메뉴 건너뛰기




Volumn 175, Issue 6, 2005, Pages 3835-3845

The crystal structure of recombinant proDer p 1, a major house-dust mite proteolytic allergen

Author keywords

[No Author keywords available]

Indexed keywords

ALLERGEN; CYSTEINE PROTEINASE; HOUSE DUST ALLERGEN; IMMUNOGLOBULIN E;

EID: 24744439695     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: 10.4049/jimmunol.175.6.3835     Document Type: Article
Times cited : (76)

References (53)
  • 3
    • 6344222889 scopus 로고    scopus 로고
    • Allergy vaccine engineering: Epitope modulation of recombinant Bet v 1 reduces IgE binding but retains protein folding pattern for induction of protective blocking-antibody responses
    • Holm, J., M. Gajhede, M. Ferreras, A. Henriksen, H. Ipsen, J. N. Larsen, L. Lund, H. Jacobi, A. Millner, P. A. Wurtzen, et al. 2004. Allergy vaccine engineering: epitope modulation of recombinant Bet v 1 reduces IgE binding but retains protein folding pattern for induction of protective blocking-antibody responses. J. Immunol. 173: 5258-5267.
    • (2004) J. Immunol. , vol.173 , pp. 5258-5267
    • Holm, J.1    Gajhede, M.2    Ferreras, M.3    Henriksen, A.4    Ipsen, H.5    Larsen, J.N.6    Lund, L.7    Jacobi, H.8    Millner, A.9    Wurtzen, P.A.10
  • 6
    • 0023277095 scopus 로고
    • Selection and characterization of monoclonal antibodies against a major allergen in Dermatophagoides pteronyssinus: Species-specific and common epitopes in three dermatophagoides species
    • Horn, N., and P. Lind. 1987. Selection and characterization of monoclonal antibodies against a major allergen in Dermatophagoides pteronyssinus: species-specific and common epitopes in three dermatophagoides species. Int. Arch. Allergy Appl. Immunol. 83: 404-409.
    • (1987) Int. Arch. Allergy Appl. Immunol. , vol.83 , pp. 404-409
    • Horn, N.1    Lind, P.2
  • 7
    • 0023683647 scopus 로고
    • The binding of mouse hybridoma and human IgE antibodies to the major fecal allergen, der p I, of Dermatophagoides pteronyssinus: Relative binding site location and species specificity studied by solid-phase inhibition assays with radiolabeled antigen
    • Lind, P., O. C. Hansen, and N. Horn. 1988. The binding of mouse hybridoma and human IgE antibodies to the major fecal allergen, Der p I, of Dermatophagoides pteronyssinus: relative binding site location and species specificity studied by solid-phase inhibition assays with radiolabeled antigen. J. Immunol. 140: 4256-4264.
    • (1988) J. Immunol. , vol.140 , pp. 4256-4264
    • Lind, P.1    Hansen, O.C.2    Horn, N.3
  • 8
    • 0029973947 scopus 로고    scopus 로고
    • The isolation and characterization of a novel collagenolytic serine protease allergen (Der p 9) from the dust mite Dermatophagoides pteronyssinus
    • King, C., R. J. Simpson, R. L. Moritz, G. E. Reed, P. J. Thompson, and G. A. Stewart. 1996. The isolation and characterization of a novel collagenolytic serine protease allergen (Der p 9) from the dust mite Dermatophagoides pteronyssinus. J. Allergy Clin. Immunol. 98: 739-747.
    • (1996) J. Allergy Clin. Immunol. , vol.98 , pp. 739-747
    • King, C.1    Simpson, R.J.2    Moritz, R.L.3    Reed, G.E.4    Thompson, P.J.5    Stewart, G.A.6
  • 9
    • 0022217487 scopus 로고
    • Purification and partial characterization of two major allergens from the house dust mite Dermatophagoides pteronyssinus
    • Lind, P. 1985. Purification and partial characterization of two major allergens from the house dust mite Dermatophagoides pteronyssinus. J. Allergy Clin. Immunol. 76: 753-761.
