메뉴 건너뛰기




Volumn 115, Issue 1, 2005, Pages 14-23

Molecular properties of food allergens

Author keywords

aggregation; Food allergens; glycation; glycosylation; ligand binding; membrane interaction; protein mobility; protein stability; repetitive sequences; rheomorphism

Indexed keywords

FOOD ALLERGEN; OLIGOMER;

EID: 11344257641     PISSN: 00916749     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jaci.2004.10.022     Document Type: Review
Times cited : (311)

References (111)
  • 1
    • 3442895900 scopus 로고    scopus 로고
    • Prevalence of seafood allergy in the United States determined by a random telephone survey
    • S.H. Sicherer, A. Munoz-Furlong, and H.A. Sampson Prevalence of seafood allergy in the United States determined by a random telephone survey J Allergy Clin Immunol 114 2004 159 165
    • (2004) J Allergy Clin Immunol , vol.114 , pp. 159-165
    • Sicherer, S.H.1    Munoz-Furlong, A.2    Sampson, H.A.3
  • 2
    • 0033064254 scopus 로고    scopus 로고
    • Food allergy. Part 1: Immunopathogenesis and clinical disorders
    • H.A. Sampson Food allergy. Part 1: immunopathogenesis and clinical disorders J Allergy Clin Immunol 103 1999 717 728
    • (1999) J Allergy Clin Immunol , vol.103 , pp. 717-728
    • Sampson, H.A.1
  • 5
    • 11344255717 scopus 로고    scopus 로고
    • Structural relatedness of plant food allergens with specific reference to cross-reactive allergens - An in silico analysis
    • J.A. Jenkins, Griffiths-Jones, P.R. Shewry, H. Breiteneder, and E.N.C. Mills Structural relatedness of plant food allergens with specific reference to cross-reactive allergens - an in silico analysis J Allergy Clin Immunol 115 2005 163 170
    • (2005) J Allergy Clin Immunol , vol.115 , pp. 163-170
    • Jenkins, J.A.1    Griffiths-Jones, P.R.2    Shewry, P.R.3    Breiteneder, H.4    Mills, E.N.C.5
  • 8
    • 0033990061 scopus 로고    scopus 로고
    • Flexible sequence similarity searching with the FASTA3 program package
    • W.R. Pearson Flexible sequence similarity searching with the FASTA3 program package Methods Mol Biol 132 2000 185 219
    • (2000) Methods Mol Biol , vol.132 , pp. 185-219
    • Pearson, W.R.1
  • 9
    • 0038380463 scopus 로고    scopus 로고
    • Allergenicity prediction by protein sequence
    • M.B. Stadler, and B.M. Stadler Allergenicity prediction by protein sequence FASEB J 17 2003 1141 1143
    • (2003) FASEB J , vol.17 , pp. 1141-1143
    • Stadler, M.B.1    Stadler, B.M.2
  • 10
    • 1542316862 scopus 로고    scopus 로고
    • Statistical evaluation of local alignment features predicting allergenicity using supervised classification algorithms
    • D. Soeria-Atmadja, A. Zorzet, M.G. Gustafsson, and U. Hammerling Statistical evaluation of local alignment features predicting allergenicity using supervised classification algorithms Int Arch Allergy Immunol 133 2004 101 112
    • (2004) Int Arch Allergy Immunol , vol.133 , pp. 101-112
    • Soeria-Atmadja, D.1    Zorzet, A.2    Gustafsson, M.G.3    Hammerling, U.4
  • 11
    • 85044702737 scopus 로고    scopus 로고
    • Screening of transgenic proteins expressed in genetically modified food crops for the presence of six amino acid sequences identical to potential, IgE-binding linear epitopes of allergens
    • G.A. Kleter, and A.C.M. Peijnenberg Screening of transgenic proteins expressed in genetically modified food crops for the presence of six amino acid sequences identical to potential, IgE-binding linear epitopes of allergens BMC Struct Biol 2 2002 8
    • (2002) BMC Struct Biol , vol.2 , pp. 8
    • Kleter, G.A.1    Peijnenberg, A.C.M.2
  • 12
    • 0042303843 scopus 로고    scopus 로고
    • Detecting potential IgE-reactive sites on food proteins using a sequence and structure database, SDAP-Food
    • O. Ivanciuc, V. Mathura, T. Midoro-Horiuti, W. Braun, R.M. Goldblum, and C.H. Schein Detecting potential IgE-reactive sites on food proteins using a sequence and structure database, SDAP-Food J Agric Food Chem 51 2003 4830 4837
    • (2003) J Agric Food Chem , vol.51 , pp. 4830-4837
    • Ivanciuc, O.1    Mathura, V.2    Midoro-Horiuti, T.3    Braun, W.4    Goldblum, R.M.5    Schein, C.H.6
  • 13
    • 0036330905 scopus 로고    scopus 로고
    • Intrinsic properties of allergens and environmental exposure as determinants of allergenicity
    • A. Pomes Intrinsic properties of allergens and environmental exposure as determinants of allergenicity Allergy 57 2002 673 679
    • (2002) Allergy , vol.57 , pp. 673-679
    • Pomes, A.1
  • 14
    • 0033836431 scopus 로고    scopus 로고
    • Structural biology of allergens
    • R.C. Aalberse Structural biology of allergens J Allergy Clin Immunol 106 2000 228 238
    • (2000) J Allergy Clin Immunol , vol.106 , pp. 228-238
    • Aalberse, R.C.1
  • 16
    • 2142643110 scopus 로고    scopus 로고
    • What makes a food protein an allergen?
