메뉴 건너뛰기




Volumn 62, Issue 29, 2014, Pages 7010-7021

Novel strategy to create hypoallergenic peanut protein-polyphenol edible matrices for oral immunotherapy

Author keywords

basophil; cranberry; mouse model; peanut allergy; polyphenols

Indexed keywords

ALLERGENS; ALLERGIES; EPITOPES; FOURIER TRANSFORM INFRARED SPECTROSCOPY; MAMMALS; PROTEINS;

EID: 84905588654     PISSN: 00218561     EISSN: 15205118     Source Type: Journal    
DOI: 10.1021/jf405773b     Document Type: Article
Times cited : (57)

References (69)
  • 2
    • 38149119534 scopus 로고    scopus 로고
    • Analysis of food-allergic and anaphylactic events in the National Electronic Injury Surveillance System
    • Ross, M. P.; Ferguson, M.; Street, D.; Klontz, K.; Schroeder, T.; Luccioli, S. Analysis of food-allergic and anaphylactic events in the National Electronic Injury Surveillance System J. Allergy Clin. Immunol. 2008, 121, 166-171
    • (2008) J. Allergy Clin. Immunol. , vol.121 , pp. 166-171
    • Ross, M.P.1    Ferguson, M.2    Street, D.3    Klontz, K.4    Schroeder, T.5    Luccioli, S.6
  • 5
    • 34047122018 scopus 로고    scopus 로고
    • Further fatalities caused by anaphylactic reactions to food, 2001-2006
    • Bock, S. A.; Muñoz-Furlong, A.; Sampson, H. A. Further fatalities caused by anaphylactic reactions to food, 2001-2006 J. Allergy Clin. Immunol. 2007, 119, 1016-1018
    • (2007) J. Allergy Clin. Immunol. , vol.119 , pp. 1016-1018
    • Bock, S.A.1    Muñoz-Furlong, A.2    Sampson, H.A.3
  • 7
    • 43049150812 scopus 로고    scopus 로고
    • Peanut allergy
    • Burks, A. W. Peanut allergy Lancet 2008, 371, 1538-1546
    • (2008) Lancet , vol.371 , pp. 1538-1546
    • Burks, A.W.1
  • 9
    • 77952744759 scopus 로고    scopus 로고
    • US prevalence of self-reported peanut, tree nut, and sesame allergy: 11-year follow-up
    • Sicherer, S. H.; Muñoz-Furlong, A.; Godbold, J. H.; Sampson, H. A. US prevalence of self-reported peanut, tree nut, and sesame allergy: 11-year follow-up J. Allergy Clin. Immunol. 2010, 125, 1322-1326
    • (2010) J. Allergy Clin. Immunol. , vol.125 , pp. 1322-1326
    • Sicherer, S.H.1    Muñoz-Furlong, A.2    Godbold, J.H.3    Sampson, H.A.4
  • 13
    • 36148935581 scopus 로고    scopus 로고
    • Phenolics from walnut (Juglans regia L.) kernels: Antioxidant activity and interactions with proteins
    • Labuckas, D. O.; Maestri, D. M.; Perelló, M.; Martínez, M. L.; Lamarque, A. L. Phenolics from walnut (Juglans regia L.) kernels: antioxidant activity and interactions with proteins Food Chem. 2008, 107, 607-612
    • (2008) Food Chem. , vol.107 , pp. 607-612
    • Labuckas, D.O.1    Maestri, D.M.2    Perelló, M.3    Martínez, M.L.4    Lamarque, A.L.5
  • 14
    • 43649106465 scopus 로고    scopus 로고
    • The antioxidant capacity of red wine in relationship with its polyphenolic constituents
    • Majo, D. D.; La Guardia, M.; Giammanco, S.; La Neve, L.; Giammanco, M. The antioxidant capacity of red wine in relationship with its polyphenolic constituents Food Chem. 2008, 111, 45-49
    • (2008) Food Chem. , vol.111 , pp. 45-49
    • Majo, D.D.1    La Guardia, M.2    Giammanco, S.3    La Neve, L.4    Giammanco, M.5
  • 15
    • 80052971352 scopus 로고    scopus 로고
    • Dietary polyphenols in the prevention and treatment of allergic diseases
    • Singh, A.; Holvoet, S.; Mercenier, A. Dietary polyphenols in the prevention and treatment of allergic diseases Clin. Exp. Allergy 2011, 41, 1346-1359
