| pubmed-article:11741890 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11741890 | lifeskim:mentions | umls-concept:C0034861 | lld:lifeskim |
| pubmed-article:11741890 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
| pubmed-article:11741890 | lifeskim:mentions | umls-concept:C1171362 | lld:lifeskim |
| pubmed-article:11741890 | lifeskim:mentions | umls-concept:C0001057 | lld:lifeskim |
| pubmed-article:11741890 | lifeskim:mentions | umls-concept:C0021467 | lld:lifeskim |
| pubmed-article:11741890 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
| pubmed-article:11741890 | lifeskim:mentions | umls-concept:C1515670 | lld:lifeskim |
| pubmed-article:11741890 | lifeskim:mentions | umls-concept:C0021469 | lld:lifeskim |
| pubmed-article:11741890 | lifeskim:mentions | umls-concept:C0872366 | lld:lifeskim |
| pubmed-article:11741890 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:11741890 | pubmed:dateCreated | 2002-2-11 | lld:pubmed |
| pubmed-article:11741890 | pubmed:abstractText | We investigated the ability of a baculovirus-insect cell system to produce sialylated glycoproteins. Despite the presence of enzymes for synthesizing complex-type N-glycans, the most frequent structure of insect N-glycan is the paucimannosidic type, Man(3)GlcNAc(2)(+/-Fuc). The reason for the overwhelming assembly of paucimannosidic N-glycans is not yet well understood. We hypothesized that this predominance might be due to insect-specific, Golgi-associated beta-N-acetylglucosaminidase (GlcNAcase)-mediated removal of N-acetylglucosamine residues from the precursor N-glycan, thereby preventing its galactosylation and terminal sialylation. As we expected, the suppression of intrinsic GlcNAcase activity with a specific inhibitor, 2-acetamido-1,2-dideoxynojirimycin, allowed the accumulation of sialylated glycoproteins in the supernatants of insect cell cultures after baculoviral infection. Our observation indicates that GlcNAcase-dependent depletion of N-acetylglucosamine residues from intermediate N-glycans is critical for the assembly of paucimannosidic N-glycans in insect cells and, more importantly, that insect cells (under specific conditions) retain the ability to construct sialylated N-glycans like those in mammalian cells. | lld:pubmed |
| pubmed-article:11741890 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11741890 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11741890 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11741890 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11741890 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11741890 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11741890 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11741890 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11741890 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11741890 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11741890 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11741890 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11741890 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11741890 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:11741890 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:11741890 | pubmed:author | pubmed-author:WatanabeSatok... | lld:pubmed |
| pubmed-article:11741890 | pubmed:author | pubmed-author:KokuhoTakehir... | lld:pubmed |
| pubmed-article:11741890 | pubmed:author | pubmed-author:TakahashiHito... | lld:pubmed |
| pubmed-article:11741890 | pubmed:author | pubmed-author:TakahashiMasa... | lld:pubmed |
| pubmed-article:11741890 | pubmed:author | pubmed-author:KubotaTakayuk... | lld:pubmed |
| pubmed-article:11741890 | pubmed:author | pubmed-author:InumaruShigek... | lld:pubmed |
| pubmed-article:11741890 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11741890 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:11741890 | pubmed:volume | 277 | lld:pubmed |
| pubmed-article:11741890 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11741890 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11741890 | pubmed:pagination | 5090-3 | lld:pubmed |
| pubmed-article:11741890 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
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| pubmed-article:11741890 | pubmed:meshHeading | pubmed-meshheading:11741890... | lld:pubmed |
| pubmed-article:11741890 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:11741890 | pubmed:articleTitle | Sialylation of N-glycans on the recombinant proteins expressed by a baculovirus-insect cell system under beta-N-acetylglucosaminidase inhibition. | lld:pubmed |
| pubmed-article:11741890 | pubmed:affiliation | Department of Immunology, National Institute of Animal Health, 3-1-5 Kannondai, Tsukuba, Ibaraki 305-0856, Japan. satochan@affrc.go.jp | lld:pubmed |
| pubmed-article:11741890 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11741890 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11741890 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11741890 | lld:pubmed |
