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Volumn 9, Issue 1, 2007, Pages 1-18

The peanut allergy epidemic: Allergen molecular characterisation and prospects for specific therapy

Author keywords

[No Author keywords available]

Indexed keywords

CHINESE DRUG; EPITOPE; FOOD ALLERGEN; FOOD ALLERGY HERBAL FORMULA 1; HAZELNUT EXTRACT; IMMUNOGLOBULIN E; IMMUNOGLOBULIN E ANTIBODY; INTERLEUKIN 12; MESSENGER RNA; OMALIZUMAB; PEANUT EXTRACT; PHOSPHOLIPASE A2; PLANT EXTRACT; PROTEIN ARA H 1; PROTEIN ARA H 2; PROTEIN ARA H 3; UNCLASSIFIED DRUG; VICILIN;

EID: 33846042229     PISSN: 14623994     EISSN: 14623994     Source Type: Journal    
DOI: 10.1017/S1462399407000208     Document Type: Review
Times cited : (60)

References (95)
  • 1
    • 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: A 5-year follow-up study
    • Sicherer, S.H., Munoz-Furlong, A. and Sampson, H.A. (2003) Prevalence of peanut and tree nut allergy in the United States determined by means of a random digit dial telephone survey: A 5-year follow-up study. J Allergy Clin Immunol 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
  • 2
    • 0036857413 scopus 로고    scopus 로고
    • Rising prevalence of allergy to peanut in children: Data from 2 sequential cohorts
    • Grundy, J. et al. (2002) Rising prevalence of allergy to peanut in children: Data from 2 sequential cohorts. J Allergy Clin Immunol 110, 784-789
    • (2002) J Allergy Clin Immunol , vol.110 , pp. 784-789
    • Grundy, J.1
  • 3
    • 0026638876 scopus 로고
    • Fatal and near-fatal anaphylactic reactions to food in children and adolescents
    • Sampson, H.A., Mendelson, L. and Rosen, J.P. (1992) Fatal and near-fatal anaphylactic reactions to food in children and adolescents. N Engl J Med 327, 380-384
    • (1992) N Engl J Med , vol.327 , pp. 380-384
    • Sampson, H.A.1    Mendelson, L.2    Rosen, J.P.3
  • 5
    • 0037434920 scopus 로고    scopus 로고
    • Factors associated with the development of peanut allergy in childhood
    • Lack, G. et al. (2003) Factors associated with the development of peanut allergy in childhood. N Engl J Med 348, 977-985
    • (2003) N Engl J Med , vol.348 , pp. 977-985
    • Lack, G.1
  • 6
    • 84990407356 scopus 로고
    • Allergy in the newborn: Skin test reactions confirmed by the Prausnitz-Kustner test at birth
    • Kaufman, H.S. (1971) Allergy in the newborn: Skin test reactions confirmed by the Prausnitz-Kustner test at birth. Clin Allergy 1, 363-367
    • (1971) Clin Allergy , vol.1 , pp. 363-367
    • Kaufman, H.S.1
  • 7
    • 0035804855 scopus 로고    scopus 로고
    • Detection of peanut allèrgens in breast milk of lactating women
    • Vadas, P. et al. (2001) Detection of peanut allèrgens in breast milk of lactating women. JAMA 285, 1746-1748
    • (2001) JAMA , vol.285 , pp. 1746-1748
    • Vadas, P.1
  • 8
    • 0037171695 scopus 로고    scopus 로고
    • Peanut allergy
    • Sampson, H.A. (2002) Peanut allergy. N Engl J Med 346, 1294-1299
    • (2002) N Engl J Med , vol.346 , pp. 1294-1299
    • Sampson, H.A.1
  • 9
    • 0024311923 scopus 로고
    • The natural history of peanut allergy
    • Bock, S.A. and Atkins, F.M. (1989) The natural history of peanut allergy. J Allergy Clin Immunol 83, 900-904
    • (1989) J Allergy Clin Immunol , vol.83 , pp. 900-904
    • Bock, S.A.1    Atkins, F.M.2
  • 10
    • 0035113288 scopus 로고    scopus 로고
    • The natural history of peanut allergy
    • Skolnick, H.S. et al. (2001) The natural history of peanut allergy. J Allergy Clin Immunol 107, 367-374
    • (2001) J Allergy Clin Immunol , vol.107 , pp. 367-374
    • Skolnick, H.S.1
  • 11
    • 22644443548 scopus 로고    scopus 로고
    • Mucosal immunity and allergic responses: Lack of regulation and/or lack of microbial stimulation?
