메뉴 건너뛰기




Volumn 54, Issue 1, 2010, Pages 93-112

Characterization of plant food allergens: An overview on physicochemical and immunological techniques

Author keywords

Class i food allergen; Class ii food allergen; Immunological characterization; Physicochemical characterization; Plant food allergens

Indexed keywords

PLANT ANTIGEN;

EID: 74349119173     PISSN: 16134125     EISSN: 16134133     Source Type: Journal    
DOI: 10.1002/mnfr.200900096     Document Type: Review
Times cited : (32)

References (156)
  • 1
    • 2342650734 scopus 로고    scopus 로고
    • Update on food allergy
    • quiz 820
    • Sampson, H. A., Update on food allergy. J. Allergy Clin. Immunol. 2004, 113, 805-819; quiz 820.
    • (2004) J. Allergy Clin. Immunol. , vol.113 , pp. 805-819
    • Sampson, H.A.1
  • 2
    • 2342525840 scopus 로고    scopus 로고
    • A classification of plant food allergens
    • quiz 831
    • Breiteneder, H., Radauer, C., A classification of plant food allergens. J. Allergy Clin. Immunol. 2004, 113, 821-830; quiz 831.
    • (2004) J. Allergy Clin. Immunol. , vol.113 , pp. 821-830
    • Breiteneder, H.1    Radauer, C.2
  • 3
    • 41449094497 scopus 로고    scopus 로고
    • Allergens are distributed into few protein families and possess a restricted number of biochemical functions
    • e847
    • Radauer, C., Bublin, M., Wagner, S., Mari, A., Breiteneder, H., Allergens are distributed into few protein families and possess a restricted number of biochemical functions. J. Allergy Clin. Immunol. 2008, 121, 847-852; e847.
    • (2008) J. Allergy Clin. Immunol. , vol.121 , pp. 847-852
    • Radauer, C.1    Bublin, M.2    Wagner, S.3    Mari, A.4    Breiteneder, H.5
  • 4
    • 61349088594 scopus 로고    scopus 로고
    • Molecular properties of plant food allergens, a current classification into protein families
    • Hauser, M., Egger, M., Wallner, M., Wopfner, N. et al., Molecular properties of plant food allergens, a current classification into protein families. Open Immunol. J. 2008, 1, 1-12.
    • (2008) Open Immunol. J. , vol.1 , pp. 1-12
    • Hauser, M.1    Egger, M.2    Wallner, M.3    Wopfner, N.4
  • 5
    • 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., Gadermaier, G. 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    Gadermaier, G.4
  • 6
    • 45149132069 scopus 로고    scopus 로고
    • Reported food allergy to peanut, tree nuts and fruit: Comparison of clinical manifestations, prescription of medication and impact on daily life
    • Le, T. M., Lindner, T. M., Pasmans, S. G., Guikers, C. L. et al., Reported food allergy to peanut, tree nuts and fruit: comparison of clinical manifestations, prescription of medication and impact on daily life. Allergy 2008, 63, 910-916.
    • (2008) Allergy , vol.63 , pp. 910-916
    • Le, T.M.1    Lindner, T.M.2    Pasmans, S.G.3    Guikers, C.L.4
  • 7
    • 0035044994 scopus 로고    scopus 로고
    • Lipid transfer protein: A pan-allergen in plant-derived foods that is highly resistant to pepsin digestion
    • Asero, R., Mistrello, G., Roncarolo, D., de Vries, S. C. et al., Lipid transfer protein: a pan-allergen in plant-derived foods that is highly resistant to pepsin digestion. Int. Arch. Allergy Immunol. 2001, 124, 67-69.
    • (2001) Int. Arch. Allergy Immunol. , vol.124 , pp. 67-69
    • Asero, R.1    Mistrello, G.2    Roncarolo, D.3    de Vries, S.C.4
  • 8
    • 0026542305 scopus 로고
    • Profilins constitute a novel family of functional plant pan- allergens
    • Valenta, R., Duchene, M., Ebner, C., Valent, P. et al., Profilins constitute a novel family of functional plant pan- allergens. J. Exp. Med. 1992, 175, 377-385.
    • (1992) J. Exp. Med. , vol.175 , pp. 377-385
    • Valenta, R.1    Duchene, M.2    Ebner, C.3    Valent, P.4
  • 9
    • 0033998580 scopus 로고    scopus 로고
    • Fennel, cucumber, and melon allergy success- fully treated with pollen-specific injection immunotherapy
    • Asero, R., Fennel, cucumber, and melon allergy success- fully treated with pollen-specific injection immunotherapy. Ann. Allergy Asthma Immunol. 2000, 84, 460-462.
    • (2000) Ann. Allergy Asthma Immunol. , vol.84 , pp. 460-462
    • Asero, R.1
  • 10
    • 4544368011 scopus 로고    scopus 로고
    • Prevalence of sensitization to Artemisia allergens Art v 1, Art v 3 and Art v 60kDa. Cross-reactivity among Art v 3 and other relevant lipid-transfer protein allergens
    • Lombardero, M., Garcia-Selles, F. J., Polo, F., Jimeno, L. et al., Prevalence of sensitization to Artemisia allergens Art v 1, Art v 3 and Art v 60kDa. Cross-reactivity among Art v 3 and other relevant lipid-transfer protein allergens. Clin. Exp. Allergy 2004, 34, 1415-1421.
    • (2004) Clin. Exp. Allergy , vol.34 , pp. 1415-1421
    • Lombardero, M.1    Garcia-Selles, F.J.2    Polo, F.3    Jimeno, L.4
  • 11
    • 0041960276 scopus 로고    scopus 로고
    • Clinically relevant peach allergy is related to peach lipid transfer protein, Pru p 3, in the Spanish population
    • Fernandez-Rivas, M., Gonzalez-Mancebo, E., Rodriguez-Perez, R., Benito, C. et al., Clinically relevant peach allergy is related to peach lipid transfer protein, Pru p 3, in the Spanish population. J. Allergy Clin. Immunol. 2003, 112, 789-795.
    • (2003) J. Allergy Clin. Immunol. , vol.112 , pp. 789-795
    • Fernandez-Rivas, M.1    Gonzalez-Mancebo, E.2    Rodriguez-Perez, R.3    Benito, C.4
  • 12
    • 0032978679 scopus 로고    scopus 로고
    • Cross-reactivity and epitope analysis of Pru a 1, the major cherry allergen
    • Scheurer, S., Son, D. Y., Boehm, M., Karamloo, F. et al., Cross-reactivity and epitope analysis of Pru a 1, the major cherry allergen. Mol. Immunol. 1999, 36, 155-167.
    • (1999) Mol. Immunol. , vol.36 , pp. 155-167
    • Scheurer, S.1    Son, D.Y.2    Boehm, M.3    Karamloo, F.4
  • 13
  • 14
    • 0025612425 scopus 로고
    • Correlation between stability of a protein and its dipeptide composition: A novel approach for predicting in vivo stability of a protein from its primary sequence
    • Guruprasad, K., Reddy, B. V., Pandit, M. W., Correlation between stability of a protein and its dipeptide composition: a novel approach for predicting in vivo stability of a protein from its primary sequence. Protein Eng. 1990, 4, 155-161.
    • (1990) Protein Eng , vol.4 , pp. 155-161
    • Guruprasad, K.1    Reddy, B.V.2    Pandit, M.W.3
  • 15
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J., Doolittle, R. F., A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 1982, 157, 105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 16
    • 33646249121 scopus 로고    scopus 로고
    • Structure and stability of 2S albumin-type peanut aller- gens: Implications for the severity of peanut allergic reactions
    • Lehmann, K., Schweimer, K., Reese, G., Randow, S. et al., Structure and stability of 2S albumin-type peanut aller- gens: implications for the severity of peanut allergic reactions. Biochem. J. 2006, 395, 463-472.
    • (2006) Biochem. J. , vol.395 , pp. 463-472
    • Lehmann, K.1    Schweimer, K.2    Reese, G.3    Randow, S.4
  • 17
    • 56749160255 scopus 로고    scopus 로고
    • Purification and structural stability of the peach allergens Pru p 1 and Pru p 3
    • Gaier, S., Marsh, J., Oberhuber, C., Rigby, N. M. et al., Purification and structural stability of the peach allergens Pru p 1 and Pru p 3. Mol. Nutr. Food Res. 2008, 52, S220-S229.
    • (2008) Mol. Nutr. Food Res. , vol.52
    • Gaier, S.1    Marsh, J.2    Oberhuber, C.3    Rigby, N.M.4
  • 18
    • 33746280250 scopus 로고    scopus 로고
    • In silico predictability of allergenicity: From amino acid sequence via 3-D structure to allergenicity
    • Aalberse, R. C., Stadler, B. M., In silico 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
  • 19
    • 0034515409 scopus 로고    scopus 로고
    • Recombinant allergens for diagnosis and therapy of allergic disease
    • Chapman, M. D., Smith, A. M., Vailes, L. D., Arruda, L. K. et al., Recombinant allergens for diagnosis and therapy of allergic disease. J. Allergy Clin. Immunol. 2000, 106, 409-418.
    • (2000) J. Allergy Clin. Immunol. , vol.106 , pp. 409-418
    • Chapman, M.D.1    Smith, A.M.2    Vailes, L.D.3    Arruda, L.K.4
  • 21
    • 11344257641 scopus 로고    scopus 로고
    • Molecular properties of food allergens
    • quiz 24
    • Breiteneder, H., Mills, E. N., Molecular properties of food allergens. J. Allergy Clin. Immunol. 2005, 115, 14-23; quiz 24.
    • (2005) J. Allergy Clin. Immunol. , vol.115 , pp. 14-23
    • Breiteneder, H.1    Mills, E.N.2
  • 22
    • 0016711037 scopus 로고
    • High resolution two-dimensional electrophoresis of proteins
    • O'Farrell, P. H., High resolution two-dimensional electrophoresis of proteins. J. Biol. Chem. 1975, 250, 4007-4021.
