Evidence map›Paper›PMID 26346541›Full record

ArticleScientific reports2015

Dimerization of lipocalin allergens.

Merja H Niemi, Marja Rytkönen-Nissinen, Ilja Miettinen, Janne Jänis, Tuomas Virtanen, Juha Rouvinen

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 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
4.1field-weighted citation impact, top 6% 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

21 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Clinical and Biological Features of a Thickened Basement Membrane Zone in Asthma.American journal of respiratory and critical care medicine · 2025
    Article
  5. Review
  6. Role of Small Molecule Ligands in IgE-Mediated Allergy.Current allergy and asthma reports · 2023
    Review
  7. Review
  8. Impact of oligomerization on the allergenicity of allergens.Clinical and molecular allergy : CMA · 2022
    Review
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Ligand binding complexes in lipocalins: Underestimation of the stoichiometry parameter (n).Biochimica et biophysica acta. Proteins and proteomics · 2018
    Article
  18. Article
  19. Article
  20. 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

6 authors at 1 institution in 1 country.

Merja H NiemiDepartment of Chemistry and Biocenter Kuopio, University of Eastern Finland, PO BOX 111, 80101 Joensuu, Finland.
Marja Rytkönen-NissinenDepartment of Clinical Microbiology, Institute of Clinical Medicine and Biocenter Kuopio, University of Eastern Finland, PO BOX 1627, 70211 Kuopio, Finland.
Ilja MiettinenDepartment of Chemistry and Biocenter Kuopio, University of Eastern Finland, PO BOX 111, 80101 Joensuu, Finland.
Janne JänisDepartment of Chemistry and Biocenter Kuopio, University of Eastern Finland, PO BOX 111, 80101 Joensuu, Finland.
Tuomas VirtanenDepartment of Clinical Microbiology, Institute of Clinical Medicine and Biocenter Kuopio, University of Eastern Finland, PO BOX 1627, 70211 Kuopio, Finland.
Juha RouvinenDepartment of Chemistry and Biocenter Kuopio, University of Eastern Finland, PO BOX 111, 80101 Joensuu, Finland.
University of Eastern Finland · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lipocalins are one of the most important groups of inhalant animal allergens. The analysis of structural features of these proteins is important to get insights into their allergenicity. We have determined two different dimeric crystal structures for bovine dander lipocalin Bos d 2, which was earlier described as a monomeric allergen. The crystal structure analysis of all other determined lipocalin allergens also revealed oligomeric structures which broadly utilize inherent structural features of the β-sheet in dimer formation. According to the moderate size of monomer-monomer interfaces, most of these dimers would be transient in solution. Native mass spectrometry was employed to characterize quantitatively transient dimerization of two lipocalin allergens, Bos d 2 and Bos d 5, in solution.

Indexed as

Protein MultimerizationAllergensLipocalinsMass SpectrometryModels, MolecularProtein ConformationAllergensBos d 2 allergenLipocalins

Identifiers

PMID26346541
PMCPMC4561914
OpenAlexW1414614345

What OpenQuestion holds

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LicenceCC BY
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.