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Volumn 129, Issue 3, 2002, Pages 189-197

Carbohydrate epitopes and their relevance for the diagnosis and treatment of allergic diseases

Author keywords

Carbohydrate epitopes; Diagnostic tests; IgE; Immunotherapy; Recombinant allergens

Indexed keywords

CARBOHYDRATE; EPITOPE; FUCOSE; IMMUNOGLOBULIN E ANTIBODY; MANNOSE; N ACETYLGLUCOSAMINE; XYLOSE;

EID: 0036436846     PISSN: 10182438     EISSN: None     Source Type: Journal    
DOI: 10.1159/000066770     Document Type: Review
Times cited : (184)

References (157)
  • 1
    • 0019859015 scopus 로고
    • Immunoglobulin E antibodies that crossreact with vegetable foods, pollen, and Hymenoptera venom
    • Aalberse RC, Koshte V, Clemens JG: Immunoglobulin E antibodies that crossreact with vegetable foods, pollen, and Hymenoptera venom. J Allergy Clin Immunol 1981;68:356-364.
    • (1981) J Allergy Clin Immunol , vol.68 , pp. 356-364
    • Aalberse, R.C.1    Koshte, V.2    Clemens, J.G.3
  • 2
    • 0026764006 scopus 로고
    • Interaction of lectins with human IgE: IgE-binding property and histamine-releasing activity of twelve plant lectins
    • Shibasaki M, Sumazaki R, Isoyama S, Takita H: Interaction of lectins with human IgE: IgE-binding property and histamine-releasing activity of twelve plant lectins. Int Arch Allergy Immunol 1992;98:18-25.
    • (1992) Int Arch Allergy Immunol , vol.98 , pp. 18-25
    • Shibasaki, M.1    Sumazaki, R.2    Isoyama, S.3    Takita, H.4
  • 4
    • 0024971782 scopus 로고
    • Sugar sequences of allergenically active oligosaccharide alcohols isolated from a large-molecular-size sea squirt antigen termed H-antigen
    • Ohta M, Shigeta S, Ono K, Takao T, Shimonishi Y, Oka S: Sugar sequences of allergenically active oligosaccharide alcohols isolated from a large-molecular-size sea squirt antigen termed H-antigen. Arch Biochem Biophys 1989;275:151-165.
    • (1989) Arch Biochem Biophys , vol.275 , pp. 151-165
    • Ohta, M.1    Shigeta, S.2    Ono, K.3    Takao, T.4    Shimonishi, Y.5    Oka, S.6
  • 5
    • 0025095623 scopus 로고
    • IgE-, IgA- and IgG-antibody responses to carbohydrate and protein antigens of Candida albicans in asthmatic children
    • Savolainen J, Viander M, Koivikko A: IgE-, IgA- and IgG-antibody responses to carbohydrate and protein antigens of Candida albicans in asthmatic children. Allergy 1990;45:54-63.
    • (1990) Allergy , vol.45 , pp. 54-63
    • Savolainen, J.1    Viander, M.2    Koivikko, A.3
  • 6
    • 0026712842 scopus 로고
    • Role of carbohydrate moieties in cross-reactivity between different components of Parietaria judaica pollen extract
    • Mucci N, Liberatore P, Federico R, Forlani F, Di Felice G, Afferni C, et al: Role of carbohydrate moieties in cross-reactivity between different components of Parietaria judaica pollen extract. Allergy 1992;47:424-430.
    • (1992) Allergy , vol.47 , pp. 424-430
    • Mucci, N.1    Liberatore, P.2    Federico, R.3    Forlani, F.4    Di Felice, G.5    Afferni, C.6
  • 7
    • 0027426870 scopus 로고
    • Fucose alpha 1,3-linked to the core region of glycoprotein N-glycans creates an important epitope for IgE from honeybee venom allergic individuals
    • Tretter V, Altmann F, Kubelka V, März L, Becker WM: Fucose alpha 1,3-linked to the core region of glycoprotein N-glycans creates an important epitope for IgE from honeybee venom allergic individuals. Int Arch Allergy Immunol 1993;102:259-266.
    • (1993) Int Arch Allergy Immunol , vol.102 , pp. 259-266
    • Tretter, V.1    Altmann, F.2    Kubelka, V.3    März, L.4    Becker, W.M.5
  • 8
    • 0028343779 scopus 로고
    • Allergens in Aspergillus fumigatus. I. Characterization of two different allergen extracts and evaluation of their stability and the importance of carbohydrate for IgE binding
    • Hansen MY, Wold JK, Smestad PB, Cohen EH, Karlsson-Borga A: Allergens in Aspergillus fumigatus. I. Characterization of two different allergen extracts and evaluation of their stability and the importance of carbohydrate for IgE binding. Allergy 1994;49:235-241.
    • (1994) Allergy , vol.49 , pp. 235-241
    • Hansen, M.Y.1    Wold, J.K.2    Smestad, P.B.3    Cohen, E.H.4    Karlsson-Borga, A.5
  • 10
    • 0029964855 scopus 로고    scopus 로고
    • Ubiquitous structures responsible for IgE cross-reactivity between tomato fruit and grass pollen allergens
    • Petersen A, Vieths S, Aulepp H, Schlaak M, Becker WM: Ubiquitous structures responsible for IgE cross-reactivity between tomato fruit and grass pollen allergens. J Allergy Clin Immunol 1996;98:805-815.
    • (1996) J Allergy Clin Immunol , vol.98 , pp. 805-815
    • Petersen, A.1    Vieths, S.2    Aulepp, H.3    Schlaak, M.4    Becker, W.M.5
  • 11
    • 0029954108 scopus 로고    scopus 로고
    • Allergic sensitization to native and heated celery root in pollen-sensitive patients investigated by skin test and IgE binding
    • Jankiewicz A, Aulepp H, Baltes W, Bogl KW, Dehne LI, Zuberbier T, et al: Allergic sensitization to native and heated celery root in pollen-sensitive patients investigated by skin test and IgE binding. Int Arch Allergy Immunol 1996;111:268-278.
    • (1996) Int Arch Allergy Immunol , vol.111 , pp. 268-278
    • Jankiewicz, A.1    Aulepp, H.2    Baltes, W.3    Bogl, K.W.4    Dehne, L.I.5    Zuberbier, T.6
  • 13
    • 0032797422 scopus 로고    scopus 로고
    • Role of carbohydrate moieties in IgE binding to allergenic components of Cupressus arizonica pollen extract
    • Afferni C, Iacovacci P, Barletta B, Di Felice G, Tinghino R, Mari A, et al: Role of carbohydrate moieties in IgE binding to allergenic components of Cupressus arizonica pollen extract. Clin Exp Allergy 1999;29:1087-1094.
    • (1999) Clin Exp Allergy , vol.29 , pp. 1087-1094
    • Afferni, C.1    Iacovacci, P.2    Barletta, B.3    Di Felice, G.4    Tinghino, R.5    Mari, A.6
  • 15
    • 0032815622 scopus 로고    scopus 로고
    • Specific IgE to cross-reactive carbohydrate determinants strongly affect the in vitro diagnosis of allergic diseases
    • Mari A, Iacovacci P, Afferni C, Barletta B, Tinghino R, Di Felice G, et al: Specific IgE to cross-reactive carbohydrate determinants strongly affect the in vitro diagnosis of allergic diseases. J Allergy Clin Immunol 1999;103:1005-1011.
    • (1999) J Allergy Clin Immunol , vol.103 , pp. 1005-1011
    • Mari, A.1    Iacovacci, P.2    Afferni, C.3    Barletta, B.4    Tinghino, R.5    Di Felice, G.6
  • 16
    • 0032926720 scopus 로고    scopus 로고
    • IgE-binding and histamine-release capabilities of the main carbohydrate component isolated from the major allergen of olive tree pollen, Ole e 1
    • Batanero E, Crespo JF, Monsalve RI, Martin-Esteban M, Villalba M, Rodriguez R: IgE-binding and histamine-release capabilities of the main carbohydrate component isolated from the major allergen of olive tree pollen, Ole e 1. J Allergy Clin Immunol 1999;103:147-153.
    • (1999) J Allergy Clin Immunol , vol.103 , pp. 147-153
    • Batanero, E.1    Crespo, J.F.2    Monsalve, R.I.3    Martin-Esteban, M.4    Villalba, M.5    Rodriguez, R.6
  • 17
    • 0344631775 scopus 로고    scopus 로고
    • Involvement of carbohydrate epitopes in the IgE response of celery-allergic patients
    • Fötisch K, Altmann F, Haustein D, Vieths S: Involvement of carbohydrate epitopes in the IgE response of celery-allergic patients. Int Arch Allergy Immunol 1999;120:30-42.