    • (1975) J. Biol. Chem. , vol.250 , pp. 4007-4021
    • O'Farrell, P.H.1
  • 23
    • 44649090661 scopus 로고    scopus 로고
    • Purification and characterization of natural Ara h 8, the Bet v 1 homologous allergen from peanut, provides a novel isoform
    • Riecken, S., Lindner, B., Petersen, A., Jappe, U., Becker, W. M., Purification and characterization of natural Ara h 8, the Bet v 1 homologous allergen from peanut, provides a novel isoform. Biol. Chem. 2008, 389, 415-423.
    • (2008) Biol. Chem. , vol.389 , pp. 415-423
    • Riecken, S.1    Lindner, B.2    Petersen, A.3    Jappe, U.4    Becker, W.M.5
  • 24
    • 66749110446 scopus 로고    scopus 로고
    • Standardization of allergen products: 1. Detailed characterization of GMP-produced recombinant Bet v 1.0101 as biological reference preparation
    • Himly, M., Nony, E., Chabre, H., Van Overtvelt, L. et al., Standardization of allergen products: 1. Detailed characterization of GMP-produced recombinant Bet v 1.0101 as biological reference preparation. Allergy 2009, 64, 1038-1045.
    • (2009) Allergy , vol.64 , pp. 1038-1045
    • Himly, M.1    Nony, E.2    Chabre, H.3    van Overtvelt, L.4
  • 25
    • 56749178798 scopus 로고    scopus 로고
    • Purification and characterisation of relevant natural and recombinant apple allergens
    • Oberhuber, C., Ma, Y., Marsh, J., Rigby, N. et al., Purification and characterisation of relevant natural and recombinant apple allergens. Mol. Nutr. Food Res. 2008, 52, S208-S219.
    • (2008) Mol. Nutr. Food Res. , vol.52
    • Oberhuber, C.1    Ma, Y.2    Marsh, J.3    Rigby, N.4
  • 26
    • 61449146289 scopus 로고    scopus 로고
    • All three subunits of soybean beta-conglycinin are potential food allergens
    • Krishnan, H. B., Kim, W. S., Jang, S., Kerley, M. S., All three subunits of soybean beta-conglycinin are potential food allergens. J. Agric. Food Chem. 2009, 57, 938-943.
    • (2009) J. Agric. Food Chem. , vol.57 , pp. 938-943
    • Krishnan, H.B.1    Kim, W.S.2    Jang, S.3    Kerley, M.S.4
  • 27
    • 67649204161 scopus 로고    scopus 로고
    • Unambiguous characterization and tissue localization of Pru P 3 peach allergen by electrospray mass spectrometry and MALDI imaging
    • Cavatorta, V., Sforza, S., Mastrobuoni, G., Pieraccini, G. et al., Unambiguous characterization and tissue localization of Pru P 3 peach allergen by electrospray mass spectrometry and MALDI imaging. J. Mass Spectrom. 2009, 44, 891-897.
    • (2009) J. Mass Spectrom. , vol.44 , pp. 891-897
    • Cavatorta, V.1    Sforza, S.2    Mastrobuoni, G.3    Pieraccini, G.4
  • 28
    • 35848949043 scopus 로고    scopus 로고
    • Decoding protein modifications using top-down mass spectrometry
    • Siuti, N., Kelleher, N. L., Decoding protein modifications using top-down mass spectrometry. Nat. Methods 2007, 4, 817-821.
    • (2007) Nat. Methods , vol.4 , pp. 817-821
    • Siuti, N.1    Kelleher, N.L.2
  • 29
    • 0001433809 scopus 로고
    • Methods for the determination of the amino acid sequence in peptides. Acta
    • Edman, P., Methods for the determination of the amino acid sequence in peptides. Acta Chem. Scand. 1950, 4, 283-293.
    • (1950) Chem. Scand. , vol.4 , pp. 283-293
    • Edman, P.1
  • 30
    • 56749180903 scopus 로고    scopus 로고
    • Production and characterization of an allergen panel for component-resolved diagnosis of celery allergy
    • Bublin, M., Lauer, I., Oberhuber, C., Alessandri, S. et al., Production and characterization of an allergen panel for component-resolved diagnosis of celery allergy. Mol. Nutr. Food Res. 2008, 52, S241-S250.
    • (2008) Mol. Nutr. Food Res. , vol.52
    • Bublin, M.1    Lauer, I.2    Oberhuber, C.3    Alessandri, S.4
  • 31
    • 56749182232 scopus 로고    scopus 로고
    • Characterization of Bet v 1-related allergens from kiwifruit relevant for patients with combined kiwifruit and birch pollen allergy
    • Oberhuber, C., Bulley, S. M., Ballmer-Weber, B. K., Bublin, M. et al., Characterization of Bet v 1-related allergens from kiwifruit relevant for patients with combined kiwifruit and birch pollen allergy. Mol. Nutr. Food Res. 2008, 52, S230-S240.
    • (2008) Mol. Nutr. Food Res. , vol.52
    • Oberhuber, C.1    Bulley, S.M.2    Ballmer-Weber, B.K.3    Bublin, M.4
  • 32
    • 27644475556 scopus 로고    scopus 로고
    • Expression in Escherichia coli and disulfide bridge mapping of PSC33, an allergenic 2S albumin from peanut
    • Clement, G., Boquet, D., Mondoulet, L., Lamourette, P. et al., Expression in Escherichia coli and disulfide bridge mapping of PSC33, an allergenic 2S albumin from peanut. Protein Expr. Purif. 2005, 44, 110-120.
    • (2005) Protein Expr. Purif. , vol.44 , pp. 110-120
    • Clement, G.1    Boquet, D.2    Mondoulet, L.3    Lamourette, P.4
  • 33
    • 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., Bruijnzeel-Koomen, C., Hessing, M., de Jongh, H., Heat-induced conformational changes of Ara h 1, a major peanut allergen, do not affect its allergenic properties. J. Biol. Chem. 1999, 274, 4770-4777.
    • (1999) J. Biol. Chem. , vol.274 , pp. 4770-4777
    • Koppelman, S.1    Bruijnzeel-Koomen, C.2    Hessing, M.3    de Jongh, H.4
  • 34
    • 11244333145 scopus 로고    scopus 로고
    • Reversible denaturation of Brazil nut 2S albumin (Ber e1) and implication of structural destabilization on digestion by pepsin
    • Koppelman, S. J., Nieuwenhuizen, W. F., Gaspari, M., Knippels, L. M. et al., Reversible denaturation of Brazil nut 2S albumin (Ber e1) and implication of structural destabilization on digestion by pepsin. J. Agric. Food Chem. 2005, 53,123-131.
    • (2005) J. Agric. Food Chem. , vol.53 , pp. 123-131
    • Koppelman, S.J.1    Nieuwenhuizen, W.F.2    Gaspari, M.3    Knippels, L.M.4
  • 35
    • 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
    • Scheurer, S., Lauer, I., Foetisch, K., San Miguel Moncin, M. et al., 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. 2004, 114, 900-907.
    • (2004) J. Allergy Clin. Immunol. , vol.114 , pp. 900-907
    • Scheurer, S.1    Lauer, I.2    Foetisch, K.3    San Miguel Moncin, M.4
  • 36
    • 0037100401 scopus 로고    scopus 로고
    • Protein structure plays a critical role in peanut allergen stability and may determine immunodominant IgE-binding epitopes
    • Sen, M., Kopper, R., Pons, L., Abraham, E. C. et al., Protein structure plays a critical role in peanut allergen stability and may determine immunodominant IgE-binding epitopes. J. Immunol. 2002, 169, 882-887.
    • (2002) J. Immunol. , vol.169 , pp. 882-887
    • Sen, M.1    Kopper, R.2    Pons, L.3    Abraham, E.C.4
  • 37
    • 56749165009 scopus 로고    scopus 로고
    • The purification and characterisation of allergenic hazelnut seed proteins
    • Rigby, N. M., Marsh, J., Sancho, A. I., Wellner, K. et al., The purification and characterisation of allergenic hazelnut seed proteins. Mol. Nutr. Food Res. 2008, 52, S251-S261.
    • (2008) Mol. Nutr. Food Res. , vol.52
    • Rigby, N.M.1    Marsh, J.2    Sancho, A.I.3    Wellner, K.4
  • 38
    • 3242742115 scopus 로고    scopus 로고
    • The optimization of protein secondary structure determination with infrared and circular dichroism spectra
    • Oberg, K. A., Ruysschaert, J. M., Goormaghtigh, E., The optimization of protein secondary structure determination with infrared and circular dichroism spectra. Eur. J. Biochem. 2004, 271, 2937-2948.
    • (2004) Eur. J. Biochem. , vol.271 , pp. 2937-2948
    • Oberg, K.A.1    Ruysschaert, J.M.2    Goormaghtigh, E.3
  • 39
    • 12644251992 scopus 로고    scopus 로고
    • Response surface methods for optimizing and improving reproducibility of crystal growth
    • Carter, C., Response surface methods for optimizing and improving reproducibility of crystal growth. Methods Enzymol. 1997, 276, 74-99.
    • (1997) Methods Enzymol. , vol.276 , pp. 74-99
    • Carter, C.1
  • 40
    • 31344451312 scopus 로고    scopus 로고
    • Crystal structure of peach Pru p 3, the prototypic member of the family of plant non-specific lipid transfer protein panallergens
    • Pasquato, N., Berni, R., Folli, C., Folloni, S. et al., Crystal structure of peach Pru p 3, the prototypic member of the family of plant non-specific lipid transfer protein panallergens. J. Mol. Biol. 2006, 356, 684-694.
    • (2006) J. Mol. Biol. , vol.356 , pp. 684-694
    • Pasquato, N.1    Berni, R.2    Folli, C.3    Folloni, S.4
  • 41
    • 64149104207 scopus 로고    scopus 로고
    • Crystal structure of Ara h 3, a major allergen in peanut
    • Jin, T., Guo, F., Chen, Y. W., Howard, A., Zhang, Y. Z., Crystal structure of Ara h 3, a major allergen in peanut. Mol. Immunol. 2009, 46, 1796-1804.