    • Prioult, G. and Nagler-Anderson, C. (2005) Mucosal immunity and allergic responses: Lack of regulation and/or lack of microbial stimulation? Immunol Rev 206, 204-218
    • (2005) Immunol Rev , vol.206 , pp. 204-218
    • Prioult, G.1    Nagler-Anderson, C.2
  • 12
    • 33745553603 scopus 로고    scopus 로고
    • Oral tolerance and allergic responses to food proteins
    • Strobel, S. and Mowat, A.M. (2006) Oral tolerance and allergic responses to food proteins. Curr Opin Allergy Clin Immunol 6, 207-213
    • (2006) Curr Opin Allergy Clin Immunol , vol.6 , pp. 207-213
    • Strobel, S.1    Mowat, A.M.2
  • 13
    • 0022640843 scopus 로고
    • Two types of murine helper T cell clone. I. Definition according to profiles of lymphokine activities and secreted proteins
    • Mosmann, T.R. et al. (1986) Two types of murine helper T cell clone. I. Definition according to profiles of lymphokine activities and secreted proteins. J Immunol 136, 2348-2357
    • (1986) J Immunol , vol.136 , pp. 2348-2357
    • Mosmann, T.R.1
  • 14
    • 0034049677 scopus 로고    scopus 로고
    • Mechanisms of eosinophil-associated inflammation
    • Gleich, G.J. (2000) Mechanisms of eosinophil-associated inflammation. J Allergy Clin Immunol 105, 651-663
    • (2000) J Allergy Clin Immunol , vol.105 , pp. 651-663
    • Gleich, G.J.1
  • 15
    • 0001683342 scopus 로고    scopus 로고
    • Randomised, double blind, crossover challenge study of allergenicity of peanut oils in subjects allergic to peanuts
    • Hourihane, J.O. et al. (1997) Randomised, double blind, crossover challenge study of allergenicity of peanut oils in subjects allergic to peanuts. BMJ 314, 1084-1088
    • (1997) BMJ , vol.314 , pp. 1084-1088
    • Hourihane, J.O.1
  • 16
    • 0028347006 scopus 로고
    • Cold pressed peanut oils may contain peanut allergen
    • Hoffmann, D.R. and Collins-Williams, C. (1994) Cold pressed peanut oils may contain peanut allergen. J Allergy Clin Immunol 93, 801-802
    • (1994) J Allergy Clin Immunol , vol.93 , pp. 801-802
    • Hoffmann, D.R.1    Collins-Williams, C.2
  • 17
    • 0027443372 scopus 로고
    • Allergen immunotherapy decreases interleukin 4 production in CD4+ T cells from allergic individuals
    • Secrist, H. et al. (1993) Allergen immunotherapy decreases interleukin 4 production in CD4+ T cells from allergic individuals. J Exp Med 178, 2123-2130
    • (1993) J Exp Med , vol.178 , pp. 2123-2130
    • Secrist, H.1
  • 18
    • 4143137472 scopus 로고    scopus 로고
    • Induction of T 'regulatory' cells by standardized house dust mite immuncitherapy: An increase in CD4+ CD25+ interleukin-10+ T cells expressing peripheral tissue trafficking markers
    • Gardner, L.M. et al. (2004) Induction of T 'regulatory' cells by standardized house dust mite immuncitherapy: An increase in CD4+ CD25+ interleukin-10+ T cells expressing peripheral tissue trafficking markers. Clin Exp Allergy 34, 1209-1219
    • (2004) Clin Exp Allergy , vol.34 , pp. 1209-1219
    • Gardner, L.M.1
  • 19
    • 0030956363 scopus 로고    scopus 로고
    • Insect venom immunotherapy induces interleukin-10 production and a Th2-to-Th1 shift, and changes surface marker expression in venom-allergic subjects
    • Bellinghausen, I. et al. (1997) Insect venom immunotherapy induces interleukin-10 production and a Th2-to-Th1 shift, and changes surface marker expression in venom-allergic subjects. Eur J Immunol 27, 1131-1139
    • (1997) Eur J Immunol , vol.27 , pp. 1131-1139
    • Bellinghausen, I.1
  • 20
    • 0038363534 scopus 로고    scopus 로고
    • IL-10 and TGF-beta cooperate in the regulatory T cell response to mucosal allergens in normal immunity and specific immunotherapy
    • Jutel, M. et al. (2003) IL-10 and TGF-beta cooperate in the regulatory T cell response to mucosal allergens in normal immunity and specific immunotherapy. Eur J Immunol 33, 1205-1214
    • (2003) Eur J Immunol , vol.33 , pp. 1205-1214
    • Jutel, M.1
  • 21
    • 0141958643 scopus 로고    scopus 로고
    • Renaissance of the blocking antibody concept in type I allergy
    • Flicker, S. and Valenta, R. (2003) Renaissance of the blocking antibody concept in type I allergy. Int Arch Allergy Immunol 132, 13-24
    • (2003) Int Arch Allergy Immunol , vol.132 , pp. 13-24
    • Flicker, S.1    Valenta, R.2
  • 22
    • 33645862861 scopus 로고    scopus 로고
    • Oral rush desensitization in peanut allergy: A case report
    • Patriarca, G. et al. (2006) Oral rush desensitization in peanut allergy: a case report. Dig Dis Sci 51, 471-473
    • (2006) Dig Dis Sci , vol.51 , pp. 471-473
    • Patriarca, G.1
  • 23
    • 0026700960 scopus 로고
    • Treatment of peanut allergy with rush immunotherapy
    • Oppenheimer, J.J. et al. (1992) Treatment of peanut allergy with rush immunotherapy. J Allergy Clin Immunol 90, 256-262
