메뉴 건너뛰기




Volumn 7, Issue , 2016, Pages 191-220

Food Allergy

Author keywords

Allergy; Epitope; Food; Processing; Protein

Indexed keywords

ALLERGENS; ALLERGIES; EPITOPES; FOOD PROCESSING; FOOD PRODUCTS; PROCESSING; PROTEINS;

EID: 84959934393     PISSN: 19411413     EISSN: 19411421     Source Type: Journal    
DOI: 10.1146/annurev-food-041715-033308     Document Type: Article
Times cited : (82)

References (184)
  • 1
    • 0033836431 scopus 로고    scopus 로고
    • Structural biology of allergens
    • Aalberse RC. 2000. Structural biology of allergens. J. Allergy Clin. Immunol. 106:228-38
    • (2000) J. Allergy Clin. Immunol. , vol.106 , pp. 228-238
    • Aalberse, R.C.1
  • 2
    • 84878401698 scopus 로고    scopus 로고
    • Thermal processing, salt and high pressure treatment effects on molecular structure and antigenicity of sesame protein isolate
    • Achouri A, Boye JI. 2013. Thermal processing, salt and high pressure treatment effects on molecular structure and antigenicity of sesame protein isolate. Food Res. Int. 53:240-51
    • (2013) Food Res. Int. , vol.53 , pp. 240-251
    • Achouri, A.1    Boye, J.I.2
  • 5
    • 84910649365 scopus 로고    scopus 로고
    • Precautionary labelling of foods for allergen content: Are we ready for a global framework?
    • Allen KJ, Turner PJ, Pawankar R, Taylor S, Sicherer S, et al. 2014b. Precautionary labelling of foods for allergen content: Are we ready for a global framework? World Allergy Organ. J. 7:10
    • (2014) World Allergy Organ J. , vol.7 , pp. 10
    • Allen, K.J.1    Turner, P.J.2    Pawankar, R.3    Taylor, S.4    Sicherer, S.5
  • 6
    • 84906748714 scopus 로고    scopus 로고
    • Detection of Ara h 1 (a major peanut allergen) in food using an electrochemical gold nanoparticle-coated screen-printed immunosensor
    • Alves RC, Pimentel FB, Nouws HP, Marques RC, González-García MB, et al. 2015. Detection of Ara h 1 (a major peanut allergen) in food using an electrochemical gold nanoparticle-coated screen-printed immunosensor. Biosens. Bioelectron. 64:19-24
    • (2015) Biosens. Bioelectron. , vol.64 , pp. 19-24
    • Alves, R.C.1    Pimentel, F.B.2    Nouws, H.P.3    Marques, R.C.4    González-García, M.B.5
  • 7
    • 84882834576 scopus 로고    scopus 로고
    • Filaggrin gene mutation associations with peanut allergy persist despite variations in peanut allergy diagnostic criteria or asthma status
    • Asai Y, Greenwood C, Hull PR, Alizadehfar R, Ben-Shoshan M, et al. 2013. Filaggrin gene mutation associations with peanut allergy persist despite variations in peanut allergy diagnostic criteria or asthma status. J. Allergy Clin. Immunol. 132:239-42. E7
    • (2013) J. Allergy Clin. Immunol. , vol.132 , pp. 239-42e7
    • Asai, Y.1    Greenwood, C.2    Hull, P.R.3    Alizadehfar, R.4    Ben-Shoshan, M.5
  • 8
    • 77952742360 scopus 로고    scopus 로고
    • Greater epitope recognition of shrimp allergens by children than by adults suggests that shrimp sensitization decreases with age
    • Ayuso R, Sánchez-Garcia S, Lin J, Fu Z, Ibáñez MD, et al. 2010. Greater epitope recognition of shrimp allergens by children than by adults suggests that shrimp sensitization decreases with age. J. Allergy Clin. Immunol. 125:1286-93. E3
    • (2010) J. Allergy Clin. Immunol. , vol.125 , pp. 1286-93E3
    • Ayuso, R.1    Sánchez-Garcia, S.2    Lin, J.3    Fu, Z.4    Ibáñez, M.D.5
  • 9
    • 0000016467 scopus 로고    scopus 로고
    • Effect of polysaccharide conjugation or transglutaminase treatment on the allergenicity and functional properties of soy protein
    • Babiker EE, Hiroyuki A, Matsudomi N, Iwata H, Ogawa T, et al. 1998. Effect of polysaccharide conjugation or transglutaminase treatment on the allergenicity and functional properties of soy protein. J. Agric. Food Chem. 46:866-71
    • (1998) J. Agric. Food Chem. , vol.46 , pp. 866-871
    • Babiker, E.E.1    Hiroyuki, A.2    Matsudomi, N.3    Iwata, H.4    Ogawa, T.5
  • 11
    • 84871834613 scopus 로고    scopus 로고
    • Can we produce true tolerance in patients with food allergy
    • Berin MC, Mayer L. 2013. Can we produce true tolerance in patients with food allergy? J. Allergy Clin. Immunol. 131:14-22
    • (2013) J. Allergy Clin. Immunol. , vol.131 , pp. 14-22
    • Berin, M.C.1    Mayer, L.2
  • 12
    • 84877299772 scopus 로고    scopus 로고
    • Mucosal immunology of food allergy
    • Berin MC, Sampson HA. 2013. Mucosal immunology of food allergy. Curr. Biol. 23:R389-R400
    • (2013) Curr. Biol. , vol.23 , pp. R389-R400
    • Berin, M.C.1    Sampson, H.A.2
  • 14
    • 82955161705 scopus 로고    scopus 로고
    • Boiling peanut Ara h 1 results in the formation of aggregates with reduced allergenicity
    • Blanc F, Vissers YM, Adel-Patient K, Rigby NM, Mackie AR, et al. 2011. Boiling peanut Ara h 1 results in the formation of aggregates with reduced allergenicity. Mol. Nutr. Food Res. 55:1887-94
    • (2011) Mol. Nutr. Food Res. , vol.55 , pp. 1887-1894
    • Blanc, F.1    Vissers, Y.M.2    Adel-Patient, K.3    Rigby, N.M.4    Mackie, A.R.5
  • 16
    • 34047122018 scopus 로고    scopus 로고
    • Further fatalities caused by anaphylactic reactions to food, 2001-2006
    • Bock SA, Muñoz-Furlong A, Sampson HA. 2007. Further fatalities caused by anaphylactic reactions to food, 2001-2006. J. Allergy Clin. Immunol. 119:1016-18
    • (2007) J. Allergy Clin. Immunol. , vol.119 , pp. 1016-1018
    • Bock, S.A.1    Muñoz-Furlong, A.2    Sampson, H.A.3
  • 17
    • 79952190426 scopus 로고    scopus 로고
    • Seafood hypersensitivity in mite sensitized individuals: Is tropomyosin the only responsible allergen
    • Boquete M, Iraola V, MoralesM, Pinto H, Francisco C, et al. 2011. Seafood hypersensitivity in mite sensitized individuals: Is tropomyosin the only responsible allergen? Ann. Allergy Asthma Immunol. 106:223-29
    • (2011) Ann. Allergy Asthma Immunol. , vol.106 , pp. 223-229
    • Boquete, M.1    Iraola, V.2    Morales, M.3    Pinto, H.4    Francisco, C.5
  • 18
    • 78649828230 scopus 로고    scopus 로고
    • Guidelines for the diagnosis and management of food allergy in the US: Report of the NIAID-sponsored expert panel
    • Boyce JA, Assa'ad A, Burks AW, Jones SM, Sampson HA, et al. 2010. Guidelines for the diagnosis and management of food allergy in the US: report of the NIAID-sponsored expert panel. J. Allergy Clin. Immunol. 126:S1-58
    • (2010) J. Allergy Clin. Immunol. , vol.126 , pp. S1-58
    • Boyce, J.A.1    Assa'Ad, A.2    Burks, A.W.3    Jones, S.M.4    Sampson, H.A.5
  • 19
    • 85006237906 scopus 로고    scopus 로고
    • Food allergies in developing and emerging economies: Need for comprehensive data on prevalence rates
    • Boye JI. 2012. Food allergies in developing and emerging economies: need for comprehensive data on prevalence rates. Clin. Transl. Allergy 2:25
    • (2012) Clin. Transl. Allergy , vol.2 , pp. 25
    • Boye, J.I.1
  • 20
    • 0033928258 scopus 로고    scopus 로고
    • Molecular and biochemical classification of plant-derived food allergens
    • Breiteneder H, Ebner C. 2000. Molecular and biochemical classification of plant-derived food allergens. J. Allergy Clin. Immunol. 106:27-36
    • (2000) J. Allergy Clin. Immunol. , vol.106 , pp. 27-36
    • Breiteneder, H.1    Ebner, C.2
  • 26
    • 33847218656 scopus 로고    scopus 로고
    • ICP-MS as a novel detection system for quantitative element-tagged immunoassay of hidden peanut allergens in foods
    • Careri M, Elviri L, Mangia A, Mucchino C. 2007. ICP-MS as a novel detection system for quantitative element-tagged immunoassay of hidden peanut allergens in foods. Anal. Bioanal. Chem. 387:1851-54
    • (2007) Anal. Bioanal. Chem. , vol.387 , pp. 1851-1854
    • Careri, M.1    Elviri, L.2    Mangia, A.3    Mucchino, C.4
  • 27
    • 41149177388 scopus 로고    scopus 로고
    • Determination of peanut allergens in cereal-chocolate-based snacks: Metal-tag inductively coupled plasma mass spectrometry immunoassay versus liquid chromatography/electrospray ionization tandem mass spectrometry
