ArticleBiomolecular NMR assignments2016
NMR resonance assignments of the major apple allergen Mal d 1.
Article in Biomolecular NMR assignments, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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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.
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Who cites it
8 citing papers in PubMed.
- Advances in Food Processing Techniques for Allergenicity Reduction and Allergen Identification.Foods (Basel, Switzerland) · 2025Review
- Multianalytical Approach to Understand Polyphenol-Mal d 1 Interactions to Predict Their Impact on the Allergenic Potential of Apples.Journal of agricultural and food chemistry · 2024Article
- New Mass Spectrometric Approach to Quantify the Major Isoallergens of the Apple Allergen Mal d 1.Journal of agricultural and food chemistry · 2022Article
- Ascorbylation of a Reactive Cysteine in the Major Apple Allergen Mal d 1.Foods (Basel, Switzerland) · 2022Article
- The Structural Flexibility of PR-10 Food Allergens.International journal of molecular sciences · 2022Article
- NMR resonance assignments of the PR-10 allergens Act c 8 and Act d 8 from golden and green kiwifruit.Biomolecular NMR assignments · 2021Article
- Purification and Characterization of Recombinant Expressed Apple Allergen Mal d 1.Methods and protocols · 2020Article
- Structure of the Major Apple Allergen Mal d 1.Journal of agricultural and food chemistry · 2017Article
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Authors and funding
3 authors.
Funding
Abstract
The major apple allergen Mal d 1 is the predominant cause of apple (Malus domestica) allergies in large parts of Europe and Northern America. Allergic reactions against this 17.5 kDa protein are the consequence of initial sensitization to the structurally homologous major allergen from birch pollen, Bet v 1. Consumption of apples can subsequently provoke immunologic cross-reactivity of Bet v 1-specific antibodies with Mal d 1 and trigger severe oral allergic syndroms, affecting more than 70 % of all individuals that are sensitized to birch pollen. While the accumulated immunological data suggest that Mal d 1 has a three-dimensional fold that is similar to Bet v 1, experimental structural data for this protein are not available to date. In a first step towards structural characterization of Mal d 1, backbone and side chain (1)H, (13)C and (15)N chemical shifts of the isoform Mal d 1.0101 were assigned. The NMR-chemical shift data show that this protein is composed of seven β-strands and three α-helices, which is in accordance with the reported secondary structure of the major birch pollen allergen, indicating that Mal d 1 and Bet v 1 indeed have similar three-dimensional folds. The next stage in the characterization of Mal d 1 will be to utilize these resonance assignments in solving the solution structure of this protein.
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