메뉴 건너뛰기




Volumn 3, Issue 6, 2011, Pages 505-512

An innovative approach for the characterization of the isoforms of a monoclonal antibody product

Author keywords

Charge heterogeneity; Glycosylation; IgG1; Isoforms; Monoclonal antibody; Silaic acid

Indexed keywords

IMMUNOGLOBULIN G1; LYSINE; SIALIDASE; CARBOXYPEPTIDASE; IMMUNOGLOBULIN G; ISOPROTEIN; MONOCLONAL ANTIBODY; N ACETYLNEURAMINIC ACID;

EID: 81255211544     PISSN: 19420862     EISSN: 19420870     Source Type: Journal    
DOI: 10.4161/mabs.3.6.18090     Document Type: Article
Times cited : (34)

References (40)
  • 1
    • 0037264969 scopus 로고    scopus 로고
    • Therapeutic antibodies for human diseases at the dawn of the twenty-first century
    • PMID:12509759; DOI:10.1038/nrd984
    • Brekke OH, Sandlie I. Therapeutic antibodies for human diseases at the dawn of the twenty-first century. Nat Rev Drug Discov 2003; 2:52-62; PMID:12509759; DOI:10.1038/nrd984.
    • (2003) Nat Rev Drug Discov , vol.2 , pp. 52-62
    • Brekke, O.H.1    Sandlie, I.2
  • 2
    • 57049154860 scopus 로고    scopus 로고
    • Antibodies for the treatment of bacterial infections: Current experience and future prospects
    • PMID:19000762; DOI:10.1016/j.copbio.2008.10.002
    • Bebbington C, Yarranton G. Antibodies for the treatment of bacterial infections: current experience and future prospects. Curr Opin Biotechnol 2008; 19:613-9; PMID:19000762; DOI:10.1016/j.copbio.2008.10.002.
    • (2008) Curr Opin Biotechnol , vol.19 , pp. 613-619
    • Bebbington, C.1    Yarranton, G.2
  • 3
    • 51549091266 scopus 로고    scopus 로고
    • Recombinant antibodies as therapeutic agents: Pathways for modeling new biodrugs
    • PMID:18778112
    • Aires da Silva F, Corte-Real S, Goncalves J. Recombinant antibodies as therapeutic agents: pathways for modeling new biodrugs. BioDrugs 2008; 22:301-14; PMID:18778112.
    • (2008) BioDrugs , vol.22 , pp. 301-314
    • Aires Da Silva, F.1    Corte-Real, S.2    Goncalves, J.3
  • 4
    • 0025290953 scopus 로고
    • A comparative study of N-linked oligosaccharide structures of human IgG subclass proteins
    • PMID:2363690
    • Jefferis R, Lund J, Mizutani H, Nakagawa H, Kawazoe Y, Arata Y, et al. A comparative study of N-linked oligosaccharide structures of human IgG subclass proteins. Biochem J 1990; 268:529-37; PMID:2363690.
    • (1990) Biochem J , vol.268 , pp. 529-537
    • Jefferis, R.1    Lund, J.2    Mizutani, H.3    Nakagawa, H.4    Kawazoe, Y.5    Arata, Y.6
  • 5
    • 0031015976 scopus 로고    scopus 로고
    • Glycosylation of antibody molecules. Structural and functional significance
    • PMID:9018875; DOI:10.1159/000319352
    • Jefferis R, Lund J. Glycosylation of antibody molecules. Structural and functional significance. Chem Immunol 1997; 65:111-28; PMID:9018875; DOI:10.1159/000319352.
    • (1997) Chem Immunol , vol.65 , pp. 111-128
    • Jefferis, R.1    Lund, J.2
  • 6
    • 0024806396 scopus 로고
    • Stability of protein pharmaceuticals
    • PMID:2687836; DOI:10.1023/A:1015929109894
    • Manning MC, Patel K, Borchardt R. Stability of protein pharmaceuticals. Pharm Res 1989; 6:903-18; PMID:2687836; DOI:10.1023/A:1015929109894.
    • (1989) Pharm Res , vol.6 , pp. 903-918
    • Manning, M.C.1    Patel, K.2    Borchardt, R.3
  • 7
    • 0031241608 scopus 로고    scopus 로고
    • Degradative covalent reactions important to protein stability
    • PMID:9406181
    • Volkin DB, Mach H, Middaugh CR. Degradative covalent reactions important to protein stability. Mol Biotechnol 1997; 8:105-22; PMID:9406181.
