(Q52840752)

8 May 2018

title

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

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8 May 2018

author

Lucie Mondoulet

3

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8 May 2018

author name string

T Eiwegger

1

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8 May 2018

N Rigby

2

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8 May 2018

H Bernard

4

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8 May 2018

M-T Krauth

5

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8 May 2018

A Boehm

6

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8 May 2018

E Dehlink

7

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8 May 2018

P Valent

8

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8 May 2018

J M Wal

9

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8 May 2018

E N C Mills

10

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8 May 2018

Z Szépfalusi

11

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8 May 2018

publication date

1 October 2006

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8 May 2018

Clinical & Experimental Allergy

published in

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8 May 2018

volume

36

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8 May 2018

page(s)

1281-1288

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8 May 2018

issue

10

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8 May 2018

Rising prevalence of allergy to peanut in children: Data from 2 sequential cohorts

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Pepsin-digested peanut contains T-cell epitopes but no IgE epitopes

21 January 2018

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Gastrointestinal digestion of Bet v 1-homologous food allergens destroys their mediator-releasing, but not T cell-activating, capacity

21 January 2018

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Structure of the major peanut allergen Ara h 1 may protect IgE-binding epitopes from degradation.

21 January 2018

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Biochemical and structural analysis of the IgE binding sites on ara h1, an abundant and highly allergenic peanut protein.

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Peanut protein allergens: gastric digestion is carried out exclusively by pepsin

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21 January 2018

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Stability of the major allergen Brazil nut 2S albumin (Ber e 1) to physiologically relevant in vitro gastrointestinal digestion.

21 January 2018

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21 January 2018

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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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The production of interferon-gamma in response to a major peanut allergy, Ara h II correlates with serum levels of IgE anti-Ara h II.

21 January 2018

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21 January 2018

Identifiers

DOI

1 reference

8 May 2018

PubMed ID

17014437

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8 May 2018