The 2.5 Å crystal structure of the SIRT1 catalytic domain bound to nicotinamide adenine dinucleotide (NAD+) and an indole (EX527 analogue) reveals a novel mechanism of histone deacetylase inhibition - Wikidata - awgldk - TriplyDB

The 2.5 Å crystal structure of the SIRT1 catalytic domain bound to nicotinamide adenine dinucleotide (NAD+) and an indole (EX527 analogue) reveals a novel mechanism of histone deacetylase inhibition

The 2.5 Å crystal structure of the SIRT1 catalytic domain bound to nicotinamide adenine dinucleotide (NAD+) and an indole (EX527 analogue) reveals a novel mechanism of histone deacetylase inhibition

http://www.wikidata.org/entity/Q27683752

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Design of small molecule epigenetic modulators Ex-527 inhibits Sirtuins by exploiting their unique NAD+-dependent deacetylation mechanism Structural and Functional Analysis of Human SIRT1 Structures of human sirtuin 3 complexes with ADP-ribose and with carba-NAD+ and SRT1720: binding details and inhibition mechanism Computational studies on sirtuins from Trypanosoma cruzi: structures, conformations and interactions with phytochemicals Selective Sirt2 inhibition by ligand-induced rearrangement of the active site.A potent and selective Sirtuin 1 inhibitor alleviates pathology in multiple animal and cell models of Huntington's disease.The Synergistic Role of Light-Feeding Phase Relations on Entraining Robust Circadian Rhythms in the Periphery.Cerebrospinal fluid levels of inflammation, oxidative stress and NAD+ are linked to differences in plasma carotenoid concentrations.Nicotinamide-mediated inhibition of SIRT1 deacetylase is associated with the viability of cancer cells exposed to antitumor agents and apoptosis.Mechanism of inhibition of the human sirtuin enzyme SIRT3 by nicotinamide: computational and experimental studies Molecular modelling studies of sirtuin 2 inhibitors using three-dimensional structure-activity relationship analysis and molecular dynamics simulations.Selectivity hot-spots of sirtuin catalytic cores.Structural basis for allosteric, substrate-dependent stimulation of SIRT1 activity by resveratrol Finding Potent Sirt Inhibitor in Coffee: Isolation, Confirmation and Synthesis of Javamide-II (N-Caffeoyltryptophan) as Sirt1/2 Inhibitor SIRT6 Is a Positive Regulator of Aldose Reductase Expression in U937 and HeLa cells under Osmotic Stress: In Vitro and In Silico Insights.Investigating the Sensitivity of NAD+-dependent Sirtuin Deacylation Activities to NADH Anaplasma phagocytophilum increases the levels of histone modifying enzymes to inhibit cell apoptosis and facilitate pathogen infection in the tick vector Ixodes scapularis.Rhamnetin and cirsiliol induce radiosensitization and inhibition of epithelial-mesenchymal transition (EMT) by miR-34a-mediated suppression of Notch-1 expression in non-small cell lung cancer cell lines.The emerging and diverse roles of sirtuins in cancer: a clinical perspective.Changes in oxidative damage, inflammation and [NAD(H)] with age in cerebrospinal fluid.Evaluation of benzoic acid derivatives as sirtuin inhibitors.Regulation of a Protein Acetyltransferase in Myxococcus xanthus by the Coenzyme NADP.Schistosome sirtuins as drug targets.Seeding for sirtuins: microseed matrix seeding to obtain crystals of human Sirt3 and Sirt2 suitable for soaking.NAD and the aging process: Role in life, death and everything in between.Selective histone deacetylase small molecule inhibitors: recent progress and perspectives.The Current State of NAD(+) -Dependent Histone Deacetylases (Sirtuins) as Novel Therapeutic Targets.Carboxamide SIRT1 inhibitors block DBC1 binding via an acetylation-independent mechanism.Crystallographic structure of a small molecule SIRT1 activator-enzyme complex.Ligand-based virtual screening and inductive learning for identification of SIRT1 inhibitors in natural products.The SIRT1 inhibitor EX-527 suppresses mTOR activation and alleviates acute lung injury in mice with endotoxiemia.ADP-ribosyl-N₃: A Versatile Precursor for Divergent Syntheses of ADP-ribosylated Compounds.Sirtuins are Unaffected by PARP Inhibitors Containing Planar Nicotinamide Bioisosteres.In-silico analysis of Sirt2 from Schistosoma mansoni: structures, conformations, and interactions with inhibitors.IRF8 is the target of SIRT1 for the inflammation response in macrophages.Natural polyphenols as sirtuin 6 modulators.High protein intake is associated with low plasma NAD+ levels in a healthy human cohort Metformin Is a Direct SIRT1-Activating Compound: Computational Modeling and Experimental Validation

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The 2.5 Å crystal structure of the SIRT1 catalytic domain bound to nicotinamide adenine dinucleotide (NAD+) and an indole (EX527 analogue) reveals a novel mechanism of histone deacetylase inhibition

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2013 nî lūn-bûn

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2013 թուականի Փետրուարին հրատարակուած գիտական յօդուած

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Aiping Zhang

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Bradley Condon

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Feiyu Zhang

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Iain MacEwan

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James A Jamison

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Sheela Ashok

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10.1021/JM301431Y

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23311358

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crystal structure