    • (1999) Int Arch Allergy Immunol , vol.120 , pp. 30-42
    • Fötisch, K.1    Altmann, F.2    Haustein, D.3    Vieths, S.4
  • 18
    • 0033233118 scopus 로고    scopus 로고
    • Core alpha 1,3-fucose is a common modification of N-glycans in parasitic helminths and constitutes an important epitope for IgE from Haemonchus contortus infected sheep
    • van Die I, Gomord V, Kooyman FN, van den Berg TK, Cummings RD, Vervelde L: Core alpha 1,3-fucose is a common modification of N-glycans in parasitic helminths and constitutes an important epitope for IgE from Haemonchus contortus infected sheep. FEBS Lett 1999;463:189-193.
    • (1999) FEBS Lett , vol.463 , pp. 189-193
    • Van Die, I.1    Gomord, V.2    Kooyman, F.N.3    Van den Berg, T.K.4    Cummings, R.D.5    Vervelde, L.6
  • 19
    • 0033822839 scopus 로고    scopus 로고
    • Occurrence of IgE antibody-recognizing N-linked glycan moiety of a soybean allergen, Gly m Bd 28K
    • Hiemori M, Bando N, Ogawa T, Shimada H, Tsuji H, Yamanishi R, et al: Occurrence of IgE antibody-recognizing N-linked glycan moiety of a soybean allergen, Gly m Bd 28K. Int Arch Allergy Immunol 2000;122:238-245.
    • (2000) Int Arch Allergy Immunol , vol.122 , pp. 238-245
    • Hiemori, M.1    Bando, N.2    Ogawa, T.3    Shimada, H.4    Tsuji, H.5    Yamanishi, R.6
  • 20
    • 0033840609 scopus 로고    scopus 로고
    • Allergy caused by ingestion of zucchini (Cucurbita pepo): Characterization of allergens and cross-reactivity to pollen and other foods
    • Reindl J, Anliker MD, Karamloo F, Vieths S, Wuthrich B: Allergy caused by ingestion of zucchini (Cucurbita pepo): Characterization of allergens and cross-reactivity to pollen and other foods. J Allergy Clin Immunol 2000;106:379-385.
    • (2000) J Allergy Clin Immunol , vol.106 , pp. 379-385
    • Reindl, J.1    Anliker, M.D.2    Karamloo, F.3    Vieths, S.4    Wuthrich, B.5
  • 21
    • 0007657028 scopus 로고    scopus 로고
    • O-glycans as a source of cross-reactivity in determinations of human serum antibodies to Anisakis simplex antigens
    • Lorenzo S, Romaris F, Iglesias R, Audicana MT, Alonso JM, Leiro J, et al: O-glycans as a source of cross-reactivity in determinations of human serum antibodies to Anisakis simplex antigens. Clin Exp Allergy 2000;30:551-559.
    • (2000) Clin Exp Allergy , vol.30 , pp. 551-559
    • Lorenzo, S.1    Romaris, F.2    Iglesias, R.3    Audicana, M.T.4    Alonso, J.M.5    Leiro, J.6
  • 22
    • 0036723928 scopus 로고    scopus 로고
    • Allergologic exploration of germins and germin-like proteins, a new class of plant allergens
    • Jensen-Jarolim E, Schmid B, Bernier F, Berna A, Kinaciyan T, Focke M, et al: Allergologic exploration of germins and germin-like proteins, a new class of plant allergens. Allergy 2002;57:805-810.
    • (2002) Allergy , vol.57 , pp. 805-810
    • Jensen-Jarolim, E.1    Schmid, B.2    Bernier, F.3    Berna, A.4    Kinaciyan, T.5    Focke, M.6
  • 24
    • 0036112851 scopus 로고    scopus 로고
    • Cross-reactivities between date palm (Phoenix dactylifera L.) polypeptides and foods implicated in the oral allergy syndrome
    • Kwaasi AA, Harfi HA, Parhar RS, Saleh S, Collison KS, Panzani RC, et al: Cross-reactivities between date palm (Phoenix dactylifera L.) polypeptides and foods implicated in the oral allergy syndrome. Allergy 2002;57:508-518.
    • (2002) Allergy , vol.57 , pp. 508-518
    • Kwaasi, A.A.1    Harfi, H.A.2    Parhar, R.S.3    Saleh, S.4    Collison, K.S.5    Panzani, R.C.6
  • 25
    • 0036233195 scopus 로고    scopus 로고
    • Allergenic components of a novel food, Micronesian nut nangai (Canarium indicum), shows IgE cross-reactivity in pollen allergic patients
    • Sten E, Stahl SP, Andersen SB, Torp AM, Olesen A, Bindslev-Jensen U, et al: Allergenic components of a novel food, Micronesian nut nangai (Canarium indicum), shows IgE cross-reactivity in pollen allergic patients. Allergy 2002;57:398-404.
    • (2002) Allergy , vol.57 , pp. 398-404
    • Sten, E.1    Stahl, S.P.2    Andersen, S.B.3    Torp, A.M.4    Olesen, A.5    Bindslev-Jensen, U.6
  • 27
    • 0036196769 scopus 로고    scopus 로고
    • Influence of food processing on the allergenicity of celery: DBPCFC with celery spice and cooked celery in patients with celery allergy
    • Ballmer-Weber BK, Hoffmann A, Wüthrich B, Lüttkopf D, Pompei C, Wangorsch A, 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.
    • (2002) Allergy , vol.57 , pp. 228-235
    • Ballmer-Weber, B.K.1    Hoffmann, A.2    Wüthrich, B.3    Lüttkopf, D.4    Pompei, C.5    Wangorsch, A.6
  • 29
    • 0030006293 scopus 로고    scopus 로고
    • O-linked protein glycosylation structure and function
    • Hounsell EF, Davies MJ, Renouf DV: O-linked protein glycosylation structure and function. Glycoconj J 1996;13:19-26.
    • (1996) Glycoconj J , vol.13 , pp. 19-26
    • Hounsell, E.F.1    Davies, M.J.2    Renouf, D.V.3
  • 31
    • 0032754473 scopus 로고    scopus 로고
    • On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database
    • Apweiler R, Hermjakob H, Sharon N: On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database. Biochim Biophys Acta 1999;1473:4-8.
    • (1999) Biochim Biophys Acta , vol.1473 , pp. 4-8
    • Apweiler, R.1    Hermjakob, H.2    Sharon, N.3
  • 32
    • 0024655425 scopus 로고
    • O-glycosylation pathway for mucin-type glycoproteins
    • Carraway KL, Hull SR: O-glycosylation pathway for mucin-type glycoproteins. Bioessays 1989;10:117-121.
    • (1989) Bioessays , vol.10 , pp. 117-121
    • Carraway, K.L.1    Hull, S.R.2
  • 33
    • 0028371792 scopus 로고
    • Extensin: Repetitive motifs, functional sites, post-translational codes, and phylogeny
    • Kieliszewski MJ, Lamport DT: Extensin: Repetitive motifs, functional sites, post-translational codes, and phylogeny. Plant J 1994;5:157-172.
    • (1994) Plant J , vol.5 , pp. 157-172
    • Kieliszewski, M.J.1    Lamport, D.T.2
  • 34
    • 0030764614 scopus 로고    scopus 로고
    • Discovery of the shortest sequence motif for high level mucin-type O-glycosylation
    • Yoshida A, Suzuki M, Ikenaga H, Takeuchi M: Discovery of the shortest sequence motif for high level mucin-type O-glycosylation. J Biol Chem 1997;272:16884-16888.
    • (1997) J Biol Chem , vol.272 , pp. 16884-16888
    • Yoshida, A.1    Suzuki, M.2    Ikenaga, H.3    Takeuchi, M.4
  • 35
    • 0033592904 scopus 로고    scopus 로고
    • Synthetic genes for glycoprotein design and the elucidation of hydroxyproline-O-glycosylation codes
    • Shpak E, Leykam JF, Kieliszewski MJ: Synthetic genes for glycoprotein design and the elucidation of hydroxyproline-O-glycosylation codes. Proc Natl Acad Sci USA 1999;96:14736-14741.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 14736-14741
    • Shpak, E.1    Leykam, J.F.2    Kieliszewski, M.J.3
  • 36
    • 0035371614 scopus 로고    scopus 로고
    • The latest hype on Hyp-O-glycosylation codes
    • Kieliszewski MJ: The latest hype on Hyp-O-glycosylation codes. Phytochemistry 2001;57:319-323.
    • (2001) Phytochemistry , vol.57 , pp. 319-323
    • Kieliszewski, M.J.1
  • 37
    • 0022565411 scopus 로고
    • 2. Evidence for the presence of terminal N-acetylglucosamine and fucose in an insect glycoprotein
    • 2. Evidence for the presence of terminal N-acetylglucosamine and fucose in an insect glycoprotein. Comp Biochem Physiol B 1986;83:321-324.
    • (1986) Comp Biochem Physiol B , vol.83 , pp. 321-324
    • Weber, A.1    März, L.2    Altmann, F.3
  • 38
    • 0034441282 scopus 로고    scopus 로고
    • The joys of HexNAc. The synthesis and function of N- and O-glycan branches
    • Schachter H: The joys of HexNAc. The synthesis and function of N- and O-glycan branches. Glycoconj J 2000;17:465-483.
