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Table 5 List of most relevant peer-reviewed papers from the ImpARAS network

From: COST Action ‘ImpARAS’: what have we learnt to improve food allergy risk assessment. A summary of a 4 year networking consortium

No

Title

Reference (DOI)

1

Current (food) allergenic risk assessment: is it fit for novel foods? status quo and identification of gaps

Mazzucchelli (2018)

(https://doi.org/10.1002/mnfr.201700278)

2

Application of the Adverse Outcome Pathway (AOP) concept to structure the available in vivo and in vitro mechanistic data for allergic sensitisation to food proteins

Van Bilsen (2017)

(https://doi.org/10.1186/s13601-017-0152-0)

3

Current challenges facing the assessment of the allergenic capacity of food allergens in animal models.

Bøgh (2016)

https://doi.org/10.1186/s13601-016-0110-2

4

Allergenicity risk assessment of new or modified dietary proteins: a critical review of current strategies.

Remington (2018)

https://doi.org/10.1016/j.fct.2017.12.025

5

Experimental food allergy models to study the role of innate immune cells as initiators of allergen specific Th2 immune responses

Hussain (2015)

https://doi.org/10.1016/j.ddmod.2016.08.001

6

The use of animal models to discover immunological mechanisms underpinning sensitization to food allergens

Smit (2015)

https://doi.org/10.1016/j.ddmod.2016.09.001

7

A review of animal models used to evaluate potential allergenicity of genetically modified organisms (GMOs)

Marsteller (2015)

https://doi.org/10.1016/j.ddmod.2016.11.001

8

In silico tools for exploring potential human allergy to proteins.

Hayes (2015)

https://doi.org/10.1016/j.ddmod.2016.06.001

9

Non-IgE mediated food allergy

Lozano-Ojalvo (2015)

https://doi.org/10.1016/j.ddmod.2016.09.003

10

Applicability of epithelial models in protein permeability/transport studies and food allergy

Cubells-Baeza (2015)

https://doi.org/10.1016/j.ddmod.2016.08.002

11

Epithelial models to study food allergen induced barrier disruption and immune activation

Gavrovic-Jankulovic (2015)

https://doi.org/10.1016/j.ddmod.2016.09.002

12

IgE—the main player of food allergy

Broekman (2015)

https://doi.org/10.1016/j.ddmod.2016.07.001

13

Influence of microbiome and diet on immune responses in food allergy models

Barcik (2015)

https://doi.org/10.1016/j.ddmod.2016.06.003

14

Static and dynamic in vitro digestion models to study proteins stability in the gastrointestinal tract

Dupont (2015)

https://doi.org/10.1016/j.ddmod.2016.06.002

15

Kiwifruit cysteine protease actinidin compromises the intestinal barrier by disrupting tight junctions

Grozdanovic (2016)

https://doi.org/10.1016/j.bbagen.2015.12.005

16

Glycation of the major milk allergen β‐lactoglobulin changes its allergenicity by alterations in cellular uptake and degradation

Perusko (2018)

https://doi.org/10.1002/mnfr.201800341

17

Proteomics in food: quality, safety, microbes and allergens.

Piras (2016)

https://doi.org/10.1002/pmic.201500369

18

Allergenic and novel food proteins: state of the art and challenges in the allergenicity assessment

Pali-Schöl (2018)

https://doi.org/10.1016/j.tifs.2018.03.007

19

Cross-reactivity in fish allergy: a double-blind, placebo-controlled food-challenge trial

Sørensen (2017)

https://doi.org/10.1016/j.jaci.2017.03.043

20

Important plant food allergens (part I): what is shaping their allergenic potency—physicochemical properties and beyond

Costa, In Prep

21

Important animal food allergens (part II): what is shaping their allergenic potency—physicochemical properties and beyond

Costa, In prep

22

The relevance of a digestibility evaluation in the allergenicity risk assessment of novel proteins. Opinion of a joined initiative of COST Action ImpARAS and COST Action INFOGEST

Verhoeckx (2019)

https://doi.org/10.1016/j.fct.2019.04.052

23

Applying the adverse outcome pathway (AOP) for food sensitization to support in vitro testing strategies

Lozano-Ojalvo (2019)

https://doi.org/10.1016/j.tifs.2019.01.014

24

Overview of in vivo and ex vivo endpoints in murine food allergy models: suitable for evaluation of the sensitizing capacity of novel proteins?

Castan (2020)

https://doi.org/10.1111/all.13943

25

Defining the targets for the assessment of IgE-mediated allergenicity of new or modified food proteins

Houben (2019)

https://doi.org/10.1016/j.fct.2019.02.036

26

Jug r 6 is the allergenic vicilin present in walnut responsible for IgE cross-reactivities to other tree nuts and seeds

Dubiela (2018)

https://doi.org/10.1038/s41598-018-29656-4

27

Fish-allergic patients tolerate ray based on the low allergenicity of its parvalbumin

Kalic (2018)

https://doi.org/10.1016/j.jaip.2018.11.011

28

Homologous tropomyosins from vertebrate and invertebrate: recombinant calibrator proteins in functional biological assays for allergenicity assessment of novel animal foods

Klueber (2020)

https://doi.org/10.1111/cea.13503

29

Hypothesis paper/concept introduction: is it possible to establish a generic threshold of exposure for allergic sensitization to food proteins

Bernard Madsen, In prep