| pubmed-article:1717839 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1717839 | lifeskim:mentions | umls-concept:C0008109 | lld:lifeskim |
| pubmed-article:1717839 | lifeskim:mentions | umls-concept:C0034721 | lld:lifeskim |
| pubmed-article:1717839 | lifeskim:mentions | umls-concept:C0034693 | lld:lifeskim |
| pubmed-article:1717839 | lifeskim:mentions | umls-concept:C0205145 | lld:lifeskim |
| pubmed-article:1717839 | lifeskim:mentions | umls-concept:C0020846 | lld:lifeskim |
| pubmed-article:1717839 | lifeskim:mentions | umls-concept:C0162825 | lld:lifeskim |
| pubmed-article:1717839 | lifeskim:mentions | umls-concept:C0162826 | lld:lifeskim |
| pubmed-article:1717839 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:1717839 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:1717839 | pubmed:dateCreated | 1991-11-13 | lld:pubmed |
| pubmed-article:1717839 | pubmed:abstractText | Three rat monoclonal antibodies specific for mouse IgE (C12B9, 23G3, and B1E3) were established by using monoclonal anti-DNP mouse IgE (mIgE) as immunogen. These antibodies, as well as a fourth, (R1E4) were characterized. It was found that one antibody (C12B9) recognizes an allotypic determinant (Igh-7a) found on the C epsilon chain of mIgE. Antibody cross-blocking studies and epitope mapping studies using recombinant mIgE indicated that 3 antibodies (C12B9, R1E4 and 23G3) were directed against the C epsilon 3 domain while one (B1E3) was directed against the C epsilon 4 domain. A highly specific sandwich RIA for mIgE was developed using these antibodies. Use of these monoclonal anti-mIgE antibodies in conjunction with recombinant chimeric mIgE-human IgG1 molecules, demonstrated that the C epsilon 3 domain is important in the binding of mIgE to the murine B cell Fc epsilon RII as well as to the murine mast cell F epsilon RI. The presence of the C epsilon 4 domain influenced the binding of the recombinant IgE to the Fc epsilon RII; in contrast to the C epsilon 4 domain had no effect on binding to the Fc epsilon RI. | lld:pubmed |
| pubmed-article:1717839 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1717839 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1717839 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1717839 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1717839 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1717839 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1717839 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1717839 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1717839 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1717839 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1717839 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1717839 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1717839 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1717839 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1717839 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1717839 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:1717839 | pubmed:issn | 0161-5890 | lld:pubmed |
| pubmed-article:1717839 | pubmed:author | pubmed-author:ConradD HDH | lld:pubmed |
| pubmed-article:1717839 | pubmed:author | pubmed-author:BairdBB | lld:pubmed |
| pubmed-article:1717839 | pubmed:author | pubmed-author:KeeganA DAD | lld:pubmed |
| pubmed-article:1717839 | pubmed:author | pubmed-author:ShopesBB | lld:pubmed |
| pubmed-article:1717839 | pubmed:author | pubmed-author:FratazziCC | lld:pubmed |
| pubmed-article:1717839 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1717839 | pubmed:volume | 28 | lld:pubmed |
| pubmed-article:1717839 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1717839 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1717839 | pubmed:pagination | 1149-54 | lld:pubmed |
| pubmed-article:1717839 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:1717839 | pubmed:meshHeading | pubmed-meshheading:1717839-... | lld:pubmed |
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| pubmed-article:1717839 | pubmed:meshHeading | pubmed-meshheading:1717839-... | lld:pubmed |
| pubmed-article:1717839 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:1717839 | pubmed:articleTitle | Characterization of new rat anti-mouse IgE monoclonals and their use along with chimeric IgE to further define the site that interacts with Fc epsilon RII and Fc epsilon RI. | lld:pubmed |
| pubmed-article:1717839 | pubmed:affiliation | Department of Medicine, Johns Hopkins University School of Medicine, Baltimore, MD 21239. | lld:pubmed |
| pubmed-article:1717839 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1717839 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:1717839 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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