    • (2011) Clin. Exp. Allergy , vol.41 , pp. 1346-1359
    • Singh, A.1    Holvoet, S.2    Mercenier, A.3
  • 16
    • 1542380558 scopus 로고    scopus 로고
    • Characterization of protein-polyphenol interactions
    • Papadopoulou, A.; Frazier, R. A. Characterization of protein-polyphenol interactions Trends Food Sci. Technol. 2004, 15, 186-190
    • (2004) Trends Food Sci. Technol. , vol.15 , pp. 186-190
    • Papadopoulou, A.1    Frazier, R.A.2
  • 18
    • 0032967327 scopus 로고    scopus 로고
    • Effects of protein-polyphenol interactions on beverage haze, stabilization, and analysis
    • Siebert, K. J. Effects of protein-polyphenol interactions on beverage haze, stabilization, and analysis J. Agric. Food Chem. 1999, 47, 353-362
    • (1999) J. Agric. Food Chem. , vol.47 , pp. 353-362
    • Siebert, K.J.1
  • 19
    • 29844432563 scopus 로고    scopus 로고
    • Polyphenol oxidase/caffeic acid may reduce the allergenic properties of peanut allergens
    • Chung, S. Y.; Kato, Y.; Champagne, E. T. Polyphenol oxidase/caffeic acid may reduce the allergenic properties of peanut allergens J. Sci. Food Agric 2005, 85, 2631-2637
    • (2005) J. Sci. Food Agric , vol.85 , pp. 2631-2637
    • Chung, S.Y.1    Kato, Y.2    Champagne, E.T.3
  • 20
    • 36148968860 scopus 로고    scopus 로고
    • Effects of phytic acid on peanut allergens and allergenic properties of extracts
    • Chung, S. Y.; Champagne, E. T. Effects of phytic acid on peanut allergens and allergenic properties of extracts J. Agric. Food Chem. 2007, 55, 9054-9058
    • (2007) J. Agric. Food Chem. , vol.55 , pp. 9054-9058
    • Chung, S.Y.1    Champagne, E.T.2
  • 21
    • 80051930409 scopus 로고    scopus 로고
    • Using phenolic compounds to reduce the allergenic properties of peanut extracts and peanut butter slurries
    • Chung, S. Y.; Champagne, E. T. Using phenolic compounds to reduce the allergenic properties of peanut extracts and peanut butter slurries J. Allergy Clin. Immunol. 2008, 121, S249
    • (2008) J. Allergy Clin. Immunol. , vol.121 , pp. 249
    • Chung, S.Y.1    Champagne, E.T.2
  • 22
    • 84861095266 scopus 로고    scopus 로고
    • Removing peanut allergens by tannic acid
    • Chung, S. Y.; Reed, S. Removing peanut allergens by tannic acid Food Chem. 2012, 134, 1468-1473
    • (2012) Food Chem. , vol.134 , pp. 1468-1473
    • Chung, S.Y.1    Reed, S.2
  • 23
    • 84865310823 scopus 로고    scopus 로고
    • In vivo and in vitro antidiabetic effects of aqueous cinnamon extract and cinnamon polyphenol-enhanced food matrix
    • Cheng, D. M.; Kuhn, P.; Poulev, A.; Rojo, L. E.; Lila, M. A.; Raskin, I. In vivo and in vitro antidiabetic effects of aqueous cinnamon extract and cinnamon polyphenol-enhanced food matrix Food Chem. 2012, 135, 2994-3002
    • (2012) Food Chem. , vol.135 , pp. 2994-3002
    • Cheng, D.M.1    Kuhn, P.2    Poulev, A.3    Rojo, L.E.4    Lila, M.A.5    Raskin, I.6
  • 24
    • 84880133164 scopus 로고    scopus 로고
    • Bioactive polyphenols from muscadine grape and blackcurrant stably concentrated onto protein-rich matrices for topical applications
    • Plundrich, N.; Grace, M. H.; Raskin, I.; Lila, M. A. Bioactive polyphenols from muscadine grape and blackcurrant stably concentrated onto protein-rich matrices for topical applications Int. J. Cosmetic Sci. 2013, 35, 394-401
    • (2013) Int. J. Cosmetic Sci. , vol.35 , pp. 394-401
    • Plundrich, N.1    Grace, M.H.2    Raskin, I.3    Lila, M.A.4
  • 25