    • (2009) Mol. Immunol. , vol.46 , pp. 1796-1804
    • Jin, T.1    Guo, F.2    Chen, Y.W.3    Howard, A.4    Zhang, Y.Z.5
  • 42
    • 0141928674 scopus 로고    scopus 로고
    • TROSY in NMR studies of the structure and function of large biological macromolecules
    • Fernandez, C., Wider, G., TROSY in NMR studies of the structure and function of large biological macromolecules. Curr. Opin. Struct. Biol. 2003, 13, 570-580.
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 570-580
    • Fernandez, C.1    Wider, G.2
  • 43
    • 85056063589 scopus 로고    scopus 로고
    • Clemente, A., 2S albumin storage proteins: What makes them food allergens
    • Moreno, F. J., Clemente, A., 2S albumin storage proteins: what makes them food allergens? Open Biochem. J. 2008, 2,16-28.
    • (2008) Open Biochem. J. , vol.2 , pp. 16-28
    • Moreno, F.J.1
  • 44
    • 0344011459 scopus 로고    scopus 로고
    • Solution structure of RicC3, a 2S albumin storage protein from Ricinus communis
    • Pantoja-Uceda, D., Bruix, M., Gimenez-Gallego, G., Rico, M., Santoro, J., Solution structure of RicC3, a 2S albumin storage protein from Ricinus communis. Biochemistry 2003,42,13839-13847.
    • (2003) Biochemistry , vol.42 , pp. 13839-13847
    • Pantoja-Uceda, D.1    Bruix, M.2    Gimenez-Gallego, G.3    Rico, M.4    Santoro, J.5
  • 45
    • 11144348726 scopus 로고    scopus 로고
    • Solution structure and stability against digestion of rproBnIb, a recombinant 2S albumin from rapeseed: Relationship to its allergenic properties
    • Pantoja-Uceda, D., Palomares, O., Bruix, M., Villalba, M. et al., Solution structure and stability against digestion of rproBnIb, a recombinant 2S albumin from rapeseed: relationship to its allergenic properties. Biochemistry 2004, 43, 16036-16045.
    • (2004) Biochemistry , vol.43 , pp. 16036-16045
    • Pantoja-Uceda, D.1    Palomares, O.2    Bruix, M.3    Villalba, M.4
  • 46
    • 56749185704 scopus 로고    scopus 로고
    • Expression and characterization of three important panallergens from hazelnut
    • Lauer, I., Alessandri, S., Pokoj, S., Reuter, A. et al., Expression and characterization of three important panallergens from hazelnut. Mol. Nutr. Food Res. 2008, 52, S262-S271.
    • (2008) Mol. Nutr. Food Res. , vol.52
    • Lauer, I.1    Alessandri, S.2    Pokoj, S.3    Reuter, A.4
  • 48
    • 0035933875 scopus 로고    scopus 로고
    • Allergic cross-reactivity made visible: Solution structure of the major cherry allergen Pru av 1
    • Neudecker, P., Schweimer, K., Nerkamp, J., Scheurer, S. et al., Allergic cross-reactivity made visible: solution structure of the major cherry allergen Pru av 1. J. Biol. Chem. 2001, 276, 22756-22763.
    • (2001) J. Biol. Chem. , vol.276 , pp. 22756-22763
    • Neudecker, P.1    Schweimer, K.2    Nerkamp, J.3    Scheurer, S.4
  • 49
    • 0030471602 scopus 로고    scopus 로고
    • X-ray and NMR structure of Bet v 1, the origin of birch pollen allergy
    • Gajhede, M., Osmark, P., Poulsen, F. M., Ipsen, H. et al., X-ray and NMR structure of Bet v 1, the origin of birch pollen allergy. Nat. Struct. Biol. 1996, 3, 1040-1045.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 1040-1045
    • Gajhede, M.1    Osmark, P.2    Poulsen, F.M.3    Ipsen, H.4
  • 50
    • 52949121796 scopus 로고    scopus 로고
    • Structural biology by NMR: Structure, dynamics, and interactions
    • Markwick, P. R., Malliavin, T., Nilges, M., Structural biology by NMR: structure, dynamics, and interactions. PLoS Comput. Biol. 2008, 4, e1000168.
    • (2008) Plos Comput. Biol. , vol.e1000168 , pp. 4
    • Markwick, P.R.1    Malliavin, T.2    Nilges, M.3
  • 51
    • 33846567968 scopus 로고    scopus 로고
    • Gastrointestinal digestion of food allergens: Effect on their allergenicity
    • Moreno, F. J., Gastrointestinal digestion of food allergens: effect on their allergenicity. Biomed. Pharmacother. 2007, 61,50-60.
    • (2007) Biomed. Pharmacother. , vol.61 , pp. 50-60
    • Moreno, F.J.1
  • 52
    • 27744453915 scopus 로고    scopus 로고
    • Allergenic reactivity of the melon profilin Cuc m 2 and its identification as major allergen
    • Lopez-Torrejon, G., Crespo, J. F., Sanchez-Monge, R., Sanchez-Jimenez, M. et al., Allergenic reactivity of the melon profilin Cuc m 2 and its identification as major allergen. Clin. Exp. Allergy 2005, 35, 1065-1072.
    • (2005) Clin. Exp. Allergy , vol.35 , pp. 1065-1072
    • Lopez-Torrejon, G.1    Crespo, J.F.2    Sanchez-Monge, R.3    Sanchez-Jimenez, M.4
  • 53
    • 67149101221 scopus 로고    scopus 로고
    • Structural stability of amandin, a major allergen from almond (Prunus dulcis), and its acidic and basic polypeptides
    • Albillos, S. M., Menhart, N., Fu, T. J., Structural stability of amandin, a major allergen from almond (Prunus dulcis), and its acidic and basic polypeptides. J. Agric. Food Chem. 2009,57,4698-4705.
    • (2009) J. Agric. Food Chem. , vol.57 , pp. 4698-4705
    • Albillos, S.M.1    Menhart, N.2    Fu, T.J.3
  • 54
    • 5444259323 scopus 로고    scopus 로고
    • Structural, biological, and evolutionary relationships of plant food allergens sensitizing via the gastrointestinal tract
    • Mills, E. N., Jenkins, J. A., Alcocer, M. J., Shewry, P. R., Structural, biological, and evolutionary relationships of plant food allergens sensitizing via the gastrointestinal tract. Crit. Rev. Food Sci. Nutr. 2004, 44, 379-407.
    • (2004) Crit. Rev. Food Sci. Nutr. , vol.44 , pp. 379-407
    • Mills, E.N.1    Jenkins, J.A.2    Alcocer, M.J.3    Shewry, P.R.4
  • 55
    • 0035844711 scopus 로고    scopus 로고
    • Formation of thermally induced aggregates of the soya globulin beta-conglycinin
    • Mills, E. N., Huang, L., Noel, T. R., Gunning, A. P., Morris, V. J., Formation of thermally induced aggregates of the soya globulin beta-conglycinin. Biochim. Biophys. Acta 2001,1547,339-350.
    • (2001) Biochim. Biophys. Acta , vol.1547 , pp. 339-350
    • Mills, E.N.1    Huang, L.2    Noel, T.R.3    Gunning, A.P.4    Morris, V.J.5
  • 56
    • 55449094462 scopus 로고    scopus 로고
    • Effects of gastrointestinal digestion and heating on the allergenicity of the kiwi allergens Act d 1, actinidin, and Act d 2, a thaumatin-like protein
    • Bublin, M., Radauer, C., Knulst, A., Wagner, S. et al., Effects of gastrointestinal digestion and heating on the allergenicity of the kiwi allergens Act d 1, actinidin, and Act d 2, a thaumatin-like protein. Mol. Nutr. Food Res. 2008, 52, 1130-1139.
    • (2008) Mol. Nutr. Food Res. , vol.52 , pp. 1130-1139
    • Bublin, M.1    Radauer, C.2    Knulst, A.3    Wagner, S.4
  • 57
    • 0038644459 scopus 로고    scopus 로고
    • Thermally induced structural changes in glycinin, the 11S globulin of soya bean (Glycine max) - an in situ spectroscopic study
    • Mills, E. N., Marigheto, N. A., Wellner, N., Fairhurst, S. A. et al., Thermally induced structural changes in glycinin, the 11S globulin of soya bean (Glycine max) - an in situ spectroscopic study. Biochim. Biophys. Acta 2003, 1648, 105-114.
    • (2003) Biochim. Biophys. Acta , vol.1648 , pp. 105-114
    • Mills, E.N.1    Marigheto, N.A.2    Wellner, N.3    Fairhurst, S.A.4
  • 58
    • 49649091116 scopus 로고    scopus 로고
    • Legumin allergens from peanuts and soybeans: Effects of denaturation and aggregation on allergenicity
    • van Boxtel, E. L., van den Broek, L. A., Koppelman, S. J., Gruppen, H., Legumin allergens from peanuts and soybeans: effects of denaturation and aggregation on allergenicity. Mol. Nutr. Food Res. 2008, 52, 674-682.
    • (2008) Mol. Nutr. Food Res. , vol.52 , pp. 674-682
    • van Boxtel, E.L.1    van den Broek, L.A.2    Koppelman, S.J.3    Gruppen, H.4
  • 59
    • 33748437518 scopus 로고    scopus 로고
    • Effects of enzymatic deamidation by protein-glutaminase on structure and functional properties of wheat gluten
    • Yong, Y. H., Yamaguchi, S., Matsumura, Y., Effects of enzymatic deamidation by protein-glutaminase on structure and functional properties of wheat gluten. J. Agric. Food Chem. 2006, 54, 6034-6040.
