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1
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34548297579
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The prevalence of food allergy: A metaanalysis
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An analysis of published epidemiology studies this gives in indication of the major foods implicated in food allergy in unselected populations
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Rona RJ, Keil T, Summers C, et al. The prevalence of food allergy: a metaanalysis. J Allergy Clin Immunol 2007; 120:638-646. An analysis of published epidemiology studies this gives in indication of the major foods implicated in food allergy in unselected populations.
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(2007)
J Allergy Clin Immunol
, vol.120
, pp. 638-646
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Rona, R.J.1
Keil, T.2
Summers, C.3
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3
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0242552764
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Presentation of allergen in different food preparations affects the nature of the allergic reaction: A case series
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Grimshaw KEC, King RM, Nordlee JA, et al. Presentation of allergen in different food preparations affects the nature of the allergic reaction: a case series. Clin Exp Allergy 2003; 33:1581-1585.
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(2003)
Clin Exp Allergy
, vol.33
, pp. 1581-1585
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Grimshaw, K.E.C.1
King, R.M.2
Nordlee, J.A.3
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4
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0001930144
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Molecular dissection of protein antigens
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Van Regenmortel MHV, editor, Florida: CRC Press Inc;
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Van Regenmortel MHV. Molecular dissection of protein antigens. In: Van Regenmortel MHV, editor. Structure of Antigens Vol 1 Florida: CRC Press Inc; 1992, pp. 1-28.
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(1992)
Structure of Antigens
, vol.1
, pp. 1-28
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Van Regenmortel, M.H.V.1
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5
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34548285780
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Wijesinha-Bettoni R, Gao C, Jenkins JA, et al. Heat treatment of bovine alphalactalbumin results in partially folded, disulfide bond shuffled states with enhanced surface activity. Biochemistry 2007; 46:9774-9784. Shows that thermal denaturation results in the formation of partially unfolded alphalactalbumin, retaining much of its native secondary structure but with increased polypeptide mobility. The modified forms are stabilized by rearranged disulphide bonds.
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Wijesinha-Bettoni R, Gao C, Jenkins JA, et al. Heat treatment of bovine alphalactalbumin results in partially folded, disulfide bond shuffled states with enhanced surface activity. Biochemistry 2007; 46:9774-9784. Shows that thermal denaturation results in the formation of partially unfolded alphalactalbumin, retaining much of its native secondary structure but with increased polypeptide mobility. The modified forms are stabilized by rearranged disulphide bonds.
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6
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0030471602
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X-ray and NMR structure of Bet v 1, the origin of birch pollen allergy
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Gajhede M, Osmark P, Poulsen FM, et al. X-ray and NMR structure of Bet v 1, the origin of birch pollen allergy. Nature Struct Biol 1996; 3:1040- 1045.
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(1996)
Nature Struct Biol
, vol.3
, pp. 1040-1045
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Gajhede, M.1
Osmark, P.2
Poulsen, F.M.3
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7
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0035933875
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Allergic cross-reactivity made visible: Solution structure of the major cherry allergen Pru av 1
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Neudecker P, Schweimer K, Nerkamp J, et al. Allergic cross-reactivity made visible: solution structure of the major cherry allergen Pru av 1. J Biol Chem 2001; 276:22756-22763.
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(2001)
J Biol Chem
, vol.276
, pp. 22756-22763
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Neudecker, P.1
Schweimer, K.2
Nerkamp, J.3
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9
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0036196769
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Influence of food processing on the allergenicity of celery: DBPCFC with celery spice and cooked celery in patients with celery allergy
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Ballmer-Weber BK, Hoffmann A, Wü thrich B, et al. Influence of food processing on the allergenicity of celery: DBPCFC with celery spice and cooked celery in patients with celery allergy. Allergy 2002; 57:228- 235.