    • G.A. Bannon What makes a food protein an allergen? Curr Allergy Asthma Rep 4 2004 43 46
    • (2004) Curr Allergy Asthma Rep , vol.4 , pp. 43-46
    • Bannon, G.A.1
  • 17
    • 0028989022 scopus 로고
    • Effect of sodium dodecyl sulfate and palmitic acid on the equilibrium unfolding of bovine beta-lactoglobulin
    • L.K. Creamer Effect of sodium dodecyl sulfate and palmitic acid on the equilibrium unfolding of bovine beta-lactoglobulin Biochemistry 34 1995 7170 7176
    • (1995) Biochemistry , vol.34 , pp. 7170-7176
    • Creamer, L.K.1
  • 18
    • 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
    • J.P. Douliez, S. Jegou, C. Pato, D. Molle, V. Tran, and D. Marion 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 268 2001 384 388
    • (2001) Eur J Biochem , vol.268 , pp. 384-388
    • Douliez, J.P.1    Jegou, S.2    Pato, C.3    Molle, D.4    Tran, V.5    Marion, D.6
  • 20
    • 0030032040 scopus 로고    scopus 로고
    • Calcium binding and conformational response in EF-hand proteins
    • M. Ikura Calcium binding and conformational response in EF-hand proteins Trends Biochem Sci 21 1996 14 17
    • (1996) Trends Biochem Sci , vol.21 , pp. 14-17
    • Ikura, M.1
  • 21
    • 0025870926 scopus 로고
    • Ionic interactions with parvalbumins. Crystal structure determination of pike 4.10 parvalbumin in four different ionic environments
    • J.P. Declercq, B. Tinant, J. Parello, and J. Rambaud Ionic interactions with parvalbumins. Crystal structure determination of pike 4.10 parvalbumin in four different ionic environments J Mol Biol 220 1991 1017 1039
    • (1991) J Mol Biol , vol.220 , pp. 1017-1039
    • Declercq, J.P.1    Tinant, B.2    Parello, J.3    Rambaud, J.4
  • 22
    • 0030577844 scopus 로고    scopus 로고
    • The Ca2+(-)binding proteins parvalbumin and oncomodulin and their genes: New structural and functional findings
    • T.L. Pauls, J.A. Cox, and M.W. Berchtold The Ca2+(-)binding proteins parvalbumin and oncomodulin and their genes: new structural and functional findings Biochim Biophys Acta 1306 1996 39 54
    • (1996) Biochim Biophys Acta , vol.1306 , pp. 39-54
    • Pauls, T.L.1    Cox, J.A.2    Berchtold, M.W.3
  • 23
    • 0031915243 scopus 로고    scopus 로고
    • Parvalbumin, a cross-reactive fish allergen, contains IgE-binding epitopes sensitive to periodate treatment and Ca2+ depletion
    • A. Bugajska-Schretter, L. Elfman, T. Fuchs, S. Kapiotis, H. Rumpold, and R. Valenta Parvalbumin, a cross-reactive fish allergen, contains IgE-binding epitopes sensitive to periodate treatment and Ca2+ depletion J Allergy Clin Immunol 101 1998 67 74
    • (1998) J Allergy Clin Immunol , vol.101 , pp. 67-74
    • Bugajska-Schretter, A.1    Elfman, L.2    Fuchs, T.3    Kapiotis, S.4    Rumpold, H.5    Valenta, R.6
  • 24
    • 2942550553 scopus 로고    scopus 로고
    • IgE antibodies of fish allergic patients cross-react with frog parvalbumin
    • C. Hilger, L. Thill, F. Grigioni, C. Lehners, P. Falagiani, and A. Ferrara IgE antibodies of fish allergic patients cross-react with frog parvalbumin Allergy 59 2004 653 660
    • (2004) Allergy , vol.59 , pp. 653-660
    • Hilger, C.1    Thill, L.2    Grigioni, F.3    Lehners, C.4    Falagiani, P.5    Ferrara, A.6
  • 25
    • 0004844595 scopus 로고    scopus 로고
    • Purification, biochemical, and immunological characterisation of a major food allergen: Different immunoglobulin e recognition of the apo- and calcium-bound forms of carp parvalbumin
    • A. Bugajska-Schretter, M. Grote, L. Vangelista, P. Valent, W.R. Sperr, and H. Rumpold Purification, biochemical, and immunological characterisation of a major food allergen: different immunoglobulin E recognition of the apo- and calcium-bound forms of carp parvalbumin Gut 46 2000 661 669
    • (2000) Gut , vol.46 , pp. 661-669
    • Bugajska-Schretter, A.1    Grote, M.2    Vangelista, L.3    Valent, P.4    Sperr, W.R.5    Rumpold, H.6
  • 26
    • 0015057207 scopus 로고
    • Characterization of a major allergen (cod). Observations on effect of denaturation on the allergenic activity
    • S. Elsayed, and K. Aas Characterization of a major allergen (cod). Observations on effect of denaturation on the allergenic activity J Allergy 47 1971 283 291
    • (1971) J Allergy , vol.47 , pp. 283-291
    • Elsayed, S.1    Aas, K.2
  • 27
    • 0026722948 scopus 로고
    • Fish hypersensitivity. II: Clinical relevance of altered fish allergenicity caused by various preparation methods
    • J. Bernhisel-Broadbent, D. Strause, and H.A. Sampson Fish hypersensitivity. II: Clinical relevance of altered fish allergenicity caused by various preparation methods J Allergy Clin Immunol 90 1992 622 629
    • (1992) J Allergy Clin Immunol , vol.90 , pp. 622-629
    • Bernhisel-Broadbent, J.1    Strause, D.2    Sampson, H.A.3
  • 28
    • 0026553913 scopus 로고
    • Fish hypersensitivity. I. In vitro and oral challenge results in fish-allergic patients
