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http://purl.uniprot.org/citations/7875291http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7875291http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7875291http://www.w3.org/2000/01/rdf-schema#comment"We have detected sialyltransferase activity of recombinant mouse STX, which was cloned from rat brain as a new member of the sialyltransferase family, but sialyltransferase activity of which had not been detected previously [Livingston and Paulson, J. Biol. Chem. (1993) 268, 11504-11507]. The activity of mouse STX was specific toward sialylated glycoproteins. N-Glycanase treatment and linkage-specific sialidase treatment of glycoproteins revealed that STX transfers sialic acids through alpha 2,8-linkages to only N-linked oligosaccharides of glycoproteins. However, polymerase activity for polysialic acid synthesis was not detected for this sialyltransferase. Since this alpha 2,8-sialyltransferase gene is highly restricted in fetal and newborn brain, it may be involved in the polysialylation of glycoproteins, especially of N-CAM."xsd:string
http://purl.uniprot.org/citations/7875291http://purl.org/dc/terms/identifier"doi:10.1016/0014-5793(95)00059-i"xsd:string
http://purl.uniprot.org/citations/7875291http://purl.org/dc/terms/identifier"doi:10.1016/0014-5793(95)00059-i"xsd:string
http://purl.uniprot.org/citations/7875291http://purl.uniprot.org/core/author"Kurosawa N."xsd:string
http://purl.uniprot.org/citations/7875291http://purl.uniprot.org/core/author"Kurosawa N."xsd:string
http://purl.uniprot.org/citations/7875291http://purl.uniprot.org/core/author"Yoshida Y."xsd:string
http://purl.uniprot.org/citations/7875291http://purl.uniprot.org/core/author"Yoshida Y."xsd:string
http://purl.uniprot.org/citations/7875291http://purl.uniprot.org/core/author"Kojima N."xsd:string
http://purl.uniprot.org/citations/7875291http://purl.uniprot.org/core/author"Kojima N."xsd:string
http://purl.uniprot.org/citations/7875291http://purl.uniprot.org/core/author"Lee Y.C."xsd:string
http://purl.uniprot.org/citations/7875291http://purl.uniprot.org/core/author"Lee Y.C."xsd:string
http://purl.uniprot.org/citations/7875291http://purl.uniprot.org/core/author"Tsuji S."xsd:string
http://purl.uniprot.org/citations/7875291http://purl.uniprot.org/core/author"Tsuji S."xsd:string
http://purl.uniprot.org/citations/7875291http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7875291http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7875291http://purl.uniprot.org/core/name"FEBS Lett."xsd:string
http://purl.uniprot.org/citations/7875291http://purl.uniprot.org/core/name"FEBS Lett."xsd:string
http://purl.uniprot.org/citations/7875291http://purl.uniprot.org/core/pages"1-4"xsd:string
http://purl.uniprot.org/citations/7875291http://purl.uniprot.org/core/pages"1-4"xsd:string
http://purl.uniprot.org/citations/7875291http://purl.uniprot.org/core/title"Enzymatic activity of a developmentally regulated member of the sialyltransferase family (STX): evidence for alpha 2,8-sialyltransferase activity toward N-linked oligosaccharides."xsd:string
http://purl.uniprot.org/citations/7875291http://purl.uniprot.org/core/title"Enzymatic activity of a developmentally regulated member of the sialyltransferase family (STX): evidence for alpha 2,8-sialyltransferase activity toward N-linked oligosaccharides."xsd:string
http://purl.uniprot.org/citations/7875291http://purl.uniprot.org/core/volume"360"xsd:string
http://purl.uniprot.org/citations/7875291http://purl.uniprot.org/core/volume"360"xsd:string