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Volumn 28, Issue 3, 2012, Pages 277-298

Allergenic Diversity among Plant and Animal Food Proteins

Author keywords

2S albumins; Anaphylaxis; Disulfide bonds; Epitope mapping; Food allergy; IgE binding proteins

Indexed keywords

ANIMALIA;

EID: 84861642088     PISSN: 87559129     EISSN: 15256103     Source Type: Journal    
DOI: 10.1080/87559129.2011.635391     Document Type: Review
Times cited : (21)

References (103)
  • 2
    • 0038321369 scopus 로고    scopus 로고
    • Anaphylaxis and emergency treatment
    • Sampson, H.A. 2003. Anaphylaxis and emergency treatment. Pediatrics, 111: 1601-1608.
    • (2003) Pediatrics , vol.111 , pp. 1601-1608
    • Sampson, H.A.1
  • 3
    • 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. and Clare Mills, E.N. 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    Clare Mills, E.N.2
  • 5
    • 77950206110 scopus 로고    scopus 로고
    • Serological and clinical characteristics of children with peanut sensitization in an Asian community
    • Chiang, W.C., Laurent, P., Mona, I.K., Woei, K.L., Anne, G. and Burks, A.W. 2010. Serological and clinical characteristics of children with peanut sensitization in an Asian community. Pediatr. Allergy Immunol., 21: 429-438.
    • (2010) Pediatr. Allergy Immunol. , vol.21 , pp. 429-438
    • Chiang, W.C.1    Laurent, P.2    Mona, I.K.3    Woei, K.L.4    Anne, G.5    Burks, A.W.6
  • 6
    • 13844267013 scopus 로고    scopus 로고
    • Allergenic proteins in soybean: Processing and reduction of P34 allergenicity
    • Wilson, S., Blaschek, K., Gonzalez and de, M.E. 2005. Allergenic proteins in soybean: Processing and reduction of P34 allergenicity. Nutr. Rev., 63: 47-58.
    • (2005) Nutr. Rev. , vol.63 , pp. 47-58
    • Wilson, S.1    Blaschek, K.2    de Gonzalez, M.E.3
  • 7
    • 54249168572 scopus 로고    scopus 로고
    • In vitro and in vivo cross-reactivity studies of legume allergy in a Mediterranean population
    • Mercedes, M.S.I., María, D.I., Enrique, F.C. and Jerónimo, C. 2008. In vitro and in vivo cross-reactivity studies of legume allergy in a Mediterranean population. Int. Arch. Allergy Immunol., 147: 222-230.
    • (2008) Int. Arch. Allergy Immunol. , vol.147 , pp. 222-230
    • Mercedes, M.S.I.1    María, D.I.2    Enrique, F.C.3    Jerónimo, C.4
  • 9
    • 77956341001 scopus 로고    scopus 로고
    • Partial characterization of red gram (Cajanus cajan L. Millsp) polypeptides recognized by patients exhibiting rhinitis and bronchial asthma
    • Misra, A., Kumar, R., Mishra, V., Chaudhari, B.P., Tripathi, A., Das, M. and Dwivedi, P.D. 2010. Partial characterization of red gram (Cajanus cajan L. Millsp) polypeptides recognized by patients exhibiting rhinitis and bronchial asthma. Food Chem. Toxicol., 48: 2725-2736.
    • (2010) Food Chem. Toxicol. , vol.48 , pp. 2725-2736
    • Misra, A.1    Kumar, R.2    Mishra, V.3    Chaudhari, B.P.4    Tripathi, A.5    Das, M.6    Dwivedi, P.D.7
  • 10
    • 79960394742 scopus 로고    scopus 로고
    • Potential allergens of green gram (Vigna radiata L. Millsp) identified as members of cupin superfamily and seed albumin
    • Misra, A., Kumar, R., Mishra, V., Chaudhari, B.P., Raisuddin, S., Mukul, Das and Dwivedi, P.D. 2011. Potential allergens of green gram (Vigna radiata L. Millsp) identified as members of cupin superfamily and seed albumin. Clin. Exp. Allergy., 41: 1157-1168.
    • (2011) Clin. Exp. Allergy. , vol.41 , pp. 1157-1168
    • Misra, A.1    Kumar, R.2    Mishra, V.3    Chaudhari, B.P.4    Raisuddin, S.5    Mukul, D.6    Dwivedi, P.D.7
  • 12
    • 33845879657 scopus 로고    scopus 로고
    • pepsin resistant 20 kDa protein found in red kidney bean (Phaseolus vulgaris L.) identified as basic subunit of legumin, Biosci
    • Momma, M. A. 2006. pepsin resistant 20 kDa protein found in red kidney bean (Phaseolus vulgaris L.) identified as basic subunit of legumin, Biosci. Biotechnol. Biochem., 70: 3058-3061.