    • J. Bernhisel-Broadbent, S.M. Scanlon, and H.A. Sampson Fish hypersensitivity. I. In vitro and oral challenge results in fish-allergic patients J Allergy Clin Immunol 89 1992 730 737
    • (1992) J Allergy Clin Immunol , vol.89 , pp. 730-737
    • Bernhisel-Broadbent, J.1    Scanlon, S.M.2    Sampson, H.A.3
  • 29
    • 0032520111 scopus 로고    scopus 로고
    • A core-shell model of calcium phosphate nanoclusters stabilized by beta-casein phosphopeptides, derived from sedimentation equilibrium and small-angle X-ray and neutron-scattering measurements
    • C. Holt, P.A. Timmins, N. Errington, and J. Leaver A core-shell model of calcium phosphate nanoclusters stabilized by beta-casein phosphopeptides, derived from sedimentation equilibrium and small-angle X-ray and neutron-scattering measurements Eur J Biochem 252 1998 73 78
    • (1998) Eur J Biochem , vol.252 , pp. 73-78
    • Holt, C.1    Timmins, P.A.2    Errington, N.3    Leaver, J.4
  • 30
    • 0037101011 scopus 로고    scopus 로고
    • Stability of casein micelles in milk
    • R. Tuinier, and C.G. de Kruif Stability of casein micelles in milk J Chem Phys 117 2002 1290 1295
    • (2002) J Chem Phys , vol.117 , pp. 1290-1295
    • Tuinier, R.1    De Kruif, C.G.2
  • 31
    • 0033962437 scopus 로고    scopus 로고
    • Post-translational phosphorylation affects the IgE binding capacity of caseins
    • H. Bernard, H. Meisel, C. Creminon, and J.M. Wal Post-translational phosphorylation affects the IgE binding capacity of caseins FEBS Lett 467 2000 239 244
    • (2000) FEBS Lett , vol.467 , pp. 239-244
    • Bernard, H.1    Meisel, H.2    Creminon, C.3    Wal, J.M.4
  • 32
    • 33845282222 scopus 로고
    • Binding of alkanone flavours to beta-lactoglobulin: Effects of conformational and chemical modification
    • T.E. O'Neill, and J.E. Kinsella Binding of alkanone flavours to beta-lactoglobulin: Effects of conformational and chemical modification J Agric Food Chem 35 1987 770 774
    • (1987) J Agric Food Chem , vol.35 , pp. 770-774
    • O'Neill, T.E.1    Kinsella, J.E.2
  • 33
    • 0036037132 scopus 로고    scopus 로고
    • The ligand-binding site of bovine beta-lactoglobulin: Evidence for a function?
    • G. Kontopidis, C. Holt, and L. Sawyer The ligand-binding site of bovine beta-lactoglobulin: evidence for a function? J Mol Biol 318 2002 1043 1055
    • (2002) J Mol Biol , vol.318 , pp. 1043-1055
    • Kontopidis, G.1    Holt, C.2    Sawyer, L.3
  • 34
    • 0141755209 scopus 로고    scopus 로고
    • EF loop conformational change triggers ligand binding in beta-lactoglobulins
    • L. Ragona, F. Fogolari, M. Catalano, R. Ugolini, L. Zetta, and H. Molinari EF loop conformational change triggers ligand binding in beta-lactoglobulins J Biol Chem 278 2003 38840 38846
    • (2003) J Biol Chem , vol.278 , pp. 38840-38846
    • Ragona, L.1    Fogolari, F.2    Catalano, M.3    Ugolini, R.4    Zetta, L.5    Molinari, H.6
  • 35
    • 0034738520 scopus 로고    scopus 로고
    • Steady-state tyrosine fluorescence to study the lipid-binding properties of a wheat non-specific lipid-transfer protein (nsLTP1)
    • J.P. Douliez, T. Michon, and D. Marion Steady-state tyrosine fluorescence to study the lipid-binding properties of a wheat non-specific lipid-transfer protein (nsLTP1) Biochim Biophys Acta 1467 2000 65 72
    • (2000) Biochim Biophys Acta , vol.1467 , pp. 65-72
    • Douliez, J.P.1    Michon, T.2    Marion, D.3
  • 36
    • 0033951882 scopus 로고    scopus 로고
    • The wide binding properties of a wheat nonspecific lipid transfer protein. Solution structure of a complex with prostaglandin B2
    • S. Tassin-Moindrot, A. Caille, J.P. Douliez, D. Marion, and F. Vovelle The wide binding properties of a wheat nonspecific lipid transfer protein. Solution structure of a complex with prostaglandin B2 Eur J Biochem 267 2000 1117 1124
    • (2000) Eur J Biochem , vol.267 , pp. 1117-1124
    • Tassin-Moindrot, S.1    Caille, A.2    Douliez, J.P.3    Marion, D.4    Vovelle, F.5
  • 38
    • 0032539972 scopus 로고    scopus 로고
    • Solution structure of Ace-AMP1, a potent antimicrobial protein extracted from onion seeds. Structural analogies with plant nonspecific lipid transfer proteins
    • S. Tassin, W.F. Broekaert, D. Marion, D.P. Acland, M. Ptak, and F. Vovelle Solution structure of Ace-AMP1, a potent antimicrobial protein extracted from onion seeds. Structural analogies with plant nonspecific lipid transfer proteins Biochemistry 37 1998 3623 3637
    • (1998) Biochemistry , vol.37 , pp. 3623-3637
    • Tassin, S.1    Broekaert, W.F.2    Marion, D.3    Acland, D.P.4    Ptak, M.5    Vovelle, F.6
  • 39
    • 0034064138 scopus 로고    scopus 로고
    • Structure and lipid transport mechanism of a StAR-related domain
    • Y. Tsujishita, and J.H. Hurley Structure and lipid transport mechanism of a StAR-related domain Nat Struct Biol 7 2000 408 414
    • (2000) Nat Struct Biol , vol.7 , pp. 408-414
    • Tsujishita, Y.1    Hurley, J.H.2
  • 40
    • 0035933875 scopus 로고    scopus 로고