    • (2006) J. Agric. Food Chem. , vol.54 , pp. 6034-6040
    • Yong, Y.H.1    Yamaguchi, S.2    Matsumura, Y.3
  • 60
    • 25144519047 scopus 로고    scopus 로고
    • Thermostability and in vitro digestibility of a purified major allergen 2S albumin (Ses i 1) from white sesame seeds (Sesamum indicum L.)
    • Moreno, F. J., Maldonado, B. M., Wellner, N., Mills, E. N., Thermostability and in vitro digestibility of a purified major allergen 2S albumin (Ses i 1) from white sesame seeds (Sesamum indicum L.). Biochim. Biophys. Acta 2005,1752,142-153.
    • (2005) Biochim. Biophys. Acta , vol.1752 , pp. 142-153
    • Moreno, F.J.1    Maldonado, B.M.2    Wellner, N.3    Mills, E.N.4
  • 61
    • 0037070353 scopus 로고    scopus 로고
    • Effect of heat-induced aggregation on the IgE binding of patatin (Sol t 1) is dominated by other potato proteins
    • Koppelman, S. J., van Koningsveld, G. A., Knulst, A. C., Gruppen, H. et al., Effect of heat-induced aggregation on the IgE binding of patatin (Sol t 1) is dominated by other potato proteins. J. Agric. Food Chem. 2002, 50, 1562-1568.
    • (2002) J. Agric. Food Chem. , vol.50 , pp. 1562-1568
    • Koppelman, S.J.1    van Koningsveld, G.A.2    Knulst, A.C.3    Gruppen, H.4
  • 62
    • 0030571043 scopus 로고    scopus 로고
    • Size-exclusion chromatography with on-line light-scattering, absorbance, and refractive index detectors for studying proteins and their interactions
    • Wen, J., Arakawa, T., Philo, J. S., Size-exclusion chromatography with on-line light-scattering, absorbance, and refractive index detectors for studying proteins and their interactions. Anal. Biochem. 1996, 240, 155-166.
    • (1996) Anal. Biochem. , vol.240 , pp. 155-166
    • Wen, J.1    Arakawa, T.2    Philo, J.S.3
  • 63
    • 55049135664 scopus 로고    scopus 로고
    • Structure and molecular mobility of soy glycinin in the solid state
    • Kealley, C. S., Rout, M. K., Dezfouli, M. R., Strounina, E. et al., Structure and molecular mobility of soy glycinin in the solid state. Biomacromolecules 2008, 9, 2937-2946.
    • (2008) Biomacromolecules , vol.9 , pp. 2937-2946
    • Kealley, C.S.1    Rout, M.K.2    Dezfouli, M.R.3    Strounina, E.4
  • 64
    • 33846425336 scopus 로고    scopus 로고
    • IgE-mediated food allergy diagnosis: Current status and new perspectives
    • Asero, R., Ballmer-Weber, B. K., Beyer, K., Conti, A. 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    Conti, A.4
  • 65
    • 45749085640 scopus 로고    scopus 로고
    • Predictive value of the sulfidoleukotriene release assay in oral allergy syndrome to celery, hazelnut, and carrot
    • Ballmer-Weber, B. K., Weber, J. M., Vieths, S., Wuthrich, B., Predictive value of the sulfidoleukotriene release assay in oral allergy syndrome to celery, hazelnut, and carrot. J. Investig. Allergol. Clin. Immunol. 2008, 18, 93-99.
    • (2008) J. Investig. Allergol. Clin. Immunol. , vol.18 , pp. 93-99
    • Ballmer-Weber, B.K.1    Weber, J.M.2    Vieths, S.3    Wuthrich, B.4
  • 67
    • 2042449746 scopus 로고    scopus 로고
    • Relevance of Ara h1, Ara h2 and Ara h3 in peanut-allergic patients, as determined by immunoglobu- lin E Western blotting, basophil-histamine release and intracutaneous testing: Ara h2 is the most important peanut allergen
    • Koppelman, S. J., Wensing, M., Ertmann, M., Knulst, A. C., Knol, E. F., Relevance of Ara h1, Ara h2 and Ara h3 in peanut-allergic patients, as determined by immunoglobu- lin E Western blotting, basophil-histamine release and intracutaneous testing: Ara h2 is the most important peanut allergen. Clin. Exp. Allergy 2004, 34, 583-590.
    • (2004) Clin. Exp. Allergy , vol.34 , pp. 583-590
    • Koppelman, S.J.1    Wensing, M.2    Ertmann, M.3    Knulst, A.C.4    Knol, E.F.5
  • 68
    • 33646271835 scopus 로고    scopus 로고
    • The role of profilin and lipid transfer protein in strawberry allergy in the Mediterranean area
    • Zuidmeer, L., Salentijn, E., Rivas, M. F., Mancebo, E. G. et al., The role of profilin and lipid transfer protein in strawberry allergy in the Mediterranean area. Clin. Exp. Allergy 2006, 36, 666-675.
    • (2006) Clin. Exp. Allergy , vol.36 , pp. 666-675
    • Zuidmeer, L.1    Salentijn, E.2    Rivas, M.F.3    Mancebo, E.G.4
  • 69
    • 33747258350 scopus 로고    scopus 로고
    • Diagnostic tests based on human basophils: Potentials, pitfalls and perspectives
    • Kleine-Tebbe, J., Erdmann, S., Knol, E. F., MacGlashan, D. W., Jr. et al., Diagnostic tests based on human basophils: potentials, pitfalls and perspectives. Int. Arch. Allergy Immunol. 2006, 141, 79-90.
    • (2006) Int. Arch. Allergy Immunol. , vol.141 , pp. 79-90
    • Kleine-Tebbe, J.1    Erdmann, S.2    Knol, E.F.3    MacGlashan, D.W.4
  • 70
    • 1042264226 scopus 로고    scopus 로고
    • Improving diagnostic tests for food allergy with recombinant allergens
    • Bohle, B., Vieths, S., Improving diagnostic tests for food allergy with recombinant allergens. Methods 2004, 32, 292-299.
    • (2004) Methods , vol.32 , pp. 292-299
    • Bohle, B.1    Vieths, S.2
  • 71
    • 36849082377 scopus 로고    scopus 로고
    • Methodo- logical issues in the diagnostic work-up of food allergy: A real challenge
    • Gellerstedt, M., Bengtsson, U., Niggemann, B., Methodo- logical issues in the diagnostic work-up of food allergy: A real challenge. J. Investig. Allergol. Clin. Immunol. 2007, 17,350-356.
    • (2007) J. Investig. Allergol. Clin. Immunol. , vol.17 , pp. 350-356
    • Gellerstedt, M.1    Bengtsson, U.2    Niggemann, B.3
  • 72
    • 34250661359 scopus 로고    scopus 로고
    • Pitfalls in double-blind, placebo- controlled oral food challenges
    • Niggemann, B., Beyer, K., Pitfalls in double-blind, placebo- controlled oral food challenges. Allergy 2007, 62, 729-732.
    • (2007) Allergy , vol.62 , pp. 729-732
    • Niggemann, B.1    Beyer, K.2
  • 76
    • 0019944341 scopus 로고
    • Food hyper- sensitivity in patients with pollen allergy
    • Eriksson, N. E., Formgren, H., Svenonius, E., Food hyper- sensitivity in patients with pollen allergy. Allergy 1982, 37, 437-443.
    • (1982) Allergy , vol.37 , pp. 437-443
    • Eriksson, N.E.1    Formgren, H.2    Svenonius, E.3
  • 78
    • 0037395067 scopus 로고    scopus 로고
    • Biological activity of IgE specific for cross-reactive carbohydrate determinants
    • Foetisch, K., Westphal, S., Lauer, I., Retzek, M. et al., Biological activity of IgE specific for cross-reactive carbohydrate determinants. J. Allergy Clin. Immunol. 2003, 111, 889-896.
    • (2003) J. Allergy Clin. Immunol. , vol.111 , pp. 889-896
    • Foetisch, K.1    Westphal, S.2    Lauer, I.3    Retzek, M.4
  • 79
    • 34247850788 scopus 로고    scopus 로고
    • Potato lectin activates basophils and mast cells of atopic subjects by its interaction with core chitobiose of cell-bound non-specific immunoglobulin
    • Pramod, S. N., Venkatesh, Y. P., Mahesh, P. A., Potato lectin activates basophils and mast cells of atopic subjects by its interaction with core chitobiose of cell-bound non-specific immunoglobulin E. Clin. Exp. Immunol. 2007, 148, 391-401.
    • (2007) E. Clin. Exp. Immunol. , vol.148 , pp. 391-401
    • Pramod, S.N.1    Venkatesh, Y.P.2    Mahesh, P.A.3
  • 80
    • 0030822565 scopus 로고    scopus 로고
    • Poor biologic activity of cross-reactive IgE directed to carbohydrate determinants of glycoproteins
    • van der Veen, M. J., van Ree, R., Aalberse, R. C., Akkerdaas, J. et al., Poor biologic activity of cross-reactive IgE directed to carbohydrate determinants of glycoproteins. J. Allergy Clin. Immunol. 1997, 100, 327-334.
    • (1997) J. Allergy Clin. Immunol. , vol.100 , pp. 327-334
    • van der Veen, M.J.1    van Ree, R.2    Aalberse, R.C.3    Akkerdaas, J.4
  • 81
    • 33746301106 scopus 로고    scopus 로고
    • Evaluation of available IgE- binding epitope data and its utility in bioinformatics
    • Bannon, G. A., Ogawa, T., Evaluation of available IgE- binding epitope data and its utility in bioinformatics. Mol. Nutr. Food Res. 2006, 50, 638-644.
    • (2006) Mol. Nutr. Food Res. , vol.50 , pp. 638-644
    • Bannon, G.A.1    Ogawa, T.2
  • 82
    • 0028240998 scopus 로고
    • Epitope analysis of isoforms of the major allergen Phl p V by fingerprinting and microsequencing
    • Petersen, A., Becker, W. M., Schlaak, M., Epitope analysis of isoforms of the major allergen Phl p V by fingerprinting and microsequencing. Clin. Exp. Allergy 1994, 24, 250-256.
