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

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

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

http://www.wikidata.org/entity/Q24564290

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Interactomic and pharmacological insights on human sirt-1 Crystal structures of human SIRT3 displaying substrate-induced conformational changes Structure-function analysis of the yeast NAD+-dependent tRNA 2'-phosphotransferase Tpt1 Structure of a human ASF1a-HIRA complex and insights into specificity of histone chaperone complex assembly Nuclear ADP-ribosylation reactions in mammalian cells: where are we today and where are we going?Potential Modulation of Sirtuins by Oxidative Stress Acylation of Biomolecules in Prokaryotes: a Widespread Strategy for the Control of Biological Function and Metabolic Stress Structural basis for sirtuin activity and inhibition Protective effects and mechanisms of sirtuins in the nervous system The role of mammalian sirtuins in the regulation of metabolism, aging, and longevity Structural Basis for Nicotinamide Inhibition and Base Exchange in Sir2 Enzymes NADH oxidase activity of Bacillus subtilis nitroreductase NfrA1: insight into its biological role The Bicyclic Intermediate Structure Provides Insights into the Desuccinylation Mechanism of Human Sirtuin 5 (SIRT5)A Molecular Mechanism for Direct Sirtuin Activation by Resveratrol Structural basis for allosteric stimulation of Sir2 activity by Sir4 binding Structural and Functional Analysis of Human SIRT1 Epigenetic polypharmacology: from combination therapy to multitargeted drugs Identification of a Class of Protein ADP-Ribosylating Sirtuins in Microbial Pathogens Mimetics of hormetic agents: stress-resistance triggers Damped-dynamics flexible fitting.Modulation of epigenetic targets for anticancer therapy: clinicopathological relevance, structural data and drug discovery perspectives Human sirt-1: molecular modeling and structure-function relationships of an unordered protein.Entamoeba histolytica sirtuin EhSir2a deacetylates tubulin and regulates the number of microtubular assemblies during the cell cycle.Sirt1 carboxyl-domain is an ATP-repressible domain that is transferrable to other proteins.SIRT3 substrate specificity determined by peptide arrays and machine learning.Reaction-driven de novo design, synthesis and testing of potential type II kinase inhibitors.Sirtuin chemical mechanisms Design and synthesis of compounds that extend yeast replicative lifespan.Insight the C-site pocket conformational changes responsible for sirtuin 2 activity using molecular dynamics simulations.Structure and biochemical functions of SIRT6.Sirtuins in neurodegenerative diseases: a biological-chemical perspective.Insight into the Mechanism of Intramolecular Inhibition of the Catalytic Activity of Sirtuin 2 (SIRT2).Swapping the gene-specific and regional silencing specificities of the Hst1 and Sir2 histone deacetylases.Nampt/PBEF/Visfatin: a regulator of mammalian health and longevity?A Genome-Wide Screen with Nicotinamide to Identify Sirtuin-Dependent Pathways in Saccharomyces cerevisiae.Mitochondrial sirtuins and metabolic homeostasis Sir2 protein deacetylases: evidence for chemical intermediates and functions of a conserved histidine.Selective overexpression of human SIRT1 in adipose tissue enhances energy homeostasis and prevents the deterioration of insulin sensitivity with ageing in mice Chemistry of acetyl transfer by histone modifying enzymes: structure, mechanism and implications for effector design.Mechanisms and molecular probes of sirtuins.

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P2860

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

http://www.wikidata.org/entity/Q24564290

description

2004 nî lūn-bûn

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2004 թուականի Մայիսին հրատարակուած գիտական յօդուած

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2004 թվականի մայիսին հրատարակված գիտական հոդված

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2004年の論文

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Structural basis for nicotinam ...... 2 histone/protein deacetylases

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Structural basis for nicotinam ...... 2 histone/protein deacetylases

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Structural basis for nicotinam ...... 2 histone/protein deacetylases

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Structural basis for nicotinam ...... 2 histone/protein deacetylases

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Structural basis for nicotinam ...... 2 histone/protein deacetylases

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Structural basis for nicotinam ...... 2 histone/protein deacetylases

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prefLabel

Structural basis for nicotinam ...... 2 histone/protein deacetylases

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Structural basis for nicotinam ...... 2 histone/protein deacetylases

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Structural basis for nicotinam ...... 2 histone/protein deacetylases

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PNAS.0401057101

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Proceedings of the National Academy of Sciences of the United States of America

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Structural basis for nicotinam ...... histone/protein deacetylases.

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P2093

Kehao Zhao

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

Robyn Harshaw

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Ronen Marmorstein

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Xiaomei Chai

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P2860

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

Human SIR2 deacetylates p53 and antagonizes PML/p53-induced cellular senescence.

p53 sites acetylated in vitro by PCAF and p300 are acetylated in vivo in response to DNA damage

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

Structure of a Sir2 enzyme bound to an acetylated p53 peptide

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