    • (1997) Mol Biotechnol , vol.8 , pp. 105-122
    • Volkin, D.B.1    Mach, H.2    Middaugh, C.R.3
  • 8
    • 0004125932 scopus 로고    scopus 로고
    • United States Food and Drug Administration. US department of Health and Human services, FDA Center for Biologics Evaluation and Research, February 28
    • United States Food and Drug Administration. Points to consider in the manufacture and testing of monoclonal antibody products for human use. US department of Health and Human services, FDA Center for Biologics Evaluation and Research, February 28, 1997.
    • (1997) Points to Consider in the Manufacture and Testing of Monoclonal Antibody Products for Human Use
  • 9
    • 78651387929 scopus 로고    scopus 로고
    • Antibody-based therapeutics to watch in 2011
    • PMID:21051951; DOI:10.4161/mabs.3.1.13895
    • Reichert JM. Antibody-based therapeutics to watch in 2011. MAbs 2011; 3:76-99; PMID:21051951; DOI:10.4161/mabs.3.1.13895.
    • (2011) MAbs , vol.3 , pp. 76-99
    • Reichert, J.M.1
  • 10
    • 78649669018 scopus 로고    scopus 로고
    • Metrics for antibody development
    • PMID:20930555; DOI:10.4161/mabs.2.6.13603
    • Reichert JM. Metrics for antibody development. MAbs 2010; 2:695-700; PMID:20930555; DOI:10.4161/mabs.2.6.13603.
    • (2010) MAbs , vol.2 , pp. 695-700
    • Reichert, J.M.1
  • 11
    • 77349115530 scopus 로고    scopus 로고
    • Current and emerging treatment strategies for cutaneous T-cell lymphoma
    • PMID:20166766; DOI:10.2165/11532190
    • Lansigan F, Foss FM. Current and emerging treatment strategies for cutaneous T-cell lymphoma. Drugs 2010; 70:273-86; PMID:20166766; DOI:10.2165/11532190.
    • (2010) Drugs , vol.70 , pp. 273-286
    • Lansigan, F.1    Foss, F.M.2
  • 12
    • 80052536175 scopus 로고    scopus 로고
    • New drugs in melanoma: It's whole new world
    • PMID:21802280; DOI:10.1016/j.ejca.2011.06.052
    • Eggermont AM, Robert C. New drugs in melanoma: It's whole new world. Eur J Cancer 2011; 47:2150-7; PMID:21802280; DOI:10.1016/j.ejca.2011.06.052.
    • (2011) Eur J Cancer , vol.47 , pp. 2150-2157
    • Eggermont, A.M.1    Robert, C.2
  • 13
    • 60849102492 scopus 로고    scopus 로고
    • Heterogeneity of monoclonal antibodies revealed by charge sensitive methods
    • PMID:19075686; DOI:10.2174/138920108786786402
    • Vlasak J, Ionescu R. Heterogeneity of monoclonal antibodies revealed by charge sensitive methods. Curr Pharm Biotechnol 2008; 9:468-81; PMID:19075686; DOI:10.2174/138920108786786402.
    • (2008) Curr Pharm Biotechnol , vol.9 , pp. 468-481
    • Vlasak, J.1    Ionescu, R.2
  • 14
    • 77951789012 scopus 로고    scopus 로고
    • Characterization of antibody charge heterogeneity resolved by preparative immobilized pH gradients
    • PMID:20364842; DOI:10.1021/ac902408r
    • Meert CD, Brady LJ, Guo A, Balland A. Characterization of antibody charge heterogeneity resolved by preparative immobilized pH gradients. Anal Chem 2010; 82:3510-8; PMID:20364842; DOI:10.1021/ac902408r.
    • (2010) Anal Chem , vol.82 , pp. 3510-3518
    • Meert, C.D.1    Brady, L.J.2    Guo, A.3    Balland, A.4
  • 15
    • 0029411975 scopus 로고
    • N-glycans of recombinant human interferon-gamma change during batch culture of Chinese hamster ovary cells
    • PMID:18623533; DOI:10.1002/bit.260480612
    • Hooker AD, Goldman MH, Markham MH, James DC, Ison AP, Bull AT, et al. N-glycans of recombinant human interferon-gamma change during batch culture of Chinese hamster ovary cells. Biotechnol Bioeng 1995; 48:639-48; PMID:18623533; DOI:10.1002/bit.260480612.
