Evidence map›Paper›PMID 26417906›Full record

ArticleJournal of agricultural and food chemistry2015

Structural and Functional Characterization of the Hazelnut Allergen Cor a 8.

Lesa R Offermann, Merima Bublin, Makenzie L Perdue, Sabine Pfeifer, Pawel Dubiela, Tomasz Borowski, Maksymilian Chruszcz, Karin Hoffmann-Sommergruber

Abstract read
In one paragraph

Article in Journal of agricultural and food chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
–field-weighted citation impact
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

21 citing papers in PubMed.

  1. Review
  2. Article
  3. Calcium-binding proteins as allergens.Frontiers in allergy · 2026
    Review
  4. Article
  5. Role of Small Molecule Ligands in IgE-Mediated Allergy.Current allergy and asthma reports · 2023
    Review
  6. Article
  7. Food Allergens of Plant Origin.Foods (Basel, Switzerland) · 2023
    Review
  8. Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. High-resolution structure of a Kazal-type serine protease inhibitor from the dengue vector Aedes aegypti.Acta crystallographica. Section F, Structural biology communications · 2017
    Article
  20. Review
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

8 authors.

Lesa R OffermannDepartment of Chemistry and Biochemistry, University of South Carolina , Columbia, South Carolina 29208, United States.
Merima BublinDepartment of Pathophysiology and Allergy Research, Center for Pathophysiology, Infectiology and Immunology, Medical University of Vienna , Vienna, Austria.
Makenzie L PerdueDepartment of Chemistry and Biochemistry, University of South Carolina , Columbia, South Carolina 29208, United States.
Sabine PfeiferDepartment of Pathophysiology and Allergy Research, Center for Pathophysiology, Infectiology and Immunology, Medical University of Vienna , Vienna, Austria.
Pawel DubielaDepartment of Pathophysiology and Allergy Research, Center for Pathophysiology, Infectiology and Immunology, Medical University of Vienna , Vienna, Austria.
Tomasz BorowskiJerzy Haber Institute of Catalysis and Surface Chemistry, Polish Academy of Sciences , Kraków, Poland.
Maksymilian ChruszczDepartment of Chemistry and Biochemistry, University of South Carolina , Columbia, South Carolina 29208, United States.
Karin Hoffmann-SommergruberDepartment of Pathophysiology and Allergy Research, Center for Pathophysiology, Infectiology and Immunology, Medical University of Vienna , Vienna, Austria.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nonspecific lipid transfer proteins (nsLTPs) are basic proteins, stabilized by four disulfide bonds, and are expressed throughout the plant kingdom. These proteins are also known as important allergens in fruits and tree nuts. In this study, the nsLTP from hazelnuts, Cor a 8, was purified and its crystal structure determined. The protein is stable at low pH and refolds after thermal denaturation. Molecular dynamics simulations were used to provide an insight into conformational changes of Cor a 8 upon ligand binding. When known epitope areas from Pru p 3 were compared to those of Cor a 8, differences were obvious, which may contribute to limited cross-reactivity between peach and hazelnut allergens. Differences in epitope regions may contribute to limited cross-reactivity between Cor a 8 and nsLTPs from other plant sources. The structure of Cor a 8 represents the first resolved structure of a hazelnut allergen.

Indexed as

AllergensAntigens, PlantCorylusCross ReactionsCrystallography, X-RayEpitopesPlant ProteinsAllergensAntigens, PlantEpitopesPlant Proteinsallergenfood allergyhazelnutnonspecific lipid transfer proteinprotein crystallization

Identifiers

PMID26417906
PMCPMC4616228

What OpenQuestion holds

Textmetadata
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Registered trials

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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.