    • 84866382224 scopus 로고    scopus 로고
    • Biochemical analysis and in vivo hypoglycemic activity of grape polyphenol-soybean flour complex
    • Roopchand, D. E.; Kuhn, P.; Poulev, A.; Oren, A.; Lila, M. A.; Raskin, I. Biochemical analysis and in vivo hypoglycemic activity of grape polyphenol-soybean flour complex J. Agric. Food Chem. 2012, 60, 8860-8865
    • (2012) J. Agric. Food Chem. , vol.60 , pp. 8860-8865
    • Roopchand, D.E.1    Kuhn, P.2    Poulev, A.3    Oren, A.4    Lila, M.A.5    Raskin, I.6
  • 28
    • 84864018538 scopus 로고    scopus 로고
    • High-throughput micro plate assays for screening flavonoid content and DPPH-scavenging activity in sorghum bran and flour
    • Herald, T. J.; Gadgil, P.; Tilley, M. High-throughput micro plate assays for screening flavonoid content and DPPH-scavenging activity in sorghum bran and flour J. Sci. Food Agric. 2012, 92, 2326-2331
    • (2012) J. Sci. Food Agric. , vol.92 , pp. 2326-2331
    • Herald, T.J.1    Gadgil, P.2    Tilley, M.3
  • 29
    • 77957124607 scopus 로고    scopus 로고
    • Evaluation of parameters that affect the 4-dimethylaminocinnamaldehyde assay for flavanols and proanthocyanidins
    • Wallace, T. C.; Giusti, M. M. Evaluation of parameters that affect the 4-dimethylaminocinnamaldehyde assay for flavanols and proanthocyanidins J. Food Sci. 2010, 75, C619-C625
    • (2010) J. Food Sci. , vol.75
    • Wallace, T.C.1    Giusti, M.M.2
  • 30
    • 64449085329 scopus 로고    scopus 로고
    • Hypoglycemic activity of a novel anthocyanin-rich formulation from lowbush blueberry, Vaccinium angustifolium Aiton
    • Grace, M. H.; Ribnicky, D. M.; Kuhn, P.; Poulev, A.; Logendra, S.; Yousef, G. G.; Raskin, I.; Lila, M. A. Hypoglycemic activity of a novel anthocyanin-rich formulation from lowbush blueberry, Vaccinium angustifolium Aiton Phytomedicine 2009, 16, 406-415
    • (2009) Phytomedicine , vol.16 , pp. 406-415
    • Grace, M.H.1    Ribnicky, D.M.2    Kuhn, P.3    Poulev, A.4    Logendra, S.5    Yousef, G.G.6    Raskin, I.7    Lila, M.A.8
  • 32
    • 0037077372 scopus 로고    scopus 로고
    • Fractionation of polymeric procyanidins from lowbush blueberry and quantification of procyanidins in selected foods with an optimized normal-phase HPLC-MS fluorescent detection method
    • Gu, L.; Kelm, M.; Hammerstone, J. F.; Beecher, G.; Cunningham, D.; Vannozzi, S.; Prior, R. L. Fractionation of polymeric procyanidins from lowbush blueberry and quantification of procyanidins in selected foods with an optimized normal-phase HPLC-MS fluorescent detection method J. Agric. Food Chem. 2002, 50, 4852-4860
    • (2002) J. Agric. Food Chem. , vol.50 , pp. 4852-4860
    • Gu, L.1    Kelm, M.2    Hammerstone, J.F.3    Beecher, G.4    Cunningham, D.5    Vannozzi, S.6    Prior, R.L.7
  • 33
    • 0033004275 scopus 로고    scopus 로고
    • Identification of procyanidins in cocoa (Theobroma cacao) and chocolate using high-performance liquid chromatography/mass spectrometry
    • Hammerstone, J. F.; Lazarus, S. A.; Mitchell, A. E.; Rucker, R.; Schmitz, H. H. Identification of procyanidins in cocoa (Theobroma cacao) and chocolate using high-performance liquid chromatography/mass spectrometry J. Agric. Food Chem. 1999, 47, 490-496
    • (1999) J. Agric. Food Chem. , vol.47 , pp. 490-496
    • Hammerstone, J.F.1    Lazarus, S.A.2    Mitchell, A.E.3    Rucker, R.4    Schmitz, H.H.5
  • 34
    • 84868124505 scopus 로고    scopus 로고
