메뉴 건너뛰기




Volumn 85, Issue 3, 2010, Pages 535-542

Glycosylation pattern of humanized IgG-like bispecific antibody produced by recombinant CHO cells

Author keywords

Bispecific diabody; Bispecific IgG like antibody; Chinese hamster ovary cells; Glycosylation; Immunoglobulin G

Indexed keywords

ANTI-EGFR; BISPECIFIC DIABODY; CHINESE HAMSTER OVARY CELLS; CHO CELL; DIABODY; HUMAN SERUM; IMMUNOGLOBULIN G; MATRIX-ASSISTED LASER DESORPTION/IONIZATION-TIME-OF-FLIGHT MASS SPECTROMETRY; N-LINKED; NEUTRAL OLIGOSACCHARIDES; OLIGOSACCHARIDE STRUCTURE; SIALYLATION;

EID: 74149087566     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00253-009-2152-z     Document Type: Article
Times cited : (23)

References (32)
  • 1
    • 0028061380 scopus 로고
    • The effect of cell-culture conditions on the oligosaccharide structures of secreted glycoproteins
    • DOI 10.1016/0958-1669(94)90072-8
    • DC Anderson CF Goochee 1994 The effect of cell-culture conditions on the oligosaccharide structures of secreted glycoproteins Curr Opin Biotechnol 5 546 549 10.1016/0958-1669(94)90072-8 (Pubitemid 24321425)
    • (1994) Current Opinion in Biotechnology , vol.5 , Issue.5 , pp. 546-549
    • Andersen, D.C.1    Goochee, C.F.2
  • 2
    • 34948911585 scopus 로고    scopus 로고
    • Highly effective recombinant format of a humanized IgG-like bispecific antibody for cancer immunotherapy with retargeting of lymphocytes to tumor cells
    • DOI 10.1074/jbc.M704719200
    • R Asano Y Watanabe H Kawaguchi H Fukazawa T Nakanishi M Umetsu Y Katayose M Unno T Kudo I Kumagai 2007 Highly effective recombinant format of a humanized IgG-like bispecific antibody for cancer immunotherapy with retargeting of lymphocytes to tumor cells J Biol Chem 282 27659 27665 10.1074/jbc.M704719200 1:CAS:528:DC%2BD2sXhtVeju7rN (Pubitemid 47529493)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.38 , pp. 27659-27665
    • Asano, R.1    Watanabe, Y.2    Kawaguchi, H.3    Fukazawa, H.4    Nakanishi, T.5    Umetsu, M.6    Hayashi, H.7    Katayose, Y.8    Unno, M.9    Kudo, T.10    Kumagai, I.11
  • 3
    • 59849088809 scopus 로고    scopus 로고
    • Diabody-based recombinant formats of humanized IgG-like bispecific antibody with effective retargeting of lymphocytes to tumor cells
    • 10.1097/CJI.0b013e3181849071 1:CAS:528:DC%2BD1cXhtFCrtLzK
    • R Asano K Kawaguchi Y Watanabe T Nakanishi M Umetsu H Hayashi Y Katayose M Unno T Kudo I Kumagai 2008 Diabody-based recombinant formats of humanized IgG-like bispecific antibody with effective retargeting of lymphocytes to tumor cells J Immunother 31 752 761 10.1097/CJI.0b013e3181849071 1:CAS:528: DC%2BD1cXhtFCrtLzK
    • (2008) J Immunother , vol.31 , pp. 752-761
    • Asano, R.1    Kawaguchi, K.2    Watanabe, Y.3    Nakanishi, T.4    Umetsu, M.5    Hayashi, H.6    Katayose, Y.7    Unno, M.8    Kudo, T.9    Kumagai, I.10
  • 4
    • 0029558207 scopus 로고
    • The effect of the removal of sialic acid, galactose and total carbohydrate on the functional activity of Campath-1H
    • DOI 10.1016/0161-5890(95)00118-2
    • PN Boyd AC Lines AK Patel 1995 The effect of the removal of sialic acid, galactose and total carbohydrate on the functional activity of Campath-1H Mol Immun 32 1311 1318 10.1016/0161-5890(95)00118-2 1:CAS:528:DyaK28Xhs1aiu78%3D (Pubitemid 26064897)
