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http://purl.uniprot.org/citations/7559387http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7559387http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7559387http://www.w3.org/2000/01/rdf-schema#comment"P-selectin glycoprotein ligand-1 (PSGL-1) is a mucin-like glycoprotein on leukocytes that is a high affinity ligand for P-selectin. Previous studies have shown that sialylation and fucosylation of PSGL-1 are required for its binding to P-selectin, but other post-translational modifications of PSGL-1 may also be important. We demonstrate that PSGL-1 synthesized in human HL-60 cells can be metabolically labeled with [35S]sulfate that is incorporated primarily into tyrosine sulfate. Treatment of PSGL-1 with a bacterial arylsulfatase releases sulfate from tyrosine, resulting in a concordant decrease in binding to P-selectin. These studies demonstrate that tyrosine sulfate on PSGL-1 functions in conjunction with sialylated and fucosylated glycans to mediate high affinity binding to P-selectin."xsd:string
http://purl.uniprot.org/citations/7559387http://purl.org/dc/terms/identifier"doi:10.1074/jbc.270.39.22677"xsd:string
http://purl.uniprot.org/citations/7559387http://purl.org/dc/terms/identifier"doi:10.1074/jbc.270.39.22677"xsd:string
http://purl.uniprot.org/citations/7559387http://purl.uniprot.org/core/author"Cummings R.D."xsd:string
http://purl.uniprot.org/citations/7559387http://purl.uniprot.org/core/author"Cummings R.D."xsd:string
http://purl.uniprot.org/citations/7559387http://purl.uniprot.org/core/author"McEver R.P."xsd:string
http://purl.uniprot.org/citations/7559387http://purl.uniprot.org/core/author"McEver R.P."xsd:string
http://purl.uniprot.org/citations/7559387http://purl.uniprot.org/core/author"Moore K.L."xsd:string
http://purl.uniprot.org/citations/7559387http://purl.uniprot.org/core/author"Moore K.L."xsd:string
http://purl.uniprot.org/citations/7559387http://purl.uniprot.org/core/author"Wilkins P.P."xsd:string
http://purl.uniprot.org/citations/7559387http://purl.uniprot.org/core/author"Wilkins P.P."xsd:string
http://purl.uniprot.org/citations/7559387http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7559387http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7559387http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/7559387http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/7559387http://purl.uniprot.org/core/pages"22677-22680"xsd:string
http://purl.uniprot.org/citations/7559387http://purl.uniprot.org/core/pages"22677-22680"xsd:string
http://purl.uniprot.org/citations/7559387http://purl.uniprot.org/core/title"Tyrosine sulfation of P-selectin glycoprotein ligand-1 is required for high affinity binding to P-selectin."xsd:string
http://purl.uniprot.org/citations/7559387http://purl.uniprot.org/core/title"Tyrosine sulfation of P-selectin glycoprotein ligand-1 is required for high affinity binding to P-selectin."xsd:string
http://purl.uniprot.org/citations/7559387http://purl.uniprot.org/core/volume"270"xsd:string
http://purl.uniprot.org/citations/7559387http://purl.uniprot.org/core/volume"270"xsd:string
http://purl.uniprot.org/citations/7559387http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/7559387
http://purl.uniprot.org/citations/7559387http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/7559387