    • (1992) J Allergy Clin Immunol , vol.90 , pp. 256-262
    • Oppenheimer, J.J.1
  • 24
    • 0026045826 scopus 로고
    • Identification of a major peanut allergen, Ara h I, in patients with atopic dermatitis and positive peanut challenges
    • Burks, A.W. et al. (1991) Identification of a major peanut allergen, Ara h I, in patients with atopic dermatitis and positive peanut challenges. J Allergy Clin Immunol 88, 172-179
    • (1991) J Allergy Clin Immunol , vol.88 , pp. 172-179
    • Burks, A.W.1
  • 25
    • 0027049679 scopus 로고
    • Identification and characterization of a second major peanut allergen, Ara h II, with use of the sera of patients with atopic dermatitis and positive peanut challenge
    • Burks, A.W. et al. (1992) Identification and characterization of a second major peanut allergen, Ara h II, with use of the sera of patients with atopic dermatitis and positive peanut challenge. J Allergy Clin Immunol 90, 962-969
    • (1992) J Allergy Clin Immunol , vol.90 , pp. 962-969
    • Burks, A.W.1
  • 26
    • 0028807372 scopus 로고
    • Recombinant peanut allergen Ara h I expression and IgE binding in patients with peanut hypersensitivity
    • Burks, A.W. et al. (1995) Recombinant peanut allergen Ara h I expression and IgE binding in patients with peanut hypersensitivity. J Clin Invest 96, 1715-1721
    • (1995) J Clin Invest , vol.96 , pp. 1715-1721
    • Burks, A.W.1
  • 27
    • 0033557358 scopus 로고    scopus 로고
    • Molecular cloning and epitope analysis of the peanut allergen Ara h 3
    • Rabjohn, P. et al. (1999) Molecular cloning and epitope analysis of the peanut allergen Ara h 3. J Clin Invest 103, 535-542
    • (1999) J Clin Invest , vol.103 , pp. 535-542
    • Rabjohn, P.1
  • 28
    • 13944258766 scopus 로고    scopus 로고
    • Identification of the basic subunit of Ara h 3 as the major allergen in a group of children allergic to peanuts
    • Restani, P. et al. (2005) Identification of the basic subunit of Ara h 3 as the major allergen in a group of children allergic to peanuts. Ann Allergy Asthma Immunol 94, 262-266
    • (2005) Ann Allergy Asthma Immunol , vol.94 , pp. 262-266
    • Restani, P.1
  • 29
    • 0032812397 scopus 로고    scopus 로고
    • Selective cloning of peanut allergens, including profilin and 2S albumins, by phage display technology
    • Kleber-Janke, T. et al. (1999) Selective cloning of peanut allergens, including profilin and 2S albumins, by phage display technology. Int Arch Allergy Immunol 119, 265-274
    • (1999) Int Arch Allergy Immunol , vol.119 , pp. 265-274
    • Kleber-Janke, T.1
  • 30
    • 9644262438 scopus 로고    scopus 로고
    • Ara h 8, a Bet v 1-homologous allergen from peanut, is a major allergen in patients with combined birch pollen and peanut allergy
    • Mittag, D. et al. (2004) Ara h 8, a Bet v 1-homologous allergen from peanut, is a major allergen in patients with combined birch pollen and peanut allergy. J Allergy Clin Immunol 114, 1410-1417
    • (2004) J Allergy Clin Immunol , vol.114 , pp. 1410-1417
    • Mittag, D.1
  • 31
    • 0033928258 scopus 로고    scopus 로고
    • Molecular and biochemical classification of plant-derived food allergens
    • Breiteneder, H. and 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
  • 32
    • 0033582479 scopus 로고    scopus 로고
    • Heat-induced conformational changes of Ara h 1, a major peanut allergen, do not affect its allergenic properties
    • Koppelman, S.J. et al. (1999) Heat-induced conformational changes of Ara h 1, a major peanut allergen, do not affect its allergenic properties. J Biol Chem 274, 4770-4777
    • (1999) J Biol Chem , vol.274 , pp. 4770-4777
    • Koppelman, S.J.1
  • 33
    • 0034120710 scopus 로고    scopus 로고
    • Structure of the major peanut allergen Ara h 1 may protect IgE-binding epitopes from degradation
    • Maleki, S.J. et al. (2000) Structure of the major peanut allergen Ara h 1 may protect IgE-binding epitopes from degradation. J Immunol 164, 5844-5849
    • (2000) J Immunol , vol.164 , pp. 5844-5849
    • Maleki, S.J.1
  • 34
    • 8744286502 scopus 로고    scopus 로고
    • Isolation and characterization of natural Ara h 6: Evidence for a further peanut allergen with putative clinical relevance based on resistance to pepsin digestion and heat
    • Suhr, M. et al. (2004) Isolation and characterization of natural Ara h 6: Evidence for a further peanut allergen with putative clinical relevance based on resistance to pepsin digestion and heat. Mol Nutr Food Res 48, 390-399
    • (2004) Mol Nutr Food Res , vol.48 , pp. 390-399
    • Suhr, M.1
  • 35
    • 33646249121 scopus 로고    scopus 로고
    • Structure and stability of 2S albumin-type peanut allergens: Implications for the severity of peanut allergic reactions
