| pubmed-article:2265605 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2265605 | lifeskim:mentions | umls-concept:C0337611 | lld:lifeskim |
| pubmed-article:2265605 | lifeskim:mentions | umls-concept:C0003320 | lld:lifeskim |
| pubmed-article:2265605 | lifeskim:mentions | umls-concept:C0019630 | lld:lifeskim |
| pubmed-article:2265605 | lifeskim:mentions | umls-concept:C1709915 | lld:lifeskim |
| pubmed-article:2265605 | pubmed:issue | 13 | lld:pubmed |
| pubmed-article:2265605 | pubmed:dateCreated | 1991-2-14 | lld:pubmed |
| pubmed-article:2265605 | pubmed:abstractText | This report describes a detailed mutational analysis of a major histocompatibility complex class II molecule--the alpha chain of the Ak complex. Each residue from 50-79 was replaced by an alanine, and the effects on recognition of Ak by panels of antibodies and T cells determined. The results provide the strongest existing experimental evidence that the antigen binding site on a class II molecule can be modelled on the crystal structure of a class I molecule. The data have also permitted the delineation of residues that actually contact antigenic peptides. | lld:pubmed |
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| pubmed-article:2265605 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:2265605 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2265605 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2265605 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:2265605 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:2265605 | pubmed:author | pubmed-author:AllenPP | lld:pubmed |
| pubmed-article:2265605 | pubmed:author | pubmed-author:BenoistCC | lld:pubmed |
| pubmed-article:2265605 | pubmed:author | pubmed-author:MathisDD | lld:pubmed |
| pubmed-article:2265605 | pubmed:author | pubmed-author:DellabonaPP | lld:pubmed |
| pubmed-article:2265605 | pubmed:author | pubmed-author:PeccoudJJ | lld:pubmed |
| pubmed-article:2265605 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2265605 | pubmed:volume | 9 | lld:pubmed |
| pubmed-article:2265605 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2265605 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2265605 | pubmed:pagination | 4215-23 | lld:pubmed |
| pubmed-article:2265605 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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