    • (2000) Glycoconj J , vol.17 , pp. 465-483
    • Schachter, H.1
  • 39
    • 0026691179 scopus 로고
    • 2. The role of alpha 1,3-fucosylation of the asparagine-bound N-acetylglucosamine
    • 2. The role of alpha 1,3-fucosylation of the asparagine-bound N-acetylglucosamine. Biochem J 1992;284(pt 2):377-380.
    • (1992) Biochem J , vol.284 , Issue.PART 2 , pp. 377-380
    • Prenner, C.1    Mach, L.2    Glossl, J.3    März, L.4
  • 40
    • 0020578434 scopus 로고
    • Rabbit anti-carbohydrate antibody elicited by the lymphocyte mitogenic glycoprotein from Wistaria floribunda seeds
    • Kaladas PM, Goldberg R, Poretz RD: Rabbit anti-carbohydrate antibody elicited by the lymphocyte mitogenic glycoprotein from Wistaria floribunda seeds. Mol Immunol 1983;20:727-735.
    • (1983) Mol Immunol , vol.20 , pp. 727-735
    • Kaladas, P.M.1    Goldberg, R.2    Poretz, R.D.3
  • 41
    • 0009620955 scopus 로고
    • Common antigenic determinants in the glycoproteins of plants molluscs and insects
    • Faye L, Chrispeels MJ: Common antigenic determinants in the glycoproteins of plants molluscs and insects. Glycoconj J 1988;5:245-256.
    • (1988) Glycoconj J , vol.5 , pp. 245-256
    • Faye, L.1    Chrispeels, M.J.2
  • 42
    • 0024203985 scopus 로고
    • Significant immunological cross-reactivity of plant glycoproteins
    • Laine AC, Faye L: Significant immunological cross-reactivity of plant glycoproteins. Electrophoresis 1988;9:841-844.
    • (1988) Electrophoresis , vol.9 , pp. 841-844
    • Laine, A.C.1    Faye, L.2
  • 43
    • 0027453187 scopus 로고
    • Affinity purification of antibodies specific for Asn-linked glycans containing alpha 1,3 fucose or beta 1,2 xylose
    • Faye L, Gomord V, Fitchette-Laine AC, Chrispeels MJ: Affinity purification of antibodies specific for Asn-linked glycans containing alpha 1,3 fucose or beta 1,2 xylose. Anal Biochem 1993;209:104-108.
    • (1993) Anal Biochem , vol.209 , pp. 104-108
    • Faye, L.1    Gomord, V.2    Fitchette-Laine, A.C.3    Chrispeels, M.J.4
  • 44
    • 0028533476 scopus 로고
    • Immunogenicity of the N-glycans of peanut peroxidase
    • Wan L, van Huystee RB: Immunogenicity of the N-glycans of peanut peroxidase. Phytochemistry 1994;37:933-940
    • (1994) Phytochemistry , vol.37 , pp. 933-940
    • Wan, L.1    Van Huystee, R.B.2
  • 45
    • 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
    • van Ree R, Cabanes-Macheteau M, Akkerdaas J, Milazzo JP, Loutelier-Bourhis C, Rayon C, et al: Beta(1,2)-xylose and alpha(1,3)-fucose residues have a strong contribution in IgE binding to plant glycoallergens. J Biol Chem 2000;275:11451-11458.
    • (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
  • 46
    • 0014934330 scopus 로고
    • The composition and structure of carbohydrate moiety of stem bromelain
    • Yasuda Y, Takahashi N, Murachi T: The composition and structure of carbohydrate moiety of stem bromelain. Biochemistry 1970;9:25-32.
    • (1970) Biochemistry , vol.9 , pp. 25-32
    • Yasuda, Y.1    Takahashi, N.2    Murachi, T.3
  • 47
    • 0018566969 scopus 로고
    • Complete structure of the carbohydrate moiety of stem bromelain. An application of the almond glycopeptidase for structural studies of glycopeptides
    • Ishihara H, Takahashi N, Oguri S, Tejima S: Complete structure of the carbohydrate moiety of stem bromelain. An application of the almond glycopeptidase for structural studies of glycopeptides. J Biol Chem 1979;254:10715-10719.
    • (1979) J Biol Chem , vol.254 , pp. 10715-10719
    • Ishihara, H.1    Takahashi, N.2    Oguri, S.3    Tejima, S.4
  • 48
    • 0025303628 scopus 로고
    • Structure and biosynthesis of the xylose-containing carbohydrate moiety of rice alpha-amylase
    • Hayashi M, Tsuru A, Mitsui T, Takahashi N, Hanzawa H, Arata Y, et al: Structure and biosynthesis of the xylose-containing carbohydrate moiety of rice alpha-amylase. Eur J Biochem 1990;191:287-295.
    • (1990) Eur J Biochem , vol.191 , pp. 287-295
    • Hayashi, M.1    Tsuru, A.2    Mitsui, T.3    Takahashi, N.4    Hanzawa, H.5    Arata, Y.6
  • 49
    • 0029911095 scopus 로고    scopus 로고
    • The carbohydrate moiety of the bermuda grass antigen BG60. New oligosaccharides of plant origin
    • Ohsuga H, Su SN, Takahashi N, Yang SY, Nakagawa H, Shimada I, et al: The carbohydrate moiety of the bermuda grass antigen BG60. New oligosaccharides of plant origin. J Biol Chem 1996;271:26653-26658.
    • (1996) J Biol Chem , vol.271 , pp. 26653-26658
    • Ohsuga, H.1    Su, S.N.2    Takahashi, N.3    Yang, S.Y.4    Nakagawa, H.5    Shimada, I.6
  • 50
    • 0029741668 scopus 로고    scopus 로고
    • Structures and contribution to the antigenicity of oligosaccharides of Japanese cedar (Cryptomeria japonica) pollen allergen Cryj I: Relationship between the structures and antigenic epitopes of plant N-linked complex-type glycans
    • Ogawa H, Hijikata A, Amano M, Kojima K, Fukushima H, Ishizuka I, et al: Structures and contribution to the antigenicity of oligosaccharides of Japanese cedar (Cryptomeria japonica) pollen allergen Cryj I: Relationship between the structures and antigenic epitopes of plant N-linked complex-type glycans. Glycoconj J 1996;13:555-566.
    • (1996) Glycoconj J , vol.13 , pp. 555-566
    • Ogawa, H.1    Hijikata, A.2    Amano, M.3    Kojima, K.4    Fukushima, H.5    Ishizuka, I.6
  • 51
    • 0031907279 scopus 로고    scopus 로고
    • Structures of the N-linked carbohydrate of ascorbic acid oxidase from zucchini
    • Altmann F: Structures of the N-linked carbohydrate of ascorbic acid oxidase from zucchini. Glycoconj J 1998;15:79-82.
    • (1998) Glycoconj J , vol.15 , pp. 79-82
    • Altmann, F.1
  • 52
    • 0029011319 scopus 로고
    • Conformational analysis of the xylose-containing N-glycan of pineapple stem bromelain as part of the intact glycoprotein
    • Lommerse JP, Kroon-Batenburg LM, Kamerling JP, Vliegenthart JF: Conformational analysis of the xylose-containing N-glycan of pineapple stem bromelain as part of the intact glycoprotein. Biochemistry 1995;34:8196-8206.
    • (1995) Biochemistry , vol.34 , pp. 8196-8206
    • Lommerse, J.P.1    Kroon-Batenburg, L.M.2    Kamerling, J.P.3    Vliegenthart, J.F.4
  • 53
    • 0023279259 scopus 로고
    • Cross-reactivity among birch pollen, vegetables and fruits as detected by IgE antibodies is due to at least three distinct cross-reactive structures
    • Calkhoven PG, Aalbers M, Koshte VL, Pos O, Oei HD, Aalberse RC: Cross-reactivity among birch pollen, vegetables and fruits as detected by IgE antibodies is due to at least three distinct cross-reactive structures. Allergy 1987;42:382-390.
    • (1987) Allergy , vol.42 , pp. 382-390
    • Calkhoven, P.G.1    Aalbers, M.2    Koshte, V.L.3    Pos, O.4    Oei, H.D.5    Aalberse, R.C.6
  • 54
    • 0027274914 scopus 로고
    • Pollen-vegetable food crossreactivity: Serological and clinical relevance of crossreactive IgE
    • van Ree R, Aalberse RC: Pollen-vegetable food crossreactivity: Serological and clinical relevance of crossreactive IgE. J Clin Immunoassay 1993;16:124-130.
