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Computationally predicted IgE epitopes of walnut allergens contribute to cross‐reactivity with peanuts

Allergy (Copenhagen), 2011-12, Vol.66 (12), p.1522-1529

2011

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Identification of Maillard reaction products on peanut allergens that influence binding to the receptor for advanced glycation end products

Allergy (Copenhagen), 2013-12, Vol.68 (12), p.1546-1554

2013

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The effects of roasting on the allergenic properties of peanut proteins

Journal of allergy and clinical immunology, 2000-10, Vol.106 (4), p.763-768

2000

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The major peanut allergen, Ara h 2, functions as a trypsin inhibitor, and roasting enhances this function

Journal of allergy and clinical immunology, 2003-07, Vol.112 (1), p.190-195

2003

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

The Journal of immunology (1950), 2000-06, Vol.164 (11), p.5844-5849

2000

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Biochemical and Structural Analysis of the IgE Binding Sites on Ara h1, an Abundant and Highly Allergenic Peanut Protein

The Journal of biological chemistry, 1998-05, Vol.273 (22), p.13753-13759

1998

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cDNA Clone of a Putative Peanut (Arachis hypogaea L.) Trypsin Inhibitor Has Homology with Peanut Allergens Ara h 3 and Ara h 4

Journal of agricultural and food chemistry, 2004-03, Vol.52 (5), p.1404-1409

2004

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Characterization of lymphocyte responses to peanuts in normal children, peanut-allergic children, and allergic children who acquired tolerance to peanuts

The Journal of clinical investigation, 2003-04, Vol.111 (7), p.1065-1072

2003

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Staphylococcus aureus AgrA Binding to the RNAIII-agr Regulatory Region

Journal of Bacteriology, 2004-11, Vol.186 (22), p.7549-7555

2004

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MyoD−E12 Heterodimers and MyoD−MyoD Homodimers Are Equally Stable

Biochemistry (Easton), 1997-06, Vol.36 (22), p.6762-6767

1997

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Computationally predicted IgE epitopes of walnut allergens contribute to cross-reactivity with peanuts: Computationally predicted IgE epitopes of walnut

Allergy (Copenhagen), 2011-12, Vol.66 (12), p.1522-1529

2011

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High-Level Expression and Purification of MyoD, Myogenin, and E12

Protein expression and purification, 1997-02, Vol.9 (1), p.91-99

1997

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Differences In IgE Binding To Raw, Roasted And Denatured Ara h 1, A Major Peanut Allergen

Journal of allergy and clinical immunology, 2010-02, Vol.125 (2), p.AB224-AB224

2010

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Structural and functional alterations in major peanut allergens caused by thermal processing

Journal of AOAC International, 2004-11, Vol.87 (6), p.1475

2004

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Allergenicity of Topical Flucinolone Acetonide 0.01% in Peanut Oil in a Patient Previously Sensitized to Peanuts

Journal of allergy and clinical immunology, 2011-02, Vol.127 (2), p.AB194-AB194

2011

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High Level Expression of the Acidic and Basic Subunits of Recombinant Ara h 3

Journal of allergy and clinical immunology, 2011-02, Vol.127 (2), p.AB31-AB31

2011

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High Level Expression and Purification of The Acidic Subunit of Recombinant Ara h 3

Journal of allergy and clinical immunology, 2010-02, Vol.125 (2), p.AB225-AB225

2010

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IgE Binding Areas with Similar Physicochemical Properties Mediate Cross-Reactivity Between Peanut and Tree Nut Allergens

Journal of allergy and clinical immunology, 2011-02, Vol.127 (2), p.AB111-AB111

2011

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Molecular Characterization of Ara h 1 Before and After Thermal Processing

Journal of allergy and clinical immunology, 2011-02, Vol.127 (2), p.AB113-AB113

2011

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Structural and Chemical Modifications are Important in IgE binding to Ara h 1

Journal of allergy and clinical immunology, 2009-02, Vol.123 (2), p.S249-S249

2009

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Identifying Similar IgE-epitopes in Peanut and Walnut Allergens

Journal of allergy and clinical immunology, 2010-02, Vol.125 (2), p.AB147-AB147

2010

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The Role of Chemical Modifications And Structural Changes in IgE Binding By Ara h 2

Journal of allergy and clinical immunology, 2010-02, Vol.125 (2), p.AB225-AB225

2010

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Contribution of Structure to IgE Binding by Ara h 2

Journal of allergy and clinical immunology, 2009-02, Vol.123 (2), p.S32-S32

2009

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Linking Peanut Allergenicity to the Processes of Maturation, Curing, and Roasting

Journal of agricultural and food chemistry, 2003-07, Vol.51 (15), p.4273-4277

2003

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Allergenic Properties of Roasted Peanut Allergens May Be Reduced by Peroxidase

Journal of agricultural and food chemistry, 2004-07, Vol.52 (14), p.4541-4545

2004

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Computationally predicted IgE epitopes of walnut allergens contribute to cross‐reactivity with peanuts

Identification of Maillard reaction products on peanut allergens that influence binding to the receptor for advanced glycation end products

The effects of roasting on the allergenic properties of peanut proteins

The major peanut allergen, Ara h 2, functions as a trypsin inhibitor, and roasting enhances this function

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

Biochemical and Structural Analysis of the IgE Binding Sites on Ara h1, an Abundant and Highly Allergenic Peanut Protein

cDNA Clone of a Putative Peanut (Arachis hypogaea L.) Trypsin Inhibitor Has Homology with Peanut Allergens Ara h 3 and Ara h 4

Characterization of lymphocyte responses to peanuts in normal children, peanut-allergic children, and allergic children who acquired tolerance to peanuts

Staphylococcus aureus AgrA Binding to the RNAIII-agr Regulatory Region

MyoD−E12 Heterodimers and MyoD−MyoD Homodimers Are Equally Stable

Computationally predicted IgE epitopes of walnut allergens contribute to cross-reactivity with peanuts: Computationally predicted IgE epitopes of walnut

High-Level Expression and Purification of MyoD, Myogenin, and E12

Differences In IgE Binding To Raw, Roasted And Denatured Ara h 1, A Major Peanut Allergen

Structural and functional alterations in major peanut allergens caused by thermal processing

Allergenicity of Topical Flucinolone Acetonide 0.01% in Peanut Oil in a Patient Previously Sensitized to Peanuts

High Level Expression of the Acidic and Basic Subunits of Recombinant Ara h 3

High Level Expression and Purification of The Acidic Subunit of Recombinant Ara h 3

IgE Binding Areas with Similar Physicochemical Properties Mediate Cross-Reactivity Between Peanut and Tree Nut Allergens

Molecular Characterization of Ara h 1 Before and After Thermal Processing

Structural and Chemical Modifications are Important in IgE binding to Ara h 1

Identifying Similar IgE-epitopes in Peanut and Walnut Allergens

The Role of Chemical Modifications And Structural Changes in IgE Binding By Ara h 2

Contribution of Structure to IgE Binding by Ara h 2

Linking Peanut Allergenicity to the Processes of Maturation, Curing, and Roasting

Allergenic Properties of Roasted Peanut Allergens May Be Reduced by Peroxidase

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