Biochemical and structural analysis of the IgE binding sites on ara h1, an abundant and highly allergenic peanut protein.
about
Microbial relatives of the seed storage proteins of higher plants: conservation of structure and diversification of function during evolution of the cupin superfamilyPeanut Allergy, Allergen Composition, and Methods of Reducing Allergenicity: A ReviewRedefining the major peanut allergensStructural and immunologic characterization of Ara h 1, a major peanut allergen.Food allergy--towards predictive testing for novel foodsPurification and immunoglobulin E-binding properties of peanut allergen Ara h 6: evidence for cross-reactivity with Ara h 2.Molecular cloning and epitope analysis of the peanut allergen Ara h 3.TILLING for allergen reduction and improvement of quality traits in peanut (Arachis hypogaea L.).Peanut and soy allergy: a clinical and therapeutic dilemma.Mechanisms of allergen-specific immunotherapy.Characterization of potential allergens in fenugreek (Trigonella foenum-graecum) using patient sera and MS-based proteomic analysis.Electrochemical immunosensors for antibodies to peanut allergen ara h2 using gold nanoparticle-peptide filmsEpitope analysis of peanut allergen Ara h1 with human monoclonal IgM antibody 92-2Allergic rhinitis caused by food allergies.AllerML: markup language for allergensTILLING by sequencing to identify induced mutations in stress resistance genes of peanut (Arachis hypogaea).Purification and recombinant expression of major peanut allergen Ara h 1.Bioinformatics approaches to classifying allergens and predicting cross-reactivityMucosal immunity and allergic responses: lack of regulation and/or lack of microbial stimulation?Generation of mouse-human hybridomas secreting antibodies against peanut allergen Ara h1A bioinformatics approach to identify patients with symptomatic peanut allergy using peptide microarray immunoassay.Epitope analysis of peanut allergen Ara h1 with oligoclonal IgM antibody from human B-lymphoblastoid cells.Characteristic motifs for families of allergenic proteinsStructural analysis of linear and conformational epitopes of allergens.Comparison of the Digestibility of the Major Peanut Allergens in Thermally Processed Peanuts and in Pure Form.Computationally predicted IgE epitopes of walnut allergens contribute to cross-reactivity with peanutsBioinformatic screening and detection of allergen cross-reactive IgE-binding epitopes.Application of phage peptide display technology for the study of food allergen epitopes.Monoclonal antibody against the Plasmodium falciparum chitinase, PfCHT1, recognizes a malaria transmission-blocking epitope in Plasmodium gallinaceum ookinetes unrelated to the chitinase PgCHT1.Boiling peanut Ara h 1 results in the formation of aggregates with reduced allergenicity.Antigenic cross-reactivity between Schistosoma mansoni and peanut: a role for cross-reactive carbohydrate determinants (CCDs) and implications for the hygiene hypothesis.Monoclonal Antibodies to Recombinant Fag e 3 Buckwheat Allergen and Development of a Two-site ELISA for Its QuantificationEvaluating pH-induced gastrointestinal aggregation of Arachis hypogaea 1 fragments as potential components of peanut allergy.Purification of Recombinant Peanut Allergen Ara h 1 and Comparison of IgE Binding to the Natural Protein.In vitro evaluation of digestive and endolysosomal enzymes to cleave CML-modified Ara h 1 peptides.IgE epitope proximity determines immune complex shape and effector cell activation capacityRelevance of Ara h1, Ara h2 and Ara h3 in peanut-allergic patients, as determined by immunoglobulin E Western blotting, basophil-histamine release and intracutaneous testing: Ara h2 is the most important peanut allergen.Ara h 1 structure is retained after roasting and is important for enhanced binding to IgE.Quantification of major peanut allergens Ara h 1 and Ara h 2 in the peanut varieties Runner, Spanish, Virginia, and Valencia, bred in different parts of the world.Immunotherapy of Food Allergy: a Comprehensive Review.
P2860
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P2860
Biochemical and structural analysis of the IgE binding sites on ara h1, an abundant and highly allergenic peanut protein.
description
1998 nî lūn-bûn
@nan
1998 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի մայիսին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Biochemical and structural ana ...... hly allergenic peanut protein.
@ast
Biochemical and structural ana ...... hly allergenic peanut protein.
@en
Biochemical and structural ana ...... hly allergenic peanut protein.
@nl
type
label
Biochemical and structural ana ...... hly allergenic peanut protein.
@ast
Biochemical and structural ana ...... hly allergenic peanut protein.
@en
Biochemical and structural ana ...... hly allergenic peanut protein.
@nl
prefLabel
Biochemical and structural ana ...... hly allergenic peanut protein.
@ast
Biochemical and structural ana ...... hly allergenic peanut protein.
@en
Biochemical and structural ana ...... hly allergenic peanut protein.
@nl
P2093
P2860
P356
P1476
Biochemical and structural ana ...... ghly allergenic peanut protein
@en
P2093
G A Bannon
R A Kopper
S J Maleki
P2860
P304
13753-13759
P356
10.1074/JBC.273.22.13753
P407
P577
1998-05-01T00:00:00Z