About: Characterization of the histone acetyltransferase (HAT) domain of a bifunctional protein with activable O-GlcNAcase and HAT activities

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About: Characterization of the histone acetyltransferase (HAT) domain of a bifunctional protein with activable O-GlcNAcase and HAT activities Goto Sponge NotDistinct Permalink

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rdf:type	Item
description	artículu científicu espublizáu en 2004 (ast) vědecký článek publikovaný v roce 2004 (cs) 2004 թվականի դեկտեմբերին հրատարակված գիտական հոդված (hy) наукова стаття, опублікована в грудні 2004 (uk) 2004 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած (hyw) im Dezember 2004 veröffentlichter wissenschaftlicher Artikel (de) vedecký článok (publikovaný 2004/12/17) (sk) wetenschappelijk artikel (gepubliceerd op 2004/12/17) (nl) مقالة علمية (نشرت في 17-12-2004) (ar) article publié dans la revue scientifique Journal of Biological Chemistry (fr) scientific journal article (en)
publication date	wds:Q28579795-B839676B-14B4-4E8D-ABCF-378EA5419FA3
publication date	2004-12-17 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q28579795-94A55679-D262-4B3A-A8CE-338ECC705316
language of work or name	English
author name string	wds:Q28579795-17D5B206-ACCA-4E7F-B61E-FBB782E45B33 wds:Q28579795-34366499-A26B-4025-ABB4-53BDD1EF0C02 wds:Q28579795-B2373C84-1B7E-4CB9-A5C0-3F948A6DE0C8 wds:Q28579795-F9DF44EE-BF12-4BE7-AA7E-658762BEAE5D
author name string	Jeffrey E. Kudlow Andrew J. Paterson Thomas R. Whisenhunt Clifford Toleman
rdfs:label	Characterization of the histone acetyltransferase (HAT) domain of a bifunctional protein with activable O-GlcNAcase and HAT activities (en) Characterization of the histone acetyltransferase (HAT) domain of a bifunctional protein with activable O-GlcNAcase and HAT activities (nl) Characterization of the histone acetyltransferase (HAT) domain of a bifunctional protein with activable O-GlcNAcase and HAT activities (ast)
skos:prefLabel	Characterization of the histone acetyltransferase (HAT) domain of a bifunctional protein with activable O-GlcNAcase and HAT activities (en) Characterization of the histone acetyltransferase (HAT) domain of a bifunctional protein with activable O-GlcNAcase and HAT activities (nl) Characterization of the histone acetyltransferase (HAT) domain of a bifunctional protein with activable O-GlcNAcase and HAT activities (ast)
name	Characterization of the histone acetyltransferase (HAT) domain of a bifunctional protein with activable O-GlcNAcase and HAT activities (en) Characterization of the histone acetyltransferase (HAT) domain of a bifunctional protein with activable O-GlcNAcase and HAT activities (nl) Characterization of the histone acetyltransferase (HAT) domain of a bifunctional protein with activable O-GlcNAcase and HAT activities (ast)
title	wds:Q28579795-940A76FF-C314-46E2-AD2D-0EDF86E283D8
title	Characterization of the histone acetyltransferase (HAT) domain of a bifunctional protein with activable O-GlcNAcase and HAT activities (en)
page(s)	wds:Q28579795-C34BD6CE-C699-441B-BEAB-7DF65A172F70
page(s)	53665–53673
instance of	wds:Q28579795-6AF911D6-986F-4C0B-868D-8F3B593309CD
instance of	scholarly article
PubMed ID	wds:Q28579795-25EF306D-AAAC-465B-8646-DF09C01AB651
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/15485860
PubMed ID	15485860
published in	wds:Q28579795-0DA3811C-9418-4DB1-9A84-76938AAE128C
published in	Journal of Biological Chemistry
issue	wds:Q28579795-04D7C9AC-A8E5-4A5E-95EF-28C36799180B
volume	wds:Q28579795-FDB0C972-C6C2-4B5F-8FE9-CD3CA93C1E3B
issue	51
volume	279
DOI	wds:Q28579795-FF619D19-2F9F-497C-AD8E-9A017ADEBC60
DOI	http://dx.doi.org/10.1074/JBC.M410406200
DOI	10.1074/JBC.M410406200
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q28579795