    • Lehmann, K. et al. (2006) Structure and stability of 2S albumin-type peanut allergens: Implications for the severity of peanut allergic reactions. Biochem J 395, 463-472
    • (2006) Biochem J , vol.395 , pp. 463-472
    • Lehmann, K.1
  • 36
    • 0038342584 scopus 로고    scopus 로고
    • The major peanut allergen, Ara h 2, functions as a trypsin inhibitor, and roasting enhances this function
    • Maleki, S.J. et al. (2003) The major peanut allergen, Ara h 2, functions as a trypsin inhibitor, and roasting enhances this function. J Allergy Clin Immunol 112, 190-195
    • (2003) J Allergy Clin Immunol , vol.112 , pp. 190-195
    • Maleki, S.J.1
  • 37
    • 0033401394 scopus 로고    scopus 로고
    • Allergenicity of Maillard reaction products from peanut proteins
    • Chung, S.Y. and Champagne, E.T. (1999) Allergenicity of Maillard reaction products from peanut proteins. J Agric Food Chem 47, 5227-5231
    • (1999) J Agric Food Chem , vol.47 , pp. 5227-5231
    • Chung, S.Y.1    Champagne, E.T.2
  • 38
    • 0033792578 scopus 로고    scopus 로고
    • The effects of roasting on the allergenic properties of peanut proteins
    • Maleki, S.J. et al. (2000) The effects of roasting on the allergenic properties of peanut proteins. J Allergy Clin Immunol 106, 763-768
    • (2000) J Allergy Clin Immunol , vol.106 , pp. 763-768
    • Maleki, S.J.1
  • 39
    • 0037070050 scopus 로고    scopus 로고
    • High-oleic peanuts are not different from normal peanuts in allergenic properties
    • Chung, S.Y. et al. (2002) High-oleic peanuts are not different from normal peanuts in allergenic properties. J Agric Food Chem 50, 878-882
    • (2002) J Agric Food Chem , vol.50 , pp. 878-882
    • Chung, S.Y.1
  • 40
    • 0024232562 scopus 로고
    • Chemistry of Maillard reactions: Recent studies on the browning reaction mechanism and the development of antioxidants and mutagens
    • Namiki, M. (1988) Chemistry of Maillard reactions: Recent studies on the browning reaction mechanism and the development of antioxidants and mutagens. Adv Food Res 32, 115-184
    • (1988) Adv Food Res , vol.32 , pp. 115-184
    • Namiki, M.1
  • 41
    • 0034795756 scopus 로고    scopus 로고
    • Role of conformational and linear epitopes in the achievement of tolerance in cow's milk allergy
    • Vila, L. et al. (2001) Role of conformational and linear epitopes in the achievement of tolerance in cow's milk allergy. Clin Exp Allergy 31, 1599-1606
    • (2001) Clin Exp Allergy , vol.31 , pp. 1599-1606
    • Vila, L.1
  • 42
    • 8244232505 scopus 로고    scopus 로고
    • Mapping and mutational analysis of the IgE-binding epitopes on Ara h 1, a legume vicilin protein and a major allergen in peanut hypersensitivity
    • Burks, A.W. et al. (1997) Mapping and mutational analysis of the IgE-binding epitopes on Ara h 1, a legume vicilin protein and a major allergen in peanut hypersensitivity. Eur J Biochem 245, 334-339
    • (1997) Eur J Biochem , vol.245 , pp. 334-339
    • Burks, A.W.1
  • 43
    • 0031570734 scopus 로고    scopus 로고
    • Identification and mutational analysis of the immunodominant IgE binding epitopes of the major peanut allergen Ara h 2
    • Stanley, J.S. et al. (1997) Identification and mutational analysis of the immunodominant IgE binding epitopes of the major peanut allergen Ara h 2. Arch Biochem Biophys 342, 244-253
    • (1997) Arch Biochem Biophys , vol.342 , pp. 244-253
    • Stanley, J.S.1
  • 44
    • 0032916159 scopus 로고    scopus 로고
    • Tertiary structure and biophysical properties of a major peanut allergen, implications for the production of a hypoallergenic protein
    • Bannon, G.A. et al. (1999) Tertiary structure and biophysical properties of a major peanut allergen, implications for the production of a hypoallergenic protein. Int Arch Allergy Immunol 118, 315-316
    • (1999) Int Arch Allergy Immunol , vol.118 , pp. 315-316
    • Bannon, G.A.1
  • 45
    • 0032577580 scopus 로고    scopus 로고
    • Biochemical and structural analysis of the IgE binding sites on Ara h1, an abundant and highly allergenic peanut protein
    • Shin, D.S. et al. (1998) Biochemical and structural analysis of the IgE binding sites on Ara h1, an abundant and highly allergenic peanut protein. J Biol Chem 273, 13753-13759
    • (1998) J Biol Chem , vol.273 , pp. 13753-13759
    • Shin, D.S.1
  • 46
    • 1942467835 scopus 로고    scopus 로고
    • Microarray immunoassay: Association of clinical history, in vitro IgE function, and heterogeneity of allergenic peanut epitopes
    • Shreffler, W.G. et al. (2004) Microarray immunoassay: Association of clinical history, in vitro IgE function, and heterogeneity of allergenic peanut epitopes. J Allergy Clin Immunol 113, 776-782
    • (2004) J Allergy Clin Immunol , vol.113 , pp. 776-782
    • Shreffler, W.G.1
  • 47
    • 12444292119 scopus 로고    scopus 로고