    • (2006) Biotechnol. Biochem. , vol.70 , pp. 3058-3061
    • Momma, M.A.1
  • 13
    • 80054678810 scopus 로고    scopus 로고
    • Allergenic responses of red kidney bean (Phaseolus vulgaris cv chitra) polypeptides in BALB/c mice recognized by bronchial asthma and allergic rhinitis patients
    • Kumar, S., Verma, A.K., Misra, A., Tripathi, A., Chaudhari, B.P., Prasad, R., Jain, S.K., Das, M. and Dwivedi, P.D. 2011. Allergenic responses of red kidney bean (Phaseolus vulgaris cv chitra) polypeptides in BALB/c mice recognized by bronchial asthma and allergic rhinitis patients. Food Res. Int., 44: 2868-2879.
    • (2011) Food Res. Int. , vol.44 , pp. 2868-2879
    • Kumar, S.1    Verma, A.K.2    Misra, A.3    Tripathi, A.4    Chaudhari, B.P.5    Prasad, R.6    Jain, S.K.7    Das, M.8    Dwivedi, P.D.9
  • 15
    • 84872142995 scopus 로고    scopus 로고
    • Allergenicity of pulses in humans. Grain Legumes No. 35-1st quarter 2002
    • Lallès, J.P. and Peltre, G. "Allergenicity of pulses in humans. Grain Legumes No. 35-1st quarter 2002". In Project report
    • Project report
    • Lallès, J.P.1    Peltre, G.2
  • 16
    • 0037338907 scopus 로고    scopus 로고
    • Profilin is a relevant melon allergen susceptible to pepsin digestion in patients with oral allergy syndrome
    • Rosa, R.P., Jesus, F.C., Julia, R. and Gabriel, S. 2003. Profilin is a relevant melon allergen susceptible to pepsin digestion in patients with oral allergy syndrome. J. Allergy Clin. Immunol., 111: 634-639.
    • (2003) J. Allergy Clin. Immunol. , vol.111 , pp. 634-639
    • Rosa, R.P.1    Jesus, F.C.2    Julia, R.3    Gabriel, S.4
  • 17
    • 4944222065 scopus 로고    scopus 로고
    • Strong allergenicity of Pru av 3, the lipid transfer protein from cherry, is related to high stability against thermal processing and digestion
    • Stephan, S., Iris, L., Kay, F., Mar, S.M.M., Mechthild, R., Christina, H., Ernesto, E., Jonas, L., Anna, C.B. and Stefan, V. 2004. Strong allergenicity of Pru av 3, the lipid transfer protein from cherry, is related to high stability against thermal processing and digestion. J. Allergy Clin. Immunol., 114: 900-907.
    • (2004) J. Allergy Clin. Immunol. , vol.114 , pp. 900-907
    • Stephan, S.1    Iris, L.2    Kay, F.3    Mar, S.M.M.4    Mechthild, R.5    Christina, H.6    Ernesto, E.7    Jonas, L.8    Anna, C.B.9    Stefan, V.10
  • 18
    • 72449124198 scopus 로고    scopus 로고
    • Apple (Malus domestica L. Borkh.) Allergen Mal d 1: Effect of cultivar, cultivation system, and storage conditions
    • Anne, M. and Michaela, S.E. 2009. Apple (Malus domestica L. Borkh.) Allergen Mal d 1: Effect of cultivar, cultivation system, and storage conditions. J. Agric. Food Chem., 57: 10548-10553.
    • (2009) J. Agric. Food Chem. , vol.57 , pp. 10548-10553
    • Anne, M.1    Michaela, S.E.2
  • 19
    • 85056063589 scopus 로고    scopus 로고
    • 2S Albumin storage proteins: What makes them food allergens?
    • Moreno, F.J. and Alfonso, C. 2008. 2S Albumin storage proteins: What makes them food allergens?. Open Biochem. J., 2: 16-28.
    • (2008) Open Biochem. J. , vol.2 , pp. 16-28
    • Moreno, F.J.1    Alfonso, C.2
  • 21
    • 0036864152 scopus 로고    scopus 로고
    • Clinical importance of non-specific lipid transfer proteins as food allergens
    • Van, R.R. 2002. Clinical importance of non-specific lipid transfer proteins as food allergens. Biochem. Soc. Trans., 30: 910-913.
    • (2002) Biochem. Soc. Trans. , vol.30 , pp. 910-913
    • Van, R.R.1
  • 24
    • 2342477126 scopus 로고    scopus 로고
    • In: In: Mills E., Shewry P., editors Oxford: Plant Food Allergens; Blackwell
    • Radauer, C. and Hoffmann-Sommergruber, K. 2004. Edited by: In: Mills, E. and Shewry, P. 105-124. Oxford: Plant Food Allergens; Blackwell.
