About: Regulation of a cytosolic and nuclear O-GlcNAc transferase. Role of the tetratricopeptide repeats

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rdf:type	Item
description	наукова стаття, опублікована в листопаді 1999 (uk) artículu científicu espublizáu en 1999 (ast) 1999 թվականի նոյեմբերին հրատարակված գիտական հոդված (hy) vědecký článek publikovaný v roce 1999 (cs) 1999 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած (hyw) article publié dans la revue scientifique Journal of Biological Chemistry (fr) im November 1999 veröffentlichter wissenschaftlicher Artikel (de) scientific journal article (en) wetenschappelijk artikel (gepubliceerd op 1999/11/05) (nl) vedecký článok (publikovaný 1999/11/05) (sk) مقالة علمية (نشرت في 5-11-1999) (ar)
publication date	wds:Q28581400-DCE5ADD7-A9A3-4E3A-B1F6-0FD4DAFF93D3
publication date	1999-11-05 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q28581400-B0C46300-3189-4ABB-99D6-D5FCC5296C16
language of work or name	English
author name string	wds:Q28581400-3AD3069E-C737-4A66-B089-85A544A42672 wds:Q28581400-E68881A7-5BD0-41BE-AA47-586E2FF534EE
OpenCitations bibliographic resource ID	wds:Q28581400-175FB18B-B886-489F-A3B4-7AA2EE30321F
OpenCitations bibliographic resource ID	https://w3id.org/oc/corpus/br/3736777
author name string	G. W. Hart L. K. Kreppel
OpenCitations bibliographic resource ID	3736777
rdfs:label	Regulation of a cytosolic and nuclear O-GlcNAc transferase. Role of the tetratricopeptide repeats (en) Regulation of a cytosolic and nuclear O-GlcNAc transferase. Role of the tetratricopeptide repeats (nl) Regulation of a cytosolic and nuclear O-GlcNAc transferase. Role of the tetratricopeptide repeats (ast)
skos:prefLabel	Regulation of a cytosolic and nuclear O-GlcNAc transferase. Role of the tetratricopeptide repeats (en) Regulation of a cytosolic and nuclear O-GlcNAc transferase. Role of the tetratricopeptide repeats (nl) Regulation of a cytosolic and nuclear O-GlcNAc transferase. Role of the tetratricopeptide repeats (ast)
name	Regulation of a cytosolic and nuclear O-GlcNAc transferase. Role of the tetratricopeptide repeats (en) Regulation of a cytosolic and nuclear O-GlcNAc transferase. Role of the tetratricopeptide repeats (nl) Regulation of a cytosolic and nuclear O-GlcNAc transferase. Role of the tetratricopeptide repeats (ast)
title	wds:Q28581400-8FF5EC06-5732-4DEF-A4A0-16B9ADBACB25
title	Regulation of a cytosolic and nuclear O-GlcNAc transferase. Role of the tetratricopeptide repeats (en)
page(s)	wds:Q28581400-028E136F-0B23-4F15-96A1-BB4DC9C87AA7
page(s)	32015–32022
instance of	wds:Q28581400-1A6F52E7-88C8-43DB-A12A-97B0EB90ED50
instance of	scholarly article
PubMed ID	wds:Q28581400-724F7984-EEEC-45E8-A38A-C0AC8A2D3B3F
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/10542233
PubMed ID	10542233
published in	wds:Q28581400-B35331DC-319E-4A21-BC44-16BDA0DDF805
published in	Journal of Biological Chemistry
issue	wds:Q28581400-F17CC161-715A-4386-AF46-DC953EB83FC4
volume	wds:Q28581400-DC38E47C-8E27-43E9-A180-B46651B8DFB0
issue	45
volume	274
DOI	wds:Q28581400-654AFC93-9D20-4989-844A-D6957D88630E
DOI	http://dx.doi.org/10.1074/JBC.274.45.32015
DOI	10.1074/JBC.274.45.32015
ResearchGate publication ID	wds:Q28581400-51B30C9E-188A-437E-9CFF-0D2D91EB9293
ResearchGate publication ID	12758976
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q28581400
is cites work of	Tet proteins connect the O-linked N-acetylglucosamine transferase Ogt to chromatin in embryonic stem cells TET2 promotes histone O-GlcNAcylation during gene transcription Elevation of Global O-GlcNAc Levels in 3T3-L1 Adipocytes by Selective Inhibition of O-GlcNAcase Does Not Induce Insulin Resistance The hexosamine signaling pathway: O-GlcNAc cycling in feast or famine O-GlcNAcylation: The Sweet Side of the Cancer O-Linked N-Acetylglucosamine and Cancer: Messages from the Glycosylation of C-Myc Cross-talk between GlcNAcylation and phosphorylation: roles in insulin resistance and glucose toxicity Site-specific interplay between O-GlcNAcylation and phosphorylation in cellular regulation Glucosamine protects