    • Characterization of the T-cell epitopes of a major peanut allergen, Ara h 2
    • Glaspole, I.N. et al. (2005) Characterization of the T-cell epitopes of a major peanut allergen, Ara h 2. Allergy 60, 35-40
    • (2005) Allergy , vol.60 , pp. 35-40
    • Glaspole, I.N.1
  • 48
    • 0029938999 scopus 로고    scopus 로고
    • Clinical study of peanut and nut allergy in 62 consecutive patients: New features and associations
    • Ewan, P.W. (1996) Clinical study of peanut and nut allergy in 62 consecutive patients: New features and associations. BMJ 312, 1074-1078
    • (1996) BMJ , vol.312 , pp. 1074-1078
    • Ewan, P.W.1
  • 49
    • 4243260167 scopus 로고    scopus 로고
    • Clinical features of acute allergic reactions to peanut and tree nuts in children
    • Sicherer, S.H., Burks, A.W. and Sampson, H.A. (1998) Clinical features of acute allergic reactions to peanut and tree nuts in children. Pediatrics 102, e6
    • (1998) Pediatrics , vol.102
    • Sicherer, S.H.1    Burks, A.W.2    Sampson, H.A.3
  • 50
    • 0027756799 scopus 로고
    • Pistachio nut hypersensitivity: Identification of pistachio nut allergens
    • Parra, F.M. et al. (1993) Pistachio nut hypersensitivity: Identification of pistachio nut allergens. Clin Exp Allergy 23, 996-1001
    • (1993) Clin Exp Allergy , vol.23 , pp. 996-1001
    • Parra, F.M.1
  • 51
    • 0033502369 scopus 로고    scopus 로고
    • Macadamia nut anaphylaxis: Demonstration of specific IgE reactivity and partial cross-reactivity with hazelnut
    • Sutherland, M.F. et al. (1999) Macadamia nut anaphylaxis: Demonstration of specific IgE reactivity and partial cross-reactivity with hazelnut. J Allergy Clin Immunol 104, 889-890
    • (1999) J Allergy Clin Immunol , vol.104 , pp. 889-890
    • Sutherland, M.F.1
  • 52
    • 0043237875 scopus 로고    scopus 로고
    • Immunological analysis of allergenic cross-reactivity between peanut and tree nuts
    • de Leon, M.P. et al. (2003) Immunological analysis of allergenic cross-reactivity between peanut and tree nuts. Clin Exp Allergy 33, 1273-1280
    • (2003) Clin Exp Allergy , vol.33 , pp. 1273-1280
    • de Leon, M.P.1
  • 53
    • 33747857691 scopus 로고    scopus 로고
    • IgE cross-reactivity between the major peanut allergen Ara h 2 and tree nut allergens
    • de Leon, M.P. et al. (2007) IgE cross-reactivity between the major peanut allergen Ara h 2 and tree nut allergens. Mol Immunol 44, 463-471
    • (2007) Mol Immunol , vol.44 , pp. 463-471
    • de Leon, M.P.1
  • 54
    • 0033406009 scopus 로고    scopus 로고
    • Identification and cloning of a complementary DNA encoding a vicilin-like proprotein, Jug r 2, from English walnut kernel (Juglans regia), a major food allergen
    • Teuber, S.S. et al. (1999) Identification and cloning of a complementary DNA encoding a vicilin-like proprotein, Jug r 2, from English walnut kernel (Juglans regia), a major food allergen. J Allergy Clin Immunol 104, 1311-1320
    • (1999) J Allergy Clin Immunol , vol.104 , pp. 1311-1320
    • Teuber, S.S.1
  • 55
    • 0036971325 scopus 로고    scopus 로고
    • Ana o 1, a cashew (Anacardium occidental) allergen of the vicilin seed storage protein family
    • Wang, F. et al. (2002) Ana o 1, a cashew (Anacardium occidental) allergen of the vicilin seed storage protein family. J Allergy Clin Immunol 110, 160-166
    • (2002) J Allergy Clin Immunol , vol.110 , pp. 160-166
    • Wang, F.1
  • 56
    • 0036128335 scopus 로고    scopus 로고
    • Identification of hazelnut major allergens in sensitive patients with positive double-blind, placebo-controlled food challenge results
    • Pastorello, E.A. et al. (2002) Identification of hazelnut major allergens in sensitive patients with positive double-blind, placebo-controlled food challenge results. J Allergy Clin Immunol. 109, 563-570
    • (2002) J Allergy Clin Immunol , vol.109 , pp. 563-570
    • Pastorello, E.A.1
  • 57
    • 0036281796 scopus 로고    scopus 로고
    • Identification and characterisation of the IgE-binding proteins 2S albumin and conglutin gamma in almond (Prunus dulcis) seeds
    • Poltronieri, P. et al. (2002) Identification and characterisation of the IgE-binding proteins 2S albumin and conglutin gamma in almond (Prunus dulcis) seeds. Int Arch Allergy Immunol 128, 97-104
    • (2002) Int Arch Allergy Immunol , vol.128 , pp. 97-104
    • Poltronieri, P.1
  • 58
    • 0032415814 scopus 로고    scopus 로고
    • Sensitization to the major allergen of Brazil nut is correlated with the clinical expression of allergy
    • Pastorello, E.A. et al. (1998) Sensitization to the major allergen of Brazil nut is correlated with the clinical expression of allergy. J Allergy Clin Immunol 102, 1021-1027
    • (1998) J Allergy Clin Immunol , vol.102 , pp. 1021-1027
    • Pastorello, E.A.1
  • 59
