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Volumn 57, Issue 1, 2013, Pages 145-152

Impact of dietary factors and food processing on food allergy

Author keywords

Allergen modification; Allergenicity; Food allergy; Food processing; Oral tolerance

Indexed keywords

ALLERGEN; ALPHA TOCOPHEROL; ANTIGEN; POLYPHENOL; PREBIOTIC AGENT; RETINOIC ACID; UNSATURATED FATTY ACID;

EID: 84872138225     PISSN: 16134125     EISSN: 16134133     Source Type: Journal    
DOI: 10.1002/mnfr.201200472     Document Type: Review
Times cited : (49)

References (76)
  • 2
    • 43049168908 scopus 로고    scopus 로고
    • The prevalence of plant food allergies: a systematic review
    • e4.
    • Zuidmeer, L., Goldhahn, K., Rona, R. J., Gislason, D. et al., The prevalence of plant food allergies: a systematic review. J. Allergy Clin. Immunol. 2008, 121, 1210-1218.e4.
    • (2008) J. Allergy Clin. Immunol. , vol.121 , pp. 1210-1218
    • Zuidmeer, L.1    Goldhahn, K.2    Rona, R.J.3    Gislason, D.4
  • 3
    • 38949111702 scopus 로고    scopus 로고
    • Original article: prevalence and cumulative incidence of food hypersensitivity in the first 3 years of life
    • Venter, C., Pereira, B., Voigt, K., Grundy, J. et al., Original article: prevalence and cumulative incidence of food hypersensitivity in the first 3 years of life. Allergy. 2008, 63, 354-359.
    • (2008) Allergy. , vol.63 , pp. 354-359
    • Venter, C.1    Pereira, B.2    Voigt, K.3    Grundy, J.4
  • 6
    • 77950251400 scopus 로고    scopus 로고
    • A human gut microbial gene catalogue established by metagenomic sequencing
    • Qin, J., A human gut microbial gene catalogue established by metagenomic sequencing. Nature 2010, 464, 59-65.
    • (2010) Nature , vol.464 , pp. 59-65
    • Qin, J.1
  • 7
    • 59849113547 scopus 로고    scopus 로고
    • Microbes in gastrointestinal health and disease
    • Neish, A. S., Microbes in gastrointestinal health and disease. Gastroenterology 2009, 136, 65-80.
    • (2009) Gastroenterology , vol.136 , pp. 65-80
    • Neish, A.S.1
  • 9
    • 11344286028 scopus 로고    scopus 로고
    • Oral tolerance and its relation to food hypersensitivities
    • Chehade, M., Mayer, L., Oral tolerance and its relation to food hypersensitivities. J. Allergy Clin. Immunol. 2005, 115, 3-12.
    • (2005) J. Allergy Clin. Immunol. , vol.115 , pp. 3-12
    • Chehade, M.1    Mayer, L.2
  • 10
    • 0021273088 scopus 로고
    • Direct evidence for an integrated function of J chain and secretory component in epithelial transport of immunoglobulins
    • Brandtzaeg, P., Prydz, H., Direct evidence for an integrated function of J chain and secretory component in epithelial transport of immunoglobulins. Nature 1984, 311, 71-73.
    • (1984) Nature , vol.311 , pp. 71-73
    • Brandtzaeg, P.1    Prydz, H.2
  • 11
    • 27944504324 scopus 로고    scopus 로고
    • Secretory IgA and mucin-mediated biofilm formation by environmental strains of Escherichia coli: role of type 1 pili
    • Bollinger, R. R., Secretory IgA and mucin-mediated biofilm formation by environmental strains of Escherichia coli: role of type 1 pili. Mol. Immunol. 2006, 43, 378-387.
    • (2006) Mol. Immunol. , vol.43 , pp. 378-387
    • Bollinger, R.R.1
  • 12
    • 77955810123 scopus 로고    scopus 로고
    • Food allergy: separating the science from the mythology
    • Brandtzaeg, P., Food allergy: separating the science from the mythology. Nat. Rev. Gastroenterol. Hepatol. 2010, 7, 380-400.
    • (2010) Nat. Rev. Gastroenterol. Hepatol. , vol.7 , pp. 380-400
    • Brandtzaeg, P.1
  • 13
    • 3242754344 scopus 로고    scopus 로고
    • Tolerance induced by inhaled antigen involves CD4(+) T cells expressing membrane-bound TGF-beta and FOXP3
    • Ostroukhova, M., Seguin-Devaux, C., Oriss, T. B., Dixon-McCarthy, B. et al., Tolerance induced by inhaled antigen involves CD4(+) T cells expressing membrane-bound TGF-beta and FOXP3. J. Clin. Invest. 2004, 114, 28-38.
