SIRT3 substrate specificity determined by peptide arrays and machine learning. - Test2 - elhamkhani - TriplyDB

SIRT3 substrate specificity determined by peptide arrays and machine learning.

SIRT3 substrate specificity determined by peptide arrays and machine learning.

http://www.wikidata.org/entity/Q33718384

about

SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways Histone recognition and large-scale structural analysis of the human bromodomain family An acetylome peptide microarray reveals specificities and deacetylation substrates for all human sirtuin isoforms.Insights into Lysine Deacetylation of Natively Folded Substrate Proteins by Sirtuins.Rejuvenating sirtuins: the rise of a new family of cancer drug targets A Chemical Biology Approach to Reveal Sirt6-targeted Histone H3 Sites in Nucleosomes.Biotinylation of lysine method identifies acetylated histone H3 lysine 79 in Saccharomyces cerevisiae as a substrate for Sir2 Sirtuin catalysis and regulation Sirt3 promotes the urea cycle and fatty acid oxidation during dietary restriction Profiling deacetylase activities in cell lysates with peptide arrays and SAMDI mass spectrometry.Metabolic Regulation by Lysine Malonylation, Succinylation, and Glutarylation.Mechanisms and Dynamics of Protein Acetylation in Mitochondria.Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.Widespread and enzyme-independent Nε-acetylation and Nε-succinylation of proteins in the chemical conditions of the mitochondrial matrix.Identification of lysine succinylation substrates and the succinylation regulatory enzyme CobB in Escherichia coli Roles of SIRT3 in heart failure: from bench to bedside.Substrate Specificity Profiling of Histone-Modifying Enzymes by Peptide Microarray.ArrayNinja: An Open Source Platform for Unified Planning and Analysis of Microarray Experiments.Deciphering enzyme function using peptide arrays.Fine tuning our cellular factories: sirtuins in mitochondrial biology.Intramolecular long-distance nucleophilic reactions as a rapid fluorogenic switch applicable to the detection of enzymatic activity.Mitochondrial Sirtuin Network Reveals Dynamic SIRT3-Dependent Deacetylation in Response to Membrane Depolarization.Site-specific reactivity of nonenzymatic lysine acetylation.Mechanism of Sirt1 NAD+-dependent Protein Deacetylase Inhibition by Cysteine S-Nitrosation.Characterization of CobB kinetics and inhibition by nicotinamide.Sirtuin 1-Chromatin-Binding Dynamics Points to a Common Mechanism Regulating Inflammatory Targets in SIV Infection and in the Aging Brain.Metabolically Derived Lysine Acylations and Neighboring Modifications Tune the Binding of the BET Bromodomains to Histone H4.The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications.

P2860

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P2860

SIRT3 substrate specificity determined by peptide arrays and machine learning.

http://www.wikidata.org/entity/Q33718384

description

2010 nî lūn-bûn

@nan

2010 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի նոյեմբերին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年学术文章

@wuu

2010年学术文章

@zh-cn

2010年学术文章

@zh-hans

2010年学术文章

@zh-my

2010年学术文章

@zh-sg

2010年學術文章

@yue

name

SIRT3 substrate specificity determined by peptide arrays and machine learning.

@ast

SIRT3 substrate specificity determined by peptide arrays and machine learning.

@en

type

label

SIRT3 substrate specificity determined by peptide arrays and machine learning.

@ast

SIRT3 substrate specificity determined by peptide arrays and machine learning.

@en

prefLabel

SIRT3 substrate specificity determined by peptide arrays and machine learning.

@ast

SIRT3 substrate specificity determined by peptide arrays and machine learning.

@en

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P1433

ACS Chemical Biology

P1476

SIRT3 substrate specificity determined by peptide arrays and machine learning.

@en

P2093

Burr Settles

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

John M Denu

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

Mark W Craven

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

William C Hallows

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

P2860

Negative control of p53 by Sir2alpha promotes cell survival under stress

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

Reversible lysine acetylation controls the activity of the mitochondrial enzyme acetyl-CoA synthetase 2

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

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

Regulation of cellular metabolism by protein lysine acetylation

SIRT6 is a histone H3 lysine 9 deacetylase that modulates telomeric chromatin

Identification and characterization of proteins interacting with SIRT1 and SIRT3: implications in the anti-aging and metabolic effects of sirtuins

Substrates and regulation mechanisms for the human mitochondrial sirtuins Sirt3 and Sirt5

Crystal structures of human SIRT3 displaying substrate-induced conformational changes

P304

146-157

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10.1021/CB100218D

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2

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6

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2010-11-01T00:00:00Z

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47427576

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20945913

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machine learning

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3042044

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