    • (1995) Molecular Immunology , vol.32 , Issue.17-18 , pp. 1311-1318
    • Boyd, P.N.1    Lines, A.C.2    Patel, A.K.3
  • 5
    • 23844433927 scopus 로고    scopus 로고
    • Animal cell cultures: Recent achievements and perspectives in the production of biopharmaceuticals
    • DOI 10.1007/s00253-005-1980-8
    • M Butler 2005 Animal cell cultures: recent achievements and perspectives in the production of biopharmaceuticals Appl Microbiol Biotechnol 68 283 291 10.1007/s00253-005-1980-8 1:CAS:528:DC%2BD2MXnsl2gtrk%3D (Pubitemid 41159998)
    • (2005) Applied Microbiology and Biotechnology , vol.68 , Issue.3 , pp. 283-291
    • Butler, M.1
  • 6
    • 33747362656 scopus 로고    scopus 로고
    • Optimisation of the cellular metabolism of glycosylation for recombinant proteins produced by mammalian cell systems
    • DOI 10.1007/s10616-005-4537-x
    • M Butler 2006 Optimisation of the cellular metabolism of glycosylation for recombinant proteins produced by mammalian cell systems Cytotechnology 50 57 76 10.1007/s10616-005-4537-x 1:CAS:528:DC%2BD28XotFChs7o%3D (Pubitemid 44243933)
    • (2006) Cytotechnology , vol.50 , Issue.1-3 , pp. 57-76
    • Butler, M.1
  • 7
    • 0035251453 scopus 로고    scopus 로고
    • Bispecific human IgG by design
    • DOI 10.1016/S0022-1759(00)00339-2, PII S0022175900003392
    • P Carter 2001 Bispecific human IgG by design J Immunol Methods 248 7 15 10.1016/S0022-1759(00)00339-2 1:CAS:528:DC%2BD3MXht12gu7w%3D (Pubitemid 32167021)
    • (2001) Journal of Immunological Methods , vol.248 , Issue.1-2 , pp. 7-15
    • Carter, P.1
  • 8
    • 34748837881 scopus 로고    scopus 로고
    • Analysis of N-glycans from recombinant immunoglobulin G by on-line reversed-phase high-performance liquid chromatography/mass spectrometry
    • DOI 10.1016/j.ab.2007.08.012, PII S0003269707005052
    • X Chen GC Flynn 2007 Analysis of N-glycans from recombinant immunoglobulin G by on-line reversed-phase high-performance liquid chromatography/mass spectrometry Anal Biochem 370 147 161 10.1016/j.ab.2007.08. 012 1:CAS:528:DC%2BD2sXhtFSls7jK (Pubitemid 47484317)
    • (2007) Analytical Biochemistry , vol.370 , Issue.2 , pp. 147-161
    • Chen, X.1    Flynn, G.C.2
  • 9
    • 0038105203 scopus 로고    scopus 로고
    • Reduction of CMP-N-acetylneuraminic acid hydroxylase activity in engineered Chinese hamster ovary cells using an antisense-RNA strategy
    • 1:CAS:528:DC%2BD3sXls1Ons74%3D
    • S Chenu A Grégoire Y Malykh A Visvikis L Monaco L Shaw R Schauer A Marc JL Goergen 2003 Reduction of CMP-N-acetylneuraminic acid hydroxylase activity in engineered Chinese hamster ovary cells using an antisense-RNA strategy Biochim Biophys Acta 1622 133 144 1:CAS:528:DC%2BD3sXls1Ons74%3D
    • (2003) Biochim Biophys Acta , vol.1622 , pp. 133-144
    • Chenu, S.1    Grégoire, A.2    Malykh, Y.3    Visvikis, A.4    Monaco, L.5    Shaw, L.6    Schauer, R.7    Marc, A.8    Goergen, J.L.9
  • 10
    • 0343134556 scopus 로고    scopus 로고
    • Unusual N-glycosylation of a recombinant human erythropoietin expressed in a human lymphoblastoid cell line does not alter its biological properties
    • 10.1093/glycob/10.5.511 1:CAS:528:DC%2BD3cXislSmu7c%3D
