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Volumn 5, Issue 5, 2013, Pages 646-654

Improving biophysical properties of a bispecific antibody scaffold to aid developability: Quality by molecular design

Author keywords

Antibody engineering; Antibody stability; Biophysical characterization of antibody; Bispecific antibody; Fc engineering; Heterodimeric antibody; LC MS of antibody; Quality by design

Indexed keywords

BISPECIFIC ANTIBODY; HOMODIMER; MOLECULAR SCAFFOLD; TRASTUZUMAB;

EID: 84883876685     PISSN: 19420862     EISSN: 19420870     Source Type: Journal    
DOI: 10.4161/mabs.25632     Document Type: Article
Times cited : (96)

References (52)
  • 1
    • 84858257263 scopus 로고    scopus 로고
    • Dual targeting strategies with bispecific antibodies
    • PMID:22453100
    • Kontermann R. Dual targeting strategies with bispecific antibodies. MAbs 2012; 4:182-97; PMID:22453100; http://dx.doi.org/10.4161/mabs.4.2.19000
    • (2012) MAbs , vol.4 , pp. 182-197
    • Kontermann, R.1
  • 2
    • 79955666020 scopus 로고    scopus 로고
    • Introduction to current and future protein therapeutics: A protein engineering perspective
    • PMID:21371474
    • Carter PJ. Introduction to current and future protein therapeutics: a protein engineering perspective. Exp Cell Res 2011; 317:1261-9; PMID:21371474; http://dx.doi.org/10.1016/j.yexcr.2011.02.013
    • (2011) Exp Cell Res , vol.317 , pp. 1261-1269
    • Carter, P.J.1
  • 3
    • 0035251463 scopus 로고    scopus 로고
    • Introduction: Bispecific antibodies
    • PMID:11223064
    • Segal DM, Weiner GJ, Weiner LM. Introduction: bispecific antibodies. J Immunol Methods 2001; 248:1-6; PMID:11223064; http://dx.doi.org/10.1016/S0022- 1759(00)00338-0
    • (2001) J Immunol Methods , vol.248 , pp. 1-6
    • Segal, D.M.1    Weiner, G.J.2    Weiner, L.M.3
  • 4
    • 0035251453 scopus 로고    scopus 로고
    • Bispecific human IgG by design
    • PMID:11223065
    • Carter P. Bispecific human IgG by design. J Immunol Methods 2001; 248:7-15; PMID:11223065; http://dx.doi.org/10.1016/S0022-1759(00)00339-2
    • (2001) J Immunol Methods , vol.248 , pp. 7-15
    • Carter, P.1
  • 5
    • 48549089295 scopus 로고    scopus 로고
    • Considerations for the development of therapeutic monoclonal antibodies
    • PMID:18586093
    • Swann PG, Tolnay M, Muthukkumar S, Shapiro MA, Rellahan BL, Clouse KA. Considerations for the development of therapeutic monoclonal antibodies. Curr Opin Immunol 2008; 20:493-9; PMID:18586093; http://dx.doi.org/10.1016/j.coi. 2008.05.013
    • (2008) Curr Opin Immunol , vol.20 , pp. 493-499
    • Swann, P.G.1    Tolnay, M.2    Muthukkumar, S.3    Shapiro, M.A.4    Rellahan, B.L.5    Clouse, K.A.6
  • 6
    • 0029946383 scopus 로고    scopus 로고
    • Knobs-into-holes engineering of antibody CH3 domains for heavy chain heterodimerization
    • PMID:8844834
    • Ridgway JB, Presta LG, Carter P. 'Knobs-into-holes' engineering of antibody CH3 domains for heavy chain heterodimerization. Protein Eng 1996; 9:617-21; PMID:8844834; http://dx.doi.org/10.1093/protein/9.7.617
    • (1996) Protein Eng , vol.9 , pp. 617-621
    • Ridgway, J.B.1    Presta, L.G.2    Carter, P.3
  • 7
    • 0031552589 scopus 로고    scopus 로고
    • Stable heterodimers from remodeling the domain interface of a homodimer using a phage display library
    • PMID:9231898
