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Combination of two epitope identification techniques enables the rational design of soy allergen Gly m 4 mutants
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
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A versatile coupled cell‐free transcription–translation system based on tobacco BY‐2 cell lysates
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Mapping B‐cell epitopes of major and minor peanut allergens and identifying residues contributing to IgE binding
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V ig r 6, the cytokinin‐specific binding protein from mung bean ( V igna radiata) sprouts, cross‐reacts with B et v 1‐related allergens and binds I g E from birch pollen allergic patients’ sera
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A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye Binding
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Production of recombinant allergens in plants
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Allergen-specific immunotherapy with recombinant grass pollen allergens
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IgE and IgG4 epitope mapping by microarray immunoassay reveals the diversity of immune response to the peanut allergen, Ara h 2
inferredcites →https://doi.org/10.1016/j.jaci.2008.05.026openalex-snapshot
Several distinct properties of the IgE repertoire determine effector cell degranulation in response to allergen challenge
inferredcites →https://doi.org/10.1016/j.jaci.2009.12.994openalex-snapshot
The natural history of soy allergy
inferredcites →https://doi.org/10.1016/j.jaci.2013.12.1073openalex-snapshot
Chimeras of Bet v 1 and Api g 1 reveal heterogeneous IgE responses in patients with birch pollen allergy
inferredcites →https://doi.org/10.1016/j.jaci.2016.06.019openalex-snapshot
Linear epitope mapping of peanut allergens demonstrates individualized and persistent antibody-binding patterns
inferredcites →https://doi.org/10.1016/j.molimm.2005.02.008openalex-snapshot
A novel approach for investigation of specific and cross-reactive IgE epitopes on Bet v 1 and homologous food allergens in individual patients
inferredcites →https://doi.org/10.1016/j.molimm.2014.09.012openalex-snapshot
Multiple IgE recognition on the major allergen of the Parietaria pollen Par j 2
inferredcites →https://doi.org/10.1038/srep12913openalex-snapshot
High-throughput sequencing enhanced phage display enables the identification of patient-specific epitope motifs in serum
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Mutational epitope analysis of Pru av 1 and Api g 1, the major allergens of cherry (Prunus avium) and celery (Apium graveolens): correlating IgE reactivity with three-dimensional structure
inferredcites →https://doi.org/10.1067/mpd.2002.121935openalex-snapshot
Allergy to soy formula and to extensively hydrolyzed whey formula in infants with cow’s milk allergy: A prospective, randomized study with a follow-up to the age of 2 years
inferredcites →https://doi.org/10.1081/rrs-120026973openalex-snapshot
Phage Display of Random Peptide Libraries: Applications, Limits, and Potential
inferredcites →https://doi.org/10.1093/bioinformatics/bti770openalex-snapshot
The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling
inferredcites →https://doi.org/10.1096/fasebj.12.2.231openalex-snapshot
Modulation of IgE reactivity of allergens by site‐directed mutagenesis: potential use of hypoallergenic variants for immunotherapy
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WebLogo: A Sequence Logo Generator: Figure 1
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IgG-mediated down-regulation of IgE bound to mast cells: a potential novel mechanism of allergen-specific desensitization
inferredcites →https://doi.org/10.1159/000089756openalex-snapshot
Mutational Analysis of Amino Acid Positions Crucial for IgE-Binding Epitopes of the Major Apple (Malus domestica) Allergen, Mal d 1
inferredcites →https://doi.org/10.1159/000345970openalex-snapshot
Allergen Chip Diagnosis for Soy-Allergic Patients: Gly m 4 as a Marker for Severe Food-Allergic Reactions to Soy
inferredcites →https://doi.org/10.1186/1472-6750-14-3openalex-snapshot
