메뉴 건너뛰기




Volumn 81, Issue 4, 2013, Pages 545-554

Assessment of 3D models for allergen research

Author keywords

Allergenic proteins; IgE epitopes; Structural database of allergenic proteins; Template based modeling

Indexed keywords

ALLERGEN; IMMUNOGLOBULIN E; LATEX; SOYASAPOGENOL A;

EID: 84874805505     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.24239     Document Type: Article
Times cited : (17)

References (91)
  • 2
    • 33846631464 scopus 로고    scopus 로고
    • Bioinformatics approaches to classifying allergens and predicting cross-reactivity
    • Schein CH, Ivanciuc O, Braun W. Bioinformatics approaches to classifying allergens and predicting cross-reactivity. Immunol Allergy Clin N Am 2007; 27: 1-27.
    • (2007) Immunol Allergy Clin N Am , vol.27 , pp. 1-27
    • Schein, C.H.1    Ivanciuc, O.2    Braun, W.3
  • 3
    • 67249164480 scopus 로고    scopus 로고
    • Cross-reactivity of pollen and food allergens: soybean Gly m 4 is a member of the Bet v 1 superfamily and closely resembles yellow lupine proteins
    • Berkner H, Neudecker P, Mittag D, Ballmer-Weber BK, Schweimer K, Vieths S, Rosch P. Cross-reactivity of pollen and food allergens: soybean Gly m 4 is a member of the Bet v 1 superfamily and closely resembles yellow lupine proteins. Biosci Rep 2009; 29: 183-192.
    • (2009) Biosci Rep , vol.29 , pp. 183-192
    • Berkner, H.1    Neudecker, P.2    Mittag, D.3    Ballmer-Weber, B.K.4    Schweimer, K.5    Vieths, S.6    Rosch, P.7
  • 4
    • 68749117388 scopus 로고    scopus 로고
    • Linear IgE-epitope mapping and comparative structural homology modeling of hazelnut and English walnut 11S globulins
    • Robotham JM, Hoffman GG, Teuber SS, Beyer K, Sampson HA, Sathe SK, Roux KH. Linear IgE-epitope mapping and comparative structural homology modeling of hazelnut and English walnut 11S globulins. Mol Immunol 2009; 46: 2975-2984.
    • (2009) Mol Immunol , vol.46 , pp. 2975-2984
    • Robotham, J.M.1    Hoffman, G.G.2    Teuber, S.S.3    Beyer, K.4    Sampson, H.A.5    Sathe, S.K.6    Roux, K.H.7
  • 6
    • 77954352242 scopus 로고    scopus 로고
    • Molecular and immunological characterization of Can f 4: a dog dander allergen cross-reactive with a 23 kDa odorant-binding protein in cow dander
    • Mattsson L, Lundgren T, Olsson P, Sundberg M, Lidholm J. Molecular and immunological characterization of Can f 4: a dog dander allergen cross-reactive with a 23 kDa odorant-binding protein in cow dander. Clin Exp Allergy 2010; 40: 1276-1287.
    • (2010) Clin Exp Allergy , vol.40 , pp. 1276-1287
    • Mattsson, L.1    Lundgren, T.2    Olsson, P.3    Sundberg, M.4    Lidholm, J.5
  • 7
    • 82955247856 scopus 로고    scopus 로고
    • Computationally predicted IgE epitopes of walnut allergens contribute to cross-reactivity with peanuts
    • Maleki SJ, Teuber SS, Cheng H, Chen D, Comstock SS, Ruan S, Schein CH. Computationally predicted IgE epitopes of walnut allergens contribute to cross-reactivity with peanuts. Allergy 2011; 66: 1522-1529.
    • (2011) Allergy , vol.66 , pp. 1522-1529
    • Maleki, S.J.1    Teuber, S.S.2    Cheng, H.3    Chen, D.4    Comstock, S.S.5    Ruan, S.6    Schein, C.H.7
  • 9
    • 79955953910 scopus 로고    scopus 로고
    • Epitope grafting, re-creating a conformational Bet v 1 antibody epitope on the surface of the homologous apple allergen Mal d 1
    • Holm J, Ferreras M, Ipsen H, Wurtzen PA, Gajhede M, Larsen JN, Lund K, Spangfort MD. Epitope grafting, re-creating a conformational Bet v 1 antibody epitope on the surface of the homologous apple allergen Mal d 1. J Biol Chem 2011; 286: 17569-17578.