    • (1995) Biotechnol Bioeng , vol.48 , pp. 639-648
    • Hooker, A.D.1    Goldman, M.H.2    Markham, M.H.3    James, D.C.4    Ison, A.P.5    Bull, A.T.6
  • 16
    • 0343417035 scopus 로고    scopus 로고
    • Influence of Primatone RL supplementation on sialylation of recombinant human interferon-gamma produced by Chinese hamster ovary cell culture using serum-free media
    • PMID:18642238; DOI:10.1002/(SICI)1097-0290(19971120)56:4353::AID-BIT13.0. CO;2-N
    • Gu X, Xie L, Harmon BJ, Wang DI. Influence of Primatone RL supplementation on sialylation of recombinant human interferon-gamma produced by Chinese hamster ovary cell culture using serum-free media. Biotechnol Bioeng 1997; 56:353-60; PMID:18642238; DOI:10.1002/(SICI)1097-0290(19971120)56:4353:: AID-BIT13.0.CO;2-N.
    • (1997) Biotechnol Bioeng , vol.56 , pp. 353-360
    • Gu, X.1    Xie, L.2    Harmon, B.J.3    Wang, D.I.4
  • 17
    • 0026641016 scopus 로고
    • Different culture methods lead to differences in glycosylation of a murine IgG monoclonal antibody
    • PMID:1497622
    • Patel TP, Parkeh RB, Moellering BJ, Prior CP. Different culture methods lead to differences in glycosylation of a murine IgG monoclonal antibody. Biochem J 1992; 285:839-45; PMID:1497622.
    • (1992) Biochem J , vol.285 , pp. 839-845
    • Patel, T.P.1    Parkeh, R.B.2    Moellering, B.J.3    Prior, C.P.4
  • 18
    • 0032493787 scopus 로고    scopus 로고
    • Real time isoform analysis by two dimensional chromatography of a monoclonal antibody during bioreactor fermentations
    • PMID:9741099; DOI:10.1016/S0021-9673(98)00032-6
    • Fang Y, Dumont L, Larsen B. Real time isoform analysis by two dimensional chromatography of a monoclonal antibody during bioreactor fermentations. J Chromatogr A 1998; 816:39-47; PMID:9741099; DOI:10.1016/S0021-9673(98)00032-6.
    • (1998) J Chromatogr A , vol.816 , pp. 39-47
    • Fang, Y.1    Dumont, L.2    Larsen, B.3
  • 19
    • 0026463719 scopus 로고
    • Identification of sites of degradation in a therapeutic monoclonal antibody by peptide mapping
    • PMID:1475223; DOI:10.1023/A:1015894409623
    • Kroon DJ, Baldwin-Ferro A, Lalan L. Identification of sites of degradation in a therapeutic monoclonal antibody by peptide mapping. Pharm Res 1992; 9:1386-93; PMID:1475223; DOI:10.1023/A:1015894409623.
    • (1992) Pharm Res , vol.9 , pp. 1386-1393
    • Kroon, D.J.1    Baldwin-Ferro, A.2    Lalan, L.3
  • 20
    • 0004330520 scopus 로고    scopus 로고
    • Cleavage at Asn-Gly bonds with hydroxylamine
    • Hirs CHW, Serge N, Timasheff N, Editors. Enzyme Structure (Part E), Academic Press, New York
    • Bornstein P, Balian G. Cleavage at Asn-Gly bonds with hydroxylamine. In: Hirs CHW, Serge N, Timasheff N, Editors. Methods in Enzymol. Vol XLVIII, Enzyme Structure (Part E), Academic Press, New York 1997.
    • (1997) Methods in Enzymol , vol.48
    • Bornstein, P.1    Balian, G.2
  • 21
    • 0024516367 scopus 로고
    • Succimide formation from aspartyl and asparaginal peptides as a model for spontaneous degradation of proteins
    • PMID:2703484
    • Stephenson RC, Clarke S. Succimide formation from aspartyl and asparaginal peptides as a model for spontaneous degradation of proteins. J Biol Chem 1989; 264:6164-70; PMID:2703484.