    • Value-added processing of peanut skins: Antioxidant capacity, total phenolics, and procyanidin content of spray-dried extracts
    • Constanza, K. E.; White, B. L.; Davis, J. P.; Sanders, T. H.; Dean, L. L. Value-added processing of peanut skins: antioxidant capacity, total phenolics, and procyanidin content of spray-dried extracts J. Agric. Food Chem. 2012, 60, 10776-10783
    • (2012) J. Agric. Food Chem. , vol.60 , pp. 10776-10783
    • Constanza, K.E.1    White, B.L.2    Davis, J.P.3    Sanders, T.H.4    Dean, L.L.5
  • 36
    • 84926662026 scopus 로고    scopus 로고
    • Simulated gastric fluid and simulated intestinal fluid, The National Formulary 18; U.S. Pharmacopeial Convention: Rockville, MD, USA
    • U.S. Pharmacopeia 23, Simulated gastric fluid and simulated intestinal fluid, The National Formulary 18; U.S. Pharmacopeial Convention: Rockville, MD, USA, 2006; 3171 pp.
    • (2006) U.S. Pharmacopeia 23 , pp. 3171
  • 38
    • 34447634492 scopus 로고    scopus 로고
    • Antibacterial properties and major bioactive components of cinnamon stick (Cinnamomum burmannii): Activity against foodborne pathogenic bacteria
    • Shan, B.; Cai, Y. Z.; Brooks, J. D.; Corke, H. Antibacterial properties and major bioactive components of cinnamon stick (Cinnamomum burmannii): activity against foodborne pathogenic bacteria J. Agric. Food Chem. 2007, 55, 5484-5490
    • (2007) J. Agric. Food Chem. , vol.55 , pp. 5484-5490
    • Shan, B.1    Cai, Y.Z.2    Brooks, J.D.3    Corke, H.4
  • 39
    • 34447515810 scopus 로고    scopus 로고
    • Cranberry and blueberry: Evidence for protective effects against cancer and vascular diseases
    • Neto, C. C. Cranberry and blueberry: evidence for protective effects against cancer and vascular diseases Mol. Nutr. Food Res. 2007, 51, 652-664
    • (2007) Mol. Nutr. Food Res. , vol.51 , pp. 652-664
    • Neto, C.C.1
  • 40
    • 33947574075 scopus 로고    scopus 로고
    • Green tea proanthocyanidins inhibit cyclooxygenase-2 expression in LPS-activated mouse macrophages: Molecular mechanisms and structure-activity relationship
    • Hou, D. X.; Masuzaki, S.; Hashimoto, F.; Uto, T.; Tanigawa, S.; Fujii, M.; Sakata, Y. Green tea proanthocyanidins inhibit cyclooxygenase-2 expression in LPS-activated mouse macrophages: molecular mechanisms and structure-activity relationship Arch. Biochem. Biophys. 2007, 460, 67-74
    • (2007) Arch. Biochem. Biophys. , vol.460 , pp. 67-74
    • Hou, D.X.1    Masuzaki, S.2    Hashimoto, F.3    Uto, T.4    Tanigawa, S.5    Fujii, M.6    Sakata, Y.7
  • 41
    • 29144534046 scopus 로고    scopus 로고
    • Aronia melanocarpa phenolics and their antioxidant activity
    • Oszmianski, J.; Wojdylo, A. Aronia melanocarpa phenolics and their antioxidant activity Eur. Food Res. Technol. 2005, 221, 809-813
    • (2005) Eur. Food Res. Technol. , vol.221 , pp. 809-813
    • Oszmianski, J.1    Wojdylo, A.2
  • 42
    • 0017787237 scopus 로고
    • Flavonoid glycosides and hydroxycinnamic acid esters of blackcurrants (Ribes nigrum). Phenolics of fruits 9
    • Koeppen, B. H.; Herrmann, K. Flavonoid glycosides and hydroxycinnamic acid esters of blackcurrants (Ribes nigrum). Phenolics of fruits 9 Z. Lebensm. Unters. Forsch. 1977, 164, 263-268
    • (1977) Z. Lebensm. Unters. Forsch. , vol.164 , pp. 263-268
    • Koeppen, B.H.1    Herrmann, K.2
  • 44
    • 11144234817 scopus 로고    scopus 로고
    • Characterization of anthocyanins and proanthocyanidins in some cultivars of Ribes, Aronia, and Sambucus and their antioxidant capacity