    • Allergic cross-reactivity made visible: Solution structure of the major cherry allergen Pru av 1
    • P. Neudecker, K. Schweimer, J. Nerkamp, S. Scheurer, S. Vieths, and H. Sticht Allergic cross-reactivity made visible: solution structure of the major cherry allergen Pru av 1 J Biol Chem 276 2001 22756 22763
    • (2001) J Biol Chem , vol.276 , pp. 22756-22763
    • Neudecker, P.1    Schweimer, K.2    Nerkamp, J.3    Scheurer, S.4    Vieths, S.5    Sticht, H.6
  • 41
    • 0037255538 scopus 로고    scopus 로고
    • Crystal structure of a hypoallergenic isoform of the major birch pollen allergen Bet v 1 and its likely biological function as a plant steroid carrier
    • Z. Markovic-Housley, M. Degano, D. Lamba, E. von Roepenack-Lahaye, S. Clemens, and M. Susani Crystal structure of a hypoallergenic isoform of the major birch pollen allergen Bet v 1 and its likely biological function as a plant steroid carrier J Mol Biol 325 2003 123 133
    • (2003) J Mol Biol , vol.325 , pp. 123-133
    • Markovic-Housley, Z.1    Degano, M.2    Lamba, D.3    Von Roepenack-Lahaye, E.4    Clemens, S.5    Susani, M.6
  • 42
    • 0036264052 scopus 로고    scopus 로고
    • Current understanding of cross-reactivity of food allergens and pollen
    • S. Vieths, S. Scheurer, and B. Ballmer-Weber Current understanding of cross-reactivity of food allergens and pollen Ann N Y Acad Sci 964 2002 47 68
    • (2002) Ann N Y Acad Sci , vol.964 , pp. 47-68
    • Vieths, S.1    Scheurer, S.2    Ballmer-Weber, B.3
  • 43
    • 0036858612 scopus 로고    scopus 로고
    • Severe oral allergy syndrome and anaphylactic reactions caused by a Bet v 1-related PR-10 protein in soybean, SAM22
    • J. Kleine-Tebbe, L. Vogel, D.N. Crowell, U.F. Haustein, and S. Vieths Severe oral allergy syndrome and anaphylactic reactions caused by a Bet v 1-related PR-10 protein in soybean, SAM22 J Allergy Clin Immunol 110 2002 797 804
    • (2002) J Allergy Clin Immunol , vol.110 , pp. 797-804
    • Kleine-Tebbe, J.1    Vogel, L.2    Crowell, D.N.3    Haustein, U.F.4    Vieths, S.5
  • 45
    • 2342578126 scopus 로고    scopus 로고
    • Thaumatin-like proteins - A new family of pollen and fruit allergens
    • H. Breiteneder Thaumatin-like proteins - a new family of pollen and fruit allergens Allergy 59 2004 479 481
    • (2004) Allergy , vol.59 , pp. 479-481
    • Breiteneder, H.1
  • 46
    • 0037716584 scopus 로고    scopus 로고
    • Plant-based heterologous expression of Mal d 2, a thaumatin-like protein and allergen of apple (Malus domestica), and its characterization as an antifungal protein
    • M. Krebitz, B. Wagner, F. Ferreira, C. Peterbauer, N. Campillo, and M. Witty Plant-based heterologous expression of Mal d 2, a thaumatin-like protein and allergen of apple (Malus domestica), and its characterization as an antifungal protein J Mol Biol 329 2003 721 730
    • (2003) J Mol Biol , vol.329 , pp. 721-730
    • Krebitz, M.1    Wagner, B.2    Ferreira, F.3    Peterbauer, C.4    Campillo, N.5    Witty, M.6
  • 49
    • 0026635585 scopus 로고
    • Analysis of two novel classes of plant antifungal proteins from radish (Raphanus sativus L.) seeds
    • F.R. Terras, H.M. Schoofs, M.F. De Bolle, F. Van Leuven, S.B. Rees, and J. Vanderleyden Analysis of two novel classes of plant antifungal proteins from radish (Raphanus sativus L.) seeds J Biol Chem 267 1992 15301 15309
    • (1992) J Biol Chem , vol.267 , pp. 15301-15309
    • Terras, F.R.1    Schoofs, H.M.2    De Bolle, M.F.3    Van Leuven, F.4    Rees, S.B.5    Vanderleyden, J.6
  • 50
    • 0027132885 scopus 로고
    • Synergistic enhancement of the antifungal activity of wheat and barley thionins by radish and oilseed rape 2S albumins and by barley trypsin inhibitors
    • F. Terras, H. Schoofs, K. Thevissen, R.W. Osborn, J. Vanderleyden, and B. Cammue Synergistic enhancement of the antifungal activity of wheat and barley thionins by radish and oilseed rape 2S albumins and by barley trypsin inhibitors Plant Physiol 103 1993 1311 1319
    • (1993) Plant Physiol , vol.103 , pp. 1311-1319
    • Terras, F.1    Schoofs, H.2    Thevissen, K.3    Osborn, R.W.4    Vanderleyden, J.5    Cammue, B.6
  • 52
    • 0027179487 scopus 로고
    • Phospholipids in animal eukaryotic membranes: Transverse asymmetry and movement
    • A. Zachowski Phospholipids in animal eukaryotic membranes: transverse asymmetry and movement Biochem J 294 1993 1 14
    • (1993) Biochem J , vol.294 , pp. 1-14
    • Zachowski, A.1
  • 53
    • 0031081348 scopus 로고    scopus 로고
    • Lipid-transfer proteins: A puzzling family of plant proteins
    • J.C. Kader Lipid-transfer proteins: a puzzling family of plant proteins Trends Plant Sci 2 1997 66 70
    • (1997) Trends Plant Sci , vol.2 , pp. 66-70
    • Kader, J.C.1
  • 54
    • 0029116486 scopus 로고    scopus 로고
    • Interaction of non-specific wheat lipid transfer protein with phospholipid monolyers imaged by fluorescence microscopy and studied by infrared spectroscopy