    • CareriM, Elviri L, Maffini M, Mangia A, Mucchino C, TerenghiM. 2008. Determination of peanut allergens in cereal-chocolate-based snacks: metal-tag inductively coupled plasma mass spectrometry immunoassay versus liquid chromatography/electrospray ionization tandem mass spectrometry. Rapid Commun. Mass Spectrom. 22:807-11
    • (2008) Rapid Commun. Mass Spectrom. , vol.22 , pp. 807-811
    • Careri, M.1    Elviri, L.2    Maffini, M.3    Mangia, A.4    Mucchino, C.5    Terenghi, M.6
  • 28
    • 77956261769 scopus 로고    scopus 로고
    • The role of inhalant food allergens in occupational asthma
    • Cartier A. 2010. The role of inhalant food allergens in occupational asthma. Curr. Allergy Asthma Rep. 10:349-56
    • (2010) Curr. Allergy Asthma Rep. , vol.10 , pp. 349-356
    • Cartier, A.1
  • 29
    • 84857189219 scopus 로고    scopus 로고
    • Cutaneous lymphocyte antigen and 47 T-lymphocyte responses are associated with peanut allergy and tolerance in children
    • Chan S, Turcanu V, Stephens A, Fox A, Grieve A, Lack G. 2012. Cutaneous lymphocyte antigen and 47 T-lymphocyte responses are associated with peanut allergy and tolerance in children. Allergy 67:336-42
    • (2012) Allergy , vol.67 , pp. 336-342
    • Chan, S.1    Turcanu, V.2    Stephens, A.3    Fox, A.4    Grieve, A.5    Lack, G.6
  • 31
    • 20544471460 scopus 로고    scopus 로고
    • Severe food-allergic reactions in children across the UK and Ireland, 1998-2000
    • Colver AF, Nevantaus H, Macdougall CF, Cant AJ. 2005. Severe food-allergic reactions in children across the UK and Ireland, 1998-2000. Acta Paediatr. 94:689-95
    • (2005) Acta Paediatr. , vol.94 , pp. 689-695
    • Colver, A.F.1    Nevantaus, H.2    Macdougall, C.F.3    Cant, A.J.4
  • 33
    • 59449088566 scopus 로고    scopus 로고
    • Delayed anaphylaxis, angioedema, or urticaria after consumption of red meat in patients with IgE antibodies specific for galactose-1, 3-galactose
    • Commins SP, Satinover SM, Hosen J, Mozena J, Borish L, et al. 2009. Delayed anaphylaxis, angioedema, or urticaria after consumption of red meat in patients with IgE antibodies specific for galactose-1, 3-galactose. J. Allergy Clin. Immunol. 123:426-33. E2
    • (2009) J. Allergy Clin. Immunol. , vol.123 , pp. 426-33E2
    • Commins, S.P.1    Satinover, S.M.2    Hosen, J.3    Mozena, J.4    Borish, L.5
  • 34
    • 84866038850 scopus 로고    scopus 로고
    • ELISA-based detection of soybean proteins: A comparative study using antibodies against modified and native proteins
    • Cucu T, Devreese B, Kerkaert B, Rogge M, Vercruysse L, De Meulenaer B. 2012. ELISA-based detection of soybean proteins: a comparative study using antibodies against modified and native proteins. Food Anal. Methods 5:1121-30
    • (2012) Food Anal. Methods , vol.5 , pp. 1121-1130
    • Cucu, T.1    Devreese, B.2    Kerkaert, B.3    Rogge, M.4    Vercruysse, L.5    De Meulenaer, B.6
  • 35
    • 84879360327 scopus 로고    scopus 로고
    • Analysis to support allergen risk management: Which way to go
    • Cucu T, Jacxsens L, De Meulenaer B. 2013. Analysis to support allergen risk management: which way to go? J. Agric. Food Chem. 61:5624-33
    • (2013) J. Agric. Food Chem. , vol.61 , pp. 5624-5633
    • Cucu, T.1    Jacxsens, L.2    De Meulenaer, B.3
  • 36
    • 0034978333 scopus 로고    scopus 로고
    • How can thermal processing modify the antigenicity of proteins
    • Davis PJ, Smales CM, James DC. 2001. How can thermal processing modify the antigenicity of proteins? Allergy 56:56-60
    • (2001) Allergy , vol.56 , pp. 56-60
    • Davis, P.J.1    Smales, C.M.2    James, D.C.3
  • 38
    • 84893663106 scopus 로고    scopus 로고
    • Acute and long-term management of food allergy: Systematic review
    • de Silva D, GeromiM, Panesar S, Muraro A, Werfel T, et al. 2014. Acute and long-term management of food allergy: systematic review. Allergy 69:159-67
    • (2014) Allergy , vol.69 , pp. 159-167
    • De Silva, D.1    Geromi, M.2    Panesar, S.3    Muraro, A.4    Werfel, T.5
  • 39
    • 34147110830 scopus 로고    scopus 로고
    • Effect of pasta drying temperature on GI digestibility and allergenicity of durum wheat proteins
    • De Zorzi M, Curioni A, Simonato B, Giannattasio M, Pasini G. 2007. Effect of pasta drying temperature on GI digestibility and allergenicity of durum wheat proteins. Food Chem. 104:353-63
    • (2007) Food Chem. , vol.104 , pp. 353-363
    • De Zorzi, M.1    Curioni, A.2    Simonato, B.3    Giannattasio, M.4    Pasini, G.5
  • 40
    • 0343415612 scopus 로고    scopus 로고
    • Molecular characterization of human IgG monoclonal antibodies specific for the major birch pollen allergen Bet v 1. Anti-allergen IgG can enhance the anaphylactic reaction
    • Denépoux S, Eibensteiner PB, Steinberger P, Vrtala S, Visco V, et al. 2000. Molecular characterization of human IgG monoclonal antibodies specific for the major birch pollen allergen Bet v 1. Anti-allergen IgG can enhance the anaphylactic reaction. FEBS Lett. 465:39-46
    • (2000) FEBS Lett. , vol.465 , pp. 39-46
    • Denépoux, S.1    Eibensteiner, P.B.2    Steinberger, P.3    Vrtala, S.4    Visco, V.5
  • 42
    • 85061760127 scopus 로고    scopus 로고
    • Scientific opinion on the evaluation of allergenic foods and food ingredients for labelling purposes
    • EFSA NDA Panel
    • EFSA NDA Panel. 2014. Scientific opinion on the evaluation of allergenic foods and food ingredients for labelling purposes. EFSA J. 12:3894
    • (2014) EFSA J. , vol.12 , pp. 3894
  • 43
    • 84864395861 scopus 로고    scopus 로고
    • Electrochemical immunosensor for the milk allergen lactoglobulin based on electrografting of organic film on graphene modified screen-printed carbon electrodes
    • Eissa S, Tlili C, L'Hocine L, Zourob M. 2012. Electrochemical immunosensor for the milk allergen lactoglobulin based on electrografting of organic film on graphene modified screen-printed carbon electrodes. Biosens. Bioelectron. 38:308-13
    • (2012) Biosens. Bioelectron. , vol.38 , pp. 308-313
    • Eissa, S.1    Tlili, C.2    L'Hocine, L.3    Zourob, M.4
  • 44
    • 79951659609 scopus 로고    scopus 로고
    • Liquid chromatography and mass spectrometry in food allergen detection
    • Fæste CK, Rønning HT, Christians U, Granum PE. 2011. Liquid chromatography and mass spectrometry in food allergen detection. J. Food Prot. 74:316-45
    • (2011) J. Food Prot. , vol.74 , pp. 316-345
    • Fæste, C.K.1    Rønning, H.T.2    Christians, U.3    Granum, P.E.4
  • 46
    • 0033043827 scopus 로고    scopus 로고
    • A study on severe food reactions in Sweden-is soy protein an underestimated cause of food anaphylaxis
    • Foucard T, Malmheden Yman I. 1999. A study on severe food reactions in Sweden-is soy protein an underestimated cause of food anaphylaxis? Allergy 54:261-65
    • (1999) Allergy , vol.54 , pp. 261-265
    • Foucard, T.1    Malmheden Yman, I.2
  • 47
    • 85026950813 scopus 로고    scopus 로고
    • Rhinoconjunctival sensitization to hydrolyzed wheat protein in facial soap and induce wheat-dependant exercise-induced anaphylaxis
    • Fukutomi Y, Itagaki Y, Taniguchi M, Saito A, Yasueda H, et al. 2011. Rhinoconjunctival sensitization to hydrolyzed wheat protein in facial soap and induce wheat-dependant exercise-induced anaphylaxis. Clin. Transl. Allergy 1:49
    • (2011) Clin. Transl. Allergy , vol.1 , pp. 49
    • Fukutomi, Y.1    Itagaki, Y.2    Taniguchi, M.3    Saito, A.4    Yasueda, H.5
  • 48
    • 84924085164 scopus 로고    scopus 로고
    • From respiratory sensitization to food allergy: Anaphylactic reaction after ingestion of mushrooms (Agaricus bisporus)
    • GabrielMF, González-DelgadoP, Postigo I, Fernández J, SorianoV, et al. 2015. From respiratory sensitization to food allergy: anaphylactic reaction after ingestion of mushrooms (Agaricus bisporus). Med. Mycol. Case Rep. 8:14-16
