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High‐pressure microfluidisation‐induced changes in the antigenicity and conformation of allergen Ara h 2 purified from Chinese peanut
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1006/abbi.1997.9998openalex-snapshot
Identification and Mutational Analysis of the Immunodominant IgE Binding Epitopes of the Major Peanut AllergenAra h 2
inferredcites →https://doi.org/10.1016/0003-2697(78)90812-6openalex-snapshot
Circular dichroic analysis of protein conformation: Inclusion of the β-turns
inferredcites →https://doi.org/10.1016/0003-9861(59)90090-6openalex-snapshot
Tissue sulfhydryl groups
inferredcites →https://doi.org/10.1016/0167-4838(89)90117-9openalex-snapshot
Monoclonal antibodies as probes for monitoring the denaturation process of bovine β-lactoglobulin
inferredcites →https://doi.org/10.1016/j.bbapap.2005.11.010openalex-snapshot
High pressure-induced changes in bovine milk proteins: A review
inferredcites →https://doi.org/10.1016/j.biotechadv.2005.05.008openalex-snapshot
Effects of food processing on the stability of food allergens
inferredcites →https://doi.org/10.1016/j.foodchem.2008.06.051openalex-snapshot
Conformational changes of Mal d 2, a thaumatin-like apple allergen, induced by food processing
inferredcites →https://doi.org/10.1016/j.imlet.2005.03.014openalex-snapshot
Homology modelling of the major peanut allergen Ara h 2 and surface mapping of IgE-binding epitopes
inferredcites →https://doi.org/10.1016/j.jaci.2008.09.012openalex-snapshot
Allergenicity and antigenicity of fenugreek (Trigonella foenum-graecum) proteins in foods
inferredcites →https://doi.org/10.1016/j.molimm.2007.01.023openalex-snapshot
Homology modelling and conformational analysis of IgE-binding epitopes of Ara h 3 and other legumin allergens with a cupin fold from tree nuts
inferredcites →https://doi.org/10.1016/s0021-9258(19)52451-6openalex-snapshot
PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENT
inferredcites →https://doi.org/10.1016/s0091-6749(03)02026-8openalex-snapshot
Prevalence of peanut and tree nut allergy in the United States determined by means of a random digit dial telephone survey
inferredcites →https://doi.org/10.1016/s0268-005x(98)00073-3openalex-snapshot
Interactions of ovalbumin with sulphated polysaccharides: effects of pH, ionic strength, heat and high pressure treatment
inferredcites →https://doi.org/10.1016/s1466-8564(03)00043-2openalex-snapshot
Influence of high pressure on conformational changes of soybean glycinin
inferredcites →https://doi.org/10.1016/s1466-8564(03)00061-4openalex-snapshot
High pressure microfluidization treatment of heat denatured whey proteins for improved functionality
inferredcites →https://doi.org/10.1021/bi030115qopenalex-snapshot
Effects of Disulfide Bonds on Compactness of Protein Molecules Revealed by Volume, Compressibility, and Expansibility Changes during Reduction
inferredcites →https://doi.org/10.1021/jf050091popenalex-snapshot
Influence of Thermal Processing on the Allergenicity of Peanut Proteins
inferredcites →https://doi.org/10.1021/jf9006642openalex-snapshot
Characterization and High-Pressure Microfluidization-Induced Activation of Polyphenoloxidase from Chinese Pear (Pyrus pyrifolia Nakai)
inferredcites →https://doi.org/10.1021/jf990393popenalex-snapshot
Comparison of Protein Surface Hydrophobicity Measured at Various pH Values Using Three Different Fluorescent Probes
inferredcites →https://doi.org/10.1038/227680a0openalex-snapshot
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
inferredcites →https://doi.org/10.1042/bj20051728openalex-snapshot
Structure and stability of 2S albumin-type peanut allergens: implications for the severity of peanut allergic reactions
inferredcites →https://doi.org/10.1067/mai.2002.128802openalex-snapshot
Rising prevalence of allergy to peanut in children: Data from 2 sequential cohorts
inferredcites →https://doi.org/10.1067/mai.2003.1551openalex-snapshot