    • (2004) J. Clin. Invest. , vol.114 , pp. 28-38
    • Ostroukhova, M.1    Seguin-Devaux, C.2    Oriss, T.B.3    Dixon-McCarthy, B.4
  • 14
    • 38349135985 scopus 로고    scopus 로고
    • Dietary allergenic proteins and intestinal immunity: a shift from oral tolerance to sensitization
    • Hogan, S. P., Rothenberg, M. E., Dietary allergenic proteins and intestinal immunity: a shift from oral tolerance to sensitization. Clin. Exp. Allergy 2008, 38, 229-232.
    • (2008) Clin. Exp. Allergy , vol.38 , pp. 229-232
    • Hogan, S.P.1    Rothenberg, M.E.2
  • 15
    • 50249179101 scopus 로고    scopus 로고
    • Vitamin effects on the immune system: vitamins A and D take centre stage
    • Mora, J. R., Iwata, M., Andrian, U. H. von, Vitamin effects on the immune system: vitamins A and D take centre stage. Nat. Rev. Immunol. 2008, 8, 685-698.
    • (2008) Nat. Rev. Immunol. , vol.8 , pp. 685-698
    • Mora, J.R.1    Iwata, M.2    Andrian von, U.H.3
  • 16
    • 0036444413 scopus 로고    scopus 로고
    • Loss of ileal IgA+ plasma cells and of CD4+ lymphocytes in ileal Peyer's patches of vitamin A deficient rats
    • Bjersing, J. L., Telemo, E., Dahlgren, U., Hanson, L. A., Loss of ileal IgA+ plasma cells and of CD4+ lymphocytes in ileal Peyer's patches of vitamin A deficient rats. Clin. Exp. Immunol. 2002, 130, 404-408.
    • (2002) Clin. Exp. Immunol. , vol.130 , pp. 404-408
    • Bjersing, J.L.1    Telemo, E.2    Dahlgren, U.3    Hanson, L.A.4
  • 17
    • 34547788180 scopus 로고    scopus 로고
    • A functionally specialized population of mucosal CD103+ DCs induces Foxp3 +regulatory T cells via a TGF- and retinoic acid dependent mechanism
    • Coombes, J. L., Siddiqui, K. R., Arancibia-Carcamo, C. V., Hall, J. et al., A functionally specialized population of mucosal CD103+ DCs induces Foxp3 +regulatory T cells via a TGF- and retinoic acid dependent mechanism. J. Exp. Med. 2007, 204, 1757-1764.
    • (2007) J. Exp. Med. , vol.204 , pp. 1757-1764
    • Coombes, J.L.1    Siddiqui, K.R.2    Arancibia-Carcamo, C.V.3    Hall, J.4
  • 19
    • 0020556109 scopus 로고
    • Increased mortality in children with mild vitamin A deficiency
    • Sommer, A., Hussaini, G., Tarwotjo, I., Susanto, D., Increased mortality in children with mild vitamin A deficiency. The Lancet 1983, 322, 585-588.
    • (1983) The Lancet , vol.322 , pp. 585-588
    • Sommer, A.1    Hussaini, G.2    Tarwotjo, I.3    Susanto, D.4
  • 21
    • 79959396339 scopus 로고    scopus 로고
    • Bile retinoids imprint intestinal CD103+ dendritic cells with the ability to generate gut-tropic T cells
    • Jaensson-Gyllenbäck, E., Kotarsky, K., Zapata, F., Persson, E. K. et al., Bile retinoids imprint intestinal CD103+ dendritic cells with the ability to generate gut-tropic T cells. Mucosal Immunol. 2011, 4, 438-447.
    • (2011) Mucosal Immunol. , vol.4 , pp. 438-447
    • Jaensson-Gyllenbäck, E.1    Kotarsky, K.2    Zapata, F.3    Persson, E.K.4
  • 22
    • 33646413182 scopus 로고    scopus 로고
    • Mechanisms of disease: the hygiene hypothesis revisited
    • Guarner, F., Mechanisms of disease: the hygiene hypothesis revisited. Nat. Clin. Pract. Gastroenterol. Hepatol. 2006, 3, 275-284.
    • (2006) Nat. Clin. Pract. Gastroenterol. Hepatol. , vol.3 , pp. 275-284
    • Guarner, F.1
  • 24
    • 7944231342 scopus 로고    scopus 로고
    • Does the microbiota regulate immune responses outside the gut?
    • Noverr, M. C., Huffnagle, G. B., Does the microbiota regulate immune responses outside the gut? Trends Microbiol. 2004, 12, 562-568.
    • (2004) Trends Microbiol. , vol.12 , pp. 562-568
    • Noverr, M.C.1    Huffnagle, G.B.2
  • 25
    • 44949127290 scopus 로고    scopus 로고
    • Effect of intestinal microbiota on the induction of regulatory CD25 CD4 T cells
    • Ishikawa, H., Tanaka, K., Maeda, Y., Aiba, Y. et al., Effect of intestinal microbiota on the induction of regulatory CD25 CD4 T cells. Clin. Exp. Immunol. 2008, 153, 127-135.