    • (2015) Med. Mycol. Case Rep. , vol.8 , pp. 14-16
    • Gabriel, M.F.1    González-Delgado, P.2    Postigo, I.3    Fernández, J.4    Soriano, V.5
  • 50
    • 32344447223 scopus 로고    scopus 로고
    • Reversed-phase high-performance liquid chromatography applied to the determination of soybean proteins in commercial heat-processed meat products
    • García MC, Domínguez M, García-Ruiz C, Marina ML. 2006. Reversed-phase high-performance liquid chromatography applied to the determination of soybean proteins in commercial heat-processed meat products. Anal. Chim. Acta 559:215-20
    • (2006) Anal. Chim. Acta , vol.559 , pp. 215-220
    • García, M.C.1    Domínguez, M.2    García-Ruiz, C.3    Marina, M.L.4
  • 51
    • 84861203680 scopus 로고    scopus 로고
    • Comparison of international food allergen labeling regulations
    • Gendel SM. 2012. Comparison of international food allergen labeling regulations. Regul. Toxicol. Pharmacol. 63:279-85
    • (2012) Regul. Toxicol. Pharmacol. , vol.63 , pp. 279-285
    • Gendel, S.M.1
  • 52
    • 84888410446 scopus 로고    scopus 로고
    • Analysis of US Food and Drug Administration food allergen recalls after implementation of the food allergen labeling and consumer protection act
    • Gendel SM, Zhu J. 2013. Analysis of US Food and Drug Administration food allergen recalls after implementation of the food allergen labeling and consumer protection act. J. Food Prot. 76:1933-38
    • (2013) J. Food Prot. , vol.76 , pp. 1933-1938
    • Gendel, S.M.1    Zhu, J.2
  • 53
    • 79952283941 scopus 로고    scopus 로고
    • Birch pollen-related food allergy: Clinical aspects and the role of allergen-specific IgE and IgG 4 antibodies
    • Geroldinger-Simic M, Zelniker T, Aberer W, Ebner C, Egger C, et al. 2011. Birch pollen-related food allergy: clinical aspects and the role of allergen-specific IgE and IgG 4 antibodies. J. Allergy Clin. Immunol. 127:616-22. E1
    • (2011) J. Allergy Clin. Immunol. , vol.127 , pp. 616-22E1
    • Geroldinger-Simic, M.1    Zelniker, T.2    Aberer, W.3    Ebner, C.4    Egger, C.5
  • 54
    • 84919629422 scopus 로고    scopus 로고
    • Simultaneous detection of multi-allergens in an incurred food matrix using ELISA, multiplex flow cytometry and liquid chromatography mass spectrometry (LC-MS)
    • Gomaa A, Boye J. 2015. Simultaneous detection of multi-allergens in an incurred food matrix using ELISA, multiplex flow cytometry and liquid chromatography mass spectrometry (LC-MS). Food Chem. 175:585-92
    • (2015) Food Chem. , vol.175 , pp. 585-592
    • Gomaa, A.1    Boye, J.2
  • 58
    • 17144405680 scopus 로고    scopus 로고
    • Potential role of interleukin-10-secreting regulatory T cells in allergy and asthma
    • Hawrylowicz C, O'Garra A. 2005. Potential role of interleukin-10-secreting regulatory T cells in allergy and asthma. Nat. Rev. Immunol. 5:271-83
    • (2005) Nat. Rev. Immunol. , vol.5 , pp. 271-283
    • Hawrylowicz, C.1    O'Garra, A.2
  • 59
    • 6344219843 scopus 로고    scopus 로고
    • Anaphylaxis to excipient mannitol: Evidence for an immunoglobulin Emediated mechanism
    • Hegde VL, Venkatesh YP. 2004. Anaphylaxis to excipient mannitol: evidence for an immunoglobulin Emediated mechanism. Clin. Exp. Allergy 34:1602-9
    • (2004) Clin. Exp. Allergy , vol.34 , pp. 1602-1609
    • Hegde, V.L.1    Venkatesh, Y.P.2
  • 62
    • 84901413364 scopus 로고    scopus 로고
    • Clinical spectrum of food allergies: A comprehensive review
    • Ho MH-K, WongWH-S, Chang C. 2014. Clinical spectrum of food allergies: a comprehensive review. Clin. Rev. Allergy Immunol. 46:225-40
    • (2014) Clin. Rev. Allergy Immunol. , vol.46 , pp. 225-240
    • Mh-K, H.1    WongWH-S2    Chang, C.3
  • 63
    • 68949162032 scopus 로고    scopus 로고
    • Food allergen protein families and their structural characteristics and application in component-resolved diagnosis: New data from the EuroPrevall project
    • Hoffmann-Sommergruber K, Mills EC. 2009. Food allergen protein families and their structural characteristics and application in component-resolved diagnosis: new data from the EuroPrevall project. Anal. Bioanal. Chem. 395:25-35
    • (2009) Anal. Bioanal. Chem. , vol.395 , pp. 25-35
    • Hoffmann-Sommergruber, K.1    Mills, E.C.2
  • 64
    • 0001096135 scopus 로고    scopus 로고
    • Rocket immunoelectrophoresis (RIE) for determination of potentially allergenic peanut proteins in processed foods as a simple means for quality assurance and food safety
    • Holzhauser T, Dehne L, Hoffmann A, Haustein D, Vieths S. 1998. Rocket immunoelectrophoresis (RIE) for determination of potentially allergenic peanut proteins in processed foods as a simple means for quality assurance and food safety. Z. Lebensm. Unters. Forsch. 206:1-8
    • (1998) Z. Lebensm. Unters. Forsch. , vol.206 , pp. 1-8
    • Holzhauser, T.1    Dehne, L.2    Hoffmann, A.3    Haustein, D.4    Vieths, S.5
  • 65
    • 0037048737 scopus 로고    scopus 로고
    • Detection of potentially allergenic hazelnut (Corylus avellana) residues in food: A comparative study with DNA PCR-ELISA and protein sandwich-ELISA
    • Holzhauser T, Stephan O, Vieths S. 2002. Detection of potentially allergenic hazelnut (Corylus avellana) residues in food: a comparative study with DNA PCR-ELISA and protein sandwich-ELISA. J. Agric. Food Chem. 50:5808-15
    • (2002) J. Agric. Food Chem. , vol.50 , pp. 5808-5815
    • Holzhauser, T.1    Stephan, O.2    Vieths, S.3
  • 66
    • 0001587664 scopus 로고    scopus 로고
    • Polymerase chain reaction (PCR) for detection of potentially allergenic hazelnut residues in complex food matrixes
    • Holzhauser T, Wangorsch A, Vieths S. 2000. Polymerase chain reaction (PCR) for detection of potentially allergenic hazelnut residues in complex food matrixes. Eur. Food Res. Technol. 211:360-65
    • (2000) Eur. Food Res. Technol. , vol.211 , pp. 360-365
    • Holzhauser, T.1    Wangorsch, A.2    Vieths, S.3
  • 67
    • 79959921847 scopus 로고    scopus 로고
    • High-pressure treatment reduces the immunoreactivity of the major allergens in apple and celeriac
    • Husband FA, Aldick T, van der Plancken I, Grauwet T, Hendrickx M, et al. 2011. High-pressure treatment reduces the immunoreactivity of the major allergens in apple and celeriac. Mol. Nutr. Food Res. 55:1087-95
    • (2011) Mol. Nutr. Food Res. , vol.55 , pp. 1087-1095
    • Husband, F.A.1    Aldick, T.2    Van Der Plancken, I.3    Grauwet, T.4    Hendrickx, M.5
  • 69
    • 73149101622 scopus 로고    scopus 로고
    • Glycation of a food allergen by the Maillard reaction enhances its T-cell immunogenicity: Role of macrophage scavenger receptor class A type i and II
    • Ilchmann A, Burgdorf S, Scheurer S, Waibler Z, Nagai R, et al. 2010. Glycation of a food allergen by the Maillard reaction enhances its T-cell immunogenicity: role of macrophage scavenger receptor class A type I and II. J. Allergy Clin. Immunol. 125:175-83. E11
    • (2010) J. Allergy Clin. Immunol. , vol.125 , pp. 175-83e11
    • Ilchmann, A.1    Burgdorf, S.2    Scheurer, S.3    Waibler, Z.4    Nagai, R.5
  • 70
    • 69949147603 scopus 로고    scopus 로고
    • Selective IgA deficiency in early life: Association to infections and allergic diseases during childhood
    • Janzi M, Kull I, Sjöberg R, Wan J, Melén E, et al. 2009. Selective IgA deficiency in early life: association to infections and allergic diseases during childhood. Clin. Immunol. 133:78-85
    • (2009) Clin. Immunol. , vol.133 , pp. 78-85
    • Janzi, M.1    Kull, I.2    Sjöberg, R.3    Wan, J.4    Melén, E.5
  • 71
    • 68049142071 scopus 로고    scopus 로고
    • Mammalian milk allergy: Clinical suspicion, cross-reactivities and diagnosis
    • Järvinen KM, Chatchatee P. 2009. Mammalian milk allergy: clinical suspicion, cross-reactivities and diagnosis. Curr. Opin. Allergy Clin. Immunol. 9:251-58
