPM1A and PPM1B, with SIRT2 essential for controlling H3K18 deacetylation and SIRT2-mediated gene repression during infection and necessary for a productive Listeria infection.
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Therefore, the significant prognostic value of NQO1 in predicting outcome of cancer patients might be explained in part due to the functional contribution of NQO1-SIRT2 axis to mitotic stress.
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Sirtuin 2 (Sirt2) expression is an independent prognostic predictor for esophageal squamous cell carcinoma (ESCC) patients.
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SIRT2-deficient (SIRT2-KO) mice exhibit increased acetylation of JNK, which is associated with markedly reduced catalytic activity of JNK in the liver.
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SIRT2-mediated inactivation of p73 is critical for the proliferation and tumorigenicity of glioblastoma cells.
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Here, the authors report that GSK3alpha and GSK3beta are acetylated at Lys246 and Lys183, respectively. They found that SIRT2 deacetylates GSK3beta, and thus enhances its binding to ATP.
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SIRT2-C/T-EMs are the best responders. Some Sirtuin modulators might be potential candidates for AD treatment.
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SIRT2 gene expression is altered in adipose tissue from overweight and obese subjects compared to normal weight subjects.
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SIRT1 and SIRT2 expression and AMPK levels decrease in children with obesity and insulin resistance (IR); targeting SIRT1 can be valuable in preventing obesity-associated IR in childhood and adolescence
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miR-486-3p binds to the 3' UTR of SIRT2 and influences the translation of SIRT2.
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Study discovered that histone lysine benzoylation (Kbz) marks are associated with gene expression and have physiological relevance distinct from histone acetylation and demonstrated that SIRT2, a NAD+-dependent protein deacetylase, removes histone Kbz both in vitro and in vivo.
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Our data provide strong evidence that sirtuin-2 controls the functional ability of the autophagic system through acetylation and highlight the association between mitochondrial metabolism and neurodegeneration in sporadic Parkinson's disease.
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Data found that SIRT2 is a novel deacetylase of HSP90, enhances its ubiquitination-mediated proteasomal degradation, and consequently down-regulates HSP90/LIMK1/cofilin-linked actin polymerization regulation pathway. The deacetylase activity of SIRT2 is required to reduce cell motility by regulating the stability of HSP90. These results demonstrate that SIRT2 functions as a tumor suppressor.
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we provide insight into the regulation of SIRT2 on gastric cancer metabolism and metastasis. SIRT2 increased PEPCK1 protein levels and mitochondrial activity, as well as induced cell migration and invasion by activating the RAS/ERK/JNK/MMP-9 pathway
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MiR150 plays an important role in the development of lung cancer by serving as an oncogene via the SIRT2/JMJD2A signaling pathway.
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Studied association of SIRT2 and p53/NF-kB p65 signal pathways in preventing high glucose-induced vascular endothelial cell injury. Results demonstrated that SIRT2 overexpression is associated with deacetylation of p53 and NF-kB p65, which inhibits the high glucose induced apoptosis and vascular endothelial cell inflammation response.
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The authors report that one of the K-Ras splice variants, K-Ras4a, is subject to lysine fatty acylation, a previously under-studied protein post-translational modification. Sirtuin 2 (SIRT2), one of the mammalian nicotinamide adenine dinucleotide (NAD)-dependent lysine deacylases, catalyzes the removal of fatty acylation from K-Ras4a.
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Low SIRT2 expression is associated with recurrence in prostate cancer.
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SIRT2 participates in the activation of fibroblasts and tubulointerstitial fibrosis, which is mediated via regulation of the MDM2 pathway, and the downregulation of SIRT2.
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Findings suggested that the DNA sequence variants may increase SIRT2 gene promoter activity and SIRT2 levels, contributing to T2D development as a risk factor.