    • (2008) Clin. Exp. Immunol. , vol.153 , pp. 127-135
    • Ishikawa, H.1    Tanaka, K.2    Maeda, Y.3    Aiba, Y.4
  • 26
    • 77957075815 scopus 로고    scopus 로고
    • Impact of diet in shaping gut microbiota revealed by a comparative study in children from Europe and rural Africa
    • Filippo, C. de, Cavalieri, D., Di Paola, M., Ramazzotti, M. et al., Impact of diet in shaping gut microbiota revealed by a comparative study in children from Europe and rural Africa. Proc. Natl. Acad. Sci. USA 2010, 107, 14691-14696.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 14691-14696
    • Filippo de, C.1    Cavalieri, D.2    Di Paola, M.3    Ramazzotti, M.4
  • 27
    • 70350666634 scopus 로고    scopus 로고
    • Regulation of inflammatory responses by gut microbiota and chemoattractant receptor GPR43
    • Maslowski, K. M., Vieira, A. T., Ng, A., Kranich, J. et al., Regulation of inflammatory responses by gut microbiota and chemoattractant receptor GPR43. Nature 2009, 461, 1282-1286.
    • (2009) Nature , vol.461 , pp. 1282-1286
    • Maslowski, K.M.1    Vieira, A.T.2    Ng, A.3    Kranich, J.4
  • 28
    • 0038491435 scopus 로고    scopus 로고
    • Functional characterization of human receptors for short chain fatty acids and their role in polymorphonuclear cell activation
    • Le Poul, E., Functional characterization of human receptors for short chain fatty acids and their role in polymorphonuclear cell activation. J. Biol. Chem. 2003, 278, 25481-25489.
    • (2003) J. Biol. Chem. , vol.278 , pp. 25481-25489
    • Le Poul, E.1
  • 29
    • 77954738601 scopus 로고    scopus 로고
    • Inducible Foxp3+ regulatory T-cell development by a commensal bacterium of the intestinal microbiota
    • Round, J. L., Mazmanian, S. K., Inducible Foxp3+ regulatory T-cell development by a commensal bacterium of the intestinal microbiota. Proc. Natl. Acad. Sci. USA 2010, 107, 12204-12209.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 12204-12209
    • Round, J.L.1    Mazmanian, S.K.2
  • 30
    • 78449248773 scopus 로고    scopus 로고
    • Prebiotic oligosaccharides: in vitro evidence for gastrointestinal epithelial transfer and immunomodulatory properties
    • Eiwegger, T., Stahl, B., Haidl, P., Schmitt, J. et al., Prebiotic oligosaccharides: in vitro evidence for gastrointestinal epithelial transfer and immunomodulatory properties. Pediatr. Allergy Immunol. 2010, 21, 1179-1188.
    • (2010) Pediatr. Allergy Immunol. , vol.21 , pp. 1179-1188
    • Eiwegger, T.1    Stahl, B.2    Haidl, P.3    Schmitt, J.4
  • 31
    • 84857158723 scopus 로고    scopus 로고
    • Galectin-9 induced by dietary synbiotics is involved in suppression of allergic symptoms in mice and humans
    • Kivit, S., Saeland, E., Kraneveld, A. D., Kant, H. J. G. et al., Galectin-9 induced by dietary synbiotics is involved in suppression of allergic symptoms in mice and humans. Allergy 2012, 67, 343-352.
    • (2012) Allergy , vol.67 , pp. 343-352
    • Kivit, S.1    Saeland, E.2    Kraneveld, A.D.3    Kant, H.J.G.4
  • 32
    • 0034605680 scopus 로고    scopus 로고
    • Dietary vitamin E, IgE concentrations, and atopy
    • Fogarty, A., Lewis, S., Weiss, S., Britton, J., Dietary vitamin E, IgE concentrations, and atopy. The Lancet 2000, 356, 1573-1574.
    • (2000) The Lancet , vol.356 , pp. 1573-1574
    • Fogarty, A.1    Lewis, S.2    Weiss, S.3    Britton, J.4
  • 33
    • 0036738755 scopus 로고    scopus 로고
    • Vitamin E inhibits IL-4 gene expression in peripheral blood T cells
    • Li-Weber, M., Giaisi, M., Treiber, M. K., Krammer, P. H., Vitamin E inhibits IL-4 gene expression in peripheral blood T cells. Eur. J. Immunol. 2002, 32, 2401-2408.
