| pubmed-article:9765412 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9765412 | lifeskim:mentions | umls-concept:C0035870 | lld:lifeskim |
| pubmed-article:9765412 | lifeskim:mentions | umls-concept:C0014372 | lld:lifeskim |
| pubmed-article:9765412 | lifeskim:mentions | umls-concept:C0108187 | lld:lifeskim |
| pubmed-article:9765412 | lifeskim:mentions | umls-concept:C0243041 | lld:lifeskim |
| pubmed-article:9765412 | lifeskim:mentions | umls-concept:C1533691 | lld:lifeskim |
| pubmed-article:9765412 | lifeskim:mentions | umls-concept:C1515655 | lld:lifeskim |
| pubmed-article:9765412 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:9765412 | pubmed:dateCreated | 1998-11-5 | lld:pubmed |
| pubmed-article:9765412 | pubmed:abstractText | Calnexin is an endoplasmic reticulum (ER)-associated molecular chaperone proposed to promote folding and assembly of glycoproteins that traverse the secretory pathway in eukaryotic cells. In this study we examined if calnexin interacts with the ER-associated luminal (VP7) and transmembrane (NSP4) proteins of rotavirus. Only glycosylated NSP4 interacted with calnexin and did so in a time-dependent manner (half-life, 20 min). In vitro translation experiments programmed with gene 10 of rhesus rotavirus confirmed that calnexin recognizes only glycosylated NSP4. Castanospermine (a glucosidase I and II inhibitor) experiments established that calnexin associates only with partly deglucosylated (di- or monoglucosylated) NSP4. Furthermore, enzymatic removal of the remaining glucose residues on the N-linked glycan units was essential to disengage the NSP4-calnexin complex. Novel experiments with castanospermine revealed that glucose trimming and the calnexin-NSP4 interaction were not critical for the assembly of infectious virus. | lld:pubmed |
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| pubmed-article:9765412 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9765412 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9765412 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:9765412 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9765412 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:9765412 | pubmed:issn | 0022-538X | lld:pubmed |
| pubmed-article:9765412 | pubmed:author | pubmed-author:NilssonMM | lld:pubmed |
| pubmed-article:9765412 | pubmed:author | pubmed-author:SvenssonLL | lld:pubmed |
| pubmed-article:9765412 | pubmed:author | pubmed-author:MirazimiAA | lld:pubmed |
| pubmed-article:9765412 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9765412 | pubmed:volume | 72 | lld:pubmed |
| pubmed-article:9765412 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9765412 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9765412 | pubmed:pagination | 8705-9 | lld:pubmed |
| pubmed-article:9765412 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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