neonatal cardiomyocytes from ischemia-reperfusion injury via increased protein-associated O-GlcNAc A neutral diphosphate mimic crosslinks the active site of human O-GlcNAc transferase Combining high-energy C-trap dissociation and electron transfer dissociation for protein O-GlcNAc modification site assignment SPINDLY and GIGANTEA interact and act in Arabidopsis thaliana pathways involved in light responses, flowering, and rhythms in cotyledon movements. Metabolism, cell surface organization, and disease Hexosamines, insulin resistance, and the complications of diabetes: current status Elevated nucleocytoplasmic glycosylation by O-GlcNAc results in insulin resistance associated with defects in Akt activation in 3T3-L1 adipocytes Reduced O-GlcNAcylation links lower brain glucose metabolism and tau pathology in Alzheimer's disease Two O-linked N-acetylglucosamine transferase genes of Arabidopsis thaliana L. Heynh. have overlapping functions necessary for gamete and seed development O-GlcNAc: a regulatory post-translational modification. Ogt-dependent X-chromosome-linked protein glycosylation is a requisite modification in somatic cell function and embryo viability Perturbations in O-linked beta-N-acetylglucosamine protein modification cause severe defects in mitotic progression and cytokinesis Mutational analysis of the catalytic domain of O-linked N-acetylglucosaminyl transferase Bittersweet memories: linking metabolism to epigenetics through O-GlcNAcylation Hyaluronan synthase 1 (HAS1) requires higher cellular UDP-GlcNAc concentration than HAS2 and HAS3. A chemical approach for identifying O-GlcNAc-modified proteins in cells Insights into O-linked N-acetylglucosamine ([0-9]O-GlcNAc) processing and dynamics through kinetic analysis of O-GlcNAc transferase and O-GlcNAcase activity on protein substrates. O-GlcNAcylation of TAB1 modulates TAK1-mediated cytokine release. The coactivator of transcription CREB-binding protein interacts preferentially with the glycosylated form of Stat5. O-GlcNAcylation/phosphorylation cycling at Ser10 controls both transcriptional activity and stability of delta-lactoferrin Genome of the extremely radiation-resistant bacterium Deinococcus radiodurans viewed from the perspective of comparative genomics Structure of human O-GlcNAc transferase and its complex with a peptide substrate The hexosamine signaling pathway: deciphering the "O-GlcNAc code" Regulation of the O-linked beta-N-acetylglucosamine transferase by insulin signaling. Localization of the O-GlcNAc transferase and O-GlcNAc-modified proteins in rat cerebellar cortex Systematic identification of genes with coding microsatellites mutated in DNA mismatch repair-deficient cancer cells. Dysregulation of insulin signaling, glucose transporters, O-GlcNAcylation, and phosphorylation of tau and neurofilaments in the brain: Implication for Alzheimer's disease Structural insights into mechanism and specificity of O-GlcNAc transferase Alloxan is an inhibitor of the enzyme O-linked N-acetylglucosamine transferase O-linked beta-N-acetylglucosamine (O-GlcNAc): Extensive crosstalk with phosphorylation to regulate signaling and transcription in response to nutrients and stress O-GlcNAc turns twenty: functional implications for post-translational modification of nuclear and cytosolic proteins with a sugar Mitochondrial and nucleocytoplasmic isoforms of O-linked GlcNAc transferase encoded by a single mammalian gene The Early Metazoan Trichoplax adhaerens Possesses a Functional O-GlcNAc System Intracellular glycosylation and development Roles of the Tetratricopeptide Repeat Domain in O-GlcNAc Transferase Targeting and Protein Substrate Specificity Gibberellin signaling: biosynthesis, catabolism, and response pathways SPINDLY is a nuclear-localized repressor of gibberellin signal transduction expressed throughout the plant Ectopic expression of the tetratricopeptide repeat domain of SPINDLY causes defects in gibberellin response O-GlcNAc modifications regulate cell survival and epiboly during zebrafish development

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