References/Publications for Mass spectrometry (MS) of Ara h 6

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19538351 Clin Exp Allergy. 2009 Aug;39(8):1277-85. doi:
1111/j.1365-2222.2009.03294.x. Epub 2009 Jun 15.

Capacity of purified peanut allergens to induce degranulation in a functional in
vitro assay: Ara h 2 and Ara h 6 are the most efficient elicitors.

Blanc F(1), Adel-Patient K, Drumare MF, Paty E, Wal JM, Bernard H.

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22495983 Mol Nutr Food Res. 2012 Apr;56(4):548-57. doi: 10.1002/mnfr.201100614.

Trypsin resistance of the major peanut allergen Ara h 6 and allergenicity of the
digestion products are abolished after selective disruption of disulfide bonds.

Hazebrouck S(1), Guillon B, Drumare MF, Paty E, Wal JM, Bernard H.

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24145103 Biochim Biophys Acta. 2013 Dec;1834(12):2832-42. doi:
1016/j.bbapap.2013.10.004. Epub 2013 Oct 18.

Reduction and alkylation of peanut allergen isoforms Ara h 2 and Ara h 6;
characterization of intermediate- and end products.

Apostolovic D(1), Luykx D, Warmenhoven H, Verbart D, Stanic-Vucinic D, de Jong
GA, Velickovic TC, Koppelman SJ.

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27377129 Sci Rep. 2016 Jul 5;6:29249. doi: 10.1038/srep29249.

Conformational stability of digestion-resistant peptides of peanut conglutins
reveals the molecular basis of their allergenicity.

Apostolovic D(1), Stanic-Vucinic D(1), de Jongh HH(2), de Jong GA(3), Mihailovic
J(1), Radosavljevic J(1), Radibratovic M(4), Nordlee JA(5), Baumert JL(5),
Milcic M(1), Taylor SL(5), Garrido Clua N(2), Cirkovic Velickovic T(1),
Koppelman SJ(5).

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28634114 Food Chem Toxicol. 2017 Sep;107(Pt A):88-98. doi: 10.1016/j.fct.2017.06.029.
Epub 2017 Jun 17.

Peanut digestome: Identification of digestion resistant IgE binding peptides.

Di Stasio L(1), Picariello G(2), Mongiello M(2), Nocerino R(3), Berni Canani
R(3), Bavaro S(4), Monaci L(4), Ferranti P(5), Mamone G(6).

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32125467 Anal Bioanal Chem. 2020 May;412(12):2815-2827. doi:
1007/s00216-020-02508-9. Epub 2020 Mar 3.

A multiple reaction monitoring method for determining peanut (Arachis hypogea)
allergens in serum using quadrupole and time-of-flight mass spectrometry.

Hands CM(1), Sayers RL(1), Nitride C(1), Gethings LA(2), Mills ENC(3).

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33217527 Food Chem Toxicol. 2021 Jan;147:111866. doi: 10.1016/j.fct.2020.111866. Epub
2020 Nov 17.

Purification of soybean cupins and comparison of IgE binding with peanut
allergens in a population of allergic subjects.

Ramadan S(1), Marsh J(2), El-Sherbeny GA(1), El-Halawany EF(1), Luan F(3),
Baumert JL(2), Johnson P(2), Osman Y(1), Goodman RE(4).

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35769555 Front Allergy. 2022 May 24;3:872714. doi: 10.3389/falgy.2022.872714.
eCollection 2022.

Determination of Allergen Levels, Isoforms, and Their Hydroxyproline
Modifications Among Peanut Genotypes by Mass Spectrometry.

Marsh JT(1), Palmer LK(1), Koppelman SJ(1), Johnson PE(1).

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36553735 Foods. 2022 Dec 9;11(24):3993. doi: 10.3390/foods11243993.

Proteomic Profiling of Major Peanut Allergens and Their Post-Translational
Modifications Affected by Roasting.

Đukić T(1), Smiljanić K(1), Mihailović J(1), Prodić I(2), Apostolović D(3), Liu
SH(4), Epstein MM(4), van Hage M(3), Stanić-Vučinić D(1), Ćirković Veličković
T(1)(5)(6)(7).

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37028524 J Allergy Clin Immunol. 2023 Apr 5:S0091-6749(23)00426-8. doi:
1016/j.jaci.2023.03.025. Online ahead of print.

IgE cross-inhibition between Ara h 1 and Ara h 2 is explained by complex
formation of both major peanut allergens.

Warmenhoven HJM(1), Hulsbos L(2), Dreskin SC(3), Akkerdaas JH(4), Versteeg
SA(4), van Ree R(5).

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37256970 J Agric Food Chem. 2023 Jun 14;71(23):9110-9119. doi:
1021/acs.jafc.3c01482. Epub 2023 May 31.

IgE Recognition and Structural Analysis of Disulfide Bond Rearrangement and
Chemical Modifications in Allergen Aggregations in Roasted Peanuts.

Zhang Y(1)(2), Song M(1)(2), Xu J(1)(2), Li X(1)(2), Yang A(1)(3), Tong P(1)(2),
Wu Z(1)(3), Chen H(1)(3).

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