    • D Cointe R Beliard S Jorieux Y Leroy A Glacet A Verbert D Bourel F Chirat 2000 Unusual N-glycosylation of a recombinant human erythropoietin expressed in a human lymphoblastoid cell line does not alter its biological properties Glycobiology 10 511 519 10.1093/glycob/10.5.511 1:CAS:528:DC%2BD3cXislSmu7c%3D
    • (2000) Glycobiology , vol.10 , pp. 511-519
    • Cointe, D.1    Beliard, R.2    Jorieux, S.3    Leroy, Y.4    Glacet, A.5    Verbert, A.6    Bourel, D.7    Chirat, F.8
  • 11
    • 0029154557 scopus 로고
    • Glycobiology: More functions for oligosaccharides
    • 10.1126/science.7652569 1:CAS:528:DyaK2MXnvVeqt7k%3D
    • RA Dwek 1995 Glycobiology: more functions for oligosaccharides Science 269 1234 1235 10.1126/science.7652569 1:CAS:528:DyaK2MXnvVeqt7k%3D
    • (1995) Science , vol.269 , pp. 1234-1235
    • Dwek, R.A.1
  • 12
    • 34248137611 scopus 로고    scopus 로고
    • Production of mouse monoclonal antibody with galactose-extended sugar chain by suspension cultured tobacco BY2 cells expressing human β(1,4)-galactosyltransferase
    • DOI 10.1016/j.bbrc.2007.04.054, PII S0006291X07007772
    • K Fujiyama A Furukawa A Katsura R Misaki T Omasa T Seki 2007 Production of mouse monoclonal antibody with galactose-extended sugar chain by suspension cultured tobacco BY2 cells expressing human β(1,4)-galactosyltransferase Biochem Biophys Res Commun 358 85 91 10.1016/j.bbrc.2007.04.054 1:CAS:528:DC%2BD2sXlt1ertLc%3D (Pubitemid 46719084)
    • (2007) Biochemical and Biophysical Research Communications , vol.358 , Issue.1 , pp. 85-91
    • Fujiyama, K.1    Furukawa, A.2    Katsura, A.3    Misaki, R.4    Omasa, T.5    Seki, T.6
  • 13
    • 34250676983 scopus 로고    scopus 로고
    • Fetal calf serum-free culture of Chinese hamster ovary cells employing fish serum
    • DOI 10.1007/s00253-007-0897-9
    • M Fujiwara R Tsukada Y Tsujinaga M Takagi 2007 Fetal calf serum-free culture of Chinese hamster ovary cells employing fish serum Appl Microbiol Biotechnol 75 983 987 10.1007/s00253-007-0897-9 1:CAS:528:DC%2BD2sXmsVKqsbc%3D (Pubitemid 46944525)
    • (2007) Applied Microbiology and Biotechnology , vol.75 , Issue.5 , pp. 983-987
    • Fujiwara, M.1    Tsukada, R.2    Tsujinaga, Y.3    Takagi, M.4
  • 14
    • 0023175723 scopus 로고
    • Fluorometric high-performance liquid chromatography of N-acetyl- and N-glycolylneuraminic acids and its application to their microdetermination in human and animal sera, glycoproteins, and glycolipids
    • DOI 10.1016/0003-2697(87)90377-0
    • S Hara Y Takemori M Yamaguchi M Nakamura Y Ohkura 1987 Fluorometric high-performance liquid chromatography of N-acetyl- and N-glycolylneuraminic acids and its application to their microdetermination in human and animal sera, glycoproteins, and glycolipids Anal Biochem 164 138 145 10.1016/0003-2697(87) 90377-0 1:CAS:528:DyaL2sXltlSntr8%3D (Pubitemid 17099609)
    • (1987) Analytical Biochemistry , vol.164 , Issue.1 , pp. 138-145
    • Hara, S.1    Takemori, Y.2    Yamaguchi, M.3
  • 15
    • 0035937505 scopus 로고    scopus 로고
    • Intracellular functions of N-linked glycans
    • 1:CAS:528:DC%2BD3MXit1KnsLw%3D
    • A Helenius M Aebi 2001 Intracellular functions of N-linked glycans Carbohydr Glycobiol 291 2364 2369 1:CAS:528:DC%2BD3MXit1KnsLw%3D
