| pubmed-article:2333291 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2333291 | lifeskim:mentions | umls-concept:C0567416 | lld:lifeskim |
| pubmed-article:2333291 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
| pubmed-article:2333291 | lifeskim:mentions | umls-concept:C0036849 | lld:lifeskim |
| pubmed-article:2333291 | lifeskim:mentions | umls-concept:C1145667 | lld:lifeskim |
| pubmed-article:2333291 | lifeskim:mentions | umls-concept:C0062822 | lld:lifeskim |
| pubmed-article:2333291 | lifeskim:mentions | umls-concept:C0086414 | lld:lifeskim |
| pubmed-article:2333291 | pubmed:issue | 9 | lld:pubmed |
| pubmed-article:2333291 | pubmed:dateCreated | 1990-6-6 | lld:pubmed |
| pubmed-article:2333291 | pubmed:abstractText | T-cell recognition of peptides that are bound and presented by class I major histocompatibility complex molecules is highly specific. At present it is unclear what role class I peptide binding plays relative to T-cell receptor specificity in determination of immune recognition. A previous study from our group demonstrated that the HLA-A2.1 molecule could bind to 25% of the members of a panel of unrelated synthetic peptides as assessed by a functional peptide competition assay. To determine the peptide-binding specificity of another HLA class I molecule, we have examined the capacity of this panel of peptides to compete for the presentation of influenza virus nucleoprotein peptide NP-(335-350) by HLA-B37 to NP-peptide-specific HLA-B37-restricted cytotoxic T-lymphocyte lines. Forty-two percent of peptides tested were capable of inhibiting NP-(335-350) presentation by HLA-B37. Remarkably, none of these HLA-B37-binding peptides belong to the subset that was previously shown to bind to the HLA-A2.1 molecule. Only the NP-(335-350) peptide was capable of binding to both HLA-A2.1 and HLA-B37. These findings demonstrate that the peptide-binding specificities of HLA-B37 and HLA-A2.1 are largely nonoverlapping and suggest that, from the universe of peptides, individual HLA class I molecules can bind to clearly distinct subsets of these peptides. | lld:pubmed |
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| pubmed-article:2333291 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2333291 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2333291 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2333291 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2333291 | pubmed:month | May | lld:pubmed |
| pubmed-article:2333291 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:2333291 | pubmed:author | pubmed-author:ColiganJ EJE | lld:pubmed |
| pubmed-article:2333291 | pubmed:author | pubmed-author:AndersonR WRW | lld:pubmed |
| pubmed-article:2333291 | pubmed:author | pubmed-author:BiddisonW EWE | lld:pubmed |
| pubmed-article:2333291 | pubmed:author | pubmed-author:CarrenoB MBM | lld:pubmed |
| pubmed-article:2333291 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2333291 | pubmed:volume | 87 | lld:pubmed |
| pubmed-article:2333291 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2333291 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2333291 | pubmed:pagination | 3420-4 | lld:pubmed |
| pubmed-article:2333291 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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| pubmed-article:2333291 | pubmed:year | 1990 | lld:pubmed |
| pubmed-article:2333291 | pubmed:articleTitle | HLA-B37 and HLA-A2.1 molecules bind largely nonoverlapping sets of peptides. | lld:pubmed |
| pubmed-article:2333291 | pubmed:affiliation | Molecular Immunology Section, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892. | lld:pubmed |
| pubmed-article:2333291 | pubmed:publicationType | Journal Article | lld:pubmed |
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