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(2002)
Allergy
, vol.57
, pp. 228-235
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Ballmer-Weber, B.K.1
Hoffmann, A.2
Wü thrich, B.3
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10
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33947359861
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Mogensen JE, Ferreras M, Wimmer R, et al. The major allergen from birch tree pollen, Bet v 1, binds and permeabilizes membranes. Biochemistry 2007; 46:3356-3365. This is an excellent paper describing the molecular properties of Bet v 1 in terms of its membrane activity. It brings considerable insight into the potential behaviour and role of this important protein in plants.
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Mogensen JE, Ferreras M, Wimmer R, et al. The major allergen from birch tree pollen, Bet v 1, binds and permeabilizes membranes. Biochemistry 2007; 46:3356-3365. This is an excellent paper describing the molecular properties of Bet v 1 in terms of its membrane activity. It brings considerable insight into the potential behaviour and role of this important protein in plants.
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11
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11344255717
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Structural relatedness of plant food allergens with specifc reference to cross-reactive allergens: An in silico analysis
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Jenkins JA, Griffith-Jones S, Shewry PR, et al. Structural relatedness of plant food allergens with specifc reference to cross-reactive allergens: an in silico analysis. J Allergy Clin Immunol 2005; 115:163-170.
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(2005)
J Allergy Clin Immunol
, vol.115
, pp. 163-170
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Jenkins, J.A.1
Griffith-Jones, S.2
Shewry, P.R.3
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12
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24744433515
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Mills ENC The effect of thermal processing on the IgE reactivity of the nonspecific lipid transfer protein from apple. Mal d 3
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Sancho AI, Rigby NM, Zuidmeer L, et al. Mills ENC The effect of thermal processing on the IgE reactivity of the nonspecific lipid transfer protein from apple. Mal d 3. Allergy 2005; 60:1262-1268.
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(2005)
Allergy
, vol.60
, pp. 1262-1268
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Sancho, A.I.1
Rigby, N.M.2
Zuidmeer, L.3
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13
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15844419406
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Wine anaphylaxis in a German patient: IgEmediated allergy against a lipid transfer protein of grapes
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Schad SG, Trcka J, Vieths S, et al. Wine anaphylaxis in a German patient: IgEmediated allergy against a lipid transfer protein of grapes. Int Arch Allergy Immunol 2005; 136:159-164.
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(2005)
Int Arch Allergy Immunol
, vol.136
, pp. 159-164
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Schad, S.G.1
Trcka, J.2
Vieths, S.3
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14
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34247258971
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Rice: Another potential cause of food allergy in patients sensitized to lipid transfer protein
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This paper describes individuals with the LTP allergy syndrome suffering from associated allergic reactions to rice and includes an assessment of effects of cooking
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Asero R, Amato S, Alfieri B, et al. Rice: another potential cause of food allergy in patients sensitized to lipid transfer protein. Int Arch Allergy Immunol 2007; 143:69-74. This paper describes individuals with the LTP allergy syndrome suffering from associated allergic reactions to rice and includes an assessment of effects of cooking.
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(2007)
Int Arch Allergy Immunol
, vol.143
, pp. 69-74
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Asero, R.1
Amato, S.2
Alfieri, B.3
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15
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20744450734
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Influence of thermal processing on the allergenicity of peanut proteins
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Mondoulet L, Paty E, Drumare MF, et al. Influence of thermal processing on the allergenicity of peanut proteins. J Agric Food Chem 2005; 53:4547- 4553.
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(2005)
J Agric Food Chem
, vol.53
, pp. 4547-4553
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Mondoulet, L.1
Paty, E.2
Drumare, M.F.3
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16
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34547755941
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Pastorello EA, Farioli L, Conti A, et al. Wheat IgE-mediated food allergy in European patients: alpha-amylase inhibitors, lipid transfer proteins and lowmolecular- weight glutenins. Allergenic molecules recognized by double-blind, placebo-controlled food challenge. Int Arch Allergy Immunol 2007; 144:10- 22. This article brings together detailed study of both clinical and biochemical work in a way that is much needed if the relevance of processing effects on allergenicity are to be understood and support better patient management. It uses a group of well defined allergic patients coupled with proteomic analysis of cereal allergens.
