| pubmed-article:7606781 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7606781 | lifeskim:mentions | umls-concept:C0330390 | lld:lifeskim |
| pubmed-article:7606781 | lifeskim:mentions | umls-concept:C0017349 | lld:lifeskim |
| pubmed-article:7606781 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
| pubmed-article:7606781 | lifeskim:mentions | umls-concept:C0086168 | lld:lifeskim |
| pubmed-article:7606781 | lifeskim:mentions | umls-concept:C2003941 | lld:lifeskim |
| pubmed-article:7606781 | lifeskim:mentions | umls-concept:C0175722 | lld:lifeskim |
| pubmed-article:7606781 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
| pubmed-article:7606781 | lifeskim:mentions | umls-concept:C1561603 | lld:lifeskim |
| pubmed-article:7606781 | lifeskim:mentions | umls-concept:C1708715 | lld:lifeskim |
| pubmed-article:7606781 | lifeskim:mentions | umls-concept:C2346689 | lld:lifeskim |
| pubmed-article:7606781 | lifeskim:mentions | umls-concept:C0596448 | lld:lifeskim |
| pubmed-article:7606781 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:7606781 | pubmed:dateCreated | 1995-8-17 | lld:pubmed |
| pubmed-article:7606781 | pubmed:abstractText | Human leukocyte antigen DM (HLA-DM) molecules are structurally related to classical MHC class II molecules and reside in the lysosome-like compartment where class II-restricted antigen processing is thought to occur. Mutant cell lines lacking HLA-DM are defective in antigen processing and accumulate class II molecules associated with a nested set of invariant chain-derived peptides (class II-associated invariant chain peptides, CLIP). Here we show that HLA-DM catalyzes the dissociation of CLIP from MHC class II-CLIP complexes in vitro and facilitates the binding of antigenic peptides. The reaction has an acidic pH optimum, consistent with its occurrence in a lysosome-like compartment in vivo. Antibody blocking experiments suggest that a transient interaction between HLA-DM and the MHC class II-CLIP complex is required. | lld:pubmed |
| pubmed-article:7606781 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7606781 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7606781 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7606781 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7606781 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:7606781 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:7606781 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7606781 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7606781 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:7606781 | pubmed:issn | 0092-8674 | lld:pubmed |
| pubmed-article:7606781 | pubmed:author | pubmed-author:CresswellPP | lld:pubmed |
| pubmed-article:7606781 | pubmed:author | pubmed-author:DenzinL KLK | lld:pubmed |
| pubmed-article:7606781 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7606781 | pubmed:day | 14 | lld:pubmed |
| pubmed-article:7606781 | pubmed:volume | 82 | lld:pubmed |
| pubmed-article:7606781 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7606781 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7606781 | pubmed:pagination | 155-65 | lld:pubmed |
| pubmed-article:7606781 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
| pubmed-article:7606781 | pubmed:meshHeading | pubmed-meshheading:7606781-... | lld:pubmed |
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| pubmed-article:7606781 | pubmed:meshHeading | pubmed-meshheading:7606781-... | lld:pubmed |
| pubmed-article:7606781 | pubmed:meshHeading | pubmed-meshheading:7606781-... | lld:pubmed |
| pubmed-article:7606781 | pubmed:meshHeading | pubmed-meshheading:7606781-... | lld:pubmed |
| pubmed-article:7606781 | pubmed:meshHeading | pubmed-meshheading:7606781-... | lld:pubmed |
| pubmed-article:7606781 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7606781 | pubmed:articleTitle | HLA-DM induces CLIP dissociation from MHC class II alpha beta dimers and facilitates peptide loading. | lld:pubmed |
| pubmed-article:7606781 | pubmed:affiliation | Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, Connecticut 06510-8011, USA. | lld:pubmed |
| pubmed-article:7606781 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7606781 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:7606781 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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