    • M. Subriade, D. Salesse, D. Marion, and M. Pézolet Interaction of non-specific wheat lipid transfer protein with phospholipid monolyers imaged by fluorescence microscopy and studied by infrared spectroscopy Biophys J 69 1999 974 988
    • (1999) Biophys J , vol.69 , pp. 974-988
    • Subriade, M.1    Salesse, D.2    Marion, D.3    Pézolet, M.4
  • 55
    • 0036813742 scopus 로고    scopus 로고
    • Interaction of surfactants and polymer-grafted lipids with a plant lipid transfer protein, LTP1
    • J.P. Douliez, D. Sy, F. Vovelle, and D. Marion Interaction of surfactants and polymer-grafted lipids with a plant lipid transfer protein, LTP1 Langmuir 18 2002 7309 7312
    • (2002) Langmuir , vol.18 , pp. 7309-7312
    • Douliez, J.P.1    Sy, D.2    Vovelle, F.3    Marion, D.4
  • 57
    • 0345711506 scopus 로고    scopus 로고
    • Surface functional properties of native, acid-treated, and reduced soy glycinin. 2. Emulsifying properties
    • J.R. Wagner, and J. Gueguen Surface functional properties of native, acid-treated, and reduced soy glycinin. 2. Emulsifying properties J Agric Food Chem 47 1999 2181 2187
    • (1999) J Agric Food Chem , vol.47 , pp. 2181-2187
    • Wagner, J.R.1    Gueguen, J.2
  • 58
    • 0033385322 scopus 로고    scopus 로고
    • Structure-physicochemical function relationships of soybean beta-conglycinin constituent subunits
    • N. Maruyama, R. Sato, Y. Wada, Y. Matsumura, H. Goto, and E. Okuda Structure-physicochemical function relationships of soybean beta-conglycinin constituent subunits J Agric Food Chem 47 1999 5278 5284
    • (1999) J Agric Food Chem , vol.47 , pp. 5278-5284
    • Maruyama, N.1    Sato, R.2    Wada, Y.3    Matsumura, Y.4    Goto, H.5    Okuda, E.6
  • 59
    • 0034629222 scopus 로고    scopus 로고
    • Bovine beta-lactoglobulin receptors on transformed mammalian cells (hybridomas MARK-3): Characterization by flow cytometry
    • N.S. Palupi, P. Franck, C. Guimont, G. Linden, D. Dumas, and J. Stoltz Bovine beta-lactoglobulin receptors on transformed mammalian cells (hybridomas MARK-3): characterization by flow cytometry J Biotechnol 78 2000 171 184
    • (2000) J Biotechnol , vol.78 , pp. 171-184
    • Palupi, N.S.1    Franck, P.2    Guimont, C.3    Linden, G.4    Dumas, D.5    Stoltz, J.6
  • 60
    • 0141567953 scopus 로고    scopus 로고
    • Casein binds to the cell membrane and induces intracellular calcium signals in the enteroendocrine cell: A brief communication
    • T. Hira, H. Hara, F. Tomita, and Y. Aoyama Casein binds to the cell membrane and induces intracellular calcium signals in the enteroendocrine cell: a brief communication Exp Biol Med 228 2003 850 854
    • (2003) Exp Biol Med , vol.228 , pp. 850-854
    • Hira, T.1    Hara, H.2    Tomita, F.3    Aoyama, Y.4
  • 61
    • 0035976883 scopus 로고    scopus 로고
    • A lipid transfer protein binds to a receptor involved in the control of plant defence responses
    • N. Buhot, J.P. Douliez, A. Jacquemard, D. Marion, V. Tran, and B.F. Maume A lipid transfer protein binds to a receptor involved in the control of plant defence responses FEBS Lett 509 2001 27 30
    • (2001) FEBS Lett , vol.509 , pp. 27-30
    • Buhot, N.1    Douliez, J.P.2    Jacquemard, A.3    Marion, D.4    Tran, V.5    Maume, B.F.6
  • 62
    • 0034677790 scopus 로고    scopus 로고
    • Elucidation of determinants of protein stability through genome sequence analysis
    • S. Chakravarty, and R. Varadarajan Elucidation of determinants of protein stability through genome sequence analysis FEBS Lett 470 2000 65 69
    • (2000) FEBS Lett , vol.470 , pp. 65-69
    • Chakravarty, S.1    Varadarajan, R.2
  • 63
    • 0033538553 scopus 로고    scopus 로고
    • Transproteomic evidence of a loop-deletion mechanism for enhancing protein thermostability
    • M.J. Thompson, and D. Eisenberg Transproteomic evidence of a loop-deletion mechanism for enhancing protein thermostability J Mol Biol 290 1999 595 604
    • (1999) J Mol Biol , vol.290 , pp. 595-604
    • Thompson, M.J.1    Eisenberg, D.2
  • 64
    • 0025304590 scopus 로고
    • Purification and characterization of an allergen of mustard seed
    • J. Dominguez, M. Cuevas, V. Urena, T. Munoz, and I. Moneo Purification and characterization of an allergen of mustard seed Ann Allergy 64 1990 352 357
    • (1990) Ann Allergy , vol.64 , pp. 352-357
    • Dominguez, J.1    Cuevas, M.2    Urena, V.3    Munoz, T.4    Moneo, I.5
  • 65
    • 0043123380 scopus 로고    scopus 로고
    • In vitro stability and immunoreactivity of the native and recombinant plant food 2S albumins Ber e 1 and SFA-8
    • G.J. Murtagh, D.B. Archer, M. Dumoulin, S. Ridout, S. Matthews, and S.H. Arshad In vitro stability and immunoreactivity of the native and recombinant plant food 2S albumins Ber e 1 and SFA-8 Clin Exp Allergy 33 2003 1147 1152
    • (2003) Clin Exp Allergy , vol.33 , pp. 1147-1152
    • Murtagh, G.J.1    Archer, D.B.2    Dumoulin, M.3    Ridout, S.4    Matthews, S.5    Arshad, S.H.6
