Conformational stability of digestion-resistant peptides of peanut conglutins reveals the molecular basis of their allergenicity-Reference-Cited by-同舟云学术

Conformational stability of digestion-resistant peptides of peanut conglutins reveals the molecular basis of their allergenicity

Published:2016-07 Issue:1 Volume:6 Page:
ISSN:2045-2322
Container-title:Scientific Reports
language:en
Short-container-title:Sci Rep

Author:

Apostolovic Danijela,Stanic-Vucinic Dragana,de Jongh Harmen H. J.,de Jong Govardus A. H.,Mihailovic Jelena,Radosavljevic Jelena,Radibratovic Milica,Nordlee Julie A.,Baumert Joseph L.,Milcic Milos,Taylor Steve L.,Garrido Clua Nuria,Cirkovic Velickovic Tanja,Koppelman Stef J.

Publisher

Springer Science and Business Media LLC

Subject

Multidisciplinary

Link

http://www.nature.com/articles/srep29249.pdf

Reference52 articles.

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2. Koppelman, S. J., Wensing, M., Ertmann, M., Knulst, A. C. & Knol, E. F. 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. Clin Exp Allergy 34, 583–590, 10.1111/j.1365-2222.2004.1923.x (2004).

3. Peeters, K. A. et al. Does skin prick test reactivity to purified allergens correlate with clinical severity of peanut allergy? Clin Exp Allergy 37, 108–115, 10.1111/j.1365-2222.2006.02628.x (2007).

4. Blanc, F. et al. Capacity of purified peanut allergens to induce degranulation in a functional in vitro assay: Ara h 2 and Ara h 6 are the most efficient elicitors. Clin Exp Allergy 39, 1277–1285, 10.1111/j.1365-2222.2009.03294.x (2009).

5. Mayorga, C. et al. Basophil response to peanut allergens in Mediterranean peanut-allergic patients. Allergy 69, 964–968, 10.1111/all.12421 (2014).

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