The active site of O-GlcNAc transferase imposes constraints on substrate sequence
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Proteolysis of HCF-1 by Ser/Thr glycosylation-incompetent O-GlcNAc transferase:UDP-GlcNAc complexes.Activity Based High-Throughput Screening for Novel O-GlcNAc Transferase Substrates Using a Dynamic Peptide MicroarrayDual functionality of O-GlcNAc transferase is required for Drosophila development.O-GlcNAcylation Antagonizes Phosphorylation of CDH1 (CDC20 Homologue 1)Global Analysis of O-GlcNAc Glycoproteins in Activated Human T CellsNew insights: A role for O-GlcNAcylation in diabetic complications.Direct Monitoring of Protein O-GlcNAcylation by High-Resolution Native Mass SpectrometryMutations in N-acetylglucosamine (O-GlcNAc) transferase in patients with X-linked intellectual disabilityIn Vitro Biochemical Assays for O-GlcNAc-Processing Enzymes.Protein O-GlcNAcylation: emerging mechanisms and functions.Recognition of a glycosylation substrate by the O-GlcNAc transferase TPR repeatsA study of the structural properties of sites modified by the O-linked 6-N-acetylglucosamine transferase.Elucidating crosstalk mechanisms between phosphorylation and O-GlcNAcylation.Structural insights into the substrate binding adaptability and specificity of human O-GlcNAcaseDiscovery of a Low Toxicity O-GlcNAc Transferase (OGT) Inhibitor by Structure-based Virtual Screening of Natural ProductsElectrophilic probes for deciphering substrate recognition by O-GlcNAc transferase.Structures of human O-GlcNAcase and its complexes reveal a new substrate recognition mode.Carb cutting works better with a partner.Peptide microarray analysis of the cross-talk between O-GlcNAcylation and tyrosine phosphorylation.Mapping and quantification of over 2,000 O-linked glycopeptides in activated human T cells with isotope-targeted glycoproteomics (IsoTaG).Structural Basis for the Initiation of Glycosaminoglycan Biosynthesis by Human Xylosyltransferase 1.The O-GlcNAc Transferase Intellectual Disability Mutation L254F Distorts the TPR Helix.Thio-Linked UDP-Peptide Conjugates as O-GlcNAc Transferase Inhibitors.OGT (O-GlcNAc Transferase) Selectively Modifies Multiple Residues Unique to Lamin A.O-GlcNAc: A Sweetheart of the Cell Cycle and DNA Damage Response
P2860
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P2860
The active site of O-GlcNAc transferase imposes constraints on substrate sequence
description
2015 nî lūn-bûn
@nan
2015年の論文
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2015年論文
@yue
2015年論文
@zh-hant
2015年論文
@zh-hk
2015年論文
@zh-mo
2015年論文
@zh-tw
2015年论文
@wuu
2015年论文
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2015年论文
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name
The active site of O-GlcNAc transferase imposes constraints on substrate sequence
@ast
The active site of O-GlcNAc transferase imposes constraints on substrate sequence
@en
type
label
The active site of O-GlcNAc transferase imposes constraints on substrate sequence
@ast
The active site of O-GlcNAc transferase imposes constraints on substrate sequence
@en
prefLabel
The active site of O-GlcNAc transferase imposes constraints on substrate sequence
@ast
The active site of O-GlcNAc transferase imposes constraints on substrate sequence
@en
P2093
P2860
P356
P1476
The active site of O-GlcNAc transferase imposes constraints on substrate sequence
@en
P2093
David E Blair
Jana Alonso
Marianne Schimpl
Osama Albarbarawi
Shalini Pathak
Vladimir S Borodkin
P2860
P2888
P304
P356
10.1038/NSMB.3063
P577
2015-08-03T00:00:00Z