    • (1993) J Clin Immunoassay , vol.16 , pp. 124-130
    • Van Ree, R.1    Aalberse, R.C.2
  • 55
    • 0029905483 scopus 로고    scopus 로고
    • Cross-reactivity between the major allergen from olive pollen and unrelated glycoproteins: Evidence of an epitope in the glycan moiety of the allergen
    • Batanero E, Villalba M, Monsalve RI, Rodriguez R: Cross-reactivity between the major allergen from olive pollen and unrelated glycoproteins: Evidence of an epitope in the glycan moiety of the allergen. J Allergy Clin Immunol 1996;97:1264-1271.
    • (1996) J Allergy Clin Immunol , vol.97 , pp. 1264-1271
    • Batanero, E.1    Villalba, M.2    Monsalve, R.I.3    Rodriguez, R.4
  • 56
    • 0030329624 scopus 로고    scopus 로고
    • Cross-reactive carbohydrate determinants
    • Aalberse RC, van Ree R: Cross-reactive carbohydrate determinants. Monogr Allergy 1996;32:78-83.
    • (1996) Monogr Allergy , vol.32 , pp. 78-83
    • Aalberse, R.C.1    Van Ree, R.2
  • 58
    • 0029964855 scopus 로고    scopus 로고
    • Ubiquitous structures responsible for IgE cross-reactivity between tomato fruit and grass pollen allergens
    • Petersen A, Vieths S, Aulepp H, Schlaak M, Becker WM: Ubiquitous structures responsible for IgE cross-reactivity between tomato fruit and grass pollen allergens. J Allergy Clin Immunol 1996;98:805-815.
    • (1996) J Allergy Clin Immunol , vol.98 , pp. 805-815
    • Petersen, A.1    Vieths, S.2    Aulepp, H.3    Schlaak, M.4    Becker, W.M.5
  • 61
    • 0031453279 scopus 로고    scopus 로고
    • Allergenic cross-reactivity, food allergy and pollen
    • Vieths S: Allergenic cross-reactivity, food allergy and pollen. Evironm Toxicol Pharmacol 1997;4:61-70.
    • (1997) Evironm Toxicol Pharmacol , vol.4 , pp. 61-70
    • Vieths, S.1
  • 62
    • 0034995912 scopus 로고    scopus 로고
    • Cross-reactivity of IgE antibodies to allergens
    • Aalberse RC, Akkerdaas J, van Ree R: Cross-reactivity of IgE antibodies to allergens. Allergy 2001;56:478-490.
    • (2001) Allergy , vol.56 , pp. 478-490
    • Aalberse, R.C.1    Akkerdaas, J.2    Van Ree, R.3
  • 63
    • 0036264052 scopus 로고    scopus 로고
    • Current understanding of cross-reactivity of food allergens and pollen
    • Vieths S, Scheurer S, Ballmer-Weber B: Current understanding of cross-reactivity of food allergens and pollen. Ann NY Acad Sci 2002;964:47-68.
    • (2002) Ann NY Acad Sci , vol.964 , pp. 47-68
    • Vieths, S.1    Scheurer, S.2    Ballmer-Weber, B.3
  • 64
    • 0029664756 scopus 로고    scopus 로고
    • Type 1 allergic reactions to plant-derived food: A consequence of primary sensitization to pollen allergens
    • Valenta R, Kraft D: Type 1 allergic reactions to plant-derived food: A consequence of primary sensitization to pollen allergens. J Allergy Clin Immunol 1996;97:893-895.
    • (1996) J Allergy Clin Immunol , vol.97 , pp. 893-895
    • Valenta, R.1    Kraft, D.2
  • 65
    • 0029809256 scopus 로고    scopus 로고
    • IgE cross-reactivity between birch pollen, mugwort pollen and celery is due to at least three distinct cross-reacting allergens: Immunoblot investigation of the birch-mugwort-celery syndrome
    • Bauer L, Ebner C, Hirschwehr R, Wüthrich B, Pichler C, Fritsch R, et al: IgE cross-reactivity between birch pollen, mugwort pollen and celery is due to at least three distinct cross-reacting allergens: Immunoblot investigation of the birch-mugwort-celery syndrome. Clin Exp Allergy 1996;26:1161-1170.
    • (1996) Clin Exp Allergy , vol.26 , pp. 1161-1170
    • Bauer, L.1    Ebner, C.2    Hirschwehr, R.3    Wüthrich, B.4    Pichler, C.5    Fritsch, R.6
  • 66
    • 0029764078 scopus 로고    scopus 로고
    • Stability of food allergens to digestion in vitro
    • Astwood JD, Leach JN, Fuchs RL: Stability of food allergens to digestion in vitro. Nat Biotechnol 1996;14:1269-1273.
    • (1996) Nat Biotechnol , vol.14 , pp. 1269-1273
    • Astwood, J.D.1    Leach, J.N.2    Fuchs, R.L.3
  • 69
  • 70
    • 0002724526 scopus 로고    scopus 로고
    • Factors modulating allergen-induced histamine release
    • Bousquet J, Yssel H (eds), New York, Marcel Dekker
    • van Ree R: Factors modulating allergen-induced histamine release: in Bousquet J, Yssel H (eds): Immunotherapy in Asthma. New York, Marcel Dekker, 1999, pp 399-409.
    • (1999) Immunotherapy in Asthma , pp. 399-409
    • Van Ree, R.1
  • 71
    • 0036122621 scopus 로고    scopus 로고
    • Evidence of an affinity threshold for IgE-allergen binding in the percutaneous skin test reaction
    • Pierson-Mullany LK, Jackola DR, Blumenthal MN, Rosenberg A: Evidence of an affinity threshold for IgE-allergen binding in the percutaneous skin test reaction. Clin Exp Allergy 2002;32:107-116.
    • (2002) Clin Exp Allergy , vol.32 , pp. 107-116
    • Pierson-Mullany, L.K.1    Jackola, D.R.2    Blumenthal, M.N.3    Rosenberg, A.4
  • 74
    • 0028817553 scopus 로고
    • Demonstration of carbohydrate-specific immunoglobulin G4 antibodies in sera of patients receiving grass pollen immunotherapy
    • van Ree R, Aalberse RC: Demonstration of carbohydrate-specific immunoglobulin G4 antibodies in sera of patients receiving grass pollen immunotherapy. Int Arch Allergy Immunol 1995;106:146-148.
    • (1995) Int Arch Allergy Immunol , vol.106 , pp. 146-148
    • Van Ree, R.1    Aalberse, R.C.2
  • 77
    • 0027257525 scopus 로고
    • Introduction: Basophil histamine release and the diagnosis of food allergy
    • Du Buske LM: Introduction: Basophil histamine release and the diagnosis of food allergy. Allergy Proc 1993;14:243-249.
    • (1993) Allergy Proc , vol.14 , pp. 243-249
    • Du Buske, L.M.1
  • 78
    • 0027268294 scopus 로고
    • The clinical utility of basophil histamine release
    • Nolte H: The clinical utility of basophil histamine release. Allergy Proc 1993;14:251-254.
    • (1993) Allergy Proc , vol.14 , pp. 251-254
    • Nolte, H.1
  • 79
    • 0028605535 scopus 로고
    • The surface membrane antigen phenotype of human blood basophils
    • Fureder W, Agis H, Sperr WR, Lechner K, Valent P: The surface membrane antigen phenotype of human blood basophils. Allergy 1994;49:861-865.
    • (1994) Allergy , vol.49 , pp. 861-865
    • Fureder, W.1    Agis, H.2    Sperr, W.R.3    Lechner, K.4    Valent, P.5
  • 80
    • 0036331003 scopus 로고    scopus 로고
    • Validation of a two-color flow cytometric assay detecting in vitro basophil activation for the diagnosis of IgE-mediated natural rubber latex allergy
    • Ebo DG, Lechkar B, Schuerwegh AJ, Bridts CH, De Clerck LS, Stevens WJ: Validation of a two-color flow cytometric assay detecting in vitro basophil activation for the diagnosis of IgE-mediated natural rubber latex allergy. Allergy 2002;57:706-712.
    • (2002) Allergy , vol.57 , pp. 706-712
    • Ebo, D.G.1    Lechkar, B.2    Schuerwegh, A.J.3    Bridts, C.H.4    De Clerck, L.S.5    Stevens, W.J.6
  • 82
    • 0031667332 scopus 로고    scopus 로고
    • Recombinant allergens: The future of the diagnosis and treatment of atopic allergy
    • Kraft D, Ferreira F, Ebner C, Valenta R, Breiteneder H, Susani M, et al: Recombinant allergens: The future of the diagnosis and treatment of atopic allergy. Allergy 1998;53:62-66.
    • (1998) Allergy , vol.53 , pp. 62-66
    • Kraft, D.1    Ferreira, F.2    Ebner, C.3    Valenta, R.4    Breiteneder, H.5    Susani, M.6
  • 84
    • 0005629635 scopus 로고    scopus 로고
    • The recombinant allergen-based concept of component-resolved diagnostics and immunotherapy (CRD and CRIT)
    • Valenta R, Lidholm J, Niederberger V, Hayek B, Kraft D, Gronlund H: The recombinant allergen-based concept of component-resolved diagnostics and immunotherapy (CRD and CRIT). Clin Exp Allergy 1999;29:896-904.