    • (2002) Eur. J. Immunol. , vol.32 , pp. 2401-2408
    • Li-Weber, M.1    Giaisi, M.2    Treiber, M.K.3    Krammer, P.H.4
  • 34
    • 77952044210 scopus 로고    scopus 로고
    • Polyphenol-enriched apple extract attenuates food allergy in mice
    • Zuercher, A. W., Holvoet, S., Weiss, M., Mercenier, A., Polyphenol-enriched apple extract attenuates food allergy in mice. Clin. Exp. Allergy 2010, 40, 942-950.
    • (2010) Clin. Exp. Allergy , vol.40 , pp. 942-950
    • Zuercher, A.W.1    Holvoet, S.2    Weiss, M.3    Mercenier, A.4
  • 35
    • 0031031345 scopus 로고    scopus 로고
    • Dietary fat and asthma: is there a connection?
    • Black, P., Sharpe, S., Dietary fat and asthma: is there a connection? Eur. Resp. J. 1997, 10, 6-12.
    • (1997) Eur. Resp. J. , vol.10 , pp. 6-12
    • Black, P.1    Sharpe, S.2
  • 36
    • 0031179646 scopus 로고    scopus 로고
    • IL-12-deficient dendritic cells, generated in the presence of prostaglandin E2, promote type 2 cytokine production in maturing human naive T helper cells
    • Kaliński, P., Hilkens, C. M., Snijders, A., Snijdewint, F. G. et al., IL-12-deficient dendritic cells, generated in the presence of prostaglandin E2, promote type 2 cytokine production in maturing human naive T helper cells. J. Immunol. 1997, 159, 28-35.
    • (1997) J. Immunol. , vol.159 , pp. 28-35
    • Kaliński, P.1    Hilkens, C.M.2    Snijders, A.3    Snijdewint, F.G.4
  • 37
    • 0028984631 scopus 로고
    • Prostaglandin E2 promotes B lymphocyte Ig isotype switching to IgE
    • Roper, R. L., Brown, D. M., Phipps, R. P., Prostaglandin E2 promotes B lymphocyte Ig isotype switching to IgE. J. Immunol. 1995, 154, 162-170.
    • (1995) J. Immunol. , vol.154 , pp. 162-170
    • Roper, R.L.1    Brown, D.M.2    Phipps, R.P.3
  • 38
    • 77956165390 scopus 로고    scopus 로고
    • GPR120 is an omega-3 fatty acid receptor mediating potent anti-inflammatory and insulin-sensitizing effects
    • Oh, D. Y., Talukdar, S., Bae, E. J., Imamura, T. et al., GPR120 is an omega-3 fatty acid receptor mediating potent anti-inflammatory and insulin-sensitizing effects. Cell 2010, 142, 687-698.
    • (2010) Cell , vol.142 , pp. 687-698
    • Oh, D.Y.1    Talukdar, S.2    Bae, E.J.3    Imamura, T.4
  • 39
    • 12344321136 scopus 로고    scopus 로고
    • Stereochemical assignment, antiinflammatory properties, and receptor for the omega-3 lipid mediator resolvin E1
    • Arita, M., Stereochemical assignment, antiinflammatory properties, and receptor for the omega-3 lipid mediator resolvin E1. J. Exp. Med. 2005, 201, 713-722.
    • (2005) J. Exp. Med. , vol.201 , pp. 713-722
    • Arita, M.1
  • 40
    • 79960520649 scopus 로고    scopus 로고
    • Allergic disease in infants up to 2 years of age in relation to plasma omega-3 fatty acids and maternal fish oil supplementation in pregnancy and lactation
    • Furuhjelm, C., Warstedt, K., Fagerås, M., Fälth-Magnusson, K. et al., Allergic disease in infants up to 2 years of age in relation to plasma omega-3 fatty acids and maternal fish oil supplementation in pregnancy and lactation. Pediatr. Allergy Immunol. 2011, 22, 505-514.
    • (2011) Pediatr. Allergy Immunol. , vol.22 , pp. 505-514
    • Furuhjelm, C.1    Warstedt, K.2    Fagerås, M.3    Fälth-Magnusson, K.4
  • 41
    • 3543045059 scopus 로고    scopus 로고
    • The ratio of n-6 to n-3 fatty acids in maternal diet influences the induction of neonatal immunological tolerance to ovalbumin
    • Korotkova, M., Telemo, E., Yamashiro, Y., Hanson, L. Å. et al., The ratio of n-6 to n-3 fatty acids in maternal diet influences the induction of neonatal immunological tolerance to ovalbumin. Clin. Exp. Immunol. 2004, 137, 237-244.
    • (2004) Clin. Exp. Immunol. , vol.137 , pp. 237-244
    • Korotkova, M.1    Telemo, E.2    Yamashiro, Y.3    Hanson, L.A.4
  • 42
    • 10844244091 scopus 로고    scopus 로고
    • Structural and functional alterations in major peanut allergens caused by thermal processing
    • Maleki, S. J., Hurlburt, B. K., Structural and functional alterations in major peanut allergens caused by thermal processing. J. AOAC Int. 2004, 87, 1475-1479.