  • 66
    • 0036864152 scopus 로고    scopus 로고
    • Clinical importance of non-specific lipid transfer proteins as food allergens
    • R. van Ree Clinical importance of non-specific lipid transfer proteins as food allergens Biochem Soc Trans 30 2002 910 913
    • (2002) Biochem Soc Trans , vol.30 , pp. 910-913
    • Van Ree, R.1
  • 67
    • 0141921988 scopus 로고    scopus 로고
    • Lipid-transfer protein is the major maize allergen maintaining IgE-binding activity after cooking at 100 degrees C, as demonstrated in anaphylactic patients and patients with positive double-blind, placebo-controlled food challenge results
    • E.A. Pastorello, C. Pompei, V. Pravettoni, L. Farioli, A.M. Calamari, and J. Scibilia Lipid-transfer protein is the major maize allergen maintaining IgE-binding activity after cooking at 100 degrees C, as demonstrated in anaphylactic patients and patients with positive double-blind, placebo-controlled food challenge results J Allergy Clin Immunol 112 2003 775 783
    • (2003) J Allergy Clin Immunol , vol.112 , pp. 775-783
    • Pastorello, E.A.1    Pompei, C.2    Pravettoni, V.3    Farioli, L.4    Calamari, A.M.5    Scibilia, J.6
  • 69
    • 0030021265 scopus 로고    scopus 로고
    • The crystal structure of the antifungal protein zeamatin, a member of the thaumatin-like, PR-5 protein family
    • M.A. Batalia, A.F. Monzingo, S. Ernst, W. Roberts, and J.D. Robertus The crystal structure of the antifungal protein zeamatin, a member of the thaumatin-like, PR-5 protein family Nat Struct Biol 3 1996 19 23
    • (1996) Nat Struct Biol , vol.3 , pp. 19-23
    • Batalia, M.A.1    Monzingo, A.F.2    Ernst, S.3    Roberts, W.4    Robertus, J.D.5
  • 70
    • 0033525649 scopus 로고    scopus 로고
    • Crystal structure of tobacco PR-5d protein at 1.8 a resolution reveals a conserved acidic cleft structure in antifungal thaumatin-like proteins
    • H. Koiwa, H. Kato, T. Nakatsu, J. Oda, Y. Yamada, and F. Sato Crystal structure of tobacco PR-5d protein at 1.8 A resolution reveals a conserved acidic cleft structure in antifungal thaumatin-like proteins J Mol Biol 286 1999 1137 1145
    • (1999) J Mol Biol , vol.286 , pp. 1137-1145
    • Koiwa, H.1    Kato, H.2    Nakatsu, T.3    Oda, J.4    Yamada, Y.5    Sato, F.6
  • 72
    • 0027096460 scopus 로고
    • Crystal structure of a sweet tasting protein thaumatin I, at 1.65 a resolution
    • C.M. Ogata, P.F. Gordon, A.M. de Vos, and S.H. Kim Crystal structure of a sweet tasting protein thaumatin I, at 1.65 A resolution J Mol Biol 228 1992 893 908
    • (1992) J Mol Biol , vol.228 , pp. 893-908
    • Ogata, C.M.1    Gordon, P.F.2    De Vos, A.M.3    Kim, S.H.4
  • 73
    • 0025063227 scopus 로고
    • Zeamatin, an antifungal protein from maize with membrane-permeabilizing activity
    • W.K. Roberts, and C.P. Selitrennikoff Zeamatin, an antifungal protein from maize with membrane-permeabilizing activity J Gen Microbiol 136 1990 1771 1778
    • (1990) J Gen Microbiol , vol.136 , pp. 1771-1778
    • Roberts, W.K.1    Selitrennikoff, C.P.2
  • 75
    • 1542373564 scopus 로고    scopus 로고
    • Antifungal proteins: Targets, mechanisms and prospective applications
    • T. Theis, and U. Stahl Antifungal proteins: targets, mechanisms and prospective applications Cell Mol Life Sci 61 2004 437 455
    • (2004) Cell Mol Life Sci , vol.61 , pp. 437-455
    • Theis, T.1    Stahl, U.2
  • 77
  • 78
    • 0023055086 scopus 로고
    • Correlation between sites of limited proteolysis and segmental mobility in thermolysin
    • A. Fontana, G. Fassina, C. Vita, D. Dalzoppo, M. Zamai, and M. Zambonin Correlation between sites of limited proteolysis and segmental mobility in thermolysin Biochemistry 25 1986 1847 1851
    • (1986) Biochemistry , vol.25 , pp. 1847-1851
    • Fontana, A.1    Fassina, G.2    Vita, C.3    Dalzoppo, D.4    Zamai, M.5    Zambonin, M.6
  • 80
    • 0001517504 scopus 로고
    • Caseins as rheomorphic proteins: Interpretation of the primary and secondary structures of alpha S1-beta- and kappa- caseins
    • C. Holt, and L. Sawyer Caseins as rheomorphic proteins: interpretation of the primary and secondary structures of alpha S1-beta- and kappa- caseins J Chem Soc Farad Trans 89 1993 2683 2692
    • (1993) J Chem Soc Farad Trans , vol.89 , pp. 2683-2692
    • Holt, C.1    Sawyer, L.2
  • 82
    • 0036436846 scopus 로고    scopus 로고
    • Carbohydrate epitopes and their relevance for the diagnosis and treatment of allergic diseases
    • R. van Ree Carbohydrate epitopes and their relevance for the diagnosis and treatment of allergic diseases Int Arch Allergy Immunol 129 2002 189 197
    • (2002) Int Arch Allergy Immunol , vol.129 , pp. 189-197
    • Van Ree, R.1
  • 84
    • 0036887227 scopus 로고    scopus 로고
    • IgE to cross-reactive carbohydrate determinants: Analysis of the distribution and appraisal of the in vivo and in vitro reactivity