    • (2004) , pp. 105-124
    • Radauer, C.1    Hoffmann-Sommergruber, K.2
  • 25
    • 0031568307 scopus 로고    scopus 로고
    • The molecular basis for allergen cross-reactivity: Crystal structure and IgE-epitope mapping of birch pollen profilin
    • Fedorov, A.A., Ball, T., Mahoney, N.M., Valenta, R. and Almo, S.C. 1997. The molecular basis for allergen cross-reactivity: Crystal structure and IgE-epitope mapping of birch pollen profilin. Structure, 5: 33-45.
    • (1997) Structure , vol.5 , pp. 33-45
    • Fedorov, A.A.1    Ball, T.2    Mahoney, N.M.3    Valenta, R.4    Almo, S.C.5
  • 27
    • 0036724482 scopus 로고    scopus 로고
    • The 18 kDa peanut oleosin is a candidate allergen for IgE-mediated reactions to peanuts
    • Pons, L., Chery, C., Romano, A., Namour, F., Artesani, M.C. and Gueant, J.L. 2002. The 18 kDa peanut oleosin is a candidate allergen for IgE-mediated reactions to peanuts. Allergy, 57: 88-93.
    • (2002) Allergy , vol.57 , pp. 88-93
    • Pons, L.1    Chery, C.2    Romano, A.3    Namour, F.4    Artesani, M.C.5    Gueant, J.L.6
  • 28
    • 0033909638 scopus 로고    scopus 로고
    • Plant allergens and pathogenesis-related proteins. What do they have in common? Int
    • Hoffmann-Sommergruber, K. 2000. Plant allergens and pathogenesis-related proteins. What do they have in common? Int. Arch. Allergy Immunol., 122: 155-166.
    • (2000) Arch. Allergy Immunol. , vol.122 , pp. 155-166
    • Hoffmann-Sommergruber, K.1
  • 29
    • 0001008022 scopus 로고
    • Functional implications of the subcellular localization of ethylene-induced chitinase and [beta]-1,3-glucanase in bean leaves
    • Mauch, F. and Staehelin, L.A. 1989. Functional implications of the subcellular localization of ethylene-induced chitinase and [beta]-1,3-glucanase in bean leaves. Plant Cell, 1: 447-457.
    • (1989) Plant Cell , vol.1 , pp. 447-457
    • Mauch, F.1    Staehelin, L.A.2
  • 30
    • 2342578126 scopus 로고    scopus 로고
    • Thaumatin-like proteins-A new family of pollen and fruit allergens
    • Breiteneder, H. 2004. Thaumatin-like proteins-A new family of pollen and fruit allergens. Allergy, 59: 479-481.
    • (2004) Allergy , vol.59 , pp. 479-481
    • Breiteneder, H.1
  • 31
    • 7744242401 scopus 로고    scopus 로고
    • Identification of the 23-kDa peptide derived from the precursor of Gly m Bd 28K, a major soybean allergen, as a new allergen
    • Hiemori, M., Ito, H., Kimoto, M., Yamashita, H., Nishizawa, K., Maruyama, N., Utsumi, S. and Tsuji, H. 2004. Identification of the 23-kDa peptide derived from the precursor of Gly m Bd 28K, a major soybean allergen, as a new allergen. Biochim. Biophys. Acta, 18: 174-183.
    • (2004) Biochim. Biophys. Acta , vol.18 , pp. 174-183
    • Hiemori, M.1    Ito, H.2    Kimoto, M.3    Yamashita, H.4    Nishizawa, K.5    Maruyama, N.6    Utsumi, S.7    Tsuji, H.8
  • 34
    • 0029791731 scopus 로고    scopus 로고
    • Identification of casein as the major allergenic and antigenic protein of cow's milk
    • Docena, G.H., Fernandez, R., Chirdo, F.G. and Fossati, C.A. 1996. Identification of casein as the major allergenic and antigenic protein of cow's milk. Allergy, 51: 412-416.
    • (1996) Allergy , vol.51 , pp. 412-416
    • Docena, G.H.1    Fernandez, R.2    Chirdo, F.G.3    Fossati, C.A.4
  • 36
    • 0030779139 scopus 로고    scopus 로고
    • Relationship between food-specific concentrations and risk of positive food challenges in children and adolescents
    • Sampson, H.A. and Ho, D.G. 1997. Relationship between food-specific concentrations and risk of positive food challenges in children and adolescents. J. Allergy Clin. Immunol., 100: 444-451.
    • (1997) J. Allergy Clin. Immunol. , vol.100 , pp. 444-451
    • Sampson, H.A.1    Ho, D.G.2
  • 37
    • 0142025335 scopus 로고    scopus 로고
    • Seafood allergy and allergens: A review
    • Lehrere, S.B., Ayuso, R. and Reese, G. 2003. Seafood allergy and allergens: A review. Mar. Biotechnol., 5: 339-348.
