Sirtuin 2 inhibitors rescue alpha-synuclein-mediated toxicity in models of Parkinson's disease - Wikidata - wikimedia - TriplyDB

Sirtuin 2 inhibitors rescue alpha-synuclein-mediated toxicity in models of Parkinson's disease

Sirtuin 2 inhibitors rescue alpha-synuclein-mediated toxicity in models of Parkinson's disease

http://www.wikidata.org/entity/Q28307422

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SIRT2 as a Therapeutic Target for Age-Related Disorders SIRT2 regulates tumour hypoxia response by promoting HIF-1α hydroxylation Regulation of G6PD acetylation by SIRT2 and KAT9 modulates NADPH homeostasis and cell survival during oxidative stress Dysregulated LRRK2 signaling in response to endoplasmic reticulum stress leads to dopaminergic neuron degeneration in C. elegans Synthesis and evaluation of substituted chroman-4-one and chromone derivatives as sirtuin 2-selective inhibitors Identifying druggable disease-modifying gene products Nicotinamide restores cognition in Alzheimer's disease transgenic mice via a mechanism involving sirtuin inhibition and selective reduction of Thr231-phosphotau Calorie restriction and the exercise of chromatin Potential Role of Epigenetic Mechanism in Manganese Induced Neurotoxicity Sirtuin functions and modulation: from chemistry to the clinic Targeting New Candidate Genes by Small Molecules Approaching Neurodegenerative Diseases The cytoskeletal arrangements necessary to neurogenesis 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 SIRT2, a multi-talented deacetylase Lysine deacetylase (KDAC) regulatory pathways: an alternative approach to selective modulation Epigenetic landscape of Parkinson's disease: emerging role in disease mechanisms and therapeutic modalities Evaluation of traditional medicines for neurodegenerative diseases using Drosophila models The Bicyclic Intermediate Structure Provides Insights into the Desuccinylation Mechanism of Human Sirtuin 5 (SIRT5)Ex-527 inhibits Sirtuins by exploiting their unique NAD+-dependent deacetylation mechanism The role of sirtuins in cardiac disease Alpha-synuclein is part of a diverse and highly conserved interaction network that includes PARK9 and manganese toxicity Dietary Phytochemicals in Neuroimmunoaging: A New Therapeutic Possibility for Humans?Parkinson's disease as a result of aging The NAD-dependent deacetylase SIRT2 is required for programmed necrosis Acetylation regulates gluconeogenesis by promoting PEPCK1 degradation via recruiting the UBR5 ubiquitin ligase 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 inhibition achieves neuroprotection by decreasing sterol biosynthesis The tumor suppressor SirT2 regulates cell cycle progression and genome stability by modulating the mitotic deposition of H4K20 methylation Neuroprotective Sirtuin ratio reversed by ApoE4 Environmental enrichment and brain repair: harnessing the therapeutic effects of cognitive stimulation and physical activity to enhance experience-dependent plasticity Cellular stress responses, the hormesis paradigm, and vitagenes: novel targets for therapeutic intervention in neurodegenerative disorders C. elegans model identifies genetic modifiers of alpha-synuclein inclusion formation during aging Formation of toxic oligomeric alpha-synuclein species in living cells SIRT2 ablation has no effect on tubulin acetylation in brain, cholesterol biosynthesis or the progression of Huntington's disease phenotypes in vivo The proteome response to amyloid protein expression in vivo Identification of inhibitor binding site in human sirtuin 2 using molecular docking and dynamics simulations Diabetes and risk of Parkinson's disease: an updated meta-analysis of case-control studies

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Sirtuin 2 inhibitors rescue alpha-synuclein-mediated toxicity in models of Parkinson's disease

http://www.wikidata.org/entity/Q28307422

description

2007 nî lūn-bûn

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2007 թուականի Յուլիսին հրատարակուած գիտական յօդուած

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2007 թվականի հուլիսին հրատարակված գիտական հոդված

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2007年の論文

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Sirtuin 2 inhibitors rescue al ...... models of Parkinson's disease

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Sirtuin 2 inhibitors rescue al ...... models of Parkinson's disease

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Sirtuin 2 inhibitors rescue al ...... models of Parkinson's disease

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Aleksey G Kazantsev

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Allison M Amore

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Anne B Young

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Catherine B Volk

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Eirene Kontopoulos

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Irina Kufareva

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Jean-Christophe Rochet

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Katherine E Strathearn

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Mel B Feany

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Michele M Maxwell

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P2860

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

The deacetylase HDAC6 regulates aggresome formation and cell viability in response to misfolded protein stress

Alpha-synuclein acts in the nucleus to inhibit histone acetylation and promote neurotoxicity

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

alpha-Synuclein locus triplication causes Parkinson's disease

Alpha-synuclein in Lewy bodies

Microtubule-associated protein 1B is a component of cortical Lewy bodies and binds alpha-synuclein filaments

Aggresomes formed by alpha-synuclein and synphilin-1 are cytoprotective

Mechanism of sirtuin inhibition by nicotinamide: altering the NAD(+) cosubstrate specificity of a Sir2 enzyme

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17588900

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Parkinson's disease