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Pastorello EA, Farioli L, Conti A, et al. Wheat IgE-mediated food allergy in European patients: alpha-amylase inhibitors, lipid transfer proteins and lowmolecular- weight glutenins. Allergenic molecules recognized by double-blind, placebo-controlled food challenge. Int Arch Allergy Immunol 2007; 144:10- 22. This article brings together detailed study of both clinical and biochemical work in a way that is much needed if the relevance of processing effects on allergenicity are to be understood and support better patient management. It uses a group of well defined allergic patients coupled with proteomic analysis of cereal allergens.
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17
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33646508515
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Stability of barley and malt lipid transfer protein 1 (LTP1) toward heating and reducing agents; relationship with the brewing process
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Perrocheau L, Bakan B, Poivin P, Marion D. Stability of barley and malt lipid transfer protein 1 (LTP1) toward heating and reducing agents; relationship with the brewing process. J Agric Food Chem 2006; 54:3108-3113.
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(2006)
J Agric Food Chem
, vol.54
, pp. 3108-3113
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Perrocheau, L.1
Bakan, B.2
Poivin, P.3
Marion, D.4
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18
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34548667473
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Posttranslational modification of barley LTP1b: The lipid adduct lies in the hydrophobic cavity and alters the protein dynamics
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Wijesinha-Bettoni R, Gao C, Jenkins JA, et al. Posttranslational modification of barley LTP1b: the lipid adduct lies in the hydrophobic cavity and alters the protein dynamics. FEBS Lett 2007; 581:4557-4561.
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(2007)
FEBS Lett
, vol.581
, pp. 4557-4561
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Wijesinha-Bettoni, R.1
Gao, C.2
Jenkins, J.A.3
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19
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35649013814
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Wheat lipid transfer protein is a major allergen associated with baker's asthma
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Palacin A, Quirce S, Armentia A, et al. Wheat lipid transfer protein is a major allergen associated with baker's asthma. J Allergy Clin Immunol 2007; 120:1132-1138.
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(2007)
J Allergy Clin Immunol
, vol.120
, pp. 1132-1138
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Palacin, A.1
Quirce, S.2
Armentia, A.3
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20
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34047227335
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Transglutaminase polymerization of peanut proteins
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Clare DA, Gharst G, Sanders TH. Transglutaminase polymerization of peanut proteins. J Agric Food Chem 2007; 55:432-438.
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(2007)
J Agric Food Chem
, vol.55
, pp. 432-438
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Clare, D.A.1
Gharst, G.2
Sanders, T.H.3
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21
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0037841653
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Transglutaminase- mediated crosslinking of a peptic fraction of omega-5 gliadin enhances IgE reactivity in wheatdependent, exercise-induced anaphylaxis
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Palosuo K, Varjonen E, Nurkkala J, et al. Transglutaminase- mediated crosslinking of a peptic fraction of omega-5 gliadin enhances IgE reactivity in wheatdependent, exercise-induced anaphylaxis. J Allergy Clin Immunol 2003; 111:1386-1392.
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(2003)
J Allergy Clin Immunol
, vol.111
, pp. 1386-1392
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Palosuo, K.1
Varjonen, E.2
Nurkkala, J.3
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22
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0033048929
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Thioredoxin treatment increases digestibility and lowers allergenicity of milk
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del Val G, Yee BC, Lozano RM, et al. Thioredoxin treatment increases digestibility and lowers allergenicity of milk. Allergy Clin Immunol 1999; 103:690-697.
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(1999)
Allergy Clin Immunol
, vol.103
, pp. 690-697
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del Val, G.1
Yee, B.C.2
Lozano, R.M.3
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23
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34250658872
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Mitigated binding of IgE to thioredoxintreated salt-soluble wheat allergens in a child with baker's asthma
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Matsumoto T, Shimada Y, Hirai S. Mitigated binding of IgE to thioredoxintreated salt-soluble wheat allergens in a child with baker's asthma. Ann Allergy Asthma Immunol 2007; 98:599-600.
