메뉴 건너뛰기




Volumn , Issue , 2008, Pages 219-235

Food allergens

Author keywords

[No Author keywords available]

Indexed keywords

ALLERGEN;

EID: 58149462857     PISSN: None     EISSN: None     Source Type: Book    
DOI: None     Document Type: Chapter
Times cited : (10)

References (146)
  • 1
  • 3
    • 34047122018 scopus 로고    scopus 로고
    • Further fatalities caused by anaphylactic reactions to food, 2001-2006
    • Bock SA, Munoz-Furlong A, Sampson HA. Further fatalities caused by anaphylactic reactions to food, 2001-2006. J Allergy Clin Immunol 2007; 119: 1016-1018.
    • (2007) J Allergy Clin Immunol , vol.119 , pp. 1016-1018
    • Bock, S.A.1    Munoz-Furlong, A.2    Sampson, H.A.3
  • 4
    • 85057400765 scopus 로고    scopus 로고
    • Further fatalities caused by anaphylactic reactions to food, 2001-2006
    • Pumphrey RSH, Gowland MH. Further fatalities caused by anaphylactic reactions to food, 2001-2006. J Allergy Clin Immunol 119: 118-119.
    • J Allergy Clin Immunol , vol.119 , pp. 118-119
    • Pumphrey, R.S.H.1    Gowland, M.H.2
  • 5
    • 0346995202 scopus 로고    scopus 로고
    • Prevalence of peanut and tree nut allergy in the United States determined by means of a random digit dial telephone survey
    • Sicherer SH, Munoz-Furlong A, Sampson HA. Prevalence of peanut and tree nut allergy in the United States determined by means of a random digit dial telephone survey. J Allergy Clin Immunol 2003; 112: 1203-1207.
    • (2003) J Allergy Clin Immunol , vol.112 , pp. 1203-1207
    • Sicherer, S.H.1    Munoz-Furlong, A.2    Sampson, H.A.3
  • 6
    • 34249811772 scopus 로고    scopus 로고
    • Advances in allergic skin disease, anaphylaxis, and hypersensitivity reactions to foods, drugs, and insects
    • Sicherer SH, Leung DYM. Advances in allergic skin disease, anaphylaxis, and hypersensitivity reactions to foods, drugs, and insects. J Allergy Clin Immunol 2007; 119: 1463-1469.
    • (2007) J Allergy Clin Immunol , vol.119 , pp. 1463-1469
    • Sicherer, S.H.1    Leung, D.Y.M.2
  • 7
    • 0038321352 scopus 로고    scopus 로고
    • The natural history of food allergy
    • Wood RA. The natural history of food allergy. Pediatrics 2003; 111: 1631-1637.
    • (2003) Pediatrics , vol.111 , pp. 1631-1637
    • Wood, R.A.1
  • 9
    • 21844446378 scopus 로고    scopus 로고
    • Allergic reactions in the community: A questionnaire survey of members of the anaphylaxis campaign
    • Uguz A, Lack G, Pumphrey R, et al. Allergic reactions in the community: a questionnaire survey of members of the anaphylaxis campaign. Clin Exp Allergy 2005; 35: 746-750.
    • (2005) Clin Exp Allergy , vol.35 , pp. 746-750
    • Uguz, A.1    Lack, G.2    Pumphrey, R.3
  • 10
    • 1142273126 scopus 로고    scopus 로고
    • Multicenter study of emergency department visits for food allergies
    • Clark S, Bock SA, Gaeta TJ, et al. Multicenter study of emergency department visits for food allergies. J Allergy Clin Immunol 2004; 113: 346-352.
    • (2004) J Allergy Clin Immunol , vol.113 , pp. 346-352
    • Clark, S.1    Bock, S.A.2    Gaeta, T.J.3
  • 11
    • 2342635826 scopus 로고    scopus 로고
    • Patterns of anaphylaxis: Acute and late phase features of allergic reactions
    • Golden DB. Patterns of anaphylaxis: acute and late phase features of allergic reactions. Novartis Found Symp 2004; 257: 101-115.
    • (2004) Novartis Found Symp , vol.257 , pp. 101-115
    • Golden, D.B.1
  • 12
    • 20444452784 scopus 로고    scopus 로고
    • Does absorption across the buccal mucosa explain early onset of food-induced allergic systemic reactions
    • Dirks CG, Pedersen MH, Platzer MH, et al. Does absorption across the buccal mucosa explain early onset of food-induced allergic systemic reactions. J Allergy Clin Immunol 2005; 115: 1321-1323.
    • (2005) J Allergy Clin Immunol , vol.115 , pp. 1321-1323
    • Dirks, C.G.1    Pedersen, M.H.2    Platzer, M.H.3
  • 13
    • 21844458478 scopus 로고    scopus 로고
    • Epicutaneous exposure to peanut protein prevents oral tolerance and enhances allergic sensitization
    • Strid J, Hourihane J, Kimber I, et al. Epicutaneous exposure to peanut protein prevents oral tolerance and enhances allergic sensitization. Clin Exp Allergy 2005; 35(6): 757-766.
    • (2005) Clin Exp Allergy , vol.35 , Issue.6 , pp. 757-766
    • Strid, J.1    Hourihane, J.2    Kimber, I.3
  • 14
    • 8844269282 scopus 로고    scopus 로고
    • Rapid in vivo transport of proteins from digested allergens across pre-sensitized gut
    • Chambers SJ, Wickman MS, Regoi M, et al. Rapid in vivo transport of proteins from digested allergens across pre-sensitized gut. Biochem Biophys Res Commun 2004; 325: 1258-1263.
    • (2004) Biochem Biophys Res Commun , vol.325 , pp. 1258-1263
    • Chambers, S.J.1    Wickman, M.S.2    Regoi, M.3
  • 15
    • 27744593458 scopus 로고    scopus 로고
    • Food safety: In vitro digestion tests are non-predictive for allergenic potential of food in stomach insufficiency
    • Jensen-Jarolim E, Untersmayr E. Food safety: in vitro digestion tests are non-predictive for allergenic potential of food in stomach insufficiency. Immunol Lett 2006; 102: 118-119.
    • (2006) Immunol Lett , vol.102 , pp. 118-119
    • Jensen-Jarolim, E.1    Untersmayr, E.2
  • 17
  • 18
    • 12244250129 scopus 로고    scopus 로고
    • Molecular and immunological characterization of profilin from mugwort pollen
    • Wopfner N, Willeroidee M, Hebenstreit D, et al. Molecular and immunological characterization of profilin from mugwort pollen. Biol Chem 2002; 383(11): 1779-1789.
    • (2002) Biol Chem , vol.383 , Issue.11 , pp. 1779-1789
    • Wopfner, N.1    Willeroidee, M.2    Hebenstreit, D.3
  • 19
    • 0036048803 scopus 로고    scopus 로고
    • A new oligomeric parvalbumin allergen of Atlantic cod (Gad m I) encoded by a gene distinct from that of Gad c I
    • Das Dores S, Chopin C, Villaume C, et al. A new oligomeric parvalbumin allergen of Atlantic cod (Gad m I) encoded by a gene distinct from that of Gad c I. Allergy 2002; 57(suppl 72): 79-83.
    • (2002) Allergy , vol.57 , pp. 79-83
    • Das Dores, S.1    Chopin, C.2    Villaume, C.3
  • 20
    • 33749671702 scopus 로고    scopus 로고
    • Allergen Ara h 1 occurs in peanuts as a large oligomer rather than as a trimer
    • van Boxtel EL, van Beers MM, Koppelman SJ, et al. Allergen Ara h 1 occurs in peanuts as a large oligomer rather than as a trimer. J Agric Food Chem 2006; 54(19): 7180-7186.
