References/Publications for Western/Immunoblot of Ara h 1

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1880317 J Allergy Clin Immunol. 1991 Aug;88(2):172-9.

Identification of a major peanut allergen, Ara h I, in patients with atopic
dermatitis and positive peanut challenges.

Burks AW(1), Williams LW, Helm RM, Connaughton C, Cockrell G, O'Brien T.


7560062 J Clin Invest. 1995 Oct;96(4):1715-21.

Recombinant peanut allergen Ara h I expression and IgE binding in patients with
peanut hypersensitivity.

Burks AW(1), Cockrell G, Stanley JS, Helm RM, Bannon GA.


9151961 Eur J Biochem. 1997 Apr 15;245(2):334-9.

Mapping and mutational analysis of the IgE-binding epitopes on Ara h 1, a legume
vicilin protein and a major allergen in peanut hypersensitivity.

Burks AW(1), Shin D, Cockrell G, Stanley JS, Helm RM, Bannon GA.


9130498 Int Arch Allergy Immunol. 1997 May-Jul;113(1-3):118-21.

Characterization of Ara h 1 by two-dimensional electrophoresis immunoblot and
recombinant techniques: new digestion experiments with peanuts imitating the
gastrointestinal tract.

Becker WM(1).


9677140 Clin Exp Allergy. 1998 Jun;28(6):743-51.

Identification and partial characterization of multiple major allergens in peanut
proteins.

de Jong EC(1), Van Zijverden M, Spanhaak S, Koppelman SJ, Pellegrom H, Penninks
AH.


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.


10820263 J Immunol. 2000 Jun 1;164(11):5844-9.

Structure of the major peanut allergen Ara h 1 may protect IgE-binding epitopes
from degradation.

Maleki SJ(1), Kopper RA, Shin DS, Park CW, Compadre CM, Sampson H, Burks AW,
Bannon GA.


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.


12589366 J Allergy Clin Immunol. 2003 Feb;111(2):420-4.

Patients with anaphylaxis to pea can have peanut allergy caused by cross-reactive
IgE to vicilin (Ara h 1).

Wensing M(1), Knulst AC, Piersma S, O'Kane F, Knol EF, Koppelman SJ.


12956750 Clin Exp Allergy. 2003 Sep;33(9):1273-80.

Immunological analysis of allergenic cross-reactivity between peanut and tree
nuts.

de Leon MP(1), Glaspole IN, Drew AC, Rolland JM, O'Hehir RE, Suphioglu C.


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.


15264933 J Agric Food Chem. 2004 Jul 28;52(15):4903-7.

The major peanut allergen Ara h 1 and its cleaved-off N-terminal peptide;
possible implications for peanut allergen detection.

Wichers HJ(1), De Beijer T, Savelkoul HF, Van Amerongen A.


15714473 Proteomics. 2005 Feb;5(3):675-86.

Analysis of the composition of an immunoglobulin E reactive high molecular weight
protein complex of peanut extract containing Ara h 1 and Ara h 3/4.

Boldt A(1), Fortunato D, Conti A, Petersen A, Ballmer-Weber B, Lepp U, Reese G,
Becker WM.


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.


15969668 Clin Exp Allergy. 2005 Jun;35(6):767-73.

The promiscuity of immunoglobulin E binding to peanut allergens, as determined by
Western blotting, correlates with the severity of clinical symptoms.

Lewis SA(1), Grimshaw KE, Warner JO, Hourihane JO.


21132984 J Food Prot. 2005 Aug;68(8):1712-9.

Effects of twin-screw extrusion of peanut flour on in vitro digestion of
potentially allergenic peanut proteins.

Chen L(1), Phillips RD.


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.


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.


18298062 J Agric Food Chem. 2008 Mar 26;56(6):2223-30. doi: 10.1021/jf072907n. Epub 2008
Feb 26.

Determination of pepsin-susceptible and pepsin-resistant epitopes in native and
heat-treated peanut allergen Ara h 1.

van Boxtel EL(1), Koppelman SJ, van den Broek LA, Gruppen H.


18338408 Mol Nutr Food Res. 2008 Jun;52(6):674-82. doi: 10.1002/mnfr.200700299.

Legumin allergens from peanuts and soybeans: effects of denaturation and
aggregation on allergenicity.

van Boxtel EL(1), van den Broek LA, Koppelman SJ, Gruppen H.