    • (2003) Mar. Biotechnol. , vol.5 , pp. 339-348
    • Lehrere, S.B.1    Ayuso, R.2    Reese, G.3
  • 38
    • 39049167419 scopus 로고    scopus 로고
    • Molluscan shellfish allergy
    • Taylor, S.L. 2008. Molluscan shellfish allergy. Adv. Food Nutr. Res., 54: 139-177.
    • (2008) Adv. Food Nutr. Res. , vol.54 , pp. 139-177
    • Taylor, S.L.1
  • 41
    • 53049084916 scopus 로고    scopus 로고
    • Myosin light chain is a novel shrimp allergen, Lit v 3
    • Ayuso, R., Grishina, G. and Bardina, L. 2008. Myosin light chain is a novel shrimp allergen, Lit v 3. J. Allergy Clin. Immunol, 122: 795-802.
    • (2008) J. Allergy Clin. Immunol , vol.122 , pp. 795-802
    • Ayuso, R.1    Grishina, G.2    Bardina, L.3
  • 43
    • 0036265416 scopus 로고    scopus 로고
    • Electrosorption of pectin onto casein micelles
    • Tuinier, R., Rolin, C. and de Kruif, C.G. 2002. Electrosorption of pectin onto casein micelles. Biomacromolecules, 3: 632-638.
    • (2002) Biomacromolecules , vol.3 , pp. 632-638
    • Tuinier, R.1    Rolin, C.2    de Kruif, C.G.3
  • 45
    • 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
    • Karin Hoffmann-Sommergruber and Clare Mills, E.N. 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
    • Karin, H.-S.1    Clare Mills, E.N.2
  • 46
    • 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, H.M., Dintzis, R.Z. and Sampson, H.A. 1994. 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., 93: 1047-1059.
    • (1994) J. Allergy Clin. Immunol. , vol.93 , pp. 1047-1059
    • Bernhisel-Broadbent, J.1    Dintzis, H.M.2    Dintzis, R.Z.3    Sampson, H.A.4
  • 47
    • 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
    • Karin, H.S. and Mills, E.N.C. 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
    • Karin, H.S.1    Mills, E.N.C.2
  • 48
    • 0036977345 scopus 로고    scopus 로고
    • Cow's milk proteins/allergens
    • Wa, J.M. 2002. Cow's milk proteins/allergens. Ann. Allergy Asthma Immunol., 89: 3-10.
    • (2002) Ann. Allergy Asthma Immunol. , vol.89 , pp. 3-10
    • Wa, J.M.1
  • 49
    • 77955565827 scopus 로고    scopus 로고
    • DBT, Department of Biotechnology, Ministry of Science and Technology, Government of India: New Delhi
    • DBT. Protocols for Food and Feed Safety Assessment of GE Crops, Department of Biotechnology, Ministry of Science and Technology, Government of India: New Delhi, 2008.
    • (2008) Protocols for Food and Feed Safety Assessment of GE Crops
  • 50
    • 0037145909 scopus 로고    scopus 로고
    • Digestibility of food allergens and nonallergenic proteins in simulated gastric fluid and simulated intestinal fluids: A comparative study
    • Fu, T., Abbott, U.R. and Hatzos, C. 2002. Digestibility of food allergens and nonallergenic proteins in simulated gastric fluid and simulated intestinal fluids: A comparative study. J. Agric. Food Chem., 50: 7154-7160.
    • (2002) J. Agric. Food Chem. , vol.50 , pp. 7154-7160
    • Fu, T.1    Abbott, U.R.2    Hatzos, C.3
  • 51
    • 0027052241 scopus 로고
    • Allergenicity of peanut and soybean extracts altered by chemical or thermal denaturation in patients with atopic dermatitis and positive food challenges
    • Burks, A.W., Williams, L.W., Thresher, W., Connaughton, C., Cockrell, G. and Helm, R.M. 1992. Allergenicity of peanut and soybean extracts altered by chemical or thermal denaturation in patients with atopic dermatitis and positive food challenges. J. Allergy Clin. Immunol., 90: 889-897.
    • (1992) J. Allergy Clin. Immunol. , vol.90 , pp. 889-897
    • Burks, A.W.1    Williams, L.W.2    Thresher, W.3    Connaughton, C.4    Cockrell, G.5    Helm, R.M.6
  • 52
    • 20744457806 scopus 로고    scopus 로고
    • Allergy to peanuts
    • Pastorello, E. 2004. Allergy to peanuts. EFSA J., 34: 76-84.
