Ubiquitin-dependent rapid degradation conceals a cell-protective function of cytoplasmic SIRT3 against oxidative stress
T Hayashi, T Matsushita, S Hisahara… - The Journal of …, 2022 - academic.oup.com
SIRT3 is an NAD+-dependent protein deacetylase localized in mitochondria. Several
studies reported localization of SIRT3 in the cytoplasm or nucleus, but data of these studies …
studies reported localization of SIRT3 in the cytoplasm or nucleus, but data of these studies …
The NAD+-dependent protein deacetylase activity of SIRT1 is regulated by its oligomeric status
Abstract SIRT1, a NAD+-dependent protein deacetylase, is an important regulator in cellular
stress response and energy metabolism. While the list of SIRT1 substrates is growing, how …
stress response and energy metabolism. While the list of SIRT1 substrates is growing, how …
Modulation of SIRT1 expression in different neurodegenerative models and human pathologies
M Pallas, JG Pizarro, J Gutierrez-Cuesta… - Neuroscience, 2008 - Elsevier
We examined the expression of SIRT1 in several experimental paradigms of human
pathologies. We used a neuroblastoma cell line (B65), neuronal primary cultures …
pathologies. We used a neuroblastoma cell line (B65), neuronal primary cultures …
Biochemical characterization, localization, and tissue distribution of the longer form of mouse SIRT3
L Jin, H Galonek, K Israelian, W Choy… - Protein …, 2009 - Wiley Online Library
SIRT3 is a key mitochondrial protein deacetylase proposed to play key roles in regulating
mitochondrial metabolism but there has been considerable debate about its actual size, the …
mitochondrial metabolism but there has been considerable debate about its actual size, the …
[HTML][HTML] Sirt6 deacetylase: a potential key regulator in the prevention of obesity, diabetes and neurodegenerative disease
Sirtuins, NAD+ dependent proteins belonging to class III histone deacetylases, are involved
in regulating numerous cellular processes including cellular stress, insulin resistance …
in regulating numerous cellular processes including cellular stress, insulin resistance …
Research progress on SIRT1 and sepsis.
L Li, M Liu, M Cao, X Bai - 2019 - digitum.um.es
SIRT1, a member of the sirtuin family, belongs to the NAD+-dependent class III histone
deacetylase. SIRT1 can regulate gene expression by catalyzing non-histone and histone …
deacetylase. SIRT1 can regulate gene expression by catalyzing non-histone and histone …
Ligand and structure-based approaches for the identification of SIRT1 activators
SIRT1 is a NAD+-dependent deacetylase that involved in various important metabolic
pathways. Combined ligand and structure-based approach was utilized for identification of …
pathways. Combined ligand and structure-based approach was utilized for identification of …
Identification of benzofuran-3-yl (phenyl) methanones as novel SIRT1 inhibitors: binding mode, inhibitory mechanism and biological action
J Wu, Y Li, K Chen, H Jiang, MH Xu, D Liu - European Journal of Medicinal …, 2013 - Elsevier
SIRT1 is a NAD+-dependent deacetylase. Here we described new SIRT1 inhibitors with the
scaffold of benzofuran-3-yl (phenyl) methanone. The inhibitors were predicted to bind in C …
scaffold of benzofuran-3-yl (phenyl) methanone. The inhibitors were predicted to bind in C …
[HTML][HTML] The expression and correlation of SIRT1 and Phospho-SIRT1 in colorectal cancer
X Zhang, S Chen, M Cheng, F Cao… - International Journal of …, 2015 - ncbi.nlm.nih.gov
SIRT1 is the homologue of sir2 in mammals, which is a nicotinamide adenine dinucleotide
(NAD+) dependent histone deacetylase. SIRT1 is involved in many physiological processes …
(NAD+) dependent histone deacetylase. SIRT1 is involved in many physiological processes …