    • 0031846740 scopus 로고    scopus 로고
    • Cloning and sequencing of a gene encoding a 2S albumin seed storage protein precursor from English walnut (Juglans regia), a major food allergen
    • Teuber, S.S. et al. (1998) Cloning and sequencing of a gene encoding a 2S albumin seed storage protein precursor from English walnut (Juglans regia), a major food allergen. J Allergy Clin Immunol 101, 807-814
    • (1998) J Allergy Clin Immunol , vol.101 , pp. 807-814
    • Teuber, S.S.1
  • 60
    • 0042044486 scopus 로고    scopus 로고
    • Ana o 2, a major cashew (Anacardium occidentale L.) nut allergen of the legumin family
    • Wang, F. et al. (2003) Ana o 2, a major cashew (Anacardium occidentale L.) nut allergen of the legumin family. Int Arch Allergy Immunol 132, 27-39
    • (2003) Int Arch Allergy Immunol , vol.132 , pp. 27-39
    • Wang, F.1
  • 61
    • 0036740044 scopus 로고    scopus 로고
    • Identification of an 11S globulin as a major hazelnut food allergen in hazelnut-induced systemic reactions
    • Beyer, K. et al. (2002) Identification of an 11S globulin as a major hazelnut food allergen in hazelnut-induced systemic reactions. J Allergy Clin Immunol 110, 517-523
    • (2002) J Allergy Clin Immunol , vol.110 , pp. 517-523
    • Beyer, K.1
  • 62
    • 0043046161 scopus 로고    scopus 로고
    • Identification and cloning of Jug r 4, a major food allergen from English walnut belonging to the legumin group
    • Teuber, S.S. et al. (2003) Identification and cloning of Jug r 4, a major food allergen from English walnut belonging to the legumin group. J Allergy Clin Immunol 111, S248
    • (2003) J Allergy Clin Immunol , vol.111
    • Teuber, S.S.1
  • 63
    • 0024549931 scopus 로고
    • Cross-allergenicity in the legume botanical family in children with food hypersensitivity
    • Bernhisel-Broadbent, J. and Sampson, H.A. (1989) Cross-allergenicity in the legume botanical family in children with food hypersensitivity. J Allergy Clin Immunol 83, 435-440
    • (1989) J Allergy Clin Immunol , vol.83 , pp. 435-440
    • Bernhisel-Broadbent, J.1    Sampson, H.A.2
  • 64
    • 0024308792 scopus 로고
    • Cross-allergenicity in the legume botanical family in children with food hypersensitivity. II. Laboratory correlates
    • Bernhisel-Broadbent, J., Taylor, S. and Sampson, H.A. (1989) Cross-allergenicity in the legume botanical family in children with food hypersensitivity. II. Laboratory correlates. J Allergy Clin Immunol 84, 701-709
    • (1989) J Allergy Clin Immunol , vol.84 , pp. 701-709
    • Bernhisel-Broadbent, J.1    Taylor, S.2    Sampson, H.A.3
  • 65
    • 0030822565 scopus 로고    scopus 로고
    • Poor biologic activity of cross-reactive IgE directed to carbohydrate determinants of glycoproteins
    • van der Veen, M.J. et al. (1997) Poor biologic activity of cross-reactive IgE directed to carbohydrate determinants of glycoproteins. J Allergy Clin Immunol 100, 327-334
    • (1997) J Allergy Clin Immunol , vol.100 , pp. 327-334
    • van der Veen, M.J.1
  • 66
    • 0029905483 scopus 로고    scopus 로고
    • Cross-reactivity between the major allergen from olive pollen and unrelated glycoproteins: Evidence of an epitope in the glycan moiety of the allergen
    • Batanero, E. et al. (1996) Cross-reactivity between the major allergen from olive pollen and unrelated glycoproteins: Evidence of an epitope in the glycan moiety of the allergen. J Allergy Clin Immunol 97, 1264-1271
    • (1996) J Allergy Clin Immunol , vol.97 , pp. 1264-1271
    • Batanero, E.1
  • 67
    • 0029964855 scopus 로고    scopus 로고
    • Ubiquitous structures responsible for IgE cross-reactivity between tomato fruit and grass pollen allergens
    • Petersen, A. et al. (1996) Ubiquitous structures responsible for IgE cross-reactivity between tomato fruit and grass pollen allergens. J Allergy Clin Immunol 98, 805-815
    • (1996) J Allergy Clin Immunol , vol.98 , pp. 805-815
    • Petersen, A.1
  • 68
    • 27744455188 scopus 로고    scopus 로고
    • Functional analysis of cross-reactive immunoglobulin E antibodies: Peanut-specific immunoglobulin E sensitizes basophils; to tree nut allergens
    • de Leon, M.P. et al. (2005) Functional analysis of cross-reactive immunoglobulin E antibodies: Peanut-specific immunoglobulin E sensitizes basophils; to tree nut allergens. Clin Exp Allergy 35, 1056-1064
    • (2005) Clin Exp Allergy , vol.35 , pp. 1056-1064
    • de Leon, M.P.1
  • 69
    • 0032959071 scopus 로고    scopus 로고
    • Modification of a major peanut allergen leads to loss of IgE binding
    • Burks, A.W., King, N. and Bannon, G.A. (1999) Modification of a major peanut allergen leads to loss of IgE binding. Int Arch Allergy Immunol. 118, 313-314
    • (1999) Int Arch Allergy Immunol , vol.118 , pp. 313-314
    • Burks, A.W.1    King, N.2    Bannon, G.A.3