    • (1985) J. Allergy Clin. Immunol. , vol.76 , pp. 753-761
    • Lind, P.1
  • 10
    • 0032902043 scopus 로고    scopus 로고
    • The interaction between the dust mite antigen der p 1 and cell-signalling molecules in amplifying allergic disease
    • Schulz, O., H. F. Sewell, and F. Shakib. 1999. The interaction between the dust mite antigen Der p 1 and cell-signalling molecules in amplifying allergic disease. Clin. Exp. Allergy 29: 439-444.
    • (1999) Clin. Exp. Allergy , vol.29 , pp. 439-444
    • Schulz, O.1    Sewell, H.F.2    Shakib, F.3
  • 11
    • 0023877882 scopus 로고
    • Sequence analysis of cDNA coding for a major house dust mite allergen, der p 1: Homology with cysteine proteases
    • Chua, K. Y., G. A. Stewart, W. R. Thomas, R. J. Simpson, R. J. Dilworth, T. M. Plozza, and K. J. Turner. 1988. Sequence analysis of cDNA coding for a major house dust mite allergen, Der p 1: homology with cysteine proteases. J. Exp. Med. 167: 175-182.
    • (1988) J. Exp. Med. , vol.167 , pp. 175-182
    • Chua, K.Y.1    Stewart, G.A.2    Thomas, W.R.3    Simpson, R.J.4    Dilworth, R.J.5    Plozza, T.M.6    Turner, K.J.7
  • 12
    • 0027214181 scopus 로고
    • Sequence polymorphisms of cDNA clones encoding the mite allergen der p 1
    • Chua, K. Y., P. K. Kehal, and W. R. Thomas. 1993. Sequence polymorphisms of cDNA clones encoding the mite allergen Der p 1. Int. Arch. Allergy Immunol. 101: 364-368.
    • (1993) Int. Arch. Allergy Immunol. , vol.101 , pp. 364-368
    • Chua, K.Y.1    Kehal, P.K.2    Thomas, W.R.3
  • 13
    • 0025787912 scopus 로고
    • Processing of the papain precursor: Purification of the zymogeti and characterization of its mechanism of processing
    • Vernet, T., H. E. Khouri, P. Laflamme, D. C. Tessier, R. Musil, B. J. Gour-Salin, A. C. Storer, and D. Y. Thomas. 1991. Processing of the papain precursor: purification of the zymogeti and characterization of its mechanism of processing. J. Biol. Chem. 266: 21451-21457.
    • (1991) J. Biol. Chem. , vol.266 , pp. 21451-21457
    • Vernet, T.1    Khouri, H.E.2    Laflamme, P.3    Tessier, D.C.4    Musil, R.5    Gour-Salin, B.J.6    Storer, A.C.7    Thomas, D.Y.8
  • 14
    • 0023644876 scopus 로고
    • Requirement of pro-sequence for the production of active subtilisin e in Escherichia coli
    • Ikemura, H., H. Takagi, and M. Inouye. 1987. Requirement of pro-sequence for the production of active subtilisin E in Escherichia coli. J. Biol. Chem. 262: 7859-7864.
    • (1987) J. Biol. Chem. , vol.262 , pp. 7859-7864
    • Ikemura, H.1    Takagi, H.2    Inouye, M.3
  • 15
    • 0025748612 scopus 로고
    • IgE and IgG binding of peptides expressed from fragments of cDNA encoding the major house dust mite allergen der p 1
    • Greene, W. K., J. G. Cyster, K. Y. Chua, R. M. O'Brien, and W. R. Thomas. 1991. IgE and IgG binding of peptides expressed from fragments of cDNA encoding the major house dust mite allergen Der p 1. J. Immunol. 147: 3768-3773.