18727014 Mol Nutr Food Res. 2008 Nov;52 Suppl 2:S272-85. doi: 10.1002/mnfr.200700524.

Purification and characterisation of a panel of peanut allergens suitable for use
in allergy diagnosis.

Marsh J(1), Rigby N, Wellner K, Reese G, Knulst A, Akkerdaas J, van Ree R,
Radauer C, Lovegrove A, Sancho A, Mills C, Vieths S, Hoffmann-Sommergruber K,
Shewry PR.


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.


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, Nørgaard JV, Maleki SJ, van Hengel AJ.


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.


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.


20412153 Allergy. 2010 Nov;65(11):1485-6. doi: 10.1111/j.1398-9995.2010.02371.x.

Clinical reactivity to raw peanut correlates with IgE binding to conformational
epitopes of Ara h 1: a case report.

Ditto AM(1), Neilsen CV, Neerukonda S, Shreffler WG, Bryce PJ.


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.


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.


21917921 J Biol Chem. 2011 Nov 11;286(45):39318-27. doi: 10.1074/jbc.M111.270132. Epub
2011 Sep 14.

Structural and immunologic characterization of Ara h 1, a major peanut allergen.

Chruszcz M(1), Maleki SJ, Majorek KA, Demas M, Bublin M, Solberg R, Hurlburt BK,
Ruan S, Mattison CP, Breiteneder H, Minor W.


22998620 J Agric Food Chem. 2012 Oct 17;60(41):10352-8. doi: 10.1021/jf302800e. Epub 2012
Oct 9.

Purification and characterization of Ara h1 and Ara h3 from four peanut market
types revealed higher order oligomeric structures.

Yusnawan E(1), Marquis CP, Lee NA.


22996799 Mol Nutr Food Res. 2012 Nov;56(11):1739-47. doi: 10.1002/mnfr.201100815. Epub
2012 Sep 20.

Ara h 1 structure is retained after roasting and is important for enhanced
binding to IgE.

Nesbit JB(1), Hurlburt BK, Schein CH, Cheng H, Wei H, Maleki SJ.


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.


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.


25036339 Prep Biochem Biotechnol. 2015;45(5):438-46. doi: 10.1080/10826068.2014.940972.

Purification and recombinant expression of major peanut allergen Ara h 1.

Wu Z(1), Yan F, Wei X, Li X, Tong P, Yang A, Tang R, Chen H.


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).


28234343 Foods. 2014 Dec 18;3(4):642-657. doi: 10.3390/foods3040642.

Purification of Recombinant Peanut Allergen Ara h 1 and Comparison of IgE Binding
to the Natural Protein.

Hurlburt BK(1), McBride JK(2), Nesbit JB(3), Ruan S(4), Maleki SJ(5).


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).


29803434
Food Res Int. 2018 Jul;109:126-137. doi: 10.1016/j.foodres.2018.04.021. Epub 2018
Apr 17.

Effect of thermal/pressure processing and simulated human digestion on the
immunoreactivity of extractable peanut allergens.

Bavaro SL(1), Di Stasio L(2), Mamone G(3), De Angelis E(1), Nocerino R(4), Canani
RB(4), Logrieco AF(1), Montemurro N(1), Monaci L(5).


30258615 Food Sci Nutr. 2018 Jul 27;6(6):1706-1714. doi: 10.1002/fsn3.742. eCollection
2018 Sep.

Effects of different thermal processing methods on the structure and
allergenicity of peanut allergen Ara h 1.

Tian Y(1)(2), Rao H(1)(2), Zhang K(1)(2), Tao S(3), Xue WT(1)(2).


--DOI:10.1016/j.ifset.2019.02.001
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).


33096617 Foods. 2020 Oct 21;9(10). pii: E1508. doi: 10.3390/foods9101508.

Crosslinked Recombinant-Ara h 1 Catalyzed by Microbial Transglutaminase:
Preparation, Structural Characterization and Allergic Assessment.

Tian Y(1)(2), Liu C(3), Xue W(3), Wang Z(1)(2).


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).


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).


33980880 Sci Rep. 2021 May 12;11(1):10141. doi: 10.1038/s41598-021-89402-1.

Human monocyte-derived type 1 and 2 macrophages recognize Ara h 1, a major peanut
allergen, by different mechanisms.

Krause M(1), Crauwels P(2)(3), Blanco-Pérez F(1), Globisch M(4), Wangorsch A(1),
Henle T(4), Lidholm J(5), van Zandbergen G(2)(6)(7), Vieths S(1), Scheurer S(1),
Toda M(8)(9).


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).