    • (2009) Curr. Opin. Allergy Clin. Immunol. , vol.9 , pp. 251-258
    • Järvinen, K.M.1    Chatchatee, P.2
  • 72
    • 84923226752 scopus 로고    scopus 로고
    • Comparison of six commercial ELISA kits for their specificity and sensitivity in detecting different major peanut allergens
    • Jayasena S, Smits M, Fiechter D, de Jong A, Nordlee J, et al. 2015. Comparison of six commercial ELISA kits for their specificity and sensitivity in detecting different major peanut allergens. J. Agric. Food Chem. 63:1849-55
    • (2015) J. Agric. Food Chem. , vol.63 , pp. 1849-1855
    • Jayasena, S.1    Smits, M.2    Fiechter, D.3    De Jong, A.4    Nordlee, J.5
  • 73
    • 36749050495 scopus 로고    scopus 로고
    • Evolutionary distance from human homologs reflects allergenicity of animal food proteins
    • Jenkins JA, BreitenederH, Mills EC. 2007. Evolutionary distance from human homologs reflects allergenicity of animal food proteins. J. Allergy Clin. Immunol. 120:1399-405
    • (2007) J. Allergy Clin. Immunol. , vol.120 , pp. 1399-1405
    • Jenkins, J.A.1    Breiteneder, H.2    Mills, E.C.3
  • 74
    • 11344255717 scopus 로고    scopus 로고
    • Structural relatedness of plant food allergens with specific reference to cross-reactive allergens: An in silico analysis
    • Jenkins JA, Griffiths-Jones S, Shewry PR, Breiteneder H, Mills EC. 2005. Structural relatedness of plant food allergens with specific reference to cross-reactive allergens: an in silico analysis. J. Allergy Clin. Immunol. 115:163-70
    • (2005) J. Allergy Clin. Immunol. , vol.115 , pp. 163-170
    • Jenkins, J.A.1    Griffiths-Jones, S.2    Shewry, P.R.3    Breiteneder, H.4    Mills, E.C.5
  • 75
    • 84880357975 scopus 로고    scopus 로고
    • Mast cell-based electrochemical biosensor for quantification of the major shrimp allergen Pen a 1 (tropomyosin)
    • Jiang D, Ji J, Sun X, Zhang Y, Zhang G, Tang L. 2013. Mast cell-based electrochemical biosensor for quantification of the major shrimp allergen Pen a 1 (tropomyosin). Biosens. Bioelectron. 50:150-56
    • (2013) Biosens. Bioelectron. , vol.50 , pp. 150-156
    • Jiang, D.1    Ji, J.2    Sun, X.3    Zhang, Y.4    Zhang, G.5    Tang, L.6
  • 76
    • 80053093893 scopus 로고    scopus 로고
    • Human immunoglobulin e (IgE) binding to heated and glycated ovalbumin and ovomucoid before and after in vitro digestion
    • Jiménez-Saiz R, Belloque J, Molina E, López-Fandino R. 2011. Human immunoglobulin E (IgE) binding to heated and glycated ovalbumin and ovomucoid before and after in vitro digestion. J. Agric. Food Chem. 59:10044-51
    • (2011) J. Agric. Food Chem. , vol.59 , pp. 10044-10051
    • Jiménez-Saiz, R.1    Belloque, J.2    Molina, E.3    López-Fandino, R.4
  • 77
    • 84884634149 scopus 로고    scopus 로고
    • Impact of heat processing on the detection of the major shellfish allergen tropomyosin in crustaceans and molluscs using specific monoclonal antibodies
    • Kamath SD, Rahman AMA, Komoda T, Lopata AL. 2013. Impact of heat processing on the detection of the major shellfish allergen tropomyosin in crustaceans and molluscs using specific monoclonal antibodies. Food Chem. 141:4031-39
    • (2013) Food Chem. , vol.141 , pp. 4031-4039
    • Kamath, S.D.1    Rahman, A.M.A.2    Komoda, T.3    Lopata, A.L.4
  • 78
    • 84896804037 scopus 로고    scopus 로고
    • Effect of heat processing on antibody reactivity to allergen variants and fragments of black tiger prawn: A comprehensive allergenomic approach
    • Kamath SD, Rahman AMA, Voskamp A, Komoda T, Rolland JM, et al. 2014. Effect of heat processing on antibody reactivity to allergen variants and fragments of black tiger prawn: a comprehensive allergenomic approach. Mol. Nutr. Food Res. 58:1144-55
    • (2014) Mol. Nutr. Food Res. , vol.58 , pp. 1144-1155
    • Kamath, S.D.1    Rahman, A.M.A.2    Voskamp, A.3    Komoda, T.4    Rolland, J.M.5
  • 79
    • 84862841853 scopus 로고    scopus 로고
    • Intrauterine sensitization of allergenspecific IgE analyzed by a highly sensitive new allergen microarray
    • Kamemura N, Tada H, Shimojo N, Morita Y, Kohno Y, et al. 2012. Intrauterine sensitization of allergenspecific IgE analyzed by a highly sensitive new allergen microarray. J. AllergyClin. Immunol. 130:113-21. E2
    • (2012) J. AllergyClin. Immunol. , vol.130 , pp. 113-21e2
    • Kamemura, N.1    Tada, H.2    Shimojo, N.3    Morita, Y.4    Kohno, Y.5
  • 80
    • 73249126020 scopus 로고    scopus 로고
    • Detection of hen's egg white lysozyme in food: Comparison between a sensitive HPLC and a commercial ELISA method
    • Kerkaert B, Mestdagh F, De Meulenaer B. 2010. Detection of hen's egg white lysozyme in food: comparison between a sensitive HPLC and a commercial ELISA method. Food Chem. 120:580-84
    • (2010) Food Chem. , vol.120 , pp. 580-584
    • Kerkaert, B.1    Mestdagh, F.2    De Meulenaer, B.3
  • 81
    • 84907324908 scopus 로고    scopus 로고
    • Effects of processing on the recovery of food allergens from a model dark chocolate matrix
    • Khuda SE, Jackson LS, Fu T-J, Williams KM. 2015. Effects of processing on the recovery of food allergens from a model dark chocolate matrix. Food Chem. 168:580-87
    • (2015) Food Chem. , vol.168 , pp. 580-587
    • Khuda, S.E.1    Jackson, L.S.2    Fu, T.-J.3    Williams, K.M.4
  • 84
    • 84867737688 scopus 로고    scopus 로고
    • Two quantitative hexaplex real-time PCR systems for the detection and quantification of DNA from twelve allergens in food
    • Köppel R, van Velsen-Zimmerli F, Bucher T. 2012. Two quantitative hexaplex real-time PCR systems for the detection and quantification of DNA from twelve allergens in food. Eur. Food Res. Technol. 235:843-52
    • (2012) Eur. Food Res. Technol. , vol.235 , pp. 843-852
    • Köppel, R.1    Van Velsen-Zimmerli, F.2    Bucher, T.3
  • 85
    • 33749016485 scopus 로고    scopus 로고
    • Immunological mechanisms of allergen-specific immunotherapy
    • LarchéM, Akdis CA, Valenta R. 2006. Immunological mechanisms of allergen-specific immunotherapy. Nat. Rev. Immunol. 6:761-71
    • (2006) Nat. Rev. Immunol. , vol.6 , pp. 761-771
    • Larchém1    Akdis, C.A.2    Valenta, R.3
  • 86
    • 33847355098 scopus 로고    scopus 로고
    • Comparison of the changes of the antigenicities of a hen's egg albumin by a gamma and an electron beam irradiation
    • Lee J-W, Seo J-H, Kim J-H, Lee S-Y, Byun M-W. 2007. Comparison of the changes of the antigenicities of a hen's egg albumin by a gamma and an electron beam irradiation. Rad. Phys. Chem. 76:879-85
    • (2007) Rad. Phys. Chem. , vol.76 , pp. 879-885
    • Lee, J.-W.1    Seo, J.-H.2    Kim, J.-H.3    Lee, S.-Y.4    Byun, M.-W.5
  • 87
    • 84855898320 scopus 로고    scopus 로고
    • Lessons from cases of mortality due to food allergy in Israel: Cow's milk protein should be considered a potentially fatal allergen
    • Levy MB, Goldberg MR, Nachshon L, Tabachnik E, Katz Y. 2012. Lessons from cases of mortality due to food allergy in Israel: cow's milk protein should be considered a potentially fatal allergen. IMAJ 14:29
    • (2012) IMAJ , vol.14 , pp. 29
    • Levy, M.B.1    Goldberg, M.R.2    Nachshon, L.3    Tabachnik, E.4    Katz, Y.5
  • 88
    • 84855674654 scopus 로고    scopus 로고
    • Effects of high hydrostatic pressure treatment on allergenicity and structural properties of soybean protein isolate for infant formula
    • Li H, Zhu K, Zhou H, Peng W. 2012. Effects of high hydrostatic pressure treatment on allergenicity and structural properties of soybean protein isolate for infant formula. Food Chem. 132:808-14
    • (2012) Food Chem. , vol.132 , pp. 808-814
    • Li, H.1    Zhu, K.2    Zhou, H.3    Peng, W.4
  • 90
    • 68549136672 scopus 로고    scopus 로고
    • The role of immunoglobulin E-binding epitopes in the characterization of food allergy
    • Lin J, Sampson HA. 2009. The role of immunoglobulin E-binding epitopes in the characterization of food allergy. Curr. Opin. Allergy Clin. Immunol. 9:357-63