Solubility of recombinant Src homology 2 domains expressed in E. colican be predicted by TANGO
inferredcites →https://doi.org/10.1186/1472-6750-14-37openalex-snapshot
Tobacco BY-2 cell-free lysate: an alternative and highly-productive plant-based in vitro translation system
inferredcites →https://doi.org/10.1515/hsz-2013-0206openalex-snapshot
Roasting and lipid binding provide allergenic and proteolytic stability to the peanut allergen Ara h 8
inferredcites →https://doi.org/10.4049/jimmunol.1000804openalex-snapshot
Mapping of Conformational IgE Epitopes with Peptide-Specific Monoclonal Antibodies Reveals Simultaneous Binding of Different IgE Antibodies to a Surface Patch on the Major Birch Pollen Allergen, Bet v 1
inferredcites →https://doi.org/10.4049/jimmunol.157.1.221openalex-snapshot
High-affinity oligonucleotide ligands to human IgE inhibit binding to Fc ε receptor I
inferredcites →https://doi.org/10.4049/jimmunol.165.1.331openalex-snapshot
Dominant Epitopes and Allergic Cross-Reactivity: Complex Formation Between a Fab Fragment of a Monoclonal Murine IgG Antibody and the Major Allergen from Birch Pollen Bet v 1
inferredcites →https://doi.org/10.4049/jimmunol.171.6.3084openalex-snapshot
Dominating IgE-Binding Epitope of Bet v 1, the Major Allergen of Birch Pollen, Characterized by X-ray Crystallography and Site-Directed Mutagenesis
inferredcites →https://doi.org/10.4049/jimmunol.173.8.5258openalex-snapshot
Allergy Vaccine Engineering: Epitope Modulation of Recombinant Bet v 1 Reduces IgE Binding but Retains Protein Folding Pattern for Induction of Protective Blocking-Antibody Responses
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
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Heat-Induced Changes in Epitopes and Ige Binding Capacity of Soybean Proteins
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Plant-Based Cell-Free Transcription and Translation of Recombinant Proteins
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Mammalian Cell Display with Automated Oligo Design and Library Assembly Allows for Rapid Residue Level Conformational Epitope Mapping
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Delivery of Drugs and Vaccines Through Plant Molecular Farming
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Plant Molecular Farming for the Bulk Production of Industrial Enzymes
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Investigation of the differences in the effect of (−)-epigallocatechin gallate and proanthocyanidins on the functionality and allergenicity of soybean protein isolate
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Structural and proteomic characteristics of the extracted protein from thermal sterilized soy seeds and their effects on IgE reactivity, antioxidant activity and interfacial properties
inferred← citeshttps://doi.org/10.1016/j.foodchem.2022.134820openalex-snapshot
Protein modification, IgE binding capacity, and functional properties of soybean protein upon conjugation with polyphenols
inferred← citeshttps://doi.org/10.1016/j.foodchem.2022.134830openalex-snapshot
Heat-induced changes in epitopes and IgE binding capacity of soybean protein isolate
inferred← citeshttps://doi.org/10.1016/j.foodchem.2025.145654openalex-snapshot
Polyphenol-mediated alterations in soybean protein allergenicity and function: a review of current research and future directions
inferred← citeshttps://doi.org/10.1016/j.foodres.2019.108942openalex-snapshot
Food allergomics based on high-throughput and bioinformatics technologies
inferred← citeshttps://doi.org/10.1016/j.foodres.2020.109199openalex-snapshot
Location of destroyed antigenic sites of Gly m Bd 60 K after three processing technologies
inferred← citeshttps://doi.org/10.1016/j.foodres.2025.117424openalex-snapshot
Impact of ultrasound on food allergenicity: A review of current research and future perspective
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2019.09.042openalex-snapshot
Identification of antigenic sites destructed by high hydrostatic pressure (HHP) of the β subunit of β-conglycinin
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2022.08.154openalex-snapshot
