ArticleFoods (Basel, Switzerland)2022
Proteomic Profiling of Major Peanut Allergens and Their Post-Translational Modifications Affected by Roasting.
Article in Foods (Basel, Switzerland), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed, 9 citations in OpenAlex.
- Article
- Modeling Early Events in Food Sensitization: Complementary Insights from Caco-2 and T84 Epithelial Barriers Exposed to Peanut Allergens.Foods (Basel, Switzerland) · 2026Article
- Shotgun proteomics for biomarker discovery in microbial pathogens and allergens in food: a review.Frontiers in bioengineering and biotechnology · 2026Review
- Shrimp allergen extract immunotherapy induces prolonged immune tolerance in a gastro-food allergy mouse model.PloS one · 2024Article
- Antioxidant Properties of Protein-Rich Plant Foods in Gastrointestinal Digestion-Peanuts as Our Antioxidant Friend or Foe in Allergies.Antioxidants (Basel, Switzerland) · 2023Review
- Peanut Allergenicity: An Insight into Its Mitigation Using Thermomechanical Processing.Foods (Basel, Switzerland) · 2023Review
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 5 countries.
Funding
Abstract
Post-translational modifications (PTMs) are covalent changes occurring on amino acid side chains of proteins and yet are neglected structural and functional aspects of protein architecture. The objective was to detect differences in PTM profiles that take place after roasting using open PTM search. We conducted a bottom-up proteomic study to investigate the impact of peanut roasting on readily soluble allergens and their PTM profiles. Proteomic PTM profiling of certain modifications was confirmed by Western blotting with a series of PTM-specific antibodies. In addition to inducing protein aggregation and denaturation, roasting may facilitate change in their PTM pattern and relative profiling. We have shown that Ara h 1 is the most modified major allergen in both samples in terms of modification versatility and extent. The most frequent PTM was methionine oxidation, especially in roasted samples. PTMs uniquely found in roasted samples were hydroxylation (Trp), formylation (Arg/Lys), and oxidation or hydroxylation (Asn). Raw and roasted peanut extracts did not differ in the binding of IgE from the serum of peanut-sensitised individuals done by ELISA. This study provides a better understanding of how roasting impacts the PTM profile of major peanut allergens and provides a good foundation for further exploration of PTMs.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.