Results 101 to 110 of about 11,198 (208)

The role of NAD-dependent deacetylase sirtuin-2 in liver metabolic stress through regulating pyruvate kinase M2 ubiquitination

open access: yesJournal of Translational Medicine
NAD-dependent deacetylase Sirt2 is involved in mammalian metabolic activities, matching energy demand with energy production and expenditure, and is relevant to a variety of metabolic diseases.
Jingru Guo   +11 more
doaj   +1 more source

MicroRNA-212-5p Prevents Dopaminergic Neuron Death by Inhibiting SIRT2 in MPTP-Induced Mouse Model of Parkinson’s Disease

open access: yesFrontiers in Molecular Neuroscience, 2018
Recently, emerging evidences show that sirtuins (SIRTs) modulate aging progress and affect neurodegenerative diseases. For example, inhibition of SIRT2 has been recognized to exert neuroprotective effects in Parkinson’s disease (PD).
Sifan Sun   +10 more
doaj   +1 more source

Mutational analysis of SIRT2 NES sequence.

open access: yes, 2013
(A) HeLa cells were transfected with GFP-SIRT2 wild-type or single and double point mutants of the proposed NES sequence. (B) Subcellular distribution results of all single and double mutants of SIRT2 NES analyzed in (A).
Brian J. North (78353)   +1 more
core   +1 more source

Microglial SIRT2 deficiency aggravates cognitive decline and amyloid pathology in Alzheimer's disease

open access: yes
Sirtuin 2 (SIRT2), a NAD+-dependent deacetylase, has been implicated in aging and neurodegenerative diseases such as Alzheimer's disease (AD). While global SIRT2 inhibition has shown promise in reducing amyloid-beta pathology and cognitive deficits in ...
Fernández-Irigoyen, Joaquín   +13 more
core   +1 more source

MicroRNA-339/Sirt2/NF B/FOXO1 Axis

open access: yes, 2020
Recently, we have found that a number of microRNAs (miRNAs) and proteins are involved in the response to acupuncture therapy in hypertensive rats. Our bioinformatics study suggests an association between these miRNAs and proteins, which include miR-339 ...
Shu-Feng Zhou   +5 more
core  

Colocalization of SIRT2 with the centrosome.

open access: yes, 2013
(A) U2OS cells expressing SIRT2-HA were stained for HA (green) and for γ-tubulin (red) and analyzed by confocal microscopy. (B) HeLa cells were stained with antisera for endogenous SIRT2 (green) and Aurora A (red) and analyzed by confocal microscopy. (C)
Brian J. North (78353)   +1 more
core   +1 more source

HF SIRT2 KO mice exhibit increased adiposity and energy expenditure.

open access: yes, 2018
(A) Body weight of the chow WT and SIRT2 KO mice. Lean (B) and fat mass (C) in WT and SIRT2 KO mice on a chow diet at 12 weeks of age. Energy Expenditure (EE) over time (D) or ANCOVA-adjusted 12h average of EE (E) in chow-fed WT or SIRT2 KO mice. RQ over
David H. Wasserman (293778)   +7 more
core   +1 more source

Charakterisierung kernständiger Funktionen der NAD+-abhängigen Deacetylase SIRT2 [PDF]

open access: yes, 2010
The human Sirtuin SIRT2 is a deacetylase predominantly found in the cytoplasm during the cell cycle, which co-localizes with the chromatin at the G2/M transition. During this transition SIRT2 was described) to deacetylate lysine-16 of histone 4.
Waibel, Susanne
core   +1 more source

Efficient Generation of Apo Sirt2 Crystals to Facilitate Investigation of Sirt2 Inhibitor Interactions

open access: yes
The selectivity pocket is a key binding site for selective inhibitors of the NAD+-dependent lysine deacylase Sirtuin 2 (Sirt2), a promising drug target due to its involvement in diseases like cancer and neurodegeneration. This pocket typically opens only upon binding of long fatty-acylated substrates or selective inhibitors. While crystal soaking could
Florian Friedrich   +7 more
openaire   +1 more source

SIRT1 and SIRT2 are upregulated in NSCLC.

open access: yes, 2015
(A, B) Immunoblotting of SIRT1 (A) and SIRT2 (B) in NSCLC cell lines and normal immortalized lung epithelial HBEC-3KT cells. The figure is representative of three different experiments. β-actin was used as control.
Jackeline Agorreta (730816)   +9 more
core   +1 more source

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