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Selective Sirt2 inhibition by ligand-induced rearrangement of the active site.

Selective Sirt2 inhibition by ligand-induced rearrangement of the active site.

http://www.wikidata.org/entity/Q30316777

about

Sirtuin functions and modulation: from chemistry to the clinic Structure-Based Development of an Affinity Probe for Sirtuin 2 SIRT2 activates G6PD to enhance NADPH production and promote leukaemia cell proliferation Selectivity 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 Inhibitor Sirtuin 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 deacetylases An 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 SIRT2 MicroRNA-212-5p Prevents Dopaminergic Neuron Death by Inhibiting SIRT2 in MPTP-Induced Mouse Model of Parkinson's Disease Metformin Is a Direct SIRT1-Activating Compound: Computational Modeling and Experimental Validation

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P2860

Selective Sirt2 inhibition by ligand-induced rearrangement of the active site.

http://www.wikidata.org/entity/Q30316777

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

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Nature Communications

P1476

Selective Sirt2 inhibition by ligand-induced rearrangement of the active site

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P2093

Attila Lehotzky

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

Brian J North

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

Claudia Roessler

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

Clemens Steegborn

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

Karin Schmidtkunz

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

Kathrin I Ladwein

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

Markus Gajer

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

Martin Pannek

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

Tobias Rumpf

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

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SIRT2 as a Therapeutic Target for Age-Related Disorders

Structure of the histone deacetylase SIRT2

Negative control of p53 by Sir2alpha promotes cell survival under stress

hSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase

SIRT2 maintains genome integrity and suppresses tumorigenesis through regulating APC/C activity

Sirt5 is a NAD-dependent protein lysine demalonylase and desuccinylase

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

SIRT2 induces the checkpoint kinase BubR1 to increase lifespan

HDAC6 is a microtubule-associated deacetylase

A role for SIRT2-dependent histone H3K18 deacetylation in bacterial infection

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6263

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scholarly article

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10.1038/NCOMMS7263

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P478

6

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Stefan Gerhardt

Matthias Schiedel

Mike Schutkowski

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2015-02-12T00:00:00Z

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272190360

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1011862102

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25672491

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4339887

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