    • (2006) J Agric Food Chem , vol.54 , Issue.19 , pp. 7180-7186
    • van Boxtel, E.L.1    van Beers, M.M.2    Koppelman, S.J.3
  • 21
  • 22
    • 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, et al. Structural relatedness of plant food allergens with specific reference to cross-reactive allergens: an in silico analysis. J Allergy Clin Immunol 2005; 115: 163-170.
    • (2005) J Allergy Clin Immunol , vol.115 , pp. 163-170
    • Jenkins, J.A.1    Griffiths-Jones, S.2    Shewry, P.R.3
  • 24
    • 2342591290 scopus 로고    scopus 로고
    • Revised nomenclature for allergy for global use: Report of the Nomenclature Review Committee of the World Allergy Organization, October, 2003
    • Johansson SG, Bieber T, Dahl R, et al. Revised nomenclature for allergy for global use: report of the Nomenclature Review Committee of the World Allergy Organization, October, 2003. J Allergy Clin Immunol 2004; 113: 832-836.
    • (2004) J Allergy Clin Immunol , vol.113 , pp. 832-836
    • Johansson, S.G.1    Bieber, T.2    Dahl, R.3
  • 26
    • 34248138941 scopus 로고    scopus 로고
    • Lipid transfer protein allergy: Primary food allergy or pollen/food syndrome in some cases
    • Zuidmeer L, van Rhee R. Lipid transfer protein allergy: primary food allergy or pollen/food syndrome in some cases. Curr Opin Allergy Clin Immunol 2007; 7: 269-273.
    • (2007) Curr Opin Allergy Clin Immunol , vol.7 , pp. 269-273
    • Zuidmeer, L.1    van Rhee, R.2
  • 27
    • 85057392195 scopus 로고    scopus 로고
    • Downloaded from AllFam version of May 5
    • AllFAm allergen family chart. Downloaded from AllFam version of May 5, 2007. Available at: http://www.meduniwien.ac.at/allergens/allfam/.
    • (2007) AllFAm allergen family chart
  • 28
    • 34548260617 scopus 로고    scopus 로고
    • The AllFam database-a resource for classifying allergenic proteins
    • Radauer C, Marl A, Breiteneder H. The AllFam database-a resource for classifying allergenic proteins. Allergy 2007; 62(suppl 83): 154.
    • (2007) Allergy , vol.62 , pp. 154
    • Radauer, C.1    Marl, A.2    Breiteneder, H.3
  • 29
    • 0031966706 scopus 로고    scopus 로고
    • Immune responses to dietary antigens: Oral tolerance
    • Strobel S, Mowat AM. Immune responses to dietary antigens: oral tolerance. Immunol Today 1998; 19(4): 173-181.
    • (1998) Immunol Today , vol.19 , Issue.4 , pp. 173-181
    • Strobel, S.1    Mowat, A.M.2
  • 30
    • 0036424566 scopus 로고    scopus 로고
    • Identification of sequential IgE-binding epitopes on bovine alpha(s2)- casein in cow’s milk allergic patients
    • Busse PJ, Jarvinen KM, Vila L, et al. Identification of sequential IgE-binding epitopes on bovine alpha(s2)- casein in cow’s milk allergic patients. Int Arch Allergy Immunol 2002; 129: 93-96.
    • (2002) Int Arch Allergy Immunol , vol.129 , pp. 93-96
    • Busse, P.J.1    Jarvinen, K.M.2    Vila, L.3
  • 31
    • 0035208510 scopus 로고    scopus 로고
    • IgE and IgG binding epitopes on alpha-lactalbumin and beta-lactoglobulin in cow’s milk allergy
    • Jarvinen KM, Chatchatee P, Bardina L, et al. IgE and IgG binding epitopes on alpha-lactalbumin and beta-lactoglobulin in cow’s milk allergy. Int Arch Allergy Immunol 2001; 126(2): 111-118.
    • (2001) Int Arch Allergy Immunol , vol.126 , Issue.2 , pp. 111-118
    • Jarvinen, K.M.1    Chatchatee, P.2    Bardina, L.3
  • 32
    • 0036676859 scopus 로고    scopus 로고
    • B-cell epitopes as a screening instrument for persistent cow’s milk allergy
    • Jarvinen KM, Beyer K, Vila L, et al. B-cell epitopes as a screening instrument for persistent cow’s milk allergy. J Allergy Clin Immunol 2002; 110(2): 293-297.
    • (2002) J Allergy Clin Immunol , vol.110 , Issue.2 , pp. 293-297
    • Jarvinen, K.M.1    Beyer, K.2    Vila, L.3
  • 33
    • 0035113608 scopus 로고    scopus 로고
    • Identification of IgE- and IgG-binding epitopes on alpha (s1)-casein: Differences in patients with persistent and transient cow’s milk allergy
    • Chatchatee P, Jarvinen KM, Bardina L, et al. Identification of IgE- and IgG-binding epitopes on alpha (s1)-casein: differences in patients with persistent and transient cow’s milk allergy. J Allergy Clin Immunol 2001; 107(2): 379-383.
    • (2001) J Allergy Clin Immunol , vol.107 , Issue.2 , pp. 379-383
    • Chatchatee, P.1    Jarvinen, K.M.2    Bardina, L.3
  • 34
    • 0036157496 scopus 로고    scopus 로고
    • Factors affecting the determination of threshold doses for allergenic foods: How much is too much?
    • Taylor SL, Hefle SL, Bindslev-Jensen C, et al. Factors affecting the determination of threshold doses for allergenic foods: how much is too much? J Allergy Clin Immunol 2002; 109: 24-30.
    • (2002) J Allergy Clin Immunol , vol.109 , pp. 24-30
    • Taylor, S.L.1    Hefle, S.L.2    Bindslev-Jensen, C.3
  • 35
    • 0041620647 scopus 로고    scopus 로고
    • Thresholds of clinical reactivity to milk, egg, peanut, and sesame in immunoglobulin E-dependent allergies: Evaluation by double-blind or singleblind placebo-controlled oral challenges
    • Morisset M, Moneret-Vautrin DA, Kanny G, et al. Thresholds of clinical reactivity to milk, egg, peanut, and sesame in immunoglobulin E-dependent allergies: evaluation by double-blind or singleblind placebo-controlled oral challenges. Clin Exp Allergy 2003; 33: 1046-1051.
    • (2003) Clin Exp Allergy , vol.33 , pp. 1046-1051
    • Morisset, M.1    Moneret-Vautrin, D.A.2    Kanny, G.3
  • 36
  • 37
    • 0021815002 scopus 로고
    • Allergens in the white and yolk of hen’s egg. A study of IgE binding by egg proteins
    • Anet J, Back JF, Baker RS, et al. Allergens in the white and yolk of hen’s egg. A study of IgE binding by egg proteins. Int Arch Allergy Appl Immunol 1985; 77(3): 364-371.
    • (1985) Int Arch Allergy Appl Immunol , vol.77 , Issue.3 , pp. 364-371
    • Anet, J.1    Back, J.F.2    Baker, R.S.3
  • 38
    • 0020598226 scopus 로고
    • Immunochemical identification of the allergens in egg white
    • Hoffman DR. Immunochemical identification of the allergens in egg white. J Allergy Clin Immunol 1983; 71(5): 481-486.
    • (1983) J Allergy Clin Immunol , vol.71 , Issue.5 , pp. 481-486
    • Hoffman, D.R.1
  • 39
    • 0028276761 scopus 로고
    • Allergenicity and antigenicity of chicken egg ovomucoid (Gal d III) compared with ovalbumin (Gal d I) in children with egg allergy and in mice
    • Bernhisel-Broadbent J, Dintzis HM, Dintzis RZ, et al. Allergenicity and antigenicity of chicken egg ovomucoid (Gal d III) compared with ovalbumin (Gal d I) in children with egg allergy and in mice. J Allergy Clin Immunol 1994; 93(6): 1047-1059.