    • (2009) Curr. Opin. Allergy Clin. Immunol. , vol.9 , pp. 357-363
    • Lin, J.1    Sampson, H.A.2
  • 91
    • 53549121442 scopus 로고    scopus 로고
    • Increasing anaphylaxis hospitalizations in the first 2 decades of life: New York State, 1990-2006
    • Lin RY, Anderson AS, Shah SN, Nurruzzaman F. 2008. Increasing anaphylaxis hospitalizations in the first 2 decades of life: New York State, 1990-2006. Ann. Allergy Asthma Immunol. 101:387-93
    • (2008) Ann. Allergy Asthma Immunol. , vol.101 , pp. 387-393
    • Lin, R.Y.1    Anderson, A.S.2    Shah, S.N.3    Nurruzzaman, F.4
  • 93
    • 84865328213 scopus 로고    scopus 로고
    • Shellfish allergy diagnosis-gaps and needs: Review article
    • Lopata AL, Kamath S. 2012. Shellfish allergy diagnosis-gaps and needs: review article. Curr. Allergy Clin. Immunol. 25:60-66
    • (2012) Curr. Allergy Clin. Immunol. , vol.25 , pp. 60-66
    • Lopata, A.L.1    Kamath, S.2
  • 95
    • 84923196714 scopus 로고    scopus 로고
    • Development of real-time PCR assays to detect cashew (Anacardium occidentale) and macadamia (Macadamia intergrifolia) residues in market analysis of processed food products
    • López-Calleja IM, de la Cruz S, González I, García T, Martín R. 2015. Development of real-time PCR assays to detect cashew (Anacardium occidentale) and macadamia (Macadamia intergrifolia) residues in market analysis of processed food products. LWT Food Sci. Technol. 62:233-41
    • (2015) LWT Food Sci. Technol. , vol.62 , pp. 233-241
    • López-Calleja, I.M.1    De La Cruz, S.2    González, I.3    García, T.4    Martín, R.5
  • 96
    • 56749179441 scopus 로고    scopus 로고
    • Comparison of natural and recombinant forms of the major fish allergen parvalbumin from cod and carp
    • Ma Y, Griesmeier U, Susani M, Radauer C, Briza P, et al. 2008. Comparison of natural and recombinant forms of the major fish allergen parvalbumin from cod and carp. Mol. Nutr. Food Res. 52:S196-207
    • (2008) Mol. Nutr. Food Res. , vol.52 , pp. S196-207
    • Ma, Y.1    Griesmeier, U.2    Susani, M.3    Radauer, C.4    Briza, P.5
  • 97
    • 33746701360 scopus 로고    scopus 로고
    • Characterization of recombinant Mal d 4 and its application for component-resolved diagnosis of apple allergy
    • Ma Y, Zuidmeer L, Bohle B, Bolhaar S, Gadermaier G, et al. 2006. Characterization of recombinant Mal d 4 and its application for component-resolved diagnosis of apple allergy. Clin. Exp. Allergy 36:1087-96
    • (2006) Clin. Exp. Allergy , vol.36 , pp. 1087-1096
    • Ma, Y.1    Zuidmeer, L.2    Bohle, B.3    Bolhaar, S.4    Gadermaier, G.5
  • 101
    • 84897085870 scopus 로고    scopus 로고
    • In vitro digestion of soluble cashew proteins and characterization of surviving IgE-reactive peptides
    • Mattison CP, Grimm CC, Wasserman RL. 2014. In vitro digestion of soluble cashew proteins and characterization of surviving IgE-reactive peptides. Mol. Nutr. Food Res. 58:884-93
    • (2014) Mol. Nutr. Food Res. , vol.58 , pp. 884-893
    • Mattison, C.P.1    Grimm, C.C.2    Wasserman, R.L.3
  • 103
    • 0031779478 scopus 로고    scopus 로고
    • Tissue transglutaminase selectively modifies gliadin peptides that are recognized by gut-derived T cells in celiac disease
    • Molberg O, McAdam SN, Körner R, Quarsten H, Kristiansen C, et al. 1998. Tissue transglutaminase selectively modifies gliadin peptides that are recognized by gut-derived T cells in celiac disease. Nat. Med. 4:713-17
    • (1998) Nat. Med. , vol.4 , pp. 713-717
    • Molberg, O.1    McAdam, S.N.2    Körner, R.3    Quarsten, H.4    Kristiansen, C.5
  • 104
    • 42649101981 scopus 로고    scopus 로고
    • Development of a method for the quantification of whey allergen traces in mixed-fruit juices based on liquid chromatography with mass spectrometric detection
    • Monaci L, van Hengel AJ. 2008. Development of a method for the quantification of whey allergen traces in mixed-fruit juices based on liquid chromatography with mass spectrometric detection. J. Chromatogr. A 1192:113-20
    • (2008) J. Chromatogr. A , vol.1192 , pp. 113-120
    • Monaci, L.1    Van Hengel, A.J.2
  • 105
    • 67349171915 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics methods for analysis of food allergens
    • Monaci L, Visconti A. 2009. Mass spectrometry-based proteomics methods for analysis of food allergens. Trends Anal. Chem. 28:581-91
    • (2009) Trends Anal. Chem. , vol.28 , pp. 581-591
    • Monaci, L.1    Visconti, A.2
  • 106
    • 80051860074 scopus 로고    scopus 로고
    • Enzyme-linked immunosorbent assay (ELISA) for detection of sulfur-rich protein (SRP) in soybeans (Glycine max L.) and certain other edible plant seeds
    • Monaghan EK, Venkatachalam M, SeavyM, Beyer K, Sampson HA, et al. 2008. Enzyme-linked immunosorbent assay (ELISA) for detection of sulfur-rich protein (SRP) in soybeans (Glycine max L.) and certain other edible plant seeds. J. Agric. Food Chem. 56:765-77
    • (2008) J. Agric. Food Chem. , vol.56 , pp. 765-777
    • Monaghan, E.K.1    Venkatachalam, M.2    Seavy, M.3    Beyer, K.4    Sampson, H.A.5
  • 107
    • 84923556588 scopus 로고    scopus 로고
    • Detection of peanut (Arachis hypogaea) allergens in processed foods by immunoassay: Influence of selected target protein and ELISA format applied
    • Montserrat M, Sanz D, Juan T, Herrero A, Sánchez L, et al. 2015. Detection of peanut (Arachis hypogaea) allergens in processed foods by immunoassay: influence of selected target protein and ELISA format applied. Food Control 54:300-7
    • (2015) Food Control , vol.54 , pp. 300-307
    • Montserrat, M.1    Sanz, D.2    Juan, T.3    Herrero, A.4    Sánchez, L.5
  • 108
    • 79957931918 scopus 로고    scopus 로고
    • Multiplex, quantitative, ligation-dependent probe amplification for determination of allergens in food
    • Mustorp SL, Drømtorp SM, Holck AL. 2011. Multiplex, quantitative, ligation-dependent probe amplification for determination of allergens in food. J. Agric. Food Chem. 59:5231-39
    • (2011) J. Agric. Food Chem. , vol.59 , pp. 5231-5239
    • Mustorp, S.L.1    Drømtorp, S.M.2    Holck, A.L.3
  • 109
    • 84908146409 scopus 로고    scopus 로고
    • Does maternal diet during pregnancy and lactation affect outcomes in offspring A systematic review of food-based approaches
    • Netting MJ, Middleton PF, Makrides M. 2014. Does maternal diet during pregnancy and lactation affect outcomes in offspring A systematic review of food-based approaches. Nutrition 30:1225-41
    • (2014) Nutrition , vol.30 , pp. 1225-1241
    • Netting, M.J.1    Middleton, P.F.2    Makrides, M.3
  • 111
    • 61449212919 scopus 로고    scopus 로고
    • High-affinity IgE recognition of a conformational epitope of the major respiratory allergen Phl p 2 as revealed by ray crystallography
    • Padavattan S, Flicker S, Schirmer T, Madritsch C, Randow S, et al. 2009. High-affinity IgE recognition of a conformational epitope of the major respiratory allergen Phl p 2 as revealed by ray crystallography. J. Immunol. 182:2141-51
    • (2009) J. Immunol. , vol.182 , pp. 2141-2151
    • Padavattan, S.1    Flicker, S.2    Schirmer, T.3    Madritsch, C.4    Randow, S.5
  • 112
    • 84964265714 scopus 로고    scopus 로고
    • Development and validation of a triplex real-time PCR assay for the simultaneous detection of three mustard species and three celery varieties in food
    • Palle-Reisch M, Hochegger R, Cichna-Markl M. 2015. Development and validation of a triplex real-time PCR assay for the simultaneous detection of three mustard species and three celery varieties in food. Food Chem. 184:46-56
    • (2015) Food Chem. , vol.184 , pp. 46-56
    • Palle-Reisch, M.1    Hochegger, R.2    Cichna-Markl, M.3
  • 113
    • 69149110073 scopus 로고    scopus 로고
    • Aspects of food processing and its effect on allergen structure