    • (2004) J. AOAC Int. , vol.87 , pp. 1475-1479
    • Maleki, S.J.1    Hurlburt, B.K.2
  • 43
    • 69149109662 scopus 로고    scopus 로고
    • Impact of food processing on the structural and allergenic properties of food allergens
    • Mills, E. N. C., Sancho, A. I., Rigby, N. M., Jenkins, J. A. et al., Impact of food processing on the structural and allergenic properties of food allergens. Mol. Nutr. Food Res. 2009, 53, 963-969.
    • (2009) Mol. Nutr. Food Res. , vol.53 , pp. 963-969
    • Mills, E.N.C.1    Sancho, A.I.2    Rigby, N.M.3    Jenkins, J.A.4
  • 44
    • 84860473202 scopus 로고    scopus 로고
    • Effect of processing on recovery and variability associated with immunochemical analytical methods for multiple allergens in a single matrix: dark chocolate
    • Khuda, S., Slate, A., Pereira, M., Al-Taher, F. et al., Effect of processing on recovery and variability associated with immunochemical analytical methods for multiple allergens in a single matrix: dark chocolate. J. Agric. Food Chem. 2012, 60, 4204-4211.
    • (2012) J. Agric. Food Chem. , vol.60 , pp. 4204-4211
    • Khuda, S.1    Slate, A.2    Pereira, M.3    Al-Taher, F.4
  • 45
    • 84860473202 scopus 로고    scopus 로고
    • Effect of processing on recovery and variability associated with immunochemical analytical methods for multiple allergens in a single matrix: sugar cookies
    • Khuda, S., Slate, A., Pereira, M., Al-Taher, F. et al., Effect of processing on recovery and variability associated with immunochemical analytical methods for multiple allergens in a single matrix: sugar cookies. J. Agric. Food Chem. 2012, 60, 4195-4203.
    • (2012) J. Agric. Food Chem. , vol.60 , pp. 4195-4203
    • Khuda, S.1    Slate, A.2    Pereira, M.3    Al-Taher, F.4
  • 46
    • 68549136672 scopus 로고    scopus 로고
    • The role of immunoglobulin E-binding epitopes in the characterization of food allergy
    • Lin, J., Sampson, H. A., The role of immunoglobulin E-binding epitopes in the characterization of food allergy. Curr. Opin. Allergy Clin. Immunol. 2009, 9, 357-363.
    • (2009) Curr. Opin. Allergy Clin. Immunol. , vol.9 , pp. 357-363
    • Lin, J.1    Sampson, H.A.2
  • 47
    • 85004829961 scopus 로고
    • Murine passive cutaneous anaphylaxis test (PCA) for the 'all or none' determination of allergenicity of bovine whey proteins and peptides
    • Poulsen, O. M., Hau, J., Murine passive cutaneous anaphylaxis test (PCA) for the 'all or none' determination of allergenicity of bovine whey proteins and peptides. Clin. Allergy 1987, 17, 75-83.
    • (1987) Clin. Allergy , vol.17 , pp. 75-83
    • Poulsen, O.M.1    Hau, J.2
  • 48
    • 78951484854 scopus 로고    scopus 로고
    • Controlling the aggregation propensity and thereby digestibility of allergens by Maillardation as illustrated for cod fish parvalbumin
    • De Jongh, H. H., Taylor, S. L., Koppelman, S. J., Controlling the aggregation propensity and thereby digestibility of allergens by Maillardation as illustrated for cod fish parvalbumin. J. Biosci. Bioengin. 2011, 111, 204-211.
    • (2011) J. Biosci. Bioengin. , vol.111 , pp. 204-211
    • De Jongh, H.H.1    Taylor, S.L.2    Koppelman, S.J.3
  • 49
    • 69149106437 scopus 로고    scopus 로고
    • In vitro digestion methods for assessing the effect of food structure on allergen breakdown
    • Wickham, M., Faulks, R., Mills, C., In vitro digestion methods for assessing the effect of food structure on allergen breakdown. Mol. Nutr. Food Res. 2009, 53, 952-958.
    • (2009) Mol. Nutr. Food Res. , vol.53 , pp. 952-958
    • Wickham, M.1    Faulks, R.2    Mills, C.3
  • 50
    • 80053093893 scopus 로고    scopus 로고
    • Human immunoglobulin E (IgE) binding to heated and glycated ovalbumin and ovomucoid before and after in vitro digestion
    • Jiménez-Saiz, R., Belloque, J., Molina, E., López-Fandiño, R., Human immunoglobulin E (IgE) binding to heated and glycated ovalbumin and ovomucoid before and after in vitro digestion. J. Agric. Food Chem. 2011, 59, 10044-10051.