    • Atwell S, Ridgway JB, Wells JA, Carter P. Stable heterodimers from remodeling the domain interface of a homodimer using a phage display library. J Mol Biol 1997; 270:26-35; PMID:9231898; http://dx.doi. org/10.1006/jmbi.1997. 1116
    • (1997) J Mol Biol , vol.270 , pp. 26-35
    • Atwell, S.1    Ridgway, J.B.2    Wells, J.A.3    Carter, P.4
  • 9
    • 84870302675 scopus 로고    scopus 로고
    • A bispecific antibody to factors IXa and X restores factor VIII hemostatic activity in a hemophilia A model
    • PMID:23023498
    • Kitazawa T, Igawa T, Sampei Z, Muto A, Kojima T, Soeda T, et al. A bispecific antibody to factors IXa and X restores factor VIII hemostatic activity in a hemophilia A model. Nat Med 2012; 18:1570-4; PMID:23023498; http://dx.doi.org/10.1038/nm.2942
    • (2012) Nat Med , vol.18 , pp. 1570-1574
    • Kitazawa, T.1    Igawa, T.2    Sampei, Z.3    Muto, A.4    Kojima, T.5    Soeda, T.6
  • 10
    • 79957439772 scopus 로고    scopus 로고
    • Boosting brain uptake of a therapeutic antibody by reducing its affinity for a transcytosis target?
    • PMID:21613623
    • Yu YJ, Zhang Y, Kenrick M, Hoyte K, Luk W, Lu Y, et al. Boosting brain uptake of a therapeutic antibody by reducing its affinity for a transcytosis target. Sci Transl Med 2011; 3:84ra44; PMID:21613623; http://dx.doi. org/10.1126/scitranslmed.3002230
    • (2011) Sci Transl Med , vol.3
    • Yu, Y.J.1    Zhang, Y.2    Kenrick, M.3    Hoyte, K.4    Luk, W.5    Lu, Y.6
  • 11
    • 79960592856 scopus 로고    scopus 로고
    • Immunoglobulin domain crossover as a generic approach for the production of bispecific IgG antibodies
    • PMID:21690412
    • Schaefer W, Regula JT, Bähner M, Schanzer J, Croasdale R, Dürr H, et al. Immunoglobulin domain crossover as a generic approach for the production of bispecific IgG antibodies. Proc Natl Acad Sci U S A 2011; 108:11187-92; PMID:21690412; http://dx.doi. org/10.1073/pnas.1019002108
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 11187-11192
    • Schaefer, W.1    Regula, J.T.2    Bähner, M.3    Schanzer, J.4    Croasdale, R.5    Dürr, H.6
  • 12
    • 84869783247 scopus 로고    scopus 로고
    • Progress in overcoming the chain association issue in bispecific heterodimeric IgG antibodies
    • PMID:22925968
    • Klein C, Sustmann C, Thomas M, Stubenrauch K, Croasdale R, Schanzer J, et al. Progress in overcoming the chain association issue in bispecific heterodimeric IgG antibodies. MAbs 2012; 4:653-63; PMID:22925968; http://dx.doi.org/10.4161/mabs.21379
    • (2012) MAbs , vol.4 , pp. 653-663
    • Klein, C.1    Sustmann, C.2    Thomas, M.3    Stubenrauch, K.4    Croasdale, R.5    Schanzer, J.6
  • 13
    • 49249100382 scopus 로고    scopus 로고
    • MetMAb, the one-armed 5D5 anti-c-Met antibody, inhibits orthotopic pancreatic tumor growth and improves survival
    • PMID:18519697
    • Jin H, Yang R, Zheng Z, Romero M, Ross J, Bou-Reslan H, et al. MetMAb, the one-armed 5D5 anti-c-Met antibody, inhibits orthotopic pancreatic tumor growth and improves survival. Cancer Res 2008; 68:4360-8; PMID:18519697; http://dx.doi. org/10.1158/0008-5472.CAN-07-5960
    • (2008) Cancer Res , vol.68 , pp. 4360-4368
    • Jin, H.1    Yang, R.2    Zheng, Z.3    Romero, M.4    Ross, J.5    Bou-Reslan, H.6
  • 15
    • 77954225154 scopus 로고    scopus 로고
    • Development of a two-part strategy to identify a therapeutic human bispecific antibody that inhibits IgE receptor signaling
    • PMID:20444694