    • (2011) J Biol Chem , vol.286 , pp. 17569-17578
    • Holm, J.1    Ferreras, M.2    Ipsen, H.3    Wurtzen, P.A.4    Gajhede, M.5    Larsen, J.N.6    Lund, K.7    Spangfort, M.D.8
  • 11
    • 77955415947 scopus 로고    scopus 로고
    • Characterization of IgE-binding epitopes of peanut (Arachis hypogaea) PNA lectin allergen cross-reacting with other structurally related legume lectins
    • Rouge P, Culerrier R, Granier C, Rance F, Barre A. Characterization of IgE-binding epitopes of peanut (Arachis hypogaea) PNA lectin allergen cross-reacting with other structurally related legume lectins. Mol Immunol 2010; 47: 2359-2366.
    • (2010) Mol Immunol , vol.47 , pp. 2359-2366
    • Rouge, P.1    Culerrier, R.2    Granier, C.3    Rance, F.4    Barre, A.5
  • 12
  • 13
    • 42149144705 scopus 로고    scopus 로고
    • Three-dimensional structure of the cross-reactive pollen allergen Che a 3: visualizing cross-reactivity on the molecular surfaces of weed, grass, and tree pollen allergens
    • Verdino P, Barderas R, Villalba M, Westritschnig K, Valenta R, Rodriguez R, Keller W. Three-dimensional structure of the cross-reactive pollen allergen Che a 3: visualizing cross-reactivity on the molecular surfaces of weed, grass, and tree pollen allergens. J Immunol 2008; 180: 2313-2321.
    • (2008) J Immunol , vol.180 , pp. 2313-2321
    • Verdino, P.1    Barderas, R.2    Villalba, M.3    Westritschnig, K.4    Valenta, R.5    Rodriguez, R.6    Keller, W.7
  • 14
    • 80053568367 scopus 로고    scopus 로고
    • Prediction of IgE-binding epitopes by means of allergen surface comparison and correlation to cross-reactivity
    • Dall'Antonia F, Gieras A, Devanaboyina SC, Valenta R, Keller W. Prediction of IgE-binding epitopes by means of allergen surface comparison and correlation to cross-reactivity. J Allergy Clin Immunol 2011; 128: 872-879e878.
    • (2011) J Allergy Clin Immunol , vol.128
    • Dall'Antonia, F.1    Gieras, A.2    Devanaboyina, S.C.3    Valenta, R.4    Keller, W.5
  • 18
    • 79960301160 scopus 로고    scopus 로고
    • Mechanisms of allergen-antibody interaction of cockroach allergen Bla g 2 with monoclonal antibodies that inhibit IgE antibody binding
    • Glesner J, Wunschmann S, Li M, Gustchina A, Wlodawer A, Himly M, Chapman MD, Pomes A. Mechanisms of allergen-antibody interaction of cockroach allergen Bla g 2 with monoclonal antibodies that inhibit IgE antibody binding. PLoS One 2011; 6: e22223.
    • (2011) PLoS One , vol.6
    • Glesner, J.1    Wunschmann, S.2    Li, M.3    Gustchina, A.4    Wlodawer, A.5    Himly, M.6    Chapman, M.D.7    Pomes, A.8
  • 20
    • 67650493168 scopus 로고    scopus 로고
    • Utility of animal models for predicting human allergenicity
    • Lehrer SB, McClain S. Utility of animal models for predicting human allergenicity. Regul Toxicol Pharmacol 2009; 54 (Suppl 3): S46-S51.
    • (2009) Regul Toxicol Pharmacol , vol.54 , Issue.SUPPL 3
    • Lehrer, S.B.1    McClain, S.2
  • 21
    • 67649230179 scopus 로고    scopus 로고
    • Safety assessment of biotechnology products for potential risk of food allergy: implications of new research
    • Selgrade MK, Bowman CC, Ladics GS, Privalle L, Laessig SA. Safety assessment of biotechnology products for potential risk of food allergy: implications of new research. Toxicol Sci 2009; 110: 31-39.
    • (2009) Toxicol Sci , vol.110 , pp. 31-39
    • Selgrade, M.K.1    Bowman, C.C.2    Ladics, G.S.3    Privalle, L.4    Laessig, S.A.5
  • 24
    • 0037251966 scopus 로고    scopus 로고
    • SDAP: Database and computational tools for allergenic proteins
    • Ivanciuc O, Schein CH, Braun W. SDAP: Database and computational tools for allergenic proteins. Nucleic Acids Res 2003; 31: 359-362.