    • (1999) Clin Exp Allergy , vol.29 , pp. 896-904
    • Valenta, R.1    Lidholm, J.2    Niederberger, V.3    Hayek, B.4    Kraft, D.5    Gronlund, H.6
  • 87
    • 0031056155 scopus 로고    scopus 로고
    • The production of recombinant glycoproteins with special reference to simple eukaryotes including Dictyostelium discoideum
    • Jung E, Williams KL: The production of recombinant glycoproteins with special reference to simple eukaryotes including Dictyostelium discoideum. Biotechnol Appl Biochem 1997;25(pt 1):3-8.
    • (1997) Biotechnol Appl Biochem , vol.25 , Issue.PART 1 , pp. 3-8
    • Jung, E.1    Williams, K.L.2
  • 88
    • 0032848027 scopus 로고    scopus 로고
    • Insect cells as hosts for the expression of recombinant glycoproteins
    • Altmann F, Staudacher E, Wilson IB, Marz L: Insect cells as hosts for the expression of recombinant glycoproteins. Glycoconj J 1999;16:109-123.
    • (1999) Glycoconj J , vol.16 , pp. 109-123
    • Altmann, F.1    Staudacher, E.2    Wilson, I.B.3    Marz, L.4
  • 89
    • 0032884573 scopus 로고    scopus 로고
    • Recombinant protein expression in Escherichia coli
    • Baneyx F: Recombinant protein expression in Escherichia coli. Curr Opin Biotechnol 1999;10:411-421.
    • (1999) Curr Opin Biotechnol , vol.10 , pp. 411-421
    • Baneyx, F.1
  • 90
    • 0033402046 scopus 로고    scopus 로고
    • Glycosylation of Pichia pastoris-derived proteins
    • Bretthauer RK, Castellino FJ: Glycosylation of Pichia pastoris-derived proteins. Biotechnol Appl Biochem 1999;30(pt 3):193-200.
    • (1999) Biotechnol Appl Biochem , vol.30 , Issue.PART 3 , pp. 193-200
    • Bretthauer, R.K.1    Castellino, F.J.2
  • 91
    • 0032848329 scopus 로고    scopus 로고
    • Genetic engineering of recombinant glycoproteins and the glycosylation pathway in mammalian host cells
    • Grabenhorst E, Schlenke P, Pohl S, Nimtz M, Conradt HS: Genetic engineering of recombinant glycoproteins and the glycosylation pathway in mammalian host cells. Glycoconj J 1999;16:81-97.
    • (1999) Glycoconj J , vol.16 , pp. 81-97
    • Grabenhorst, E.1    Schlenke, P.2    Pohl, S.3    Nimtz, M.4    Conradt, H.S.5
  • 92
    • 0002596901 scopus 로고    scopus 로고
    • Filamentous fungi as production organisms for glycoproteins of biomedical interest
    • Maras M, van D, I, Contreras R, van den Hondel CA: Filamentous fungi as production organisms for glycoproteins of biomedical interest. Glycoconj J 1999;16:99-107.
    • (1999) Glycoconj J , vol.16 , pp. 99-107
    • Maras, M.1    Van, D.I.2    Contreras, R.3    Van den Hondel, C.A.4
  • 93
    • 0034570433 scopus 로고    scopus 로고
    • N-glycosylation of recombinant pharmaceutical glycoproteins produced in transgenic plants: Towards an humanisation of plant N-glycans
    • Lerouge P, Bardor M, Pagny S, Gomord V, Faye L: N-glycosylation of recombinant pharmaceutical glycoproteins produced in transgenic plants: Towards an humanisation of plant N-glycans. Curr Pharm Biotechnol 2000;1:347-354.
    • (2000) Curr Pharm Biotechnol , vol.1 , pp. 347-354
    • Lerouge, P.1    Bardor, M.2    Pagny, S.3    Gomord, V.4    Faye, L.5
  • 94
    • 0033955337 scopus 로고    scopus 로고
    • Heterologous protein expression in the methylotrophic yeast Pichia pastoris
    • Cereghino JL, Cregg JM: Heterologous protein expression in the methylotrophic yeast Pichia pastoris. FEMS Microbiol Rev 2000;24:45-66.
    • (2000) FEMS Microbiol Rev , vol.24 , pp. 45-66
    • Cereghino, J.L.1    Cregg, J.M.2
  • 95
    • 0035169206 scopus 로고    scopus 로고
    • Understanding the art of producing protein and nonprotein molecules in Escherichia coli
    • Balbas P: Understanding the art of producing protein and nonprotein molecules in Escherichia coli. Mol Biotechnol 2001;19:251-267.
    • (2001) Mol Biotechnol , vol.19 , pp. 251-267
    • Balbas, P.1
  • 97
    • 0025349149 scopus 로고
    • Expression of Dermatophagoides pteronyssinus allergen, Der p II, in Escherichia coli and the binding studies with human IgE
    • Chua KY, Dilworth RJ, Thomas WR: Expression of Dermatophagoides pteronyssinus allergen, Der p II, in Escherichia coliand the binding studies with human IgE. Int Arch Allergy Appl Immunol 1990;91:124-129.
    • (1990) Int Arch Allergy Appl Immunol , vol.91 , pp. 124-129
    • Chua, K.Y.1    Dilworth, R.J.2    Thomas, W.R.3
  • 98
    • 0026163998 scopus 로고
    • Cloning and expression of cDNA coding for the major house dust mite allergen Der f II in Escherichia coli
    • Yuuki T, Okumura Y, Ando T, Yamakawa H, Suko M, Haida M, et al: Cloning and expression of cDNA coding for the major house dust mite allergen Der f II in Escherichia coli. Agric Biol Chem 1991;55:1233-1238.
    • (1991) Agric Biol Chem , vol.55 , pp. 1233-1238
    • Yuuki, T.1    Okumura, Y.2    Ando, T.3    Yamakawa, H.4    Suko, M.5    Haida, M.6
  • 99
    • 0026052714 scopus 로고
    • Complete sequence of the allergen Amb alpha II. Recombinant expression and reactivity with T cells from ragweed allergic patients
    • Rogers BL, Morgenstern JP, Griffith IJ, Yu XB, Counsell CM, Brauer AW, et al: Complete sequence of the allergen Amb alpha II. Recombinant expression and reactivity with T cells from ragweed allergic patients. J Immunol 1991;147:2547-2552.
    • (1991) J Immunol , vol.147 , pp. 2547-2552
    • Rogers, B.L.1    Morgenstern, J.P.2    Griffith, I.J.3    Yu, X.B.4    Counsell, C.M.5    Brauer, A.W.6
  • 101
    • 0026724280 scopus 로고
    • Cloning and expression of recombinant Aspergillus fumigatus allergen I/a (rAsp f I/a) with IgE binding and type I skin test activity
    • Moser M, Crameri R, Menz G, Schneider T, Dudler T, Virchow C, et al: Cloning and expression of recombinant Aspergillus fumigatus allergen I/a (rAsp f I/a) with IgE binding and type I skin test activity. J Immunol 1992;149:454-460.
    • (1992) J Immunol , vol.149 , pp. 454-460
    • Moser, M.1    Crameri, R.2    Menz, G.3    Schneider, T.4    Dudler, T.5    Virchow, C.6
  • 102
    • 0026703078 scopus 로고
    • Expression and analysis of recombinant Amb a V and Amb t V allergens. Comparison with native proteins by immunological assays and NMR spectroscopy
    • Rafnar T, Ghosh B, Metzler WJ, Huang SK, Perry MP, Mueller L, et al: Expression and analysis of recombinant Amb a V and Amb t V allergens. Comparison with native proteins by immunological assays and NMR spectroscopy. J Biol Chem 1992;267:21119-21123.
    • (1992) J Biol Chem , vol.267 , pp. 21119-21123
    • Rafnar, T.1    Ghosh, B.2    Metzler, W.J.3    Huang, S.K.4    Perry, M.P.5    Mueller, L.6
  • 103
    • 0036137102 scopus 로고    scopus 로고
    • Comparison of four variants of a major allergen in hazelnut (Corylus avellana) Cor a 1.04 with the major hazel pollen allergen Cor a 1.01
    • Lüttkopf D, Muller U, Skov PS, Ballmer-Weber BK, Wüthrich B, Skamstrup HK, et al: Comparison of four variants of a major allergen in hazelnut (Corylus avellana) Cor a 1.04 with the major hazel pollen allergen Cor a 1.01. Mol Immunol 2002;38:515-525.
