Select | PubMed ID | Description |
| 1460200 | J Allergy Clin Immunol. 1992 Dec;90(6 Pt 1):962-9.
Identification and characterization of a second major peanut allergen, Ara h II, with use of the sera of patients with atopic dermatitis and positive peanut challenge.
Burks AW(1), Williams LW, Connaughton C, Cockrell G, O'Brien TJ, Helm RM.
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| 9186485 | Arch Biochem Biophys. 1997 Jun 15;342(2):244-53.
Identification and mutational analysis of the immunodominant IgE binding epitopes of the major peanut allergen Ara h 2.
Stanley JS(1), King N, Burks AW, Huang SK, Sampson H, Cockrell G, Helm RM, West CM, Bannon GA.
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| 10474031 | Int Arch Allergy Immunol. 1999 Aug;119(4):265-74.
Selective cloning of peanut allergens, including profilin and 2S albumins, by phage display technology.
Kleber-Janke T(1), Crameri R, Appenzeller U, Schlaak M, Becker WM.
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| 11398088 | J Allergy Clin Immunol. 2001 Jun;107(6):1077-81.
Effects of cooking methods on peanut allergenicity.
Beyer K(1), Morrow E, Li XM, Bardina L, Bannon GA, Burks AW, Sampson HA.
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| 12097392 | J Immunol. 2002 Jul 15;169(2):882-7.
Protein structure plays a critical role in peanut allergen stability and may determine immunodominant IgE-binding epitopes.
Sen M(1), Kopper R, Pons L, Abraham EC, Burks AW, Bannon GA.
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| 15080811 | Clin Exp Allergy. 2004 Apr;34(4):583-90.
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.
Koppelman SJ(1), Wensing M, Ertmann M, Knulst AC, Knol EF.
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| 15237964 | J Agric Food Chem. 2004 Jul 14;52(14):4541-5.
Allergenic properties of roasted peanut allergens may be reduced by peroxidase.
Chung SY(1), Maleki SJ, Champagne ET.
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| 15836759 | Clin Exp Allergy. 2005 Apr;35(4):490-7.
Purification and immunoglobulin E-binding properties of peanut allergen Ara h 6: evidence for cross-reactivity with Ara h 2.
Koppelman SJ(1), de Jong GA, Laaper-Ertmann M, Peeters KA, Knulst AC, Hefle SL, Knol EF.
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| 15893698 | Clin Immunol. 2005 Jun;115(3):302-12.
Comparative potency of Ara h 1 and Ara h 2 in immunochemical and functional assays of allergenicity.
Palmer GW(1), Dibbern DA Jr, Burks AW, Bannon GA, Bock SA, Porterfield HS, McDermott RA, Dreskin SC.
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| 16189800 | Mol Nutr Food Res. 2005 Oct;49(10):963-71.
Allergenic characteristics of a modified peanut allergen.
King N(1), Helm R, Stanley JS, Vieths S, Lüttkopf D, Hatahet L, Sampson H, Pons L, Burks W, Bannon GA.
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| 16580071 | Mol Immunol. 2007 Jan;44(4):463-71. Epub 2006 Mar 31.
IgE cross-reactivity between the major peanut allergen Ara h 2 and tree nut allergens.
de Leon MP(1), Drew AC, Glaspole IN, Suphioglu C, O'Hehir RE, Rolland JM.
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| 17210048 | Clin Exp Allergy. 2007 Jan;37(1):108-15.
Does skin prick test reactivity to purified allergens correlate with clinical severity of peanut allergy?
Peeters KA(1), Koppelman SJ, van Hoffen E, van der Tas CW, den Hartog Jager CF, Penninks AH, Hefle SL, Bruijnzeel-Koomen CA, Knol EF, Knulst AC.
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| 17651153 | Clin Exp Allergy. 2007 Aug;37(8):1221-8.
Children with peanut allergy recognize predominantly Ara h2 and Ara h6, which remains stable over time.
Flinterman AE(1), van Hoffen E, den Hartog Jager CF, Koppelman S, Pasmans SG, Hoekstra MO, Bruijnzeel-Koomen CA, Knulst AC, Knol EF.
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| 18680451 | Protein Pept Lett. 2008;15(6):567-77.
Proteomic analysis of peanut seed storage proteins and genetic variation in a potential peanut allergen.
Guo B(1), Liang X, Chung SY, Holbrook CC, Maleki SJ.
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| 19007236 | J Agric Food Chem. 2008 Dec 10;56(23):11225-33. doi: 10.1021/jf802600r.
Reduction of IgE binding and nonpromotion of Aspergillus flavus fungal growth by simultaneously silencing Ara h 2 and Ara h 6 in peanut.
Chu Y(1), Faustinelli P, Ramos ML, Hajduch M, Stevenson S, Thelen JJ, Maleki SJ, Cheng H, Ozias-Akins P.