    • (2004) EFSA J. , vol.34 , pp. 76-84
    • Pastorello, E.1
  • 53
    • 0035947026 scopus 로고    scopus 로고
    • Determination of the allergenicity of various hazelnut products by immunoblotting and enzyme allergosorbent test inhibition
    • Wigotzki, M., Steinhart, H. and Paschke, A. 2001. Determination of the allergenicity of various hazelnut products by immunoblotting and enzyme allergosorbent test inhibition. J. Chromatogr. B Biomed. Sci. Appl., 756: 239-248.
    • (2001) J. Chromatogr. B Biomed. Sci. Appl. , vol.756 , pp. 239-248
    • Wigotzki, M.1    Steinhart, H.2    Paschke, A.3
  • 54
    • 22244464599 scopus 로고    scopus 로고
    • Plant food allergens-Structural and functional aspects of allergenicity
    • Breiteneder, H. and Mills, E.N.C. 2005. Plant food allergens-Structural and functional aspects of allergenicity. Biotechnol. Adv., 23: 395-399.
    • (2005) Biotechnol. Adv. , vol.23 , pp. 395-399
    • Breiteneder, H.1    Mills, E.N.C.2
  • 56
    • 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
  • 57
    • 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
  • 58
    • 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. and Clare Mills, E.N. 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    Clare Mills, E.N.2
  • 59
    • 0030038821 scopus 로고    scopus 로고
    • The main IgE-binding epitope of a major latex allergen, prohevein, is present in its N-terminal 43-amino acid fragment, hevein
    • Alenius, H., Kalkkinen, N., Reunala, T. and Turjanmaa, K.P.T. 1996. The main IgE-binding epitope of a major latex allergen, prohevein, is present in its N-terminal 43-amino acid fragment, hevein. J. Immunol., 156: 1618-1625.
    • (1996) J. Immunol. , vol.156 , pp. 1618-1625
    • Alenius, H.1    Kalkkinen, N.2    Reunala, T.3    Turjanmaa, K.P.T.4
  • 60
    • 0024308792 scopus 로고
    • Cross-allergenicity in the legume botanical family in children with food hypersensitivity. II. Laboratory correlates
    • Bernhisel, B.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, B.J.1    Taylor, S.2    Sampson, H.A.3
  • 61
    • 0024549931 scopus 로고
    • Cross-allergenicity in the legume botanical family in children with food hypersensitivity
    • Bernhisel, B.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, B.J.1    Sampson, H.A.2
  • 62
    • 33847370670 scopus 로고    scopus 로고
    • Relevance of serum IgE estimation in allergic bronchial asthma with special reference to food allergy
    • Kumar, R., Singh, B.P., Srivastava, P., Sridhara, S., Arora, N. and Gaur, S.N. 2006. Relevance of serum IgE estimation in allergic bronchial asthma with special reference to food allergy. Asian Pac. J. Allergy Immunol., 24: 191-199.
    • (2006) Asian Pac. J. Allergy Immunol. , vol.24 , pp. 191-199
    • Kumar, R.1    Singh, B.P.2    Srivastava, P.3    Sridhara, S.4    Arora, N.5    Gaur, S.N.6
  • 65
    • 40349087275 scopus 로고    scopus 로고
    • Severe immediate type hypersensitivity reactions in 105 German adults: When to diagnose anaphylaxis
    • Treudler, R., Kozovska, Y. and Simon, J.C. 2008. Severe immediate type hypersensitivity reactions in 105 German adults: When to diagnose anaphylaxis. J. Invest. Allergol. Clin. Immunol., 18: 52-58.
    • (2008) J. Invest. Allergol. Clin. Immunol. , vol.18 , pp. 52-58
    • Treudler, R.1    Kozovska, Y.2    Simon, J.C.3
  • 66
    • 0022326904 scopus 로고
    • T-lymphocyte recognition of antigen in association with gene products of the major histocompatibility complex
    • Schwartz, R.H. 1985. T-lymphocyte recognition of antigen in association with gene products of the major histocompatibility complex. Annu. Rev. Immunol., 3: 237-61.
    • (1985) Annu. Rev. Immunol. , vol.3 , pp. 237-261
    • Schwartz, R.H.1
  • 67
    • 0023388061 scopus 로고
    • Antigen requirements for activation of MHC restricted responses
    • Moller, G. 1987. Antigen requirements for activation of MHC restricted responses. Immunol. Rev., 98: 1-187.
    • (1987) Immunol. Rev. , vol.98 , pp. 1-187
    • Moller, G.1
  • 68
    • 0023720148 scopus 로고
    • cell antigen receptor genes and T cell recognition
    • Davis, M.M. and Bjorkman, P. T. 1988. cell antigen receptor genes and T cell recognition. Nature, 334: 395-402.
