pubmed-article:9256200 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:9256200 | lifeskim:mentions | umls-concept:C0039195 | lld:lifeskim |
pubmed-article:9256200 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
pubmed-article:9256200 | lifeskim:mentions | umls-concept:C0019627 | lld:lifeskim |
pubmed-article:9256200 | lifeskim:mentions | umls-concept:C0205234 | lld:lifeskim |
pubmed-article:9256200 | lifeskim:mentions | umls-concept:C0205369 | lld:lifeskim |
pubmed-article:9256200 | lifeskim:mentions | umls-concept:C0205164 | lld:lifeskim |
pubmed-article:9256200 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:9256200 | pubmed:dateCreated | 1997-9-4 | lld:pubmed |
pubmed-article:9256200 | pubmed:abstractText | Alloreactive T cells are often specific for individual peptides that are bound to allogeneic major histocompatibility complex (MHC) molecules. Other alloreactive T cells are reported to be peptide-independent or to recognize MHC conformational changes that are induced by multiple peptides. We tested 12 anti-HLA-B7 alloreactive cytotoxic T lymphocyte (CTL) clones that bind a restricted region of HLA-B7, including three CTL clones that were generated in a protocol designed to stimulate peptide-independent T cells. All 12 CTLs recognized multiple point mutations in the HLA-B7 peptide-binding groove. Eleven of the 12 CTLs recognized specific peptides that eluted in one or two fractions on high-performance liquid chromatography (HPLC). None of the CTLs promiscuously recognized 16 HLA-B7-binding synthetic peptides, although one CTL recognized minor by-products in one synthetic peptide preparation. CTL clone KID-9 cross-reacted with allogeneic HLA-B7 and HLA-B27 molecules and recognized a distinct peptide bound to each MHC molecule. CTL clone KD-11 recognized peptides that eluted in two HPLC fractions and recognized HLA-B7-transfected peptide antigen processing defective T2 cells. These results indicate that CTL allorecognition is peptide-specific whether the allogeneic MHC molecules are expressed on normal cells or antigen processing-deficient cells. | lld:pubmed |
pubmed-article:9256200 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9256200 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9256200 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9256200 | pubmed:language | eng | lld:pubmed |
pubmed-article:9256200 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9256200 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:9256200 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9256200 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9256200 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:9256200 | pubmed:month | Jul | lld:pubmed |
pubmed-article:9256200 | pubmed:issn | 0041-1337 | lld:pubmed |
pubmed-article:9256200 | pubmed:author | pubmed-author:LiY YYY | lld:pubmed |
pubmed-article:9256200 | pubmed:author | pubmed-author:MogaDD | lld:pubmed |
pubmed-article:9256200 | pubmed:author | pubmed-author:EngelhardV... | lld:pubmed |
pubmed-article:9256200 | pubmed:author | pubmed-author:SmithK DKD | lld:pubmed |
pubmed-article:9256200 | pubmed:author | pubmed-author:HuczkoEE | lld:pubmed |
pubmed-article:9256200 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:9256200 | pubmed:day | 27 | lld:pubmed |
pubmed-article:9256200 | pubmed:volume | 64 | lld:pubmed |
pubmed-article:9256200 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:9256200 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:9256200 | pubmed:pagination | 351-9 | lld:pubmed |
pubmed-article:9256200 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
pubmed-article:9256200 | pubmed:meshHeading | pubmed-meshheading:9256200-... | lld:pubmed |
pubmed-article:9256200 | pubmed:meshHeading | pubmed-meshheading:9256200-... | lld:pubmed |
pubmed-article:9256200 | pubmed:meshHeading | pubmed-meshheading:9256200-... | lld:pubmed |
pubmed-article:9256200 | pubmed:meshHeading | pubmed-meshheading:9256200-... | lld:pubmed |
pubmed-article:9256200 | pubmed:meshHeading | pubmed-meshheading:9256200-... | lld:pubmed |
pubmed-article:9256200 | pubmed:meshHeading | pubmed-meshheading:9256200-... | lld:pubmed |
pubmed-article:9256200 | pubmed:meshHeading | pubmed-meshheading:9256200-... | lld:pubmed |
pubmed-article:9256200 | pubmed:meshHeading | pubmed-meshheading:9256200-... | lld:pubmed |
pubmed-article:9256200 | pubmed:meshHeading | pubmed-meshheading:9256200-... | lld:pubmed |
pubmed-article:9256200 | pubmed:year | 1997 | lld:pubmed |
pubmed-article:9256200 | pubmed:articleTitle | Alloreactive cytotoxic T lymphocytes focus on specific major histocompatibility complex-bound peptides. | lld:pubmed |
pubmed-article:9256200 | pubmed:affiliation | Department of Pathology, the university of Iowa College of Medicine, Iowa City 52242, USA. | lld:pubmed |
pubmed-article:9256200 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:9256200 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:9256200 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9256200 | lld:pubmed |