http://purl.uniprot.org/citations/12634323 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/12634323 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/12634323 | http://www.w3.org/2000/01/rdf-schema#comment | "Lec1 CHO cell mutants lack N-acetylglucosaminyltransferase I (GlcNAc-TI) activity and do not synthesize complex or hybrid N-glycans. The origins of six independent lec1 mutations are shown to reside in the coding region of the Mgat1 gene, proving that GlcNAc-TI is mutated in Lec1 mutants. One mutant has Mgat1 gene transcripts of reduced size, whereas the others possess transcripts of approximately normal size and amount containing a unique insertion or transition mutation that leads to a premature stop codon in the Mgat1 gene coding region. The lec1 mutation in the Lec3.2.8.1 mutant, a line used to generate minimally glycosylated membrane glycoproteins for X-ray crystallography, is a G insertion that leads to a nonsense codon after amino acid 391. The Pro-Lec1.3C line from the ATCC and in laboratory stocks, a line used widely for diverse purposes, possesses a C insertion in the Mgat1 gene coding exon, causing a frame shift and producing a stable, truncated approximately 24-kDa product. Mgat1 gene mutations were confirmed by sequencing genomic DNA PCR products. Mutant cDNAs were reverted by site-directed mutagenesis and shown to confer wild-type lectin binding and GlcNAc-TI activity on Lec1 transfectants. Surprisingly, three Mgat1 gene nucleotide changes previously reported in Pro-Lec1.3C cells (Puthalakath et al. [1996] J. Biol. Chem., 271, 27818-27822) were not detected in this study. These Lec1 mutants provide a novel cohort for investigating the effects on Golgi trafficking and kin recognition of deletion mutants of GlcNAc-TI expressed at endogenous rather than nonphysiological levels."xsd:string |
http://purl.uniprot.org/citations/12634323 | http://purl.org/dc/terms/identifier | "doi:10.1093/glycob/cwg003"xsd:string |
http://purl.uniprot.org/citations/12634323 | http://purl.org/dc/terms/identifier | "doi:10.1093/glycob/cwg003"xsd:string |
http://purl.uniprot.org/citations/12634323 | http://purl.uniprot.org/core/author | "Chen W."xsd:string |
http://purl.uniprot.org/citations/12634323 | http://purl.uniprot.org/core/author | "Chen W."xsd:string |
http://purl.uniprot.org/citations/12634323 | http://purl.uniprot.org/core/author | "Stanley P."xsd:string |
http://purl.uniprot.org/citations/12634323 | http://purl.uniprot.org/core/author | "Stanley P."xsd:string |
http://purl.uniprot.org/citations/12634323 | http://purl.uniprot.org/core/date | "2003"xsd:gYear |
http://purl.uniprot.org/citations/12634323 | http://purl.uniprot.org/core/date | "2003"xsd:gYear |
http://purl.uniprot.org/citations/12634323 | http://purl.uniprot.org/core/name | "Glycobiology"xsd:string |
http://purl.uniprot.org/citations/12634323 | http://purl.uniprot.org/core/name | "Glycobiology"xsd:string |
http://purl.uniprot.org/citations/12634323 | http://purl.uniprot.org/core/pages | "43-50"xsd:string |
http://purl.uniprot.org/citations/12634323 | http://purl.uniprot.org/core/pages | "43-50"xsd:string |
http://purl.uniprot.org/citations/12634323 | http://purl.uniprot.org/core/title | "Five Lec1 CHO cell mutants have distinct Mgat1 gene mutations that encode truncated N-acetylglucosaminyltransferase I."xsd:string |
http://purl.uniprot.org/citations/12634323 | http://purl.uniprot.org/core/title | "Five Lec1 CHO cell mutants have distinct Mgat1 gene mutations that encode truncated N-acetylglucosaminyltransferase I."xsd:string |
http://purl.uniprot.org/citations/12634323 | http://purl.uniprot.org/core/volume | "13"xsd:string |
http://purl.uniprot.org/citations/12634323 | http://purl.uniprot.org/core/volume | "13"xsd:string |
http://purl.uniprot.org/citations/12634323 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/12634323 |
http://purl.uniprot.org/citations/12634323 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/12634323 |
http://purl.uniprot.org/citations/12634323 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/12634323 |
http://purl.uniprot.org/citations/12634323 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/12634323 |
http://purl.uniprot.org/uniprot/Q924C0 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/12634323 |
http://purl.uniprot.org/uniprot/Q8CJ47 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/12634323 |