Investigation of differences in allergenicity of protein from different soybean cultivars through LC/MS-MS
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2022.10.174openalex-snapshot
Effect of proanthocyanidins on protein composition, conformational structure, IgE binding capacities and functional properties in soybean protein
inferred← citeshttps://doi.org/10.1016/j.jplph.2020.153359openalex-snapshot
Plant molecular farming for the production of valuable proteins – Critical evaluation of achievements and future challenges
inferred← citeshttps://doi.org/10.1016/j.lwt.2021.112678openalex-snapshot
Effects of thermal sterilization on the allergenicity of soybeans
inferred← citeshttps://doi.org/10.1016/j.tifs.2021.10.006openalex-snapshot
Effect of processing on soybean allergens and their allergenicity
inferred← citeshttps://doi.org/10.1021/acs.jafc.4c13046openalex-snapshot
Proteomic Analysis of Antinutritional Protein in Wild and Cultivated Soybean Seeds Based on Four-Dimensional Data-Independent Acquisition and Matrix-Assisted Laser Desorption/Ionization–Mass Spectrometry Imaging
inferred← citeshttps://doi.org/10.1021/acs.jafc.9b02717openalex-snapshot
Simplified Tracking of a Soy Allergen in Processed Food Using a Monoclonal Antibody-Based Sandwich ELISA Targeting the Soybean 2S Albumin Gly m 8
inferred← citeshttps://doi.org/10.1021/acsfoodscitech.2c00380openalex-snapshot
Soybean (Glycine max) allergens─A Review on an Outstanding Plant Food with Allergenic Potential
inferred← citeshttps://doi.org/10.1038/s42003-024-06508-8openalex-snapshot
Mammalian cell display with automated oligo design and library assembly allows for rapid residue level conformational epitope mapping
inferred← citeshttps://doi.org/10.1111/cea.13285openalex-snapshot
The immunome of soy bean allergy: Comprehensive identification and characterization of epitopes
inferred← citeshttps://doi.org/10.1111/cea.14224openalex-snapshot
Peptide epitopes as biomarkers of soya sensitization in rBet v 1 immunotherapy of birch‐related soya allergy
inferred← citeshttps://doi.org/10.1111/ddg.15157openalex-snapshot
Food allergy ‐ New risks through vegan diet? Overview of new allergen sources and current data on the potential risk of anaphylaxis
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Nahrungsmittelallergie ‐ Neue Risiken durch vegane Ernährung? Überblick zu neuen Allergenquellen und aktuelle Daten zum Anaphylaxierisiko
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Identification of Seasonal Variations of Antibodies against PR-10-Specific Epitopes Can Be Improved Using Peptide-Phage Display
inferred← citeshttps://doi.org/10.1186/s12870-026-08130-8openalex-snapshot
CRISPR/Cas9 editing of β-Conglycinin subunits reduces IgE binding in soybean [Glycine max (L.) Merr.]
inferred← citeshttps://doi.org/10.21931/rb/cs/2019.02.01.2openalex-snapshot
Antibody response after hepatitis B vaccine boost mapped with peptide-phage display
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Critical Analysis of the Commercial Potential of Plants for the Production of Recombinant Proteins
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Plant-Derived Cell-Free Biofactories for the Production of Secondary Metabolites
inferred← citeshttps://doi.org/10.3389/fpls.2026.1739979openalex-snapshot
CRISPR/Cas9 ribonucleoprotein-mediated knockout of Gly m 4-L1 eliminates allergen accumulation in soybean
inferred← citeshttps://doi.org/10.3390/antib7020019openalex-snapshot
Anti-Drug Antibodies: Emerging Approaches to Predict, Reduce or Reverse Biotherapeutic Immunogenicity
inferred← citeshttps://doi.org/10.3390/foods13233932openalex-snapshot
Heat Treatment of Hazelnut Allergens Monitored by Polyclonal Sera and Epitope Fingerprinting
inferred← citeshttps://doi.org/10.3390/ijms232315386openalex-snapshot
Structural and Immunologic Properties of the Major Soybean Allergen Gly m 4 Causing Anaphylaxis
inferred← citeshttps://doi.org/10.3390/plants12010038openalex-snapshot
Three Parts of the Plant Genome: On the Way to Success in the Production of Recombinant Proteins
inferred← citeshttps://doi.org/10.3390/vaccines10111861openalex-snapshot
Recent Progress on Vaccines Produced in Transgenic Plants
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