메뉴 건너뛰기




Volumn 9, Issue 8, 2010, Pages 957-969

Plant-made pharmaceuticals for the prevention and treatment of autoimmune diseases: Where are we?

Author keywords

autoantigen; autoimmune disease; oral tolerance; plant made pharmaceutical; recombinant protein; transgenic plant

Indexed keywords

ADJUVANT; AUTOANTIGEN; GLUTAMATE DECARBOXYLASE 67; INSULIN; INTERLEUKIN 10; INTERLEUKIN 13; INTERLEUKIN 4; PROINSULIN; RECOMBINANT PROTEIN;

EID: 77955263232     PISSN: 14760584     EISSN: 17448395     Source Type: Journal    
DOI: 10.1586/erv.10.82     Document Type: Review
Times cited : (14)

References (97)
  • 1
    • 74049110516 scopus 로고    scopus 로고
    • Checkpoints in lymphocyte development and autoimmune disease
    • von Boehmer H, Melchers F. Checkpoints in lymphocyte development and autoimmune disease. Nat. Immunol. 11(1), 14-20 (2010).
    • (2010) Nat. Immunol. , vol.11 , Issue.1 , pp. 14-20
    • Von Boehmer, H.1    Melchers, F.2
  • 2
    • 71649083353 scopus 로고    scopus 로고
    • Clustering and commonalities among autoimmune diseases
    • Mackay IR. Clustering and commonalities among autoimmune diseases. J. Autoimmun. 33(3-4), 170-177 (2009).
    • (2009) J. Autoimmun. , vol.33 , Issue.3-4 , pp. 170-177
    • MacKay, I.R.1
  • 3
    • 2442484053 scopus 로고    scopus 로고
    • Naturally arising CD4+ regulatory T cells for immunologic self-tolerance and negative control of immune responses
    • Sakaguchi S. Naturally arising CD4+ regulatory T cells for immunologic self-tolerance and negative control of immune responses. Annu. Rev. Immunol. 22, 531-562 (2004).
    • (2004) Annu. Rev. Immunol. , vol.22 , pp. 531-562
    • Sakaguchi, S.1
  • 4
    • 0034655277 scopus 로고    scopus 로고
    • Persistence of physiological self antigen is required for the regulation of self tolerance
    • Garza KM, Agersborg SS, Baker E, Tung KS. Persistence of physiological self antigen is required for the regulation of self tolerance. J. Immunol. 164(8), 3982-3989 (2000).
    • (2000) J. Immunol. , vol.164 , Issue.8 , pp. 3982-3989
    • Garza, K.M.1    Agersborg, S.S.2    Baker, E.3    Tung, K.S.4
  • 5
    • 0001131263 scopus 로고    scopus 로고
    • Immunology of insulin-dependent diabetes mellitus
    • Pickup J, Williams G (Eds). Blackwell Science Ltd, Oxford, UK
    • Lernmark A, Falorni A. Immunology of insulin-dependent diabetes mellitus. In: Textbook of Diabetes. Pickup J, Williams G (Eds). Blackwell Science Ltd, Oxford, UK, 15.11-15.23 (1997).
    • (1997) Textbook of Diabetes , pp. 1511-1523
    • Lernmark, A.1    Falorni, A.2
  • 6
    • 0027370108 scopus 로고
    • The effect of intensive treatment of diabetes on the development and progression of long-term complications in insulin-dependent diabetes mellitus
    • The Diabetes Control and Complications Trial Research Group
    • The effect of intensive treatment of diabetes on the development and progression of long-term complications in insulin-dependent diabetes mellitus. The Diabetes Control and Complications Trial Research Group. N. Engl. J. Med. 329(14), 977-986 (1993).
    • (1993) N. Engl. J. Med. , vol.329 , Issue.14 , pp. 977-986
  • 7
    • 77951901513 scopus 로고    scopus 로고
    • Immunotherapy of Type 1 diabetes: Where are we and where should we be going?
    • Luo X, Herold KC, Miller SD. Immunotherapy of Type 1 diabetes: where are we and where should we be going? Immunity 32(4), 488-499 (2010).
    • (2010) Immunity , vol.32 , Issue.4 , pp. 488-499
    • Luo, X.1    Herold, K.C.2    Miller, S.D.3
  • 8
    • 0038011833 scopus 로고    scopus 로고
    • Evolving concepts of rheumatoid arthritis
    • Firestein GS. Evolving concepts of rheumatoid arthritis. Nature 423(6937), 356-361 (2003).
    • (2003) Nature , vol.423 , Issue.6937 , pp. 356-361
    • Firestein, G.S.1
  • 9
    • 75649131191 scopus 로고    scopus 로고
    • Developments in the scientific understanding of rheumatoid arthritis
    • Goronzy JJ, Weyand CM. Developments in the scientific understanding of rheumatoid arthritis. Arthritis Res. Ther. 11(5), 249 (2009).
    • (2009) Arthritis Res. Ther. , vol.11 , Issue.5 , pp. 249
    • Goronzy, J.J.1    Weyand, C.M.2
  • 10
    • 60449096601 scopus 로고    scopus 로고
    • Current concepts in the pathogenesis of early rheumatoid arthritis
    • Pratt AG, Isaacs JD, Mattey DL. Current concepts in the pathogenesis of early rheumatoid arthritis. BestPract. Res. Clin. Rheumatol. 23(1), 37-48 (2009).
    • (2009) BestPract. Res. Clin. Rheumatol. , vol.23 , Issue.1 , pp. 37-48
    • Pratt, A.G.1    Isaacs, J.D.2    Mattey, D.L.3
  • 11
    • 34248136828 scopus 로고    scopus 로고
    • Inflammatory bowel disease: Cause and immunobiology
    • Baumgart DC, Carding SR. Inflammatory bowel disease: cause and immunobiology. Lancet 369(9573), 1627-1640 (2007).
    • (2007) Lancet , vol.369 , Issue.9573 , pp. 1627-1640
    • Baumgart, D.C.1    Carding, S.R.2
  • 12
    • 67650360252 scopus 로고    scopus 로고
    • Therapy with GAD in diabetes
    • Ludvigsson J. Therapy with GAD in diabetes. Diabetes Metab. Res. Rev. 25(4), 307-315 (2009).
