Structural and immunologic characterization of Ara h 1, a major peanut allergen (original) (raw)

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

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Structure of the Major Peanut Allergen Ara h 1 May Protect IgE-Binding Epitopes from Degradation

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Ara h 2: crystal structure and IgE binding distinguish two subpopulations of peanut allergic patients by epitope diversity

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Degradation 1 May Protect IgE-Binding Epitopes from Structure of the Major Peanut Allergen Ara h

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

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Crystallization and preliminary X-ray analysis of the major peanut allergen Ara h 1 core region

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High-yield expression in Escherichia coli, purification, and characterization of properly folded major peanut allergen Ara h 2

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

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

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

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Engineering of structural variants of the major peanut allergens Ara h 2 and Ara h 6 for allergen-specific immunotherapy

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

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Identification of a New Natural Ara h 6 Isoform and of Its Proteolytic Product as Major Allergens in Peanut

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

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Structure and stability of 2S albumin-type peanut allergens: implications for the severity of peanut allergic reactions

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Molecular modelling of the major peanut allergen Ara h 1 and other homotrimeric allergens of the cupin superfamily: a structural basis for their IgE-binding cross-reactivity

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

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Boiling peanut Ara h 1 results in the formation of aggregates with reduced allergenicity

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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)

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

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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

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European Journal of Biochemistry, 1997

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Heating Affects Structure, Enterocyte Adsorption and Signalling, As Well as Immunogenicity of the Peanut Allergen Ara h 2

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

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

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

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Purification and Recombinant Expression of Major Peanut Allergen Ara h 1

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Structural and immunologic characterization of Ara h 1, a major peanut allergen (original) (raw)

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