    • (1994) J Allergy Clin Immunol , vol.93 , Issue.6 , pp. 1047-1059
    • Bernhisel-Broadbent, J.1    Dintzis, H.M.2    Dintzis, R.Z.3
  • 40
    • 0036288997 scopus 로고    scopus 로고
    • Identification and fine mapping of IgG and IgE epitopes in ovomucoid
    • Mine Y, Wei ZJ. Identification and fine mapping of IgG and IgE epitopes in ovomucoid. Biochem Biophys Res Commun 2002; 292(4): 1070-1074.
    • (2002) Biochem Biophys Res Commun , vol.292 , Issue.4 , pp. 1070-1074
    • Mine, Y.1    Wei, Z.J.2
  • 41
    • 26944492664 scopus 로고    scopus 로고
    • Detection of four distinct groups of hen egg allergens binding IgE in sera of children with egg allergy
    • Walsh BJ, Hill DJ, Macoun P, et al. Detection of four distinct groups of hen egg allergens binding IgE in sera of children with egg allergy. Allergol Immunopathol (Madrid) 2005; 33: 183-191.
    • (2005) Allergol Immunopathol (Madrid) , vol.33 , pp. 183-191
    • Walsh, B.J.1    Hill, D.J.2    Macoun, P.3
  • 43
    • 0032565379 scopus 로고    scopus 로고
    • Resolution of peanut allergy: Case-control study
    • Hourihane JO, Roberts SA, Warner JO. Resolution of peanut allergy: case-control study. Br Med J 1998; 316: 1271-1275.
    • (1998) Br Med J , vol.316 , pp. 1271-1275
    • Hourihane, J.O.1    Roberts, S.A.2    Warner, J.O.3
  • 45
    • 0028807372 scopus 로고
    • Recombinant peanut allergen Ara h I expression and IgE binding in patients with peanut hypersensitivity
    • Burks AW, Cockrell G, Stanley JS, et al. Recombinant peanut allergen Ara h I expression and IgE binding in patients with peanut hypersensitivity. J Clin Invest 1995; 96(4): 1715-1721.
    • (1995) J Clin Invest , vol.96 , Issue.4 , pp. 1715-1721
    • Burks, A.W.1    Cockrell, G.2    Stanley, J.S.3
  • 46
    • 0036284952 scopus 로고    scopus 로고
    • Modification of peanut allergen Ara h 3: Effects on IgE binding and T cell stimulation
    • Rabjohn P, West CM, Connaughton C, et al. Modification of peanut allergen Ara h 3: effects on IgE binding and T cell stimulation. Int Arch Allergy Immunol 2002; 128(1): 15-23.
    • (2002) Int Arch Allergy Immunol , vol.128 , Issue.1 , pp. 15-23
    • Rabjohn, P.1    West, C.M.2    Connaughton, C.3
  • 47
    • 0033557358 scopus 로고    scopus 로고
    • Molecular cloning and epitope analysis of the peanut allergen Ara h 3
    • Rabjohn P, Helm EM, Stanley JS, et al. Molecular cloning and epitope analysis of the peanut allergen Ara h 3. J Clin Invest 1999; 103(4): 535-542.
    • (1999) J Clin Invest , vol.103 , Issue.4 , pp. 535-542
    • Rabjohn, P.1    Helm, E.M.2    Stanley, J.S.3
  • 48
    • 19044376267 scopus 로고    scopus 로고
    • Comparative potency of Ara h 1 and Ara h 2 in immunochemical and functional assays of allergenicity
    • Palmer GW, Dibbern DA, Burks AW, et al. Comparative potency of Ara h 1 and Ara h 2 in immunochemical and functional assays of allergenicity. Clin Immunol 2005; 115: 302-312.
    • (2005) Clin Immunol , vol.115 , pp. 302-312
    • Palmer, G.W.1    Dibbern, D.A.2    Burks, A.W.3
  • 49
    • 33748509524 scopus 로고    scopus 로고
    • The major glycoprotein form Arachis hyogaea, 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, et al. The major glycoprotein form Arachis hyogaea, Ara h 1, is a ligand of dendritic cell-specific ICAM-grabbing nonintegrin and acts as a Th2 adjuvant in vitro. J Immunol 2006; 177: 3677-3685.
    • (2006) J Immunol , vol.177 , pp. 3677-3685
    • Shreffler, W.G.1    Castro, R.R.2    Kucuk, Z.Y.3
  • 51
    • 1942467835 scopus 로고    scopus 로고
    • Microarray immunoassay: Association of clinical history, in vitro IgE function, and heterogeneity of allergenic peanut epitopes
    • Shreffler WG, Beyer K, Chu TH, et al. Microarray immunoassay: association of clinical history, in vitro IgE function, and heterogeneity of allergenic peanut epitopes. J Allergy Clin Immunol 2004; 113: 776-782.
    • (2004) J Allergy Clin Immunol , vol.113 , pp. 776-782
    • Shreffler, W.G.1    Beyer, K.2    Chu, T.H.3
  • 52
    • 25844440962 scopus 로고    scopus 로고
    • IgE and IgG4 epitope mapping by microarray immunoassay reveals the diversity of immune response to the peanut allergen Ara h 2
    • Shreffler WG, Lencer DA, Bardina L, et al. IgE and IgG4 epitope mapping by microarray immunoassay reveals the diversity of immune response to the peanut allergen Ara h 2. J Allergy Clin Immunol 2005; 116: 893-899.
    • (2005) J Allergy Clin Immunol , vol.116 , pp. 893-899
    • Shreffler, W.G.1    Lencer, D.A.2    Bardina, L.3
  • 54
    • 0023891803 scopus 로고
    • Allergenicity of major component proteins of soybean determined by enzyme-linked immunosorbent assay (ELISA) and immunoblotting in children with atopic dermatitis and positive soy challenges
    • Burks AW Jr., Brooks JR, Sampson HA. Allergenicity of major component proteins of soybean determined by enzyme-linked immunosorbent assay (ELISA) and immunoblotting in children with atopic dermatitis and positive soy challenges. J Allergy Clin Immunol 1988; 81(6): 1135-1142.
    • (1988) J Allergy Clin Immunol , vol.81 , Issue.6 , pp. 1135-1142
    • Burks, A.W.1    Brooks, J.R.2    Sampson, H.A.3
  • 55
    • 0034526947 scopus 로고    scopus 로고
    • Soybean allergens and hypoallergenic soybean products
    • Ogawa A, Samoto M, Takahashi K. Soybean allergens and hypoallergenic soybean products. J Nutr Sci Vitaminol (Tokyo) 2000; 46(6): 271-279.
    • (2000) J Nutr Sci Vitaminol (Tokyo) , vol.46 , Issue.6 , pp. 271-279
    • Ogawa, A.1    Samoto, M.2    Takahashi, K.3
  • 56
    • 0027620748 scopus 로고
    • Identification of the soybean allergenic protein, Gly m Bd 30K, with the soybean seed 34-kDa oil-body-associated protein
    • Ogawa T, Tsuji H, Bando N, et al. Identification of the soybean allergenic protein, Gly m Bd 30K, with the soybean seed 34-kDa oil-body-associated protein. Biosci Biotechnol Biochem 1993; 57(6): 1030-1033.
    • (1993) Biosci Biotechnol Biochem , vol.57 , Issue.6 , pp. 1030-1033
    • Ogawa, T.1    Tsuji, H.2    Bando, N.3
  • 57
    • 33847305451 scopus 로고    scopus 로고
    • Allergenicity of soybean: New developments in identification of allergenic proteins, cross-reactivities and hypoallergenization technologies
    • L’Hocine L, Boye JI. Allergenicity of soybean: new developments in identification of allergenic proteins, cross-reactivities and hypoallergenization technologies. Crit Rev Food Sci Nutr 2007; 47: 127-143.