    • (2003) Nucleic Acids Res , vol.31 , pp. 359-362
    • Ivanciuc, O.1    Schein, C.H.2    Braun, W.3
  • 25
    • 81555235468 scopus 로고    scopus 로고
    • In shape--the art of mapping conformational epitopes
    • Gadermaier E. In shape--the art of mapping conformational epitopes. Int Arch Allergy Immunol 2012; 157: 321-322.
    • (2012) Int Arch Allergy Immunol , vol.157 , pp. 321-322
    • Gadermaier, E.1
  • 26
    • 48149098909 scopus 로고    scopus 로고
    • Comprehensive 3D-modeling of allergenic proteins and amino acid composition of potential conformational IgE epitopes
    • Oezguen N, Zhou B, Negi SS, Ivanciuc O, Schein CH, Labesse G, Braun W. Comprehensive 3D-modeling of allergenic proteins and amino acid composition of potential conformational IgE epitopes. Mol Immunol 2008; 45: 3740-3747.
    • (2008) Mol Immunol , vol.45 , pp. 3740-3747
    • Oezguen, N.1    Zhou, B.2    Negi, S.S.3    Ivanciuc, O.4    Schein, C.H.5    Labesse, G.6    Braun, W.7
  • 27
    • 80855132939 scopus 로고    scopus 로고
    • Assessment of template based protein structure predictions in CASP9
    • Mariani V, Kiefer F, Schmidt T, Haas J, Schwede T. Assessment of template based protein structure predictions in CASP9. Proteins 2011; 79 (Suppl 10): 37-58.
    • (2011) Proteins , vol.79 , Issue.SUPPL 10 , pp. 37-58
    • Mariani, V.1    Kiefer, F.2    Schmidt, T.3    Haas, J.4    Schwede, T.5
  • 28
    • 74249104499 scopus 로고    scopus 로고
    • Fast and accurate automatic structure prediction with HHpred
    • Hildebrand A, Remmert M, Biegert A, Soding J. Fast and accurate automatic structure prediction with HHpred. Proteins 2009; 77 (Suppl 9): 128-132.
    • (2009) Proteins , vol.77 , Issue.SUPPL 9 , pp. 128-132
    • Hildebrand, A.1    Remmert, M.2    Biegert, A.3    Soding, J.4
  • 29
    • 77954065271 scopus 로고    scopus 로고
    • I-TASSER: a unified platform for automated protein structure and function prediction
    • Roy A, Kucukural A, Zhang Y. I-TASSER: a unified platform for automated protein structure and function prediction. Nat Protoc 2010; 5: 725-738.
    • (2010) Nat Protoc , vol.5 , pp. 725-738
    • Roy, A.1    Kucukural, A.2    Zhang, Y.3
  • 30
    • 84855672321 scopus 로고    scopus 로고
    • Template-based protein structure modeling using TASSER(VMT)
    • Zhou H, Skolnick J. Template-based protein structure modeling using TASSER(VMT). Proteins 2012; 80: 352-361.
    • (2012) Proteins , vol.80 , pp. 352-361
    • Zhou, H.1    Skolnick, J.2
  • 32
  • 35
    • 59349114360 scopus 로고    scopus 로고
    • Crystal structures of mite allergens Der f 1 and Der p 1 reveal differences in surface-exposed residues that may influence antibody binding
    • Chruszcz M, Chapman MD, Vailes LD, Stura EA, Saint-Remy JM, Minor W, Pomes A. Crystal structures of mite allergens Der f 1 and Der p 1 reveal differences in surface-exposed residues that may influence antibody binding. J Mol Biol 2009; 386: 520-530.
    • (2009) J Mol Biol , vol.386 , pp. 520-530
    • Chruszcz, M.1    Chapman, M.D.2    Vailes, L.D.3    Stura, E.A.4    Saint-Remy, J.M.5    Minor, W.6    Pomes, A.7
  • 37
    • 79958149376 scopus 로고    scopus 로고
    • Ara h 2: crystal structure and IgE binding distinguish two subpopulations of peanut allergic patients by epitope diversity
    • Mueller GA, Gosavi RA, Pomés A, Wünschmann S, Moon AF, London RE, Pedersen LC. Ara h 2: crystal structure and IgE binding distinguish two subpopulations of peanut allergic patients by epitope diversity. Allergy 2011; 66: 878-885.
