| pubmed-article:9019402 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9019402 | lifeskim:mentions | umls-concept:C0108187 | lld:lifeskim |
| pubmed-article:9019402 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:9019402 | lifeskim:mentions | umls-concept:C0073234 | lld:lifeskim |
| pubmed-article:9019402 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:9019402 | pubmed:dateCreated | 1997-2-7 | lld:pubmed |
| pubmed-article:9019402 | pubmed:abstractText | Calnexin is a membrane protein of the endoplasmic reticulum that associates transiently with newly synthesized N-linked glycoproteins in vivo. Using defined components, the binding of ribonuclease B (RNase B) Man7-Man9 glycoforms to the luminal domain of calnexin was observed in vitro only if RNase B was monoglucosylated. Binding was independent of the conformation of the glycoprotein. Calnexin protected monoglucosylated RNase B from the action of glucosidase II and PNGase F but not from that of Endo H, which completely released the protein from calnexin. These observations directly demonstrate that calnexin can act exclusively as a lectin. | lld:pubmed |
| pubmed-article:9019402 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9019402 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9019402 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:9019402 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9019402 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:9019402 | pubmed:issn | 0092-8674 | lld:pubmed |
| pubmed-article:9019402 | pubmed:author | pubmed-author:DwekR ARA | lld:pubmed |
| pubmed-article:9019402 | pubmed:author | pubmed-author:ThomasD YDY | lld:pubmed |
| pubmed-article:9019402 | pubmed:author | pubmed-author:BergeronJ JJJ | lld:pubmed |
| pubmed-article:9019402 | pubmed:author | pubmed-author:RuddP MPM | lld:pubmed |
| pubmed-article:9019402 | pubmed:author | pubmed-author:ZapunAA | lld:pubmed |
| pubmed-article:9019402 | pubmed:author | pubmed-author:PetrescuS MSM | lld:pubmed |
| pubmed-article:9019402 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9019402 | pubmed:day | 10 | lld:pubmed |
| pubmed-article:9019402 | pubmed:volume | 88 | lld:pubmed |
| pubmed-article:9019402 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9019402 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9019402 | pubmed:pagination | 29-38 | lld:pubmed |
| pubmed-article:9019402 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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| pubmed-article:9019402 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9019402 | pubmed:articleTitle | Conformation-independent binding of monoglucosylated ribonuclease B to calnexin. | lld:pubmed |
| pubmed-article:9019402 | pubmed:affiliation | Department of Anatomy and Cell Biology, McGill University, Montreal, Quebec, Canada. | lld:pubmed |
| pubmed-article:9019402 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9019402 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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