Results 41 to 50 of about 10,461 (217)
NAD-dependent protein deacetylase Sirtuin 2 (SIRT2), which regulates several cellular pathways by deacetylating multiple substrates, has been extensively studied in the context of Parkinson’s disease (PD). Although several studies based on the MPTP model
Jianguo Yan +9 more
doaj +1 more source
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
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Expression and clinical significance of SIRT2 in urothelial bladder cancer and its impact on cancer cell proliferation, invasion and migration [PDF]
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
Reduction of Sirt2 mRNA and an absence of the SIRT2 protein in Sirt2 knock-out mice. [PDF]
(A) Exon-intron structure of the Sirt2 gene in mouse and the location of the insertion (light blue) in exon 11 (after nucleotide 18883) in Sirt2KO mice. The positions of the sequencing forward and reverse primers are shown.
Andreas Weiss (135692) +4 more
core +1 more source
Interphase nucleo-cytoplasmic shuttling and localization of SIRT2 during mitosis. [PDF]
The human NAD+-dependent protein deacetylase SIRT2 resides predominantly in the cytoplasm where it functions as a tubulin deacetylase. Here we report that SIRT2 maintains a largely cytoplasmic localization during interphase by active nuclear export in a ...
Brian J North, Eric Verdin
doaj +1 more source
Quantitative proteomic analysis of the lysine acetylome reveals diverse SIRT2 substrates
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
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
CDC42 K153 is deacetylated by SIRT2. [PDF]
(A) CDC42 K153 acetylation is regulated by SIRT family deacetylases. HEK293T cells transfected with Flag-CDC42 were treated with the deacetylase inhibitors TSA (2 μM) and NAM (10 mM) for 16 h before harvesting.
Jian-Hui Li (2570410) +8 more
core +1 more source
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
SIRT2-mediated deacetylation and deubiquitination of C/EBPβ prevents ethanol-induced liver injury
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