    • (1989) J Biol Chem , vol.264 , pp. 6164-6170
    • Stephenson, R.C.1    Clarke, S.2
  • 22
    • 0033755938 scopus 로고    scopus 로고
    • Determination of the origin of charge heterogeneity in a murine monoclonal antibody
    • PMID:11087044; DOI:10.1023/A:1026461830617
    • Perkins M, Theiler R, Lunte S, Jeschke M. Determination of the origin of charge heterogeneity in a murine monoclonal antibody. Pharm Res 2000; 17:1110-7; PMID:11087044; DOI:10.1023/A:1026461830617.
    • (2000) Pharm Res , vol.17 , pp. 1110-1117
    • Perkins, M.1    Theiler, R.2    Lunte, S.3    Jeschke, M.4
  • 23
    • 0023464863 scopus 로고
    • Propensity for spontaneous succinimide formation from aspartyl and asparaginyl residues in cellular proteins
    • PMID:3440704; DOI:10.1111/j.1399-3011.1987.tb03390.x
    • Clarke S. Propensity for spontaneous succinimide formation from aspartyl and asparaginyl residues in cellular proteins. Int J Pept Protein Res 1987; 30:808-21; PMID:3440704; DOI:10.1111/j.1399-3011.1987.tb03390.x.
    • (1987) Int J Pept Protein Res , vol.30 , pp. 808-821
    • Clarke, S.1
  • 24
    • 0024281434 scopus 로고
    • Tertiary structure is a principal determinant to protein deamidation
    • PMID:3353715; DOI:10.1126/science.3353715
    • Kossiakoff AA. Tertiary structure is a principal determinant to protein deamidation. Science 1988; 240:191-4; PMID:3353715; DOI:10.1126/science.3353715.
    • (1988) Science , vol.240 , pp. 191-194
    • Kossiakoff, A.A.1
  • 25
    • 0025788030 scopus 로고
    • Effects of amino acid sequence, buffers and ionic strength on the rate and mechanism of deamidation of asparagines residues in small peptides
    • PMID:1939272
    • Tyler-Cross R, Schirch V. Effects of amino acid sequence, buffers and ionic strength on the rate and mechanism of deamidation of asparagines residues in small peptides. J Biol Chem 1991; 266:22549-56; PMID:1939272.
    • (1991) J Biol Chem , vol.266 , pp. 22549-22556
    • Tyler-Cross, R.1    Schirch, V.2
  • 26
    • 0037212197 scopus 로고    scopus 로고
    • Analysis of isoaspartate in a recombinant monoclonal antibody and its charge isoforms
    • PMID:12467919; DOI:10.1016/S0731-7085(02)00479-X
    • Zhang W, Czuprryn M. Analysis of isoaspartate in a recombinant monoclonal antibody and its charge isoforms. J Pharm Biomed Anal 2003; 30:1479-90; PMID:12467919; DOI:10.1016/S0731-7085(02)00479-X.
    • (2003) J Pharm Biomed Anal , vol.30 , pp. 1479-1490
    • Zhang, W.1    Czuprryn, M.2
  • 27
    • 0029017877 scopus 로고
    • Processing of C-terminal lysine and arginine residues of proteins isolated from mammalian cell culture
    • PMID:7620566; DOI:10.1016/0021-9673(94)01255-D
    • Harris RJ. Processing of C-terminal lysine and arginine residues of proteins isolated from mammalian cell culture. J Chromatogr A 1995; 705:129-34; PMID:7620566; DOI:10.1016/0021-9673(94)01255-D.
    • (1995) J Chromatogr A , vol.705 , pp. 129-134
    • Harris, R.J.1
  • 28
    • 20944441421 scopus 로고    scopus 로고
    • Characterization of a novel modification to monoclonal antibodies: Thioether cross-link of heavy and light chains
    • PMID:15859580; DOI:10.1021/ac0500582
    • Tous GI, Wei Z, Feng J, Bilbulin S, Bowen S, Smith J, et al. Characterization of a novel modification to monoclonal antibodies: thioether cross-link of heavy and light chains. Anal Chem 2005; 77:2675-82; PMID:15859580; DOI:10.1021/ac0500582.