    • (1994) Clin. Exp. Allergy , vol.24 , pp. 250-256
    • Petersen, A.1    Becker, W.M.2    Schlaak, M.3
  • 83
    • 67650249226 scopus 로고    scopus 로고
    • Antibody epitope mapping using SPOT peptide arrays
    • Reineke, U., Sabat, R., Antibody epitope mapping using SPOT peptide arrays. Methods Mol. Biol. 2009, 524, 145-167.
    • (2009) Methods Mol. Biol. , vol.524 , pp. 145-167
    • Reineke, U.1    Sabat, R.2
  • 84
    • 0000448982 scopus 로고
    • Prediction of protein antigenic determinants from amino acid sequences
    • Hopp, T. P., Woods, K. R., Prediction of protein antigenic determinants from amino acid sequences. Proc. Natl. Acad. Sci. USA 1981, 78, 3824-3828.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 3824-3828
    • Hopp, T.P.1    Woods, K.R.2
  • 85
    • 0038380463 scopus 로고    scopus 로고
    • Allergenicity prediction by protein sequence
    • Stadler, M. B., Stadler, B. M., Allergenicity prediction by protein sequence. FASEB J. 2003, 17, 1141-1143.
    • (2003) Faseb J. , vol.17 , pp. 1141-1143
    • Stadler, M.B.1    Stadler, B.M.2
  • 86
    • 0030329981 scopus 로고    scopus 로고
    • Epitope analysis with arrays of synthetic peptides prepared on cellulose membranes
    • Frank, R., Overwin, H., SPOT synthesis. Epitope analysis with arrays of synthetic peptides prepared on cellulose membranes. Methods Mol. Biol. 1996, 66, 149-169.
    • (1996) Methods. Mol. Biol. , vol.66 , pp. 149-169
    • Frank, R.1    Overwin, H.2    Synthesis, S.P.O.T.3
  • 88
    • 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., Shin, D., Cockrell, G., Stanley, J. S. et al., 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. 1997, 245,334-339.
    • (1997) Eur. J. Biochem. , vol.245 , pp. 334-339
    • Burks, A.W.1    Shin, D.2    Cockrell, G.3    Stanley, J.S.4
  • 89
    • 0033557358 scopus 로고    scopus 로고
    • Molecular cloning and epitope analysis of the peanut allergen Ara h 3
    • Rabjohn, P., Helm, E. M., Stanley, J. S., West, C. M. et al., Molecular cloning and epitope analysis of the peanut allergen Ara h 3. J. Clin. Invest. 1999, 103, 535-542.
    • (1999) J. Clin. Invest. , vol.103 , pp. 535-542
    • Rabjohn, P.1    Helm, E.M.2    Stanley, J.S.3    West, C.M.4
  • 90
    • 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., King, N., Burks, A. W., Huang, S. K. et al., Identification and mutational analysis of the immunodominant IgE binding epitopes of the major peanut allergen Ara h 2. Arch. Biochem. Biophys. 1997, 342, 244-253.
    • (1997) Arch. Biochem. Biophys. , vol.342 , pp. 244-253
    • Stanley, J.S.1    King, N.2    Burks, A.W.3    Huang, S.K.4
  • 91
    • 1942467835 scopus 로고    scopus 로고
    • Microarray immunoassay: Association of clinical history, in vitro IgE function, and heterogeneity of allergenic peanut epitopes
    • Shreffler, W. G., Beyer, K., Chu, T. H., Burks, A. W., Sampson, H. A., 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    Burks, A.W.4    Sampson, H.A.5
  • 92
    • 40049109092 scopus 로고    scopus 로고
    • Peanut epitopes for IgE and IgG4 in peanut-sensitized children in relation to severity of peanut allergy
    • e710
    • Flinterman, A. E., Knol, E. F., Lencer, D. A., Bardina, L. et al., Peanut epitopes for IgE and IgG4 in peanut-sensitized children in relation to severity of peanut allergy. J. Allergy Clin. Immunol. 2008, 121, 737-743; e710.
    • (2008) J. Allergy Clin. Immunol. , vol.121 , pp. 737-743
    • Flinterman, A.E.1    Knol, E.F.2    Lencer, D.A.3    Bardina, L.4
  • 93
    • 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, W. G., Lencer, D. A., Bardina, L., Sampson, H. A., 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    Sampson, H.A.4
  • 95
    • 0034921889 scopus 로고    scopus 로고
    • A voluntary registry for peanut and tree nut allergy: Characteristics of the first 5149 registrants
    • Sicherer, S. H., Furlong, T. J., Munoz-Furlong, A., Burks, A. W., Sampson, H. A., A voluntary registry for peanut and tree nut allergy: characteristics of the first 5149 registrants. J. Allergy Clin. Immunol. 2001, 108, 128-132.
    • (2001) J. Allergy Clin. Immunol. , vol.108 , pp. 128-132
    • Sicherer, S.H.1    Furlong, T.J.2    Munoz-Furlong, A.3    Burks, A.W.4    Sampson, H.A.5
  • 96
    • 0036152476 scopus 로고    scopus 로고
    • Linear IgE epitope mapping of the English walnut (Juglans regia) major food allergen, Jug r 1
    • Robotham, J., Teuber, S., Sathe, S., Roux, K., Linear IgE epitope mapping of the English walnut (Juglans regia) major food allergen, Jug r 1. J. Allergy Clin. Immunol. 2002,109,143-149.
    • (2002) J. Allergy Clin. Immunol. , vol.109 , pp. 143-149
    • Robotham, J.1    Teuber, S.2    Sathe, S.3    Roux, K.4
  • 97
    • 20444437511 scopus 로고    scopus 로고
    • Ana o 3, an important cashew nut (Anacardium occidentale L.) allergen of the 2S albumin family
    • Robotham, J. M., Wang, F., Seamon, V., Teuber, S. S. et al., Ana o 3, an important cashew nut (Anacardium occidentale L.) allergen of the 2S albumin family. J. Allergy Clin. Immunol. 2005, 115, 1284-1290.
    • (2005) J. Allergy Clin. Immunol. , vol.115 , pp. 1284-1290
    • Robotham, J.M.1    Wang, F.2    Seamon, V.3    Teuber, S.S.4
  • 98
    • 0042044486 scopus 로고    scopus 로고
    • Ana o 2, a major cashew (Anacardium occidentale L.) nut allergen of the legumin family
    • Wang, F., Robotham, J. M., Teuber, S. S., Sathe, S. K., Roux, K. H., Ana o 2, a major cashew (Anacardium occidentale L.) nut allergen of the legumin family. Int. Arch. Allergy Immunol. 2003, 132, 27-39.
    • (2003) Int. Arch. Allergy Immunol , vol.132 , pp. 27-39
    • Wang, F.1    Robotham, J.M.2    Teuber, S.S.3    Sathe, S.K.4    Roux, K.H.5
  • 99
    • 0036971325 scopus 로고    scopus 로고
    • Ana o 1, a cashew (Anacardium occidental) allergen of the vicilin seed storage protein family
    • Wang, F., Robotham, J. M., Teuber, S. S., Tawde, P. et al., Ana o 1, a cashew (Anacardium occidental) allergen of the vicilin seed storage protein family. J. Allergy Clin. Immu- nol. 2002, 110, 160-166.
    • (2002) J. Allergy Clin. Immunol. , vol.110 , pp. 160-166
    • Wang, F.1    Robotham, J.M.2    Teuber, S.S.3    Tawde, P.4
  • 100
    • 0033662935 scopus 로고    scopus 로고
    • A soybean G2 glycinin allergen. 2. Epitope mapping and three-dimensional modeling
    • Helm, R. M., Cockrell, G., Connaughton, C., Sampson, H. A. et al., A soybean G2 glycinin allergen. 2. Epitope mapping and three-dimensional modeling. Int. Arch. Allergy Immunol. 2000, 123, 213-219.
    • (2000) Int. Arch. Allergy Immunol. , vol.123 , pp. 213-219
    • Helm, R.M.1    Cockrell, G.2    Connaughton, C.3    Sampson, H.A.4
  • 101
    • 0033963494 scopus 로고    scopus 로고
    • Mutational analysis of the IgE-binding epitopes of P34/Gly m Bd 30 K
    • Helm, R. M., Cockrell, G., Connaughton, C., West, C. M. et al., Mutational analysis of the IgE-binding epitopes of P34/Gly m Bd 30 K. J. Allergy Clin. Immunol. 2000, 105, 378-384.
    • (2000) J. Allergy Clin. Immunol. , vol.105 , pp. 378-384
    • Helm, R.M.1    Cockrell, G.2    Connaughton, C.3    West, C.M.4
  • 102
    • 0034501229 scopus 로고    scopus 로고
    • Soybean glycinin G1 acidic chain shares IgE epitopes with peanut allergen Ara h 3
    • Beardslee, T. A., Zeece, M. G., Sarath, G., Markwell, J. P., Soybean glycinin G1 acidic chain shares IgE epitopes with peanut allergen Ara h 3. Int. Arch. Allergy Immunol. 2000, 123,299-307.
    • (2000) Int. Arch. Allergy Immunol. , vol.123 , pp. 299-307
    • Beardslee, T.A.1    Zeece, M.G.2    Sarath, G.3    Markwell, J.P.4
  • 103
    • 0036942542 scopus 로고    scopus 로고
    • Identification and analysis of a conserved immunoglobulin E-binding epitope in soybean G1a and G2a and peanut Ara h 3 glycinins
    • Xiang, P., Beardslee, T. A., Zeece, M. G., Markwell, J., Sarath, G., Identification and analysis of a conserved immunoglobulin E-binding epitope in soybean G1a and G2a and peanut Ara h 3 glycinins. Arch. Biochem. Biophys. 2002,408,51-57.