    • (2011) Allergy , vol.66 , pp. 878-885
    • Mueller, G.A.1    Gosavi, R.A.2    Pomés, A.3    Wünschmann, S.4    Moon, A.F.5    London, R.E.6    Pedersen, L.C.7
  • 38
    • 59149087891 scopus 로고    scopus 로고
    • Structures of two major allergens, Bla g 4 and Per a 4, from cockroaches and their IgE binding epitopes
    • Tan YW, Chan SL, Ong TC, Yit le Y, Tiong YS, Chew FT, Sivaraman J, Mok YK. Structures of two major allergens, Bla g 4 and Per a 4, from cockroaches and their IgE binding epitopes. J Biol Chem 2009; 284: 3148-3157.
    • (2009) J Biol Chem , vol.284 , pp. 3148-3157
    • Tan, Y.W.1    Chan, S.L.2    Ong, T.C.3    Yit le, Y.4    Tiong, Y.S.5    Chew, F.T.6    Sivaraman, J.7    Mok, Y.K.8
  • 39
    • 62649119139 scopus 로고    scopus 로고
    • Multifunctionality and mechanism of ligand binding in a mosquito antiinflammatory protein
    • Calvo E, Mans BJ, Ribeiro JM, Andersen JF. Multifunctionality and mechanism of ligand binding in a mosquito antiinflammatory protein. Proc Natl Acad Sci USA 2009; 106: 3728-3733.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 3728-3733
    • Calvo, E.1    Mans, B.J.2    Ribeiro, J.M.3    Andersen, J.F.4
  • 40
    • 0035967880 scopus 로고    scopus 로고
    • FUGUE: sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties
    • Shi J, Blundell TL, Mizuguchi K. FUGUE: sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties. J Mol Biol 2001; 310: 243-257.
    • (2001) J Mol Biol , vol.310 , pp. 243-257
    • Shi, J.1    Blundell, T.L.2    Mizuguchi, K.3
  • 41
    • 0038634975 scopus 로고    scopus 로고
    • Improvement of the GenTHREADER method for genomic fold recognition
    • McGuffin LJ, Jones DT. Improvement of the GenTHREADER method for genomic fold recognition. Bioinformatics 2003; 19: 874-881.
    • (2003) Bioinformatics , vol.19 , pp. 874-881
    • McGuffin, L.J.1    Jones, D.T.2
  • 42
    • 0034595501 scopus 로고    scopus 로고
    • Enhanced genome annotation using structural profiles in the program 3D-PSSM
    • Kelley LA, MacCallum RM, Sternberg MJ. Enhanced genome annotation using structural profiles in the program 3D-PSSM. J Mol Biol 2000; 299: 499-520.
    • (2000) J Mol Biol , vol.299 , pp. 499-520
    • Kelley, L.A.1    MacCallum, R.M.2    Sternberg, M.J.3
  • 43
    • 0035165967 scopus 로고    scopus 로고
    • A database and tools for 3-D protein structure comparison and alignment using the combinatorial extension (CE) algorithm
    • Shindyalov IN, Bourne PE. A database and tools for 3-D protein structure comparison and alignment using the combinatorial extension (CE) algorithm. Nucleic Acids Res 2001; 29: 228-229.
    • (2001) Nucleic Acids Res , vol.29 , pp. 228-229
    • Shindyalov, I.N.1    Bourne, P.E.2
  • 44
    • 1642303342 scopus 로고    scopus 로고
    • Using property based sequence motifs and 3D modeling to determine structure and functional regions of proteins
    • Ivanciuc O, Oezguen N, Mathura VS, Schein CH, Xu Y, Braun W. Using property based sequence motifs and 3D modeling to determine structure and functional regions of proteins. Curr Med Chem 2004; 11: 583-593.
    • (2004) Curr Med Chem , vol.11 , pp. 583-593
    • Ivanciuc, O.1    Oezguen, N.2    Mathura, V.S.3    Schein, C.H.4    Xu, Y.5    Braun, W.6
  • 45
    • 0033824470 scopus 로고    scopus 로고
    • DaliLite workbench for protein structure comparison
    • Holm L, Park J. DaliLite workbench for protein structure comparison. Bioinformatics 2000; 16: 566-567.
    • (2000) Bioinformatics , vol.16 , pp. 566-567
    • Holm, L.1    Park, J.2
  • 46
    • 3042581007 scopus 로고    scopus 로고
    • Flexible structure alignment by chaining aligned fragment pairs allowing twists
    • Ye Y, Godzik A. Flexible structure alignment by chaining aligned fragment pairs allowing twists. Bioinformatics 2003; 19 (Suppl 2): ii246-ii255.