    • (1991) J. Immunol. , vol.147 , pp. 3768-3773
    • Greene, W.K.1    Cyster, J.G.2    Chua, K.Y.3    O'Brien, R.M.4    Thomas, W.R.5
  • 16
    • 0035987313 scopus 로고    scopus 로고
    • High-level expression of recombinant house dust mite allergen der p 1 in Pichia postons
    • Jacquet, A., M. Magi, H. Petry, and A. Bollen. 2002. High-level expression of recombinant house dust mite allergen Der p 1 in Pichia postons. Clin. Exp. Allergy 32: 1048-1053.
    • (2002) Clin. Exp. Allergy , vol.32 , pp. 1048-1053
    • Jacquet, A.1    Magi, M.2    Petry, H.3    Bollen, A.4
  • 17
    • 0037032461 scopus 로고    scopus 로고
    • Maturation of the activities of recombinant mite allergens der p 1 and der f 1, and its implication in the blockade of proteolytic activity
    • Takai, T., R. Mineki, T. Nakazawa, M. Takaoka, H. Yasueda, K. Murayama, K. Okumura, and H. Ogawa. 2002. Maturation of the activities of recombinant mite allergens Der p 1 and Der f 1, and its implication in the blockade of proteolytic activity. FEBS Lett. 531: 265-272.
    • (2002) FEBS Lett. , vol.531 , pp. 265-272
    • Takai, T.1    Mineki, R.2    Nakazawa, T.3    Takaoka, M.4    Yasueda, H.5    Murayama, K.6    Okumura, K.7    Ogawa, H.8
  • 20
    • 0028674466 scopus 로고
    • Catalytic mechanism in papain family of cysteine peptidases
    • Storer, A. C., and R. Menard. 1994. Catalytic mechanism in papain family of cysteine peptidases. Methods Enzymol. 244: 486-500.
    • (1994) Methods Enzymol. , vol.244 , pp. 486-500
    • Storer, A.C.1    Menard, R.2
  • 21
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho, S. N., H. D. Hunt, R. M. Horton, J. K. Pullen, and L. R. Pease. 1989. Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77: 51-59.
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 22
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • C. W. Carter Jr. and R. M. Sweet, eds. Academic Press, New York
    • Otwinowski, Z., and W. Minor. 1997. Processing of X-ray diffraction data collected in oscillation mode. In Methods in Enzymology: Macromolecular Crystallography, Vol. 276, Pt. A. C. W. Carter Jr. and R. M. Sweet, eds. Academic Press, New York, p. 307-326.
    • (1997) Methods in Enzymology: Macromolecular Crystallography , vol.276 , Issue.PART A , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 23
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4. 1994. The CCP4 suite: programs for protein crystallography. Acta Cryst. D 50: 760-763.
    • (1994) Acta Cryst. D , vol.50 , pp. 760-763
  • 24
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An automated program for molecular replacement
    • Vagin, A., and A. Teplyakov. 1997. MOLREP: an automated program for molecular replacement. J. Appl. Cryst. 30: 1022-1025.
    • (1997) J. Appl. Cryst. , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 26
    • 0005797141 scopus 로고    scopus 로고
    • The ARP/WARP suite for automated construction and refinement of protein models
    • M. G. Rossmann and E. Arnold, eds. Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Lamzin, V. S., A. Perrakis, and K. S. Wilson. 2001. The ARP/WARP suite for automated construction and refinement of protein models. In Crystallography of Biological Macromolecules, Vol. F. M. G. Rossmann and E. Arnold, eds. Kluwer Academic Publishers, Dordrecht, The Netherlands, p. 720-722.
    • (2001) Crystallography of Biological Macromolecules , vol.F , pp. 720-722
    • Lamzin, V.S.1    Perrakis, A.2    Wilson, K.S.3
  • 27
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T. A., J.-Y. Zou, S. W. Cowan, and M. Kjeldgaard. 1991. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Cryst. A 47: 110-119.
