http://purl.uniprot.org/citations/12855678 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/12855678 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/12855678 | http://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/12855678 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m304928200"xsd:string |
http://purl.uniprot.org/citations/12855678 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m304928200"xsd:string |
http://purl.uniprot.org/citations/12855678 | http://purl.uniprot.org/core/author | "Bertozzi C.R."xsd:string |
http://purl.uniprot.org/citations/12855678 | http://purl.uniprot.org/core/author | "Bertozzi C.R."xsd:string |
http://purl.uniprot.org/citations/12855678 | http://purl.uniprot.org/core/author | "de Graffenried C.L."xsd:string |
http://purl.uniprot.org/citations/12855678 | http://purl.uniprot.org/core/author | "de Graffenried C.L."xsd:string |
http://purl.uniprot.org/citations/12855678 | http://purl.uniprot.org/core/date | "2003"xsd:gYear |
http://purl.uniprot.org/citations/12855678 | http://purl.uniprot.org/core/date | "2003"xsd:gYear |
http://purl.uniprot.org/citations/12855678 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
http://purl.uniprot.org/citations/12855678 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
http://purl.uniprot.org/citations/12855678 | http://purl.uniprot.org/core/pages | "40282-40295"xsd:string |
http://purl.uniprot.org/citations/12855678 | http://purl.uniprot.org/core/pages | "40282-40295"xsd:string |
http://purl.uniprot.org/citations/12855678 | http://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/12855678 | http://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/12855678 | http://purl.uniprot.org/core/volume | "278"xsd:string |
http://purl.uniprot.org/citations/12855678 | http://purl.uniprot.org/core/volume | "278"xsd:string |
http://purl.uniprot.org/citations/12855678 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/12855678 |
http://purl.uniprot.org/citations/12855678 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/12855678 |
http://purl.uniprot.org/citations/12855678 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/12855678 |
http://purl.uniprot.org/citations/12855678 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/12855678 |
http://purl.uniprot.org/uniprot/Q9GZS9 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/12855678 |
http://purl.uniprot.org/uniprot/Q8NCG5 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/12855678 |