    • Paschke A. 2009. Aspects of food processing and its effect on allergen structure. Mol. Nutr. Food Res. 53:959-62
    • (2009) Mol. Nutr. Food Res. , vol.53 , pp. 959-962
    • Paschke, A.1
  • 115
    • 78649997364 scopus 로고    scopus 로고
    • Gut permeability and food allergies
    • Perrier C, Corthesy B. 2011. Gut permeability and food allergies. Clin. Exp. Allergy 41:20-28
    • (2011) Clin. Exp. Allergy , vol.41 , pp. 20-28
    • Perrier, C.1    Corthesy, B.2
  • 116
    • 84885912265 scopus 로고    scopus 로고
    • The natural history of IgE-mediated food allergy: Can skin prick tests and serum-specific IgE predict the resolution of food allergy
    • Peters RL, Gurrin LC, Dharmage SC, Koplin JJ, Allen KJ. 2013. The natural history of IgE-mediated food allergy: Can skin prick tests and serum-specific IgE predict the resolution of food allergy? Int. J. Environ. Res. Public Health 10:5039-61
    • (2013) Int. J. Environ. Res. Public Health , vol.10 , pp. 5039-5061
    • Peters, R.L.1    Gurrin, L.C.2    Dharmage, S.C.3    Koplin, J.J.4    Allen, K.J.5
  • 117
    • 84877020840 scopus 로고    scopus 로고
    • Advances in biosensor development based on integrating nanotechnology and applied to food-allergen management
    • Pilolli R, Monaci L, ViscontiA. 2013. Advances in biosensor development based on integrating nanotechnology and applied to food-allergen management. Trends Anal. Chem. 47:12-26
    • (2013) Trends Anal. Chem. , vol.47 , pp. 12-26
    • Pilolli, R.1    Monaci, L.2    Visconti, A.3
  • 118
    • 84953378264 scopus 로고    scopus 로고
    • Rapid and label-free detection of egg allergen traces in wines by surface plasmon resonance biosensor
    • Pilolli R, Visconti A, Monaci L. 2015. Rapid and label-free detection of egg allergen traces in wines by surface plasmon resonance biosensor. Anal. Bioanal. Chem. 407:3787-97
    • (2015) Anal. Bioanal. Chem. , vol.407 , pp. 3787-3797
    • Pilolli, R.1    Visconti, A.2    Monaci, L.3
  • 119
    • 80455128692 scopus 로고    scopus 로고
    • Quantitative detection of hazelnut (Corylus avellana) in cookies: ELISA versus real-time PCR
    • Platteau C, De Loose M, De Meulenaer B, Taverniers I. 2011. Quantitative detection of hazelnut (Corylus avellana) in cookies: ELISA versus real-time PCR. J. Agric. Food Chem. 59:11395-402
    • (2011) J. Agric. Food Chem. , vol.59 , pp. 11395-11402
    • Platteau, C.1    De Loose, M.2    De Meulenaer, B.3    Taverniers, I.4
  • 120
    • 78751591226 scopus 로고    scopus 로고
    • Fast and accurate peanut allergen detection with nanobead enhanced optical fiber SPR biosensor
    • Pollet J, Delport F, Janssen K, Tran D, Wouters J, et al. 2011. Fast and accurate peanut allergen detection with nanobead enhanced optical fiber SPR biosensor. Talanta 83:1436-41
    • (2011) Talanta , vol.83 , pp. 1436-1441
    • Pollet, J.1    Delport, F.2    Janssen, K.3    Tran, D.4    Wouters, J.5
  • 121
    • 1142287446 scopus 로고    scopus 로고
    • Methods for allergen analysis in food: A review
    • Poms R, Klein C, Anklam E. 2004. Methods for allergen analysis in food: a review. Food Addit. Contam. 21:1-31
    • (2004) Food Addit. Contam. , vol.21 , pp. 1-31
    • Poms, R.1    Klein, C.2    Anklam, E.3
  • 123
    • 84925356734 scopus 로고    scopus 로고
    • Novel liquid chromatography-mass spectrometry method for sensitive determination of the mustard allergen Sin a 1 in food
    • Posada-Ayala M, Alvarez-Llamas G, Maroto AS, Maes X, Muñoz-Garcia E, et al. 2015. Novel liquid chromatography-mass spectrometry method for sensitive determination of the mustard allergen Sin a 1 in food. Food Chem. 183:58-63
    • (2015) Food Chem. , vol.183 , pp. 58-63
    • Posada-Ayala, M.1    Alvarez-Llamas, G.2    Maroto, A.S.3    Maes, X.4    Muñoz-Garcia, E.5
  • 125
    • 0033867568 scopus 로고    scopus 로고
    • Lessons for management of anaphylaxis from a study of fatal reactions
    • Pumphrey R. 2000. Lessons for management of anaphylaxis from a study of fatal reactions. Clin. Exp. Allergy 30:1144-50
    • (2000) Clin. Exp. Allergy , vol.30 , pp. 1144-1150
    • Pumphrey, R.1
  • 126
    • 34047109049 scopus 로고    scopus 로고
    • Further fatal allergic reactions to food in the United Kingdom, 1999-2006
    • Pumphrey RS, Gowland MH. 2007. Further fatal allergic reactions to food in the United Kingdom, 1999-2006. J. Allergy Clin. Immunol. 119:1018-19
    • (2007) J. Allergy Clin. Immunol. , vol.119 , pp. 1018-1019
    • Pumphrey, R.S.1    Gowland, M.H.2
  • 127
    • 0034917480 scopus 로고    scopus 로고
    • Chicken serum albumin (Gal d 5) is a partially heat-labile inhalant and food allergen implicated in the bird-egg syndrome
    • Quirce S, Maranon F, Umpierrez A, De Las Heras M, Fernández-Caldas E, Sastre J. 2001. Chicken serum albumin (Gal d 5) is a partially heat-labile inhalant and food allergen implicated in the bird-egg syndrome. Allergy 56:754-62
    • (2001) Allergy , vol.56 , pp. 754-762
    • Quirce, S.1    Maranon, F.2    Umpierrez, A.3    De Las Heras, M.4    Fernández-Caldas, E.5    Sastre, J.6
  • 128
    • 41449094497 scopus 로고    scopus 로고
    • Allergens are distributed into few protein families and possess a restricted number of biochemical functions
    • Radauer C, Bublin M, Wagner S, Mari A, Breiteneder H. 2008. Allergens are distributed into few protein families and possess a restricted number of biochemical functions. J. Allergy Clin. Immunol. 121:847-52. E7
    • (2008) J. Allergy Clin. Immunol. , vol.121 , pp. 847-52E7
    • Radauer, C.1    Bublin, M.2    Wagner, S.3    Mari, A.4    Breiteneder, H.5
  • 132
    • 0026638876 scopus 로고
    • Fatal and near-fatal anaphylactic reactions to food in children and adolescents
    • Sampson HA, Mendelson L, Rosen JP. 1992. Fatal and near-fatal anaphylactic reactions to food in children and adolescents. N. Engl. J. Med. 327:380-84
    • (1992) N. Engl. J. Med. , vol.327 , pp. 380-384
    • Sampson, H.A.1    Mendelson, L.2    Rosen, J.P.3
  • 134
    • 69149090077 scopus 로고    scopus 로고
    • Effects of food processing on food allergens
    • Sathe SK, Sharma GM. 2009. Effects of food processing on food allergens. Mol. Nutr. Food Res. 53:970-78
    • (2009) Mol. Nutr. Food Res. , vol.53 , pp. 970-978
    • Sathe, S.K.1    Sharma, G.M.2
  • 135
    • 22244434681 scopus 로고    scopus 로고
    • Effects of food processing on the stability of food allergens
    • Sathe SK, Teuber SS, Roux KH. 2005. Effects of food processing on the stability of food allergens. Biotechnol. Adv. 23:423-29
    • (2005) Biotechnol. Adv. , vol.23 , pp. 423-429
    • Sathe, S.K.1    Teuber, S.S.2    Roux, K.H.3
  • 138
    • 84875829724 scopus 로고    scopus 로고
    • Antigen sampling in the small intestine
    • Schulz O, Pabst O. 2013. Antigen sampling in the small intestine. Trends Immunol. 34:155-61
    • (2013) Trends Immunol. , vol.34 , pp. 155-161
    • Schulz, O.1    Pabst, O.2
  • 139
    • 0032033678 scopus 로고    scopus 로고
    • Crystal structures of two IA d-peptide complexes reveal that high affinity can be achieved without large anchor residues
    • Scott C, Peterson P, Teyton L, Wilson I. 1998. Crystal structures of two IA d-peptide complexes reveal that high affinity can be achieved without large anchor residues. Immunity 8:319-29
    • (1998) Immunity , vol.8 , pp. 319-329
    • Scott, C.1    Peterson, P.2    Teyton, L.3    Wilson, I.4
  • 140
    • 21844457947 scopus 로고    scopus 로고
    • Development of an in vitro system for the study of allergens and allergen-specific immunoglobulin e and immunoglobulin G: Fc receptor i supercross-linking is a possible new mechanism of immunoglobulin G-dependent enhancement of type i allergic reactions
    • Sellge G, Laffer S, Mierke C, Vrtala S, Hoffmann M, et al. 2005. Development of an in vitro system for the study of allergens and allergen-specific immunoglobulin E and immunoglobulin G: Fc receptor I supercross-linking is a possible new mechanism of immunoglobulin G-dependent enhancement of type I allergic reactions. Clin. Exp. Allergy 35:774-81