    • (2005) Anal Chem , vol.77 , pp. 2675-2682
    • Tous, G.I.1    Wei, Z.2    Feng, J.3    Bilbulin, S.4    Bowen, S.5    Smith, J.6
  • 29
    • 34250182367 scopus 로고    scopus 로고
    • β-elimination and peptide bond hydrolysis: Two distinct mechanisms of human IgG1 hinge fragmentation upon storage
    • PMID:17500521; DOI:10.1021/ja0705994
    • Cohen SL, Price C, Vlasak J. β-elimination and peptide bond hydrolysis: two distinct mechanisms of human IgG1 hinge fragmentation upon storage. J Am Chem Soc 2007; 129:6976-7; PMID:17500521; DOI:10.1021/ja0705994.
    • (2007) J Am Chem Soc , vol.129 , pp. 6976-6977
    • Cohen, S.L.1    Price, C.2    Vlasak, J.3
  • 30
    • 68049084746 scopus 로고    scopus 로고
    • Evidence for trisulfide bonds in a recombinant vaient of human IgG2 monoclonal antibody
    • PMID:19591437; DOI:10.1021/ac9006254
    • Pristatsky P, Cohen SL, Krantz D, Acevedo J, Ionescu R, Vlasak J. Evidence for trisulfide bonds in a recombinant vaient of human IgG2 monoclonal antibody. Anal Chem 2009; 81:6148-55; PMID:19591437; DOI:10.1021/ac9006254.
    • (2009) Anal Chem , vol.81 , pp. 6148-6155
    • Pristatsky, P.1    Cohen, S.L.2    Krantz, D.3    Acevedo, J.4    Ionescu, R.5    Vlasak, J.6
  • 31
    • 0028902241 scopus 로고
    • Micro-hertogeneity of erythropoietin carbohydrate structure
    • PMID:7741215; DOI:10.1021/ac00104a022
    • Rush RS, Derby PL, Smith DM, Merry C, Rogers G, Rhode MF. Micro-hertogeneity of erythropoietin carbohydrate structure. Anal Chem 1995; 67:1442-52; PMID:7741215; DOI:10.1021/ac00104a022.
    • (1995) Anal Chem , vol.67 , pp. 1442-1452
    • Rush, R.S.1    Derby, P.L.2    Smith, D.M.3    Merry, C.4    Rogers, G.5    Rhode, M.F.6
  • 32
    • 0036840574 scopus 로고    scopus 로고
    • Comparison of the isoelectric focusing patterns of darbepoetin alfa, recombinant human erythropoietin, and endogenous erythropoietin from human urine
    • Catlin DH, Breidbach A, Elliot S, Glaspy J. Comparison of isoelectric patterns of Darbepoeetin Alfa, recombinant erythropoietin and endogeneous erythropoietin from human urine. Clin Chem 2002; 11:2057-9. (Pubitemid 35222769)
    • (2002) Clinical Chemistry , vol.48 , Issue.11 , pp. 2057-2059
    • Catlin, D.H.1    Breidbach, A.2    Elliott, S.3    Glaspy, J.4
  • 33
    • 33947688082 scopus 로고    scopus 로고
    • Structural characterization of N-linked oligosaccharides on monoclonal antibody cetuximab by the combination of orthogonal matrix-assisted lase desorption/ ionization hybrid quadrupole-quadrupole time-of-fight tandem mass spectrometry and sequential enzymatic digestion
    • PMID:17362871; DOI:10.1016/j.ab.2007.01.023
    • Qian J, Liu T, Yang L, Daus A, Crowley R, Zhou Q. Structural characterization of N-linked oligosaccharides on monoclonal antibody cetuximab by the combination of orthogonal matrix-assisted lase desorption/ ionization hybrid quadrupole-quadrupole time-of-fight tandem mass spectrometry and sequential enzymatic digestion. Anal Biochem 2007; 364:8-18; PMID:17362871; DOI:10.1016/j.ab.2007.01.023.
    • (2007) Anal Biochem , vol.364 , pp. 8-18
    • Qian, J.1    Liu, T.2    Yang, L.3    Daus, A.4    Crowley, R.5    Zhou, Q.6
  • 34
    • 77950080700 scopus 로고    scopus 로고
    • Improving effector functions of antibodies for cancer treatment: Enhancing ADCC and CDC
    • PMID:19920917
    • Natsume A, Niwa R, Satoh M. Improving effector functions of antibodies for cancer treatment: Enhancing ADCC and CDC. Drug Des Devel Ther 2009; 3:7-16; PMID:19920917.
