| pubmed-article:2014234 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2014234 | lifeskim:mentions | umls-concept:C0019764 | lld:lifeskim |
| pubmed-article:2014234 | lifeskim:mentions | umls-concept:C0567416 | lld:lifeskim |
| pubmed-article:2014234 | lifeskim:mentions | umls-concept:C0178719 | lld:lifeskim |
| pubmed-article:2014234 | lifeskim:mentions | umls-concept:C0005456 | lld:lifeskim |
| pubmed-article:2014234 | lifeskim:mentions | umls-concept:C0597304 | lld:lifeskim |
| pubmed-article:2014234 | lifeskim:mentions | umls-concept:C0063356 | lld:lifeskim |
| pubmed-article:2014234 | lifeskim:mentions | umls-concept:C1149098 | lld:lifeskim |
| pubmed-article:2014234 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:2014234 | pubmed:dateCreated | 1991-5-15 | lld:pubmed |
| pubmed-article:2014234 | pubmed:abstractText | HLA-DR molecules are heterodimeric transmembrane glycoproteins that associate intracellularly with a polypeptide known as the invariant (I) chain. Shortly before expression of the HLA-DR alpha beta dimer on the cell surface, however, the I chain is removed from the intracellular alpha beta I complex by a mechanism thought to involve proteolysis. In this report, we show that treatment of purified alpha beta I with the cysteine proteinase cathepsin B results in the specific proteolysis of the HLA-DR-associated I chain in vitro. As a consequence of this, the I chain is removed and free alpha beta dimers are released from alpha beta I. Although alpha beta I fails to bind an immunogenic peptide, the released alpha beta dimers acquire the ability to bind the peptide after proteolysis of the I chain. These results suggest that the I chain inhibits immunogenic peptide binding to alpha beta I early during intracellular transport and demonstrate that proteolysis is likely to be the in vivo mechanism of I chain removal. | lld:pubmed |
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| pubmed-article:2014234 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2014234 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2014234 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2014234 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2014234 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:2014234 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:2014234 | pubmed:author | pubmed-author:CresswellPP | lld:pubmed |
| pubmed-article:2014234 | pubmed:author | pubmed-author:RocheP APA | lld:pubmed |
| pubmed-article:2014234 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2014234 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:2014234 | pubmed:volume | 88 | lld:pubmed |
| pubmed-article:2014234 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2014234 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2014234 | pubmed:pagination | 3150-4 | lld:pubmed |
| pubmed-article:2014234 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:2014234 | pubmed:meshHeading | pubmed-meshheading:2014234-... | lld:pubmed |
| pubmed-article:2014234 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:2014234 | pubmed:articleTitle | Proteolysis of the class II-associated invariant chain generates a peptide binding site in intracellular HLA-DR molecules. | lld:pubmed |
| pubmed-article:2014234 | pubmed:affiliation | Department of Microbiology and Immunology, Duke University Medical Center, Durham, NC 27710. | lld:pubmed |
| pubmed-article:2014234 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2014234 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:2014234 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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