    • (2002) Arch. Biochem. Biophys. , vol.408 , pp. 51-57
    • Xiang, P.1    Beardslee, T.A.2    Zeece, M.G.3    Markwell, J.4    Sarath, G.5
  • 104
    • 11144355420 scopus 로고    scopus 로고
    • Identification of the IgE-binding epitope in omega-5 gliadin, a major allergen in wheat-dependent exercise-induced anaphylaxis
    • Matsuo, H., Morita, E., Tatham, A. S., Morimoto, K. et al., Identification of the IgE-binding epitope in omega-5 gliadin, a major allergen in wheat-dependent exercise-induced anaphylaxis. J. Biol. Chem. 2004, 279, 12135-12140.
    • (2004) J. Biol. Chem. , vol.279 , pp. 12135-12140
    • Matsuo, H.1    Morita, E.2    Tatham, A.S.3    Morimoto, K.4
  • 105
    • 0033836431 scopus 로고    scopus 로고
    • Structural biology of allergens
    • Aalberse, R. C., Structural biology of allergens. J. Allergy Clin. Immunol. 2000, 106, 228-238.
    • (2000) J. Allergy Clin. Immunol. , vol.106 , pp. 228-238
    • Aalberse, R.C.1
  • 106
    • 0025117762 scopus 로고
    • Conformational stability of B cell epitopes on group I and group II Dermatophagoides spp. allergens. Effect of thermal and chemical denaturation on the binding of murine IgG and human IgE antibodies
    • Lombardero, M., Heymann, P. W., Platts-Mills, T. A., Fox, J. W., Chapman, M. D., Conformational stability of B cell epitopes on group I and group II Dermatophagoides spp. allergens. Effect of thermal and chemical denaturation on the binding of murine IgG and human IgE antibodies. J. Immunol. 1990, 144, 1353-1360.
    • (1990) J. Immunol. , vol.144 , pp. 1353-1360
    • Lombardero, M.1    Heymann, P.W.2    Platts-Mills, T.A.3    Fox, J.W.4    Chapman, M.D.5
  • 107
    • 0029999352 scopus 로고    scopus 로고
    • Reduction in IgE binding to allergen variants generated by site-directed mutagenesis: Contribution of disulfide bonds to the antigenic structure of the major house dust mite allergen Der p 2
    • Smith, A. M., Chapman, M. D., Reduction in IgE binding to allergen variants generated by site-directed mutagenesis: contribution of disulfide bonds to the antigenic structure of the major house dust mite allergen Der p 2. Mol. Immunol. 1996, 33, 399-405.
    • (1996) Mol. Immunol. , vol.33 , pp. 399-405
    • Smith, A.M.1    Chapman, M.D.2
  • 108
    • 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., Haase, T. 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, 376, 97-107.
    • (2003) Biochem. J. , vol.376 , pp. 97-107
    • Neudecker, P.1    Lehmann, K.2    Nerkamp, J.3    Haase, T.4
  • 109
    • 62449233400 scopus 로고    scopus 로고
    • Identification of B-cell epitopes of Bet v 1 involved in cross-reactivity with food allergens
    • Klinglmayr, E., Hauser, M., Zimmermann, F., Dissertori, O. et al., Identification of B-cell epitopes of Bet v 1 involved in cross-reactivity with food allergens. Allergy 2009, 64, 647-651.
    • (2009) Allergy , vol.64 , pp. 647-651
    • Klinglmayr, E.1    Hauser, M.2    Zimmermann, F.3    Dissertori, O.4
  • 110
    • 25644434412 scopus 로고    scopus 로고
    • A novel approach for investigation of specific and cross-reactive IgE epitopes on Bet v 1 and homologous food allergens in individual patients
    • Mittag, D., Batori, V., Neudecker, P., Wiche, R. et al., A novel approach for investigation of specific and cross-reactive 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    Wiche, R.4
  • 111
    • 40349111103 scopus 로고    scopus 로고
    • Mimotope mapping as a complementary strategy to define allergen IgE-epitopes: Peach Pru p 3 allergen as a model
    • Pacios, L. F., Tordesillas, L., Cuesta-Herranz, J., Compes, E. et al., Mimotope mapping as a complementary strategy to define allergen IgE-epitopes: peach Pru p 3 allergen as a model. Mol. Immunol. 2008, 45, 2269-2276.
    • (2008) Mol. Immunol. , vol.45 , pp. 2269-2276
    • Pacios, L.F.1    Tordesillas, L.2    Cuesta-Herranz, J.3    Compes, E.4
  • 112
    • 0035937834 scopus 로고    scopus 로고
    • Hydrogen exchange nuclear magnetic resonance spectroscopy mapping of antibody epitopes on the house dust mite allergen Der p 2
    • Mueller, G. A., Smith, A. M., Chapman, M. D., Rule, G. S., Benjamin, D. C., Hydrogen exchange nuclear magnetic resonance spectroscopy mapping of antibody epitopes on the house dust mite allergen Der p 2. J. Biol. Chem. 2001, 276,9359-9365.
    • (2001) J. Biol. Chem. , vol.276 , pp. 9359-9365
    • Mueller, G.A.1    Smith, A.M.2    Chapman, M.D.3    Rule, G.S.4    Benjamin, D.C.5
  • 113
    • 0035753065 scopus 로고    scopus 로고
    • High resolution, high- throughput amide deuterium exchange-mass spectrometry (DXMS) determination of protein binding site structure and dynamics: Utility in pharmaceutical design
    • Woods, V. L., Jr., Hamuro, Y., High resolution, high- throughput amide deuterium exchange-mass spectrometry (DXMS) determination of protein binding site structure and dynamics: utility in pharmaceutical design. J. Cell Biochem. Suppl. 2001, 37, 89-98.
    • (2001) J. Cell Biochem. Suppl. , vol.37 , pp. 89-98
    • Woods Jr., V.L.1    Hamuro, Y.2
  • 114
    • 1842508816 scopus 로고    scopus 로고
    • Mapping intersubunit interactions of the regulatory subunit (RIalpha) in the type I holoenzyme of protein kinase A by amide hydrogen/deuterium exchange mass spectrometry (DXMS)
    • Hamuro, Y., Anand, G. S., Kim, J. S., Juliano, C. et al., Mapping intersubunit interactions of the regulatory subunit (RIalpha) in the type I holoenzyme of protein kinase A by amide hydrogen/deuterium exchange mass spectrometry (DXMS). J. Mol. Biol. 2004, 340, 1185-1196.
    • (2004) J. Mol. Biol. , vol.340 , pp. 1185-1196
    • Hamuro, Y.1    Anand, G.S.2    Kim, J.S.3    Juliano, C.4
  • 115
    • 0041385755 scopus 로고    scopus 로고
    • Dominating IgE-binding epitope of Bet v 1, the major allergen of birch pollen, characterized by X-ray crystal- lography and site-directed mutagenesis
    • Spangfort, M. D., Mirza, O., Ipsen, H., Van Neerven, R. J. et al., Dominating IgE-binding epitope of Bet v 1, the major allergen of birch pollen, characterized by X-ray crystal- lography and site-directed mutagenesis. J. Immunol. 2003, 171,3084-3090.
    • (2003) J. Immunol. , vol.171 , pp. 3084-3090
    • Spangfort, M.D.1    Mirza, O.2    Ipsen, H.3    van Neerven, R.J.4
  • 116
    • 34047171268 scopus 로고    scopus 로고
    • Identification of a B-cell epitope of hyaluronidase, a major bee venom allergen, from its crystal structure in complex with a specific Fab
    • Padavattan, S., Schirmer, T., Schmidt, M., Akdis, C. et al., Identification of a B-cell epitope of hyaluronidase, a major bee venom allergen, from its crystal structure in complex with a specific Fab. J. Mol. Biol. 2007, 368, 742-752.
    • (2007) J. Mol. Biol. , vol.368 , pp. 742-752
    • Padavattan, S.1    Schirmer, T.2    Schmidt, M.3    Akdis, C.4
  • 117
    • 61449212919 scopus 로고    scopus 로고
    • High-affinity IgE recognition of a conformational epitope of the major respiratory allergen Phl p 2 as revealed by X- ray crystallography
    • Padavattan, S., Flicker, S., Schirmer, T., Madritsch, C. et al., High-affinity IgE recognition of a conformational epitope of the major respiratory allergen Phl p 2 as revealed by X- ray crystallography. J. Immunol. 2009, 182, 2141-2151.
    • (2009) J. Immunol. , vol.182 , pp. 2141-2151
    • Padavattan, S.1    Flicker, S.2    Schirmer, T.3    Madritsch, C.4
  • 119
    • 24344485188 scopus 로고    scopus 로고
    • Homology modelling of the major peanut allergen Ara h 2 and surface mapping of IgE-binding epitopes
    • Barre, A., Borges, J. P., Culerrier, R., Rouge, P., Homology modelling of the major peanut allergen Ara h 2 and surface mapping of IgE-binding epitopes. Immunol. Lett. 2005, 100,153-158.
    • (2005) Immunol. Lett. , vol.100 , pp. 153-158
    • Barre, A.1    Borges, J.P.2    Culerrier, R.3    Rouge, P.4
  • 120
    • 61349195794 scopus 로고    scopus 로고
    • Mapping and conformational analysis of IgE-binding epitopic regions on the molecular surface of the major Ara h 3 legumin allergen of peanut (Arachis hypogaea)
    • Rouge, P., Culerrier, R., Sabatier, V., Granier, C. et al., Mapping and conformational analysis of IgE-binding epitopic regions on the molecular surface of the major Ara h 3 legumin allergen of peanut (Arachis hypogaea). Mol. Immunol. 2009, 46, 1067-1075.
    • (2009) Mol. Immunol. , vol.46 , pp. 1067-1075
    • Rouge, P.1    Culerrier, R.2    Sabatier, V.3    Granier, C.4
  • 121
    • 37049037250 scopus 로고    scopus 로고
    • Lipid transfer proteins from Rosaceae fruits share consensus epitopes responsible for their IgE-binding cross-reactivity
    • Borges, J. P., Barre, A., Culerrier, R., Granier, C. et al., Lipid transfer proteins from Rosaceae fruits share consensus epitopes responsible for their IgE-binding cross-reactivity. Biochem. Biophys. Res. Commun. 2008, 365, 685-690.