    • (2003) Bioinformatics , vol.19 , Issue.SUPPL 2
    • Ye, Y.1    Godzik, A.2
  • 47
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: a program for display and analysis of macromolecular structures
    • 29-32.
    • Koradi R, Billeter M, Wuthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J Mol Graph 1996; 14: 51-55, 29-32.
    • (1996) J Mol Graph , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 48
    • 0001528720 scopus 로고    scopus 로고
    • Exact and efficient analytical calculation of the accessible surface areas and their gradients for macromolecules
    • Fraczkiewicz R, Braun W. Exact and efficient analytical calculation of the accessible surface areas and their gradients for macromolecules. J Comput Chem 1998; 19: 319-333.
    • (1998) J Comput Chem , vol.19 , pp. 319-333
    • Fraczkiewicz, R.1    Braun, W.2
  • 49
    • 79551613290 scopus 로고    scopus 로고
    • Toward the estimation of the absolute quality of individual protein structure models
    • Benkert P, Biasini M, Schwede T. Toward the estimation of the absolute quality of individual protein structure models. Bioinformatics 2011; 27: 343-350.
    • (2011) Bioinformatics , vol.27 , pp. 343-350
    • Benkert, P.1    Biasini, M.2    Schwede, T.3
  • 50
    • 34547566446 scopus 로고    scopus 로고
    • ProSA-web: interactive web service for the recognition of errors in three-dimensional structures of proteins
    • Wiederstein M, Sippl MJ. ProSA-web: interactive web service for the recognition of errors in three-dimensional structures of proteins. Nucleic Acids Res 2007; 35: W407-410.
    • (2007) Nucleic Acids Res , vol.35
    • Wiederstein, M.1    Sippl, M.J.2
  • 51
    • 0025830469 scopus 로고
    • A method to identify protein sequences that fold into a known three-dimensional structure
    • Bowie JU, Luthy R, Eisenberg D. A method to identify protein sequences that fold into a known three-dimensional structure. Science 1991; 253: 164-170.
    • (1991) Science , vol.253 , pp. 164-170
    • Bowie, J.U.1    Luthy, R.2    Eisenberg, D.3
  • 53
    • 0029379568 scopus 로고
    • beta-1,3-Glucanase is highly-expressed in laticifers of Hevea brasiliensis
    • Chye ML, Cheung KY. beta-1, 3-Glucanase is highly-expressed in laticifers of Hevea brasiliensis. Plant Mol Biol 1995; 29: 397-402.
    • (1995) Plant Mol Biol , vol.29 , pp. 397-402
    • Chye, M.L.1    Cheung, K.Y.2
  • 54
    • 0032488931 scopus 로고    scopus 로고
    • Crystal structure of barley 1,3-1,4-beta-glucanase at 2.0-A resolution and comparison with Bacillus 1,3-1,4-beta-glucanase
    • Muller JJ, Thomsen KK, Heinemann U. Crystal structure of barley 1, 3-1, 4-beta-glucanase at 2.0-A resolution and comparison with Bacillus 1, 3-1, 4-beta-glucanase. J Biol Chem 1998; 273: 3438-3446.
    • (1998) J Biol Chem , vol.273 , pp. 3438-3446
    • Muller, J.J.1    Thomsen, K.K.2    Heinemann, U.3
  • 55
    • 27744566919 scopus 로고    scopus 로고
    • Common physical-chemical properties correlate with similar structure of the IgE epitopes of peanut allergens
    • Schein CH, Ivanciuc O, Braun W. Common physical-chemical properties correlate with similar structure of the IgE epitopes of peanut allergens. J Agric Food Chem 2005; 53: 8752-8759.
    • (2005) J Agric Food Chem , vol.53 , pp. 8752-8759
    • Schein, C.H.1    Ivanciuc, O.2    Braun, W.3
  • 56
    • 0041819527 scopus 로고    scopus 로고
    • Structure of a specific alcohol-binding site defined by the odorant binding protein LUSH from Drosophila melanogaster
    • Kruse SW, Zhao R, Smith DP, Jones DN. Structure of a specific alcohol-binding site defined by the odorant binding protein LUSH from Drosophila melanogaster. Nat Struct Biol 2003; 10: 694-700.
    • (2003) Nat Struct Biol , vol.10 , pp. 694-700
    • Kruse, S.W.1    Zhao, R.2    Smith, D.P.3    Jones, D.N.4
  • 58
    • 0028807372 scopus 로고
    • Recombinant peanut allergen Ara h I expression and IgE binding in patients with peanut hypersensitivity
    • Burks AW, Cockrell G, Stanley JS, Helm RM, Bannon GA. Recombinant peanut allergen Ara h I expression and IgE binding in patients with peanut hypersensitivity. J Clin Invest 1995; 96: 1715-1721.
