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http://purl.uniprot.org/citations/12754521http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12754521http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12754521http://www.w3.org/2000/01/rdf-schema#comment"We describe here a strategy for the large-scale identification of N-glycosylated proteins from a complex biological sample. The approach, termed isotope-coded glycosylation-site-specific tagging (IGOT), is based on the lectin column-mediated affinity capture of a set of glycopeptides generated by tryptic digestion of protein mixtures, followed by peptide-N-glycosidase-mediated incorporation of a stable isotope tag, 18O, specifically into the N-glycosylation site. The 18O-tagged peptides are then identified by multi-dimensional liquid chromatography-mass spectrometry (LC-MS)-based technology. The application of this method to the characterization of N-linked high-mannose and/or hybrid-type glycoproteins from an extract of Caenorhabditis elegans proteins allowed the identification of 250 glycoproteins, including 83 putative transmembrane proteins, with the simultaneous determination of 400 unique N-glycosylation sites. Because the method is applicable to the systematic identification of a wide range of glycoproteins, it should facilitate basic glycobiology research and may be useful for diagnostic applications, such as genome-wide screening for disease-related glycoproteins."xsd:string
http://purl.uniprot.org/citations/12754521http://purl.org/dc/terms/identifier"doi:10.1038/nbt829"xsd:string
http://purl.uniprot.org/citations/12754521http://purl.org/dc/terms/identifier"doi:10.1038/nbt829"xsd:string
http://purl.uniprot.org/citations/12754521http://purl.uniprot.org/core/author"Hirabayashi J."xsd:string
http://purl.uniprot.org/citations/12754521http://purl.uniprot.org/core/author"Hirabayashi J."xsd:string
http://purl.uniprot.org/citations/12754521http://purl.uniprot.org/core/author"Isobe T."xsd:string
http://purl.uniprot.org/citations/12754521http://purl.uniprot.org/core/author"Isobe T."xsd:string
http://purl.uniprot.org/citations/12754521http://purl.uniprot.org/core/author"Saito H."xsd:string
http://purl.uniprot.org/citations/12754521http://purl.uniprot.org/core/author"Saito H."xsd:string
http://purl.uniprot.org/citations/12754521http://purl.uniprot.org/core/author"Yamauchi Y."xsd:string
http://purl.uniprot.org/citations/12754521http://purl.uniprot.org/core/author"Yamauchi Y."xsd:string
http://purl.uniprot.org/citations/12754521http://purl.uniprot.org/core/author"Takahashi N."xsd:string
http://purl.uniprot.org/citations/12754521http://purl.uniprot.org/core/author"Takahashi N."xsd:string
http://purl.uniprot.org/citations/12754521http://purl.uniprot.org/core/author"Kaji H."xsd:string
http://purl.uniprot.org/citations/12754521http://purl.uniprot.org/core/author"Kaji H."xsd:string
http://purl.uniprot.org/citations/12754521http://purl.uniprot.org/core/author"Shinkawa T."xsd:string
http://purl.uniprot.org/citations/12754521http://purl.uniprot.org/core/author"Shinkawa T."xsd:string
http://purl.uniprot.org/citations/12754521http://purl.uniprot.org/core/author"Taoka M."xsd:string
http://purl.uniprot.org/citations/12754521http://purl.uniprot.org/core/author"Taoka M."xsd:string
http://purl.uniprot.org/citations/12754521http://purl.uniprot.org/core/author"Kasai K."xsd:string
http://purl.uniprot.org/citations/12754521http://purl.uniprot.org/core/author"Kasai K."xsd:string
http://purl.uniprot.org/citations/12754521http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12754521http://purl.uniprot.org/core/date"2003"xsd:gYear