    • (2009) Diabetes Metab. Res. Rev. , vol.25 , Issue.4 , pp. 307-315
    • Ludvigsson, J.1
  • 13
    • 55249110198 scopus 로고    scopus 로고
    • GAD treatment and insulin secretion in recent-onset type 1 diabetes
    • Ludvigsson J, Faresjo M, Hjorth M et al. GAD treatment and insulin secretion in recent-onset type 1 diabetes. N. Engl. J. Med. 359(18), 1909-1920 (2008).
    • (2008) N. Engl. J. Med. , vol.359 , Issue.18 , pp. 1909-1920
    • Ludvigsson, J.1    Faresjo, M.2    Hjorth, M.3
  • 14
    • 33750594907 scopus 로고    scopus 로고
    • The prospect of vaccination to prevent Type 1 diabetes
    • Harrison LC. The prospect of vaccination to prevent Type 1 diabetes. Hum. Vaccin. 1(4), 143-150 (2005).
    • (2005) Hum. Vaccin. , vol.1 , Issue.4 , pp. 143-150
    • Harrison, L.C.1
  • 15
    • 33745491280 scopus 로고    scopus 로고
    • Treating autoimmune diseases through restoration of antigen- specific immune tolerance
    • Wolfraim LA. Treating autoimmune diseases through restoration of antigen- specific immune tolerance. Arch. Immunol. Ther. Exp. (Warsz.) 54(1), 1-13 (2006).
    • (2006) Arch. Immunol. Ther. Exp. (Warsz.) , vol.54 , Issue.1 , pp. 1-13
    • Wolfraim, L.A.1
  • 17
    • 0037472399 scopus 로고    scopus 로고
    • Targeting of plant-derived vaccine antigens to immunoresponsive mucosal sites
    • Rigano MM, Sala F, Arntzen CJ, Walmsley AM. Targeting of plant-derived vaccine antigens to immunoresponsive mucosal sites. Vaccine 1(7-8), 809-811 (2003).
    • (2003) Vaccine , vol.1 , Issue.7-8 , pp. 809-811
    • Rigano, M.M.1    Sala, F.2    Arntzen, C.J.3    Walmsley, A.M.4
  • 18
    • 34250345663 scopus 로고    scopus 로고
    • Bioproduction of therapeutic proteins in the 21st Century and the role of plants and plant cells as production platforms
    • Boehm R. Bioproduction of therapeutic proteins in the 21st Century and the role of plants and plant cells as production platforms. Ann. NY Acad. Sci. 1102, 121-134 (2007).
    • (2007) Ann. NY Acad. Sci. , vol.1102 , pp. 121-134
    • Boehm, R.1
  • 19
    • 0342477466 scopus 로고
    • Biosynthesis and periplasmic segregation of human proinsulin in Escherichia coli
    • Chan SJ, Weiss J, Konrad M et al. Biosynthesis and periplasmic segregation of human proinsulin in Escherichia coli. Proc. Natl Acad. Sci. USA 78(9), 5401-5405 (1981).
    • (1981) Proc. Natl Acad. Sci. USA , vol.78 , Issue.9 , pp. 5401-5405
    • Chan, S.J.1    Weiss, J.2    Konrad, M.3
  • 20
    • 0022543650 scopus 로고
    • Secretion and processing of insulin precursors in yeast
    • Thim L, Hansen MT, Norris K et al. Secretion and processing of insulin precursors in yeast. Proc. Natl Acad. Sci. USA 83(18), 6766-6770 (1986).
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , Issue.18 , pp. 6766-6770
    • Thim, L.1    Hansen, M.T.2    Norris, K.3
  • 21
    • 0035810269 scopus 로고    scopus 로고
    • Human insulin from a precursor overexpressed in the methylotrophic yeast Pichia pastoris and a simple procedure for purifying the expression product
    • Wang Y, Liang ZH, Zhang YS et al. Human insulin from a precursor overexpressed in the methylotrophic yeast Pichia pastoris and a simple procedure for purifying the expression product. Biotechnol. Bioeng. 73(1), 74-79 (2001).
    • (2001) Biotechnol. Bioeng. , vol.73 , Issue.1 , pp. 74-79
    • Wang, Y.1    Zh, L.2    Zhang, Y.S.3
  • 22
    • 0026658003 scopus 로고
    • Processing of mutated proinsulin with tetrabasic cleavage sites to bioactive insulin in the non-endocrine cell line, COS-7
    • Yanagita M, Nakayama K, Takeuchi T. Processing of mutated proinsulin with tetrabasic cleavage sites to bioactive insulin in the non-endocrine cell line, COS-7. FEBS Lett. 311(1), 55-59 (1992).
    • (1992) FEBS Lett. , vol.311 , Issue.1 , pp. 55-59
    • Yanagita, M.1    Nakayama, K.2    Takeuchi, T.3
  • 23
    • 33645309590 scopus 로고    scopus 로고
    • Transgenic expression and recovery of biologically active recombinant human insulin from Arabidopsis thaliana seeds
    • Nykiforuk CL, Boothe JG, Murray EW et al. Transgenic expression and recovery of biologically active recombinant human insulin from Arabidopsis thaliana seeds. Plant Biotechnol. J. 4(1), 77-85 (2006).
    • (2006) Plant Biotechnol. J. , vol.4 , Issue.1 , pp. 77-85
    • Nykiforuk, C.L.1    Boothe, J.G.2    Murray, E.W.3
  • 24
    • 77955244776 scopus 로고    scopus 로고
    • Analytical characterization, safety and clinical bioequivalence of recombinant human insulin from transgenic plants
    • Presented at: New Orleans, LA, USA, 5-9 June
    • Boothe JG, Nykiforuk CL, Kuhlman PA et al. Analytical characterization, safety and clinical bioequivalence of recombinant human insulin from transgenic plants. Presented at: American Diabetes Associations 69th Scientific Sessions. New Orleans, LA, USA, 5-9 June 2009.
    • (2009) American Diabetes Associations 69th Scientific Sessions
    • Boothe, J.G.1    Nykiforuk, C.L.2    Kuhlman, P.A.3
  • 25
    • 33846098407 scopus 로고    scopus 로고
    • Engineering and expression of the intracellular domain of insulinoma-associated tyrosine phosphatase (IA-2ic), a Type 1 diabetes autoantigen, in plants
    • Mett V, Shamloul AM, Hirai H, Zhou Z, Notkins A, Yusibov V. Engineering and expression of the intracellular domain of insulinoma-associated tyrosine phosphatase (IA-2ic), a Type 1 diabetes autoantigen, in plants. Transgenic Res. 16(1), 77-84 (2007).