    • (1991) Acta Cryst. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 28
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov, G. N., A. A. Vagin, and E. J. Dodson. 1997. Refinement of macromolecular structures by the maximum-likelihood method. Acta Cryst. D 53: 240-255.
    • (1997) Acta Cryst. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 29
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger, A. T. 1992. Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 355: 472-475.
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.T.1
  • 30
    • 0030809260 scopus 로고    scopus 로고
    • ARP: Improvement and extension of crystallographic phases by weighted averaging of multiple-refined dummy atomic models
    • Perrakis, A., T. K. Sixma, K. S. Wilson, and V. S. Lamzin. 1997. wARP: improvement and extension of crystallographic phases by weighted averaging of multiple-refined dummy atomic models. Acta Cryst. D53: 448-455.
    • (1997) Acta Cryst. , vol.D53 , pp. 448-455
    • Perrakis, A.1    Sixma, T.K.2    Wilson, K.S.3    Lamzin, V.S.4
  • 31
    • 0015838530 scopus 로고
    • Crossed-line immunoelectrophoresis (73, 76)
    • Krøll, J. 1973. Crossed-line immunoelectrophoresis (73, 76). Scand. J. Immunol. 2(Suppl. 1): 79-81.
    • (1973) Scand. J. Immunol. , vol.2 , Issue.SUPPL. 1 , pp. 79-81
    • Krøll, J.1
  • 32
    • 0015878020 scopus 로고
    • Immunization, isolation of immunoglobulins, estimation of antibody titre
    • Harboe, N., and A. Ingild. 1973. Immunization, isolation of immunoglobulins, estimation of antibody titre. Scand. J. Immunol. 2(Suppl. 1): 161-164.
    • (1973) Scand. J. Immunol. , vol.2 , Issue.SUPPL. 1 , pp. 161-164
    • Harboe, N.1    Ingild, A.2
  • 33
    • 0015776376 scopus 로고
    • A manual of quantitative immunoelectrophoresis: Methods and applications. 1. General remarks on principles, equipment, reagents and procedures
    • Weeke, B. 1973. A manual of quantitative immunoelectrophoresis: methods and applications. 1. General remarks on principles, equipment, reagents and procedures. Scand. J. Immunol. 2(Suppl. 1): 15-35.
    • (1973) Scand. J. Immunol. , vol.2 , Issue.SUPPL. 1 , pp. 15-35
    • Weeke, B.1
  • 35
    • 13544249596 scopus 로고    scopus 로고
    • Molecular characterization of major cat allergen Pel d 1: Expression of heterodimer by use of a baculovirus expression system
    • Seppala, U., P. Hagglund, P. A. Wurtzen, H. Ipsen, P. Thorsted, T. Lenhard, P. Roepstorff, and M. D. Spangfort. 2005. Molecular characterization of major cat allergen Pel d 1: expression of heterodimer by use of a baculovirus expression system. J. Biol. Chem. 280: 3208-3216.
    • (2005) J. Biol. Chem. , vol.280 , pp. 3208-3216
    • Seppala, U.1    Hagglund, P.2    Wurtzen, P.A.3    Ipsen, H.4    Thorsted, P.5    Lenhard, T.6    Roepstorff, P.7    Spangfort, M.D.8
  • 37
    • 0001528720 scopus 로고    scopus 로고
    • Exact and efficient analytical calculation of the accessible surface areas and their gradients for macromolecules
    • Fraczkiewicz, R., and W. Braun. 1998. Exact and efficient analytical calculation of the accessible surface areas and their gradients for macromolecules. J. Comput. Chem. 19: 319-333.
    • (1998) J. Comput. Chem. , vol.19 , pp. 319-333
    • Fraczkiewicz, R.1    Braun, W.2
  • 38
    • 0015222647 scopus 로고
    • The interpretation of protein structures: Estimation of static accessibility
    • Lee, B., and F. M. Richards. 1971. The interpretation of protein structures: estimation of static accessibility. J. Mol. Biol. 55: 379-400.