    • Wu, X.; Gu, L.; Prior, R. L.; McKay, S. Characterization of anthocyanins and proanthocyanidins in some cultivars of Ribes, Aronia, and Sambucus and their antioxidant capacity J. Agric. Food Chem. 2004, 52, 7846-7856
    • (2004) J. Agric. Food Chem. , vol.52 , pp. 7846-7856
    • Wu, X.1    Gu, L.2    Prior, R.L.3    McKay, S.4
  • 45
  • 47
    • 0030515619 scopus 로고    scopus 로고
    • Natural polyphenols (vegetable tannins) as drugs: Possible modes of action
    • Haslam, E. Natural polyphenols (vegetable tannins) as drugs: possible modes of action J. Nat. Prod. 1996, 59, 205-215
    • (1996) J. Nat. Prod. , vol.59 , pp. 205-215
    • Haslam, E.1
  • 49
    • 69149090077 scopus 로고    scopus 로고
    • Effects of food processing on food allergens
    • Sathe, S. K.; Sharma, G. M. Effects of food processing on food allergens Mol. Nutr. Food Res. 2009, 53, 970-978
    • (2009) Mol. Nutr. Food Res. , vol.53 , pp. 970-978
    • Sathe, S.K.1    Sharma, G.M.2
  • 50
    • 0026045826 scopus 로고
    • Identification of a major peanut allergen, Ara h I, in patients with atopic dermatitis and positive peanut challenges
    • Burks, A. W.; Williams, L. W.; Helm, R. M.; Connaughton, C.; Cockrell, G.; O'Brien, T. Identification of a major peanut allergen, Ara h I, in patients with atopic dermatitis and positive peanut challenges J. Allergy Clin. Immunol. 1991, 88, 172-179
    • (1991) J. Allergy Clin. Immunol. , vol.88 , pp. 172-179
    • Burks, A.W.1    Williams, L.W.2    Helm, R.M.3    Connaughton, C.4    Cockrell, G.5    O'Brien, T.6
  • 51
    • 2042449746 scopus 로고    scopus 로고
    • Relevance of Ara h1, Ara h2 and Ara h3 in peanut-allergic patients, as determined by immunoglobulin 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 immunoglobulin 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
  • 52
    • 17744371487 scopus 로고    scopus 로고
    • Purification and immunoglobulin E-binding properties of peanut allergen Ara h 6: Evidence for cross-reactivity with Ara h 2
    • Koppelman, S. J.; de Jong, G. A.; Laaper-Ertmann, M.; Peeters, K. A.; Knulst, A. C.; Hefle, S. L.; Knol, E. F. Purification and immunoglobulin E-binding properties of peanut allergen Ara h 6: evidence for cross-reactivity with Ara h 2 Clin. Exp. Allergy 2005, 35, 490-497
    • (2005) Clin. Exp. Allergy , vol.35 , pp. 490-497
    • Koppelman, S.J.1    De Jong, G.A.2    Laaper-Ertmann, M.3    Peeters, K.A.4    Knulst, A.C.5    Hefle, S.L.6    Knol, E.F.7
  • 56
    • 34548165708 scopus 로고    scopus 로고
    • Infrared spectroscopy of proteins
    • Barth, A. Infrared spectroscopy of proteins Biochim. Biophys. Acta 2007, 1767, 1073-1101
    • (2007) Biochim. Biophys. Acta , vol.1767 , pp. 1073-1101
    • Barth, A.1
  • 57
    • 34548094323 scopus 로고    scopus 로고
    • Fourier transform infrared spectroscopic analysis of protein secondary structures
    • Kong, J.; Yu, S. Fourier transform infrared spectroscopic analysis of protein secondary structures Acta Biochim. Biophys. Sinica 2007, 39, 549-559
    • (2007) Acta Biochim. Biophys. Sinica , vol.39 , pp. 549-559
    • Kong, J.1    Yu, S.2
  • 58
    • 0042061110 scopus 로고    scopus 로고
    • Effects of non-covalent interactions with 5- O -caffeoylquinic acid (chlorogenic acid) on the heat denaturation and solubility of globular proteins
