| pubmed-article:15130086 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15130086 | lifeskim:mentions | umls-concept:C1257890 | lld:lifeskim |
| pubmed-article:15130086 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:15130086 | lifeskim:mentions | umls-concept:C0017337 | lld:lifeskim |
| pubmed-article:15130086 | lifeskim:mentions | umls-concept:C0013139 | lld:lifeskim |
| pubmed-article:15130086 | lifeskim:mentions | umls-concept:C1879647 | lld:lifeskim |
| pubmed-article:15130086 | lifeskim:mentions | umls-concept:C2700640 | lld:lifeskim |
| pubmed-article:15130086 | lifeskim:mentions | umls-concept:C1334043 | lld:lifeskim |
| pubmed-article:15130086 | pubmed:issue | Pt 1 | lld:pubmed |
| pubmed-article:15130086 | pubmed:dateCreated | 2004-8-6 | lld:pubmed |
| pubmed-article:15130086 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15130086 | pubmed:abstractText | Insects express arthro-series glycosphingolipids, which contain an alpha1,4-linked GalNAc residue. To determine the genetic basis for this linkage, we cloned a cDNA (CG17223) from Drosophila melanogaster encoding a protein with homology to mammalian alpha1,4-glycosyltransferases and expressed it in the yeast Pichia pastoris. Culture supernatants from the transformed yeast were found to display a novel UDP-GalNAc:GalNAcbeta1,4GlcNAcbeta1-R alpha-N-acetylgalactosaminyltransferase activity when using either a glycolipid, p-nitrophenylglycoside or an N-glycan carrying one or two terminal beta-N-acetylgalactosamine residues. NMR and MS in combination with glycosidase digestion and methylation analysis indicate that the cloned cDNA encodes an alpha1,4-N-acetylgalactosaminyltransferase. We hypothesize that this enzyme and its orthologues in other insects are required for the biosynthesis of the N5a and subsequent members of the arthro-series of glycolipids as well as of N-glycan receptors for Bacillus thuringiensis crystal toxin Cry1Ac. | lld:pubmed |
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| pubmed-article:15130086 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15130086 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15130086 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15130086 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15130086 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15130086 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:15130086 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15130086 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15130086 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:15130086 | pubmed:issn | 1470-8728 | lld:pubmed |
| pubmed-article:15130086 | pubmed:author | pubmed-author:KosmaPaulP | lld:pubmed |
| pubmed-article:15130086 | pubmed:author | pubmed-author:LochnitGünter... | lld:pubmed |
| pubmed-article:15130086 | pubmed:author | pubmed-author:WilsonIain... | lld:pubmed |
| pubmed-article:15130086 | pubmed:author | pubmed-author:HofingerAndre... | lld:pubmed |
| pubmed-article:15130086 | pubmed:author | pubmed-author:PaschingerKat... | lld:pubmed |
| pubmed-article:15130086 | pubmed:author | pubmed-author:Rendi?Dubravk... | lld:pubmed |
| pubmed-article:15130086 | pubmed:author | pubmed-author:MuchaJánJ | lld:pubmed |
| pubmed-article:15130086 | pubmed:author | pubmed-author:DomlatilJiríJ | lld:pubmed |
| pubmed-article:15130086 | pubmed:author | pubmed-author:HinterkörnerG... | lld:pubmed |
| pubmed-article:15130086 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:15130086 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:15130086 | pubmed:volume | 382 | lld:pubmed |
| pubmed-article:15130086 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15130086 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15130086 | pubmed:pagination | 67-74 | lld:pubmed |
| pubmed-article:15130086 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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