SIRT2 inhibition achieves neuroprotection by decreasing sterol biosynthesis - Wikidata - awgldk - TriplyDB

SIRT2 inhibition achieves neuroprotection by decreasing sterol biosynthesis

SIRT2 inhibition achieves neuroprotection by decreasing sterol biosynthesis

http://www.wikidata.org/entity/Q28279273

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SIRT2 as a Therapeutic Target for Age-Related Disorders GTPase activity and neuronal toxicity of Parkinson's disease-associated LRRK2 is regulated by ArfGAP1 SIRT2 regulates tumour hypoxia response by promoting HIF-1α hydroxylation Sir-two-homolog 2 (Sirt2) modulates peripheral myelination through polarity protein Par-3/atypical protein kinase C (aPKC) signaling Synthesis and evaluation of substituted chroman-4-one and chromone derivatives as sirtuin 2-selective inhibitors Targeting New Candidate Genes by Small Molecules Approaching Neurodegenerative Diseases Protective effects and mechanisms of sirtuins in the nervous system Growing the growth cone: remodeling the cytoskeleton to promote axon regeneration SIRT1 and SIRT2: emerging targets in neurodegeneration Sirtuins in hematological aging and malignancy From sirtuin biology to human diseases: an update Group IVA Cytosolic Phospholipase A2 Regulates the G2-to-M Transition by Modulating the Activity of Tumor Suppressor SIRT2.The promise and perils of HDAC inhibitors in neurodegeneration The Sirtuin 2 microtubule deacetylase is an abundant neuronal protein that accumulates in the aging CNS The sirtuin-2 inhibitor AK7 is neuroprotective in models of Parkinson's disease but not amyotrophic lateral sclerosis and cerebral ischemia SIRT2 ablation has no effect on tubulin acetylation in brain, cholesterol biosynthesis or the progression of Huntington's disease phenotypes in vivo Pitfalls in the detection of cholesterol in Huntington's disease models Cholesterol Modifies Huntingtin Binding to, Disruption of, and Aggregation on Lipid Membranes.Development and characterization of 3-(benzylsulfonamido)benzamides as potent and selective SIRT2 inhibitors Functional genetic variants within the SIRT2 gene promoter in acute myocardial infarction.Sirtuin-2 Protects Neural Cells from Oxidative Stress and Is Elevated in Neurodegeneration.Drosophila Sirt2/mammalian SIRT3 deacetylates ATP synthase β and regulates complex V activity.Conserved role of SIRT1 orthologs in fasting-dependent inhibition of the lipid/cholesterol regulator SREBP.Epigenetic regulation of cholesterol homeostasis.Network organization of the huntingtin proteomic interactome in mammalian brain.SIRT2 plays a key role in both cell cycle regulation and cell survival of BV2 microglia.Therapeutic approaches to preventing cell death in Huntington disease Silencing of SIRT2 induces cell death and a decrease in the intracellular ATP level of PC12 cells.Inhibition of Sirtuin 2 exerts neuroprotection in aging rats with increased neonatal iron intake Sirtuin 1 activator SRT2104 protects Huntington's disease mice.Transcription, epigenetics and ameliorative strategies in Huntington's Disease: a genome-wide perspective An exploratory double-blind, randomized clinical trial with selisistat, a SirT1 inhibitor, in patients with Huntington's disease.Recombinant NAD-dependent SIR-2 protein of Leishmania donovani: immunobiochemical characterization as a potential vaccine against visceral leishmaniasis.The human sirtuin family: evolutionary divergences and functions.Design and Evaluation of 3-(Benzylthio)benzamide Derivatives as Potent and Selective SIRT2 Inhibitors Aging-related rotenone-induced neurochemical and behavioral deficits: role of SIRT2 and redox imbalance, and neuroprotection by AK-7 Insight into the Mechanism of Intramolecular Inhibition of the Catalytic Activity of Sirtuin 2 (SIRT2).Drosophila models of proteinopathies: the little fly that could.Suppression of protein aggregation by chaperone modification of high molecular weight complexes 3-(N-arylsulfamoyl)benzamides, inhibitors of human sirtuin type 2 (SIRT2)

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P2860

SIRT2 inhibition achieves neuroprotection by decreasing sterol biosynthesis

http://www.wikidata.org/entity/Q28279273

description

2010 nî lūn-bûn

@nan

2010 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի ապրիլին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

name

SIRT2 inhibition achieves neuroprotection by decreasing sterol biosynthesis

@ast

SIRT2 inhibition achieves neuroprotection by decreasing sterol biosynthesis

@en

SIRT2 inhibition achieves neuroprotection by decreasing sterol biosynthesis

@nl

type

label

SIRT2 inhibition achieves neuroprotection by decreasing sterol biosynthesis

@ast

SIRT2 inhibition achieves neuroprotection by decreasing sterol biosynthesis

@en

SIRT2 inhibition achieves neuroprotection by decreasing sterol biosynthesis

@nl

prefLabel

SIRT2 inhibition achieves neuroprotection by decreasing sterol biosynthesis

@ast

SIRT2 inhibition achieves neuroprotection by decreasing sterol biosynthesis

@en

SIRT2 inhibition achieves neuroprotection by decreasing sterol biosynthesis

@nl

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PNAS.1002924107

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Proceedings of the National Academy of Sciences of the United States of America

P1476

SIRT2 inhibition achieves neuroprotection by decreasing sterol biosynthesis

@en

P2093

Aleksey G Kazantsev

http://www.w3.org/2001/XMLSchema#string

Alex Parker

http://www.w3.org/2001/XMLSchema#string

Alexandre Kuhn

http://www.w3.org/2001/XMLSchema#string

Allison Amore

http://www.w3.org/2001/XMLSchema#string

David M Taylor

http://www.w3.org/2001/XMLSchema#string

Donna L Smith

http://www.w3.org/2001/XMLSchema#string

Emmanuel Lambert

http://www.w3.org/2001/XMLSchema#string

Heike Runne

http://www.w3.org/2001/XMLSchema#string

Hilary Moffitt

http://www.w3.org/2001/XMLSchema#string

J Lawrence Marsh

http://www.w3.org/2001/XMLSchema#string

P2860

Huntingtin interacting proteins are genetic modifiers of neurodegeneration

The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase

SirT2 is a histone deacetylase with preference for histone H4 Lys 16 during mitosis

HDAC6 and microtubules are required for autophagic degradation of aggregated huntingtin

Interphase nucleo-cytoplasmic shuttling and localization of SIRT2 during mitosis

SIRT2 regulates adipocyte differentiation through FoxO1 acetylation/deacetylation

A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes.

Knockout of the cholesterol 24-hydroxylase gene in mice reveals a brain-specific mechanism of cholesterol turnover

Diminished hippocalcin expression in Huntington's disease brain does not account for increased striatal neuron vulnerability as assessed in primary neurons

Biological and potential therapeutic roles of sirtuin deacetylases

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7927-32

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scholarly article

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831883

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10.1073/PNAS.1002924107

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P433

17

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107

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Özgün Gökçe

Ruth Luthi-Carter

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2010-04-27T00:00:00Z

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43080162

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20378838

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2867924

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