The major peanut allergen, Ara h 2, functions as a trypsin inhibitor, and roasting enhances this function
inferredcites →https://doi.org/10.1074/jbc.273.22.13753openalex-snapshot
Biochemical and Structural Analysis of the IgE Binding Sites on Ara h1, an Abundant and Highly Allergenic Peanut Protein
inferredcites →https://doi.org/10.1080/20024091054274openalex-snapshot
Food Processing by High Hydrostatic Pressure
inferredcites →https://doi.org/10.1081/jas-120004922openalex-snapshot
Sensitization to Common Food Allergens Is a Risk Factor for Asthma in Young Chinese Children in Hong Kong
inferredcites →https://doi.org/10.1105/tpc.7.7.945openalex-snapshot
Seed Storage Proteins: Structures and Biosynthesis
inferredcites →https://doi.org/10.1111/j.1365-2222.1994.tb00987.xopenalex-snapshot
A major continuous allergenic epitope of bovine β‐lactoglobulin recognized by human IgE binding
inferredcites →https://doi.org/10.1111/j.1365-2222.2004.1923.xopenalex-snapshot
Relevance of Ara h1, Ara h2 and Ara h3 in peanut‐allergic patients, as determined by immunoglobulin E Western blotting, basophil–histamine release and intracutaneous testing: Ara h2 is the most important peanut allergen
inferredcites →https://doi.org/10.1111/j.1365-2222.2006.02466.xopenalex-snapshot
Competition enzyme‐linked immunosorbant assay (ELISA) can be a sensitive method for the specific detection of small quantities of allergen in a complex mixture
inferredcites →https://doi.org/10.1111/j.1462-5822.2007.00901.xopenalex-snapshot
Lounging in a lysosome: the intracellular lifestyle of Coxiella burnetii
inferredcites →https://doi.org/10.1111/j.1745-4514.2005.00038.xopenalex-snapshot
PHYSICOCHEMICAL AND STRUCTURAL CHARACTERISTICS OF SODIUM CASEINATE BIOPOLYMERS INDUCED BY MICROBIAL TRANSGLUTAMINASE
inferredcites →https://doi.org/10.3168/jds.s0022-0302(97)76166-6openalex-snapshot
Effects of Microfluidizer® Technology on Bacillus licheniformis Spores in Ice Cream Mix
inferredcites →https://doi.org/10.4049/jimmunol.169.2.882openalex-snapshot
Protein Structure Plays a Critical Role in Peanut Allergen Stability and May Determine Immunodominant IgE-Binding Epitopes
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
inferred← citeshttps://doi.org/10.2139/ssrn.4761184openalex-extracted
Co-Fermentation by Selected Lactic Acid Bacteria Reduces Immunoreactivity of Peanut and Enhances its Physicochemical and Sensory Attributes
inferred← citeshttps://doi.org/10.1002/jsfa.10040openalex-snapshot
Polyphenol‐oxidase‐catalyzed cross‐linking of Ara h 2: reaction sites and effect on structure and allergenicity
inferred← citeshttps://doi.org/10.1002/jsfa.12454openalex-snapshot
Mitigating the allergenicity of peanut allergen Ara h 1 by cold atmospheric pressure argon plasma jet
inferred← citeshttps://doi.org/10.1002/jsfa.7321openalex-snapshot
Reactivity change of IgE to buckwheat protein treated with high‐pressure and enzymatic hydrolysis
inferred← citeshttps://doi.org/10.1002/jsfa.7542openalex-snapshot
Crosslinking of peanut allergen Ara h 2 by polyphenol oxidase: digestibility and potential allergenicity assessment
inferred← citeshttps://doi.org/10.1002/jsfa.8489openalex-snapshot
Development of a H2O2‐sensitive quantum dots‐based fluorescent sandwich ELISA for sensitive detection of bovine β‐lactoglobulin by monoclonal antibody
inferred← citeshttps://doi.org/10.1002/mnfr.201200472openalex-snapshot
Impact of dietary factors and food processing on food allergy
inferred← citeshttps://doi.org/10.1007/978-3-032-12323-7_3openalex-snapshot
Microfluidization—Applications in Food Industry
inferred← citeshttps://doi.org/10.1007/s00217-025-04934-4openalex-snapshot
Challenges in reducing soybean allergens using combined techniques: microfluidization and enzymatic hydrolysis
inferred← citeshttps://doi.org/10.1007/s12016-020-08810-9openalex-snapshot
Are Physicochemical Properties Shaping the Allergenic Potency of Plant Allergens?