    • (2005) Clin. Exp. Allergy , vol.35 , pp. 774-781
    • Sellge, G.1    Laffer, S.2    Mierke, C.3    Vrtala, S.4    Hoffmann, M.5
  • 142
    • 33748509524 scopus 로고    scopus 로고
    • The major glycoprotein allergen from Arachis hypogaea, Ara h 1, is a ligand of dendritic cell-specific ICAM-grabbing nonintegrin and acts as a Th2 adjuvant in vitro
    • Shreffler WG, Castro RR, Kucuk ZY, Charlop-Powers Z, Grishina G, et al. 2006. The major glycoprotein allergen from Arachis hypogaea, Ara h 1, is a ligand of dendritic cell-specific ICAM-grabbing nonintegrin and acts as a Th2 adjuvant in vitro. J. Immunol. 177:3677-85
    • (2006) J. Immunol. , vol.177 , pp. 3677-3685
    • Shreffler, W.G.1    Castro, R.R.2    Kucuk, Z.Y.3    Charlop-Powers, Z.4    Grishina, G.5
  • 143
    • 0035216171 scopus 로고    scopus 로고
    • Clinical implications of cross-reactive food allergens
    • Sicherer SH. 2001. Clinical implications of cross-reactive food allergens. J. Allergy Clin. Immunol. 108:881-90
    • (2001) J. Allergy Clin. Immunol. , vol.108 , pp. 881-890
    • Sicherer, S.H.1
  • 144
  • 146
    • 84895060304 scopus 로고    scopus 로고
    • Food allergy: Epidemiology, pathogenesis, diagnosis, and treatment
    • Sicherer SH, Sampson HA. 2014. Food allergy: epidemiology, pathogenesis, diagnosis, and treatment. J. Allergy Clin. Immunol. 133:291-307. E5
    • (2014) J. Allergy Clin. Immunol. , vol.133 , pp. 291-307e5
    • Sicherer, S.H.1    Sampson, H.A.2
  • 147
    • 78649866094 scopus 로고    scopus 로고
    • Maternal consumption of peanut during pregnancy is associated with peanut sensitization in atopic infants
    • Sicherer SH, Wood RA, StableinD, Lindblad R, Burks AW, et al. 2010. Maternal consumption of peanut during pregnancy is associated with peanut sensitization in atopic infants. J. Allergy Clin. Immunol. 126:1191-97
    • (2010) J. Allergy Clin. Immunol. , vol.126 , pp. 1191-1197
    • Sicherer, S.H.1    Wood, R.A.2    Stablein, D.3    Lindblad, R.4    Burks, A.W.5
  • 148
    • 56149106300 scopus 로고    scopus 로고
    • A population-based epidemiologic analysis of deaths from anaphylaxis in Florida
    • Simon M, Mulla Z. 2008. A population-based epidemiologic analysis of deaths from anaphylaxis in Florida. Allergy 63:1077-83
    • (2008) Allergy , vol.63 , pp. 1077-1083
    • Simon, M.1    Mulla, Z.2
  • 149
    • 84932159289 scopus 로고    scopus 로고
    • IgE reactivity to carbohydrate moieties of glycoproteins in wheat allergy
    • Song TW, Hong JY, Lee KE, Kim MN, Kim YH, et al. 2015. IgE reactivity to carbohydrate moieties of glycoproteins in wheat allergy. Allergy Asthma Proc. 36:192-99
    • (2015) Allergy Asthma Proc. , vol.36 , pp. 192-199
    • Song, T.W.1    Hong, J.Y.2    Lee, K.E.3    Kim, M.N.4    Kim, Y.H.5
  • 150
    • 38049009974 scopus 로고    scopus 로고
    • Immunoreactivity reduction of soybean meal by fermentation, effect on amino acid composition and antigenicity of commercial soy products
    • Song Y-S, Frías J, Martinez-Villaluenga C, Vidal-Valdeverde C, de Mejia EG. 2008. Immunoreactivity reduction of soybean meal by fermentation, effect on amino acid composition and antigenicity of commercial soy products. Food Chem. 108:571-81
    • (2008) Food Chem. , vol.108 , pp. 571-581
    • Song, Y.-S.1    Frías, J.2    Martinez-Villaluenga, C.3    Vidal-Valdeverde, C.4    De Mejia, E.G.5
  • 152
    • 33644638676 scopus 로고    scopus 로고
    • IgG-blocking antibodies inhibit IgE-mediated anaphylaxis in vivo through both antigen interception and FcRIIb cross-linking
    • Strait RT, Morris SC, Finkelman FD. 2006. IgG-blocking antibodies inhibit IgE-mediated anaphylaxis in vivo through both antigen interception and FcRIIb cross-linking. J. Clin. Investig. 116:833
    • (2006) J. Clin. Investig. , vol.116 , pp. 833
    • Strait, R.T.1    Morris, S.C.2    Finkelman, F.D.3
  • 153
    • 84887651097 scopus 로고    scopus 로고
    • A murine monoclonal antibody based enzyme-linked immunosorbent assay for almond (Prunus dulcis L.) detection
    • Su M, Venkatachalam M, Liu C, Zhang Y, Roux KH, Sathe SK. 2013. A murine monoclonal antibody based enzyme-linked immunosorbent assay for almond (Prunus dulcis L.) detection. J. Agric. Food Chem. 61:10823-33
    • (2013) J. Agric. Food Chem. , vol.61 , pp. 10823-10833
    • Su, M.1    Venkatachalam, M.2    Liu, C.3    Zhang, Y.4    Roux, K.H.5    Sathe, S.K.6
  • 154
    • 3242881045 scopus 로고    scopus 로고
    • Impact of irradiation and thermal processing on the antigenicity of almond, cashew nut and walnut proteins
    • Su M, Venkatachalam M, Teuber SS, Roux KH, Sathe SK. 2004. Impact of irradiation and thermal processing on the antigenicity of almond, cashew nut and walnut proteins. J. Sci. Food Agric. 84:1119-25
    • (2004) J. Sci. Food Agric. , vol.84 , pp. 1119-1125
    • Su, M.1    Venkatachalam, M.2    Teuber, S.S.3    Roux, K.H.4    Sathe, S.K.5
  • 155
    • 0027715015 scopus 로고
    • The human IgE network
    • Sutton B, Gould H. 1993. The human IgE network. Nature 366:421-28
    • (1993) Nature , vol.366 , pp. 421-428
    • Sutton, B.1    Gould, H.2
  • 156
    • 67049174179 scopus 로고    scopus 로고
    • Effects of heating and glycation of lactoglobulin on its recognition by IgE of sera from cow milk allergy patients
    • Taheri-Kafrani A, Gaudin J-C, Rabesona H, Nioi C, Agarwal D, et al. 2009. Effects of heating and glycation of lactoglobulin on its recognition by IgE of sera from cow milk allergy patients. J. Agric. Food Chem. 57:4974-82
    • (2009) J. Agric. Food Chem. , vol.57 , pp. 4974-4982
    • Taheri-Kafrani, A.1    Gaudin, J.-C.2    Rabesona, H.3    Nioi, C.4    Agarwal, D.5
  • 157
    • 74649085538 scopus 로고    scopus 로고
    • Effect of food matrix on amandin, almond (Prunus dulcis L.) major protein, immunorecognition and recovery
    • Tiwari RS, Venkatachalam M, Sharma GM, Su M, Roux KH, Sathe SK. 2010. Effect of food matrix on amandin, almond (Prunus dulcis L.) major protein, immunorecognition and recovery. LWT Food Sci. Technol. 43:675-83
    • (2010) LWT Food Sci. Technol. , vol.43 , pp. 675-683
    • Tiwari, R.S.1    Venkatachalam, M.2    Sharma, G.M.3    Su, M.4    Roux, K.H.5    Sathe, S.K.6
  • 158
  • 159
    • 44849119117 scopus 로고    scopus 로고
    • The role of protein digestibility and antacids on food allergy outcomes
    • Untersmayr E, Jensen-Jarolim E. 2008. The role of protein digestibility and antacids on food allergy outcomes. J. Allergy Clin. Immunol. 121:1301-8
    • (2008) J. Allergy Clin. Immunol. , vol.121 , pp. 1301-1308
    • Untersmayr, E.1    Jensen-Jarolim, E.2
  • 160
    • 0042234344 scopus 로고    scopus 로고
    • Antacid medication inhibits digestion of dietary proteins and causes food allergy: A fish allergy model in BALB/c mice
    • Untersmayr E, Schöll I, Swoboda I, Beil WJ, Förster-Waldl E, et al. 2003. Antacid medication inhibits digestion of dietary proteins and causes food allergy: a fish allergy model in BALB/c mice. J. Allergy Clin. Immunol. 112:616-23
    • (2003) J. Allergy Clin. Immunol. , vol.112 , pp. 616-623
    • Untersmayr, E.1    Schöll, I.2    Swoboda, I.3    Beil, W.J.4    Förster-Waldl, E.5
  • 161
    • 0032528813 scopus 로고    scopus 로고
    • Cutting edge: Selective deamidation by tissue transglutaminase strongly enhances gliadin-specific T cell reactivity
    • van de Wal Y, Kooy Y, van Veelen P, Peña S, Mearin L, et al. 1998. Cutting edge: selective deamidation by tissue transglutaminase strongly enhances gliadin-specific T cell reactivity. J. Immunol. 161:1585-88
    • (1998) J. Immunol. , vol.161 , pp. 1585-1588
    • Van De Wal, Y.1    Kooy, Y.2    Van Veelen, P.3    Peña, S.4    Mearin, L.5
  • 164
    • 34548228414 scopus 로고    scopus 로고
    • Food allergen detection methods and the challenge to protect food-allergic consumers
