| pubmed-article:9523118 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9523118 | lifeskim:mentions | umls-concept:C0017349 | lld:lifeskim |
| pubmed-article:9523118 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:9523118 | lifeskim:mentions | umls-concept:C0597304 | lld:lifeskim |
| pubmed-article:9523118 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:9523118 | pubmed:dateCreated | 1998-5-22 | lld:pubmed |
| pubmed-article:9523118 | pubmed:abstractText | Newly synthesized MHC class II alpha and beta chains associate with a protein chaperone, the invariant chain, which promotes the proper assembly of MHC class II complexes and their trafficking through cells and prevents their untimely loading with peptides. Efficient loading of MHC class II heterodimers with antigenic peptides requires concurrent proteolytic processing of both the invariant chain and endocytosed proteins. Recent studies have elucidated the critical roles of specific cysteine proteases, especially cathepsins S and L, in degrading the invariant chain and regulating the convergence of processed antigen and MHC class II dimers competent for peptide loading. | lld:pubmed |
| pubmed-article:9523118 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9523118 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9523118 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9523118 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9523118 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:9523118 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9523118 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:9523118 | pubmed:issn | 0952-7915 | lld:pubmed |
| pubmed-article:9523118 | pubmed:author | pubmed-author:ChapmanH AHA | lld:pubmed |
| pubmed-article:9523118 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9523118 | pubmed:volume | 10 | lld:pubmed |
| pubmed-article:9523118 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9523118 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9523118 | pubmed:pagination | 93-102 | lld:pubmed |
| pubmed-article:9523118 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:9523118 | pubmed:meshHeading | pubmed-meshheading:9523118-... | lld:pubmed |
| pubmed-article:9523118 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9523118 | pubmed:articleTitle | Endosomal proteolysis and MHC class II function. | lld:pubmed |
| pubmed-article:9523118 | pubmed:affiliation | Department of Medicine, Brigham and Women's Hospital, Boston, MA, USA. hchapman@rics.bwh.harvard.edu | lld:pubmed |
| pubmed-article:9523118 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9523118 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:9523118 | pubmed:publicationType | Review | lld:pubmed |
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