    • (1995) J Clin Invest , vol.96 , pp. 1715-1721
    • Burks, A.W.1    Cockrell, G.2    Stanley, J.S.3    Helm, R.M.4    Bannon, G.A.5
  • 59
    • 0034307511 scopus 로고    scopus 로고
    • N-Glycan analysis by matrix-assisted laser desorption/ionization mass spectrometry of electrophoretically separated nonmammalian proteins: application to peanut allergen Ara h 1 and olive pollen allergen Ole e 1
    • Kolarich D, Altmann F. N-Glycan analysis by matrix-assisted laser desorption/ionization mass spectrometry of electrophoretically separated nonmammalian proteins: application to peanut allergen Ara h 1 and olive pollen allergen Ole e 1. Anal Biochem 2000; 285: 64-75.
    • (2000) Anal Biochem , vol.285 , pp. 64-75
    • Kolarich, D.1    Altmann, F.2
  • 60
    • 84867956722 scopus 로고    scopus 로고
    • Ara h 1 structure is retained after roasting and is important for enhanced binding t lgE
    • Nesbit JB, Hurlburt BK, Schein CH, Cheng H, Wei H, Maleki SJ. Ara h 1 structure is retained after roasting and is important for enhanced binding t lgE. Mol Nutr Res 2012; 56: 1739-1747.
    • (2012) Mol Nutr Res , vol.56 , pp. 1739-1747
    • Nesbit, J.B.1    Hurlburt, B.K.2    Schein, C.H.3    Cheng, H.4    Wei, H.5    Maleki, S.J.6
  • 62
    • 64449083074 scopus 로고    scopus 로고
    • Mapping of IgE-binding epitopes on the major latex allergen Hev b 2 and the cross-reacting 1,3beta-glucanase fruit allergens as a molecular basis for the latex-fruit syndrome
    • Barre A, Culerrier R, Granier C, Selman L, Peumans WJ, Van Damme EJ, Bienvenu F, Bienvenu J, Rouge P. Mapping of IgE-binding epitopes on the major latex allergen Hev b 2 and the cross-reacting 1, 3beta-glucanase fruit allergens as a molecular basis for the latex-fruit syndrome. Mol Immunol 2009; 46: 1595-1604.
    • (2009) Mol Immunol , vol.46 , pp. 1595-1604
    • Barre, A.1    Culerrier, R.2    Granier, C.3    Selman, L.4    Peumans, W.J.5    Van Damme, E.J.6    Bienvenu, F.7    Bienvenu, J.8    Rouge, P.9
  • 63
    • 25644434412 scopus 로고    scopus 로고
    • A novel approach for investigation of specific and cross-reactive IgE epitopes on Bet v 1 and homologous food allergens in individual patients
    • Mittag D, Batori V, Neudecker P, Wiche R, Friis EP, Ballmer-Weber BK, Vieths S, Roggen EL. A novel approach for investigation of specific and cross-reactive IgE epitopes on Bet v 1 and homologous food allergens in individual patients. Mol Immunol 2006; 43: 268-278.
    • (2006) Mol Immunol , vol.43 , pp. 268-278
    • Mittag, D.1    Batori, V.2    Neudecker, P.3    Wiche, R.4    Friis, E.P.5    Ballmer-Weber, B.K.6    Vieths, S.7    Roggen, E.L.8
  • 64
    • 0034096545 scopus 로고    scopus 로고
    • The refined structure of canavalin from jack bean in two crystal forms at 2.1 and 2.0 A resolution
    • Ko TP, Day J, McPherson A. The refined structure of canavalin from jack bean in two crystal forms at 2.1 and 2.0 A resolution. Acta Crystallogr D Biol Crystallogr 2000; 56 (Pt 4): 411-420.
    • (2000) Acta Crystallogr D Biol Crystallogr , vol.56 , Issue.PART 4 , pp. 411-420
    • Ko, T.P.1    Day, J.2    McPherson, A.3
  • 66
    • 80051563770 scopus 로고    scopus 로고
    • Abundance and functional roles of intrinsic disorder in allergenic proteins and allergen representative peptides
    • Xue B, Soeria-Atmadja D, Gustafsson MG, Hammerling U, Dunker AK, Uversky VN. Abundance and functional roles of intrinsic disorder in allergenic proteins and allergen representative peptides. Proteins 2011; 79: 2595-2606.