    • (2007) Transgenic Res. , vol.16 , Issue.1 , pp. 77-84
    • Mett, V.1    Shamloul, A.M.2    Hirai, H.3    Zhou, Z.4    Notkins, A.5    Yusibov, V.6
  • 26
    • 0041465717 scopus 로고    scopus 로고
    • Crystal structure and functional analysis of Escherichia coli glutamate decarboxylase
    • Capitani G, De Biase D, Aurizi C, Gut H, Bossa F, Grutter MG. Crystal structure and functional analysis of Escherichia coli glutamate decarboxylase. EMBO J. 22(16), 4027-4037 (2003).
    • (2003) EMBO J , vol.22 , Issue.16 , pp. 4027-4037
    • Capitani, G.1    De Biase, D.2    Aurizi, C.3    Gut, H.4    Bossa, F.5    Grutter, M.G.6
  • 27
    • 0030791484 scopus 로고    scopus 로고
    • Transgenic plants expressing autoantigens fed to mice to induce oral immune tolerance
    • Ma SW, Zhao DL, Yin ZQ et al. Transgenic plants expressing autoantigens fed to mice to induce oral immune tolerance. Nat. Med. 3(7), 793-796 (1997).
    • (1997) Nat. Med. , vol.3 , Issue.7 , pp. 793-796
    • Schmidt, M.A.W.1    Zhao, D.L.2    Yin, Z.Q.3
  • 28
    • 0033452018 scopus 로고    scopus 로고
    • Transgenic plants expressing human glutamic acid decarboxylase (GAD65), a major autoantigen in insulin-dependent diabetes mellitus
    • Porceddu A, Falorni A, Ferradini N et al. Transgenic plants expressing human glutamic acid decarboxylase (GAD65), a major autoantigen in insulin-dependent diabetes mellitus. Mol. Breeding 5(6), 553-560 (1999).
    • (1999) Mol. Breeding , vol.5 , Issue.6 , pp. 553-560
    • Porceddu, A.1    Falorni, A.2    Ferradini, N.3
  • 29
    • 0038056326 scopus 로고    scopus 로고
    • Improved in planta expression of the human islet autoantigen glutamic acid decarboxylase (GAD65)
    • Avesani L, Falorni A, Tornielli GB et al. Improved in planta expression of the human islet autoantigen glutamic acid decarboxylase (GAD65). Transgenic Res. 12(2), 203-212 (2003).
    • (2003) Transgenic Res. , vol.12 , Issue.2 , pp. 203-212
    • Avesani, L.1    Falorni, A.2    Tornielli, G.B.3
  • 30
    • 77955258362 scopus 로고    scopus 로고
    • Recombinant human GAD65 accumulates to high levels in transgenic tobacco plants when expressed as an enzymatically inactive mutant
    • DOI: 10.1111/j.1467-7652.2010.00514.x ( Epub ahead of print
    • Avesani L, Vitale A, Pedrazzini E et al. Recombinant human GAD65 accumulates to high levels in transgenic tobacco plants when expressed as an enzymatically inactive mutant. Plant Biotechnol. J. DOI: 10.1111/j.1467-7652. 2010.00514.x (2010) (Epub ahead of print).
    • (2010) Plant Biotechnol. J.
    • Avesani, L.1    Vitale, A.2    Pedrazzini, E.3
  • 31
    • 0035910379 scopus 로고    scopus 로고
    • Site-directed mutagenesis of K396R of the 65 kDa glutamic acid decarboxylase active site obliterates enzyme activity but not antibody binding
    • Hampe CS, Hammerle LP, Falorni A, Robertson J, Lernmark A. Site-directed mutagenesis of K396R of the 65 kDa glutamic acid decarboxylase active site obliterates enzyme activity but not antibody binding. FEBS Lett. 488(3), 185-189 (2001).
    • (2001) FEBS Lett. , vol.488 , Issue.3 , pp. 185-189
    • Hampe, C.S.1    Hammerle, L.P.2    Falorni, A.3    Robertson, J.4    Lernmark, A.5
  • 32
    • 58249116675 scopus 로고    scopus 로고
    • A novel expression platform for the production of diabetes-associated autoantigen human glutamic acid decarboxylase (hGAD65)
    • Wang X, Brandsma M, Tremblay R et al. A novel expression platform for the production of diabetes-associated autoantigen human glutamic acid decarboxylase (hGAD65). BMC Biotechnol. 8, 87 (2008).
    • (2008) BMC Biotechnol. , vol.8 , pp. 87
    • Wang, X.1    Brandsma, M.2    Tremblay, R.3
  • 33
    • 0026745632 scopus 로고
    • Identification of an immunodominant B-cell epitope in bovine type II collagen and the production of antibodies to type II collagen by immunization with a synthetic peptide representing this epitope
    • Morgan K, Turner SL, Reynolds I, Hajeer AH, Brass A, Worthington J. Identification of an immunodominant B-cell epitope in bovine type II collagen and the production of antibodies to type II collagen by immunization with a synthetic peptide representing this epitope. Immunology 77(4), 609-616 (1992).
    • (1992) Immunology , vol.77 , Issue.4 , pp. 609-616
    • Morgan, K.1    Turner, S.L.2    Reynolds, I.3    Hajeer, A.H.4    Brass, A.5    Worthington, J.6
  • 34
    • 0029962104 scopus 로고    scopus 로고
    • Mucosal tolerance and suppression of collagen-induced arthritis (CIA) induced by nasal inhalation of synthetic peptide 184-198 of bovine type II collagen (CII) expressing a dominant T cell epitope
    • Staines NA, Harper N, Ward FJ, Malmstrom V, Holmdahl R, Bansal S. Mucosal tolerance and suppression of collagen-induced arthritis (CIA) induced by nasal inhalation of synthetic peptide 184-198 of bovine type II collagen (CII) expressing a dominant T cell epitope. Clin. Exp. Immunol. 103(3), 368-375 (1996).
