Selective Sirt2 inhibition by ligand-induced rearrangement of the active site.
about
Sirtuin functions and modulation: from chemistry to the clinicStructure-Based Development of an Affinity Probe for Sirtuin 2SIRT2 activates G6PD to enhance NADPH production and promote leukaemia cell proliferationSelectivity hot-spots of sirtuin catalytic cores.Successful strategies in the discovery of small-molecule epigenetic modulators with anticancer potential.Finding Potent Sirt Inhibitor in Coffee: Isolation, Confirmation and Synthesis of Javamide-II (N-Caffeoyltryptophan) as Sirt1/2 InhibitorSirtuin 2 mutations in human cancers impair its function in genome maintenance.Three-Component Aminoalkylations Yielding Dihydronaphthoxazine-Based Sirtuin Inhibitors: Scaffold Modification and Exploration of Space for Polar Side-Chains.Seeding for sirtuins: microseed matrix seeding to obtain crystals of human Sirt3 and Sirt2 suitable for soaking.Sirtuin 5: a review of structure, known inhibitors and clues for developing new inhibitors.Selective histone deacetylase small molecule inhibitors: recent progress and perspectives.The Current State of NAD(+) -Dependent Histone Deacetylases (Sirtuins) as Novel Therapeutic Targets.Chemical and structural biology of protein lysine deacetylasesAn improved fluorogenic assay for SIRT1, SIRT2, and SIRT3.Potent mechanism-based sirtuin-2-selective inhibition by an in situ-generated occupant of the substrate-binding site, "selectivity pocket" and NAD+-binding site.Second German-Catalan workshop on epigenetics & cancer.Modulation Of Microtubule Acetylation By The Interplay Of TPPP/p25, SIRT2 And New Anticancer Agents With Anti-SIRT2 Potency.Inhibitors of Trypanosoma cruzi Sir2 related protein 1 as potential drugs against Chagas disease.Thienopyrimidinone Based Sirtuin-2 (SIRT2)-Selective Inhibitors Bind in the Ligand Induced Selectivity Pocket.Crystal structures of SIRT3 reveal that the α2-α3 loop and α3-helix affect the interaction with long-chain acyl lysine.The crystal structure of the Leishmania infantum Silent Information Regulator 2 related protein 1: Implications to protein function and drug design.New chemical tools for probing activity and inhibition of the NAD+-dependent lysine deacylase sirtuin 2.Biophysical characterization of hit compounds for mechanism-based enzyme activation.SIRT2 Promotes the Migration and Invasion of Gastric Cancer through RAS/ERK/JNK/MMP-9 Pathway by Increasing PEPCK1-Related Metabolism.Identification of a novel small molecule that inhibits deacetylase but not defatty-acylase reaction catalysed by SIRT2MicroRNA-212-5p Prevents Dopaminergic Neuron Death by Inhibiting SIRT2 in MPTP-Induced Mouse Model of Parkinson's DiseaseMetformin Is a Direct SIRT1-Activating Compound: Computational Modeling and Experimental Validation
P2860
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P2860
Selective Sirt2 inhibition by ligand-induced rearrangement of the active site.
description
2015 nî lūn-bûn
@nan
2015 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2015 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2015年の論文
@ja
2015年論文
@yue
2015年論文
@zh-hant
2015年論文
@zh-hk
2015年論文
@zh-mo
2015年論文
@zh-tw
2015年论文
@wuu
name
Selective Sirt2 inhibition by ligand-induced rearrangement of the active site.
@ast
Selective Sirt2 inhibition by ligand-induced rearrangement of the active site.
@en
type
label
Selective Sirt2 inhibition by ligand-induced rearrangement of the active site.
@ast
Selective Sirt2 inhibition by ligand-induced rearrangement of the active site.
@en
prefLabel
Selective Sirt2 inhibition by ligand-induced rearrangement of the active site.
@ast
Selective Sirt2 inhibition by ligand-induced rearrangement of the active site.
@en
P2093
P2860
P50
P356
P1476
Selective Sirt2 inhibition by ligand-induced rearrangement of the active site
@en
P2093
Attila Lehotzky
Brian J North
Claudia Roessler
Clemens Steegborn
Karin Schmidtkunz
Kathrin I Ladwein
Markus Gajer
Martin Pannek
Tobias Rumpf
P2860
P2888
P356
10.1038/NCOMMS7263
P407
P50
P577
2015-02-12T00:00:00Z
P5875
P6179
1011862102