    • Prigent, S. V. E.; Gruppen, H.; Visser, A.; van Koningsveld, G. A.; de Jong, G. A. H.; Voragen, A. G. J. Effects of non-covalent interactions with 5- O -caffeoylquinic acid (chlorogenic acid) on the heat denaturation and solubility of globular proteins J. Agric. Food Chem. 2003, 51, 5088-5095
    • (2003) J. Agric. Food Chem. , vol.51 , pp. 5088-5095
    • Prigent, S.V.E.1    Gruppen, H.2    Visser, A.3    Van Koningsveld, G.A.4    De Jong, G.A.H.5    Voragen, A.G.J.6
  • 59
    • 48549112829 scopus 로고
    • Haemanalysis: The relative astringency of proanthocyanidin polymers
    • Porter, L. J.; Woodruffe, J. Haemanalysis: the relative astringency of proanthocyanidin polymers Phytochemistry 1984, 23, 1255-1256
    • (1984) Phytochemistry , vol.23 , pp. 1255-1256
    • Porter, L.J.1    Woodruffe, J.2
  • 60
    • 78649887557 scopus 로고    scopus 로고
    • Digestion of peanut allergens Ara h 1, Ara h 2, Ara h 3, and Ara h 6: A comparative in vitro study and partial characterization of digestion-resistent peptides
    • Koppelman, S. J.; Hefle, S. L.; Taylor, S. L.; de Jong, G. A. H. Digestion of peanut allergens Ara h 1, Ara h 2, Ara h 3, and Ara h 6: a comparative in vitro study and partial characterization of digestion-resistent peptides Mol. Nutr. Food Res. 2010, 54, 1711-1721
    • (2010) Mol. Nutr. Food Res. , vol.54 , pp. 1711-1721
    • Koppelman, S.J.1    Hefle, S.L.2    Taylor, S.L.3    De Jong, G.A.H.4
  • 61
    • 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.; Burks, A. W.; Bannon, G. A. 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    Burks, A.W.5    Bannon, G.A.6
  • 62
    • 33646249121 scopus 로고    scopus 로고
    • Structure and stability of 2S albumin-type peanut allergens: Implications for the severity of peanut allergic reactions
    • Lehmann, K.; Schweimer, K.; Reese, G.; Randow, S.; Suhr, M.; Becker, W. M.; Vieths, S.; Rosch, P. Structure and stability of 2S albumin-type peanut allergens: 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    Suhr, M.5    Becker, W.M.6    Vieths, S.7    Rosch, P.8
  • 63
    • 0034120710 scopus 로고    scopus 로고
    • Structure of the major peanut allergen Ara h 1 may protect IgE-binding epitopes from degradation
    • Maleki, S. J.; Kopper, R. A.; Shin, D. S.; Park, C. W.; Compadre, C. M.; Sampson, H.; Bannon, G. A. Structure of the major peanut allergen Ara h 1 may protect IgE-binding epitopes from degradation J. Immunol. 2000, 164, 5844-5849
    • (2000) J. Immunol. , vol.164 , pp. 5844-5849
    • Maleki, S.J.1    Kopper, R.A.2    Shin, D.S.3    Park, C.W.4    Compadre, C.M.5    Sampson, H.6    Bannon, G.A.7
  • 64
    • 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.; Burks, A. W.; Bannon, G. A. 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    Burks, A.W.5    Bannon, G.A.6
  • 66
    • 0038004633 scopus 로고    scopus 로고
    • Persistent protective effect of heat-killed Escherichia coli producing "engineered", recombinant peanut proteins in a murine model of peanut allergy
    • Li, X. M.; Srivastava, K.; Grishin, A.; Huang, C. K.; Schofield, B.; Burks, W.; Sampson, H. A. Persistent protective effect of heat-killed Escherichia coli producing "engineered", recombinant peanut proteins in a murine model of peanut allergy J. Allergy Clin. Immunol. 2003, 112, 159-167
    • (2003) J. Allergy Clin. Immunol. , vol.112 , pp. 159-167
    • Li, X.M.1    Srivastava, K.2    Grishin, A.3    Huang, C.K.4    Schofield, B.5    Burks, W.6    Sampson, H.A.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.