    • (2001) Carbohydr Glycobiol , vol.291 , pp. 2364-2369
    • Helenius, A.1    Aebi, M.2
  • 16
    • 28844463354 scopus 로고    scopus 로고
    • Control of recombinant monoclonal antibody effector functions by Fc N-glycan remodeling in vitro
    • DOI 10.1021/bp050228w
    • J Hodoniczky YZ Zheng DC James 2005 Control of recombinant antibody effector functions by Fc N-glycan remodeling in vitro Biotechnol Prog 21 1644 1652 10.1021/bp050228w 1:CAS:528:DC%2BD2MXhtVOis7zN (Pubitemid 41778987)
    • (2005) Biotechnology Progress , vol.21 , Issue.6 , pp. 1644-1652
    • Hodoniczky, J.1    Yuan, Z.Z.2    James, D.C.3
  • 17
    • 27144432842 scopus 로고    scopus 로고
    • Engineered antibody fragments and the rise of single domains
    • DOI 10.1038/nbt1142, PII N1142
    • P Holliger PJ Hudson 2005 Engineered antibody fragments and the rise of single domains Nat Biotechnol 23 1126 1136 10.1038/nbt1142 1:CAS:528: DC%2BD2MXpvVyrtrc%3D (Pubitemid 41486394)
    • (2005) Nature Biotechnology , vol.23 , Issue.9 , pp. 1126-1136
    • Holliger, P.1    Hudson, P.J.2
  • 18
    • 13544276336 scopus 로고    scopus 로고
    • Glycosylation of recombinant antibody therapeutics
    • DOI 10.1021/bp040016j
    • R Jefferis 2005 Glycosylation of recombinant antibody therapeutics Biotechnol Prog 21 11 16 10.1021/bp040016j 1:CAS:528:DC%2BD2cXhtFSlurrP (Pubitemid 40218466)
    • (2005) Biotechnology Progress , vol.21 , Issue.1 , pp. 11-16
    • Jefferis, R.1
  • 19
    • 61649087668 scopus 로고    scopus 로고
    • Glycosylation as a strategy to improve antibody-based therapeutics
    • 10.1038/nrd2804 1:CAS:528:DC%2BD1MXisVShtb0%3D
    • R Jefferis 2009 Glycosylation as a strategy to improve antibody-based therapeutics Nat Rev Drug Discov 8 226 234 10.1038/nrd2804 1:CAS:528: DC%2BD1MXisVShtb0%3D
    • (2009) Nat Rev Drug Discov , vol.8 , pp. 226-234
    • Jefferis, R.1
  • 20
    • 33746888249 scopus 로고    scopus 로고
    • Anti-inflammatory activity of immunoglobulin G resulting from Fc sialylation
    • DOI 10.1126/science.1129594
    • Y Kaneko F Nimmerjahn JV Ravetch 2006 Anti-inflammatory activity of immunoglobulin G resulting from Fc sialylation Science 313 670 673 10.1126/science.1129594 1:CAS:528:DC%2BD28Xnsl2hsbY%3D (Pubitemid 44201145)
    • (2006) Science , vol.313 , Issue.5787 , pp. 670-673
    • Kaneko, Y.1    Nimmerjahn, F.2    Ravetch, J.V.3
  • 21
    • 40749147518 scopus 로고    scopus 로고
    • The N-linked sugar chains of human immunoglobulin G: Their unique pattern, and their functional roles
    • 1:CAS:528:DC%2BD1cXjsVSisbs%3D
    • A Kobata 2008 The N-linked sugar chains of human immunoglobulin G: their unique pattern, and their functional roles Biochim Biophys Acta 1780 472 478 1:CAS:528:DC%2BD1cXjsVSisbs%3D
    • (2008) Biochim Biophys Acta , vol.1780 , pp. 472-478
    • Kobata, A.1
  • 22
    • 0029986313 scopus 로고    scopus 로고
    • Agalactosyl IgG in aggregates from the rheumatoid joint
    • 10.1093/rheumatology/35.4.335 1:STN:280:DyaK283hs12iug%3D%3D
    • KA Leader GC Lastra JR Kirwan CJ Elson 1996 Agalactosyl IgG in aggregates from the rheumatoid joint Br J Rheumatol 35 335 341 10.1093/rheumatology/35.4. 335 1:STN:280:DyaK283hs12iug%3D%3D
    • (1996) Br J Rheumatol , vol.35 , pp. 335-341
    • Leader, K.A.1    Lastra, G.C.2    Kirwan, J.R.3    Elson, C.J.4
