rdf:type |
|
lifeskim:mentions |
umls-concept:C0001128,
umls-concept:C0002092,
umls-concept:C0003316,
umls-concept:C0020846,
umls-concept:C0037733,
umls-concept:C0061617,
umls-concept:C0062990,
umls-concept:C0237876,
umls-concept:C0325983,
umls-concept:C0337112,
umls-concept:C0949399,
umls-concept:C1262902,
umls-concept:C1524075
|
pubmed:issue |
4
|
pubmed:dateCreated |
2001-1-26
|
pubmed:abstractText |
The identification of IgE epitopes for proteins is the first step in understanding the interaction of allergens with the immune system. Proteins from the legume family have shown in vitro cross-reactivity in IgE-binding assays, but this cross-reactivity is rarely clinically significant. Resolution of this discrepancy requires IgE epitope mapping of legume family protein allergens.
|
pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Allergens,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Plant,
http://linkedlifedata.com/resource/pubmed/chemical/Epitopes,
http://linkedlifedata.com/resource/pubmed/chemical/Globulins,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin E,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Seed Storage Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Soybean Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/allergen Ara h3,
http://linkedlifedata.com/resource/pubmed/chemical/glycinin
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
|
pubmed:issn |
1018-2438
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pubmed:author |
|
pubmed:copyrightInfo |
Copyright 2000 S. Karger AG, Basel
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pubmed:issnType |
Print
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pubmed:volume |
123
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pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
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pubmed:pagination |
299-307
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:11146387-Allergens,
pubmed-meshheading:11146387-Amino Acid Sequence,
pubmed-meshheading:11146387-Antigens, Plant,
pubmed-meshheading:11146387-Arachis hypogaea,
pubmed-meshheading:11146387-Binding Sites,
pubmed-meshheading:11146387-Epitopes,
pubmed-meshheading:11146387-Food Hypersensitivity,
pubmed-meshheading:11146387-Globulins,
pubmed-meshheading:11146387-Humans,
pubmed-meshheading:11146387-Immunoglobulin E,
pubmed-meshheading:11146387-Molecular Sequence Data,
pubmed-meshheading:11146387-Peptide Fragments,
pubmed-meshheading:11146387-Recombinant Fusion Proteins,
pubmed-meshheading:11146387-Seed Storage Proteins,
pubmed-meshheading:11146387-Soybean Proteins,
pubmed-meshheading:11146387-Soybeans
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pubmed:year |
2000
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pubmed:articleTitle |
Soybean glycinin G1 acidic chain shares IgE epitopes with peanut allergen Ara h 3.
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pubmed:affiliation |
Department of Biochemistry, University of Nebraska-Lincoln, Lincoln, NE, USA. beardsl@yahoo.com
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|