| pubmed-article:9191070 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9191070 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
| pubmed-article:9191070 | lifeskim:mentions | umls-concept:C1707455 | lld:lifeskim |
| pubmed-article:9191070 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:9191070 | lifeskim:mentions | umls-concept:C2348205 | lld:lifeskim |
| pubmed-article:9191070 | lifeskim:mentions | umls-concept:C0059385 | lld:lifeskim |
| pubmed-article:9191070 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:9191070 | pubmed:dateCreated | 1997-7-14 | lld:pubmed |
| pubmed-article:9191070 | pubmed:abstractText | Staphylococcal enterotoxins and toxic shock syndrome toxin-1 are known as superantigens due to their ability to activate a large number of T-cells by crosslinking the major histocompatibility complex class II molecules with the T-cell receptor. Although superantigens seem to act by a common mechanism, they vary in many of their specific interactions and biological properties. A structural comparison of staphylococcal enterotoxins A and C2, members of the staphylococcal superantigens, has shown large conformational differences at the putative TcR interaction site (loops between alphaN-alpha2, alpha4-beta9 and beta10-alpha5 in staphylococcal enterotoxin A) that could explain the variability in their T-cell receptor specificity. A common Zn2(+)-binding site was identified in both staphylococcal enterotoxin A and C2 that is superimposable but differs somewhat in its coordination geometry between the two molecules. | lld:pubmed |
| pubmed-article:9191070 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9191070 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9191070 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9191070 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9191070 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9191070 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9191070 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9191070 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9191070 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9191070 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9191070 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9191070 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9191070 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:9191070 | pubmed:issn | 0022-2836 | lld:pubmed |
| pubmed-article:9191070 | pubmed:author | pubmed-author:SvenssonL ALA | lld:pubmed |
| pubmed-article:9191070 | pubmed:author | pubmed-author:AcharyaK RKR | lld:pubmed |
| pubmed-article:9191070 | pubmed:author | pubmed-author:PapageorgiouA... | lld:pubmed |
| pubmed-article:9191070 | pubmed:author | pubmed-author:SchadE MEM | lld:pubmed |
| pubmed-article:9191070 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9191070 | pubmed:day | 6 | lld:pubmed |
| pubmed-article:9191070 | pubmed:volume | 269 | lld:pubmed |
| pubmed-article:9191070 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9191070 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9191070 | pubmed:pagination | 270-80 | lld:pubmed |
| pubmed-article:9191070 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:9191070 | pubmed:meshHeading | pubmed-meshheading:9191070-... | lld:pubmed |
| pubmed-article:9191070 | pubmed:meshHeading | pubmed-meshheading:9191070-... | lld:pubmed |
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| pubmed-article:9191070 | pubmed:meshHeading | pubmed-meshheading:9191070-... | lld:pubmed |
| pubmed-article:9191070 | pubmed:meshHeading | pubmed-meshheading:9191070-... | lld:pubmed |
| pubmed-article:9191070 | pubmed:meshHeading | pubmed-meshheading:9191070-... | lld:pubmed |
| pubmed-article:9191070 | pubmed:meshHeading | pubmed-meshheading:9191070-... | lld:pubmed |
| pubmed-article:9191070 | pubmed:meshHeading | pubmed-meshheading:9191070-... | lld:pubmed |
| pubmed-article:9191070 | pubmed:meshHeading | pubmed-meshheading:9191070-... | lld:pubmed |
| pubmed-article:9191070 | pubmed:meshHeading | pubmed-meshheading:9191070-... | lld:pubmed |
| pubmed-article:9191070 | pubmed:meshHeading | pubmed-meshheading:9191070-... | lld:pubmed |
| pubmed-article:9191070 | pubmed:meshHeading | pubmed-meshheading:9191070-... | lld:pubmed |
| pubmed-article:9191070 | pubmed:meshHeading | pubmed-meshheading:9191070-... | lld:pubmed |
| pubmed-article:9191070 | pubmed:meshHeading | pubmed-meshheading:9191070-... | lld:pubmed |
| pubmed-article:9191070 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9191070 | pubmed:articleTitle | A structural and functional comparison of staphylococcal enterotoxins A and C2 reveals remarkable similarity and dissimilarity. | lld:pubmed |
| pubmed-article:9191070 | pubmed:affiliation | Department of Molecular Biophysics, Center for Chemistry and Chemical Engineering, Lund University, Sweden. | lld:pubmed |
| pubmed-article:9191070 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9191070 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:9191070 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9191070 | lld:pubmed |