    • (2002) Mol Immunol , vol.38 , pp. 515-525
    • Lüttkopf, D.1    Muller, U.2    Skov, P.S.3    Ballmer-Weber, B.K.4    Wüthrich, B.5    Skamstrup, H.K.6
  • 104
    • 0036310652 scopus 로고    scopus 로고
    • IgE reactivity of tandem repeats derived from cockroach allergen, Bla g 1
    • Pomes A, Vailes LD, Helm RM, Chapman MD: IgE reactivity of tandem repeats derived from cockroach allergen, Bla g 1. Eur J Biochem 2002;269:3086-3092.
    • (2002) Eur J Biochem , vol.269 , pp. 3086-3092
    • Pomes, A.1    Vailes, L.D.2    Helm, R.M.3    Chapman, M.D.4
  • 105
    • 0036307905 scopus 로고    scopus 로고
    • The crystal structure of a major dust mite allergen Der p 2, and its biological implications
    • Derewenda U, Li J, Derewenda Z, Dauter Z, Mueller GA, Rule GS, et al: The crystal structure of a major dust mite allergen Der p 2, and its biological implications. J Mol Biol 2002;318:189-197.
    • (2002) J Mol Biol , vol.318 , pp. 189-197
    • Derewenda, U.1    Li, J.2    Derewenda, Z.3    Dauter, Z.4    Mueller, G.A.5    Rule, G.S.6
  • 106
    • 0036569405 scopus 로고    scopus 로고
    • Recombinant carp parvalbumin, the major cross-reactive fish allergen: A tool for diagnosis and therapy of fish allergy
    • Swoboda I, Bugajska-Schretter A, Verdino P, Keller W, Sperr WR, Valent P, et al: Recombinant carp parvalbumin, the major cross-reactive fish allergen: A tool for diagnosis and therapy of fish allergy. J Immunol 2002;168:4576-4584.
    • (2002) J Immunol , vol.168 , pp. 4576-4584
    • Swoboda, I.1    Bugajska-Schretter, A.2    Verdino, P.3    Keller, W.4    Sperr, W.R.5    Valent, P.6
  • 108
    • 0035708061 scopus 로고    scopus 로고
    • cDNA cloning and expression of Blo t 11, the Blomia tropicalis allergen homologous to paramyosin
    • Ramos JD, Cheong N, Lee BW, Chua KY, Nge C, Wah LB, et al: cDNA cloning and expression of Blo t 11, the Blomia tropicalis allergen homologous to paramyosin. Int Arch Allergy Immunol 2001;126:286-293.
    • (2001) Int Arch Allergy Immunol , vol.126 , pp. 286-293
    • Ramos, J.D.1    Cheong, N.2    Lee, B.W.3    Chua, K.Y.4    Nge, C.5    Wah, L.B.6
  • 109
    • 0029839368 scopus 로고    scopus 로고
    • Cloning and expression in yeast Pichia pastoris of a biologically active form of Cyn d 1, the major allergen of Bermuda grass pollen
    • Smith PM, Suphioglu C, Griffith IJ, Theriault K, Knox RB, Singh MB: Cloning and expression in yeast Pichia pastoris of a biologically active form of Cyn d 1, the major allergen of Bermuda grass pollen. J Allergy Clin Immunol 1996;98:331-343.
    • (1996) J Allergy Clin Immunol , vol.98 , pp. 331-343
    • Smith, P.M.1    Suphioglu, C.2    Griffith, I.J.3    Theriault, K.4    Knox, R.B.5    Singh, M.B.6
  • 110
    • 0032561197 scopus 로고    scopus 로고
    • Identification and cloning of prs a 1, a 32-kDa endochitinase and major allergen of avocado, and its expression in the yeast Pichia pastoris
    • Sowka S, Hsieh LS, Krebitz M, Akasawa A, Martin BM, Starrett D, et al: Identification and cloning of prs a 1, a 32-kDa endochitinase and major allergen of avocado, and its expression in the yeast Pichia pastoris. J Biol Chem 1998;273:28091-28097.
    • (1998) J Biol Chem , vol.273 , pp. 28091-28097
    • Sowka, S.1    Hsieh, L.S.2    Krebitz, M.3    Akasawa, A.4    Martin, B.M.5    Starrett, D.6
  • 111
    • 0032126715 scopus 로고    scopus 로고
    • cDNA cloning of the 43-kDa latex allergen Hev b 7 with sequence similarity to patatins and its expression in the yeast Pichia pastoris
    • Sowka S, Wagner S, Krebitz M, Arija-Mad-Arif S, Yusof F, Kinaciyan T, et al: cDNA cloning of the 43-kDa latex allergen Hev b 7 with sequence similarity to patatins and its expression in the yeast Pichia pastoris. Eur J Biochem 1998;255:213-219.
    • (1998) Eur J Biochem , vol.255 , pp. 213-219
    • Sowka, S.1    Wagner, S.2    Krebitz, M.3    Arija-Mad-Arif, S.4    Yusof, F.5    Kinaciyan, T.6
  • 115
    • 0033437131 scopus 로고    scopus 로고
    • Purified natural and recombinant Fel d 1 and cat albumin in in vitro diagnostics for cat allergy
    • van Ree R, van Leeuwen WA, Bulder I, Bond J, Aalberse RC: Purified natural and recombinant Fel d 1 and cat albumin in in vitro diagnostics for cat allergy. J Allergy Clin Immunol 1999;104:1223-1230.
    • (1999) J Allergy Clin Immunol , vol.104 , pp. 1223-1230
    • Van Ree, R.1    Van Leeuwen, W.A.2    Bulder, I.3    Bond, J.4    Aalberse, R.C.5
  • 116
    • 0032964927 scopus 로고    scopus 로고
    • Cloning of the patatin-like latex allergen Hev b 7, its expression in the yeast Pichia pastoris and its immunological characterization
    • Breiteneder H, Sowka S, Wagner S, Krebitz M, Hafner C, Kinaciyan T, et al: Cloning of the patatin-like latex allergen Hev b 7, its expression in the yeast Pichia pastoris and its immunological characterization. Int Arch Allergy Immunol 1999;118:309-310.
    • (1999) Int Arch Allergy Immunol , vol.118 , pp. 309-310
    • Breiteneder, H.1    Sowka, S.2    Wagner, S.3    Krebitz, M.4    Hafner, C.5    Kinaciyan, T.6
  • 117
    • 0033561258 scopus 로고    scopus 로고
    • Production and detailed characterization of biologically active olive pollen allergen Ole e 1 secreted by the yeast Pichia pastoris
    • Huecas S, Villalba M, Gonzalez E, Martinez-Ruiz A, Rodriguez R: Production and detailed characterization of biologically active olive pollen allergen Ole e 1 secreted by the yeast Pichia pastoris. Eur J Biochem 1999;261:539-546.
    • (1999) Eur J Biochem , vol.261 , pp. 539-546
    • Huecas, S.1    Villalba, M.2    Gonzalez, E.3    Martinez-Ruiz, A.4    Rodriguez, R.5
  • 118
    • 0033668126 scopus 로고    scopus 로고
    • A recombinant group 1 house dust mite allergen, rDer f 1, with biological activities similar to those of the native allergen
    • Best EA, Stedman KE, Bozic CM, Hunter SW, Vailes L, Chapman MD, et al: A recombinant group 1 house dust mite allergen, rDer f 1, with biological activities similar to those of the native allergen. Protein Expr Purif 2000;20:462-471.
    • (2000) Protein Expr Purif , vol.20 , pp. 462-471
    • Best, E.A.1    Stedman, K.E.2    Bozic, C.M.3    Hunter, S.W.4    Vailes, L.5    Chapman, M.D.6
  • 119
    • 0033763677 scopus 로고    scopus 로고
    • Identification, cloning, and characterization of a major cat flea salivary allergen (Cte f 1)
    • McDermott MJ, Weber E, Hunter S, Stedman KE, Best E, Frank GR, et al: Identification, cloning, and characterization of a major cat flea salivary allergen (Cte f 1). Mol Immunol 2000;37:361-375.
    • (2000) Mol Immunol , vol.37 , pp. 361-375
    • McDermott, M.J.1    Weber, E.2    Hunter, S.3    Stedman, K.E.4    Best, E.5    Frank, G.R.6
  • 120
    • 0035672133 scopus 로고    scopus 로고
    • Immunochemical characterization of two Pichia pastoris-derived recombinant group 5 Dactylis glomerata isoallergens
    • van Oort E, de Heer PG, Lerouge P, Faye L, Aalberse RC, van Ree R: Immunochemical characterization of two Pichia pastoris-derived recombinant group 5 Dactylis glomerata isoallergens. Int Arch Allergy Immunol 2001;126:196-205.
    • (2001) Int Arch Allergy Immunol , vol.126 , pp. 196-205
    • Van Oort, E.1    De Heer, P.G.2    Lerouge, P.3    Faye, L.4    Aalberse, R.C.5    Van Ree, R.6
  • 121
    • 0035291498 scopus 로고    scopus 로고
    • Cloning and expression of cDNA encoding the complete preproform of an isoform of Der f 1, the major group 1 allergen from house dust mite Dermatophagoides farinae
    • Yasuhara T, Takai T, Yuuki T, Okudaira H, Okumura Y: Cloning and expression of cDNA encoding the complete preproform of an isoform of Der f 1, the major group 1 allergen from house dust mite Dermatophagoides farinae. Biosci Biotechnol Biochem 2001;65:563-569.
