Ara h 2: crystal structure and IgE binding distinguish two subpopulations of peanut allergic patients by epitope diversity
about
Anaphylaxis: opportunities of stratified medicine for diagnosis and risk assessmentThe novel structure of the cockroach allergen Bla g 1 has implications for allergenicity and exposure assessmentCross-reactivity of peanut allergens.100 Years later: Celebrating the contributions of x-ray crystallography to allergy and clinical immunology.Ara h 6 complements Ara h 2 as an important marker for IgE reactivity to peanut.IgE-binding epitopes: a reappraisal.Heating Affects Structure, Enterocyte Adsorption and Signalling, As Well as Immunogenicity of the Peanut Allergen Ara h 2Expression of a codon-optimised recombinant Ara h 2.02 peanut allergen in Escherichia coli.Conformational IgE epitopes of peanut allergens Ara h 2 and Ara h 6.The molecular basis of peanut allergyAssessment of 3D models for allergen researchIdentification of Maillard reaction products on peanut allergens that influence binding to the receptor for advanced glycation end products.Structure of allergens and structure based epitope predictions.Computationally predicted IgE epitopes of walnut allergens contribute to cross-reactivity with peanutsDetermination of Crucial Immunogenic Epitopes in Major Peanut Allergy Protein, Ara h2, via Novel Nanoallergen Platform.Identification of a common Ara h 3 epitope recognized by both the capture and the detection monoclonal antibodies in an ELISA detection kit.In vitro evaluation of digestive and endolysosomal enzymes to cleave CML-modified Ara h 1 peptides.Detection of the Peanut Allergens Ara h 2 and Ara h 6 in Human Breast Milk: Development of 2 Sensitive and Specific Sandwich ELISA Assays.Current (Food) Allergenic Risk Assessment: Is It Fit for Novel Foods? Status Quo and Identification of Gaps.Measurement of specific IgE antibodies to Ses i 1 improves the diagnosis of sesame allergy.Epitope-Resolved Detection of Peanut-Specific IgE Antibodies by Surface Plasmon Resonance Imaging.A Mutant Sumo Facilitates Quick Plasmid Construction for Expressing Proteins with Native N-termini After Tag Removal.Trypsin resistance of the major peanut allergen Ara h 6 and allergenicity of the digestion products are abolished after selective disruption of disulfide bonds.Extended boiling of peanut progressively reduces IgE allergenicity while retaining T cell reactivity.An unfolded variant of the major peanut allergen Ara h 2 with decreased anaphylactic potential.
P2860
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P2860
Ara h 2: crystal structure and IgE binding distinguish two subpopulations of peanut allergic patients by epitope diversity
description
2011 nî lūn-bûn
@nan
2011 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2011年の論文
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2011年学术文章
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2011年学术文章
@zh-cn
2011年学术文章
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2011年学术文章
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2011年学术文章
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2011年學術文章
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name
Ara h 2: crystal structure and ...... patients by epitope diversity
@ast
Ara h 2: crystal structure and ...... patients by epitope diversity
@en
type
label
Ara h 2: crystal structure and ...... patients by epitope diversity
@ast
Ara h 2: crystal structure and ...... patients by epitope diversity
@en
prefLabel
Ara h 2: crystal structure and ...... patients by epitope diversity
@ast
Ara h 2: crystal structure and ...... patients by epitope diversity
@en
P2093
P2860
P50
P1433
P1476
Ara h 2: crystal structure and ...... patients by epitope diversity
@en
P2093
R A Gosavi
R E London
S Wünschmann
P2860
P304
P356
10.1111/J.1398-9995.2010.02532.X
P577
2011-01-21T00:00:00Z