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http://purl.uniprot.org/citations/6423630http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/6423630http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/6423630http://www.w3.org/2000/01/rdf-schema#comment"Two complementing mutations in lipid-linked oligosaccharide biosynthesis have been isolated following a [3H]mannose suicide enrichment. Rather than making the wild type precursor oligosaccharide, Glc3man9Glc-NA2-P-P-dolichol, the mutants, alg5-1 and alg6-1, accumulate Man9GlcNAc2-P-P-dolichol as their largest lipid-linked oligosaccharide in vivo and in vitro. When UDP-[3H]Glc was added to microsomal membranes of each mutant, neither could elongate Man9GlcNAc2-P-P-dolichol and only alg6-1 could synthesize dolichol-phosphoglucose. When dolicholphospho[3H]glucose was added to microsomes from alg5-1, alg6-1, or the parental strain, only alg5-1 and the parental strain made glucosylated lipid-linked oligosaccharides. These results indicate that alg5-1 cells are unable to synthesize dolichol phosphoglucose while alg6-1 cells are unable to transfer glucose from dolichol phosphoglucose to the unglucosylated lipid-linked oligosaccharide. We also present evidence that both mutants transfer Man9GlcNAc2 to protein."xsd:string
http://purl.uniprot.org/citations/6423630http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(17)43676-3"xsd:string
http://purl.uniprot.org/citations/6423630http://purl.uniprot.org/core/author"Robbins P.W."xsd:string
http://purl.uniprot.org/citations/6423630http://purl.uniprot.org/core/author"Runge K.W."xsd:string
http://purl.uniprot.org/citations/6423630http://purl.uniprot.org/core/author"Huffaker T.C."xsd:string
http://purl.uniprot.org/citations/6423630http://purl.uniprot.org/core/date"1984"xsd:gYear
http://purl.uniprot.org/citations/6423630http://purl.uniprot.org/core/name"J Biol Chem"xsd:string
http://purl.uniprot.org/citations/6423630http://purl.uniprot.org/core/pages"412-417"xsd:string
http://purl.uniprot.org/citations/6423630http://purl.uniprot.org/core/title"Two yeast mutations in glucosylation steps of the asparagine glycosylation pathway."xsd:string
http://purl.uniprot.org/citations/6423630http://purl.uniprot.org/core/volume"259"xsd:string
http://purl.uniprot.org/citations/6423630http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/6423630
http://purl.uniprot.org/citations/6423630http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/6423630
http://purl.uniprot.org/citations/6423630http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/6423630
http://purl.uniprot.org/citations/6423630http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/6423630
http://purl.uniprot.org/enzyme/2.4.1.267http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/6423630
http://purl.uniprot.org/uniprot/#_Q12001-mappedCitation-6423630http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/6423630
http://purl.uniprot.org/uniprot/#_P40350-mappedCitation-6423630http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/6423630
http://purl.uniprot.org/uniprot/Q12001http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/6423630
http://purl.uniprot.org/uniprot/P40350http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/6423630