  • 23
    • 0027319101 scopus 로고
    • Control of IgG/Fc glycosylation: A comparison of oligosaccharides from chimeric human/mouse and mouse subclass immunoglobulin Gs
    • 10.1016/0161-5890(93)90145-2 1:CAS:528:DyaK3sXkslSjt7g%3D
    • J Lund N Takahashi H Nakagawa M Goodall T Bentley SA Hindley R Tyler R Jefferis 1993 Control of IgG/Fc glycosylation: a comparison of oligosaccharides from chimeric human/mouse and mouse subclass immunoglobulin Gs Mol Immunol 30 741 748 10.1016/0161-5890(93)90145-2 1:CAS:528:DyaK3sXkslSjt7g%3D
    • (1993) Mol Immunol , vol.30 , pp. 741-748
    • Lund, J.1    Takahashi, N.2    Nakagawa, H.3    Goodall, M.4    Bentley, T.5    Hindley, S.A.6    Tyler, R.7    Jefferis, R.8
  • 24
    • 51549113358 scopus 로고    scopus 로고
    • Decrease in antithrombin III fucosylation by expressing GDP-fucose transporter siRNA in Chinese hamster ovary cells
    • 10.1263/jbb.106.168 1:CAS:528:DC%2BD1cXhtlWnsrzN
    • T Omasa R Tanaka T Doi M Ando Y Kitamoto K Honda M Kishimoto H Ohtake 2008 Decrease in antithrombin III fucosylation by expressing GDP-fucose transporter siRNA in Chinese hamster ovary cells J Biosci Bioeng 106 168 173 10.1263/jbb.106.168 1:CAS:528:DC%2BD1cXhtlWnsrzN
    • (2008) J Biosci Bioeng , vol.106 , pp. 168-173
    • Omasa, T.1    Tanaka, R.2    Doi, T.3    Ando, M.4    Kitamoto, Y.5    Honda, K.6    Kishimoto, M.7    Ohtake, H.8
  • 25
    • 0022414766 scopus 로고
    • Association of rheumatoid arthritis and primary osteoarthritis with changes in the glycosylation pattern of total serum IgG
    • DOI 10.1038/316452a0
    • RB Parekh RA Dwek BJ Sutton DL Fernandes A Leung D Stanworth TW Rademacher T Mizuochi T Taniguchi K Matsuta F Takeuchi Y Nagano T Miyamoto A Kobata 1985 Association of rheumatoid arthritis and primary osteoarthritis with changes in the glycosylation pattern of total serum IgG Nature 316 452 457 10.1038/316452a0 1:CAS:528:DyaL2MXltVehurY%3D (Pubitemid 16238456)
    • (1985) Nature , vol.316 , Issue.6027 , pp. 452-457
    • Parekh, R.B.1    Dwek, R.A.2    Sutton, B.J.3
  • 26
    • 48549090941 scopus 로고    scopus 로고
    • Terminal sugars of Fc glycans influence antibody effector functions of IgGs
    • 10.1016/j.coi.2008.06.007 1:CAS:528:DC%2BD1cXpslSltL0%3D
    • TS Raju 2008 Terminal sugars of Fc glycans influence antibody effector functions of IgGs Curr Opin Immun 20 471 478 10.1016/j.coi.2008.06.007 1:CAS:528:DC%2BD1cXpslSltL0%3D
    • (2008) Curr Opin Immun , vol.20 , pp. 471-478
    • Raju, T.S.1
  • 27
    • 0037178791 scopus 로고    scopus 로고
    • Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human FcγRIII and antibody-dependent cellular toxicity
    • DOI 10.1074/jbc.M202069200
    • RL Shields J Lai R Keck LY O'Connell K Hong YG Meng SH Weikert LG Presta 2002 Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human Fcgamma RIII and antibody-dependent cellular toxicity J Biol Chem 277 26733 26740 10.1074/jbc.M202069200 1:CAS:528:DC%2BD38XlvV2isrk%3D (Pubitemid 34951677)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.30 , pp. 26733-26740
    • Shields, R.L.1    Lai, J.2    Keck, R.3    O'Connell, L.Y.4    Hong, K.5    Gloria Meng, Y.6    Weikert, S.H.A.7    Presta, L.G.8
  • 28
    • 0037474276 scopus 로고    scopus 로고