  • 70
    • 27144553159 scopus 로고    scopus 로고
    • Allergenic characteristics of a modified peanut allergen
    • King, N. et al. (2005) Allergenic characteristics of a modified peanut allergen. Mol Nutr Food Res 49, 963-971
    • (2005) Mol Nutr Food Res , vol.49 , pp. 963-971
    • King, N.1
  • 71
    • 0036284952 scopus 로고    scopus 로고
    • Modification of peanut allergen Ara h 3: Effects on IgE binding and T cell stimulation
    • Rabjohn, P. et al. (2002) Modification of peanut allergen Ara h 3: effects on IgE binding and T cell stimulation. Int Arch Allergy Immunol 128, 15-23
    • (2002) Int Arch Allergy Immunol , vol.128 , pp. 15-23
    • Rabjohn, P.1
  • 72
    • 0035044672 scopus 로고    scopus 로고
    • Engineering, characterization and in vitro efficacy of the major peanut allergens for use in immunotherapy
    • Bannon, G.A. et al. (2001) Engineering, characterization and in vitro efficacy of the major peanut allergens for use in immunotherapy. Int Arch Allergy Immunol. 124, 70-72
    • (2001) Int Arch Allergy Immunol , vol.124 , pp. 70-72
    • Bannon, G.A.1
  • 73
    • 21844468271 scopus 로고    scopus 로고
    • The promiscuity of immunoglobulin E binding to peanut allergens, as determined by Western blotting, correlates with the severity of clinical symptoms
    • Lewis, S.A. et al. (2005) The promiscuity of immunoglobulin E binding to peanut allergens, as determined by Western blotting, correlates with the severity of clinical symptoms. Clin Exp Allergy 35, 767-773
    • (2005) Clin Exp Allergy , vol.35 , pp. 767-773
    • Lewis, S.A.1
  • 74
    • 0027323846 scopus 로고
    • Peripheral T cell tolerance induced in naive and primed mice by subcutaneous injection of peptides from the major cat allergen Feld 1
    • Briner, T. et al. (1993) Peripheral T cell tolerance induced in naive and primed mice by subcutaneous injection of peptides from the major cat allergen Feld 1. Proc Natl Acad Sci USA 90, 7608-7612
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 7608-7612
    • Briner, T.1
  • 75
    • 0027451437 scopus 로고
    • Inhibition of T cell and antibody responses to house dust mite allergen by inhalation of dominant Tell epitope in naive and sensitized mice
    • Hoyne, G.F. et al. (1993) Inhibition of T cell and antibody responses to house dust mite allergen by inhalation of dominant Tell epitope in naive and sensitized mice. J Exp Med 178, 1783-1788
    • (1993) J Exp Med , vol.178 , pp. 1783-1788
    • Hoyne, G.F.1
  • 76
    • 0037031090 scopus 로고    scopus 로고
    • Effect of T-cell peptides derived from Fel d 1 on allergic reactions and cytokine production in patients sensitive to cats: A randomised controlled trial
    • Oldfield, W.L., Larche, M. and Kay, A.B. (2002) Effect of T-cell peptides derived from Fel d 1 on allergic reactions and cytokine production in patients sensitive to cats: A randomised controlled trial. Lancet 360, 47-53
    • (2002) Lancet , vol.360 , pp. 47-53
    • Oldfield, W.L.1    Larche, M.2    Kay, A.B.3
  • 77
    • 24744438448 scopus 로고    scopus 로고
    • The effect of Fel d 1-derived T-cell peptides on upper and lower airway outcome measurements in cat-allergic subjects
    • Alexander, C. et al. (2005) The effect of Fel d 1-derived T-cell peptides on upper and lower airway outcome measurements in cat-allergic subjects. Allergy 60, 1269-1274
    • (2005) Allergy , vol.60 , pp. 1269-1274
    • Alexander, C.1
  • 78
    • 0031866059 scopus 로고    scopus 로고
    • 2 induces specific T cell anergy in bee sting allergic patients
    • 2 induces specific T cell anergy in bee sting allergic patients. J Allergy Clin Immunol. 101, 747-757
    • (1998) J Allergy Clin Immunol , vol.101 , pp. 747-757
    • Muller, U.R.1
  • 79
    • 6344225313 scopus 로고    scopus 로고
    • Hypoallergenic variants of the major latex allergen Hev b 6.01 retaining human T lymphocyte reactivity
    • Drew, A.C. et al. (2004) Hypoallergenic variants of the major latex allergen Hev b 6.01 retaining human T lymphocyte reactivity. J Immunol 173, 5872-5879
    • (2004) J Immunol , vol.173 , pp. 5872-5879
    • Drew, A.C.1
  • 80
    • 0037434895 scopus 로고    scopus 로고
    • Effect of anti-IgE therapy in patients with peanut allergy
    • Leung, D.Y. et al. (2003) Effect of anti-IgE therapy in patients with peanut allergy. N Engl J Med 348, 986-993
    • (2003) N Engl J Med , vol.348 , pp. 986-993
    • Leung, D.Y.1
  • 82
    • 0035191476 scopus 로고    scopus 로고
    • Oral administration of IL-12 suppresses anaphylactic reactions in a murine model of peanut hypersensitivity
    • Lee, S.Y. et al. (2001) Oral administration of IL-12 suppresses anaphylactic reactions in a murine model of peanut hypersensitivity. Clin Immunol 101, 220-228
    • (2001) Clin Immunol , vol.101 , pp. 220-228