    • (1996) Clin. Exp. Immunol. , vol.103 , Issue.3 , pp. 368-375
    • Staines, N.A.1    Harper, N.2    Ward, F.J.3    Malmstrom, V.4    Holmdahl, R.5    Bansal, S.6
  • 35
    • 0027255203 scopus 로고
    • T cell epitopes of type II collagen that regulate murine collagen- induced arthritis
    • Myers LK, Seyer JM, Stuart JM, Terato K, David CS, Kang AH. T cell epitopes of type II collagen that regulate murine collagen- induced arthritis. J. Immunol. 151(1), 500-505 (1993).
    • (1993) J. Immunol. , vol.151 , Issue.1 , pp. 500-505
    • Myers, L.K.1    Seyer, J.M.2    Stuart, J.M.3    Terato, K.4    David, C.S.5    Kang, A.H.6
  • 36
    • 0030584696 scopus 로고    scopus 로고
    • Characterization of the antigenic structure of human type II collagen
    • Krco CJ, Pawelski J, Harders J et al. Characterization of the antigenic structure of human type II collagen. J. Immunol. 156(8), 2761-2768 (1996).
    • (1996) J. Immunol. , vol.156 , Issue.8 , pp. 2761-2768
    • Krco, C.J.1    Pawelski, J.2    Harders, J.3
  • 37
    • 0029117917 scopus 로고
    • Oral administration of an immunodominant human collagen peptide modulates collagen-induced arthritis
    • Khare SD, Krco CJ, Griffiths MM, Luthra HS, David CS. Oral administration of an immunodominant human collagen peptide modulates collagen-induced arthritis. J. Immunol. 155(7), 3653-3659 (1995).
    • (1995) J. Immunol. , vol.155 , Issue.7 , pp. 3653-3659
    • Khare, S.D.1    Krco, C.J.2    Griffiths, M.M.3    Luthra, H.S.4    David, C.S.5
  • 38
    • 33845881672 scopus 로고    scopus 로고
    • Oral administration of type-II collagen peptide 250-270 suppresses specific cellular and humoral immune response in collagen- induced arthritis
    • Zhu P, Li XY, Wang HK et al. Oral administration of type-II collagen peptide 250-270 suppresses specific cellular and humoral immune response in collagen- induced arthritis. Clin. Immunol. 122(1), 75-84 (2007).
    • (2007) Clin. Immunol. , vol.122 , Issue.1 , pp. 75-84
    • Zhu, P.1    Li, X.Y.2    Wang, H.K.3
  • 39
    • 54949157282 scopus 로고    scopus 로고
    • Development and evaluation of transgenic rice seeds accumulating a type II-collagen tolerogenic peptide
    • Hashizume F, Hino S, Kakehashi M et al. Development and evaluation of transgenic rice seeds accumulating a type II-collagen tolerogenic peptide. Transgenic Res. 17(6), 1117-1129 (2008).
    • (2008) Transgenic Res. , vol.17 , Issue.6 , pp. 1117-1129
    • Hashizume, F.1    Hino, S.2    Kakehashi, M.3
  • 40
    • 0006245272 scopus 로고
    • The processing of a 57-kDa precursor peptide to subunits of rice glutelin
    • Sarker S, Ogawa M, Takahashi M, Asasda K. The processing of a 57-kDa precursor peptide to subunits of rice glutelin. Plant Cell Physiol. 27, 1579-1586 (1986).
    • (1986) Plant Cell Physiol. , vol.27 , pp. 1579-1586
    • Sarker, S.1    Ogawa, M.2    Takahashi, M.3    Asasda, K.4
  • 41
    • 0027057738 scopus 로고
    • Immunogenetics of collagen induced arthritis in mice: A model for human polyarthritis
    • Moder KG, Nabozny GH, Luthra HS, David CS. Immunogenetics of collagen induced arthritis in mice: a model for human polyarthritis. Reg. Immunol. 4(5), 305-313 (1992).
    • (1992) Reg. Immunol. , vol.4 , Issue.5 , pp. 305-313
    • Moder, K.G.1    Nabozny, G.H.2    Luthra, H.S.3    David, C.S.4
  • 42
    • 0031252553 scopus 로고    scopus 로고
    • Immunohistochemical study on type II collagen-induced arthritis in DBA/1J mice
    • Suzuki M, Uetsuka K, Suzuki M, Shinozuka J, Nakayama H, Doi K. Immunohistochemical study on type II collagen-induced arthritis in DBA/1J mice. Exp. Anim. 46(4), 259-267 (1997).
    • (1997) Exp. Anim. , vol.46 , Issue.4 , pp. 259-267
    • Suzuki, M.1    Uetsuka, K.2    Suzuki, M.3    Shinozuka, J.4    Nakayama, H.5    Doi, K.6
  • 43
    • 15444348180 scopus 로고    scopus 로고
    • Characterization of recombinant type II collagen: Arthritogenicity and tolerogenicity in DBA/1 mice
    • Myers LK, Brand DD, Ye XJ et al. Characterization of recombinant type II collagen: arthritogenicity and tolerogenicity in DBA/1 mice. Immunology 95(4), 631-639 (1998).
    • (1998) Immunology , vol.95 , Issue.4 , pp. 631-639
    • Myers, L.K.1    Brand, D.D.2    Ye, X.J.3
  • 45
    • 0032704261 scopus 로고    scopus 로고
    • Suppression of collagen-induced arthritis by oral or nasal administration of type II collagen
    • Garcia G, Komagata Y, Slavin AJ, Maron R, Weiner HL. Suppression of collagen-induced arthritis by oral or nasal administration of type II collagen. J. Autoimmun. 13(3), 315-324 (1999).
    • (1999) J. Autoimmun. , vol.13 , Issue.3 , pp. 315-324
    • Garcia, G.1    Komagata, Y.2    Slavin, A.J.3    Maron, R.4    Weiner, H.L.5
  • 46
    • 0017680149 scopus 로고
    • The epsilon- (g-glutamyl)lysine crosslink and the catalytic role of transglutaminases
    • Folk JE, Finlayson JS. The epsilon- (g-glutamyl)lysine crosslink and the catalytic role of transglutaminases. Adv. Protein Chem. 31, 1-133 (1977).
    • (1977) Adv. Protein Chem. , vol.31 , pp. 1-133
    • Folk, J.E.1    Finlayson, J.S.2
  • 47
    • 0030838044 scopus 로고    scopus 로고
    • Identification of tissue transglutaminase as the autoantigen of celiac disease
    • Dieterich W, Ehnis T, Bauer M et al. Identification of tissue transglutaminase as the autoantigen of celiac disease. Nat. Med. 3(7), 797-801 (1997).
