| pubmed-article:8074803 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8074803 | lifeskim:mentions | umls-concept:C0935640 | lld:lifeskim |
| pubmed-article:8074803 | lifeskim:mentions | umls-concept:C0021311 | lld:lifeskim |
| pubmed-article:8074803 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
| pubmed-article:8074803 | lifeskim:mentions | umls-concept:C0242626 | lld:lifeskim |
| pubmed-article:8074803 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:8074803 | pubmed:dateCreated | 1994-10-4 | lld:pubmed |
| pubmed-article:8074803 | pubmed:abstractText | Spodoptera frugiperda cells are the standard host system for baculovirus-vector-mediated expression of recombinant glycoproteins. In an attempt to explore their ability to produce complex N-glycans containing terminal neuraminic acid, we tested both mock- and AcMNPV-infected SF9 cells. To elucidate the structures of the carbohydrate chains of cellular glycoproteins, radiolabeled oligosaccharides were liberated by treatment with endo-H and glycopeptidase F. When the endo-H resistant material was subjected to sequential degradation with exoglycosidases, only truncated carbohydrates with the structures Man3GlcNAc2 and Man3[Fuc]GlcNAc2 were found. There was no evidence for the presence of neuraminic acid and complex N-glycans. The results indicate that SF9 cells have only a limited capacity to process N-glycans. Infection with AcMNPV has no significant effect on glycosylation in these cells. | lld:pubmed |
| pubmed-article:8074803 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8074803 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8074803 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8074803 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8074803 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8074803 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8074803 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8074803 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8074803 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8074803 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8074803 | pubmed:month | May | lld:pubmed |
| pubmed-article:8074803 | pubmed:issn | 0177-3593 | lld:pubmed |
| pubmed-article:8074803 | pubmed:author | pubmed-author:KlingD HDH | lld:pubmed |
| pubmed-article:8074803 | pubmed:author | pubmed-author:GeyerRR | lld:pubmed |
| pubmed-article:8074803 | pubmed:author | pubmed-author:KretzchmarEE | lld:pubmed |
| pubmed-article:8074803 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8074803 | pubmed:volume | 375 | lld:pubmed |
| pubmed-article:8074803 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8074803 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8074803 | pubmed:pagination | 23-7 | lld:pubmed |
| pubmed-article:8074803 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:8074803 | pubmed:meshHeading | pubmed-meshheading:8074803-... | lld:pubmed |
| pubmed-article:8074803 | pubmed:meshHeading | pubmed-meshheading:8074803-... | lld:pubmed |
| pubmed-article:8074803 | pubmed:meshHeading | pubmed-meshheading:8074803-... | lld:pubmed |
| pubmed-article:8074803 | pubmed:meshHeading | pubmed-meshheading:8074803-... | lld:pubmed |
| pubmed-article:8074803 | pubmed:meshHeading | pubmed-meshheading:8074803-... | lld:pubmed |
| pubmed-article:8074803 | pubmed:meshHeading | pubmed-meshheading:8074803-... | lld:pubmed |
| pubmed-article:8074803 | pubmed:meshHeading | pubmed-meshheading:8074803-... | lld:pubmed |
| pubmed-article:8074803 | pubmed:meshHeading | pubmed-meshheading:8074803-... | lld:pubmed |
| pubmed-article:8074803 | pubmed:meshHeading | pubmed-meshheading:8074803-... | lld:pubmed |
| pubmed-article:8074803 | pubmed:meshHeading | pubmed-meshheading:8074803-... | lld:pubmed |
| pubmed-article:8074803 | pubmed:meshHeading | pubmed-meshheading:8074803-... | lld:pubmed |
| pubmed-article:8074803 | pubmed:meshHeading | pubmed-meshheading:8074803-... | lld:pubmed |
| pubmed-article:8074803 | pubmed:meshHeading | pubmed-meshheading:8074803-... | lld:pubmed |
| pubmed-article:8074803 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:8074803 | pubmed:articleTitle | Baculovirus infection does not alter N-glycosylation in Spodoptera frugiperda cells. | lld:pubmed |
| pubmed-article:8074803 | pubmed:affiliation | Institut für Virologie, Philipps-Universität, Marburg, Germany. | lld:pubmed |
| pubmed-article:8074803 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8074803 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8074803 | lld:pubmed |