    • (2001) Biosci Biotechnol Biochem , vol.65 , pp. 563-569
    • Yasuhara, T.1    Takai, T.2    Yuuki, T.3    Okudaira, H.4    Okumura, Y.5
  • 122
    • 0035078115 scopus 로고    scopus 로고
    • Immunological and molecular characterization of the major allergens from lilac and privet pollens overproduced in Pichia pastoris
    • Gonzalez E, Villalba M, Rodriguez R: Immunological and molecular characterization of the major allergens from lilac and privet pollens overproduced in Pichia pastoris. Clin Exp Allergy 2001;31:313-321.
    • (2001) Clin Exp Allergy , vol.31 , pp. 313-321
    • Gonzalez, E.1    Villalba, M.2    Rodriguez, R.3
  • 123
    • 0035987313 scopus 로고    scopus 로고
    • High-level expression of recombinant house dust mite allergen Der p 1 in Pichia pastoris
    • Jacquet A, Magi M, Petry H, Bollen A: High-level expression of recombinant house dust mite allergen Der p 1 in Pichia pastoris. Clin Exp Allergy 2002;32:1048-1053.
    • (2002) Clin Exp Allergy , vol.32 , pp. 1048-1053
    • Jacquet, A.1    Magi, M.2    Petry, H.3    Bollen, A.4
  • 124
    • 0036310652 scopus 로고    scopus 로고
    • IgE reactivity of tandem repeats derived from cockroach allergen, Bla g 1
    • Pomes A, Vailes LD, Helm RM, Chapman MD: IgE reactivity of tandem repeats derived from cockroach allergen, Bla g 1. Eur J Biochem 2002;269:3086-3092.
    • (2002) Eur J Biochem , vol.269 , pp. 3086-3092
    • Pomes, A.1    Vailes, L.D.2    Helm, R.M.3    Chapman, M.D.4
  • 125
    • 0036105450 scopus 로고    scopus 로고
    • Recombinant pronapin precursor produced in Pichia pastoris displays structural and immunologic equivalent properties to its mature product isolated from rapeseed
    • Palomares O, Monsalve RI, Rodriguez R, Villalba M: Recombinant pronapin precursor produced in Pichia pastoris displays structural and immunologic equivalent properties to its mature product isolated from rapeseed. Eur J Biochem 2002;269:2538-2545.
    • (2002) Eur J Biochem , vol.269 , pp. 2538-2545
    • Palomares, O.1    Monsalve, R.I.2    Rodriguez, R.3    Villalba, M.4
  • 127
    • 0036159407 scopus 로고    scopus 로고
    • Maturation of Pichia pastoris-derived recombinant pro-Der p 1 induced by deglycosylation and by the natural cysteine protease Der p 1 from house dust mite
    • van Oort E, de Heer PG, van Leeuwen WA, Derksen NI, Muller M, Huveneers S, et al: Maturation of Pichia pastoris-derived recombinant pro-Der p 1 induced by deglycosylation and by the natural cysteine protease Der p 1 from house dust mite. Eur J Biochem 2002;269:671-679.
    • (2002) Eur J Biochem , vol.269 , pp. 671-679
    • Van Oort, E.1    De Heer, P.G.2    Van Leeuwen, W.A.3    Derksen, N.I.4    Muller, M.5    Huveneers, S.6
  • 128
    • 0027356476 scopus 로고
    • Expression of hornet genes encoding venom allergen antigen 5 in insects
    • Tomalski MD, King TP, Miller LK: Expression of hornet genes encoding venom allergen antigen 5 in insects. Arch Insect Biochem Physiol 1993;22:303-313.
    • (1993) Arch Insect Biochem Physiol , vol.22 , pp. 303-313
    • Tomalski, M.D.1    King, T.P.2    Miller, L.K.3
  • 129
    • 0029776726 scopus 로고    scopus 로고
    • Production of a recombinant imported fire ant venom allergen, Sol i 2, in native and immunoreactive form
    • Schmidt M, McConnell TJ, Hoffman DR: Production of a recombinant imported fire ant venom allergen, Sol i 2, in native and immunoreactive form. J Allergy Clin Immunol 1996;98:82-88.
    • (1996) J Allergy Clin Immunol , vol.98 , pp. 82-88
    • Schmidt, M.1    McConnell, T.J.2    Hoffman, D.R.3
  • 130
    • 0030119164 scopus 로고    scopus 로고
    • Production of recombinant mite allergen Der fI in insect cells and characterization of products - Removal of pro-sequence is essential to IgE-binding activity
    • Shoji H, Hanawa M, Shibuya I, Hirai M, Yas-uhara T, Okumura Y, et al: Production of recombinant mite allergen Der fI in insect cells and characterization of products - Removal of pro-sequence is essential to IgE-binding activity. Biosci Biotechnol Biochem 1996;60:621-625.
    • (1996) Biosci Biotechnol Biochem , vol.60 , pp. 621-625
    • Shoji, H.1    Hanawa, M.2    Shibuya, I.3    Hirai, M.4    Yasuhara, T.5    Okumura, Y.6
  • 131
    • 0031905832 scopus 로고    scopus 로고
    • Expression and rapid purification of an Aedes aegypti salivary allergen by a baculovirus system
    • Xu W, Simons FE, Peng Z: Expression and rapid purification of an Aedes aegypti salivary allergen by a baculovirus system. Int Arch Allergy Immunol 1998;115:245-251.
    • (1998) Int Arch Allergy Immunol , vol.115 , pp. 245-251
    • Xu, W.1    Simons, F.E.2    Peng, Z.3
  • 132
    • 0033302554 scopus 로고    scopus 로고
    • Biological activity of recombinant bee venom allergens expressed in baculovirus-infected cells
    • Soldatova LN: Biological activity of recombinant bee venom allergens expressed in baculovirus-infected cells. Arb Paul Ehrlich Inst Bundesamt Sera Impfstoffe Frankf A M. 1999;189-193.
    • (1999) Arb Paul Ehrlich Inst Bundesamt Sera Impfstoffe Frankf A M , pp. 189-193
    • Soldatova, L.N.1
  • 133
    • 0031982094 scopus 로고    scopus 로고
    • Superior biologic activity of the recombinant bee venom allergen hyaluronidase expressed in baculovirus-infected insect cells as compared with Escherichia coli
    • Soldatova LN, Crameri R, Gmachl M, Kemeny DM, Schmidt M, Weber M, et al: Superior biologic activity of the recombinant bee venom allergen hyaluronidase expressed in baculovirus-infected insect cells as compared with Escherichia coli. J Allergy Clin Immunol 1998;101:691-698.
    • (1998) J Allergy Clin Immunol , vol.101 , pp. 691-698
    • Soldatova, L.N.1    Crameri, R.2    Gmachl, M.3    Kemeny, D.M.4    Schmidt, M.5    Weber, M.6
  • 134
    • 0033763677 scopus 로고    scopus 로고
    • Identification, cloning, and characterization of a major cat flea salivary allergen (Cte f 1)
    • McDermott MJ, Weber E, Hunter S, Stedman KE, Best E, Frank GR, et al: Identification, cloning, and characterization of a major cat flea salivary allergen (Cte f 1). Mol Immunol 2000;37:361-375.
    • (2000) Mol Immunol , vol.37 , pp. 361-375
    • McDermott, M.J.1    Weber, E.2    Hunter, S.3    Stedman, K.E.4    Best, E.5    Frank, G.R.6
  • 135
    • 0035214123 scopus 로고    scopus 로고
    • Expression, purification, characterization and clinical relevance of rAed a 1 - A 68-kDa recombinant mosquito Aedes aegypti salivary allergen
    • Peng Z, Xu W, James AA, Lam H, Sun D, Cheng L, et al: Expression, purification, characterization and clinical relevance of rAed a 1 - A 68-kDa recombinant mosquito Aedes aegypti salivary allergen. Int Immunol 2001;13:1445-1452.
    • (2001) Int Immunol , vol.13 , pp. 1445-1452
    • Peng, Z.1    Xu, W.2    James, A.A.3    Lam, H.4    Sun, D.5    Cheng, L.6
  • 136
    • 0001399408 scopus 로고    scopus 로고
    • Recombinant allergens with reduced allergenicity but retaining immunogenicity of the natural allergens: Hybrids of yellow jacket and paper wasp venom allergen antigen 5s
    • King TP, Jim SY, Monsalve RI, Kagey-Sobotka A, Lichtenstein LM, Spangfort MD: Recombinant allergens with reduced allergenicity but retaining immunogenicity of the natural allergens: Hybrids of yellow jacket and paper wasp venom allergen antigen 5s. J Immunol 2001;166:6057-6065.