    • (1988) Nature , vol.334 , pp. 395-402
    • Davis, M.M.1    Bjorkman, P.T.2
  • 69
    • 0026612253 scopus 로고
    • Fc epsilon R1-mediated tyrosine phosphorylation of multiple proteins, including phospholipase C gamma 1 and the receptor beta gamma 2 complex, in RBL-2H3 rat basophilic leukemia cells
    • Li, W., Deanin, G.G., Margolis, B., Schlessinger, J. and Oliver, J.M. 1992. Fc epsilon R1-mediated tyrosine phosphorylation of multiple proteins, including phospholipase C gamma 1 and the receptor beta gamma 2 complex, in RBL-2H3 rat basophilic leukemia cells. Mol. Cell. Biol., 12: 3176-3182.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 3176-3182
    • Li, W.1    Deanin, G.G.2    Margolis, B.3    Schlessinger, J.4    Oliver, J.M.5
  • 70
    • 33847300398 scopus 로고    scopus 로고
    • Proximal signaling events in Fcε{lunate}RI-mediated mast cell activation
    • Kambayashi, T. and Koretzky, G.A. 2007. Proximal signaling events in Fcε{lunate}RI-mediated mast cell activation. J. Allergy Clin. Immunol., 119: 544-552.
    • (2007) J. Allergy Clin. Immunol. , vol.119 , pp. 544-552
    • Kambayashi, T.1    Koretzky, G.A.2
  • 71
    • 68549122812 scopus 로고    scopus 로고
    • Studies on the specific degranulation of mast cell sensitized by several allergens in vitro
    • Guo, Y., Li, Z., Hong, L., Haider, S. and Jamil, K. 2009. Studies on the specific degranulation of mast cell sensitized by several allergens in vitro. Cell. Mol. Immunol., 6: 149-153.
    • (2009) Cell. Mol. Immunol. , vol.6 , pp. 149-153
    • Guo, Y.1    Li, Z.2    Hong, L.3    Haider, S.4    Jamil, K.5
  • 72
    • 0020412872 scopus 로고
    • Food allergens and basophil histamine release in recurrent aphthous stomatitis
    • Wray, D., Vlagopoulos, T.P. and Siraganian, R.P. 1982. Food allergens and basophil histamine release in recurrent aphthous stomatitis. Oral Surg. Oral Med. Oral Pathol., 54: 388-395.
    • (1982) Oral Surg. Oral Med. Oral Pathol. , vol.54 , pp. 388-395
    • Wray, D.1    Vlagopoulos, T.P.2    Siraganian, R.P.3
  • 73
    • 48349112679 scopus 로고    scopus 로고
    • Prevalence of legume sensitization in patients with naso-bronchial allergy
    • Misra, A., Prasad, R., Das, M. and Dwivedi, P.D. 2008. Prevalence of legume sensitization in patients with naso-bronchial allergy. Immunopharmacol. Immunotoxicol., 30: 529-542.
    • (2008) Immunopharmacol. Immunotoxicol. , vol.30 , pp. 529-542
    • Misra, A.1    Prasad, R.2    Das, M.3    Dwivedi, P.D.4
  • 74
    • 77953378432 scopus 로고    scopus 로고
    • A study of skin sensitivity to various allergens by skin prick test in patients of nasobronchial allergy
    • Prasad, R., Verma, S.K., Dua, R., Kant, S., Kushwaha, R.A.S. and Agarwal, S.P. 2009. A study of skin sensitivity to various allergens by skin prick test in patients of nasobronchial allergy. Lung India., 26: 70-73.
    • (2009) Lung India. , vol.26 , pp. 70-73
    • Prasad, R.1    Verma, S.K.2    Dua, R.3    Kant, S.4    Kushwaha, R.A.S.5    Agarwal, S.P.6
  • 76
    • 3242781598 scopus 로고    scopus 로고
    • Kiwifruit is a significant allergen and is associated with differing patterns of reactivity in children and adults
    • Lucas, J.S., Grimshaw, K.E., Collins, K.W.J.O. and Hourihane, J.O. 2004. Kiwifruit is a significant allergen and is associated with differing patterns of reactivity in children and adults. Clin. Exp. Allergy, 34: 1115-1121.
    • (2004) Clin. Exp. Allergy , vol.34 , pp. 1115-1121
    • Lucas, J.S.1    Grimshaw, K.E.2    Collins, K.W.J.O.3    Hourihane, J.O.4
  • 77
    • 26944489629 scopus 로고    scopus 로고
    • Treatment of eosinophilic esophagitis with specific food elimination diet directed by a combination of skin prick and patch tests
    • Spergel, J.M., Andrews, T., Brown-Whitehorn, T.F., Beausoleil, J.L. and Liacouras, C.A. 2005. Treatment of eosinophilic esophagitis with specific food elimination diet directed by a combination of skin prick and patch tests. Ann. Allergy Asthma Immunol., 95: 336-343.