inferred← citeshttps://doi.org/10.1007/s13197-017-2972-2openalex-snapshot
High hydrostatic pressure (HHP) effects on antigenicity and structural properties of soybean β-conglycinin
inferred← citeshttps://doi.org/10.1016/b978-0-08-100722-8.00015-2openalex-snapshot
Detection and deactivation of allergens in food
inferred← citeshttps://doi.org/10.1016/b978-0-12-811449-0.00010-4openalex-snapshot
Dynamic High Pressure Effects on Biopolymers: Polysaccharides and Proteins
inferred← citeshttps://doi.org/10.1016/b978-0-323-89842-3.00012-9openalex-snapshot
Reducing allergenicity in plant-based proteins
inferred← citeshttps://doi.org/10.1016/b978-0-323-95052-7.00005-4openalex-snapshot
Emerging technologies for processing of plant proteins
inferred← citeshttps://doi.org/10.1016/j.bbapap.2013.10.004openalex-snapshot
Reduction and alkylation of peanut allergen isoforms Ara h 2 and Ara h 6; characterization of intermediate- and end products
inferred← citeshttps://doi.org/10.1016/j.fbio.2024.104408openalex-snapshot
Co-fermentation of peanut milk by selected lactic acid bacteria on its protein structure, Ara h 1's immunoreactivity, physical-chemical properties and sensory attributes
inferred← citeshttps://doi.org/10.1016/j.fct.2014.12.002openalex-snapshot
Allergenic response to squid (Todarodes pacificus) tropomyosin Tod p1 structure modifications induced by high hydrostatic pressure
inferred← citeshttps://doi.org/10.1016/j.fochx.2023.100566openalex-snapshot
Investigation of the differences in the effect of (−)-epigallocatechin gallate and proanthocyanidins on the functionality and allergenicity of soybean protein isolate
inferred← citeshttps://doi.org/10.1016/j.foodchem.2015.09.070openalex-snapshot
Allergen composition analysis and allergenicity assessment of Chinese peanut cultivars
inferred← citeshttps://doi.org/10.1016/j.foodchem.2017.01.060openalex-snapshot
Development of sandwich ELISA for testing bovine β-lactoglobulin allergenic residues by specific polyclonal antibody against human IgE binding epitopes
inferred← citeshttps://doi.org/10.1016/j.foodchem.2018.12.070openalex-snapshot
Allergenicity assessment on thermally processed peanut influenced by extraction and assessment methods
inferred← citeshttps://doi.org/10.1016/j.foodchem.2021.130805openalex-snapshot
Release and conformational changes in allergenic proteins from wheat gluten induced by high hydrostatic pressure
inferred← citeshttps://doi.org/10.1016/j.foodchem.2022.132569openalex-snapshot
Effect of high-moisture extrusion and addition of transglutaminase on major peanut allergens content extracted by three step sequential method
inferred← citeshttps://doi.org/10.1016/j.foodchem.2022.133208openalex-snapshot
Changes in IgE binding capacity, structure, physicochemical properties of peanuts through fermentation with Bacillus natto and Lactobacillus plantarum along with autoclave pretreatment
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.2024.140858openalex-snapshot
High hydrostatic pressure reduces inflammation induced by litchi thaumatin-like protein via altering active domain
inferred← citeshttps://doi.org/10.1016/j.foodchem.2025.145349openalex-snapshot
A new perspective on the regulation of food allergy: the tilt from a single component to a multi-component system
inferred← citeshttps://doi.org/10.1016/j.foodcont.2014.02.030openalex-snapshot
Effects of high pressure processing on immunoreactivity and microbiological safety of crushed peanuts
inferred← citeshttps://doi.org/10.1016/j.foodres.2014.02.021openalex-snapshot
Effect of high pressure processing on the immunoreactivity of almond milk
inferred← citeshttps://doi.org/10.1016/j.foodres.2018.04.021openalex-snapshot
Effect of thermal/pressure processing and simulated human digestion on the immunoreactivity of extractable peanut allergens
inferred← citeshttps://doi.org/10.1016/j.foodres.2022.111427openalex-snapshot
Insight into the mechanism of allergenicity decreasing in recombinant sarcoplasmic calcium-binding protein from shrimp (Litopenaeus vannamei) with thermal processing via spectroscopy and molecular dynamics simulation techniques
inferred← citeshttps://doi.org/10.1016/j.foodres.2024.114063openalex-snapshot
Degree of hydrolysis is a poor predictor of the sensitizing capacity of whey- and casein-based hydrolysates in a Brown Norway rat model of cow’s milk allergy
inferred← citeshttps://doi.org/10.1016/j.foodres.2024.114466openalex-snapshot