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| 19223023 | J Proteomics. 2009 Apr 13;72(3):511-26. doi: 10.1016/j.jprot.2009.02.002. Epub 2009 Feb 15.
Resolution and identification of major peanut allergens using a combination of fluorescence two-dimensional differential gel electrophoresis, Western blotting and Q-TOF mass spectrometry.
Chassaigne H(1), Trégoat V, Nřrgaard JV, Maleki SJ, van Hengel AJ.
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| 19609960 | Proteomics. 2009 Jul;9(13):3507-21. doi: 10.1002/pmic.200800938.
2-D DIGE analysis of the proteome of extracts from peanut variants reveals striking differences in major allergen contents.
Schmidt H(1), Gelhaus C, Latendorf T, Nebendahl M, Petersen A, Krause S, Leippe M, Becker WM, Janssen O.
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| 19639724 | J Investig Allergol Clin Immunol. 2009;19(4):283-91.
Immunoglobulin E cross-reactivity between lupine conglutins and peanut allergens in serum of lupine-allergic individuals.
Dooper MM(1), Plassen C, Holden L, Lindvik H, Faeste CK.
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| 21130383 | Ann Allergy Asthma Immunol. 2010 Dec;105(6):451-7. doi: 1016/j.anai.2010.09.025.
Differences among heat-treated, raw, and commercial peanut extracts by skin testing and immunoblotting.
Maleki SJ(1), Casillas AM, Kaza U, Wilson BA, Nesbit JB, Reimoneqnue C, Cheng H, Bahna SL.
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| 21883278 | Allergy. 2011 Dec;66(12):1522-9. doi: 10.1111/j.1398-9995.2011.02692.x. Epub 2011 Aug 23.
Computationally predicted IgE epitopes of walnut allergens contribute to cross-reactivity with peanuts.
Maleki SJ(1), Teuber SS, Cheng H, Chen D, Comstock SS, Ruan S, Schein CH.
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| 21912172 | Int Arch Allergy Immunol. 2012;157(1):41-50. doi: 10.1159/000324681. Epub 2011 Sep 6.
Influence of enzymatic hydrolysis on the allergenicity of roasted peanut protein extract.
Cabanillas B(1), Pedrosa MM, Rodríguez J, Muzquiz M, Maleki SJ, Cuadrado C, Burbano C, Crespo JF.
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| 23181796 | Clin Exp Allergy. 2012 Dec;42(12):1801-12. doi: 10.1111/cea.12031.
An unfolded variant of the major peanut allergen Ara h 2 with decreased anaphylactic potential.
Starkl P(1), Felix F, Krishnamurthy D, Stremnitzer C, Roth-Walter F, Prickett SR, Voskamp AL, Willensdorfer A, Szalai K, Weichselbaumer M, O'Hehir RE, Jensen-Jarolim E.
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| 23921317 | Int Arch Allergy Immunol. 2013;162(2):123-30. doi: 10.1159/000351920. Epub 2013 Jul 31.
Allergenic properties of enzymatically hydrolyzed peanut flour extracts.
Shi X(1), Guo R, White BL, Yancey A, Sanders TH, Davis JP, Burks AW, Kulis M.
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| 24266677 | Allergy. 2013 Dec;68(12):1546-54. doi: 10.1111/all.12261. Epub 2013 Nov 23.
Identification of Maillard reaction products on peanut allergens that influence binding to the receptor for advanced glycation end products.
Mueller GA(1), Maleki SJ, Johnson K, Hurlburt BK, Cheng H, Ruan S, Nesbit JB, Pomés A, Edwards LL, Schorzman A, Deterding LJ, Park H, Tomer KB, London RE, Williams JG.
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| 23889250 | Clin Exp Allergy. 2013 Aug;43(8):967-74. doi: 10.1111/cea.12136.
IgE binding to peanut components by four different techniques: Ara h 2 is the most relevant in peanut allergic children and adults.
Klemans RJ(1), Liu X, Knulst AC, Knol MJ, Gmelig-Meyling F, Borst E, Pasmans SG, Knol EF.
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| 25483599 | J Allergy Clin Immunol. 2015 May;135(5):1267-74.e1-8. doi: 1016/j.jaci.2014.10.025. Epub 2014 Dec 4.
Allergenicity of peanut component Ara h 2: Contribution of conformational versus linear hydroxyproline-containing epitopes.
Bernard H(1), Guillon B(1), Drumare MF(1), Paty E(2), Dreskin SC(3), Wal JM(1), Adel-Patient K(1), Hazebrouck S(4).
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| 26411458 | Appl Microbiol Biotechnol. 2016 Jan;100(2):661-71. doi: 1007/s00253-015-6953-y. Epub 2015 Sep 28.
Expression of a codon-optimised recombinant Ara h 2.02 peanut allergen in Escherichia coli.
Lew MH(1), Lim RL(2).
