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http://purl.uniprot.org/citations/20507882http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20507882http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20507882http://www.w3.org/2000/01/rdf-schema#comment"The glycosylation of the extracellular protein alpha-dystroglycan is important for its ligand-binding activity, and altered or blocked glycosylation is associated with several forms of congenital muscular dystrophies. By immunoprecipitation and sialic acid capture-and-release enrichment strategies, we isolated tryptic glycopeptides of alpha-dystroglycan from human skeletal muscle. Nano-liquid chromatography tandem mass spectrometry was used to identify both glycopeptides and peptides corresponding to the mucin-like and C-terminal domain of alpha-dystroglycan. The O-glycans found had either Hex-O-Thr or HexNAc-O-Ser/Thr anchored structures, which were often elongated and frequently, but not always, terminated with sialic acid. The HexNAc-O-Ser/Thr, but not Hex-O-Thr glycopeptides, displayed heterogeneity regarding glycan core structures and level of glycosylation site occupancy. We demonstrate for the first time glycan attachment sites of the NeuAcHexHexNAcHex-O structure corresponding to the anticipated Neu5Acalpha3Galbeta4GlcNAcbeta2Man-O-glycan (sLacNAc-Man), within the mucin-like domain of human alpha-dystroglycan from human skeletal muscle. Twenty-five glycopeptides were characterized from human alpha-dystroglycan, which provide insight to the complex in vivo O-glycosylation of alpha-dystroglycan."xsd:string
http://purl.uniprot.org/citations/20507882http://purl.org/dc/terms/identifier"doi:10.1093/glycob/cwq082"xsd:string
http://purl.uniprot.org/citations/20507882http://purl.org/dc/terms/identifier"doi:10.1093/glycob/cwq082"xsd:string
http://purl.uniprot.org/citations/20507882http://purl.uniprot.org/core/author"Nilsson J."xsd:string
http://purl.uniprot.org/citations/20507882http://purl.uniprot.org/core/author"Nilsson J."xsd:string
http://purl.uniprot.org/citations/20507882http://purl.uniprot.org/core/author"Larson G."xsd:string
http://purl.uniprot.org/citations/20507882http://purl.uniprot.org/core/author"Larson G."xsd:string
http://purl.uniprot.org/citations/20507882http://purl.uniprot.org/core/author"Grahn A."xsd:string
http://purl.uniprot.org/citations/20507882http://purl.uniprot.org/core/author"Grahn A."xsd:string
http://purl.uniprot.org/citations/20507882http://purl.uniprot.org/core/author"Nilsson J.'"xsd:string
http://purl.uniprot.org/citations/20507882http://purl.uniprot.org/core/author"Nilsson J.'"xsd:string
http://purl.uniprot.org/citations/20507882http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20507882http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20507882http://purl.uniprot.org/core/name"Glycobiology"xsd:string
http://purl.uniprot.org/citations/20507882http://purl.uniprot.org/core/name"Glycobiology"xsd:string
http://purl.uniprot.org/citations/20507882http://purl.uniprot.org/core/pages"1160-1169"xsd:string
http://purl.uniprot.org/citations/20507882http://purl.uniprot.org/core/pages"1160-1169"xsd:string
http://purl.uniprot.org/citations/20507882http://purl.uniprot.org/core/title"Characterization of site-specific O-glycan structures within the mucin-like domain of {alpha}-dystroglycan from human skeletal muscle."xsd:string
http://purl.uniprot.org/citations/20507882http://purl.uniprot.org/core/title"Characterization of site-specific O-glycan structures within the mucin-like domain of {alpha}-dystroglycan from human skeletal muscle."xsd:string
http://purl.uniprot.org/citations/20507882http://purl.uniprot.org/core/volume"20"xsd:string
http://purl.uniprot.org/citations/20507882http://purl.uniprot.org/core/volume"20"xsd:string
http://purl.uniprot.org/citations/20507882http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/20507882
http://purl.uniprot.org/citations/20507882http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/20507882