    • (2011) Proteins , vol.79 , pp. 2595-2606
    • Xue, B.1    Soeria-Atmadja, D.2    Gustafsson, M.G.3    Hammerling, U.4    Dunker, A.K.5    Uversky, V.N.6
  • 68
    • 0344011459 scopus 로고    scopus 로고
    • Solution structure of RicC3, a 2S albumin storage protein from Ricinus communis
    • Pantoja-Uceda D, Bruix M, Gimenez-Gallego G, Rico M, Santoro J. Solution structure of RicC3, a 2S albumin storage protein from Ricinus communis. Biochemistry 2003; 42: 13839-13847.
    • (2003) Biochemistry , vol.42 , pp. 13839-13847
    • Pantoja-Uceda, D.1    Bruix, M.2    Gimenez-Gallego, G.3    Rico, M.4    Santoro, J.5
  • 70
    • 51849161510 scopus 로고    scopus 로고
    • Soy allergy due to cross reactions to major birch pollen allergen Bet v 1
    • Kleine-Tebbe J, Herold DA, Vieths S. Soy allergy due to cross reactions to major birch pollen allergen Bet v 1. Allergologie 2008; 31: 303-313.
    • (2008) Allergologie , vol.31 , pp. 303-313
    • Kleine-Tebbe, J.1    Herold, D.A.2    Vieths, S.3
  • 71
    • 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
    • Kleine-Tebbe J, Vogel L, Crowell DN, Haustein UF, Vieths S. Severe oral allergy syndrome and anaphylactic reactions caused by a Bet v 1-related PR-10 protein in soybean, SAM22. J Allergy Clin Immunol 2002; 110: 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
  • 73
    • 79959973530 scopus 로고    scopus 로고
    • Epitope mapping and structural analysis of the anti-Der p 1 monoclonal antibody: insight into therapeutic potential
    • Dai YC, Chuang WJ, Chua KY, Shieh CC, Wang JY. Epitope mapping and structural analysis of the anti-Der p 1 monoclonal antibody: insight into therapeutic potential. J Mol Med (Berl) 2011; 89: 701-712.
    • (2011) J Mol Med (Berl) , vol.89 , pp. 701-712
    • Dai, Y.C.1    Chuang, W.J.2    Chua, K.Y.3    Shieh, C.C.4    Wang, J.Y.5
  • 79
    • 84859626384 scopus 로고    scopus 로고
    • Identification of critical amino acids in an immunodominant IgE epitope of Pen c 13, a major allergen from Penicillium citrinum
    • Chen JC, Chiu LL, Lee KL, Huang WN, Chuang JG, Liao HK, Chow LP. Identification of critical amino acids in an immunodominant IgE epitope of Pen c 13, a major allergen from Penicillium citrinum. PLoS One 2012; 7: e34627.
    • (2012) PLoS One , vol.7
    • Chen, J.C.1    Chiu, L.L.2    Lee, K.L.3    Huang, W.N.4    Chuang, J.G.5    Liao, H.K.6    Chow, L.P.7
  • 80
    • 77952314827 scopus 로고    scopus 로고
    • Mapping of a conformational epitope on the cashew allergen Ana o 2: a discontinuous large subunit epitope dependent upon homologous or heterologous small subunit association
    • Xia L, Willison LN, Porter L, Robotham JM, Teuber SS, Sathe SK, Roux KH. Mapping of a conformational epitope on the cashew allergen Ana o 2: a discontinuous large subunit epitope dependent upon homologous or heterologous small subunit association. Mol Immunol 2010; 47: 1808-1816.
    • (2010) Mol Immunol , vol.47 , pp. 1808-1816
    • Xia, L.1    Willison, L.N.2    Porter, L.3    Robotham, J.M.4    Teuber, S.S.5    Sathe, S.K.6    Roux, K.H.7
  • 82
    • 37449034027 scopus 로고    scopus 로고
    • Vicilin allergens of peanut and tree nuts (walnut, hazelnut and cashew nut) share structurally related IgE-binding epitopes
    • Barre A, Sordet C, Culerrier R, Rance F, Didier A, Rouge P. Vicilin allergens of peanut and tree nuts (walnut, hazelnut and cashew nut) share structurally related IgE-binding epitopes. Mol Immunol 2008; 45: 1231-1240.
