pubmed-article:16091366 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:16091366 | lifeskim:mentions | umls-concept:C0034830 | lld:lifeskim |
pubmed-article:16091366 | lifeskim:mentions | umls-concept:C0108187 | lld:lifeskim |
pubmed-article:16091366 | lifeskim:mentions | umls-concept:C0017982 | lld:lifeskim |
pubmed-article:16091366 | lifeskim:mentions | umls-concept:C0004083 | lld:lifeskim |
pubmed-article:16091366 | lifeskim:mentions | umls-concept:C1879748 | lld:lifeskim |
pubmed-article:16091366 | lifeskim:mentions | umls-concept:C1706853 | lld:lifeskim |
pubmed-article:16091366 | lifeskim:mentions | umls-concept:C1546857 | lld:lifeskim |
pubmed-article:16091366 | lifeskim:mentions | umls-concept:C1556066 | lld:lifeskim |
pubmed-article:16091366 | lifeskim:mentions | umls-concept:C1619636 | lld:lifeskim |
pubmed-article:16091366 | lifeskim:mentions | umls-concept:C1711351 | lld:lifeskim |
pubmed-article:16091366 | lifeskim:mentions | umls-concept:C1514873 | lld:lifeskim |
pubmed-article:16091366 | pubmed:issue | 40 | lld:pubmed |
pubmed-article:16091366 | pubmed:dateCreated | 2005-10-3 | lld:pubmed |
pubmed-article:16091366 | pubmed:abstractText | We investigated how asparagine (N)-linked glycosylation affects assembly of acetylcholine receptors (AChRs) in the endoplasmic reticulum (ER). Block of N-linked glycosylation inhibited AChR assembly whereas block of glucose trimming partially blocked assembly at the late stages. Removal of each of seven glycans had a distinct effect on AChR assembly, ranging from no effect to total loss of assembly. Because the chaperone calnexin (CN) associates with N-linked glycans, we examined CN interactions with AChR subunits. CN rapidly associates with 50% or more of newly synthesized AChR subunits, but not with subunits after maturation. Block of N-linked glycosylation or trimming did not alter CN-AChR subunit associations nor did subunit mutations prevent N-linked glycosylation. Additionally, CN associations with subunits lacking N-linked glycans occurred without subunit aggregation or misfolding. Our data indicate that CN associates with AChR subunits without N-linked glycan interactions. Furthermore, CN-subunit associations only occur early in AChR assembly and have no role in events later that require N-linked glycosylation. | lld:pubmed |
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pubmed-article:16091366 | pubmed:language | eng | lld:pubmed |
pubmed-article:16091366 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16091366 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:16091366 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:16091366 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:16091366 | pubmed:month | Oct | lld:pubmed |
pubmed-article:16091366 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:16091366 | pubmed:author | pubmed-author:GreenWilliam... | lld:pubmed |
pubmed-article:16091366 | pubmed:author | pubmed-author:WanamakerChri... | lld:pubmed |
pubmed-article:16091366 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:16091366 | pubmed:day | 7 | lld:pubmed |
pubmed-article:16091366 | pubmed:volume | 280 | lld:pubmed |
pubmed-article:16091366 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:16091366 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:16091366 | pubmed:pagination | 33800-10 | lld:pubmed |
pubmed-article:16091366 | pubmed:dateRevised | 2011-6-14 | lld:pubmed |
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pubmed-article:16091366 | pubmed:meshHeading | pubmed-meshheading:16091366... | lld:pubmed |
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