    • (2007) Crit Rev Food Sci Nutr , vol.47 , pp. 127-143
    • L’Hocine, L.1    Boye, J.I.2
  • 58
    • 0020043431 scopus 로고
    • Immunoglobulin E antibodies to ingested cereal flour components: Studies with sera from subjects with asthma and eczema
    • Sutton R, Hill DJ, Baldo BA, et al. Immunoglobulin E antibodies to ingested cereal flour components: studies with sera from subjects with asthma and eczema. Clin Allergy 1982; 12(1): 63-74.
    • (1982) Clin Allergy , vol.12 , Issue.1 , pp. 63-74
    • Sutton, R.1    Hill, D.J.2    Baldo, B.A.3
  • 59
    • 0029144520 scopus 로고
    • Immunologic cross-reactivity among cereal grains and grasses in children with food hypersensitivity
    • Jones SM, Magnolfi CF, Cooke SK, et al. Immunologic cross-reactivity among cereal grains and grasses in children with food hypersensitivity. J Allergy Clin Immunol 1995; 96(3): 341-351.
    • (1995) J Allergy Clin Immunol , vol.96 , Issue.3 , pp. 341-351
    • Jones, S.M.1    Magnolfi, C.F.2    Cooke, S.K.3
  • 60
    • 0030869287 scopus 로고    scopus 로고
    • Comparison of pediatric and adult IgE antibody binding to fish proteins
    • James JM, Helm RM, Burks AW, et al. Comparison of pediatric and adult IgE antibody binding to fish proteins. Ann Allergy Asthma Immunol 1997; 79(2): 131-137.
    • (1997) Ann Allergy Asthma Immunol , vol.79 , Issue.2 , pp. 131-137
    • James, J.M.1    Helm, R.M.2    Burks, A.W.3
  • 61
    • 0037486873 scopus 로고    scopus 로고
    • Food allergy to wheat: Identification of immunoglobulin Eand immunoglobulin G-binding proteins with sequential extracts and purified proteins from wheat flour
    • Battais F, Pineau F, Popineau Y, et al. Food allergy to wheat: identification of immunoglobulin Eand immunoglobulin G-binding proteins with sequential extracts and purified proteins from wheat flour. Clin Exp Allergy 2003; 33: 962-970.
    • (2003) Clin Exp Allergy , vol.33 , pp. 962-970
    • Battais, F.1    Pineau, F.2    Popineau, Y.3
  • 62
    • 20044372929 scopus 로고    scopus 로고
    • Identification of IgE-binding epitopes on gliadins for patients with food allergy to wheat
    • Battais F, Mothes T, Moneret-Vautrin DA, et al. Identification of IgE-binding epitopes on gliadins for patients with food allergy to wheat. Allergy 2005; 60: 815-821.
    • (2005) Allergy , vol.60 , pp. 815-821
    • Battais, F.1    Mothes, T.2    Moneret-Vautrin, D.A.3
  • 65
    • 32944455362 scopus 로고    scopus 로고
    • Seafood allergy: Lessons from clinical symptoms, immunological mechanisms and molecular biology
    • Chua KH, Tang CY, Wu A, et al. Seafood allergy: lessons from clinical symptoms, immunological mechanisms and molecular biology. Adv Biochem Eng Biotechnol 2005; 97: 205-235.
    • (2005) Adv Biochem Eng Biotechnol , vol.97 , pp. 205-235
    • Chua, K.H.1    Tang, C.Y.2    Wu, A.3
  • 66
    • 0013869138 scopus 로고
    • Studies of hypersensitivity to fish. A clinical study
    • Aas K. Studies of hypersensitivity to fish. A clinical study. Int Arch Allergy Appl Immunol 1966; 29(4): 346-363.
    • (1966) Int Arch Allergy Appl Immunol , vol.29 , Issue.4 , pp. 346-363
    • Aas, K.1
  • 67
    • 66349136713 scopus 로고    scopus 로고
    • Identification of major allergens of two species of local snappers: Lutjanus argentimaculatus (mera/red snapper) and Lutjanus johnii (janahak/golden snapper)
    • Rosmilah M, Shahnaz M, Masita A, et al. Identification of major allergens of two species of local snappers: Lutjanus argentimaculatus (mera/red snapper) and Lutjanus johnii (janahak/golden snapper). Trop Biomed 2005; 22: 171-177.
    • (2005) Trop Biomed , vol.22 , pp. 171-177
    • Rosmilah, M.1    Shahnaz, M.2    Masita, A.3
  • 68
    • 0020566441 scopus 로고
    • Immunochemical analysis of cod fish allergen M: Locations of the immunoglobulin binding sites as demonstrated by the native and synthetic peptides
    • Elsayed S, Apol J. Immunochemical analysis of cod fish allergen M: locations of the immunoglobulin binding sites as demonstrated by the native and synthetic peptides. Allergy 1983; 38: 449-459.
    • (1983) Allergy , vol.38 , pp. 449-459
    • Elsayed, S.1    Apol, J.2
  • 69
    • 33747243428 scopus 로고    scopus 로고
    • Changes in the allergenicity during different preparations of pomfret, hilsa, bhetki and mackerel fish as illustrated by enzyme-linked immunosorbent assay and immunoblotting
    • Chatterjee U, Mondal G, Chakraborti P, et al. Changes in the allergenicity during different preparations of pomfret, hilsa, bhetki and mackerel fish as illustrated by enzyme-linked immunosorbent assay and immunoblotting. Int Arch Allergy Immunol 2006; 141: 1-10.
    • (2006) Int Arch Allergy Immunol , vol.141 , pp. 1-10
    • Chatterjee, U.1    Mondal, G.2    Chakraborti, P.3
  • 70
    • 0025329241 scopus 로고
    • Characterization of water-soluble shrimp allergens released during boiling
    • Lehrer SB, Ibanez MD, McCants ML, et al. Characterization of water-soluble shrimp allergens released during boiling. J Allergy Clin Immunol 1990; 85(6): 1005-1013.
    • (1990) J Allergy Clin Immunol , vol.85 , Issue.6 , pp. 1005-1013
    • Lehrer, S.B.1    Ibanez, M.D.2    McCants, M.L.3
  • 71
    • 0023551257 scopus 로고
    • Immunologic evaluation of shrimp-allergic individuals
    • Daul CB, Morgan JE, Waring NP, et al. Immunologic evaluation of shrimp-allergic individuals. J Allergy Clin Immunol 1987; 80(5): 716-722.
    • (1987) J Allergy Clin Immunol , vol.80 , Issue.5 , pp. 716-722
    • Daul, C.B.1    Morgan, J.E.2    Waring, N.P.3
  • 72
    • 0036121086 scopus 로고    scopus 로고
    • Identification of continuous, allergenic regions of the major shrimp allergen Pen a 1 (tropomysin)
    • Ayuso R, Lehrer SB, Reese G. Identification of continuous, allergenic regions of the major shrimp allergen Pen a 1 (tropomysin). Int Arch Allergy Immunol 2002; 127(1): 27-37.
    • (2002) Int Arch Allergy Immunol , vol.127 , Issue.1 , pp. 27-37
    • Ayuso, R.1    Lehrer, S.B.2    Reese, G.3
  • 73
    • 0035947028 scopus 로고    scopus 로고
    • Characterization and identification of allergen epitopes: Recombinant peptide libraries and synthetic, overlapping peptides
    • Reese G, Ayuso R, Leong-Kee SM, et al. Characterization and identification of allergen epitopes: recombinant peptide libraries and synthetic, overlapping peptides. J Chromatogr B Biomed Sci Appl 2001; 756(1-2): 157-163.
    • (2001) J Chromatogr B Biomed Sci Appl , vol.756 , Issue.1-2 , pp. 157-163
    • Reese, G.1    Ayuso, R.2    Leong-Kee, S.M.3
  • 74
    • 33645316499 scopus 로고    scopus 로고
    • Structural, immunological and functional properties of natural recombinant Pan a 1, the major allergen of Brown shrimp. Penaeus aztecus
    • Reese G, Schicktanz S, Lauraer I, et al. Structural, immunological and functional properties of natural recombinant Pan a 1, the major allergen of Brown shrimp. Penaeus aztecus. Clin Exp Allergy 2006; 36: 517-524.