    • (1997) Nat. Med. , vol.3 , Issue.7 , pp. 797-801
    • Dieterich, W.1    Ehnis, T.2    Bauer, M.3
  • 48
    • 0034066733 scopus 로고    scopus 로고
    • Human recombinant tissue transglutaminase ELISA: An innovative diagnostic assay for celiac disease
    • Sblattero D, Berti I, Trevisiol C et al. Human recombinant tissue transglutaminase ELISA: an innovative diagnostic assay for celiac disease. Am. J. Gastroenterol. 95(5), 1253-1257 (2000).
    • (2000) Am. J. Gastroenterol. , vol.95 , Issue.5 , pp. 1253-1257
    • Sblattero, D.1    Berti, I.2    Trevisiol, C.3
  • 49
    • 0036865727 scopus 로고    scopus 로고
    • Production of recombinant human tissue transglutaminase using the baculovirus expression system, and its application for serological diagnosis of coeliac disease
    • Osman AA, Richter T, Stern M et al. Production of recombinant human tissue transglutaminase using the baculovirus expression system, and its application for serological diagnosis of coeliac disease. Eur. J. Gastroenterol. Hepatol. 14(11), 1217-1223 (2002).
    • (2002) Eur. J. Gastroenterol. Hepatol. , vol.14 , Issue.11 , pp. 1217-1223
    • Osman, A.A.1    Richter, T.2    Stern, M.3
  • 50
    • 0036845018 scopus 로고    scopus 로고
    • Autoantibodies to human tissue transglutaminase: Superior predictors of coeliac disease
    • Blackwell PJ, Hill PG, Holmes GK. Autoantibodies to human tissue transglutaminase: superior predictors of coeliac disease. Scand. J. Gastroenterol. 37(11), 1282-1285 (2002).
    • (2002) Scand. J. Gastroenterol. , vol.37 , Issue.11 , pp. 1282-1285
    • Blackwell, P.J.1    Hill, P.G.2    Holmes, G.K.3
  • 51
    • 0036444187 scopus 로고    scopus 로고
    • Expression in Escherichia coli and purification of hexahistidine-tagged human tissue transglutaminase
    • Shi Q, Kim SY, Blass JP, Cooper AJ. Expression in Escherichia coli and purification of hexahistidine-tagged human tissue transglutaminase. Protein Expr. Purif. 24(3), 366-373 (2002).
    • (2002) Protein Expr. Purif. , vol.24 , Issue.3 , pp. 366-373
    • Shi, Q.1    Kim, S.Y.2    Blass, J.P.3    Cooper, A.J.4
  • 52
    • 13444256361 scopus 로고    scopus 로고
    • Recombinant human tissue transglutaminase produced into tobacco suspension cell cultures is active and recognizes autoantibodies in the serum of coeliac patients
    • Sorrentino A, Schillberg S, Fischer R, Rao R, Porta R, Mariniello L. Recombinant human tissue transglutaminase produced into tobacco suspension cell cultures is active and recognizes autoantibodies in the serum of coeliac patients. Int. J. Biochem. Cell Biol. 37(4), 842-851 (2005).
    • (2005) Int. J. Biochem. Cell Biol. , vol.37 , Issue.4 , pp. 842-851
    • Sorrentino, A.1    Schillberg, S.2    Fischer, R.3    Rao, R.4    Porta, R.5    Mariniello, L.6
  • 53
  • 54
    • 0029900868 scopus 로고    scopus 로고
    • Treatment of experimental autoimmune encephalomyelitis by feeding myelin basic protein conjugated to cholera toxin B subunit
    • Sun JB, Rask C, Olsson T, Holmgren J, Czerkinsky C. Treatment of experimental autoimmune encephalomyelitis by feeding myelin basic protein conjugated to cholera toxin B subunit. Proc. Natl Acad. Sci. USA 93(14), 7196-7201 (1996).
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , Issue.14 , pp. 7196-7201
    • Sun, J.B.1    Rask, C.2    Olsson, T.3    Holmgren, J.4    Czerkinsky, C.5
  • 55
    • 20044365044 scopus 로고    scopus 로고
    • Mucosal adjuvants and anti-infection and anti-immunopathology vaccines based on cholera toxin, cholera toxin B subunit and CpG DNA
    • Holmgren J, Adamsson J, Anjuere F et al. Mucosal adjuvants and anti-infection and anti-immunopathology vaccines based on cholera toxin, cholera toxin B subunit and CpG DNA. Immunol. Lett. 97(2), 181-188 (2005).
    • (2005) Immunol. Lett. , vol.97 , Issue.2 , pp. 181-188
    • Holmgren, J.1    Adamsson, J.2    Anjuere, F.3
  • 56
    • 72349096793 scopus 로고    scopus 로고
    • Mucosally induced immunological tolerance, regulatory T cells and the adjuvant effect by cholera toxin B subunit
    • Sun JB, Czerkinsky C, Holmgren J. Mucosally induced immunological tolerance, regulatory T cells and the adjuvant effect by cholera toxin B subunit. Scand. J. Immunol. 71(1), 1-11 (2010).
    • (2010) Scand. J. Immunol. , vol.71 , Issue.1 , pp. 1-11
    • Sun, J.B.1    Czerkinsky, C.2    Holmgren, J.3
  • 57
    • 0029787628 scopus 로고    scopus 로고
    • Role of the glycocalyx in regulating access of microparticles to apical plasma membranes of intestinal epithelial cells: Implications for microbial attachment and oral vaccine targeting
    • Frey A, Giannasca KT, Weltzin R et al. Role of the glycocalyx in regulating access of microparticles to apical plasma membranes of intestinal epithelial cells: implications for microbial attachment and oral vaccine targeting. J. Exp. Med. 184(3), 1045-1059 (1996).
    • (1996) J. Exp. Med. , vol.184 , Issue.3 , pp. 1045-1059
    • Frey, A.1    Giannasca, K.T.2    Weltzin, R.3
  • 58
    • 77649232515 scopus 로고    scopus 로고
    • Expression of a ricin toxin B subunit: Insulin fusion protein in edible plant tissues
    • Carter JE 3rd, Odumosu O, Langridge WH. Expression of a ricin toxin B subunit: insulin fusion protein in edible plant tissues. Mol. Biotechnol. 44(2), 90-100 (2010).