    • A. Mari IgE to cross-reactive carbohydrate determinants: analysis of the distribution and appraisal of the in vivo and in vitro reactivity Int Arch Allergy Immunol 129 2002 286 295
    • (2002) Int Arch Allergy Immunol , vol.129 , pp. 286-295
    • Mari, A.1
  • 86
    • 0141483499 scopus 로고    scopus 로고
    • Cross-reactive N-glycans of Api g 5, a high molecular weight glycoprotein allergen from celery, are required for immunoglobulin e binding and activation of effector cells from allergic patients
    • M. Bublin, C. Radauer, I.B. Wilson, D. Kraft, O. Scheiner, and H. Breiteneder Cross-reactive N-glycans of Api g 5, a high molecular weight glycoprotein allergen from celery, are required for immunoglobulin E binding and activation of effector cells from allergic patients FASEB J 17 2003 1697 1699
    • (2003) FASEB J , vol.17 , pp. 1697-1699
    • Bublin, M.1    Radauer, C.2    Wilson, I.B.3    Kraft, D.4    Scheiner, O.5    Breiteneder, H.6
  • 87
    • 0033566020 scopus 로고    scopus 로고
    • Glyoproteins: Glycan presentation and protein-fold stability
    • M.R. Wormald, and R.A. Dwek Glyoproteins: glycan presentation and protein-fold stability Structure 7 1999 R155 R160
    • (1999) Structure , vol.7
    • Wormald, M.R.1    Dwek, R.A.2
  • 88
    • 0034667892 scopus 로고    scopus 로고
    • Selective neoglycosylation increases the structural stability of vicilin, the 7S storage globulin from pea seeds
    • C. Pedrosa, F.G. De Felice, C. Trisciuzzi, and S.T. Ferreira Selective neoglycosylation increases the structural stability of vicilin, the 7S storage globulin from pea seeds Arch Biochem Biophys 382 2000 203 210
    • (2000) Arch Biochem Biophys , vol.382 , pp. 203-210
    • Pedrosa, C.1    De Felice, F.G.2    Trisciuzzi, C.3    Ferreira, S.T.4
  • 89
    • 0034646714 scopus 로고    scopus 로고
    • Beta(1,2)-xylose and alpha(1,3)-fucose residues have a strong contribution in IgE binding to plant glycoallergens
    • R. van Ree, M. Cabanes-Macheteau, J. Akkerdaas, J.P. Milazzo, C. Loutelier-Bourhis, and C. Rayon Beta(1,2)-xylose and alpha(1,3)-fucose residues have a strong contribution in IgE binding to plant glycoallergens J Biol Chem 275 2000 11451 11458
    • (2000) J Biol Chem , vol.275 , pp. 11451-11458
    • Van Ree, R.1    Cabanes-Macheteau, M.2    Akkerdaas, J.3    Milazzo, J.P.4    Loutelier-Bourhis, C.5    Rayon, C.6
  • 90
    • 0023645611 scopus 로고
    • Structure, position, and biosynthesis of the high mannose and the complex oligosaccharide side chains of the bean storage protein phaseolin
    • A. Sturm, J.A. Van Kuik, J.F. Vliegenthart, and M.J. Chrispeels Structure, position, and biosynthesis of the high mannose and the complex oligosaccharide side chains of the bean storage protein phaseolin J Biol Chem 262 1987 13392 13403
    • (1987) J Biol Chem , vol.262 , pp. 13392-13403
    • Sturm, A.1    Van Kuik, J.A.2    Vliegenthart, J.F.3    Chrispeels, M.J.4
  • 91
    • 0028960162 scopus 로고
    • The molecular basis for N-glycosylation in the 11S globulin (legumin) of lupin seed
    • M. Duranti, C. Horstmann, J. Gilroy, and R.R. Croy The molecular basis for N-glycosylation in the 11S globulin (legumin) of lupin seed J Protein Chem 14 1995 107 110
    • (1995) J Protein Chem , vol.14 , pp. 107-110
    • Duranti, M.1    Horstmann, C.2    Gilroy, J.3    Croy, R.R.4
  • 93
    • 0842304936 scopus 로고    scopus 로고
    • Minimizing the immunogenicity of protein therapeutics
    • A.J. Chirino, M.L. Ary, and S.A. Marshall Minimizing the immunogenicity of protein therapeutics Drug Discov Today 9 2004 82 90
    • (2004) Drug Discov Today , vol.9 , pp. 82-90
    • Chirino, A.J.1    Ary, M.L.2    Marshall, S.A.3
  • 94
    • 0030856842 scopus 로고    scopus 로고
    • Protein aggregates seem to play a key role among the parameters influencing the antigenicity of interferon alpha (IFN-alpha) in normal and transgenic mice
    • A. Braun, L. Kwee, M.A. Labow, and J. Alsenz Protein aggregates seem to play a key role among the parameters influencing the antigenicity of interferon alpha (IFN-alpha) in normal and transgenic mice Pharm Res 14 1997 1472 1478
    • (1997) Pharm Res , vol.14 , pp. 1472-1478
    • Braun, A.1    Kwee, L.2    Labow, M.A.3    Alsenz, J.4
  • 95
    • 0036591301 scopus 로고    scopus 로고
    • Plasmodium falciparum: Fine-mapping of an epitope of the serine repeat antigen that is a target of parasite-inhibitory antibodies
    • B.A. Fox, T. Horii, and D.J. Bzik Plasmodium falciparum: fine-mapping of an epitope of the serine repeat antigen that is a target of parasite-inhibitory antibodies Exp Parasitol 101 2002 69 72
    • (2002) Exp Parasitol , vol.101 , pp. 69-72
    • Fox, B.A.1    Horii, T.2    Bzik, D.J.3
  • 96
    • 0023335168 scopus 로고
    • Genetic origin of diversity of human cytoskeletal tropomyosins
    • A.R. MacLeod Genetic origin of diversity of human cytoskeletal tropomyosins Bioessays 6 1987 208 212
    • (1987) Bioessays , vol.6 , pp. 208-212
    • MacLeod, A.R.1
  • 98