is cites work of	Metabolism, cytoskeleton and cellular signalling in the grip of protein Nepsilon - and O-acetylation The hexosamine signaling pathway: O-GlcNAc cycling in feast or famine Site-specific interplay between O-GlcNAcylation and phosphorylation in cellular regulation O-GlcNAcylation and oxidation of proteins: is signalling in the cardiovascular system becoming sweeter? Elevated O-GlcNAc levels activate epigenetically repressed genes and delay mouse ESC differentiation without affecting naïve to primed cell transition. Blocking O-linked GlcNAc cycling in Drosophila insulin-producing cells perturbs glucose-insulin homeostasis Phosphoinositide signalling links O-GlcNAc transferase to insulin resistance Hexosamines, insulin resistance, and the complications of diabetes: current status Disrupting the enzyme complex regulating O-GlcNAcylation blocks signaling and development Modification of histones by sugar β-N-acetylglucosamine (GlcNAc) occurs on multiple residues, including histone H3 serine 10, and is cell cycle-regulated Caenorhabditis elegans ortholog of a diabetes susceptibility locus: oga-1 (O-GlcNAcase) knockout impacts O-GlcNAc cycling, metabolism, and dauer Perturbations in O-linked beta-N-acetylglucosamine protein modification cause severe defects in mitotic progression and cytokinesis Hsp90 and environmental impacts on epigenetic states: a model for the trans-generational effects of diethylstibesterol on uterine development and cancer HATs and HDACs: from structure, function and regulation to novel strategies for therapy and prevention Homocitrate synthase connects amino acid metabolism to chromatin functions through Esa1 and DNA damage O-GlcNAcylation/phosphorylation cycling at Ser10 controls both transcriptional activity and stability of delta-lactoferrin A lipid-droplet-targeted O-GlcNAcase isoform is a key regulator of the proteasome Increased O-GlcNAc causes disrupted lens fiber cell differentiation and cataracts The hexosamine signaling pathway: deciphering the "O-GlcNAc code" Cycling of O-linked beta-N-acetylglucosamine on nucleocytoplasmic proteins O-linked beta-N-acetylglucosamine (O-GlcNAc): Extensive crosstalk with phosphorylation to regulate signaling and transcription in response to nutrients and stress The Early Metazoan Trichoplax adhaerens Possesses a Functional O-GlcNAc System Three-dimensional structure of aStreptomyces sviceusGNAT acetyltransferase with similarity to the C-terminal domain of the human GH84O-GlcNAcase Toxic effects of hyperglycemia are mediated by the hexosamine signaling pathway and o-linked glycosylation in early mouse embryos A little sugar goes a long way: the cell biology of O-GlcNAc Epigenetic switching by the metabolism-sensing factors in the generation of orexin neurons from mouse embryonic stem cells. Nutrient-driven O-GlcNAc cycling - think globally but act locally Synergy of Peptide and Sugar in O-GlcNAcase Substrate Recognition Dynamic O-GlcNAc cycling at promoters of Caenorhabditis elegans genes regulating longevity, stress, and immunity Cross talk between O-GlcNAcylation and phosphorylation: roles in signaling, transcription, and chronic disease The intersections between O-GlcNAcylation and phosphorylation: implications for multiple signaling pathways O-GlcNAc signalling: implications for cancer cell biology Protein O-GlcNAcylation: a new signaling paradigm for the cardiovascular system. Role of protein O-linked N-acetyl-glucosamine in mediating cell function and survival in the cardiovascular system AMP-activated protein kinase and p38 MAPK activate O-GlcNAcylation of neuronal proteins during glucose deprivation O-GlcNAcase is essential for embryonic development and maintenance of genomic stability O-GlcNAc cycling: implications for neurodegenerative disorders O-GlcNAc integrates the proteasome and transcriptome to regulate nuclear hormone receptors Structure and mechanism of a bacterial beta-glucosaminidase having O-GlcNAcase activity Structural insights into the mechanism and inhibition of eukaryotic O-GlcNAc hydrolysis Reduction of O-GlcNAc protein modification does not prevent insulin resistance in 3T3-L1 adipocytes Chemical approaches to understanding O-GlcNAc glycosylation in the brain O-GlcNAc signaling in the cardiovascular system Protein O-GlcNAcylation: A critical regulator of the cellular response to stress. Proteome wide purification and identification of O-GlcNAc-modified proteins using click chemistry and mass spectrometry Post-translational protein modification by O-linked N-acetyl-glucosamine: its role in mediating the adverse effects of diabetes on the heart. Characterization of beta-N-acetylglucosaminidase cleavage by caspase-3 during apoptosis O-GlcNAcylation: a novel pathway contributing to the effects of endothelin in the vasculature.

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