    • (2010) Mol. Biotechnol. , vol.44 , Issue.2 , pp. 90-100
    • Carter Iii, J.E.1    Odumosu, O.2    Langridge, W.H.3
  • 59
    • 0031762753 scopus 로고    scopus 로고
    • A plant-based cholera toxin B subunit-insulin fusion protein protects against the development of autoimmune diabetes
    • Arakawa T, Yu J, Chong DK, Hough J, Engen PC, Langridge WH. A plant-based cholera toxin B subunit-insulin fusion protein protects against the development of autoimmune diabetes. Nat. Biotechnol. 16(10), 934-938 (1998).
    • (1998) Nat. Biotechnol. , vol.16 , Issue.10 , pp. 934-938
    • Arakawa, T.1    Yu, J.2    Chong, D.K.3    Hough, J.4    Engen, P.C.5    Langridge, W.H.6
  • 60
    • 34249820528 scopus 로고    scopus 로고
    • Expression of cholera toxin B-proinsulin fusion protein in lettuce and tobacco chloroplasts - Oral administration protects against development of insulitis in non-obese diabetic mice
    • Ruhlman T, Ahangari R, Devine A, Samsam M, Daniell H. Expression of cholera toxin B-proinsulin fusion protein in lettuce and tobacco chloroplasts - oral administration protects against development of insulitis in non-obese diabetic mice. Plant Biotechnol. J. 5(4), 495-510 (2007).
    • (2007) Plant Biotechnol. J. , vol.5 , Issue.4 , pp. 495-510
    • Ruhlman, T.1    Ahangari, R.2    Devine, A.3    Samsam, M.4    Daniell, H.5
  • 61
    • 33645996068 scopus 로고    scopus 로고
    • Expression of cholera toxin B subunit and the B chain of human insulin as a fusion protein in transgenic tobacco plants
    • Li D, O'Leary J, Huang Y, Huner NP, Jevnikar AM, Schmidt M.A. Expression of cholera toxin B subunit and the B chain of human insulin as a fusion protein in transgenic tobacco plants. Plant Cell Rep. 25(5), 417-424 (2006).
    • (2006) Plant Cell Rep. , vol.25 , Issue.5 , pp. 417-424
    • Li, D.1    O'Leary, J.2    Huang, Y.3    Huner, N.P.4    Jevnikar, A.M.5    Schmidt, M.A.6
  • 62
    • 0035451681 scopus 로고    scopus 로고
    • Plasmid vaccination with insulin B chain prevents autoimmune diabetes in nonobese diabetic mice
    • Bot A, Smith D, Bot S et al. Plasmid vaccination with insulin B chain prevents autoimmune diabetes in nonobese diabetic mice. J. Immunol. 167(5), 2950-2955 (2001).
    • (2001) J. Immunol. , vol.167 , Issue.5 , pp. 2950-2955
    • Bot, A.1    Smith, D.2    Bot, S.3
  • 63
    • 1842732158 scopus 로고    scopus 로고
    • Induction of oral tolerance to prevent diabetes with transgenic plants requires glutamic acid decarboxylase (GAD) and IL-4
    • Ma S, Huang Y, Yin Z, Menassa R, Brandle JE, Jevnikar AM. Induction of oral tolerance to prevent diabetes with transgenic plants requires glutamic acid decarboxylase (GAD) and IL-4. Proc. Natl Acad. Sci. USA 101(15), 5680-5685 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , Issue.15 , pp. 5680-5685
    • Schmidt, M.A.1    Huang, Y.2    Yin, Z.3    Menassa, R.4    Brandle, J.E.5    Jevnikar, A.M.6
  • 64
    • 0024502120 scopus 로고
    • Murine interleukin-4 displays potent anti-tumor activity in vivo
    • Tepper RI, Pattengale PK, Leder P. Murine interleukin-4 displays potent anti-tumor activity in vivo. Cell 57(3), 503-512 (1989).
    • (1989) Cell , vol.57 , Issue.3 , pp. 503-512
    • Tepper, R.I.1    Pattengale, P.K.2    Leder, P.3
  • 65
    • 0025936417 scopus 로고
    • Inhibitory effect of interleukin-4 on the in vitro growth of Ph1-positive acute lymphoblastic leukemia cells
    • Okabe M, Kuni-eda Y, Sugiwura T et al. Inhibitory effect of interleukin-4 on the in vitro growth of Ph1-positive acute lymphoblastic leukemia cells. Blood 78(6), 1574-1580 (1991).
    • (1991) Blood , vol.78 , Issue.6 , pp. 1574-1580
    • Okabe, M.1    Kuni-Eda, Y.2    Sugiwura, T.3
  • 66
    • 0037234390 scopus 로고    scopus 로고
    • Interleukin-4 therapy of psoriasis induces Th2 responses and improves human autoimmune disease
    • Ghoreschi K, Thomas P, Breit S et al. Interleukin-4 therapy of psoriasis induces Th2 responses and improves human autoimmune disease. Nat. Med. 9(1), 40-46 (2003).
    • (2003) Nat. Med. , vol.9 , Issue.1 , pp. 40-46
    • Ghoreschi, K.1    Thomas, P.2    Breit, S.3
  • 67
    • 0027272228 scopus 로고
    • Interleukin 4 reverses T cell proliferative unresponsiveness and prevents the onset of diabetes in nonobese diabetic mice
    • Rapoport MJ, Jaramillo A, Zipris D et al. Interleukin 4 reverses T cell proliferative unresponsiveness and prevents the onset of diabetes in nonobese diabetic mice. J. Exp. Med. 178(1), 87-99 (1993).
    • (1993) J. Exp. Med. , vol.178 , Issue.1 , pp. 87-99
    • Rapoport, M.J.1    Jaramillo, A.2    Zipris, D.3
  • 68
    • 0023943656 scopus 로고
    • Expression, renaturation and purification of recombinant human interleukin 4 from Escherichia coli
    • van Kimmenade A, Bond MW, Schumacher JH, Laquoi C, Kastelein RA. Expression, renaturation and purification of recombinant human interleukin 4 from Escherichia coli. Eur. J. Biochem. 173(1), 109-114 (1988).
