Histone h3 glutathionylation in proliferating mammalian cells destabilizes nucleosomal structure. - Wikidata - wikimedia - TriplyDB

Histone h3 glutathionylation in proliferating mammalian cells destabilizes nucleosomal structure.

Histone h3 glutathionylation in proliferating mammalian cells destabilizes nucleosomal structure.

http://www.wikidata.org/entity/Q37216435

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Post-translational modifications of histones that influence nucleosome dynamics Histone H2A.Z deregulation in prostate cancer. Cause or effect?Proteomic characterization of novel histone post-translational modifications.Proteome-wide detection and quantitative analysis of irreversible cysteine oxidation using long column UPLC-pSRM.Non-linear impact of glutathione depletion on C. elegans life span and stress resistance Identification and interrogation of combinatorial histone modifications.Getting down to the core of histone modifications.Posttranslational modifications of human histone H3: an update.Glutathionylspermidine in the modification of protein SH groups: the enzymology and its application to study protein glutathionylation.Impact of oxidative stress during pregnancy on fetal epigenetic patterns and early origin of vascular diseases.High-throughput screening of cellular redox sensors using modern redox proteomics approaches.Comprehensive Catalog of Currently Documented Histone Modifications.Exploring the emerging complexity in transcriptional regulation of energy homeostasis.Mitochondria and the non-genetic origins of cell-to-cell variability: More is different.Impact of posttranslational modifications of engineered cysteines on the substituted cysteine accessibility method: evidence for glutathionylation.Protein S-Glutathionylation Mediates Macrophage Responses to Metabolic Cues from the Extracellular Environment.The CENP-T C-terminus is exclusively proximal to H3.1 and not to H3.2 or H3.3.Perspectives on the interactions between metabolism, redox, and epigenetics in plants.The epigenetic landscape related to reactive oxygen species formation in the cardiovascular system.Glutamine Metabolism in Cancer: Understanding the Heterogeneity.Maintenance of glutathione levels and its importance in epigenetic regulation.Oxidative stress signaling to chromatin in health and disease.Metabolic programming of the epigenome: host and gut microbial metabolite interactions with host chromatin.The siRNA suppressor RTL1 is redox-regulated through glutathionylation of a conserved cysteine in the double-stranded-RNA-binding domain.Thiol Based Redox Signaling in Plant Nucleus.

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Histone h3 glutathionylation in proliferating mammalian cells destabilizes nucleosomal structure.

http://www.wikidata.org/entity/Q37216435

description

article científic

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article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on 21 May 2013

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vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

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name

Histone h3 glutathionylation i ...... bilizes nucleosomal structure.

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Histone h3 glutathionylation i ...... bilizes nucleosomal structure.

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Histone h3 glutathionylation i ...... bilizes nucleosomal structure.

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Histone h3 glutathionylation i ...... bilizes nucleosomal structure.

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Histone h3 glutathionylation i ...... bilizes nucleosomal structure.

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Histone h3 glutathionylation i ...... bilizes nucleosomal structure.

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Antioxidants & Redox Signaling

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Histone h3 glutathionylation i ...... bilizes nucleosomal structure.

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Amparo Gimeno

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Carme Pérez-Quilis

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Clemens Bönisch

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Federico V Pallardó

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Francisco Dasí

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Gloria Òlaso

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Jelena Markovic

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José Luis García-Giménez

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José Viña

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Mercè Capdevila

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P2860

Translating the Histone Code

Crystal structure of the nucleosome core particle at 2.8 A resolution

Expression patterns and post-translational modifications associated with mammalian histone H3 variants

Alteration of the nucleosomal DNA path in the crystal structure of a human nucleosome core particle.

The redox state of free nicotinamide-adenine dinucleotide phosphate in the cytoplasm of rat liver

Covalent histone modifications--miswritten, misinterpreted and mis-erased in human cancers

Structure and mechanism of mammalian thioredoxin reductase: the active site is a redox-active selenolthiol/selenenylsulfide formed from the conserved cysteine-selenocysteine sequence

Analysis of Relative Gene Expression Data Using Real-Time Quantitative PCR and the 2−ΔΔCT Method

The language of covalent histone modifications

Chromatin modifications and their function

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1305-1320

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scholarly article

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10.1089/ARS.2012.5021

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12

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19

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2013-05-21T00:00:00Z

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23541030

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