Structural Basis for Nicotinamide Inhibition and Base Exchange in Sir2 Enzymes - Wikidata - awgldk - TriplyDB

Structural Basis for Nicotinamide Inhibition and Base Exchange in Sir2 Enzymes

Structural Basis for Nicotinamide Inhibition and Base Exchange in Sir2 Enzymes

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Crystal structures of human SIRT3 displaying substrate-induced conformational changes Histone Deacetylases and Their Inhibition in Candida Species Structural basis for sirtuin activity and inhibition A Molecular Mechanism for Direct Sirtuin Activation by Resveratrol Structural and Functional Analysis of Human SIRT1 Acetylation of TUG protein promotes the accumulation of GLUT4 glucose transporters in an insulin-responsive intracellular compartment A role for histone H4K16 hypoacetylation in Saccharomyces cerevisiae kinetochore function Modulation of epigenetic targets for anticancer therapy: clinicopathological relevance, structural data and drug discovery perspectives Opposing effects of sirtuins on neuronal survival: SIRT1-mediated neuroprotection is independent of its deacetylase activity SIRT3 substrate specificity determined by peptide arrays and machine learning.Selective small molecule inhibition of poly(ADP-ribose) glycohydrolase (PARG).Structure and biochemical functions of SIRT6.Insight into the Mechanism of Intramolecular Inhibition of the Catalytic Activity of Sirtuin 2 (SIRT2).Chemistry of acetyl transfer by histone modifying enzymes: structure, mechanism and implications for effector design.Sirtuin inhibitors.Structural basis for sirtuin function: what we know and what we don't.Sirtuin-3 (SIRT3), a therapeutic target with oncogenic and tumor-suppressive function in cancer.Sirtuin 1 (SIRT1): the misunderstood HDAC.Deacylation Mechanism by SIRT2 Revealed in the 1'-SH-2'-O-Myristoyl Intermediate Structure.New synthetic approach to paullones and characterization of their SIRT1 inhibitory activity.Intracellular NAD levels regulate tumor necrosis factor protein synthesis in a sirtuin-dependent manner.Physical nature of intermolecular interactions inside Sir2 homolog active site: molecular dynamics and ab initio study.Mechanistic studies on the effects of nicotinamide on megakaryocytic polyploidization and the roles of NAD+ levels and SIRT inhibition.Plasmodium falciparum Sir2: an unusual sirtuin with dual histone deacetylase and ADP-ribosyltransferase activity.Highly dissociative and concerted mechanism for the nicotinamide cleavage reaction in Sir2Tm enzyme suggested by ab initio QM/MM molecular dynamics simulations.beta-1,2,3-Triazolyl-nucleosides as nicotinamide riboside mimics.Characterization of CobB kinetics and inhibition by nicotinamide.Differentiation of Islet Progenitors Regulated by Nicotinamide into Transcriptome-Verified β Cells That Ameliorate Diabetes.Structure Function Analysis of Leishmania Sirtuin: An Ensemble of In Silico and Biochemical Studies Computer- and Structure-Based Lead Identification for Epigenetic Targets

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P2860

Structural Basis for Nicotinamide Inhibition and Base Exchange in Sir2 Enzymes

http://www.wikidata.org/entity/Q27643772

description

2007 nî lūn-bûn

@nan

2007 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2007 թվականի փետրվարին հրատարակված գիտական հոդված

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2007年の論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年论文

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name

Structural Basis for Nicotinamide Inhibition and Base Exchange in Sir2 Enzymes

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Structural Basis for Nicotinamide Inhibition and Base Exchange in Sir2 Enzymes

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Structural Basis for Nicotinamide Inhibition and Base Exchange in Sir2 Enzymes

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label

Structural Basis for Nicotinamide Inhibition and Base Exchange in Sir2 Enzymes

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Structural Basis for Nicotinamide Inhibition and Base Exchange in Sir2 Enzymes

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Structural Basis for Nicotinamide Inhibition and Base Exchange in Sir2 Enzymes

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prefLabel

Structural Basis for Nicotinamide Inhibition and Base Exchange in Sir2 Enzymes

@ast

Structural Basis for Nicotinamide Inhibition and Base Exchange in Sir2 Enzymes

@en

Structural Basis for Nicotinamide Inhibition and Base Exchange in Sir2 Enzymes

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J.MOLCEL.2006.12.022

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Structural Basis for Nicotinamide Inhibition and Base Exchange in Sir2 Enzymes

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Brandi D Sanders

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

James T Slama

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

Kehao Zhao

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

P2860

Negative control of p53 by Sir2alpha promotes cell survival under stress

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

Sir2 regulates skeletal muscle differentiation as a potential sensor of the redox state

Structural basis for nicotinamide cleavage and ADP-ribose transfer by NAD(+)-dependent Sir2 histone/protein deacetylases

The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms

Involvement of the histone deacetylase SIRT1 in chicken ovalbumin upstream promoter transcription factor (COUP-TF)-interacting protein 2-mediated transcriptional repression

Improved methods for building protein models in electron density maps and the location of errors in these models

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Crystal structure of a SIR2 homolog-NAD complex

Structural basis for the NAD-dependent deacetylase mechanism of Sir2

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463-72

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scholarly article

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10.1016/J.MOLCEL.2006.12.022

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3

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25

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Ronen Marmorstein

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2007-02-09T00:00:00Z

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6514626

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17289592

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