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| 26842773 | Pediatr Allergy Immunol. 2016 Jun;27(4):348-55. doi: 10.1111/pai.12533.
Prospective investigation on the transfer of Ara h 2, the most potent peanut allergen, in human breast milk.
Schocker F(1), Baumert J(2), Kull S(1), Petersen A(1), Becker WM(1), Jappe U(1)(3).
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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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| 27979211 | Food Chem. 2017 Apr 15;221:335-344. doi: 10.1016/j.foodchem.2016.10.063. Epub 2016 Oct 14.
Peanut protein extraction conditions strongly influence yield of allergens Ara h 1 and 2 and sensitivity of immunoassays.
Walczyk NE(1), Smith PMC(2), Tovey ER(3), Roberts TH(4).
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| 28441989 | Allergy Asthma Proc. 2017 May 1;38(3):192-196. doi: 10.2500/aap.2017.38.4049.
Ara h2 levels in dust from homes of individuals with peanut allergy and individuals with peanut tolerance.
Shroba J, Barnes C, Nanda M, Dinakar C, Ciaccio C.
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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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| 28638052 | Sci Rep. 2017 Jun 21;7(1):3981. doi: 10.1038/s41598-017-04268-6.
Determination of Crucial Immunogenic Epitopes in Major Peanut Allergy Protein, Ara h2, via Novel Nanoallergen Platform.
Deak PE(1), Vrabel MR(1), Kiziltepe T(1)(2), Bilgicer B(3)(4)(5).
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| 29188033 | Food Sci Nutr. 2017 Jul 25;5(6):1065-1071. doi: 10.1002/fsn3.491. eCollection 2017 Nov.
Simple methods to reduce major allergens Ara h 1 and Ana o 1/2 in peanut and cashew extracts.
Chung SY(1), Mattison CP(1), Grimm CC(1), Reed S(1).
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| 29542223 | Clin Exp Allergy. 2018 Jul;48(7):890-897. doi: 10.1111/cea.13134. Epub 2018 Apr
2S protein Ara h 7.0201 has unique epitopes compared to other Ara h 7 isoforms and is comparable to 2S proteins Ara h 2 and 6 in basophil degranulation capacity.
Hayen SM(1)(2), Ehlers AM(1)(2), den Hartog Jager CF(1), Garssen J(3)(4), Knol EF(1)(2), Knulst AC(1)(2), Suer W(5), Willemsen LEM(3), Otten HG(2).
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| 30744860 | Food Chem. 2019 Jun 30;284:287-295. doi: 10.1016/j.foodchem.2019.01.081. Epub 2019 Jan 18.
Binding of peanut allergen Ara h 2 with Vaccinium fruit polyphenols.
Plundrich NJ(1), Cook BT(2), Maleki SJ(3), Fourches D(2), Lila MA(4).
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| 31758869 | J Appl Microbiol. 2020 Mar;128(3):862-874. doi: 10.1111/jam.14524. Epub 2019 Dec
Lactococcus lactis harbouring Ara h 2.02 alleviates allergen-specific Th2-associated responses in sensitized mice.
Chan CJ(1), Yong YS(1), Song AAL(2), Abdul Rahim R(3), In LLA(1), Lim RLH(1).
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| 33046788 | Sci Rep. 2020 Oct 12;10(1):17038. doi: 10.1038/s41598-020-72636-w.
Impact of cold plasma processing on major peanut allergens.
Venkataratnam H(1), Cahill O(2), Sarangapani C(2), Cullen PJ(2)(3)(4), Barry-Ryan C(2).
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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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| 33854954 | Toxicol Rep. 2021 Mar 31;8:767-773. doi: 10.1016/j.toxrep.2021.03.027. eCollection 2021.
Ranking of 10 legumes according to the prevalence of sensitization as a parameter to characterize allergenic proteins.
Smits M(1)(2)(3), Verhoeckx K(1)(2), Knulst A(1)(2), Welsing P(1)(4), de Jong A(5)(6), Houben G(1)(2)(3), Le TM(1)(2).
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| 34118511 | Food Chem. 2021 Nov 15;362:129879. doi: 10.1016/j.foodchem.2021.129879. Epub 2021 Apr 20.
The impact of a baked muffin matrix on the bioaccessibility and IgE reactivity of egg and peanut allergens.
Mattar H(1), Padfield P(1), Simpson A(2), Mills ENC(3).
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| 35000380 | J Agric Food Chem. 2022 Jan 19;70(2):626-633. doi: 10.1021/acs.jafc.1c06828. Epub 2022 Jan 8.
Effect of Processing on the Structure and Allergenicity of Peanut Allergen Ara h 2 Roasted in a Matrix.
Chang X(1)(2), Zhou X(1)(2), Tang Y(1)(2), Zhang Y(1)(2), Yuan J(1)(3), Li X(1)(2), Yang A(1)(4), Tong P(1)(2), Wu Z(1)(4), Chen H(1)(4).
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