    • (2006) Clin Exp Allergy , vol.36 , pp. 517-524
    • Reese, G.1    Schicktanz, S.2    Lauraer, I.3
  • 76
    • 26244460970 scopus 로고    scopus 로고
    • The development and progression of allergy to multiple nuts at different ages
    • Clark AT, Ewan PW. The development and progression of allergy to multiple nuts at different ages. Pediatr Allergy Immunol 2005; 16: 507-511.
    • (2005) Pediatr Allergy Immunol , vol.16 , pp. 507-511
    • Clark, A.T.1    Ewan, P.W.2
  • 77
    • 0029873844 scopus 로고    scopus 로고
    • Identification of a Brazil-nut allergen in transgenic soybeans
    • Nordlee JA, Taylor SL, Townsend JA, et al. Identification of a Brazil-nut allergen in transgenic soybeans. N Engl J Med 1996; 334(11): 688-692.
    • (1996) N Engl J Med , vol.334 , Issue.11 , pp. 688-692
    • Nordlee, J.A.1    Taylor, S.L.2    Townsend, J.A.3
  • 78
    • 0036152476 scopus 로고    scopus 로고
    • Linear IgE epitope mapping of the English walnut (Juglans regia) major food allergen, Jug r 1
    • Robotham JM, Teuber SS, Sathe SK, et al. Linear IgE epitope mapping of the English walnut (Juglans regia) major food allergen, Jug r 1. J Allergy Clin Immunol 2002; 109(1): 143-149.
    • (2002) J Allergy Clin Immunol , vol.109 , Issue.1 , pp. 143-149
    • Robotham, J.M.1    Teuber, S.S.2    Sathe, S.K.3
  • 79
    • 22544473892 scopus 로고    scopus 로고
    • Sesame allergy: A growing allergy of global proportions?
    • Gangur V, Kelly C, Navulure L. Sesame allergy: a growing allergy of global proportions? Ann Allergy Asthma Immunol 2005; 95: 11-13.
    • (2005) Ann Allergy Asthma Immunol , vol.95 , pp. 11-13
    • Gangur, V.1    Kelly, C.2    Navulure, L.3
  • 80
    • 27844448693 scopus 로고    scopus 로고
    • Identification of potentially cross-reactive peanut-lupine proteins by computer-assisted search of amino acid sequence homology
    • Guarneri F, Guarneri C, Benvenga S. Identification of potentially cross-reactive peanut-lupine proteins by computer-assisted search of amino acid sequence homology. Int Arch Allergy Immunol 2005; 138: 273-277.
    • (2005) Int Arch Allergy Immunol , vol.138 , pp. 273-277
    • Guarneri, F.1    Guarneri, C.2    Benvenga, S.3
  • 81
    • 20744450241 scopus 로고    scopus 로고
    • One- and two-dimensional electrophoretic identification of IgE-binding polypeptides of Lupinus albus and other legume seeds
    • Magni C, Herndl A, Sironi E, et al. One- and two-dimensional electrophoretic identification of IgE-binding polypeptides of Lupinus albus and other legume seeds. J Agric Food Chem 2005; 53: 4567-4571.
    • (2005) J Agric Food Chem , vol.53 , pp. 4567-4571
    • Magni, C.1    Herndl, A.2    Sironi, E.3
  • 82
    • 3242781598 scopus 로고    scopus 로고
    • Kiwi fruit is a significant allergen and is associated with differing patterns of reactivity in children and adults
    • Lucas JS, Grimshaw KE, Collins K, et al. Kiwi fruit is a significant allergen and is associated with differing patterns of reactivity in children and adults. Clin Exp Allergy 2004; 34: 1115-1121.
    • (2004) Clin Exp Allergy , vol.34 , pp. 1115-1121
    • Lucas, J.S.1    Grimshaw, K.E.2    Collins, K.3
  • 83
    • 28344448227 scopus 로고    scopus 로고
    • Comparison of the allergenicity of Actnidia deliciosa (kiwi fruit) and Actinidia chinensis (gold kiwi)
    • Lucans JS, Lewis SA, Trewin JB, et al. Comparison of the allergenicity of Actnidia deliciosa (kiwi fruit) and Actinidia chinensis (gold kiwi). Pediatr Allergy Immunol 2005; 16: 647-654.
    • (2005) Pediatr Allergy Immunol , vol.16 , pp. 647-654
    • Lucans, J.S.1    Lewis, S.A.2    Trewin, J.B.3
  • 84
    • 28644448562 scopus 로고    scopus 로고
    • Kiwellin, a novel protein from kiwi fruit. Purification, biochemical characterization and identification as an allergen
    • Tamburrini M, Cerasuolo I, Carratore V, et al. Kiwellin, a novel protein from kiwi fruit. Purification, biochemical characterization and identification as an allergen. Protein J 2005; 24: 423-429.
    • (2005) Protein J , vol.24 , pp. 423-429
    • Tamburrini, M.1    Cerasuolo, I.2    Carratore, V.3
  • 86
    • 31944437281 scopus 로고    scopus 로고
    • Napins, 2S albumins, is major allergens in oilseed rape and turnip rape
    • Puumalainen TJ, Poikonen S, Kotovuori A, et al. Napins, 2S albumins, is major allergens in oilseed rape and turnip rape. J Allergy Clin Immunol 2006; 117: 426-432.
    • (2006) J Allergy Clin Immunol , vol.117 , pp. 426-432
    • Puumalainen, T.J.1    Poikonen, S.2    Kotovuori, A.3
  • 87
  • 88
    • 33644688551 scopus 로고    scopus 로고
    • Pollen-food syndromes associated with weed pollinosis: An update from the molecular point of view
    • Egger M, Mutschlechner S, Wopfner N, et al. Pollen-food syndromes associated with weed pollinosis: an update from the molecular point of view. Allergy 2006; 61: 461-476.
    • (2006) Allergy , vol.61 , pp. 461-476
    • Egger, M.1    Mutschlechner, S.2    Wopfner, N.3
  • 89
    • 4143094737 scopus 로고    scopus 로고
    • Sensitization to Ficus benjamina: Relationship to natural rubber latex allergy and identification of foods implicated in the Ficus-fruit syndrome
    • Hemmer W, Focke M, Gotz M, et al. Sensitization to Ficus benjamina: relationship to natural rubber latex allergy and identification of foods implicated in the Ficus-fruit syndrome. Clin Exp Allergy 2004; 34: 1251-1258.
    • (2004) Clin Exp Allergy , vol.34 , pp. 1251-1258
    • Hemmer, W.1    Focke, M.2    Gotz, M.3
  • 90
  • 91
    • 0036424565 scopus 로고    scopus 로고
    • Significance of carbohydrate epitopes in a latex allergen with beta-1,3-glucanase activity
    • Yagami T, Osuna H, Kuono M, et al. Significance of carbohydrate epitopes in a latex allergen with beta-1,3-glucanase activity. Int Arch Allergy Immunol 2002; 129: 27-37.
    • (2002) Int Arch Allergy Immunol , vol.129 , pp. 27-37
    • Yagami, T.1    Osuna, H.2    Kuono, M.3
  • 92
    • 24944552984 scopus 로고    scopus 로고
    • Oral allergy syndrome (pollen-food allergy syndrome)
    • Purohit-Sheth TS, Carr WW. Oral allergy syndrome (pollen-food allergy syndrome). Allergy Asthma Proc 2005; 26: 229-230.