Impact of pilot-scale microfluidization on soybean protein structure in powder and solution
inferred← citeshttps://doi.org/10.1016/j.ifset.2016.02.001openalex-snapshot
Effects of high hydrostatic pressure treatment on structural, allergenicity, and functional properties of proteins from ginkgo seeds
inferred← citeshttps://doi.org/10.1016/j.ifset.2016.04.003openalex-snapshot
Effects of combined high pressure and thermal treatment on the allergenic potential of peanut in a mouse model of allergy
inferred← citeshttps://doi.org/10.1016/j.ifset.2018.03.011openalex-snapshot
Investigation of conformation change of glycated ovalbumin obtained by Co-60 gamma-ray irradiation under drying treatment
inferred← citeshttps://doi.org/10.1016/j.ifset.2022.103199openalex-snapshot
Advances in legume protein extraction technologies: A review
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2023.126026openalex-snapshot
Comparison of proanthocyanidins A2 and B2 on IgE-reactivity and epitopes in Gly m 6 using multispectral, LC/MS-MS and molecular docking
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2024.129582openalex-snapshot
Insight into the allergenicity and structure changes of parvalbumin from Trachinotus ovatus induced by dense-phase carbon dioxide
inferred← citeshttps://doi.org/10.1016/j.lwt.2021.110862openalex-snapshot
Effects of fermentation with Bacillus natto on the allergenicity of peanut
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.pep.2016.12.002openalex-snapshot
Development of immunoaffinity chromatographic method for Ara h 2 isolation
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Studying on the IgG binding capacity and conformation of tropomyosin in Ovalipes punctatus meat irradiated with electron beam
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Effect of processing on conformational changes of food proteins related to allergenicity
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Principles and applications of spectroscopic techniques for evaluating food protein conformational changes: A review
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Eco-innovative technologies for extraction of proteins for human consumption from renewable protein sources of plant origin
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Research progress in peanut allergens and their allergenicity reduction
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inferred← citeshttps://doi.org/10.1021/acs.jafc.2c06359openalex-snapshot
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Structure-based modelling of hemocyanin allergenicity in squid and its response to high hydrostatic pressure
inferred← citeshttps://doi.org/10.1039/c6fo01365aopenalex-snapshot
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Is high pressure treatment able to modify the allergenicity of the largemouth bass allergens?
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Reducing peanut allergens by high pressure combined with polyphenol oxidase
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Effects of heat treatment on the antigenicity of four milk proteins in milk protein concentrates
inferred← citeshttps://doi.org/10.1080/09540105.2018.1529739openalex-snapshot
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Antiallergic activity of Lactobacillus plantarum against peanut allergy in a Balb/c mouse model
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Purification of antibody against Ara h 2 by a homemade immunoaffinity chromatography column
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inferred← citeshttps://doi.org/10.21608/ajas.2018.28370openalex-snapshot
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Untargeted metabolomic reveals changes in serum metabolism in peanut allergic mice treated by raw and roasted peanuts
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Scientific Opinion on the evaluation of allergenic foods and food ingredients for labelling purposes
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A novel IgE epitope-specific antibodies-based sandwich ELISA for sensitive measurement of immunoreactivity changes of peanut allergen Ara h 2 in processed foods
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Innovative Methods for Nuts Postharvest Processing and Preservation with Machine Learning–Based Quality Evaluation
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