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(2007)
Ann Allergy Asthma Immunol
, vol.98
, pp. 599-600
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Matsumoto, T.1
Shimada, Y.2
Hirai, S.3
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24
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33644777430
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Wheat and maize thioredoxins: A novel cross-reactive cereal allergen family related to baker's asthma
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Weichel M, Glaser AG, Ballmer-Weber BK, et al. Wheat and maize thioredoxins: a novel cross-reactive cereal allergen family related to baker's asthma. J Allergy Clin Immunol 2006; 117:676-681.
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(2006)
J Allergy Clin Immunol
, vol.117
, pp. 676-681
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Weichel, M.1
Glaser, A.G.2
Ballmer-Weber, B.K.3
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25
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0035020401
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Effects of cooking methods on peanut allergenicity
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Beyer K, Morrow E, Li XM, et al. Effects of cooking methods on peanut allergenicity. J Allergy Clin Immunol 2001; 107:1077-1081.
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(2001)
J Allergy Clin Immunol
, vol.107
, pp. 1077-1081
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Beyer, K.1
Morrow, E.2
Li, X.M.3
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27
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33847412324
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Application of electron transfer dissociation mass spectrometry in analyses of nonenzymatically glycated peptides
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Rapid advances are being made in the application of mass spectrometry to analysis of proteins. This report describes a novel method for characterizing glycated proteins and peptides, which will facilitate better characterization of Maillard modified food proteins in future
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Zhang Q, Frolov A, Tang N, et al. Application of electron transfer dissociation mass spectrometry in analyses of nonenzymatically glycated peptides. Rapid Commun Mass Spectrom 2007; 21:661-666. Rapid advances are being made in the application of mass spectrometry to analysis of proteins. This report describes a novel method for characterizing glycated proteins and peptides, which will facilitate better characterization of Maillard modified food proteins in future.
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(2007)
Rapid Commun Mass Spectrom
, vol.21
, pp. 661-666
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Zhang, Q.1
Frolov, A.2
Tang, N.3
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28
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33745753267
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Noncovalent cross-linking of casein by epigallocatechin gallate characterized by single molecule force microscopy
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Jö bstl E, Howse JR, Fairclough JP, Williamson MP. Noncovalent cross-linking of casein by epigallocatechin gallate characterized by single molecule force microscopy. J Agric Food Chem 2006; 54:4077-4081.
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(2006)
J Agric Food Chem
, vol.54
, pp. 4077-4081
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Jö bstl, E.1
Howse, J.R.2
Fairclough, J.P.3
Williamson, M.P.4
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29
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36148968860
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Effects of phytic acid on peanut allergens and allergenic properties of extracts
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This paper is a good example of the food research community seeking to identify processing procedures that canameliorate allergenicity. It illustrates thecomplexities and difficulties of this type of research and is working to a hypothesis that rendering proteins insoluble will reduce their allergenicity
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Chung SY. Champagne ET Effects of phytic acid on peanut allergens and allergenic properties of extracts. J Agric Food Chem 2007; 55:9054-9058. This paper is a good example of the food research community seeking to identify processing procedures that canameliorate allergenicity. It illustrates thecomplexities and difficulties of this type of research and is working to a hypothesis that rendering proteins insoluble will reduce their allergenicity.
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(2007)
J Agric Food Chem
, vol.55
, pp. 9054-9058
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Chung, S.Y.1
Champagne, E.T.2
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31
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34047137958
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Specific immuno-modulation and therapy by means of high pressure treated allergens
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Meyer-Pitroff R,Behrendt H, Ring J.Specific immuno-modulation and therapy by means of high pressure treated allergens. High Press Res 2007; 27:63-67.
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(2007)
High Press Res
, vol.27
, pp. 63-67
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Meyer-Pitroff, R.1
Behrendt, H.2
Ring, J.3
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