    • 0037188485 scopus 로고    scopus 로고
    • The crystal structure of the C-terminal fragment of striated-muscle alpha-tropomyosin reveals a key troponin T recognition site
    • Y. Li, S. Mui, J.H. Brown, J. Strand, L. Reshetnikova, and L.S. Tobacman The crystal structure of the C-terminal fragment of striated-muscle alpha-tropomyosin reveals a key troponin T recognition site Proc Natl Acad Sci U S A 99 2002 378 383
    • (2002) Proc Natl Acad Sci U S a , vol.99 , pp. 378-383
    • Li, Y.1    Mui, S.2    Brown, J.H.3    Strand, J.4    Reshetnikova, L.5    Tobacman, L.S.6
  • 99
    • 0024510884 scopus 로고
    • Isolation and characterization of heat-stable allergens from shrimp (Penaeus indicus)
    • S. Naqpal, L. Rajappa, D.D. Metcalfe, and P.V. Rao Isolation and characterization of heat-stable allergens from shrimp (Penaeus indicus) J Allergy Clin Immunol 83 1989 26 36
    • (1989) J Allergy Clin Immunol , vol.83 , pp. 26-36
    • Naqpal, S.1    Rajappa, L.2    Metcalfe, D.D.3    Rao, P.V.4
  • 102
    • 0001544334 scopus 로고    scopus 로고
    • Partial purification and characterization of the 15S globulin of soybeans, a dimer of glycinin
    • W.J. Wolf, and T.C. Nelsen Partial purification and characterization of the 15S globulin of soybeans, a dimer of glycinin J Agric Food Chem 44 1996 785 791
    • (1996) J Agric Food Chem , vol.44 , pp. 785-791
    • Wolf, W.J.1    Nelsen, T.C.2
  • 103
    • 34247187913 scopus 로고
    • Molecular understanding of heat-induced phenomena of soybean protein
    • F. Yamauchi, T. Yamagishi, and S. Iwabuchi Molecular understanding of heat-induced phenomena of soybean protein Food Rev Internat 7 1991 283 322
    • (1991) Food Rev Internat , vol.7 , pp. 283-322
    • Yamauchi, F.1    Yamagishi, T.2    Iwabuchi, S.3
  • 104
    • 0035844711 scopus 로고    scopus 로고
    • Formation of thermally induced aggregates of the soya globulin beta-conglycinin
    • E.N. Mills, L. Huang, T.R. Noel, A.P. Gunning, and V.J. Morris Formation of thermally induced aggregates of the soya globulin beta-conglycinin Biochim Biophys Acta 1547 2001 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
  • 105
    • 0038644459 scopus 로고    scopus 로고
    • Thermally induced structural changes in glycinin, the 11S globulin of soya bean (Glycine max) - An in situ spectroscopic study
    • E.N. Mills, N.A. Marigheto, N. Wellner, S.A. Fairhurst, J.A. Jenkins, and R. Mann Thermally induced structural changes in glycinin, the 11S globulin of soya bean (Glycine max) - an in situ spectroscopic study Biochim Biophys Acta 1648 2003 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    Jenkins, J.A.5    Mann, R.6
  • 106
    • 0019872622 scopus 로고
    • Mechanism of protein stabilization by glycerol: Preferential hydration in glycerol-water mixtures
    • K. Gekko, and S.N. Timasheff Mechanism of protein stabilization by glycerol: preferential hydration in glycerol-water mixtures Biochemistry 20 1981 4667 4676
    • (1981) Biochemistry , vol.20 , pp. 4667-4676
    • Gekko, K.1    Timasheff, S.N.2
  • 107
    • 0033582479 scopus 로고    scopus 로고
    • Heat-induced conformational changes of Ara h 1, a major peanut allergen, do not affect its allergenic properties
    • S.J. Koppelman, C.A. Bruijnzeel-Koomen, M. Hessing, and H.H. de Jongh Heat-induced conformational changes of Ara h 1, a major peanut allergen, do not affect its allergenic properties J Biol Chem 274 1999 4770 4777
    • (1999) J Biol Chem , vol.274 , pp. 4770-4777
    • Koppelman, S.J.1    Bruijnzeel-Koomen, C.A.2    Hessing, M.3    De Jongh, H.H.4
  • 108
    • 0030474676 scopus 로고    scopus 로고
    • Glycation decreases the stability of the triple-helical strands of fibrous collagen against proteolytic degradation by pepsin in a specific temperature range
    • S.F. Tian, S. Toda, H. Higashino, and S. Matsumura Glycation decreases the stability of the triple-helical strands of fibrous collagen against proteolytic degradation by pepsin in a specific temperature range J Biochem (Tokyo) 120 1996 1153 1162
    • (1996) J Biochem (Tokyo) , vol.120 , pp. 1153-1162
    • Tian, S.F.1    Toda, S.2    Higashino, H.3    Matsumura, S.4
  • 110
    • 0037816654 scopus 로고    scopus 로고
    • Linking peanut allergenicity to the processes of maturation, curing, and roasting
    • S.Y. Chung, C.L. Butts, S.J. Maleki, and E.T. Champagne Linking peanut allergenicity to the processes of maturation, curing, and roasting J Agric Food Chem 51 2003 4273 4277
    • (2003) J Agric Food Chem , vol.51 , pp. 4273-4277
    • Chung, S.Y.1    Butts, C.L.2    Maleki, S.J.3    Champagne, E.T.4
  • 111
    • 2342525840 scopus 로고    scopus 로고
    • A classification of plant food allergens
    • H. Breiteneder, and C. Radauer A classification of plant food allergens J Allergy Clin Immunol 113 2004 821 830
    • (2004) J Allergy Clin Immunol , vol.113 , pp. 821-830
    • Breiteneder, H.1    Radauer, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.