Evidence map›Paper›PMID 23811341›Full record

ReviewBiochimica et biophysica acta2013

Serum albumins-unusual allergens.

Maksymilian Chruszcz, Katarzyna Mikolajczak, Nicholas Mank, Karolina A Majorek, Przemyslaw J Porebski, Wladek Minor

Abstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing 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

40 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Modern Concept of Molecular Diagnostics of Allergy to Dogs.Bulletin of experimental biology and medicine · 2023
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Review
  17. Molecular diagnosis in cat allergy.World journal of methodology · 2021
    Review
  18. Affinity Diversification of a Polymer Probe for Pattern-recognition-based Biosensing Using Chemical Additives.Analytical sciences : the international journal of the Japan Society for Analytical Chemistry · 2021
    Article
  19. Article
  20. Equine Hypersensitivity: the Dark Horse of Allergy.Clinical reviews in allergy & immunology · 2020
    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

6 authors.

Maksymilian ChruszczDepartment of Chemistry and Biochemistry, University of South Carolina, 631 Sumter Street, Columbia, SC 29208, USA. Electronic address: chruszcz@mailbox.sc.edu.
Katarzyna Mikolajczak
Nicholas Mank
Karolina A Majorek
Przemyslaw J Porebski
Wladek Minor

Funding

The NYSGRC: A Large Scale Center for PSI:BiologyU54GM094662 · NIGMS · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI SEIDEL, RONALD D · 2010 to 2014
$32.6M
NIGMS NIH HHS GM094662NIGMS NIH HHS U54 GM094662
6 · The paper itself

Abstract

backgroundAlbumins are multifunctional proteins present in the blood serum of animals. They can bind and transport a wide variety of ligands which they accommodate due to their conformational flexibility. Serum albumins are highly conserved both in amino acid sequence and three-dimensional structure. Several mammalian and avian serum albumins (SAs) are also allergens. Sensitization to one of the SAs coupled with the high degree of conservation between SAs may result in cross-reactive antibodies in allergic individuals. Sensitivity to SA generally begins with exposure to an aeroallergen, which can then lead to cross-sensitization to serum albumins present in food. SCOPE OF REVIEW: This review focuses on the allergenicity of SAs presented in a structural context. MAJOR

conclusionsSA allergenicity is unusual taking into account the high sequence identity and similarity between SA from different species and human serum albumin. Cross-reactivity of human antibodies towards different SAs is one of the most important characteristics of these allergens. GENERAL SIGNIFICANCE: Establishing a relationship between sequence and structure of different SAs and their interactions with antibodies is crucial for understanding the mechanisms of cross-sensitization of atopic individuals. Structural information can also lead to better design and production of recombinant SAs to replace natural proteins in allergy testing and desensitization. Therefore, structural analyses are important for diagnostic and treatment purposes. This article is part of a Special Issue entitled Serum Albumin.

Indexed as

AllergensAmino Acid SequenceAnimalsCross ReactionsHumansHypersensitivityModels, MolecularMolecular Sequence DataSequence Homology, Amino AcidSerum AlbuminAllergensSerum AlbuminAllergenAntibodybovine serum albuminBSACross-reactiveCross-sensitizationfeline serum albuminFSAHSAhuman serum albuminIgEIgGimmunoglobulin Eimmunoglobulin Gmeasles–mumps–rubellameasles–mumps–rubella–varicellaMMRMMRVporcine serum albuminPSASAserum albuminSerum albumin

Identifiers

PMID23811341
PMCPMC4419372

What OpenQuestion holds

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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.