| pubmed-article:8313912 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8313912 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:8313912 | lifeskim:mentions | umls-concept:C0017349 | lld:lifeskim |
| pubmed-article:8313912 | lifeskim:mentions | umls-concept:C0567416 | lld:lifeskim |
| pubmed-article:8313912 | lifeskim:mentions | umls-concept:C0108187 | lld:lifeskim |
| pubmed-article:8313912 | lifeskim:mentions | umls-concept:C1413107 | lld:lifeskim |
| pubmed-article:8313912 | lifeskim:mentions | umls-concept:C1879748 | lld:lifeskim |
| pubmed-article:8313912 | lifeskim:mentions | umls-concept:C1706853 | lld:lifeskim |
| pubmed-article:8313912 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:8313912 | pubmed:dateCreated | 1994-3-21 | lld:pubmed |
| pubmed-article:8313912 | pubmed:abstractText | Major histocompatibility complex (MHC) class II antigens consist of alpha and beta chains that associate intracellularly with the invariant (I) chain. The HLA-DR alpha beta I complex assembles in the endoplasmic reticulum (ER) into a nonameric structure via progressive addition of three alpha beta dimers to a core invariant chain trimer. We have examined intracellular association of alpha beta I complexes with the resident ER protein calnexin. Calnexin associates rapidly (within 3 min) with newly synthesized alpha, beta and I chains, and remains associated with the assembling alpha beta I complex until the final alpha beta dimer is added, forming the complete nonamer. Dissociation of calnexin parallels egress of alpha beta I from the ER. These results suggest that calnexin retains and stabilizes both free class II subunits and partially assembled class II-I chain complexes until assembly of the nonamer is complete. | lld:pubmed |
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| pubmed-article:8313912 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8313912 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8313912 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8313912 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8313912 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:8313912 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:8313912 | pubmed:author | pubmed-author:CresswellPP | lld:pubmed |
| pubmed-article:8313912 | pubmed:author | pubmed-author:AndersonK SKS | lld:pubmed |
| pubmed-article:8313912 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8313912 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:8313912 | pubmed:volume | 13 | lld:pubmed |
| pubmed-article:8313912 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8313912 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8313912 | pubmed:pagination | 675-82 | lld:pubmed |
| pubmed-article:8313912 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:8313912 | pubmed:meshHeading | pubmed-meshheading:8313912-... | lld:pubmed |
| pubmed-article:8313912 | pubmed:meshHeading | pubmed-meshheading:8313912-... | lld:pubmed |
| pubmed-article:8313912 | pubmed:meshHeading | pubmed-meshheading:8313912-... | lld:pubmed |
| pubmed-article:8313912 | pubmed:meshHeading | pubmed-meshheading:8313912-... | lld:pubmed |
| pubmed-article:8313912 | pubmed:meshHeading | pubmed-meshheading:8313912-... | lld:pubmed |
| pubmed-article:8313912 | pubmed:meshHeading | pubmed-meshheading:8313912-... | lld:pubmed |
| pubmed-article:8313912 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:8313912 | pubmed:articleTitle | A role for calnexin (IP90) in the assembly of class II MHC molecules. | lld:pubmed |
| pubmed-article:8313912 | pubmed:affiliation | Section of Immunobiology, Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, CT 06510. | lld:pubmed |
| pubmed-article:8313912 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8313912 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:8313912 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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