    • (2005) Allergy Asthma Proc , vol.26 , pp. 229-230
    • Purohit-Sheth, T.S.1    Carr, W.W.2
  • 93
    • 33745100197 scopus 로고    scopus 로고
    • Response of respiratory flour allergics in an ingested flour challenge may involve plasmacytoid dendritic cells, CD25+and CD152+T cells
    • Hoffman HJ, Skjold T, Raithel M, et al. Response of respiratory flour allergics in an ingested flour challenge may involve plasmacytoid dendritic cells, CD25+and CD152+T cells. Int Arch Allergy Immunol 2006; 140: 252-260.
    • (2006) Int Arch Allergy Immunol , vol.140 , pp. 252-260
    • Hoffman, H.J.1    Skjold, T.2    Raithel, M.3
  • 94
    • 0034512014 scopus 로고    scopus 로고
    • Occupational asthma in a seafood restaurant worker: Cross-reactivity of shrimp and scallops
    • Goetz DW, Whisman BA. Occupational asthma in a seafood restaurant worker: cross-reactivity of shrimp and scallops. Ann Allergy Asthma Immunol 2000; 85: 461-466.
    • (2000) Ann Allergy Asthma Immunol , vol.85 , pp. 461-466
    • Goetz, D.W.1    Whisman, B.A.2
  • 98
    • 0035180521 scopus 로고    scopus 로고
    • Hidden peanut allergens detected in various foods: Findings and legal measures
    • Schäppi GF, Konrad V, Imhof D, et al. Hidden peanut allergens detected in various foods: findings and legal measures. Allergy 2001; 56: 1216-1220.
    • (2001) Allergy , vol.56 , pp. 1216-1220
    • Schäppi, G.F.1    Konrad, V.2    Imhof, D.3
  • 100
    • 17144373268 scopus 로고    scopus 로고
    • Gastrointestinal food allergy: New insights into pathophysiology and clinical perspectives
    • Bischoff S, Crowe SE. Gastrointestinal food allergy: new insights into pathophysiology and clinical perspectives. Gastroenterology 2005; 128: 1089-1013.
    • (2005) Gastroenterology , vol.128 , pp. 1013-1089
    • Bischoff, S.1    Crowe, S.E.2
  • 101
    • 0037645799 scopus 로고    scopus 로고
    • Clinical aspects of gastrointestinal food allergy in childhood
    • Sicherer SH. Clinical aspects of gastrointestinal food allergy in childhood. Pediatrics 2003; 111: 1609-1616.
    • (2003) Pediatrics , vol.111 , pp. 1609-1616
    • Sicherer, S.H.1
  • 103
    • 33846425336 scopus 로고    scopus 로고
    • IgE-mediated food allergy diagnosis: Current status and new perspectives
    • Asero R, Ballmer-Weber BK, Beyer K, et al. IgE-mediated food allergy diagnosis: current status and new perspectives. Mol Nutr Food Res 2007; 51: 135-147.
    • (2007) Mol Nutr Food Res , vol.51 , pp. 135-147
    • Asero, R.1    Ballmer-Weber, B.K.2    Beyer, K.3
  • 104
    • 34248196530 scopus 로고    scopus 로고
    • Epidemiology of food allergy: What’s new? A critical appraisal of recent population-based studies
    • Kiel T. Epidemiology of food allergy: what’s new? A critical appraisal of recent population-based studies. Curr Op Allergy Clin Immunol 2007; 7: 259-263.
    • (2007) Curr Op Allergy Clin Immunol , vol.7 , pp. 259-263
    • Kiel, T.1
  • 105
    • 33947726921 scopus 로고    scopus 로고
    • Food allergy to proteins. Nutrition Support for Infants at Risk
    • Cooke RJ, Vanderplas Y, Wahn U, eds
    • Nowak-Wergrzyn A. Food allergy to proteins. In: Cooke RJ, Vanderplas Y, Wahn U, eds. Nutrition Support for Infants at Risk. Nestle Nutr Workshop Ser Pediatr Program 2007; 59: 17-35.
    • (2007) Nestle Nutr Workshop Ser Pediatr Program , vol.59 , pp. 17-35
    • Nowak-Wergrzyn, A.1
  • 106
    • 0035021315 scopus 로고    scopus 로고
    • Utility of food-specific concentrations in predicting symptomatic food allergy
    • Sampson HA. Utility of food-specific concentrations in predicting symptomatic food allergy. J Allergy Clin Immunol 2001; 107: 891-896.
    • (2001) J Allergy Clin Immunol , vol.107 , pp. 891-896
    • Sampson, H.A.1
  • 107
    • 0033721541 scopus 로고    scopus 로고
    • Specificity of allergen skin testing in predicting positive food challenges to milk, egg, and peanut in children
    • Sporik R, Hill DJ, Hosking CS. Specificity of allergen skin testing in predicting positive food challenges to milk, egg, and peanut in children. Clin Exp Allergy 2000; 30: 1540-1546.
    • (2000) Clin Exp Allergy , vol.30 , pp. 1540-1546
    • Sporik, R.1    Hill, D.J.2    Hosking, C.S.3
  • 108
    • 3442889068 scopus 로고    scopus 로고
    • The relationship of allergen-specific IgE levels and oral food challenge outcome
    • Perry TT, Matsui EC, Conover-Walker M, et al. The relationship of allergen-specific IgE levels and oral food challenge outcome. J Allergy Clin Immunol 2004; 114: 144-149.
    • (2004) J Allergy Clin Immunol , vol.114 , pp. 144-149
    • Perry, T.T.1    Matsui, E.C.2    Conover-Walker, M.3
  • 109
    • 17144366513 scopus 로고    scopus 로고
    • The predictive value of specific immunoglobulin E levels in serum for the outcome of oral food challenges
    • Celik-Bilgili S, Mehl A, Verstege A, et al. The predictive value of specific immunoglobulin E levels in serum for the outcome of oral food challenges. Clin Exp Allergy 2005; 35: 268-273.
    • (2005) Clin Exp Allergy , vol.35 , pp. 268-273
    • Celik-Bilgili, S.1    Mehl, A.2    Verstege, A.3
  • 111
    • 0037434895 scopus 로고    scopus 로고
    • Effect of anti-IgE therapy in patients with peanut allergy
    • Leung DY, Sampson HA, Yunginger JY, et al. Effect of anti-IgE therapy in patients with peanut allergy. New Eng J Med 2003; 348: 986-993.
    • (2003) New Eng J Med , vol.348 , pp. 986-993
    • Leung, D.Y.1    Sampson, H.A.2    Yunginger, J.Y.3
  • 112
    • 0034769432 scopus 로고    scopus 로고
    • Food allergy herbal formula-1 (FAHF-1) blocks peanut-induced anaphylaxis in a murine model
    • Li XM, Zhang TF, Huang CK, et al. Food allergy herbal formula-1 (FAHF-1) blocks peanut-induced anaphylaxis in a murine model. J Allergy Clin Immunol 2001; 108: 639-646.
    • (2001) J Allergy Clin Immunol , vol.108 , pp. 639-646
    • Li, X.M.1    Zhang, T.F.2    Huang, C.K.3
  • 113
    • 2542424989 scopus 로고    scopus 로고
    • Efficacy of birch-pollen immunotherapy on crossreactive food allergy confirmed by skin tests and double-blind food challenges
    • Bolhaar T, Tiemessen MM, Zuidmeer L, et al. Efficacy of birch-pollen immunotherapy on crossreactive food allergy confirmed by skin tests and double-blind food challenges. Clin Exp Allergy 2004; 34: 761-769.
    • (2004) Clin Exp Allergy , vol.34 , pp. 761-769
    • Bolhaar, T.1    Tiemessen, M.M.2    Zuidmeer, L.3
  • 114
    • 17644388057 scopus 로고    scopus 로고
    • A chimeric human-cat fusion protein blocks cat-induced allergy
    • Zhu D, Kepley CL, Zhang K, et al. A chimeric human-cat fusion protein blocks cat-induced allergy. Nat Med 2005; 60: 11: 446-449.