    • Lee, S.Y.1
  • 83
    • 0034769432 scopus 로고    scopus 로고
    • Food Allergy Herbal Formula-1 (FAHF-1) blocks peanut-induced anaphylaxis in a murine model
    • Li, X.M. et al. (2001) Food Allergy Herbal Formula-1 (FAHF-1) blocks peanut-induced anaphylaxis in a murine model. J Allergy Clin Immunol 108, 639-646
    • (2001) J Allergy Clin Immunol , vol.108 , pp. 639-646
    • Li, X.M.1
  • 84
    • 33644907744 scopus 로고    scopus 로고
    • Immune mechanisms of allergen-specific sublingual immunotherapy
    • Moingeon, P. et al. (2006) Immune mechanisms of allergen-specific sublingual immunotherapy. Allergy 61, 151-165
    • (2006) Allergy , vol.61 , pp. 151-165
    • Moingeon, P.1
  • 85
    • 33746691245 scopus 로고    scopus 로고
    • Efficacy and safety of sublingual immunotherapy with grass allergen tablets for seasonal allergic rhinoconjunctivitis
    • Dahl, R. et al. (2006) Efficacy and safety of sublingual immunotherapy with grass allergen tablets for seasonal allergic rhinoconjunctivitis. J Allergy Clin Immunol 118, 434-440
    • (2006) J Allergy Clin Immunol , vol.118 , pp. 434-440
    • Dahl, R.1
  • 86
    • 0033006767 scopus 로고    scopus 로고
    • Sublingual-swallow immunotherapy (SLIT) in patients with asthma due to house-dust mites: A double-blind, placebo-controlled study
    • Bousquet, J. et al. (1999) Sublingual-swallow immunotherapy (SLIT) in patients with asthma due to house-dust mites: A double-blind, placebo-controlled study. Allergy 54, 249-260
    • (1999) Allergy , vol.54 , pp. 249-260
    • Bousquet, J.1
  • 87
    • 27644459770 scopus 로고    scopus 로고
    • Sublingual immunotherapy for hazelnut food allergy: A randomized, double-blind, placebo-controlled study with a standardized hazelnut extract
    • Enrique, E. et al. (2005) Sublingual immunotherapy for hazelnut food allergy: A randomized, double-blind, placebo-controlled study with a standardized hazelnut extract. J Allergy Clin Immunol 116, 1073-1079
    • (2005) J Allergy Clin Immunol , vol.116 , pp. 1073-1079
    • Enrique, E.1
  • 88
    • 0033836431 scopus 로고    scopus 로고
    • Structural biology of allergens
    • Aalberse, R.C. (2000) Structural biology of allergens. J Allergy Clin Immunol. 106, 228-238
    • (2000) J Allergy Clin Immunol , vol.106 , pp. 228-238
    • Aalberse, R.C.1
  • 89
    • 0034995912 scopus 로고    scopus 로고
    • Cross-reactivity of IgE antibodies to allergens
    • Aalberse, R.C., Akkerdaas, J.H. and van Ree, R. (2001) Cross-reactivity of IgE antibodies to allergens. Allergy 56, 478-490
    • (2001) Allergy , vol.56 , pp. 478-490
    • Aalberse, R.C.1    Akkerdaas, J.H.2    van Ree, R.3
  • 90
    • 0034966173 scopus 로고    scopus 로고
    • How to make foods safer-genetically modified foods
    • Moseley, B.E. (2001) How to make foods safer-genetically modified foods. Allergy 56 Suppl. 67, 61-63
    • (2001) Allergy , vol.56 , Issue.SUPPL. 67 , pp. 61-63
    • Moseley, B.E.1
  • 91
    • 1042308391 scopus 로고    scopus 로고
    • Reduction of 14-16 kDa allergenic proteins in transgenic rice plants by antisense gene
    • Tada, Y. et al. (1996) Reduction of 14-16 kDa allergenic proteins in transgenic rice plants by antisense gene. FEBS Lett 391, 341-345
    • (1996) FEBS Lett , vol.391 , pp. 341-345
    • Tada, Y.1
  • 92
    • 0038523728 scopus 로고    scopus 로고
    • Genetic modification removes an immunodominant allergen from soybean
    • Herman, E.M. et al. (2003) Genetic modification removes an immunodominant allergen from soybean. Plant Physiol 132, 36-43
    • (2003) Plant Physiol , vol.132 , pp. 36-43
    • Herman, E.M.1
  • 93
    • 14644435040 scopus 로고    scopus 로고
    • A genetic engineering strategy to eliminate peanut allergy
    • Dodo, H., Konan, K. and Viquez, O. (2005) A genetic engineering strategy to eliminate peanut allergy. Curr Allergy Asthma Rep 5, 67-73
    • (2005) Curr Allergy Asthma Rep , vol.5 , pp. 67-73
    • Dodo, H.1    Konan, K.2    Viquez, O.3
  • 94
    • 0034789243 scopus 로고    scopus 로고
    • Post-transcriptional gene silencing in plants
    • Vaucheret, H., Beclin, C. and Fagard, M. (2001) Post-transcriptional gene silencing in plants. J Cell Sci 114, 3083-3091
    • (2001) J Cell Sci , vol.114 , pp. 3083-3091
    • Vaucheret, H.1    Beclin, C.2    Fagard, M.3
  • 95
    • 33646941045 scopus 로고    scopus 로고
    • Spatial clustering of the IgE epitopes on the major timothy grass pollen allergen Phl p 1: Importance for allergenic activity
    • Flicker, S. et al. (2006) Spatial clustering of the IgE epitopes on the major timothy grass pollen allergen Phl p 1: Importance for allergenic activity. J Allergy Clin Immunol 117, 1336-1343
    • (2006) J Allergy Clin Immunol , vol.117 , pp. 1336-1343
    • Flicker, S.1


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