Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Molecular basis of pollen-related food allergy: identification of a second cross-reactive IgE epitope on Pru av 1, the major cherry (Prunus avium) allergen.

The Biochemical journal - 1 Jan 2005

Wiche Regina, Gubesch Michaela, König Herbert, Fötisch Kay, Hoffmann Andreas, Wangorsch Andrea, Scheurer Stephan, Vieths Stefan

Abstract excerpt

Birch (Betula verrucosa) pollen-associated food allergy is a well-characterized syndrome, which is due to the cross-reactivity of IgE antibodies to homologous allergens in various foods. One crossreacting area on the major birch pollen allergen Bet v 1 and its homologue in cherry (Prunus avium) P...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Allergens
Share to Antibody Specificity
Share to Antigens, Plant

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cross Reactions

Share to Food Hypersensitivity

Share to Immunoglobulin E

Share to Prunus

Share to Surface Plasmon Resonance

Source

Open in PubMed Open full text

Identifiers

PMID: 15330760
DOI: 10.1042/BJ20040842
PMCID: PMC1134700

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026. Prepared record publication-15330760-2026-09-01.1. Manifest publication-graph-cohort-2026-09-01.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 1 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Molecular basis of pollen-related food allergy: identification of a second cross-reactive IgE epitope on Pru av 1, the major cherry (Prunus avium) allergen.PMID 15330760Read ↗

Novel isoforms of Pru av 1 with diverging immunoglobulin E binding properties identified by a synergistic combination of molecular biology and proteomicsSemantic proximity Read ↗

Mutational epitope analysis and cross-reactivity of two isoforms of Api g 1, the major celery allergen.Semantic proximity Read ↗

Characterization of mutants of a highly cross-reactive calcium-binding protein from Brassica pollen for allergen-specific immunotherapy.Semantic proximity Read ↗

The History and Science of the Major Birch Pollen Allergen Bet v 1Semantic proximity Read ↗

The importance of recombinant allergens for diagnosis and therapy of IgE-mediated allergies.Semantic proximity Read ↗

The molecular basis for allergen cross-reactivity: crystal structure and IgE-epitope mapping of birch pollen profilinSemantic proximity Read ↗

Hypoallergenic variants of the Parietaria judaica major allergen Par j 1: a member of the non-specific lipid transfer protein plant family.Semantic proximity Read ↗

A robust method for the estimation and visualization of IgE cross-reactivity likelihood between allergens belonging to the same protein familySemantic proximity Read ↗

Modulation of IgE reactivity of allergens by site-directed mutagenesis: potential use of hypoallergenic variants for immunotherapy.Semantic proximity Read ↗

Pathogenesis-related (PR)-proteins identified as allergensSemantic proximity Read ↗

The Major Human Structural IgE Epitope of the Brazil Nut Allergen Ber e 1: A Chimaeric and Protein Microarray ApproachSemantic proximity Read ↗

Recombinant Allergens in Structural Biology, Diagnosis, and ImmunotherapySemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.