    • (2011) J. Agric. Food Chem. , vol.59 , pp. 10044-10051
    • Jiménez-Saiz, R.1    Belloque, J.2    Molina, E.3    López-Fandiño, R.4
  • 51
    • 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. C., 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 - Proteins & Proteomics 2005, 1752, 142-153.
    • (2005) Biochim. Biophys. Acta - Proteins & Proteomics , vol.1752 , pp. 142-153
    • Moreno, F.J.1    Maldonado, B.M.2    Wellner, N.3    Mills, E.C.4
  • 52
    • 0034978333 scopus 로고    scopus 로고
    • How can thermal processing modify the antigenicity of proteins?
    • Davis, P. J., Smales, C. M., James, D. C., How can thermal processing modify the antigenicity of proteins? Allergy 2001, 56(Suppl 67), 56-60.
    • (2001) Allergy , vol.56 , Issue.SUPPL 67 , pp. 56-60
    • Davis, P.J.1    Smales, C.M.2    James, D.C.3
  • 53
    • 75949094757 scopus 로고    scopus 로고
    • Effects of glycation of the model food allergen ovalbumin on antigen uptake and presentation by human dendritic cells
    • Hilmenyuk, T., Bellinghausen, I., Heydenreich, B., Ilchmann, A. et al., Effects of glycation of the model food allergen ovalbumin on antigen uptake and presentation by human dendritic cells. Immunology 2010, 129, 437-445.
    • (2010) Immunology , vol.129 , pp. 437-445
    • Hilmenyuk, T.1    Bellinghausen, I.2    Heydenreich, B.3    Ilchmann, A.4
  • 54
    • 68049123064 scopus 로고    scopus 로고
    • Rare, medium, or well done? The effect of heating and food matrix on food protein allergenicity
    • Nowak-Wegrzyn, A., Fiocchi, A., Rare, medium, or well done? The effect of heating and food matrix on food protein allergenicity. Curr Opin. Allergy Clin. Immunol. 2009, 9, 234-237.
    • (2009) Curr Opin. Allergy Clin. Immunol. , vol.9 , pp. 234-237
    • Nowak-Wegrzyn, A.1    Fiocchi, A.2
  • 55
    • 22244434681 scopus 로고    scopus 로고
    • Effects of food processing on the stability of food allergens
    • Sathe, S. K., Teuber, S. S., Roux, K. H., Effects of food processing on the stability of food allergens. Biotech. Adv. 2005, 23, 423-429.
    • (2005) Biotech. Adv. , vol.23 , pp. 423-429
    • Sathe, S.K.1    Teuber, S.S.2    Roux, K.H.3
  • 56
    • 0034817848 scopus 로고    scopus 로고
    • Binding of two mono-acylated lipid monomers by the barley lipid transfer protein, LTP1, as viewed by fluorescence, isothermal titration calorimetry and molecular modelling
    • Douliez, J. P., Jégou, S., Pato, C., Mollé, D. et al., Binding of two mono-acylated lipid monomers by the barley lipid transfer protein, LTP1, as viewed by fluorescence, isothermal titration calorimetry and molecular modelling. Eur. J. Biochem. 2001, 268, 384-388.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 384-388
    • Douliez, J.P.1    Jégou, S.2    Pato, C.3    Mollé, D.4
  • 57
    • 34548285780 scopus 로고    scopus 로고
    • Heat treatment of bovine α-lactalbumin results in partially folded, disulfide bond shuffled states with enhanced surface activity
    • Wijesinha-Bettoni, R., Gao, C., Jenkins, J. A., Mackie, A. R. et al., Heat treatment of bovine α-lactalbumin results in partially folded, disulfide bond shuffled states with enhanced surface activity. Biochemistry 2007, 46, 9774-9784.
    • (2007) Biochemistry , vol.46 , pp. 9774-9784
    • Wijesinha-Bettoni, R.1    Gao, C.2    Jenkins, J.A.3    Mackie, A.R.4
  • 58
    • 0037423721 scopus 로고    scopus 로고
    • Stable monomeric intermediate with exposed Cys-119 is formed during heat denaturation of β-lactoglobulin
    • Croguennec, T., Bouhallab, S., Mollé, D., O'Kennedy, B. T. et al., Stable monomeric intermediate with exposed Cys-119 is formed during heat denaturation of β-lactoglobulin. Biochem. Biophys. Res. Comm. 2003, 301, 465-471.
    • (2003) Biochem. Biophys. Res. Comm. , vol.301 , pp. 465-471
    • Croguennec, T.1    Bouhallab, S.2    Mollé, D.3    O'Kennedy, B.T.4
  • 59
    • 0019072753 scopus 로고
    • Heat-induced association of beta-lactoglobulin and casein micelles
    • Smits, P., van Brouwershaven, J. H., Heat-induced association of beta-lactoglobulin and casein micelles. J. Dairy Res. 1980, 47, 313-325.
