Alcohol-induced protein hyperacetylation: mechanisms and consequences - Test2 - elhamkhani - TriplyDB

Alcohol-induced protein hyperacetylation: mechanisms and consequences

Alcohol-induced protein hyperacetylation: mechanisms and consequences

http://www.wikidata.org/entity/Q37135970

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Mitochondrial acetylome analysis in a mouse model of alcohol-induced liver injury utilizing SIRT3 knockout mice Aberrant post-translational protein modifications in the pathogenesis of alcohol-induced liver injury The Altered Hepatic Tubulin Code in Alcoholic Liver Disease Alcohol-induced serotonergic modulation: the role of histone deacetylases Chronic ethanol consumption induces global hepatic protein hyperacetylation.Alcohol-related brain damage in humans.Alcohol-induced alterations of the hepatocyte cytoskeleton Moderate, chronic ethanol feeding exacerbates carbon-tetrachloride-induced hepatic fibrosis via hepatocyte-specific hypoxia inducible factor 1α Ethanol sensitizes mitochondria to the permeability transition by inhibiting deacetylation of cyclophilin-D mediated by sirtuin-3 4-Hydroxynonenal inhibits SIRT3 via thiol-specific modification.Effects of alcohol on histone deacetylase 2 (HDAC2) and the neuroprotective role of trichostatin A (TSA)Histone H3K9 modifications are a local chromatin event involved in ethanol-induced neuroadaptation of the NR2B gene.Lysine acetylation induced by chronic ethanol consumption impairs dynamin-mediated clathrin-coated vesicle release Hepatic microtubule acetylation and stability induced by chronic alcohol exposure impair nuclear translocation of STAT3 and STAT5B, but not Smad2/3.Alcohol-induced defects in hepatic transcytosis may be explained by impaired dynein function Molecular mechanisms of ethanol-associated oro-esophageal squamous cell carcinoma.Mitochondrial sirtuins and metabolic homeostasis Post-translational modification of proteins in toxicological research: focus on lysine acylation.Alcohol consumption impairs hepatic protein trafficking: mechanisms and consequences.Alterations in Histone Acetylases and Acetylated Histone Expression in Aging, Ethanol-Fed Rats.Binge ethanol-induced HDAC3 down-regulates Cpt1α expression leading to hepatic steatosis and injury.Pathogenesis of alcoholic liver disease.Cellular analysis of the action of epigenetic drugs and probes.Binge alcohol-induced microvesicular liver steatosis and injury are associated with down-regulation of hepatic Hdac 1, 7, 9, 10, 11 and up-regulation of Hdac 3.Histone acetylation and arachidonic acid cytotoxicity in HepG2 cells overexpressing CYP2E1.Multilevel regulation of autophagosome content by ethanol oxidation in HepG2 cells.β-Caryophyllene protects against alcoholic steatohepatitis by attenuating inflammation and metabolic dysregulation in mice.Ethanol exposure inhibits hepatocyte lipophagy by inactivating the small guanosine triphosphatase Rab7.

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Alcohol-induced protein hyperacetylation: mechanisms and consequences

http://www.wikidata.org/entity/Q37135970

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on March 2009

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Alcohol-induced protein hyperacetylation: mechanisms and consequences

@en

Alcohol-induced protein hyperacetylation: mechanisms and consequences.

@nl

type

label

Alcohol-induced protein hyperacetylation: mechanisms and consequences

@en

Alcohol-induced protein hyperacetylation: mechanisms and consequences.

@nl

prefLabel

Alcohol-induced protein hyperacetylation: mechanisms and consequences

@en

Alcohol-induced protein hyperacetylation: mechanisms and consequences.

@nl

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World Journal of Gastroenterology

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Alcohol-induced protein hyperacetylation: mechanisms and consequences

@en

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Blythe D Shepard

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

Pamela L Tuma

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

P2860

Three proteins define a class of human histone deacetylases related to yeast Hda1p

Characterization of five human cDNAs with homology to the yeast SIR2 gene: Sir2-like proteins (sirtuins) metabolize NAD and may have protein ADP-ribosyltransferase activity

Identification of a human histone acetyltransferase related to monocytic leukemia zinc finger protein

Identification of HDAC10, a novel class II human histone deacetylase containing a leucine-rich domain

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

The orphan nuclear receptor Rev-erbalpha recruits the N-CoR/histone deacetylase 3 corepressor to regulate the circadian Bmal1 gene

Sirtuin functions in health and disease

Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins

SIRT1 regulates circadian clock gene expression through PER2 deacetylation

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1219-1230

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scholarly article

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10.3748/WJG.15.1219

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10

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15

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2009-03-01T00:00:00Z

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50863755

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19291822

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2658852

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