Evidence map›Paper›PMID 28161953›Full record

ArticleJournal of agricultural and food chemistry2017

Structure of the Major Apple Allergen Mal d 1.

Linda Ahammer, Sarina Grutsch, Anna S Kamenik, Klaus R Liedl, Martin Tollinger

Open access · hybridAbstract read
In one paragraph

Article in Journal of agricultural and food chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
3.5field-weighted citation impact, top 7% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

25 citing papers in PubMed, 58 citations in OpenAlex.

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  12. Article
  13. The Structural Flexibility of PR-10 Food Allergens.International journal of molecular sciences · 2022
    Article
  14. Treatment Approaches to Food Allergy.Handbook of experimental pharmacology · 2022
    Review
  15. Article
  16. Article
  17. Structure and Zeatin Binding of the Peach AllergenJournal of agricultural and food chemistry · 2021
    Article
  18. Article
  19. Article
  20. Structural Bases for the Allergenicity of Fra a 1.02 in Strawberry Fruits.Journal of agricultural and food chemistry · 2020
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Linda AhammerInstitute of Organic Chemistry, Center for Molecular Biosciences Innsbruck (CMBI), University of Innsbruck , Innrain 80/82, A-6020 Innsbruck, Austria.
Sarina GrutschInstitute of Organic Chemistry, Center for Molecular Biosciences Innsbruck (CMBI), University of Innsbruck , Innrain 80/82, A-6020 Innsbruck, Austria.
Anna S KamenikInstitute of General, Inorganic and Theoretical Chemistry, Center for Molecular Biosciences Innsbruck (CMBI), University of Innsbruck , Innrain 80/82, A-6020 Innsbruck, Austria.
Klaus R LiedlInstitute of General, Inorganic and Theoretical Chemistry, Center for Molecular Biosciences Innsbruck (CMBI), University of Innsbruck , Innrain 80/82, A-6020 Innsbruck, Austria.ORCID http://orcid.org/0000-0002-0985-2299
Martin TollingerInstitute of Organic Chemistry, Center for Molecular Biosciences Innsbruck (CMBI), University of Innsbruck , Innrain 80/82, A-6020 Innsbruck, Austria.ORCID http://orcid.org/0000-0002-2177-983X
Universität Innsbruck · AT

Funding

Austrian Science Fund FWF P 26849Austrian Science Fund FWF P 30737
6 · The paper itself

Abstract

More than 70% of birch pollen-allergic patients develop allergic cross-reactions to the major allergen found in apple fruits (Malus domestica), the 17.5 kDa protein Mal d 1. Allergic reactions against this protein result from initial sensitization to the major allergen from birch pollen, Bet v 1. Immunologic cross-reactivity of Bet v 1-specific IgE antibodies with Mal d 1 after apple consumption can subsequently provoke severe oral allergic syndromes. This study presents the three-dimensional NMR solution structure of Mal d 1 (isoform Mal d 1.0101, initially cloned from 'Granny Smith' apples). This protein is composed of a seven-stranded antiparallel β-sheet and three α-helices that form a large internal cavity, similar to Bet v 1 and other cross-reactive food allergens. The Mal d 1 structure provides the basis for elucidating the details of allergic cross-reactivity between birch pollen and apple allergens on a molecular level.

Indexed as

Antigens, PlantMalusModels, MolecularPlant ProteinsProtein Conformation, beta-StrandAntigens, PlantMALD1 protein, Malus domesticaPlant ProteinsallergenMal d 1Malus domesticastructure

Identifiers

PMID28161953
PMCPMC5334782
OpenAlexW2584747621

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.