    • (1980) J. Dairy Res. , vol.47 , pp. 313-325
    • Smits, P.1    van Brouwershaven, J.H.2
  • 60
    • 0034967751 scopus 로고    scopus 로고
    • Conformational characterization of oligomeric intermediates and aggregates in beta-lactoglobulin heat aggregation
    • Carrotta, R., Bauer, R., Waninge, R., Rischel, C., Conformational characterization of oligomeric intermediates and aggregates in beta-lactoglobulin heat aggregation. Protein Sci. 2001, 10, 1312-1318.
    • (2001) Protein Sci. , vol.10 , pp. 1312-1318
    • Carrotta, R.1    Bauer, R.2    Waninge, R.3    Rischel, C.4
  • 61
    • 67651241140 scopus 로고    scopus 로고
    • Circular dichroism techniques: biomolecular and nanostructural analyses-a review
    • Ranjbar, B., Gill, P., Circular dichroism techniques: biomolecular and nanostructural analyses-a review. Chem. Biol. Drug Des. 2009, 74, 101-120.
    • (2009) Chem. Biol. Drug Des. , vol.74 , pp. 101-120
    • Ranjbar, B.1    Gill, P.2
  • 62
    • 34247643756 scopus 로고    scopus 로고
    • Effect of heat treatment on the detection of intact bovine β-lactoglobulins by LC mass spectrometry
    • Monaci, L., van Hengel, A. J., Effect of heat treatment on the detection of intact bovine β-lactoglobulins by LC mass spectrometry. J. Agric. Food Chem. 2007, 55, 2985-2992.
    • (2007) J. Agric. Food Chem. , vol.55 , pp. 2985-2992
    • Monaci, L.1    van Hengel, A.J.2
  • 63
    • 0001517504 scopus 로고
    • Caseins as rheomorphic proteins: interpretation of primary and secondary structures of the αS1-, β- and κ-caseins
    • Holt, C., Sawyer, L., Caseins as rheomorphic proteins: interpretation of primary and secondary structures of the αS1-, β- and κ-caseins. Faraday Trans. 1993, 89, 2683-2692.
    • (1993) Faraday Trans. , vol.89 , pp. 2683-2692
    • Holt, C.1    Sawyer, L.2
  • 64
    • 0027944011 scopus 로고
    • Preferential recognition of primary protein structures of alpha-casein by IgG and IgE antibodies of patients with milk allergy
    • Kohno, Y., Honma, K., Saito, K., Shimojo, N. et al., Preferential recognition of primary protein structures of alpha-casein by IgG and IgE antibodies of patients with milk allergy. Ann. Allergy. 1994, 73, 419-422.
    • (1994) Ann. Allergy. , vol.73 , pp. 419-422
    • Kohno, Y.1    Honma, K.2    Saito, K.3    Shimojo, N.4
  • 65
    • 0035189555 scopus 로고    scopus 로고
    • Food allergy to wheat products: the effect of bread baking and in vitro digestion on wheat allergenic proteins. A study with bread dough, crumb, and crust
    • Simonato, B., Pasini, G., Giannattasio, M., Peruffo, A. D. B. et al., Food allergy to wheat products: the effect of bread baking and in vitro digestion on wheat allergenic proteins. A study with bread dough, crumb, and crust. J. Agric. Food Chem. 2001, 49, 5668-5673.
    • (2001) J. Agric. Food Chem. , vol.49 , pp. 5668-5673
    • Simonato, B.1    Pasini, G.2    Giannattasio, M.3    Peruffo, A.D.B.4
  • 66
    • 0000916315 scopus 로고
    • Action des acides aminés sur les sucres: formation de mélanoïdes par voie méthodique
    • Maillard, L. C., Action des acides aminés sur les sucres: formation de mélanoïdes par voie méthodique. C.R. Acad. Sci. 1912, 154, 66-68.
    • (1912) C.R. Acad. Sci. , vol.154 , pp. 66-68
    • Maillard, L.C.1
  • 67
    • 23844498767 scopus 로고    scopus 로고
    • Carbonylation of milk powder proteins as a consequence of processing conditions
    • Fenaille, F., Parisod, V., Tabet, J.-C., Guy, P. A., Carbonylation of milk powder proteins as a consequence of processing conditions. Proteomics 2005, 5, 3097-3104.
    • (2005) Proteomics , vol.5 , pp. 3097-3104
    • Fenaille, F.1    Parisod, V.2    Tabet, J.-C.3    Guy, P.A.4
  • 68
    • 83055179019 scopus 로고    scopus 로고
    • Rapid fingerprinting of milk thermal processing history by intact protein mass spectrometry with nondenaturing chromatography
    • Johnson, P., Philo, M., Watson, A., Mills, E. N. C., Rapid fingerprinting of milk thermal processing history by intact protein mass spectrometry with nondenaturing chromatography. J. Agric. Food Chem. 2011, 59, 12420-12427.