    • (2005) Nat Med , vol.60
    • Zhu, D.1    Kepley, C.L.2    Zhang, K.3
  • 115
    • 13244249705 scopus 로고    scopus 로고
    • Allergen immunotherapy with heat-killed Listeria monocytogenes alleviates peanut and food-induced anaphylaxis in dogs
    • Frick OL, Teuber SS, Buchanan BB, et al. Allergen immunotherapy with heat-killed Listeria monocytogenes alleviates peanut and food-induced anaphylaxis in dogs. Allergy 2005; 60: 243-250.
    • (2005) Allergy , vol.60 , pp. 243-250
    • Frick, O.L.1    Teuber, S.S.2    Buchanan, B.B.3
  • 116
    • 4143072482 scopus 로고    scopus 로고
    • Dietary prevention of allergic disease in infant and small children. Part III: Critical review of published peer-reviewed observations and interventional studies and final recommendations
    • Muraro A, Dreborg S, Halken S, et al. Dietary prevention of allergic disease in infant and small children. Part III: Critical review of published peer-reviewed observations and interventional studies and final recommendations. Pediatr Allergy Immunol 2003; 15: 291-307.
    • (2003) Pediatr Allergy Immunol , vol.15 , pp. 291-307
    • Muraro, A.1    Dreborg, S.2    Halken, S.3
  • 117
    • 0033884799 scopus 로고    scopus 로고
    • Hypoallergenic infant formulas
    • American Academy of Pediatrics Committee on Nutrition. Hypoallergenic infant formulas. Pediatrics 2000; 106: 346-349.
    • (2000) Pediatrics , vol.106 , pp. 346-349
  • 118
    • 33745653149 scopus 로고    scopus 로고
    • Predictive value of skin prick tests using recombinant allergens for diagnosis of peanut allergy
    • Astier C, Morisset M, Roitel O, et al. Predictive value of skin prick tests using recombinant allergens for diagnosis of peanut allergy. J Allergy Clin Immunol 2006; 118: 250-256.
    • (2006) J Allergy Clin Immunol , vol.118 , pp. 250-256
    • Astier, C.1    Morisset, M.2    Roitel, O.3
  • 120
    • 0035021315 scopus 로고    scopus 로고
    • Utility of food-specific IgE concentrations in predicting food allergy
    • Sampson HA. Utility of food-specific IgE concentrations in predicting food allergy. J Allergy Clin Immunol 2001; 107: 891-896.
    • (2001) J Allergy Clin Immunol , vol.107 , pp. 891-896
    • Sampson, H.A.1
  • 121
    • 0030779139 scopus 로고    scopus 로고
    • Relationship between food-specific IgE concentrations and the risk of positive food challenges in children and adolescents
    • Sampson HA, Ho DG. Relationship between food-specific IgE concentrations and the risk of positive food challenges in children and adolescents. J Allergy Clin Immunol 1997; 100: 444-451.
    • (1997) J Allergy Clin Immunol , vol.100 , pp. 444-451
    • Sampson, H.A.1    Ho, D.G.2
  • 122
    • 0036219071 scopus 로고    scopus 로고
    • Food portions are positively related to energy intake and body weight in children
    • McCone KL, Sickles-Wright H, Birch LL, et al. Food portions are positively related to energy intake and body weight in children. J Pediatr 2002; 140: 340-347.
    • (2002) J Pediatr , vol.140 , pp. 340-347
    • McCone, K.L.1    Sickles-Wright, H.2    Birch, L.L.3
  • 123
    • 2542418969 scopus 로고    scopus 로고
    • Update on threshold doses of food allergens: Implications for patients and the food industry
    • Moneret-Vautrin DA, Kanny G. Update on threshold doses of food allergens: implications for patients and the food industry. Curr Opin Allergy Clin Immunol 2004; 4: 215-219.
    • (2004) Curr Opin Allergy Clin Immunol , vol.4 , pp. 215-219
    • Moneret-Vautrin, D.A.1    Kanny, G.2
  • 124
    • 0037434895 scopus 로고    scopus 로고
    • Effect of anti-IgE therapy in patients with food allergy
    • Leung DYM, Sampson HA, Yunginger JY, et al Effect of anti-IgE therapy in patients with food allergy. NEJM 2003; 348: 986-993.
    • (2003) NEJM , vol.348 , pp. 986-993
    • Leung, D.Y.M.1    Sampson, H.A.2    Yunginger, J.Y.3
  • 126
    • 33847290462 scopus 로고    scopus 로고
    • Oral desensitization in children with milk and egg allergies obtains recovery in significant proportion of cases. A randomized study of 60 children with cow’s milk allergy and 90 children with egg allergy
    • Morriset M, Moneret-Vautrin DA, Guenard L, et al. Oral desensitization in children with milk and egg allergies obtains recovery in significant proportion of cases. A randomized study of 60 children with cow’s milk allergy and 90 children with egg allergy. Allerg Immunol (Paris) 2007: 39: 12-19.
    • (2007) Allerg Immunol (Paris) , vol.39 , pp. 12-19
    • Morriset, M.1    Moneret-Vautrin, D.A.2    Guenard, L.3
  • 127
    • 0001215030 scopus 로고
    • Analysis of food proteins for verification of contamination or mislabeling
    • Malmheden Yman I, Eriksson A, Everitt G, et al. Analysis of food proteins for verification of contamination or mislabeling. Food Agric Immunol 1994; 6: 167-172.
    • (1994) Food Agric Immunol , vol.6 , pp. 167-172
    • Malmheden Yman, I.1    Eriksson, A.2    Everitt, G.3
  • 128
    • 0036157496 scopus 로고    scopus 로고
    • Factors affecting the determination of threshold doses for allergenic foods: How much is too much?
    • Taylor SL, Hefle S, Bindslev-Jensen C, et al. Factors affecting the determination of threshold doses for allergenic foods: how much is too much? J Allergy Clin Immunol 2002; 109: 24-30.
    • (2002) J Allergy Clin Immunol , vol.109 , pp. 24-30
    • Taylor, S.L.1    Hefle, S.2    Bindslev-Jensen, C.3
  • 129
    • 0041620647 scopus 로고    scopus 로고
    • Thresholds of clinical reactivity to milk, egg, peanut and sesame in immunoglobulin E-dependent allergies: Evaluation by double-blind or singleblind placebo-controlled oral challenges
    • Morisset M, Moneret-Vautrin DA, Kanny G, et al. Thresholds of clinical reactivity to milk, egg, peanut and sesame in immunoglobulin E-dependent allergies: evaluation by double-blind or singleblind placebo-controlled oral challenges. Clin Exp Allergy 2003; 33: 1046-1051.
    • (2003) Clin Exp Allergy , vol.33 , pp. 1046-1051
    • Morisset, M.1    Moneret-Vautrin, D.A.2    Kanny, G.3
  • 130
    • 34247895583 scopus 로고    scopus 로고
    • Evaluation the effect of food processing on the potential human allergenicity on novel proteins: International workshop report
    • Thomas K, Herouet-Guicheney C, Ladics G, et al. Evaluation the effect of food processing on the potential human allergenicity on novel proteins: international workshop report. Food Chem Toxicol 2007; 45: 1116-1122.
    • (2007) Food Chem Toxicol , vol.45 , pp. 1116-1122
    • Thomas, K.1    Herouet-Guicheney, C.2    Ladics, G.3
  • 131
    • 33646865695 scopus 로고    scopus 로고
    • T-cell epitopes of food allergens
    • Bohle B. T-cell epitopes of food allergens. Clin Rev Allergy Immunol 2006; 30: 97-108.
    • (2006) Clin Rev Allergy Immunol , vol.30 , pp. 97-108
    • Bohle, B.1
  • 132
    • 33645213239 scopus 로고    scopus 로고
    • Patterns of food allergen-specific cytokine production by T lymphocytes of children with multiple allergies
    • Scott-Taylor TH, Hourihane JB, Harper J, et al. Patterns of food allergen-specific cytokine production by T lymphocytes of children with multiple allergies. Clin Exp Allergy 2005; 35: 1473-1480.