    • (2008) Biochem. Biophys. Res. Commun. , vol.365 , pp. 685-690
    • Borges, J.P.1    Barre, A.2    Culerrier, R.3    Granier, C.4
  • 122
    • 0037865852 scopus 로고    scopus 로고
    • Cross-reactivity between fruit and vegetables
    • Fernandez Rivas, M., Cross-reactivity between fruit and vegetables. Allergol. Immunopathol. (Madr.) 2003, 31, 141-146.
    • (2003) Allergol. Immunopathol. (madr.) , vol.31 , pp. 141-146
    • Fernandez Rivas, M.1
  • 123
    • 33745645818 scopus 로고    scopus 로고
    • Cross-reactive and species- specific immunoglobulin E epitopes of plant profilins: An experimental and structure-based analysis
    • Radauer, C., Willerroider, M., Fuchs, H., Hoffmann-Sommergruber, K. et al., Cross-reactive and species- specific immunoglobulin E epitopes of plant profilins: an experimental and structure-based analysis. Clin. Exp. Allergy 2006, 36, 920-929.
    • (2006) Clin. Exp. Allergy , vol.36 , pp. 920-929
    • Radauer, C.1    Willerroider, M.2    Fuchs, H.3    Hoffmann-Sommergruber, K.4
  • 124
    • 34249894495 scopus 로고    scopus 로고
    • An experimental and modeling- based approach to locate IgE epitopes of plant profilin allergens
    • Lopez-Torrejon, G., Diaz-Perales, A., Rodriguez, J., Sanchez-Monge, R. et al., An experimental and modeling- based approach to locate IgE epitopes of plant profilin allergens. J. Allergy Clin. Immunol. 2007, 119, 1481-1488.
    • (2007) J. Allergy Clin. Immunol. , vol.119 , pp. 1481-1488
    • Lopez-Torrejon, G.1    Diaz-Perales, A.2    Rodriguez, J.3    Sanchez-Monge, R.4
  • 125
  • 126
    • 33746279967 scopus 로고    scopus 로고
    • Allergen-specific IgE testing in the diagnosis of food allergy and the event of a positive match in the bioinformatics search
    • van Ree, R., Vieths, S., Poulsen, L. K., Allergen-specific IgE testing in the diagnosis of food allergy and the event of a positive match in the bioinformatics search. Mol. Nutr. Food Res. 2006, 50, 645-654.
    • (2006) Mol. Nutr. Food Res. , vol.50 , pp. 645-654
    • van Ree, R.1    Vieths, S.2    Poulsen, L.K.3
  • 127
    • 0036791736 scopus 로고    scopus 로고
    • The cross-reactive calcium-binding pollen allergen, Phl p 7, reveals a novel dimer assembly
    • Verdino, P., Westritschnig, K., Valenta, R., Keller, W., The cross-reactive calcium-binding pollen allergen, Phl p 7, reveals a novel dimer assembly. EMBO J. 2002, 21, 5007-5016.
    • (2002) Embo J. , vol.21 , pp. 5007-5016
    • Verdino, P.1    Westritschnig, K.2    Valenta, R.3    Keller, W.4
  • 128
    • 21744462815 scopus 로고    scopus 로고
    • Development of a functional in vitro assay as a novel tool for the standardization of allergen extracts in the human system
    • Vogel, L., Luttkopf, D., Hatahet, L., Haustein, D., Vieths, S., Development of a functional in vitro assay as a novel tool for the standardization of allergen extracts in the human system. Allergy 2005, 60, 1021-1028.
    • (2005) Allergy , vol.60 , pp. 1021-1028
    • Vogel, L.1    Luttkopf, D.2    Hatahet, L.3    Haustein, D.4    Vieths, S.5
  • 129
    • 0029838776 scopus 로고    scopus 로고
    • Antigen- specific sulphidoleukotriene production and histamine release in pollinic patients
    • Ferrer, M., Sanz, M. L., Prieto, I., Oehling, A., Antigen- specific sulphidoleukotriene production and histamine release in pollinic patients. J. Investig. Allergol. Clin. Immunol. 1996, 6, 271-277.
    • (1996) J. Investig. Allergol. Clin. Immunol. , vol.6 , pp. 271-277
    • Ferrer, M.1    Sanz, M.L.2    Prieto, I.3    Oehling, A.4
  • 130
    • 0016467814 scopus 로고
    • Mechanism of action of concanavalin A on human basophils
    • Siraganian, R. P., Siragania, P. A., Mechanism of action of concanavalin A on human basophils. J. Immunol. 1975, 114,886-893.
    • (1975) J. Immunol. , vol.114 , pp. 886-893
    • Siraganian, R.P.1    Siragania, P.A.2
  • 131
    • 21344445672 scopus 로고    scopus 로고
    • A comparative study of the FcepsilonRI molecule on human mast cell and basophil cell lines
    • Jensen, B. M., Dissing, S., Skov, P. S., Poulsen, L. K., A comparative study of the FcepsilonRI molecule on human mast cell and basophil cell lines. Int. Arch. Allergy Immunol. 2005, 137, 93-103.
    • (2005) Int. Arch. Allergy Immunol. , vol.137 , pp. 93-103
    • Jensen, B.M.1    Dissing, S.2    Skov, P.S.3    Poulsen, L.K.4
  • 132
    • 0037939677 scopus 로고    scopus 로고
    • Characterization of novel stem cell factor responsive human mast cell lines LAD 1 and 2 established from a patient with mast cell sarcoma/leukemia; activation following aggregation of FcepsilonRI or FcgammaRI
    • Kirshenbaum, A. S., Akin, C., Wu, Y., Rottem, M. et al., Characterization of novel stem cell factor responsive human mast cell lines LAD 1 and 2 established from a patient with mast cell sarcoma/leukemia; activation following aggregation of FcepsilonRI or FcgammaRI. Leuk. Res. 2003, 27, 677-682.
    • (2003) Leuk. Res. , vol.27 , pp. 677-682
    • Kirshenbaum, A.S.1    Akin, C.2    Wu, Y.3    Rottem, M.4
  • 133
    • 21844432134 scopus 로고    scopus 로고
    • Flow cytometric analysis of in vitro activated basophils, specific IgE and skin tests in the diagnosis of pollen-associated food allergy
    • Ebo, D. G., Hagendorens, M. M., Bridts, C. H., Schuerwegh, A. J. et al., Flow cytometric analysis of in vitro activated basophils, specific IgE and skin tests in the diagnosis of pollen-associated food allergy. Cytometry B Clin. Cytom. 2005,64,28-33.
    • (2005) Cytometry B Clin. Cytom , vol.64 , pp. 28-33
    • Ebo, D.G.1    Hagendorens, M.M.2    Bridts, C.H.3    Schuerwegh, A.J.4
  • 134
    • 20144387379 scopus 로고    scopus 로고
    • In vitro analysis of birch-pollen-associated food allergy by use of recombinant allergens in the basophil activation test
    • Erdmann, S. M., Sachs, B., Schmidt, A., Merk, H. F. et al., In vitro analysis of birch-pollen-associated food allergy by use of recombinant allergens in the basophil activation test. Int. Arch. Allergy Immunol. 2005, 136, 230-238.
    • (2005) Int. Arch. Allergy Immunol. , vol.136 , pp. 230-238
    • Erdmann, S.M.1    Sachs, B.2    Schmidt, A.3    Merk, H.F.4
  • 135
    • 34447522118 scopus 로고    scopus 로고
    • Ses i 6, the sesame 11S globulin, can activate basophils and shows cross-reactivity with walnut in vitro
    • Wallowitz, M. L., Chen, R. J., Tzen, J. T., Teuber, S. S., Ses i 6, the sesame 11S globulin, can activate basophils and shows cross-reactivity with walnut in vitro. Clin. Exp. Allergy 2007, 37, 929-938.
    • (2007) Clin. Exp. Allergy , vol.37 , pp. 929-938
    • Wallowitz, M.L.1    Chen, R.J.2    Tzen, J.T.3    Teuber, S.S.4
  • 136
    • 67651151518 scopus 로고    scopus 로고
    • Antigen-induced expression of CD203c on Basophils predicts IgE-mediated wheat allergy
    • Tokuda, R., Nagao, M., Hiraguchi, Y., Hosoki, K. et al., Antigen-induced expression of CD203c on Basophils predicts IgE-mediated wheat allergy. Allergol. Int. 2009, 58, 193-199.
    • (2009) Allergol. Int. , vol.58 , pp. 193-199
    • Tokuda, R.1    Nagao, M.2    Hiraguchi, Y.3    Hosoki, K.4
  • 137
    • 15044339986 scopus 로고    scopus 로고
    • Cellular allergen stimulation test (CAST) 2003, a review
    • de Weck, A. L., Sanz, M. L., Cellular allergen stimulation test (CAST) 2003, a review. J. Investig. Allergol. Clin. Immunol. 2004, 14, 253-273.
    • (2004) J. Investig. Allergol. Clin. Immunol. , vol.14 , pp. 253-273
    • de Weck, A.L.1    Sanz, M.L.2
  • 138
    • 44249085761 scopus 로고    scopus 로고
    • Diagnostic tests based on human basophils: More potentials and perspectives than pitfalls
    • de Weck, A. L., Sanz, M. L., Gamboa, P. M., Aberer, W. et al., Diagnostic tests based on human basophils: more potentials and perspectives than pitfalls. Int. Arch. Allergy Immunol. 2008, 146, 177-189.