    • (2011) J. Agric. Food Chem. , vol.59 , pp. 12420-12427
    • Johnson, P.1    Philo, M.2    Watson, A.3    Mills, E.N.C.4
  • 69
    • 0029562744 scopus 로고
    • Anaphylactic reaction caused by neoallergens in heated pecan nut
    • Malanin, K., Lundberg, M., Johansson, S. G. O., Anaphylactic reaction caused by neoallergens in heated pecan nut. Allergy 1995, 50, 988-991.
    • (1995) Allergy , vol.50 , pp. 988-991
    • Malanin, K.1    Lundberg, M.2    Johansson, S.G.O.3
  • 70
    • 2942556579 scopus 로고    scopus 로고
    • Maillard reaction and enzymatic browning affect the allergenicity of Pru av 1, the major allergen from cherry (Prunus avium)
    • Gruber, P., Vieths, S., Wangorsch, A., Nerkamp, J. et al., Maillard reaction and enzymatic browning affect the allergenicity of Pru av 1, the major allergen from cherry (Prunus avium). J. Agric. Food Chem. 2004, 52, 4002-4007.
    • (2004) J. Agric. Food Chem. , vol.52 , pp. 4002-4007
    • Gruber, P.1    Vieths, S.2    Wangorsch, A.3    Nerkamp, J.4
  • 72
    • 82955161705 scopus 로고    scopus 로고
    • Boiling peanut Ara h 1 results in the formation of aggregates with reduced allergenicity
    • Blanc, F., Vissers, Y. M., Adel-Patient, K., Rigby, N. M. et al., Boiling peanut Ara h 1 results in the formation of aggregates with reduced allergenicity. Mol. Nutr. Food Res. 2011, 55, 1887-1894.
    • (2011) Mol. Nutr. Food Res. , vol.55 , pp. 1887-1894
    • Blanc, F.1    Vissers, Y.M.2    Adel-Patient, K.3    Rigby, N.M.4
  • 73
    • 84858720802 scopus 로고    scopus 로고
    • Impact of thermal processing and the Maillard reaction on the basophil activation of hazelnut allergic patients
    • Cucu, T., Meulenaer, B. de, Bridts, C., Devreese, B. et al., Impact of thermal processing and the Maillard reaction on the basophil activation of hazelnut allergic patients. Food Chem. Toxicol. 2012, 50, 1722-1728.
    • (2012) Food Chem. Toxicol. , vol.50 , pp. 1722-1728
    • Cucu, T.1    Meulenaer de, B.2    Bridts, C.3    Devreese, B.4
  • 74
    • 73149101622 scopus 로고    scopus 로고
    • Glycation of a food allergen by the Maillard reaction enhances its T-cell immunogenicity: role of macrophage scavenger receptor class A type I and II
    • e11.
    • Ilchmann, A., Burgdorf, S., Scheurer, S., Waibler, Z. et al., Glycation of a food allergen by the Maillard reaction enhances its T-cell immunogenicity: role of macrophage scavenger receptor class A type I and II. J. Allergy Clin. Immunol. 2010, 125, 175-183.e11.
    • (2010) J. Allergy Clin. Immunol. , vol.125 , pp. 175-183
    • Ilchmann, A.1    Burgdorf, S.2    Scheurer, S.3    Waibler, Z.4
  • 75
    • 78649854606 scopus 로고    scopus 로고
    • High pressure, thermal and pulsed electric-field-induced structural changes in selected food allergens
    • Johnson, P. E., van der Plancken, I., Balasa, A., Husband, F. A. et al., High pressure, thermal and pulsed electric-field-induced structural changes in selected food allergens. Mol. Nutr. Food Res. 2010, 54, 1701-1710.
    • (2010) Mol. Nutr. Food Res. , vol.54 , pp. 1701-1710
    • Johnson, P.E.1    van der Plancken, I.2    Balasa, A.3    Husband, F.A.4
  • 76
    • 79953703693 scopus 로고    scopus 로고
    • High-pressure microfluidisation-induced changes in the antigenicity and conformation of allergen Ara h 2 purified from Chinese peanut
    • Hu, C.-Q., Chen, H.-B., Gao, J.-Y., Luo, C.-P. et al., High-pressure microfluidisation-induced changes in the antigenicity and conformation of allergen Ara h 2 purified from Chinese peanut. J. Sci. Food Agric. 2011, 91, 1304-1309.
    • (2011) J. Sci. Food Agric. , vol.91 , pp. 1304-1309
    • Hu, C.-Q.1    Chen, H.-B.2    Gao, J.-Y.3    Luo, C.-P.4


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