| pubmed-article:9345295 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9345295 | lifeskim:mentions | umls-concept:C0002092 | lld:lifeskim |
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| pubmed-article:9345295 | lifeskim:mentions | umls-concept:C0003316 | lld:lifeskim |
| pubmed-article:9345295 | lifeskim:mentions | umls-concept:C1521991 | lld:lifeskim |
| pubmed-article:9345295 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
| pubmed-article:9345295 | lifeskim:mentions | umls-concept:C1824952 | lld:lifeskim |
| pubmed-article:9345295 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
| pubmed-article:9345295 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:9345295 | lifeskim:mentions | umls-concept:C2911684 | lld:lifeskim |
| pubmed-article:9345295 | lifeskim:mentions | umls-concept:C0185117 | lld:lifeskim |
| pubmed-article:9345295 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:9345295 | pubmed:dateCreated | 1997-11-24 | lld:pubmed |
| pubmed-article:9345295 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9345295 | pubmed:abstractText | Birch pollen belongs to the most potent elicitors of Type I allergic reactions in early spring. Using serum IgE from a birch pollen allergic patient, two cDNA clones (clone 6 and clone 13) were isolated from a birch pollen expression cDNA library constructed in phage lambda gt11. Clone 6 encoded a 9.3 kD two EF-hand calcium-binding protein, designated Bet v 4, with significant end to end sequence homology to EF-hand calcium-binding allergens from weed and grass pollen. Recombinant Bet v 4, expressed as beta-galactosidase fusion protein, reacted with serum IgE from approximately 20% of pollen allergic individuals. Depletion of allergenbound calcium by EGTA treatment lead to a substantial reduction of IgE-binding to Bet v 4, indicating that protein-bound calcium is necessary for the maintenance of IgE-epitopes. The greatly reduced IgE-binding capacity of clone 13, a Bet v 4 fragment that lacked the 16 N-terminal amino acids, indicated that the N-terminus contributes significantly to the proteins IgE-binding capacity. By IgE-inhibition experiments it was demonstrated that recombinant Bet v 4 shared IgE-epitopes with natural Bet v 4 and a homologous timothy grass pollen allergen. Recombinant Bet v 4 may therefore be considered as a relevant crossreactive plant allergen, which may be used for diagnosis and treatment of patients suffering from multivalent plant allergies. | lld:pubmed |
| pubmed-article:9345295 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9345295 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9345295 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:9345295 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9345295 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:9345295 | pubmed:issn | 0006-291X | lld:pubmed |
| pubmed-article:9345295 | pubmed:author | pubmed-author:KraftDD | lld:pubmed |
| pubmed-article:9345295 | pubmed:author | pubmed-author:HayesJJ | lld:pubmed |
| pubmed-article:9345295 | pubmed:author | pubmed-author:ElfmanLL | lld:pubmed |
| pubmed-article:9345295 | pubmed:author | pubmed-author:ValentaRR | lld:pubmed |
| pubmed-article:9345295 | pubmed:author | pubmed-author:SeiberlerSS | lld:pubmed |
| pubmed-article:9345295 | pubmed:author | pubmed-author:VangelistaLL | lld:pubmed |
| pubmed-article:9345295 | pubmed:author | pubmed-author:GrönlundHH | lld:pubmed |
| pubmed-article:9345295 | pubmed:author | pubmed-author:TwardoszAA | lld:pubmed |
| pubmed-article:9345295 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9345295 | pubmed:day | 9 | lld:pubmed |
| pubmed-article:9345295 | pubmed:volume | 239 | lld:pubmed |
| pubmed-article:9345295 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9345295 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9345295 | pubmed:pagination | 197-204 | lld:pubmed |
| pubmed-article:9345295 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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| pubmed-article:9345295 | pubmed:meshHeading | pubmed-meshheading:9345295-... | lld:pubmed |
| pubmed-article:9345295 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9345295 | pubmed:articleTitle | Molecular characterization, expression in Escherichia coli, and epitope analysis of a two EF-hand calcium-binding birch pollen allergen, Bet v 4. | lld:pubmed |
| pubmed-article:9345295 | pubmed:affiliation | Institute of General and Experimental Pathology, AKH, University of Vienna, Austria. | lld:pubmed |
| pubmed-article:9345295 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9345295 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:9345295 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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