    • (2001) J Immunol , vol.166 , pp. 6057-6065
    • King, T.P.1    Jim, S.Y.2    Monsalve, R.I.3    Kagey-Sobotka, A.4    Lichtenstein, L.M.5    Spangfort, M.D.6
  • 137
    • 0033949742 scopus 로고    scopus 로고
    • Rapid production of the major birch pollen allergen Bet v 1 in Nicotiana benthamiana plants and its immunological in vitro and in vivo characterization
    • Krebitz M, Wiedermann U, Essl D, Steinkellner H, Wagner B, Turpen TH, et al: Rapid production of the major birch pollen allergen Bet v 1 in Nicotiana benthamiana plants and its immunological in vitro and in vivo characterization. FASEB J 2000;14:1279-1288.
    • (2000) FASEB J , vol.14 , pp. 1279-1288
    • Krebitz, M.1    Wiedermann, U.2    Essl, D.3    Steinkellner, H.4    Wagner, B.5    Turpen, T.H.6
  • 139
    • 0028800805 scopus 로고
    • New insights into the mechanisms of immunotherapy
    • Durham SR: New insights into the mechanisms of immunotherapy. Eur Arch Otorhinolaryngol 1995;252(suppl 1):S64-S67.
    • (1995) Eur Arch Otorhinolaryngol , vol.252 , Issue.SUPPL. 1
    • Durham, S.R.1
  • 140
    • 0031784380 scopus 로고    scopus 로고
    • Immunologic changes associated with allergen immunotherapy
    • Durham SR, Till SJ: Immunologic changes associated with allergen immunotherapy. J Allergy Clin Immunol 1998;102:157-164.
    • (1998) J Allergy Clin Immunol , vol.102 , pp. 157-164
    • Durham, S.R.1    Till, S.J.2
  • 141
    • 0031908032 scopus 로고    scopus 로고
    • The TH1/TH2 paradigm in allergy
    • Maggi E: The TH1/TH2 paradigm in allergy. Immunotechnology 1998;3:233-244.
    • (1998) Immunotechnology , vol.3 , pp. 233-244
    • Maggi, E.1
  • 142
    • 0034110867 scopus 로고    scopus 로고
    • Mechanisms of allergen-specific immunotherapy
    • Akdis CA, Blaser K: Mechanisms of allergen-specific immunotherapy. Allergy 2000;55:522-530.
    • (2000) Allergy , vol.55 , pp. 522-530
    • Akdis, C.A.1    Blaser, K.2
  • 143
    • 0035044954 scopus 로고    scopus 로고
    • Mechanism of IL-10-induced T cell inactivation in allergic inflammation and normal response to allergens
    • Akdis CA, Joss A, Akdis M, Blaser K: Mechanism of IL-10-induced T cell inactivation in allergic inflammation and normal response to allergens. Int Arch Allergy Immunol 2001;124:180-182.
    • (2001) Int Arch Allergy Immunol , vol.124 , pp. 180-182
    • Akdis, C.A.1    Joss, A.2    Akdis, M.3    Blaser, K.4
  • 144
    • 0030963666 scopus 로고    scopus 로고
    • Human dendritic cells require exogenous interleukin-12-inducing factors to direct the development of naive T-helper cells toward the Th1 phenotype
    • Hilkens CM, Kalinski P, de Boer M, Kapsenberg ML: Human dendritic cells require exogenous interleukin-12-inducing factors to direct the development of naive T-helper cells toward the Th1 phenotype. Blood 1997;90:1920-1926.
    • (1997) Blood , vol.90 , pp. 1920-1926
    • Hilkens, C.M.1    Kalinski, P.2    De Boer, M.3    Kapsenberg, M.L.4
  • 146
    • 0033012903 scopus 로고    scopus 로고
    • The paradigm of type 1 and type 2 antigen-presenting cells. Implications for atopic allergy
    • Kapsenberg ML, Hilkens CM, Wierenga EA, Kalinski P: The paradigm of type 1 and type 2 antigen-presenting cells. Implications for atopic allergy. Clin Exp Allergy 1999;29(suppl 2):33-36.
    • (1999) Clin Exp Allergy , vol.29 , Issue.SUPPL. 2 , pp. 33-36
    • Kapsenberg, M.L.1    Hilkens, C.M.2    Wierenga, E.A.3    Kalinski, P.4
  • 148
    • 0034193991 scopus 로고    scopus 로고
    • Development of Th1-inducing capacity in myeloid dendritic cells requires environmental instruction
    • Vieira PL, de Jong EC, Wierenga EA, Kapsenberg ML, Kalinski P: Development of Th1-inducing capacity in myeloid dendritic cells requires environmental instruction. J Immunol 2000;164:4507-4512.
    • (2000) J Immunol , vol.164 , pp. 4507-4512
    • Vieira, P.L.1    De Jong, E.C.2    Wierenga, E.A.3    Kapsenberg, M.L.4    Kalinski, P.5
  • 149
    • 0035887771 scopus 로고    scopus 로고
    • Cytokines regulate the capacity of CD8alpha(+) and CD8alpha(-) dendritic cells to prime Th1/Th2 cells in vivo
    • Maldonado-Lopez R, Maliszewski C, Urbain J, Moser M: Cytokines regulate the capacity of CD8alpha(+) and CD8alpha(-) dendritic cells to prime Th1/Th2 cells in vivo. J Immunol 2001;167:4345-4350.
    • (2001) J Immunol , vol.167 , pp. 4345-4350
    • Maldonado-Lopez, R.1    Maliszewski, C.2    Urbain, J.3    Moser, M.4
  • 150
    • 0037083298 scopus 로고    scopus 로고
    • Microbial compounds selectively induce Th1 cell-promoting or Th2 cell-promoting dendritic cells in vitro with diverse th cell-polarizing signals
    • de Jong EC, Vieira PL, Kalinski P, Schuitemaker JH, Tanaka Y, Wierenga EA, et al: Microbial compounds selectively induce Th1 cell-promoting or Th2 cell-promoting dendritic cells in vitro with diverse th cell-polarizing signals. J Immunol 2002;168:1704-1709.
    • (2002) J Immunol , vol.168 , pp. 1704-1709
    • De Jong, E.C.1    Vieira, P.L.2    Kalinski, P.3    Schuitemaker, J.H.4    Tanaka, Y.5    Wierenga, E.A.6
  • 151
    • 0036518287 scopus 로고    scopus 로고
    • Mouse and human dendritic cell subtypes
    • Shortman K, Liu YJ: Mouse and human dendritic cell subtypes. Nat Rev Immunol 2002;2:151-161.
    • (2002) Nat Rev Immunol , vol.2 , pp. 151-161
    • Shortman, K.1    Liu, Y.J.2
  • 152
    • 0037134046 scopus 로고    scopus 로고
    • Allergy, parasites and the hygiene hypothesis
    • Yazdanbakhsh M, Kremsner PG, van Ree R: Allergy, parasites and the hygiene hypothesis. Science 2002;296:490-494.
    • (2002) Science , vol.296 , pp. 490-494
    • Yazdanbakhsh, M.1    Kremsner, P.G.2    Van Ree, R.3
  • 153
    • 0035524488 scopus 로고    scopus 로고
    • Toll-like receptors and innate immunity
    • Medzhitov R: Toll-like receptors and innate immunity. Nat Rev Immunol 2001;1:135-145.
    • (2001) Nat Rev Immunol , vol.1 , pp. 135-145
    • Medzhitov, R.1
  • 155
    • 0034793409 scopus 로고    scopus 로고
    • Proinflammatory activity of glycosylphosphatidylinositol anchors derived from Trypanosoma cruzi: Structural and functional analyses
    • Almeida IC, Gazzinelli RT: Proinflammatory activity of glycosylphosphatidylinositol anchors derived from Trypanosoma cruzi: Structural and functional analyses. J Leukoc Biol 2001;70:467-477.
    • (2001) J Leukoc Biol , vol.70 , pp. 467-477
    • Almeida, I.C.1    Gazzinelli, R.T.2
  • 156
    • 0037018097 scopus 로고    scopus 로고
    • Adjuvants of immunity: Harnessing innate immunity to promote adaptive immunity
    • Bendelac A, Medzhitov R: Adjuvants of immunity: Harnessing innate immunity to promote adaptive immunity. J Exp Med 2002;195:F19-F23.
    • (2002) J Exp Med , vol.195
    • Bendelac, A.1    Medzhitov, R.2
  • 157
    • 0036606913 scopus 로고    scopus 로고
    • Lipopolysaccharide recognition: CD14, TLRs and the LPS-activation cluster
    • Triantafilou M, Triantafilou K: Lipopolysaccharide recognition: CD14, TLRs and the LPS-activation cluster. Trends Immunol 2002;23:301-304.
    • (2002) Trends Immunol , vol.23 , pp. 301-304
    • Triantafilou, M.1    Triantafilou, K.2


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