    • (1971) J. Mol. Biol. , vol.55 , pp. 379-400
    • Lee, B.1    Richards, F.M.2
  • 39
    • 0026065591 scopus 로고
    • Sequence analysis of cDNA coding for a major house dust mite allergen, der f I
    • Dilworth, R. J., K. Y. Chua, and W. R. Thomas. 1991. Sequence analysis of cDNA coding for a major house dust mite allergen, Der f I. Clin. Exp. Allergy 21: 25-32.
    • (1991) Clin. Exp. Allergy , vol.21 , pp. 25-32
    • Dilworth, R.J.1    Chua, K.Y.2    Thomas, W.R.3
  • 40
    • 0027394245 scopus 로고
    • Two distinct gene subfamilies within the family of cysteine protease genes
    • Karrer, K. M., S. L. Peiffer, and M. E. DiTomas. 1993. Two distinct gene subfamilies within the family of cysteine protease genes. Proc. Natl. Acad. Sci. USA 90: 3063-3067.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 3063-3067
    • Karrer, K.M.1    Peiffer, S.L.2    Ditomas, M.E.3
  • 41
    • 1842781469 scopus 로고    scopus 로고
    • Protein structure comparison in 3D based on secondary structure matching (SSM) followed by Cα alignment, scored by a new structural similarity function
    • A. J. Kungl and P. J. Kungl, eds. Vienna
    • Krissinel, E., and K. Henrick. 2003. Protein structure comparison in 3D based on secondary structure matching (SSM) followed by Cα alignment, scored by a new structural similarity function. In Proceedings of the 5th International Conference on Molecular Structural Biology. A. J. Kungl and P. J. Kungl, eds. Vienna, p. 88.
    • (2003) Proceedings of the 5th International Conference on Molecular Structural Biology , pp. 88
    • Krissinel, E.1    Henrick, K.2
  • 42
    • 0030587773 scopus 로고    scopus 로고
    • The prosequence of procaricain forms an α-helical domain that prevents access to the substrate-binding cleft
    • Groves, M. R., M. A. Taylor, M. Scott, N. J. Cummings, R. W. Pickersgill, and J. A. Jenkins. 1996. The prosequence of procaricain forms an α-helical domain that prevents access to the substrate-binding cleft. Structure 4: 1193-1203.
    • (1996) Structure , vol.4 , pp. 1193-1203
    • Groves, M.R.1    Taylor, M.A.2    Scott, M.3    Cummings, N.J.4    Pickersgill, R.W.5    Jenkins, J.A.6
  • 43
    • 0029902382 scopus 로고    scopus 로고
    • Structure of human procathepsin L reveals the molecular basis of inhibition by the prosegment
    • Coulombe, R., P. Grochulski, J. Sivaraman, R. Menard, J. S. Mort, and M. Cygler. 1996. Structure of human procathepsin L reveals the molecular basis of inhibition by the prosegment. EMBO J. 15: 5492-5503.
    • (1996) EMBO J. , vol.15 , pp. 5492-5503
    • Coulombe, R.1    Grochulski, P.2    Sivaraman, J.3    Menard, R.4    Mort, J.S.5    Cygler, M.6
  • 44
    • 0031826072 scopus 로고    scopus 로고
    • Structural basis for specificity of papain-like cysteine protease proregions toward their cognate enzymes
    • Groves, M. R., R. Coulombe, J. Jenkins, and M. Cygler. 1998. Structural basis for specificity of papain-like cysteine protease proregions toward their cognate enzymes. Proteins 32: 504-514.
