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http://purl.uniprot.org/citations/12464307http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12464307http://www.w3.org/2000/01/rdf-schema#comment"N-glycosylation is the most conserved form of protein glycosylation in eukaryotes, but the modifications of N-linked oligosaccharides in plants and invertebrates often differ greatly from those in vertebrates and sometimes result in immunogenic structures. By contrast, O-linked glycans tend to be a wide and disparate group of modifications. Whereas the forms of O-linked glycans in plants are unlike those in animals, studies on invertebrate O-glycosylation often yield information relevant to mammalian systems."xsd:string
http://purl.uniprot.org/citations/12464307http://purl.org/dc/terms/identifier"doi:10.1016/s0959-440x(02)00367-6"xsd:string
http://purl.uniprot.org/citations/12464307http://purl.uniprot.org/core/author"Wilson I.B."xsd:string
http://purl.uniprot.org/citations/12464307http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12464307http://purl.uniprot.org/core/name"Curr Opin Struct Biol"xsd:string
http://purl.uniprot.org/citations/12464307http://purl.uniprot.org/core/pages"569-577"xsd:string
http://purl.uniprot.org/citations/12464307http://purl.uniprot.org/core/title"Glycosylation of proteins in plants and invertebrates."xsd:string
http://purl.uniprot.org/citations/12464307http://purl.uniprot.org/core/volume"12"xsd:string
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