    • (2005) Ann. Allergy Asthma Immunol. , vol.95 , pp. 336-343
    • Spergel, J.M.1    Andrews, T.2    Brown-Whitehorn, T.F.3    Beausoleil, J.L.4    Liacouras, C.A.5
  • 79
    • 79953244010 scopus 로고    scopus 로고
    • Datau. Recurrent aphthous stomatitis caused by food allergy
    • Wardhana, E.A. 2010. Datau. Recurrent aphthous stomatitis caused by food allergy. Acta Med. Indones., 42: 236-240.
    • (2010) Acta Med. Indones. , vol.42 , pp. 236-240
    • Wardhana, E.A.1
  • 81
    • 11344253871 scopus 로고    scopus 로고
    • Food protein-induced enterocolitis syndrome: Case presentations and management lessons
    • Sicherer, S.H. 2005. Food protein-induced enterocolitis syndrome: Case presentations and management lessons. J. Allergy Clin. Immunol., 115: 149-156.
    • (2005) J. Allergy Clin. Immunol. , vol.115 , pp. 149-156
    • Sicherer, S.H.1
  • 83
    • 0030025737 scopus 로고    scopus 로고
    • Histamine release in skin monitored with the microdialysis technique does not correlate with the weal size induced by cow allergen
    • Horsmanheimo, L., Harvima, I.T. and Harvima, R.J. 1996. Histamine release in skin monitored with the microdialysis technique does not correlate with the weal size induced by cow allergen. Br. J. Dermatol., 134: 94-100.
    • (1996) Br. J. Dermatol. , vol.134 , pp. 94-100
    • Horsmanheimo, L.1    Harvima, I.T.2    Harvima, R.J.3
  • 85
    • 7944219659 scopus 로고    scopus 로고
    • Current approach to the diagnosis and management of adverse reactions to foods
    • Sicherer, S.H. and Teuber, S. 2004. Current approach to the diagnosis and management of adverse reactions to foods. J. Allergy Clin. Immunol., 114: 1146-1150.
    • (2004) J. Allergy Clin. Immunol. , vol.114 , pp. 1146-1150
    • Sicherer, S.H.1    Teuber, S.2
  • 86
    • 18844377420 scopus 로고    scopus 로고
    • Food allergy diagnostics: Scientific and unproven procedures
    • Beyer, K. and Teuber, S.S. 2005. Food allergy diagnostics: Scientific and unproven procedures. Curr. Opin. Allergy Clin. Immunol., 5: 261-266.
    • (2005) Curr. Opin. Allergy Clin. Immunol. , vol.5 , pp. 261-266
    • Beyer, K.1    Teuber, S.S.2
  • 88
    • 0035021315 scopus 로고    scopus 로고
    • Utility of food-specific IgE concentrations in predicting symptomatic food allergy
    • Sampson, H.A. 2001. Utility of food-specific IgE concentrations in predicting symptomatic food allergy. J. Allergy Clin. Immunol., 107: 891-896.
    • (2001) J. Allergy Clin. Immunol. , vol.107 , pp. 891-896
    • Sampson, H.A.1
  • 90
    • 0032944427 scopus 로고    scopus 로고
    • An unproven technique with potentially fatal outcome: Provocation/neutralization in a patient with systemic mastocytosis
    • Teuber, S.S. and Vogt, P.J. 1999. An unproven technique with potentially fatal outcome: Provocation/neutralization in a patient with systemic mastocytosis. Ann Allergy Asthma Immunol., 82: 61-65.
    • (1999) Ann Allergy Asthma Immunol. , vol.82 , pp. 61-65
    • Teuber, S.S.1    Vogt, P.J.2
  • 91
    • 1042298988 scopus 로고    scopus 로고
    • Strategies for converting allergens into hypoallergenic vaccine candidates
    • Vrtala, S., Margarete, F.T., Swoboda, I., Kraft, D. and Valenta, R. 2004. Strategies for converting allergens into hypoallergenic vaccine candidates. Methods, 32: 313-320.
    • (2004) Methods , vol.32 , pp. 313-320
    • Vrtala, S.1    Margarete, F.T.2    Swoboda, I.3    Kraft, D.4    Valenta, R.5
  • 92
    • 0033557358 scopus 로고    scopus 로고
    • Molecular cloning and epitope analysis of the peanut allergen Ara h 3
    • Rabjohn, P., Helm, E.M. and Stanley, J.S. 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    Helm, E.M.2    Stanley, J.S.3
  • 93
    • 79955164120 scopus 로고    scopus 로고
    • Effect of anti-IgE therapy on food allergen specific T cell responses in eosinophil associated gastrointestinal disorders
    • Barbara, F., Foroughi, S., Yin, Y. and Prussin, C. 2011. Effect of anti-IgE therapy on food allergen specific T cell responses in eosinophil associated gastrointestinal disorders. Clin. Mol. Allergy, 9: 7-15.
