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http://purl.uniprot.org/citations/11181563http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11181563http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11181563http://www.w3.org/2000/01/rdf-schema#comment"The cDNAs encoding two human homologs of the Xenopus oocyte lectin, XL35, were isolated from a small intestine cDNA library and termed HL-1 and HL-2. The deduced amino acid sequence of each homolog is about 60% identical and 80% similar to that of XL35, and none of these sequences contains the C-type lectin motif, although it is known that XL35 requires calcium for ligand binding. By Northern analysis, HL-1 transcripts are present at relatively high levels in heart, small intestine, colon, thymus, ovary, and testis. HL-2 transcripts, by contrast, are expressed only in small intestine. Immunocytochemistry using a polyclonal antibody produced against XL35 shows HL-1 protein to be localized exclusively in endothelial cells in colon, thymus, liver, and other tissues. Primary cultures of human aortic endothelial cells are positive for HL-1 expression by immunoblotting and by PCR analysis, but several other human cell types are not. HL-1 and -2 are both encoded at chromosome 1q23, the same locus that encodes the selectins. XL35, HL-1 and -2, and another mouse homolog are members of a new family of proteins whose members most likely perform diverse functions."xsd:string
http://purl.uniprot.org/citations/11181563http://purl.org/dc/terms/identifier"doi:10.1093/glycob/11.1.65"xsd:string
http://purl.uniprot.org/citations/11181563http://purl.org/dc/terms/identifier"doi:10.1093/glycob/11.1.65"xsd:string
http://purl.uniprot.org/citations/11181563http://purl.uniprot.org/core/author"Lee J.K."xsd:string
http://purl.uniprot.org/citations/11181563http://purl.uniprot.org/core/author"Lee J.K."xsd:string
http://purl.uniprot.org/citations/11181563http://purl.uniprot.org/core/author"Pang M."xsd:string
http://purl.uniprot.org/citations/11181563http://purl.uniprot.org/core/author"Pang M."xsd:string
http://purl.uniprot.org/citations/11181563http://purl.uniprot.org/core/author"Moremen K.W."xsd:string
http://purl.uniprot.org/citations/11181563http://purl.uniprot.org/core/author"Moremen K.W."xsd:string
http://purl.uniprot.org/citations/11181563http://purl.uniprot.org/core/author"Baum L.G."xsd:string
http://purl.uniprot.org/citations/11181563http://purl.uniprot.org/core/author"Baum L.G."xsd:string
http://purl.uniprot.org/citations/11181563http://purl.uniprot.org/core/author"Pierce M."xsd:string
http://purl.uniprot.org/citations/11181563http://purl.uniprot.org/core/author"Pierce M."xsd:string
http://purl.uniprot.org/citations/11181563http://purl.uniprot.org/core/author"Schnee J."xsd:string
http://purl.uniprot.org/citations/11181563http://purl.uniprot.org/core/author"Schnee J."xsd:string
http://purl.uniprot.org/citations/11181563http://purl.uniprot.org/core/author"Wolfert M."xsd:string
http://purl.uniprot.org/citations/11181563http://purl.uniprot.org/core/author"Wolfert M."xsd:string
http://purl.uniprot.org/citations/11181563http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11181563http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11181563http://purl.uniprot.org/core/name"Glycobiology"xsd:string
http://purl.uniprot.org/citations/11181563http://purl.uniprot.org/core/name"Glycobiology"xsd:string
http://purl.uniprot.org/citations/11181563http://purl.uniprot.org/core/pages"65-73"xsd:string
http://purl.uniprot.org/citations/11181563http://purl.uniprot.org/core/pages"65-73"xsd:string