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Grantee Research Project Results

Publications Details for Grant Number R834066

Clinically Relevant IgE-Cross-Reactivity of Nut Allergens

RFA: Exploratory Investigations in Food Allergy (2007)

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Abstract (1)
Journal Article (6)
Presentation (7)
Reference Type Reference Title Journal Author Citation Progress Report Year Document Sources
Abstract IgE binding areas with similar physiochemical properties mediate cross-reactivity between peanut and tree nut allergens. JOURNAL OF ALLERGY AND CLINICAL IMMUNOLOGY Maleki SJ, Teuber SS, Cheng H, Schein CH Maleki SJ, Teuber SS, Cheng H, Schein CH. IgE binding areas with similar physiochemical properties mediate cross-reactivity between peanut and tree nut allergens. Journal of Allergy and Clinical Immunology 2011;127(Suppl 2):AB111. R834066 (Final)
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Journal Article Simplifying complex sequence information: A PCP-consensus protein binds antibodies against all four Dengue serotypes. VACCINE Bowen DM, Lewis JA, Lu W, Schein CH Bowen DM, Lewis JA, Lu W, Schein CH. Simplifying complex sequence information: A PCP-consensus protein binds antibodies against all four Dengue serotypes. Vaccine 2012;30(42):6081-6087. R834066 (Final)
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Journal Article AllerML: markup language for allergens. REGULATORY TOXICOLOGY AND PHARMACOLOGY Ivanciuc O, Gendel SM, Power TD, Schein CH, Braun W Ivanciuc O, Gendel SM, Power TD, Schein CH, Braun W. AllerML: markup language for allergens. Regulatory Toxicology and Pharmacology 2011;60(1):151-160. R834066 (Final)
R834823 (2011)
R834823 (2013)
R834823 (Final)
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Journal Article Computationally predicted IgE epitopes of walnut allergens contribute to cross-reactivity with peanuts. ALLERGY Maleki SJ, Teuber SS, Cheng H, Chen D, Comstock SS, Ruan S, Schein CH Maleki SJ, Teuber SS, Cheng H, Chen D, Comstock SS, Ruan S, Schein CH. Computationally predicted IgE epitopes of walnut allergens contribute to cross-reactivity with peanuts. Allergy 2011;66(12):1522-1529. R834066 (2010)
R834066 (Final)
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Journal Article Ara h 1 structure is retained after roasting and is important for enhanced binding to IgE. None Nesbit JB, Hurlburt BK, Schein CH, Cheng H, Wei H, Maleki SJ Nesbit JB, Hurlburt BK, Schein CH, Cheng H, Wei H, Maleki SJ. Ara h 1 structure is retained after roasting and is important for enhanced binding to IgE. Molecular Nutrition and Food Research 2012;56(11):1739-1747. R834066 (Final)
R834823 (2012)
R834823 (2013)
R834823 (Final)
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Journal Article An allergen portrait gallery: representative structures and an overview of IgE binding surfaces. BIOINFORMATICS AND BIOLOGY INSIGHTS Schein CH, Ivanciuc O, Midoro-Horiuti T, Goldblum RM, Braun W Schein CH, Ivanciuc O, Midoro-Horiuti T, Goldblum RM, Braun W. An allergen portrait gallery: representative structures and an overview of IgE binding surfaces. Bioinformatics and Biology Insights 2010;4:113-125. R833137 (Final)
R834066 (Final)
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Journal Article Physicochemical property consensus sequences for functional analysis, design of multivalent antigens and targeted antivirals. None Schein CH, Bowen DM, Lewis JA, Choi K, Paul A, van der Heden van Noort GJ, Lu W, Filippov DV Schein CH, Bowen DM, Lewis JA, Choi K, Paul A, van der Heden van Noort GJ, Lu W, Filippov DV. Physicochemical property consensus sequences for functional analysis, design of multivalent antigens and targeted antivirals. BMC Bioinformatics 2012;13(Suppl 13):S9. R834066 (Final)
R834823 (2012)
R834823 (2013)
R834823 (Final)
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Presentation IgE binding areas with similar physicochemical properties mediate cross-reactivity between peanut and tree nut allergens. None Maleki SJ, Teuber SS, Cheng H, Schein CH Maleki SJ, Teuber SS, Cheng H, Schein CH. IgE binding areas with similar physicochemical properties mediate cross-reactivity between peanut and tree nut allergens. Presented at the American Academy of Allergy, Asthma & Immunology (AAAAI) Annual Meeting, San Francisco, CA, March 18-22, 2011. R834066 (Final)
not available
Presentation Clinically relevant IgE-cross-reactivity of nut allergens. None Maleki S Maleki S. Clinically relevant IgE-cross-reactivity of nut allergens. Presented to the National Peanut Board, Atlanta, GA, September 24, 2009. R834066 (2009)
R834066 (2010)
not available
Presentation Clinically relevant IgE-cross-reactivity of nut allergens. None Maleki S Maleki S. Clinically relevant IgE-cross-reactivity of nut allergens. Presented to the National Peanut Board, Atlanta, GA, February 22, 2010. R834066 (2009)
R834066 (2010)
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Presentation Common allergenic epitopes in nut proteins contribute to cross reactivity. None Schein CH Schein CH. Common allergenic epitopes in nut proteins contribute to cross reactivity. Presented at the ILSI Health and Environmental Sciences Institute (HESI) Food Allergy Workshop, The Beacon Hotel and Corporate Quarters, Washington, DC, October 15, 2008. R833137 (Final)
R834066 (2010)
R834066 (Final)
not available
Presentation Defining IgE epitopes involved in allergen cross reactivity. None Schein CH Schein CH. Defining IgE epitopes involved in allergen cross reactivity. Presented at the UTMB Immunology Research in Progress Seminar, The University of Texas Medical Branch Galveston, Galveston, TX, April 1, 2009. R833137 (Final)
R834066 (2010)
R834066 (Final)
not available
Presentation Identifying similar IgE-epitopes in peanut and walnut allergens. None Schein CH, Maleki SJ, Teuber S Schein CH, Maleki SJ, Teuber S. Identifying similar IgE-epitopes in peanut and walnut allergens. Presented at the American Academy of Allergy, Asthma & Immunology (AAAAI) Annual Meeting, New Orleans, LA, February 26-March 2, 2010. R833137 (Final)
R834066 (2010)
R834066 (Final)
not available
Presentation Using physicochemical-property similarity to define common IgE-epitopes in peanut and walnut allergens. None Schein CH, Maleki S, Teuber S Schein CH, Maleki S, Teuber S. Using physicochemical-property similarity to define common IgE-epitopes in peanut and walnut allergens. Presented at the 15th Annual Sealy Center for Structural Biology and Molecular Biophysics Symposium, Hotel Galvez, Galveston, TX, March 19, 2010. R833137 (Final)
R834066 (2010)
R834066 (Final)
not available

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