The Metabolic Chemical Reporter 6-Azido-6-deoxy-glucose Further Reveals the Substrate Promiscuity of O-GlcNAc Transferase and Catalyzes the Discovery of Intracellular Protein Modification by O-Glucose.

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The Metabolic Chemical Reporter 6-Azido-6-deoxy-glucose Further Reveals the Substrate Promiscuity of O-GlcNAc Transferase and Catalyzes the Discovery of Intracellular Protein Modification by O-Glucose. is …
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scholarly articleQ13442814

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P356DOI10.1021/JACS.7B13488
P932PMC publication ID6540071
P698PubMed publication ID29771506

P50authorMatthew R PrattQ58663598
Christina M. WooQ88067104
P2093author name stringNarek Darabedian
Kelly N Chuh
Jinxu Gao
P2860cites workChemistry-enabled methods for the visualization of cell-surface glycoproteins in MetazoansQ38443091
Hijacking a biosynthetic pathway yields a glycosyltransferase inhibitor within cells.Q38845236
Protein O-GlcNAcylation: emerging mechanisms and functionsQ39295247
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Quantitative time-resolved chemoproteomics reveals that stable O-GlcNAc regulates box C/D snoRNP biogenesisQ42798614
Chemical reporter for visualizing metabolic cross-talk between carbohydrate metabolism and protein modificationQ42798931
The Small Molecule 2-Azido-2-deoxy-glucose Is a Metabolic Chemical Reporter of O-GlcNAc Modifications in Mammalian Cells, Revealing an Unexpected Promiscuity of O-GlcNAc Transferase.Q42803344
N-Propargyloxycarbamate monosaccharides as metabolic chemical reporters of carbohydrate salvage pathways and protein glycosylation.Q42827963
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Artificial Cysteine S-Glycosylation Induced by Per-O-Acetylated Unnatural Monosaccharides during Metabolic Glycan LabelingQ47252874
Catalytic Promiscuity of O-GlcNAc Transferase Enables Unexpected Metabolic Engineering of Cytoplasmic Proteins with 2-Azido-2-deoxy-glucoseQ48171368
Mapping and quantification of over 2,000 O-linked glycopeptides in activated human T cells with isotope-targeted glycoproteomics (IsoTaG).Q49913262
6''-Azido-6''-deoxy-UDP-N-acetylglucosamine as a glycosyltransferase substrateQ83312805
The O-GlcNAc transferase gene resides on the X chromosome and is essential for embryonic stem cell viability and mouse ontogenyQ24685967
Proteome wide purification and identification of O-GlcNAc-modified proteins using click chemistry and mass spectrometryQ27334695
A potent mechanism-inspired O-GlcNAcase inhibitor that blocks phosphorylation of tau in vivoQ27650997
Structural snapshots of the reaction coordinate for O-GlcNAc transferaseQ27674735
Cloning of the glutamine:fructose-6-phosphate amidotransferase gene from yeast. Pheromonal regulation of its transcriptionQ27935574
Cell surface engineering by a modified Staudinger reactionQ28138842
Metabolic cross-talk allows labeling of O-linked beta-N-acetylglucosamine-modified proteins via the N-acetylgalactosamine salvage pathwayQ30498243
Glycopeptide-specific monoclonal antibodies suggest new roles for O-GlcNAcQ33802435
Changes in metabolic chemical reporter structure yield a selective probe of O-GlcNAc modificationQ34145247
A metabolic labeling approach toward proteomic analysis of mucin-type O-linked glycosylationQ34386471
Chemical reporters for fluorescent detection and identification of O-GlcNAc-modified proteins reveal glycosylation of the ubiquitin ligase NEDD4-1Q35002612
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A chemical approach for identifying O-GlcNAc-modified proteins in cellsQ35242785
A little sugar goes a long way: the cell biology of O-GlcNAcQ35261648
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.Q35939748
Isotope-targeted glycoproteomics (IsoTaG): a mass-independent platform for intact N- and O-glycopeptide discovery and analysis.Q36142717
Monoclonal antibodies identify a group of nuclear pore complex glycoproteinsQ36216116
Ogt-dependent X-chromosome-linked protein glycosylation is a requisite modification in somatic cell function and embryo viabilityQ36233025
Site-specific O-glucosylation of the epidermal growth factor-like (EGF) repeats of notch: efficiency of glycosylation is affected by proper folding and amino acid sequence of individual EGF repeatsQ36298276
Chemical Methods for Encoding and Decoding of Posttranslational ModificationsQ36654176
Chemical approaches to study O-GlcNAcylationQ36809063
Comprehensive mapping of O-GlcNAc modification sites using a chemically cleavable tagQ36998516
Drosophila O-GlcNAc transferase (OGT) is encoded by the Polycomb group (PcG) gene, super sex combs (sxc).Q37303993
O-GlcNAc processing enzymes: catalytic mechanisms, substrate specificity, and enzyme regulation.Q38059293
P433issue23
P407language of work or nameEnglishQ1860
P921main subjectgeneral chemistryQ909510
glucoseQ37525
P304page(s)7092-7100
P577publication date2018-05-30
P1433published inJournal of the American Chemical SocietyQ898902
P1476titleThe Metabolic Chemical Reporter 6-Azido-6-deoxy-glucose Further Reveals the Substrate Promiscuity of O-GlcNAc Transferase and Catalyzes the Discovery of Intracellular Protein Modification by O-Glucose
P478volume140

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cites work (P2860)
Q99557041A Pragmatic Guide to Enrichment Strategies for Mass Spectrometry-based Glycoproteomics
Q59715259Azide- and Alkyne-Bearing Metabolic Chemical Reporters of Glycosylation Show Structure-Dependent Feedback Inhibition of the Hexosamine Biosynthetic Pathway
Q90929338Legionella effector SetA as a general O-glucosyltransferase for eukaryotic proteins
Q90185969The O-GlcNAc Modification on Kinases

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