    • (2005) Clin Exp Allergy , vol.35 , pp. 1473-1480
    • Scott-Taylor, T.H.1    Hourihane, J.B.2    Harper, J.3
  • 133
    • 0344177206 scopus 로고    scopus 로고
    • Characterization of lymphocyte responses to peanuts in normal children, peanut-allergic children and allergic children who acquired tolerance to peanuts
    • Turcanu V, Maleki SJ, Lack G. Characterization of lymphocyte responses to peanuts in normal children, peanut-allergic children and allergic children who acquired tolerance to peanuts. J Clin Invest 2003; 111: 1065-1072.
    • (2003) J Clin Invest , vol.111 , pp. 1065-1072
    • Turcanu, V.1    Maleki, S.J.2    Lack, G.3
  • 134
    • 0029972295 scopus 로고    scopus 로고
    • Cytokine production in children outgrowing hen egg allergy
    • Noma T, Yoshizawa I, Aoki K, et al. Cytokine production in children outgrowing hen egg allergy. Clin Exp Allergy 1996: 26: 1298-1307.
    • (1996) Clin Exp Allergy , vol.26 , pp. 1298-1307
    • Noma, T.1    Yoshizawa, I.2    Aoki, K.3
  • 135
    • 33749353427 scopus 로고    scopus 로고
    • Human subjects without peanut allergy demonstrate T cell-dependent, Th2-based, peanut-specific cytokine and chemokine responses independent of th1 expression
    • Thottingal TB, Setfura BP, Simons FER, et al. Human subjects without peanut allergy demonstrate T cell-dependent, Th2-based, peanut-specific cytokine and chemokine responses independent of th1 expression. J Allergy Clin Immunol 2006; 118: 905-914.
    • (2006) J Allergy Clin Immunol , vol.118 , pp. 905-914
    • Thottingal, T.B.1    Setfura, B.P.2    Simons, F.E.R.3
  • 136
    • 3042594506 scopus 로고    scopus 로고
    • Allergen-responsive CD4+CD25+regulatory T cells in children who have outgrown cow’s milk allergy
    • Karlsson MR, Rugtveit J, Brandtzaeg P. Allergen-responsive CD4+CD25+regulatory T cells in children who have outgrown cow’s milk allergy. J Exp Med 2004; 199: 1679-1688.
    • (2004) J Exp Med , vol.199 , pp. 1679-1688
    • Karlsson, M.R.1    Rugtveit, J.2    Brandtzaeg, P.3
  • 137
    • 0036264052 scopus 로고    scopus 로고
    • Current understanding of cross-reactivity of food allergens and pollen
    • Vieths S, Scheurer S, Ballmer-Weber B. Current understanding of cross-reactivity of food allergens and pollen. Ann N Y Acad Sci 2002; 964: 47-68.
    • (2002) Ann N Y Acad Sci , vol.964 , pp. 47-68
    • Vieths, S.1    Scheurer, S.2    Ballmer-Weber, B.3
  • 138
    • 6344222889 scopus 로고    scopus 로고
    • Allergy vaccine engineering: Epitope modulation of recombinant Bet v 1 reduces IgE-binging but retains protein folding pattern for induction of protective blocking-antibody responses
    • Holm J, Gajhede M, Ferreras M, et al. Allergy vaccine engineering: epitope modulation of recombinant Bet v 1 reduces IgE-binging but retains protein folding pattern for induction of protective blocking-antibody responses. J Immunol 2004; 173: 5258-5267.
    • (2004) J Immunol , vol.173 , pp. 5258-5267
    • Holm, J.1    Gajhede, M.2    Ferreras, M.3
  • 139
    • 0035947028 scopus 로고    scopus 로고
    • Characterization and identification of allergen epitopes: Recombinant peptide libraries and synthetic, overlapping peptides
    • Reese G, Ayuso R, Leon-Kee SM, et al. Characterization and identification of allergen epitopes: recombinant peptide libraries and synthetic, overlapping peptides. J Chromatogr B Biomed Sci Appl 2001; 756: 157-163.
    • (2001) J Chromatogr B Biomed Sci Appl , vol.756 , pp. 157-163
    • Reese, G.1    Ayuso, R.2    Leon-Kee, S.M.3
  • 140
    • 0034235234 scopus 로고    scopus 로고
    • Dominant epitopes and allergic cross-reactivity: Complex formation between a fab fragment of a monoclonal murine IgG antibody and the major allergen from birch pollen
    • Mirza O, Henriksen A, Ipsen H, et al. Dominant epitopes and allergic cross-reactivity: complex formation between a fab fragment of a monoclonal murine IgG antibody and the major allergen from birch pollen. J Immunol 2000; 165: 331-338.
    • (2000) J Immunol , vol.165 , pp. 331-338
    • Mirza, O.1    Henriksen, A.2    Ipsen, H.3
  • 141
    • 12744253736 scopus 로고    scopus 로고
    • Molecular basis of pollen-related food allergy: Identification of a second cross-reactive IgE epitope on Pru a 1, the major cherry allergen (Prunus avium)
    • Wiche R, Gubesch M, Konig H, et al. Molecular basis of pollen-related food allergy: identification of a second cross-reactive IgE epitope on Pru a 1, the major cherry allergen (Prunus avium). Biochem J 2005; 385: 319-327.
    • (2005) Biochem J , vol.385 , pp. 319-327
    • Wiche, R.1    Gubesch, M.2    Konig, H.3
  • 142
    • 0344393658 scopus 로고    scopus 로고
    • Mutational epitope analysis of Pru av 1 and Api g 1, the major allergens of cherry (Prunus avium) and celery (Apium graveolens): Correlating IgE reactivity with three-dimensional structure
    • Neudecker P, Lehmann K, Nerkamp J, et al. Mutational epitope analysis of Pru av 1 and Api g 1, the major allergens of cherry (Prunus avium) and celery (Apium graveolens): correlating IgE reactivity with three-dimensional structure. Biochem J 2003; 15; 376: 97-107.
    • (2003) Biochem J , vol.15 , Issue.376 , pp. 97-107
    • Neudecker, P.1    Lehmann, K.2    Nerkamp, J.3
  • 143
    • 0035958621 scopus 로고    scopus 로고
    • A novel grass pollen allergen mimotope identified by phage display peptide library inhibits allergen-human IgE antibody interaction
    • Suphioglu C, Schäppi G, Kenrick J, et al. A novel grass pollen allergen mimotope identified by phage display peptide library inhibits allergen-human IgE antibody interaction. FEBS Lett 2001; 27: 502: 46-52.
    • (2001) FEBS Lett , vol.27
    • Suphioglu, C.1    Schäppi, G.2    Kenrick, J.3
  • 144
    • 25644434412 scopus 로고    scopus 로고
    • A novel approach for investigation of specific and crossreactive IgE epitopes on Bet v 1 and homologous food allergens in individual patients
    • Mittag D, Batori V, Neudecker P, et al. A novel approach for investigation of specific and crossreactive IgE epitopes on Bet v 1 and homologous food allergens in individual patients. Mol Immunol 2006; 43: 268-278.
    • (2006) Mol Immunol , vol.43 , pp. 268-278
    • Mittag, D.1    Batori, V.2    Neudecker, P.3
  • 145
    • 33746280250 scopus 로고    scopus 로고
    • In silica predictability of allergenicity: From amino acid sequence via 3-D structure to allergenicity
    • Aalberse RC, Stadler BM. In silica predictability of allergenicity: from amino acid sequence via 3-D structure to allergenicity. Mol Nutr Food Res 2006; 50: 625-627.
    • (2006) Mol Nutr Food Res , vol.50 , pp. 625-627
    • Aalberse, R.C.1    Stadler, B.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.