Results 21 to 30 of about 11,198 (208)

Development of a NanoBRET assay to validate inhibitors of Sirt2-mediated lysine deacetylation and defatty-acylation that block prostate cancer cell migration [PDF]

open access: yes, 2022
Sirtuin2 (Sirt2) with its NAD+-dependent deacetylase and defatty-acylase activities plays a central role in the regulation of specific cellular functions.
Olaf, Groß   +18 more
core   +2 more sources

The Clinical Significance of SIRT2 in Malignancies: A Tumor Suppressor or an Oncogene?

open access: yesFrontiers in Oncology, 2020
Sirtuin 2 (SIRT2) is a member of the sirtuin protein family. It is a Class III histone deacetylase (HDACs) and predominantly localized to the cytosol. SIRT2 deacetylates histones and a number of non-histone proteins and plays a pivotal role in various ...
Lin Zhang   +6 more
doaj   +1 more source

Discovery of Selective SIRT2 Inhibitors as Therapeutic Agents in B-Cell Lymphoma and Other Malignancies

open access: yesMolecules, 2020
Genetic ablation as well as pharmacological inhibition of sirtuin 2 (SIRT2), an NAD+-dependent protein deacylase, have therapeutic effects in various cancers and neurodegenerative diseases.
Sarwat Chowdhury   +8 more
doaj   +1 more source

Is SIRT2 required for necroptosis? [PDF]

open access: yesNature, 2014
Sirtuins can promote deacetylation of a wide range of substrates in diverse cellular compartments and regulate many cellular processes¹,². Recently Narayan et al., reported that SIRT2 was required for necroptosis based on their findings that SIRT2 inhibition, knock-down or knock-out prevented necroptosis.
Newton, Kim   +17 more
openaire   +3 more sources

Discovery and validation of SIRT2 inhibitors based on tenovin-6 : use of a 1H-NMR method to assess deacetylase activity [PDF]

open access: yes, 2012
The search for potent and selective sirtuin inhibitors continues as chemical tools of this type are of use in helping to assign the function of this interesting class of deacetylases.
Pirrie, L   +26 more
core   +1 more source

CDK11 negatively regulates Wnt/β-catenin signaling in the endosomal compartment by affecting microtubule stability

open access: yesCancer Biology & Medicine, 2020
Objectives: Improper activation of Wnt/β-catenin signaling has been implicated in human diseases. Beyond the well-studied glycogen synthase kinase 3β (GSK3β) and casein kinase 1 (CK1), other kinases affecting Wnt/β-catenin signaling remain to be defined.
Danmin Ou   +10 more
doaj   +1 more source

Expression of SIRT2 and SIRT6 in Retinoblastoma

open access: yesOphthalmic Research, 2015
<b><i>Purpose:</i></b> SIRT2 and SIRT6 are members of the sirtuin family and are associated with cancer development and progression in certain tumours, but their expression in retinoblastoma has not been studied. The primary objective of our study was to determine the expression of SIRT2 and SIRT6 in human retinoblastoma cases. &
Maria Eugenia Orellana   +5 more
openaire   +2 more sources

Sirtuin-2 Protects Neural Cells from Oxidative Stress and Is Elevated in Neurodegeneration

open access: yesParkinson's Disease, 2017
Sirtuins are highly conserved lysine deacetylases involved in ageing, energy production, and lifespan extension. The mammalian SIRT2 has been implicated in Parkinson’s disease (PD) where studies suggest SIRT2 promotes neurodegeneration.
Preeti Singh   +2 more
doaj   +1 more source

Role of SIRT2 in Regulation of Stemness of Cancer Stem-Like Cells in Renal Cell Carcinoma

open access: yesCellular Physiology and Biochemistry, 2018
Background/Aims: Cancer stem cells (CSCs) contribute to tumorgenesis, invasion and metastasis, and are typically resistant to chemotherapy. Recent reports showed that SIRT2 was upregulated in several cancers. However, whether SIRT2 may be a CSC marker in
Ruojing Wei, Dalin He, Xinshi Zhang
doaj   +1 more source

Inhibition of SIRT2 Alleviates Fibroblast Activation and Renal Tubulointerstitial Fibrosis via MDM2

open access: yesCellular Physiology and Biochemistry, 2018
Background/Aims: Renal tubular epithelial cells and fibroblasts are the main sources of myofibroblasts, and these cells produce the extracellular matrix during tubulointerstitial fibrosis (TIF).
Fang-Fang He   +6 more
doaj   +1 more source

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