    • (1988) Eur. J. Biochem. , vol.173 , Issue.1 , pp. 109-114
    • Van Kimmenade, A.1    Bond, M.W.2    Schumacher, J.H.3    Laquoi, C.4    Kastelein, R.A.5
  • 69
    • 0024330275 scopus 로고
    • Purification and characterization of recombinant human interleukin 4. Biological activities, receptor binding and the generation of monoclonal antibodies
    • Solari R, Quint D, Obray H et al. Purification and characterization of recombinant human interleukin 4. Biological activities, receptor binding and the generation of monoclonal antibodies. Biochem. J. 262(3), 897-908 (1989).
    • (1989) Biochem. J. , vol.262 , Issue.3 , pp. 897-908
    • Solari, R.1    Quint, D.2    Obray, H.3
  • 70
    • 0032103849 scopus 로고    scopus 로고
    • Secretion of biologically active human interleukin-2 and interleukin-4 from genetically modified tobacco cells in suspension culture
    • Magnuson NS, Linzmaier PM, Reeves R, An G, HayGlass K, Lee JM. Secretion of biologically active human interleukin-2 and interleukin-4 from genetically modified tobacco cells in suspension culture. Protein Expr. Purif. 13(1), 45-52 (1998).
    • (1998) Protein Expr. Purif. , vol.13 , Issue.1 , pp. 45-52
    • Magnuson, N.S.1    Linzmaier, P.M.2    Reeves, R.3    An, G.4    Hayglass, K.5    Lee, J.M.6
  • 71
    • 27644487558 scopus 로고    scopus 로고
    • Production of biologically active human interleukin-4 in transgenic tobacco and potato
    • Ma S, Huang Y, Davis A et al. Production of biologically active human interleukin-4 in transgenic tobacco and potato. Plant Biotechnol. J. 3(3), 309-318 (2005).
    • (2005) Plant Biotechnol. J. , vol.3 , Issue.3 , pp. 309-318
    • Schmidt, M.A.1    Huang, Y.2    Davis, A.3
  • 72
    • 0028346888 scopus 로고
    • Production of interleukin 10 by islet cells accelerates immune-mediated destruction of p cells in nonobese diabetic mice
    • Wogensen L, Lee MS, Sarvetnick N. Production of interleukin 10 by islet cells accelerates immune-mediated destruction of p cells in nonobese diabetic mice. J. Exp. Med. 179(4), 1379-1384 (1994).
    • (1994) J. Exp. Med. , vol.179 , Issue.4 , pp. 1379-1384
    • Wogensen, L.1    Lee, M.S.2    Sarvetnick, N.3
  • 73
    • 3042845733 scopus 로고    scopus 로고
    • Psoriasis and the new biologic agents: Interrupting a T-AP dance
    • Walsh SR, Shear NH. Psoriasis and the new biologic agents: interrupting a T-AP dance. CMAJ 170(13), 1933-1941 (2004).
    • (2004) CMAJ , vol.170 , Issue.13 , pp. 1933-1941
    • Walsh, S.R.1    Shear, N.H.2
  • 74
    • 0035707558 scopus 로고    scopus 로고
    • A self-contained system for the field production of plant recombinant interleukin-10
    • Menassa R, Nguyen V, Jevnikar A, Brandle J. A self-contained system for the field production of plant recombinant interleukin-10. Mol. Breeding 8, 177-185 (2001).
    • (2001) Mol. Breeding , vol.8 , pp. 177-185
    • Menassa, R.1    Nguyen, V.2    Jevnikar, A.3    Brandle, J.4
  • 76
    • 33845793938 scopus 로고    scopus 로고
    • Therapeutic effectiveness of orally administered transgenic low-alkaloid tobacco expressing human interleukin-10 in a mouse model of colitis
    • Menassa R, Du C, Yin ZQ et al. Therapeutic effectiveness of orally administered transgenic low-alkaloid tobacco expressing human interleukin-10 in a mouse model of colitis. Plant Biotechnol. J. 5(1), 50-59 (2007).
    • (2007) Plant Biotechnol. J. , vol.5 , Issue.1 , pp. 50-59
    • Menassa, R.1    Du, C.2    Yin, Z.Q.3
  • 77
    • 0038723693 scopus 로고    scopus 로고
    • Validation of the interleukin-10 knockout mouse model of colitis: Antitumour necrosis factor-antibodies suppress the progression of colitis
    • Scheinin T, Butler DM, Salway F, Scallon B, Feldmann M. Validation of the interleukin-10 knockout mouse model of colitis: antitumour necrosis factor-antibodies suppress the progression of colitis. Clin. Exp. Immunol. 133(1), 38-43 (2003).
    • (2003) Clin. Exp. Immunol. , vol.133 , Issue.1 , pp. 38-43
    • Scheinin, T.1    Butler, D.M.2    Salway, F.3    Scallon, B.4    Feldmann, M.5
  • 78
    • 0034714188 scopus 로고    scopus 로고
    • Treatment of murine colitis by Lactococcus lactis secreting interleukin-10
    • Steidler L, Hans W, Schotte L et al. Treatment of murine colitis by Lactococcus lactis secreting interleukin-10. Science 289(5483), 1352-1355 (2000).
    • (2000) Science , vol.289 , Issue.5483 , pp. 1352-1355
    • Steidler, L.1    Hans, W.2    Schotte, L.3
  • 79
    • 33947315594 scopus 로고    scopus 로고
    • Elastin-like polypeptide fusions enhance the accumulation of recombinant proteins in tobacco leaves
    • Patel J, Zhu H, Menassa R, Gyenis L, Richman A, Brandle J. Elastin-like polypeptide fusions enhance the accumulation of recombinant proteins in tobacco leaves. Transgenic Res. 16(2), 239-249 (2007).
    • (2007) Transgenic Res. , vol.16 , Issue.2 , pp. 239-249
    • Patel, J.1    Zhu, H.2    Menassa, R.3    Gyenis, L.4    Richman, A.5    Brandle, J.6
  • 80
    • 0033778539 scopus 로고    scopus 로고
    • Can interleukin-10 be used as a true immunoregulatory cytokine?
    • Wakkach A, Cottrez F, Groux H. Can interleukin-10 be used as a true immunoregulatory cytokine? Eur. Cytokine Netw. 11(2), 153-160 (2000).
