On the public citation graph
Heat-Induced Changes in Epitopes and Ige Binding Capacity of Soybean Proteins
0 signed · 33 inferred · view as graph
Inferred edges come from two machine sources: sweeps of open repository metadata (mostly SSRN and Zenodo), and a bulk OpenAlex citation snapshot. Every row below is labelled with the one it came from. Neither is a complete citation index — absence here is not evidence of absence.
Is this your work? Sign in with ORCID and put your name on the
claims that are yours.
Reference health. See whether every reference in this work resolves to a
known work and none has been retracted — and get a dated CiteStamped
badge you can embed.
What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1002/biot.201600441openalex-extracted
Combination of two epitope identification techniques enables the rational design of soy allergen Gly m 4 mutants
inferredcites →https://doi.org/10.1002/jsfa.9969openalex-extracted
Allergenicity reduction and rheology property of Lactobacillus‐fermented soymilk
inferredcites →https://doi.org/10.1007/s00425-004-1313-7openalex-extracted
C-Terminal 23�kDa polypeptide of soybean Gly�m�Bd 28�K is a potential allergen
inferredcites →https://doi.org/10.1016/j.cell.2020.12.007openalex-extracted
Food allergy as a biological food quality control system
inferredcites →https://doi.org/10.1016/j.fct.2013.02.014openalex-extracted
Prediction and characterization of the linear IgE epitopes for the major soybean allergen β-conglycinin using immunoinformatics tools
inferredcites →https://doi.org/10.1016/j.foodchem.2011.08.084openalex-extracted
Effect of heat treatment on the potential allergenicity and conformational structure of egg allergen ovotransferrin
inferredcites →https://doi.org/10.1016/j.foodchem.2012.09.091openalex-extracted
A potential practical approach to reduce Ara h 6 allergenicity by gamma irradiation
inferredcites →https://doi.org/10.1016/j.foodchem.2016.02.004openalex-extracted
Influence of heat treatment on the structure and core IgE-binding epitopes of rAra h 2.02
inferredcites →https://doi.org/10.1016/j.foodchem.2016.06.036openalex-extracted
Thermal processing effects on peanut allergen Ara h 2 allergenicity in mice and its antigenic epitope structure
inferredcites →https://doi.org/10.1016/j.foodchem.2017.10.132openalex-extracted
Thermal processing effects on the IgE-reactivity of cashew and pistachio
inferredcites →https://doi.org/10.1016/j.foodchem.2018.12.070openalex-extracted
Allergenicity assessment on thermally processed peanut influenced by extraction and assessment methods
inferredcites →https://doi.org/10.1016/j.foodchem.2020.128461openalex-extracted
Effect of heat, enzymatic hydrolysis and acid-alkali treatment on the allergenicity of silkworm pupa protein extract
inferredcites →https://doi.org/10.1016/j.foodchem.2021.130569openalex-extracted
Characterization of the protein structure of soymilk fermented by Lactobacillus and evaluation of its potential allergenicity based on the sensitized-cell model
inferredcites →https://doi.org/10.1016/j.foodchem.2022.132567openalex-extracted
Major shrimp allergen peptidomics signatures and potential biomarkers of heat processing
inferredcites →https://doi.org/10.1016/j.foodchem.2022.133031openalex-extracted
Effects of heat treatment and pH on the physicochemical and emulsifying properties of coconut (Cocos nucifera L.) globulins
inferredcites →https://doi.org/10.1016/j.foodres.2020.109199openalex-extracted
Location of destroyed antigenic sites of Gly m Bd 60 K after three processing technologies
inferredcites →https://doi.org/10.1016/j.idairyj.2018.10.004openalex-extracted
Thermal denaturation of bovine β-lactoglobulin in different protein mixtures in relation to antigenicity
inferredcites →https://doi.org/10.1016/j.jff.2019.103490openalex-extracted
Function, digestibility and allergenicity assessment of ovalbumin–EGCG conjugates
inferredcites →https://doi.org/10.1016/j.lwt.2020.110131openalex-extracted
Identification of an IgE epitope of soybean allergen Gly m Bd 60K
inferredcites →https://doi.org/10.1016/j.lwt.2021.110862openalex-extracted
Effects of fermentation with Bacillus natto on the allergenicity of peanut
inferredcites →https://doi.org/10.1016/j.lwt.2021.112678openalex-extracted
Effects of thermal sterilization on the allergenicity of soybeans
inferredcites →https://doi.org/10.1016/j.procbio.2011.11.005openalex-extracted
Development of a competitive ELISA for the detection of soybean α subunit of β-conglycinin
inferredcites →https://doi.org/10.1016/j.tifs.2018.01.007openalex-extracted
Effects of nonthermal food processing technologies on food allergens: A review of recent research advances
inferredcites →https://doi.org/10.1016/j.tifs.2021.10.006openalex-extracted
Effect of processing on soybean allergens and their allergenicity
inferredcites →https://doi.org/10.1021/acs.jafc.9b05140openalex-extracted
Simulations of Temperature and Pressure Unfolding in Soy Allergen Gly m 4 Using Molecular Modeling
inferredcites →https://doi.org/10.1021/jf001186oopenalex-extracted
Association of End-Product Adducts with Increased IgE Binding of Roasted Peanuts
inferredcites →https://doi.org/10.1080/09168451.2018.1456319openalex-extracted
Worm wounding increases levels of pollen-related food allergens in soybean (Glycine max)
inferredcites →https://doi.org/10.1080/10408398.2011.613534openalex-extracted
Advances of Research on Glycinin and β-Conglycinin: A Review of Two Major Soybean Allergenic Proteins
inferredcites →https://doi.org/10.1080/10408398.2015.1045965openalex-extracted
Review of conventional and novel food processing methods on food allergens
inferredcites →https://doi.org/10.1080/10408398.2021.1904822openalex-extracted
Food irradiation: a promising technology to produce hypoallergenic food with high quality
inferredcites →https://doi.org/10.1080/10408398.2021.1913093openalex-extracted
Recent advances in alleviating food allergenicity through fermentation
inferredcites →https://doi.org/10.3168/jds.2019-17739openalex-extracted
Characterization of the milk fat globule membrane proteome in colostrum and mature milk of Xinong Saanen goats
inferredcites →https://doi.org/10.3390/foods11030479openalex-extracted
Characterization of the Reduced IgE Binding Capacity in Boiled and Autoclaved Soybeans through Proteomic Approaches
Editorial review for independent work. ICSAC — the Institute for Complexity
Science and Advanced Computing — runs a structured editorial panel for researchers
publishing outside journals, and publishes on CiteStamp rails. Submission is free
and goes through ORCID: icsacinstitute.org/submit.