    • (2009) Drug des Devel Ther , vol.3 , pp. 7-16
    • Natsume, A.1    Niwa, R.2    Satoh, M.3
  • 35
    • 55249121695 scopus 로고    scopus 로고
    • Antibody fucosylation differently impacts cytotoxicity mediated by NK and PMN effector cells
    • PMID:18566325; DOI:10.1182/blood-2008-03-144600
    • Peipp M, Lammerts JJ, van Bueren L, Schneider-Merck TJ, Bleeker WWK, Dechant M, et al. Antibody fucosylation differently impacts cytotoxicity mediated by NK and PMN effector cells. Blood 2008; 112:2390-9; PMID:18566325; DOI:10.1182/blood-2008-03-144600.
    • (2008) Blood , vol.112 , pp. 2390-2399
    • Peipp, M.1    Lammerts, J.J.2    Van Bueren, L.3    Schneider-Merck, T.J.4    Bleeker, W.W.K.5    Dechant, M.6
  • 36
    • 33746888249 scopus 로고    scopus 로고
    • Anti inflammatory activity of immunoglobulin G resulting from Fc sialyation
    • PMID:16888140; DOI:10.1126/science.1129594
    • Kaneko Y, Nimmerijahn F, Ravetch JV. Anti inflammatory activity of immunoglobulin G resulting from Fc sialyation. Science 2006; 313:670-3; PMID:16888140; DOI:10.1126/science.1129594.
    • (2006) Science , vol.313 , pp. 670-673
    • Kaneko, Y.1    Nimmerijahn, F.2    Ravetch, J.V.3
  • 37
    • 33751253486 scopus 로고    scopus 로고
    • Higher levels of sialyated Fc glycans in immunoglobulin G molecules can adversely impact functionality
    • PMID:17045339; DOI:10.1016/j.molimm.2006.09.005
    • Scallon BJ, Tam SH, McCarthy SG, Cai AN, Raju TS. Higher levels of sialyated Fc glycans in immunoglobulin G molecules can adversely impact functionality. Mol Immunol 2007; 44:1524-34; PMID:17045339; DOI:10.1016/j. molimm.2006.09.005.
    • (2007) Mol Immunol , vol.44 , pp. 1524-1534
    • Scallon, B.J.1    Tam, S.H.2    McCarthy, S.G.3    Cai, A.N.4    Raju, T.S.5
  • 38
    • 77958531332 scopus 로고    scopus 로고
    • Engineering host cell lines to reduce terminal sialyation of secreted antibodies
    • PMID:20716959; DOI:10.4161/mabs.2.5.13078
    • Naso MF, Tam SH, Scallon BJ, Raju TS. Engineering host cell lines to reduce terminal sialyation of secreted antibodies. MAbs 2010; 2:519-27; PMID:20716959; DOI:10.4161/mabs.2.5.13078.
    • (2010) MAbs , vol.2 , pp. 519-527
    • Naso, M.F.1    Tam, S.H.2    Scallon, B.J.3    Raju, T.S.4
  • 39
    • 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
    • PMID:12427744; DOI:10.1074/jbc.M210665200
    • Shinkawa T, Nakamura K, Yamane N, Shoji-Hosaka E, Kanda Y, Sakurada M, et al. 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 2003; 278:3466-73; PMID:12427744; DOI:10.1074/jbc.M210665200.
    • (2003) J Biol Chem , vol.278 , pp. 3466-3473
    • Shinkawa, T.1    Nakamura, K.2    Yamane, N.3    Shoji-Hosaka, E.4    Kanda, Y.5    Sakurada, M.6
  • 40
    • 30744440090 scopus 로고    scopus 로고
    • Development and regulation of monoclonal antibody products: Challenges and opportunities
    • PMID:16408162; DOI:10.1007/s10555-005-6196-y
    • Weinberg W, Fraizer-Jesson MR, Wu WJ, Weir A, Hartsough M, Keegan P, et al. Development and regulation of monoclonal antibody products: Challenges and opportunities. Cancer Metastasis Rev 2005; 24:569-84; PMID:16408162; DOI:10.1007/s10555-005-6196-y.
    • (2005) Cancer Metastasis Rev , vol.24 , pp. 569-584
    • Weinberg, W.1    Fraizer-Jesson, M.R.2    Wu, W.J.3    Weir, A.4    Hartsough, M.5    Keegan, P.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.