    • (2011) Clin. Mol. Allergy , vol.9 , pp. 7-15
    • Barbara, F.1    Foroughi, S.2    Yin, Y.3    Prussin, C.4
  • 95
    • 60849124499 scopus 로고    scopus 로고
    • Allergen-related approaches to immunotherapy
    • Jennifer, M., Rolland, L.M.G. and Robyn, E.O. 2009. Allergen-related approaches to immunotherapy. Pharmacol. Ther. Vol., 121: 273-284.
    • (2009) Pharmacol. Ther. , vol.121 , pp. 273-284
    • Jennifer, M.1    Rolland, L.M.G.2    Robyn, E.O.3
  • 96
    • 0022606208 scopus 로고
    • mouse monoclonal IgE antibody anti bovine milk f-lactoglobulin allows studies of allergy in the gastrointestinal tract Clin
    • Dominique, A., Granato and Piguet, P. F. A. 1986. mouse monoclonal IgE antibody anti bovine milk f-lactoglobulin allows studies of allergy in the gastrointestinal tract Clin. Exp. Immunol., 63: 703-710.
    • (1986) Exp. Immunol. , vol.63 , pp. 703-710
    • Dominique, A.1    Granato2    Piguet, P.F.A.3
  • 97
    • 33748672467 scopus 로고    scopus 로고
    • Computational detection of allergenic proteins attains a new level of accuracy with in silico variable-length peptide extraction and machine learning
    • Soeria-Atmadja, D., Lundell, T., Gustafsson, M.G. and Hammerling, U. 2006. Computational detection of allergenic proteins attains a new level of accuracy with in silico variable-length peptide extraction and machine learning. Nucleic Acids Res., 34: 3779-3793.
    • (2006) Nucleic Acids Res. , vol.34 , pp. 3779-3793
    • Soeria-Atmadja, D.1    Lundell, T.2    Gustafsson, M.G.3    Hammerling, U.4
  • 98
    • 2942525199 scopus 로고    scopus 로고
    • Development of a real-time PCR and a sandwich ELISA for detection of potentially allergenic trace amounts of peanut (Arachis hypogaea) in processed foods
    • Stephan, O. and Vieths, S. 2004. Development of a real-time PCR and a sandwich ELISA for detection of potentially allergenic trace amounts of peanut (Arachis hypogaea) in processed foods. J. Agric. Food Chem., 52: 3754-3760.
    • (2004) J. Agric. Food Chem. , vol.52 , pp. 3754-3760
    • Stephan, O.1    Vieths, S.2
  • 99
    • 79951659609 scopus 로고    scopus 로고
    • Liquid chromatography and mass spectrometry in food allergen detection
    • Faeste, C.K., Ronning, H.T., Christians, U. and Granum, P.E. 2011. Liquid chromatography and mass spectrometry in food allergen detection. J. Food Prot., 74: 316-345.
    • (2011) J. Food Prot. , vol.74 , pp. 316-345
    • Faeste, C.K.1    Ronning, H.T.2    Christians, U.3    Granum, P.E.4
  • 100
    • 74049126605 scopus 로고    scopus 로고
    • Analysis of food proteins and peptides by mass spectrometry-based techniques
    • Mamone, G., Picariello, G., Caira, S., Addeo, F. and Ferranti, P. 2009. Analysis of food proteins and peptides by mass spectrometry-based techniques. J. Chromatogr. A, 1216: 7130-7142.
    • (2009) J. Chromatogr. A , vol.1216 , pp. 7130-7142
    • Mamone, G.1    Picariello, G.2    Caira, S.3    Addeo, F.4    Ferranti, P.5
  • 101
    • 78649506541 scopus 로고    scopus 로고
    • Inactivation of allergens and toxins
    • Morandini, P. 2010. Inactivation of allergens and toxins. N. Biotechnol., 27: 482-493.
    • (2010) N. Biotechnol. , vol.27 , pp. 482-493
    • Morandini, P.1
  • 102
    • 0038523728 scopus 로고    scopus 로고
    • Genetic modification removes an immunodominant allergen from soybean
    • Herman, E.M., Helm, R.M., Jung, R. and Kinney, A.J. 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    Helm, R.M.2    Jung, R.3    Kinney, A.J.4
  • 103
    • 0037725393 scopus 로고    scopus 로고
    • Genetically modified soybeans and food allergies
    • Herman, E.M. 2003. Genetically modified soybeans and food allergies. J. Exp. Bot., 54: 1317-1319.
    • (2003) J. Exp. Bot. , vol.54 , pp. 1317-1319
    • Herman, E.M.1


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