Sort   by:  
 Page size 
ProteomicsQualitative PTM characterization of raw and roasted peanut allergens from aqueous extracts by HRMS
Project is related to immunoproteomic profiling of soluble fractions of raw and roasted peanut. It is still unknown which peanut extract is more allergenic, the raw or roasted version and part of the answer could be in revealing differences between PTM profiles of the raw and roasted peanut.
ORGANISM(S): Arachis hypogaea (Peanut) 
2023-03-11 | PXD033166 | Pride
Roasting Modifications Peanut Allergens Ptm profiling 
ProteomicsDetermination of allergen levels, isoforms and their hydroxyproline modifications among peanut genotypes by mass spectrometry
The recently published genome of peanut enables detailed molecular description of seed storage proteins, particularly allergens, which make up the peanut seed proteome. A detailed description of the allergenic proteome was produced using peanuts of different genetic backgrounds to increase the cover...
ORGANISM(S): Arachis hypogaea (Peanut) 
2022-08-11 | PXD028086 | Pride
Hydroxyproline Food allergy Arachis hypogaea Mass spectrometry Peanut 
ProteomicsDose and route of administration determine the efficacy of prophylactic immunotherapy for peanut allergy in a Brown Norway rat model
MS/MS analysis of the peanut protein extract (PPE) confirmed the presence of the four major peanut allergens and identified the presence of Ara h 1 isotypes, Ara h 2 isotypes, Ara h 3 isotypes, Ara h 6 isotypes and Ara h 7 isotypes. Allergen-specific immunotherapy (IT) is emerging as a viable option...
ORGANISM(S): Arachis hypogaea (Peanut) 
2023-02-21 | PXD039324 | Pride
Food allergy Arachis hypogaea Mass spectrometry Peanut 
TranscriptomicsTranscription profiling by array of mouse BALBc strain mesenteric lymph nodes after response to common allergens.
In this study, MLN transcriptome profiling of female BALB/c mice was conducted in order to explore the molecular mechanism(s) of antigen sensitization using three of the most common food allergens; BLG, OVA and PNA. Analysis of cDNA microarray data revealed a complex network of genes that is modulat...
ORGANISM(S): Mus musculus 
2011-05-11 | E-MEXP-2676 | biostudies-arrayexpress
ProteomicsComparative seed proteome profile reveals no alternation of major allergens of high yielding mung bean cultivars
Mung bean contains up to 25% of the protein, is one of the great sources of plant-based protein. Since many allergens also function as defense-related proteins, it is important to determine their abundance level in the high-yielding disease-resistant cultivars. In this study, for the first time, we ...
ORGANISM(S): Vigna Radiata (ncbitaxon:157791) 
2024-01-19 | MSV000093895 | MassIVE
UnknownCross-reactivity of peanut allergens.
Not available
S-EPMC3962743 | biostudies-literature
GenomicsGene expression data from human myeloid dendritic cells stimulated with peanut protein and other allergens
Gene expression data from human myeloid dendritic cells stimulated with peanut protein and other allergens
PRJNA670228 | ENA
UnknownImpact of cold plasma processing on major peanut allergens.
Not available
S-EPMC7550356 | biostudies-literature
UnknownSkin exposure promotes a Th2-dependent sensitization to peanut allergens.
Not available
S-EPMC4347216 | biostudies-literature
UnknownPeanut allergens: new consolidated findings on structure, characteristics, and allergome.
Not available
S-EPMC6881859 | biostudies-literature
Sort   by:  
 Page size