    • The absence of fucose but not the presence of galactose or bisecting N-acetylglucosamine of human IgG1 complex-type oligosaccharides shows the critical role of enhancing antibody-dependent cellular cytotoxicity
    • DOI 10.1074/jbc.M210665200
    • T Shinkawa K Nakamura N Yamane E Shoji-Hosaka Y Kanda M Sakurada K Uchida H Anazawa M Satoh M Yamasaki N Hanai K Shitara 2003 The absence of fucose but not the presence of galactose or bisecting N-acetylglucosamine of human IgG1 complex-type oligosaccharides shows the critical role of enhancing antibody-dependent cellular cytotoxicity J Biol Chem 278 3466 3473 10.1074/jbc.M210665200 1:CAS:528:DC%2BD3sXmt1Kiuw%3D%3D (Pubitemid 36801263)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.5 , pp. 3466-3473
    • Shinkawa, T.1    Nakamura, K.2    Yamane, N.3    Shoji-Hosaka, E.4    Kanda, Y.5    Sakurada, M.6    Uchida, K.7    Anazawa, H.8    Satoh, M.9    Yamasaki, M.10    Hanai, N.11    Shitara, K.12
  • 29
    • 0037560884 scopus 로고    scopus 로고
    • Sericin, a protein derived from silkworms, accelerates the proliferation of several mammalian cell lines including a hybridoma
    • 10.1023/A:1023993400608 1:CAS:528:DC%2BD3sXktFSmtr0%3D
    • S Terada T Nishimura M Sasaki H Yamada M Miki 2002 Sericin, a protein derived from silkworms, accelerates the proliferation of several mammalian cell lines including a hybridoma Cytotechnology 40 3 12 10.1023/A:1023993400608 1:CAS:528:DC%2BD3sXktFSmtr0%3D
    • (2002) Cytotechnology , vol.40 , pp. 3-12
    • Terada, S.1    Nishimura, T.2    Sasaki, M.3    Yamada, H.4    Miki, M.5
  • 30
    • 0023948708 scopus 로고
    • Analyses of N-linked oligosaccharides using a two-dimensional mapping technique
    • 10.1016/0003-2697(88)90126-1 1:CAS:528:DyaL1cXlsVGmsL4%3D
    • N Tomiya J Awaya M Kurono S Endo Y Arata N Takahashi 1988 Analyses of N-linked oligosaccharides using a two-dimensional mapping technique Anal Biochem 171 73 90 10.1016/0003-2697(88)90126-1 1:CAS:528:DyaL1cXlsVGmsL4%3D
    • (1988) Anal Biochem , vol.171 , pp. 73-90
    • Tomiya, N.1    Awaya, J.2    Kurono, M.3    Endo, S.4    Arata, Y.5    Takahashi, N.6
  • 31
    • 0028267570 scopus 로고
    • Structure determination of the intact major sialylated oligosaccharide chains of recombinant human erythropoietin expressed in Chinese hamster ovary cells
    • 10.1093/glycob/4.2.227 1:CAS:528:DyaK2cXkt1Oju7w%3D
    • E Watson A Bhide HV Halbeek 1994 Structure determination of the intact major sialylated oligosaccharide chains of recombinant human erythropoietin expressed in Chinese hamster ovary cells Glycobiology 4 227 237 10.1093/glycob/4.2.227 1:CAS:528:DyaK2cXkt1Oju7w%3D
    • (1994) Glycobiology , vol.4 , pp. 227-237
    • Watson, E.1    Bhide, A.2    Halbeek, H.V.3
  • 32
    • 8344271026 scopus 로고    scopus 로고
    • Production of recombinant protein therapeutics in cultivated mammalian cells
    • DOI 10.1038/nbt1026
    • FM Wurm 2004 Production of recombinant protein therapeutics in cultivated mammalian cells Nat Biotechnol 22 1393 1398 10.1038/nbt1026 1:CAS:528:DC%2BD2cXptlSls7k%3D (Pubitemid 39482858)
    • (2004) Nature Biotechnology , vol.22 , Issue.11 , pp. 1393-1398
    • Wurm, F.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.