    • (2000) Eur. Cytokine Netw. , vol.11 , Issue.2 , pp. 153-160
    • Wakkach, A.1    Cottrez, F.2    Groux, H.3
  • 82
    • 64549116714 scopus 로고    scopus 로고
    • Viral and murine interleukin-10 are correctly processed and retain their biological activity when produced in tobacco
    • Bortesi L, Rossato M, Schuster F et al. Viral and murine interleukin-10 are correctly processed and retain their biological activity when produced in tobacco. BMC Biotechnol. 9, 22 (2009).
    • (2009) BMC Biotechnol. , vol.9 , pp. 22
    • Bortesi, L.1    Rossato, M.2    Schuster, F.3
  • 83
    • 0032768886 scopus 로고    scopus 로고
    • Interleukin-13 prevents autoimmune diabetes in NOD mice
    • Zaccone P, Phillips J, Conget I et al. Interleukin-13 prevents autoimmune diabetes in NOD mice. Diabetes 48(8), 1522-1528 (1999).
    • (1999) Diabetes , vol.48 , Issue.8 , pp. 1522-1528
    • Zaccone, P.1    Phillips, J.2    Conget, I.3
  • 84
    • 4143113057 scopus 로고    scopus 로고
    • Specifically targeted killing of interleukin-13 (IL-13) receptor-expressing breast cancer by IL-13 fusion cytotoxin in animal model of human disease
    • Kawakami K, Kawakami M, Puri RK. Specifically targeted killing of interleukin-13 (IL-13) receptor-expressing breast cancer by IL-13 fusion cytotoxin in animal model of human disease. Mol. Cancer Ther. 3(2), 137-147 (2004).
    • (2004) Mol. Cancer Ther. , vol.3 , Issue.2 , pp. 137-147
    • Kawakami, K.1    Kawakami, M.2    Puri, R.K.3
  • 85
    • 33747204065 scopus 로고    scopus 로고
    • The IL-4 and IL-13 pseudomonas exotoxins: New hope for brain tumor therapy
    • Shimamura T, Husain SR, Puri RK. The IL-4 and IL-13 pseudomonas exotoxins: new hope for brain tumor therapy. Neurosurg. Focus 20(4), E11 (2006).
    • (2006) Neurosurg. Focus , vol.20 , Issue.4
    • Shimamura, T.1    Husain, S.R.2    Puri, R.K.3
  • 87
    • 70349759364 scopus 로고    scopus 로고
    • Plants as bioreactors: Recent developments and emerging opportunities
    • Sharma A, Sharma M. Plants as bioreactors: recent developments and emerging opportunities. Biotechnol. Adv. 27, 811-832 (2009).
    • (2009) Biotechnol. Adv. , vol.27 , pp. 811-832
    • Sharma, A.1    Sharma, M.2
  • 88
    • 14844293838 scopus 로고    scopus 로고
    • Magnifection - A new platform for expressing recombinant vaccines in plants
    • Gleba Y, Klimyuk V, Marillonnet S. Magnifection - a new platform for expressing recombinant vaccines in plants. Vaccine 23(17-18), 2042-2048 (2005).
    • (2005) Vaccine , vol.23 , Issue.17-18 , pp. 2042-2048
    • Gleba, Y.1    Klimyuk, V.2    Marillonnet, S.3
  • 89
    • 68849097943 scopus 로고    scopus 로고
    • PEAQ: Versatile expression vectors for easy and quick transient expression of heterologous proteins in plants
    • Sainsbury F, Thuenemann EC, Lomonossoff GP. pEAQ: versatile expression vectors for easy and quick transient expression of heterologous proteins in plants. Plant Biotechnol. J. 7(7), 682-693 (2009).
    • (2009) Plant Biotechnol. J. , vol.7 , Issue.7 , pp. 682-693
    • Sainsbury, F.1    Thuenemann, E.C.2    Lomonossoff, G.P.3
  • 90
    • 0032478127 scopus 로고    scopus 로고
    • Immunization against rabies with plant-derived antigen
    • Modelska A, Dietzschold B, Sleysh N et al. Immunization against rabies with plant-derived antigen. Proc. Natl Acad. Sci. USA 95(5), 2481-2485 (1998).
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , Issue.5 , pp. 2481-2485
    • Modelska, A.1    Dietzschold, B.2    Sleysh, N.3
  • 91
    • 77953987341 scopus 로고    scopus 로고
    • Plant-made vaccines for humans and animals
    • Rybicki EP. Plant-made vaccines for humans and animals. Plant Biotechnol. J. 8(5), 620-637 (2010).
    • (2010) Plant Biotechnol. J. , vol.8 , Issue.5 , pp. 620-637
    • Rybicki, E.P.1
  • 92
    • 33645112928 scopus 로고    scopus 로고
    • Forcing single-chain variable fragment production in tobacco seeds by fusion to elastin-like polypeptides
    • Scheller J, Leps M, Conrad U. Forcing single-chain variable fragment production in tobacco seeds by fusion to elastin-like polypeptides. Plant Biotechnol. J. 4(2), 243-249 (2006).
    • (2006) Plant Biotechnol. J. , vol.4 , Issue.2 , pp. 243-249
    • Scheller, J.1    Leps, M.2    Conrad, U.3
  • 93
    • 75949109975 scopus 로고    scopus 로고
    • Hydrophobin fusions for high-level transient protein expression and purification in Nicotiana benthamiana
    • Joensuu JJ, Conley AJ, Lienemann M, Brandle JE, Linder MB, Menassa R. Hydrophobin fusions for high-level transient protein expression and purification in Nicotiana benthamiana. Plant Physiol. 152(2), 622-633 (2010).
    • (2010) Plant Physiol. , vol.152 , Issue.2 , pp. 622-633
    • Joensuu, J.J.1    Conley, A.J.2    Lienemann, M.3    Brandle, J.E.4    Linder, M.B.5    Menassa, R.6
  • 94
    • 46849111804 scopus 로고    scopus 로고
    • The human immunodeficiency virus antigen Nef forms protein bodies in leaves of transgenic tobacco when fused to zeolin
    • de Virgilio M, De Marchis F, Bellucci M et al. The human immunodeficiency virus antigen Nef forms protein bodies in leaves of transgenic tobacco when fused to zeolin. J. Exp. Bot. 59(10), 2815-2829 (2008).
    • (2008) J. Exp. Bot. , vol.59 , Issue.10 , pp. 2815-2829
    • De Virgilio, M.1    De Marchis, F.2    Bellucci, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.