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http://purl.uniprot.org/citations/12770777http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12770777http://www.w3.org/2000/01/rdf-schema#comment"UDP-GlcNAc: alpha-3-D-mannoside beta1,2-N-acetylglucosaminyltransferase I (GnT I) is a Golgi-resident enzyme which transfers a GlcNAc residue in beta1,2 linkage to the Manalpha1,3Manbeta-terminus of (Manalpha1,6(Manalpha1,3)Manalpha1,6)(Manalpha1,3)Manbeta1,4GlcNAcbeta1,4GlcNAc-Asn-protein, thereby initiating the synthesis of hybrid N-glycans. Three Caenorhabditis elegans genes homologous to mammalian GnT I (designated gly-12, gly-13 and gly-14) have been cloned. All three cDNAs encode proteins with GnT I enzyme activity. We report in this paper the preparation by ultra-violet (UV) light irradiation in the presence of trimethylpsoralen, of mutants lacking either gly-12, gly-13 or gly-14. A double null mutation in the gly-12 and gly-14 genes (gly-14; gly-12) has also been prepared. These mutations are intragene deletions, removing large portions of the GnT I catalytic domain, and are therefore, all molecular nulls. The gly-12 and gly-14 mutants as well as the gly-14; gly-12 double mutant all displayed wild-type phenotypes, indicating that neither gly-12 nor gly-14 is necessary for worm development under standard laboratory conditions. In contrast, about 60% of the mutants lacking the gly-13 gene arrested as L1 larvae at 20 degrees C and the remaining 40% homozygous worms grew to adulthood but displayed severe morphological and behavioral defects despite the presence of the other two GnT I genes, gly-12 and gly-14. Attempts to rescue the gly-13 null phenotype with the wild type transgene were not successful. However, lethality co-segregated with the gly-13 deletion within 0.02 map units (mu) in genetic mapping experiments, suggesting that the gly-13 mutation is responsible for the phenotype."xsd:string
http://purl.uniprot.org/citations/12770777http://purl.org/dc/terms/identifier"doi:10.1016/s0300-9084(03)00009-9"xsd:string
http://purl.uniprot.org/citations/12770777http://purl.uniprot.org/core/author"Chen S."xsd:string
http://purl.uniprot.org/citations/12770777http://purl.uniprot.org/core/author"Schachter H."xsd:string
http://purl.uniprot.org/citations/12770777http://purl.uniprot.org/core/author"Spence A.M."xsd:string
http://purl.uniprot.org/citations/12770777http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12770777http://purl.uniprot.org/core/name"Biochimie"xsd:string
http://purl.uniprot.org/citations/12770777http://purl.uniprot.org/core/pages"391-401"xsd:string
http://purl.uniprot.org/citations/12770777http://purl.uniprot.org/core/title"Isolation of null alleles of the Caenorhabditis elegans gly-12, gly-13 and gly-14 genes, all of which encode UDP-GlcNAc: alpha-3-D-mannoside beta1,2-N-acetylglucosaminyltransferase I activity."xsd:string
http://purl.uniprot.org/citations/12770777http://purl.uniprot.org/core/volume"85"xsd:string
http://purl.uniprot.org/citations/12770777http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12770777
http://purl.uniprot.org/citations/12770777http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/12770777
http://purl.uniprot.org/uniprot/#_A0A4V0IKI8-mappedCitation-12770777http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/12770777
http://purl.uniprot.org/uniprot/#_A0A4V0IKM3-mappedCitation-12770777http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/12770777
http://purl.uniprot.org/uniprot/#_A0A4V0IL39-mappedCitation-12770777http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/12770777
http://purl.uniprot.org/uniprot/#_A0A4V0INP7-mappedCitation-12770777http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/12770777
http://purl.uniprot.org/uniprot/#_A0A4V0INX3-mappedCitation-12770777http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/12770777
http://purl.uniprot.org/uniprot/#_P34709-mappedCitation-12770777http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/12770777
http://purl.uniprot.org/uniprot/#_G8JY28-mappedCitation-12770777http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/12770777
http://purl.uniprot.org/uniprot/#_G5EBG7-mappedCitation-12770777http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/12770777
http://purl.uniprot.org/uniprot/#_G5EFK6-mappedCitation-12770777http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/12770777
http://purl.uniprot.org/uniprot/#_Q11068-mappedCitation-12770777http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/12770777
http://purl.uniprot.org/uniprot/#_Q18530-mappedCitation-12770777http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/12770777
http://purl.uniprot.org/uniprot/#_Q22271-mappedCitation-12770777http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/12770777