    • (1998) Proteins , vol.32 , pp. 504-514
    • Groves, M.R.1    Coulombe, R.2    Jenkins, J.3    Cygler, M.4
  • 45
    • 0017138215 scopus 로고
    • Binding of chloromethyl ketone substrate analogues to crystalline papain
    • Drenth, J., K. H. Kalk, and H. M. Swen. 1976. Binding of chloromethyl ketone substrate analogues to crystalline papain. Biochemistry 15: 3731-3738.
    • (1976) Biochemistry , vol.15 , pp. 3731-3738
    • Drenth, J.1    Kalk, K.H.2    Swen, H.M.3
  • 47
    • 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., P. G. de Heer, W. A. van Leeuwen, N. I. Derksen, M. Muller, S. Huveneers, R. C. Aalberse, and R. van Ree. 2002. 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. 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    Aalberse, R.C.7    Van Ree, R.8
  • 48
    • 0035002937 scopus 로고    scopus 로고
    • Effects of site-directed mutagenesis in the cysteine residues and the N-glycosylation motif in recombinant der f 1 on secretion and protease activity
    • Takahashi, K., T. Takai, T. Yasuhara, T. Yokota, and Y. Okumura. 2001. Effects of site-directed mutagenesis in the cysteine residues and the N-glycosylation motif in recombinant Der f 1 on secretion and protease activity. Int. Arch. Allergy Immunol. 124: 454-460.
    • (2001) Int. Arch. Allergy Immunol. , vol.124 , pp. 454-460
    • Takahashi, K.1    Takai, T.2    Yasuhara, T.3    Yokota, T.4    Okumura, Y.5
  • 49
    • 0035138773 scopus 로고    scopus 로고
    • Biologically active recombinant forms of a major house dust mite group 1 allergen der f 1 with full activities of both cysteine protease and IgE binding
    • Yasuhara, T., T. Takai, T. Yuuki, H. Okudaira, and Y. Okumura. 2001. Biologically active recombinant forms of a major house dust mite group 1 allergen Der f 1 with full activities of both cysteine protease and IgE binding. Clin. Exp. Allergy 31: 116-124.
    • (2001) Clin. Exp. Allergy , vol.31 , pp. 116-124
    • Yasuhara, T.1    Takai, T.2    Yuuki, T.3    Okudaira, H.4    Okumura, Y.5
  • 50
    • 0031857266 scopus 로고    scopus 로고
    • A sensitive fluorescent assay for measuring the cysteine protease activity of der p 1, a major allergen from the dust mite Dermatophagoides pteronyssinus
    • Schulz, O., H. F. Sewell, and F. Shakib. 1998. A sensitive fluorescent assay for measuring the cysteine protease activity of Der p 1, a major allergen from the dust mite Dermatophagoides pteronyssinus. Mol. Pathol. 51: 222-224.
    • (1998) Mol. Pathol. , vol.51 , pp. 222-224
    • Schulz, O.1    Sewell, H.F.2    Shakib, F.3
  • 51
    • 0032127867 scopus 로고    scopus 로고
    • A mite subversive: Cleavage of CD23 and CD25 by der p 1 enhances allergenicity
    • Shakib, F., O. Schulz, and H. Sewell. 1998. A mite subversive: cleavage of CD23 and CD25 by Der p 1 enhances allergenicity. Immunol. Today 19: 313-316.
    • (1998) Immunol. Today , vol.19 , pp. 313-316
    • Shakib, F.1    Schulz, O.2    Sewell, H.3
  • 53
    • 0031056815 scopus 로고    scopus 로고
    • Heterogeneous proteolytic specificity and activity of the house dust mite proteinase allergen der p I
    • Hewitt, C. R., H. Horton, R. M. Jones, and D. I. Pritchard. 1997. Heterogeneous proteolytic specificity and activity of the house dust mite proteinase allergen Der p I. Clin. Exp. Allergy 27: 201-207.
    • (1997) Clin. Exp. Allergy , vol.27 , pp. 201-207
    • Hewitt, C.R.1    Horton, H.2    Jones, R.M.3    Pritchard, D.I.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.