| pubmed-article:3285344 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3285344 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
| pubmed-article:3285344 | lifeskim:mentions | umls-concept:C0002520 | lld:lifeskim |
| pubmed-article:3285344 | lifeskim:mentions | umls-concept:C0079866 | lld:lifeskim |
| pubmed-article:3285344 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:3285344 | lifeskim:mentions | umls-concept:C0522534 | lld:lifeskim |
| pubmed-article:3285344 | lifeskim:mentions | umls-concept:C2334430 | lld:lifeskim |
| pubmed-article:3285344 | lifeskim:mentions | umls-concept:C0205171 | lld:lifeskim |
| pubmed-article:3285344 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:3285344 | pubmed:dateCreated | 1988-6-22 | lld:pubmed |
| pubmed-article:3285344 | pubmed:abstractText | The interactive association between T lymphocytes and their target cells is an important system of cell-cell interactions. Major histocompatibility complex class I molecules are the cell surface structures recognized by cytolytic T lymphocytes. To define the molecular structures recognized by cytotoxic T lymphocytes, we have saturated the 270-base-pair alpha 1 exon of the H-2Dp gene with point mutations, rapidly producing a "library" of 2.5 x 10(3) independent mutants. The library contains enough recombinant clones (each clone encoding approximately one amino acid replacement mutation) to predict a mutation at each nucleotide position of the alpha 1 exon. The functional analysis of the first five transfected gene products tested has shown that mutation of a conserved tyrosine at position 27 to asparagine destroys recognition of the H-2Dp gene product by polyclonal alloreactive cytotoxic T lymphocytes. Recognition of the same mutant molecule by three monoclonal antibodies and H-2-restricted lymphocytic choriomenengitis virus-specific cytotoxic T lymphocytes is unaffected. | lld:pubmed |
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| pubmed-article:3285344 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3285344 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3285344 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:3285344 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3285344 | pubmed:month | May | lld:pubmed |
| pubmed-article:3285344 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:3285344 | pubmed:author | pubmed-author:FrelingerJ... | lld:pubmed |
| pubmed-article:3285344 | pubmed:author | pubmed-author:HutchisonC... | lld:pubmed |
| pubmed-article:3285344 | pubmed:author | pubmed-author:MurrayRR | lld:pubmed |
| pubmed-article:3285344 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3285344 | pubmed:volume | 85 | lld:pubmed |
| pubmed-article:3285344 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3285344 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3285344 | pubmed:pagination | 3535-9 | lld:pubmed |
| pubmed-article:3285344 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:3285344 | pubmed:year | 1988 | lld:pubmed |
| pubmed-article:3285344 | pubmed:articleTitle | Saturation mutagenesis of a major histocompatibility complex protein domain: identification of a single conserved amino acid important for allorecognition. | lld:pubmed |
| pubmed-article:3285344 | pubmed:affiliation | Department of Microbiology and Immunology, University of North Carolina, Chapel Hill 27599. | lld:pubmed |
| pubmed-article:3285344 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3285344 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:3285344 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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