Structural insights into mechanism and specificity of O-GlcNAc transferase
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TET2 promotes histone O-GlcNAcylation during gene transcriptionStructure of human O-GlcNAc transferase and its complex with a peptide substrateGlycosyltransferase-mediated Sweet Modification in Oral StreptococciProteolysis of HCF-1 by Ser/Thr glycosylation-incompetent O-GlcNAc transferase:UDP-GlcNAc complexes.Substrate and product analogues as human O-GlcNAc transferase inhibitorsHuman OGA binds substrates in a conserved peptide recognition grooveStructural and Functional Analysis of a New Subfamily of Glycosyltransferases Required for Glycosylation of Serine-rich Streptococcal AdhesinsStructural Insights into the Glycosyltransferase Activity of the Actinobacillus pleuropneumoniae HMW1C-like ProteinO-GlcNAc transferase invokes nucleotide sugar pyrophosphate participation in catalysisSynergy of Peptide and Sugar in O-GlcNAcase Substrate RecognitionStructure of a bacterial putative acetyltransferase defines the fold of the human O-GlcNAcase C-terminal domainHCF-1 Is Cleaved in the Active Site of O-GlcNAc TransferaseStructure of a Novel O -Linked N -Acetyl-d-glucosamine ( O -GlcNAc) Transferase, GtfA, Reveals Insights into the Glycosylation of Pneumococcal Serine-rich Repeat AdhesinsGlycomimetics Targeting Glycosyltransferases: Synthetic, Computational and Structural Studies of Less-Polar ConjugatesA molecular description of cellulose biosynthesis.Evidence for a Functional O-Linked N-Acetylglucosamine (O-GlcNAc) System in the Thermophilic Bacterium Thermobaculum terrenumThe putative eukaryote-like O-GlcNAc transferase of the cyanobacterium Synechococcus elongatus PCC 7942 hydrolyzes UDP-GlcNAc and is involved in multiple cellular processes.Regulation of calcium/calmodulin-dependent kinase IV by O-GlcNAc modification.Mechanistic study of CMP-Neu5Ac hydrolysis by α2,3-sialyltransferase from Pasteurella dagmatis.The hexosamine signaling pathway: O-GlcNAc cycling in feast or famineO-linked beta-N-acetylglucosamine (O-GlcNAc): Extensive crosstalk with phosphorylation to regulate signaling and transcription in response to nutrients and stressO-GlcNAc protein modification in plants: Evolution and function.The Actinobacillus pleuropneumoniae HMW1C-like glycosyltransferase mediates N-linked glycosylation of the Haemophilus influenzae HMW1 adhesin.Identification of O-GlcNAc sites within peptides of the Tau protein and their impact on phosphorylation.A novel deconvolution method for modeling UDP-N-acetyl-D-glucosamine biosynthetic pathways based on (13)C mass isotopologue profiles under non-steady-state conditionsThe making of a sweet modification: structure and function of O-GlcNAc transferase.Substrate specificity provides insights into the sugar donor recognition mechanism of O-GlcNAc transferase (OGT).Polycomb repressive complex 2 is necessary for the normal site-specific O-GlcNAc distribution in mouse embryonic stem cells.Cytoplasmic N-glycosyltransferase of Actinobacillus pleuropneumoniae is an inverting enzyme and recognizes the NX(S/T) consensus sequence.The active site of O-GlcNAc transferase imposes constraints on substrate sequenceCross talk between O-GlcNAcylation and phosphorylation: roles in signaling, transcription, and chronic disease.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.The roles of O-linked β-N-acetylglucosamine in cardiovascular physiology and disease.Undetectable histone O-GlcNAcylation in mammalian cellsProduction of homogeneous glycoprotein with multisite modifications by an engineered N-glycosyltransferase mutant.Dual functionality of O-GlcNAc transferase is required for Drosophila development.Chemical approaches to study O-GlcNAcylation.Protein O-GlcNAcylation: a new signaling paradigm for the cardiovascular system.O-GlcNAc cycling: implications for neurodegenerative disorders.The alpha,alpha-difluorinated phosphonate L-pSer-analogue: an accessible chemical tool for studying kinase-dependent signal transduction.
P2860
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P2860
Structural insights into mechanism and specificity of O-GlcNAc transferase
description
2008 nî lūn-bûn
@nan
2008 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
Structural insights into mechanism and specificity of O-GlcNAc transferase
@ast
Structural insights into mechanism and specificity of O-GlcNAc transferase
@en
Structural insights into mechanism and specificity of O-GlcNAc transferase
@nl
type
label
Structural insights into mechanism and specificity of O-GlcNAc transferase
@ast
Structural insights into mechanism and specificity of O-GlcNAc transferase
@en
Structural insights into mechanism and specificity of O-GlcNAc transferase
@nl
prefLabel
Structural insights into mechanism and specificity of O-GlcNAc transferase
@ast
Structural insights into mechanism and specificity of O-GlcNAc transferase
@en
Structural insights into mechanism and specificity of O-GlcNAc transferase
@nl
P2093
P2860
P356
P1433
P1476
Structural insights into mechanism and specificity of O-GlcNAc transferase
@en
P2093
Adel F M Ibrahim
Alexander W Schüttelkopf
Andrew J Clarke
Daan M F van Aalten
Ramon Hurtado-Guerrero
Shalini Pathak
Sharon M Shepherd
Vladimir Borodkin
P2860
P304
P356
10.1038/EMBOJ.2008.186
P407
P577
2008-09-25T00:00:00Z