| http://purl.uniprot.org/citations/33439436 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/33439436 | http://www.w3.org/2000/01/rdf-schema#comment | "Peanut allergies are among the most severe food allergies, and several allergenic proteins referred to as Ara h 1-Ara h 17 have been identified from peanut seeds. The molecular characterization of Ara h 1 (63 kDa), a glycosylated allergen, has almost been completed, and the occurrence of two homologous genes (clone 41B and clone P17) has been identified. In this study, we found a new variant of Ara h 1 i.e. 54 kDa, in which the N-terminal amino acid sequence was EGREGEQ-, indicating that the N-terminal domain of 63 kDa Ara h 1 had been removed. This new isoform was obtained from the run-through fraction of hydrophobic interaction chromatography while 63 kDa Ara h 1 was tightly bound to the hydrophobic resins, suggesting that the removal of the N-terminal domain resulted in extreme hydrophilic properties. We found that 63 kDa Ara h 1 occurs as higher order homo-oligomeric conformations such as decamer or nonamer, while 54 kDa Ara h 1 occurs exclusively as a homotrimer, indicating that the N-terminal domain of the 63 kDa molecule may be involved in higher order oligomerization. When antisera from peanut-allergic patients were treated with both the Ara h 1 molecules, the immunoglobulin E (IgE) antibodies in these sera reacted with each Ara h 1 molecule, suggesting that the C-terminal as well as the N-terminal domains of Ara h 1 contribute significantly to the epitope formations of this peanut glycoallergen. Furthermore, the glycoform analyses of N-glycans linked to 63 kDa and 54 kDa Ara h 1 subunits revealed that both typical high-mannose type and β-xylosylated type N-glycans are linked to the molecules. The cross-reactivity of IgE against Ara h 1 in the serum of one peanut allergy patient was completely lost by de-N-glycosylation, indicating the N-glycan of Ara h 1 was the sole epitope for the Ara h 1-specific IgE in the patient."xsd:string |
| http://purl.uniprot.org/citations/33439436 | http://purl.org/dc/terms/identifier | "doi:10.1007/s10719-020-09969-1"xsd:string |
| http://purl.uniprot.org/citations/33439436 | http://purl.uniprot.org/core/author | "Kimura Y."xsd:string |
| http://purl.uniprot.org/citations/33439436 | http://purl.uniprot.org/core/author | "Ito K."xsd:string |
| http://purl.uniprot.org/citations/33439436 | http://purl.uniprot.org/core/author | "Maeda M."xsd:string |
| http://purl.uniprot.org/citations/33439436 | http://purl.uniprot.org/core/author | "Matsui T."xsd:string |
| http://purl.uniprot.org/citations/33439436 | http://purl.uniprot.org/core/author | "Md A."xsd:string |
| http://purl.uniprot.org/citations/33439436 | http://purl.uniprot.org/core/author | "Takasato Y."xsd:string |
| http://purl.uniprot.org/citations/33439436 | http://purl.uniprot.org/core/date | "2021"xsd:gYear |
| http://purl.uniprot.org/citations/33439436 | http://purl.uniprot.org/core/name | "Glycoconj J"xsd:string |
| http://purl.uniprot.org/citations/33439436 | http://purl.uniprot.org/core/pages | "67-76"xsd:string |
| http://purl.uniprot.org/citations/33439436 | http://purl.uniprot.org/core/title | "Purification and molecular characterization of a truncated-type Ara h 1, a major peanut allergen: oligomer structure, antigenicity, and glycoform."xsd:string |
| http://purl.uniprot.org/citations/33439436 | http://purl.uniprot.org/core/volume | "38"xsd:string |
| http://purl.uniprot.org/citations/33439436 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/33439436 |
| http://purl.uniprot.org/citations/33439436 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/33439436 |
| http://purl.uniprot.org/uniprot/#_E9LFE7-mappedCitation-33439436 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/33439436 |
| http://purl.uniprot.org/uniprot/#_B2CMA3-mappedCitation-33439436 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/33439436 |
| http://purl.uniprot.org/uniprot/#_B3IXL2-mappedCitation-33439436 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/33439436 |
| http://purl.uniprot.org/uniprot/#_E5G076-mappedCitation-33439436 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/33439436 |
| http://purl.uniprot.org/uniprot/#_N1NG13-mappedCitation-33439436 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/33439436 |
| http://purl.uniprot.org/uniprot/#_P43237-mappedCitation-33439436 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/33439436 |
| http://purl.uniprot.org/uniprot/#_P43238-mappedCitation-33439436 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/33439436 |
| http://purl.uniprot.org/uniprot/#_Q6PSU3-mappedCitation-33439436 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/33439436 |
| http://purl.uniprot.org/uniprot/#_Q6PSU4-mappedCitation-33439436 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/33439436 |