    • (2008) Int. Arch. Allergy Immunol. , vol.146 , pp. 177-189
    • de Weck, A.L.1    Sanz, M.L.2    Gamboa, P.M.3    Aberer, W.4
  • 140
    • 33746276479 scopus 로고    scopus 로고
    • Requirements for effective IgE cross-linking on mast cells and basophils
    • Knol, E. F., Requirements for effective IgE cross-linking on mast cells and basophils. Mol. Nutr. Food Res. 2006, 50, 620-624.
    • (2006) Mol. Nutr. Food Res. , vol.50 , pp. 620-624
    • Knol, E.F.1
  • 141
    • 33645471330 scopus 로고    scopus 로고
    • Germin-like protein Cit s 1 and profilin Cit s 2 are major allergens in orange (Citrus sinensis) fruits
    • Crespo, J. F., Retzek, M., Foetisch, K., Sierra-Maestro, E. et al., Germin-like protein Cit s 1 and profilin Cit s 2 are major allergens in orange (Citrus sinensis) fruits. Mol. Nutr. Food Res. 2006, 50, 282-290.
    • (2006) Mol. Nutr. Food Res. , vol.50 , pp. 282-290
    • Crespo, J.F.1    Retzek, M.2    Foetisch, K.3    Sierra-Maestro, E.4
  • 142
    • 33947177572 scopus 로고    scopus 로고
    • Molecular characterisation of Lac s 1, the major allergen from lettuce (Lactuca sativa)
    • Hartz, C., San Miguel-Moncin Mdel, M., Cistero-Bahima, A., Fotisch, K. et al., Molecular characterisation of Lac s 1, the major allergen from lettuce (Lactuca sativa). Mol. Immunol. 2007, 44, 2820-2830.
    • (2007) Mol. Immunol. , vol.44 , pp. 2820-2830
    • Hartz, C.1    San Miguel-Moncin Mdel, M.2    Cistero-Bahima, A.3    Fotisch, K.4
  • 143
    • 2342633799 scopus 로고    scopus 로고
    • Tomato profilin Lyc e 1: IgE cross-reactivity and allergenic potency
    • Westphal, S., Kempf, W., Foetisch, K., Retzek, M. et al., Tomato profilin Lyc e 1: IgE cross-reactivity and allergenic potency. Allergy 2004, 59, 526-532.
    • (2004) Allergy , vol.59 , pp. 526-532
    • Westphal, S.1    Kempf, W.2    Foetisch, K.3    Retzek, M.4
  • 144
    • 12744253736 scopus 로고    scopus 로고
    • Molecular basis of pollen-related food allergy: Identifica- tion of a second cross-reactive IgE epitope on Pru av 1, the major cherry (Prunus avium) allergen
    • Wiche, R., Gubesch, M., Konig, H., Fotisch, K. et al., Molecular basis of pollen-related food allergy: identifica- tion of a second cross-reactive IgE epitope on Pru av 1, the major cherry (Prunus avium) allergen. Biochem. J. 2005, 385,319-327.
    • (2005) Biochem. J. , vol.385 , pp. 319-327
    • Wiche, R.1    Gubesch, M.2    Konig, H.3    Fotisch, K.4
  • 145
    • 28444461434 scopus 로고    scopus 로고
    • Gastrointestinal digestion of Bet v 1-homologous food allergens destroys their mediator-releasing, but not T cell-activating, capacity
    • Schimek, E. M., Zwolfer, B., Briza, P., Jahn-Schmid, B. et al., Gastrointestinal digestion of Bet v 1-homologous food allergens destroys their mediator-releasing, but not T cell-activating, capacity. J. Allergy Clin. Immunol. 2005, 116,1327-1333.
    • (2005) J. Allergy Clin. Immunol. , vol.116 , pp. 1327-1333
    • Schimek, E.M.1    Zwolfer, B.2    Briza, P.3    Jahn-Schmid, B.4
  • 146
    • 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
  • 147
    • 0346121482 scopus 로고    scopus 로고
    • Bet v 1, the major birch pollen allergen, initiates sensitization to Api g 1, the major allergen in celery: Evidence at the T-cell level
    • Bohle, B., Radakovics, A., Jahn-Schmid, B., Hoffmann-Sommergruber, K. et al., Bet v 1, the major birch pollen allergen, initiates sensitization to Api g 1, the major allergen in celery: evidence at the T-cell level. Eur. J. Immunol. 2003,33,3303-3310.
    • (2003) Eur. J. Immunol. , vol.33 , pp. 3303-3310
    • Bohle, B.1    Radakovics, A.2    Jahn-Schmid, B.3    Hoffmann-Sommergruber, K.4
  • 148
    • 28444434882 scopus 로고    scopus 로고
    • Characterization of the T-cell response to the major hazelnut allergen, Cor a 1.04: Evidence for a relevant T-cell epitope not cross-reactive with homologous pollen allergens
    • Bohle, B., Radakovics, A., Luttkopf, D., Jahn-Schmid, B. et al., Characterization of the T-cell response to the major hazelnut allergen, Cor a 1.04: evidence for a relevant T-cell epitope not cross-reactive with homologous pollen allergens. Clin. Exp. Allergy 2005, 35, 1392-1399.
    • (2005) Clin. Exp. Allergy , vol.35 , pp. 1392-1399
    • Bohle, B.1    Radakovics, A.2    Luttkopf, D.3    Jahn-Schmid, B.4
  • 149
    • 0031768652 scopus 로고    scopus 로고
    • Bet v 1, the major birch pollen allergen, and Mal d 1, the major apple allergen, cross-react at the level of allergen- specific T-helper cells
    • Fritsch, R., Bohle, B., Vollmann, U., Wiedermann, U. et al., Bet v 1, the major birch pollen allergen, and Mal d 1, the major apple allergen, cross-react at the level of allergen- specific T-helper cells. J. Allergy Clin. Immunol. 1998, 102, 679-686.
    • (1998) J. Allergy Clin. Immunol. , vol.102 , pp. 679-686
    • Fritsch, R.1    Bohle, B.2    Vollmann, U.3    Wiedermann, U.4
  • 150
    • 21344438163 scopus 로고    scopus 로고
    • Bet v 1142-156 is the dominant T-cell epitope of the major birch pollen allergen and important for cross-reactivity with Bet v 1-related food allergens
    • Jahn-Schmid, B., Radakovics, A., Luttkopf, D., Scheurer, S. et al., Bet v 1142-156 is the dominant T-cell epitope of the major birch pollen allergen and important for cross-reactivity with Bet v 1-related food allergens. J. Allergy Clin. Immunol. 2005, 116, 213-219.
    • (2005) J. Allergy Clin. Immunol. , vol.116 , pp. 213-219
    • Jahn-Schmid, B.1    Radakovics, A.2    Luttkopf, D.3    Scheurer, S.4
  • 151
    • 33845430391 scopus 로고    scopus 로고
    • The impact of pollen-related food allergens on pollen allergy
    • Bohle, B., The impact of pollen-related food allergens on pollen allergy. Allergy 2007, 62, 3-10.
    • (2007) Allergy , vol.62 , pp. 3-10
    • Bohle, B.1
  • 152
    • 67649230494 scopus 로고    scopus 로고
    • Characterization of the allergic T-cell response to Pru p 3, the nonspecific lipid transfer protein in peach
    • Schulten, V., Radakovics, A., Hartz, C., Mari, A. et al., Characterization of the allergic T-cell response to Pru p 3, the nonspecific lipid transfer protein in peach. J. Allergy Clin. Immunol. 2009, 24, 100-107.
    • (2009) J. Allergy Clin. Immunol. , vol.24 , pp. 100-107
    • Schulten, V.1    Radakovics, A.2    Hartz, C.3    Mari, A.4
  • 153
    • 58249106744 scopus 로고    scopus 로고
    • T-cell epitopes of the major peach allergen, Pru p 3: Identification and differential T-cell response of peach-allergic and non-allergic subjects
    • Tordesillas, L., Cuesta-Herranz, J., Gonzalez-Munoz, M., Pacios, L. F. et al., T-cell epitopes of the major peach allergen, Pru p 3: Identification and differential T-cell response of peach-allergic and non-allergic subjects. Mol. Immunol. 2009, 46, 722-728.
    • (2009) Mol. Immunol. , vol.46 , pp. 722-728
    • Tordesillas, L.1    Cuesta-Herranz, J.2    Gonzalez-Munoz, M.3    Pacios, L.F.4
  • 154
    • 0032972433 scopus 로고    scopus 로고
    • T-cell receptor contact and MHC binding residues of a major rye grass pollen allergen T-cell epitope
    • Burton, M. D., Blaher, B., Suphioglu, C., O'Hehir, R. E. et al., T-cell receptor contact and MHC binding residues of a major rye grass pollen allergen T-cell epitope. J. Allergy Clin. Immunol. 1999, 103, 255-261.
    • (1999) J. Allergy Clin. Immunol. , vol.103 , pp. 255-261
    • Burton, M.D.1    Blaher, B.2    Suphioglu, C.3    O'Hehir, R.E.4
  • 155
    • 0032701129 scopus 로고    scopus 로고
    • Naturally processed and presented epitopes of the islet cell autoantigen IA-2 eluted from HLA-DR4
    • Peakman, M., Stevens, E. J., Lohmann, T., Narendran, P. et al., Naturally processed and presented epitopes of the islet cell autoantigen IA-2 eluted from HLA-DR4. J. Clin. Invest. 1999, 104, 1449-1457.
    • (1999) J. Clin. Invest. , vol.104 , pp. 1449-1457
    • Peakman, M.1    Stevens, E.J.2    Lohmann, T.3    Narendran, P.4
  • 156
    • 74349117314 scopus 로고    scopus 로고
    • Development of recombinant allergens for diagnosis and therapy
    • Egger, M., Hauser, M., Himly, M., Wopfner, N. et al., Development of recombinant allergens for diagnosis and therapy. Front. Biosci. (Elite Ed) 2009, 1, 77-90.
    • (2009) Front. Biosci. (elite Ed) , vol.1 , pp. 77-90
    • Egger, M.1    Hauser, M.2    Himly, M.3    Wopfner, N.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.