    • van Hengel AJ. 2007. Food allergen detection methods and the challenge to protect food-allergic consumers. Anal. Bioanal. Chem. 389:111-18
    • (2007) Anal. Bioanal. Chem. , vol.389 , pp. 111-118
    • Van Hengel, A.J.1
  • 165
    • 0036436846 scopus 로고    scopus 로고
    • Carbohydrate epitopes and their relevance for the diagnosis and treatment of allergic diseases
    • vanRee R. 2002. Carbohydrate epitopes and their relevance for the diagnosis and treatment of allergic diseases. Int. Arch. Allergy Immunol. 129:189-97
    • (2002) Int. Arch. Allergy Immunol. , vol.129 , pp. 189-197
    • VanRee, R.1
  • 167
    • 0037023969 scopus 로고    scopus 로고
    • Effects of roasting, blanching, autoclaving, andmicrowave heating on antigenicity of almond (Prunus dulcis L.) proteins
    • Venkatachalam M, Teuber S, Roux K, Sathe S. 2002. Effects of roasting, blanching, autoclaving, andmicrowave heating on antigenicity of almond (Prunus dulcis L.) proteins. J. Agric. Food Chem. 50:3544-48
    • (2002) J. Agric. Food Chem. , vol.50 , pp. 3544-3548
    • Venkatachalam, M.1    Teuber, S.2    Roux, K.3    Sathe, S.4
  • 168
    • 33644866520 scopus 로고    scopus 로고
    • Antigenic stability of pecan [Carya illinoinensis (Wangenh.) K. Koch] proteins: Effects of thermal treatments and in vitro digestion
    • Venkatachalam M, Teuber SS, Peterson WR, Roux KH, Sathe SK. 2006. Antigenic stability of pecan [Carya illinoinensis (Wangenh.) K. Koch] proteins: effects of thermal treatments and in vitro digestion. J. Agric. Food Chem. 54:1449-58
    • (2006) J. Agric. Food Chem. , vol.54 , pp. 1449-1458
    • Venkatachalam, M.1    Teuber, S.S.2    Peterson, W.R.3    Roux, K.H.4    Sathe, S.K.5
  • 169
    • 84924265336 scopus 로고    scopus 로고
    • Rapid and sensitive detection of the food allergen glycinin in powdered milk using a lateral flow colloidal gold immunoassay strip test
    • Wang Y, Deng R, Zhang G, Li Q, Yang J, et al. 2015. Rapid and sensitive detection of the food allergen glycinin in powdered milk using a lateral flow colloidal gold immunoassay strip test. J. Agric. Food Chem. 63:2172-78
    • (2015) J. Agric. Food Chem. , vol.63 , pp. 2172-2178
    • Wang, Y.1    Deng, R.2    Zhang, G.3    Li, Q.4    Yang, J.5
  • 172
    • 58149231381 scopus 로고    scopus 로고
    • Impact of native, heat-processed and encapsulated hazelnuts on the allergic response in hazelnut-allergic patients
    • WormM, Hompes S, FiedlerEM, Illner AK, ZuberbierT, Vieths S. 2009. Impact of native, heat-processed and encapsulated hazelnuts on the allergic response in hazelnut-allergic patients. Clin. Exp. Allergy 39:159-66
    • (2009) Clin. Exp. Allergy , vol.39 , pp. 159-166
    • Worm, M.1    Hompes, S.2    Fiedler, E.M.3    Illner, A.K.4    Zuberbier, T.5    Vieths, S.6
  • 173
    • 77952314827 scopus 로고    scopus 로고
    • Mapping of a conformational epitope on the cashew allergen Ana o 2: A discontinuous large subunit epitope dependent upon homologous or heterologous small subunit association
    • Xia L, Willison LN, Porter L, Robotham JM, Teuber SS, et al. 2010. Mapping of a conformational epitope on the cashew allergen Ana o 2: a discontinuous large subunit epitope dependent upon homologous or heterologous small subunit association. Mol. Immunol. 47:1808-16
    • (2010) Mol. Immunol. , vol.47 , pp. 1808-1816
    • Xia, L.1    Willison, L.N.2    Porter, L.3    Robotham, J.M.4    Teuber, S.S.5
  • 175
    • 85009636634 scopus 로고    scopus 로고
    • Micro-assay method for evaluating the allergenicity of the major soybean allergen, Gly m Bd 30K, with mouse antiserum and RBL-2H3 cells
    • Yamanishi R, Tsuji H, Bando N, Yoshimoto I, Ogawa T. 1997. Micro-assay method for evaluating the allergenicity of the major soybean allergen, Gly m Bd 30K, with mouse antiserum and RBL-2H3 cells. Biosci. Biotechnol. Biochem. 61:19-23
    • (1997) Biosci. Biotechnol. Biochem. , vol.61 , pp. 19-23
    • Yamanishi, R.1    Tsuji, H.2    Bando, N.3    Yoshimoto, I.4    Ogawa, T.5
  • 176
    • 84875624574 scopus 로고    scopus 로고
    • Effects of Maillard reaction on allergenicity of buckwheat allergen Fag t 3 during thermal processing
    • Yang ZH, Li C, Li YY, Wang ZH. 2013. Effects of Maillard reaction on allergenicity of buckwheat allergen Fag t 3 during thermal processing. J. Sci. Food Agric. 93:1510-15
    • (2013) J. Sci. Food Agric. , vol.93 , pp. 1510-1515
    • Yang, Z.H.1    Li, C.2    Li, Y.Y.3    Wang, Z.H.4
  • 177
    • 84924853575 scopus 로고    scopus 로고
    • Study on reducing antigenic response and IgE-binding inhibitions of four milk proteins of Lactobacillus casei 1134
    • YaoM, Xu Q, Luo Y, Shi J, Li Z. 2015. Study on reducing antigenic response and IgE-binding inhibitions of four milk proteins of Lactobacillus casei 1134. J. Sci. Food Agric. 95:1303-12
    • (2015) J. Sci. Food Agric. , vol.95 , pp. 1303-1312
    • Yao, M.1    Xu, Q.2    Luo, Y.3    Shi, J.4    Li, Z.5
  • 178
    • 79952454516 scopus 로고    scopus 로고
    • Effects of different processing methods on digestibility of Scylla paramamosain allergen (tropomyosin)
    • Yu H-L, Cao M-J, Cai Q-F, Weng W-Y, Su W-J, Liu G-M. 2011. Effects of different processing methods on digestibility of Scylla paramamosain allergen (tropomyosin). Food Chem. Toxicol. 49:791-98
    • (2011) Food Chem. Toxicol. , vol.49 , pp. 791-798
    • Yu, H.-L.1    Cao, M.-J.2    Cai, Q.-F.3    Weng, W.-Y.4    Su, W.-J.5    Liu, G.-M.6
  • 179
    • 84921632636 scopus 로고    scopus 로고
    • Allergenicity of roasted peanuts treated with a non-human digestive protease
    • Yu J, Hernandez M, Li H, Goktepe I, Robinette C, et al. 2015. Allergenicity of roasted peanuts treated with a non-human digestive protease. Food Res. Int. 69:341-47
    • (2015) Food Res. Int. , vol.69 , pp. 341-347
    • Yu, J.1    Hernandez, M.2    Li, H.3    Goktepe, I.4    Robinette, C.5
  • 181
    • 36348936097 scopus 로고    scopus 로고
    • Effect of high-pressure treatment on in-vitro digestibility of lactoglobulin
    • Zeece M, Huppertz T, Kelly A. 2008. Effect of high-pressure treatment on in-vitro digestibility of lactoglobulin. Innov. Food Sci. Emerg. Technol. 9:62-69
    • (2008) Innov. Food Sci. Emerg. Technol. , vol.9 , pp. 62-69
    • Zeece, M.1    Huppertz, T.2    Kelly, A.3
  • 182
    • 80052819877 scopus 로고    scopus 로고
    • Epitope mapping of a 95 kDa antigen in complex with antibody by solution-phase amide backbone hydrogen/deuterium exchange monitored by Fourier transform ion cyclotron resonance mass spectrometry
    • Zhang Q, Willison LN, Tripathi P, Sathe SK, Roux KH, et al. 2011. Epitope mapping of a 95 kDa antigen in complex with antibody by solution-phase amide backbone hydrogen/deuterium exchange monitored by Fourier transform ion cyclotron resonance mass spectrometry. Anal. Chem. 83:7129-36
    • (2011) Anal. Chem. , vol.83 , pp. 7129-7136
    • Zhang, Q.1    Willison, L.N.2    Tripathi, P.3    Sathe, S.K.4    Roux, K.H.5
  • 183
    • 84914166036 scopus 로고    scopus 로고
    • Detection of peanut (Arachis hypogaea) allergen by real-time PCR method with internal amplification control
    • ZhangW-J, Cai Q, Guan X, Chen Q. 2015. Detection of peanut (Arachis hypogaea) allergen by real-time PCR method with internal amplification control. Food Chem. 174:547-52
    • (2015) Food Chem. , vol.174 , pp. 547-552
    • ZhangW, J.1    Cai, Q.2    Guan, X.3    Chen, Q.4
  • 184
    • 84862788671 scopus 로고    scopus 로고
    • Rapid detection of fish major allergen parvalbumin using superparamagnetic nanoparticle-based lateral flow immunoassay
    • Zheng C, Wang X, Lu Y, Liu Y. 2012. Rapid detection of fish major allergen parvalbumin using superparamagnetic nanoparticle-based lateral flow immunoassay. Food Control 26:446-52
    • (2012) Food Control , vol.26 , pp. 446-452
    • Zheng, C.1    Wang, X.2    Lu, Y.3    Liu, Y.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.