| pubmed-article:11857340 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11857340 | lifeskim:mentions | umls-concept:C0439849 | lld:lifeskim |
| pubmed-article:11857340 | lifeskim:mentions | umls-concept:C0019774 | lld:lifeskim |
| pubmed-article:11857340 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
| pubmed-article:11857340 | lifeskim:mentions | umls-concept:C1704241 | lld:lifeskim |
| pubmed-article:11857340 | lifeskim:mentions | umls-concept:C0205360 | lld:lifeskim |
| pubmed-article:11857340 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:11857340 | pubmed:dateCreated | 2002-3-7 | lld:pubmed |
| pubmed-article:11857340 | pubmed:abstractText | Immunodominant T cell epitopes from the autoantigen human cartilage glycoprotein 39 have previously been mapped in the context of HLA-DR*0401 and *0402, using mice expressing HLA-DR4 transgenes. We measured the dissociation rates of these epitopes from soluble recombinant DR*0401 and DR*0402 to assess the relationship between peptide/HLA-DR4 kinetic stability and immunogenicity. Experiments were performed at endosomal pH (5.5) and at cell surface pH (7), in the absence and presence of soluble recombinant HLA-DM (sDM). All (4/4) immunodominant peptide/HLA-DR complexes exhibit dissociation half-times of 1h to several days. In contrast, most (3/4) non-immunodominant complexes dissociate with half-times <30 min under at least one of these conditions. Interestingly, a complex which is stable except in the presence of HLA-DM at pH 5.5 is immunogenic only following peptide immunization, while a complex which is stable at acidic but not at neutral pH, is non-immunogenic following either whole protein or peptide immunization. These data indicate that kinetic stability of peptide/MHC complexes in vivo is a key determinant of immunogenicity. | lld:pubmed |
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| pubmed-article:11857340 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:11857340 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11857340 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11857340 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11857340 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11857340 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11857340 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11857340 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11857340 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11857340 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11857340 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11857340 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11857340 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11857340 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11857340 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:11857340 | pubmed:issn | 0014-2980 | lld:pubmed |
| pubmed-article:11857340 | pubmed:author | pubmed-author:HallFrances... | lld:pubmed |
| pubmed-article:11857340 | pubmed:author | pubmed-author:RabinowitzJos... | lld:pubmed |
| pubmed-article:11857340 | pubmed:author | pubmed-author:BuschRobertR | lld:pubmed |
| pubmed-article:11857340 | pubmed:author | pubmed-author:ViscontiKevin... | lld:pubmed |
| pubmed-article:11857340 | pubmed:author | pubmed-author:BelmaresMicha... | lld:pubmed |
| pubmed-article:11857340 | pubmed:author | pubmed-author:PatilNamrata... | lld:pubmed |
| pubmed-article:11857340 | pubmed:author | pubmed-author:CopeAndrew... | lld:pubmed |
| pubmed-article:11857340 | pubmed:author | pubmed-author:PatelSalilS | lld:pubmed |
| pubmed-article:11857340 | pubmed:author | pubmed-author:McConnellHard... | lld:pubmed |
| pubmed-article:11857340 | pubmed:author | pubmed-author:MellinsElizab... | lld:pubmed |
| pubmed-article:11857340 | pubmed:author | pubmed-author:SonderstrupGr... | lld:pubmed |
| pubmed-article:11857340 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11857340 | pubmed:volume | 32 | lld:pubmed |
| pubmed-article:11857340 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11857340 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11857340 | pubmed:pagination | 662-70 | lld:pubmed |
| pubmed-article:11857340 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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| pubmed-article:11857340 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:11857340 | pubmed:articleTitle | Relationship between kinetic stability and immunogenicity of HLA-DR4/peptide complexes. | lld:pubmed |
| pubmed-article:11857340 | pubmed:affiliation | Department of Microbiology and Immunology, Stanford University, Stanford, CA 94305, USA. | lld:pubmed |
| pubmed-article:11857340 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11857340 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:11857340 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:11857340 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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