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http://purl.uniprot.org/citations/12855678http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12855678http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12855678http://www.w3.org/2000/01/rdf-schema#comment"Sulfation of endothelial glycoproteins by the sulfotransferase GlcNAc6ST-2 is a regulatory modification that promotes binding of the leukocyte adhesion molecule L-selectin. GlcNAc6ST-2 is a member of a family of related enzymes that act on similar carbohydrate substrates in vitro but discrete glycoproteins in vivo. We demonstrate that GlcNAc6ST-1, -2, and -3 have distinct Golgi distributions, with GlcNAc6ST-1 confined to the trans-Golgi network, GlcNAc6ST-3 confined to the early secretory pathway, and GlcNAc6ST-2 distributed throughout the Golgi. Their localization was correlated with preferred activity on either N-linked or O-linked glycoproteins. A chimera comprising the localization domain of GlcNAc6ST-1 fused to the catalytic domain of GlcNAc6ST-2 was confined to the trans-Golgi network and adopted the substrate preference of GlcNAc6ST-1. We propose a model in which Golgi enzyme localization and competition orchestrate the biosynthesis of L-selectin ligands."xsd:string
http://purl.uniprot.org/citations/12855678http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m304928200"xsd:string
http://purl.uniprot.org/citations/12855678http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m304928200"xsd:string
http://purl.uniprot.org/citations/12855678http://purl.uniprot.org/core/author"Bertozzi C.R."xsd:string
http://purl.uniprot.org/citations/12855678http://purl.uniprot.org/core/author"Bertozzi C.R."xsd:string
http://purl.uniprot.org/citations/12855678http://purl.uniprot.org/core/author"de Graffenried C.L."xsd:string
http://purl.uniprot.org/citations/12855678http://purl.uniprot.org/core/author"de Graffenried C.L."xsd:string
http://purl.uniprot.org/citations/12855678http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12855678http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12855678http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/12855678http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/12855678http://purl.uniprot.org/core/pages"40282-40295"xsd:string
http://purl.uniprot.org/citations/12855678http://purl.uniprot.org/core/pages"40282-40295"xsd:string
http://purl.uniprot.org/citations/12855678http://purl.uniprot.org/core/title"Golgi localization of carbohydrate sulfotransferases is a determinant of L-selectin ligand biosynthesis."xsd:string
http://purl.uniprot.org/citations/12855678http://purl.uniprot.org/core/title"Golgi localization of carbohydrate sulfotransferases is a determinant of L-selectin ligand biosynthesis."xsd:string
http://purl.uniprot.org/citations/12855678http://purl.uniprot.org/core/volume"278"xsd:string
http://purl.uniprot.org/citations/12855678http://purl.uniprot.org/core/volume"278"xsd:string
http://purl.uniprot.org/citations/12855678http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12855678
http://purl.uniprot.org/citations/12855678http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12855678
http://purl.uniprot.org/citations/12855678http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/12855678
http://purl.uniprot.org/citations/12855678http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/12855678
http://purl.uniprot.org/uniprot/Q9GZS9http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/12855678
http://purl.uniprot.org/uniprot/Q8NCG5http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/12855678