Biochemical and structural analysis of the IgE binding sites on Ara h1, an abundant and highly allergenic peanut protein (original) (raw)

Identification and Mutational Analysis of the Immunodominant IgE Binding Epitopes of the Major Peanut Allergen Ara H 2

… of biochemistry and …, 1997

Protein structure plays a critical role in peanut allergen Ara h 2 stability and may determine immunodominant IgE binding epitopes

Moon Sen

Journal of Allergy and Clinical Immunology, 2002

Protein structure plays a critical role in peanut allergen stability and may determine immunodominant IgE-binding epitopes

Moon Sen

Journal of immunology (Baltimore, Md. : 1950), 2002

Isoforms of the Major Peanut Allergen Ara h 2: IgE Binding in Children with Peanut Allergy

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International Archives of Allergy and Immunology, 2004

Structural and immunologic characterization of Ara h 1, a major peanut allergen

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Journal of Biological Chemistry, 2011

Purification of Recombinant Peanut Allergen Ara h 1 and Comparison of IgE Binding to the Natural Protein

Jane McBride, Jacqueline Nesbit, Barry Hurlburt

Foods, 2014

Recombinant peanut allergen Ara h I expression and IgE binding in patients with peanut hypersensitivity

Journal of Clinical …, 1995

Homology modelling of the major peanut allergen Ara h 2 and surface mapping of IgE-binding epitopes

Annick Barre

Immunology Letters, 2005

Peanut allergen Ara h 3: Isolation from peanuts and biochemical characterization

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Mapping and Mutational Analysis of the IgE-Binding Epitopes on Ara H 1, a Legume Vicilin Protein and a Major Allergen In Peanut Hypersensitivity

European Journal …, 1997

Purification and immunoglobulin E-binding properties of peanut allergen Ara h 6: evidence for cross-reactivity with Ara h 2

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Crystal structure of Ara h 3, a major allergen in peanut

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Common Physical−Chemical Properties Correlate with Similar Structure of the IgE Epitopes of Peanut Allergens

Catherine Schein

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Molecular Cloning and Epitope Analysis of the Peanut Allergen Ara H 3

Journal of Clinical …, 1999

IgE binding to peanut components by four different techniques: Ara h 2 is the most relevant in peanut allergic children and adults

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Mapping and conformational analysis of IgE-binding epitopic regions on the molecular surface of the major Ara h 3 legumin allergen of peanut (Arachis hypogaea)

Pierre Rouge

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IgE epitopes of Ara h 9, Jug r 3, and Pru p 3 in peanut-allergic individuals from Spain and the US

Jacqueline Nesbit

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Characterisation of the IgE-binding immunodominant epitopes on Ara h1

fei lou

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Relevance of ara h1, ara h2, and ara h3 in peanut allergic patients, as determined by IgE-western-blotting, basophil histamine release, and intracultaneous testing: Ara h2 is the most important peanut allergen

The Journal of Allergy and Clinical Immunology, 2003

Immunodominant IgE-Binding Epitopes DeterminePeanut Allergen Stability and May Protein Structure Plays a Critical Role in

2002

Relevance 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

André Knulst, Edward Knol

Clinical <html_ent glyph="@amp;" ascii="&"/> Experimental Allergy, 2004

Peanut panallergen Ara h 8 IgE and IgG4 epitopes

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Gastro-duodenal digestion products of the major peanut allergen Ara h 1 retain an allergenic potential

Neil Rigby, Lucie Mondoulet

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Mapping B-cell epitopes of major and minor peanut allergens and identifying residues contributing to IgE binding

Anuja Jain

Journal of the Science of Food and Agriculture, 2015

Effector activity of peanut allergens: a critical role for Ara h 2, Ara h 6, and their variants

Mark W Duncan

Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology, 2009

Structural Biology of Peanut Allergens

Barry Hurlburt

Journal of Contemporary Immunology, 2015

Component-Resolved IgE Profiles in Austrian Patients with a Convincing History of Peanut Allergy

Heimo Breiteneder

International Archives of Allergy and Immunology, 2015

Specific IgE to peanut 2S albumin Ara h 7 has a discriminative ability comparable to Ara h 2 and 6

Clinical & Experimental Allergy, 2017