    • (2008) Mol Immunol , vol.45 , pp. 1231-1240
    • Barre, A.1    Sordet, C.2    Culerrier, R.3    Rance, F.4    Didier, A.5    Rouge, P.6
  • 84
    • 80052819877 scopus 로고    scopus 로고
    • Epitope mapping of a 95 kDa antigen in complex with antibody by solution-phase amide backbone hydrogen/deuterium exchange monitored by Fourier transform ion cyclotron resonance mass spectrometry
    • Zhang Q, Willison LN, Tripathi P, Sathe SK, Roux KH, Emmett MR, Blakney GT, Zhang HM, Marshall AG. Epitope mapping of a 95 kDa antigen in complex with antibody by solution-phase amide backbone hydrogen/deuterium exchange monitored by Fourier transform ion cyclotron resonance mass spectrometry. Anal Chem 2011; 83: 7129-7136.
    • (2011) Anal Chem , vol.83 , pp. 7129-7136
    • Zhang, Q.1    Willison, L.N.2    Tripathi, P.3    Sathe, S.K.4    Roux, K.H.5    Emmett, M.R.6    Blakney, G.T.7    Zhang, H.M.8    Marshall, A.G.9
  • 85
    • 80855147432 scopus 로고    scopus 로고
    • Automated protein structure modeling in CASP9 by I-TASSER pipeline combined with QUARK-based ab initio folding and FG-MD-based structure refinement
    • Xu D, Zhang J, Roy A, Zhang Y. Automated protein structure modeling in CASP9 by I-TASSER pipeline combined with QUARK-based ab initio folding and FG-MD-based structure refinement. Proteins 2011; 79 (Suppl 10): 147-160.
    • (2011) Proteins , vol.79 , Issue.SUPPL 10 , pp. 147-160
    • Xu, D.1    Zhang, J.2    Roy, A.3    Zhang, Y.4
  • 86
    • 80054685109 scopus 로고    scopus 로고
    • Critical assessment of methods of protein structure prediction (CASP)--round IX
    • Moult J, Fidelis K, Kryshtafovych A, Tramontano A. Critical assessment of methods of protein structure prediction (CASP)--round IX. Proteins 2011; 79 (Suppl 10): 1-5.
    • (2011) Proteins , vol.79 , Issue.SUPPL 10 , pp. 1-5
    • Moult, J.1    Fidelis, K.2    Kryshtafovych, A.3    Tramontano, A.4
  • 87
    • 80855144748 scopus 로고    scopus 로고
    • CASP9 results compared to those of previous CASP experiments
    • Kryshtafovych A, Fidelis K, Moult J. CASP9 results compared to those of previous CASP experiments. Proteins 2011; 79 (Suppl 10): 196-207.
    • (2011) Proteins , vol.79 , Issue.SUPPL 10 , pp. 196-207
    • Kryshtafovych, A.1    Fidelis, K.2    Moult, J.3
  • 88
    • 82655175485 scopus 로고    scopus 로고
    • A comprehensive overview of computational protein disorder prediction methods
    • Deng X, Eickholt J, Cheng J. A comprehensive overview of computational protein disorder prediction methods. Mol Biosyst 2012; 8: 114-121.
    • (2012) Mol Biosyst , vol.8 , pp. 114-121
    • Deng, X.1    Eickholt, J.2    Cheng, J.3
  • 89
    • 79959564695 scopus 로고    scopus 로고
    • The IntFOLD server: an integrated web resource for protein fold recognition, 3D model quality assessment, intrinsic disorder prediction, domain prediction and ligand binding site prediction
    • Roche DB, Buenavista MT, Tetchner SJ, McGuffin LJ. The IntFOLD server: an integrated web resource for protein fold recognition, 3D model quality assessment, intrinsic disorder prediction, domain prediction and ligand binding site prediction. Nucleic Acids Res 2011; 39: W171-176.
    • (2011) Nucleic Acids Res , vol.39
    • Roche, D.B.1    Buenavista, M.T.2    Tetchner, S.J.3    McGuffin, L.J.4
  • 90
    • 41449094497 scopus 로고    scopus 로고
    • Allergens are distributed into few protein families and possess a restricted number of biochemical functions
    • Radauer C, Bublin M, Wagner S, Mari A, Breiteneder H. Allergens are distributed into few protein families and possess a restricted number of biochemical functions. J Allergy Clin Immunol 2008; 121: 847-852.e847.
    • (2008) J Allergy Clin Immunol , vol.121
    • Radauer, C.1    Bublin, M.2    Wagner, S.3    Mari, A.4    Breiteneder, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.