    • Jackman J, Chen Y, Huang A, Moffat B, Scheer JM, Leong SR, et al. Development of a two-part strategy to identify a therapeutic human bispecific antibody that inhibits IgE receptor signaling. J Biol Chem 2010; 285:20850-9; PMID:20444694; http://dx.doi. org/10.1074/jbc.M110.113910
    • (2010) J Biol Chem , vol.285 , pp. 20850-20859
    • Jackman, J.1    Chen, Y.2    Huang, A.3    Moffat, B.4    Scheer, J.M.5    Leong, S.R.6
  • 16
    • 84871565611 scopus 로고    scopus 로고
    • LUZ-Y, a novel platform for the mammalian cell production of full-length IgGbispecific antibodies
    • PMID:23118228
    • Wranik BJ, Christensen EL, Schaefer G, Jackman JK, Vendel AC, Eaton D. LUZ-Y, a novel platform for the mammalian cell production of full-length IgGbispecific antibodies. J Biol Chem 2012; 287:43331-9; PMID:23118228; http://dx.doi.org/10.1074/jbc. M112.397869
    • (2012) J Biol Chem , vol.287 , pp. 43331-43339
    • Wranik, B.J.1    Christensen, E.L.2    Schaefer, G.3    Jackman, J.K.4    Vendel, A.C.5    Eaton, D.6
  • 17
    • 84862015979 scopus 로고    scopus 로고
    • Generating bispecific human IgG1 and IgG2 antibodies from any antibody pair
    • PMID:22543237
    • Strop P, Ho WH, Boustany LM, Abdiche YN, Lindquist KC, Farias SE, et al. Generating bispecific human IgG1 and IgG2 antibodies from any antibody pair. J Mol Biol 2012; 420:204-19; PMID:22543237; http://dx.doi.org/10.1016/j.jmb.2012. 04.020
    • (2012) J Mol Biol , vol.420 , pp. 204-219
    • Strop, P.1    Ho, W.H.2    Boustany, L.M.3    Abdiche, Y.N.4    Lindquist, K.C.5    Farias, S.E.6
  • 19
    • 77953485268 scopus 로고    scopus 로고
    • Enhancing antibody Fc heterodimer formation through electrostatic steering effects: Applications to bispecific molecules and monovalent IgG
    • PMID:20400508
    • Gunasekaran K, Pentony M, Shen M, Garrett L, Forte C, Woodward A, et al. Enhancing antibody Fc heterodimer formation through electrostatic steering effects: applications to bispecific molecules and monovalent IgG. J Biol Chem 2010; 285:19637-46; PMID:20400508; http://dx.doi.org/10.1074/jbc. M110.117382
    • (2010) J Biol Chem , vol.285 , pp. 19637-19646
    • Gunasekaran, K.1    Pentony, M.2    Shen, M.3    Garrett, L.4    Forte, C.5    Woodward, A.6
  • 20
    • 77954628740 scopus 로고    scopus 로고
    • SEEDbodies: Fusion proteins based on strandexchange engineered domain (SEED) CH3 heterodimers in an Fc analogue platform for asymmetric binders or immunofusions and bispecific antibodies
    • PMID:20299542
    • Davis JH, Aperlo C, Li Y, Kurosawa E, Lan Y, Lo KM, et al. SEEDbodies: fusion proteins based on strandexchange engineered domain (SEED) CH3 heterodimers in an Fc analogue platform for asymmetric binders or immunofusions and bispecific antibodies. Protein Eng Des Sel 2010; 23:195-202; PMID:20299542; http://dx.doi.org/10.1093/protein/gzp094
    • (2010) Protein Eng des Sel , vol.23 , pp. 195-202
    • Davis, J.H.1    Aperlo, C.2    Li, Y.3    Kurosawa, E.4    Lan, Y.5    Lo, K.M.6
  • 21
    • 81255210896 scopus 로고    scopus 로고
    • A novel bispecific antibody format enables simultaneous bivalent and monovalent co-engagement of distinct target antigens
    • PMID:22123055
    • Moore GL, Bautista C, Pong E, Nguyen DH, Jacinto J, Eivazi A, et al. A novel bispecific antibody format enables simultaneous bivalent and monovalent co-engagement of distinct target antigens. MAbs 2011; 3:546-57; PMID:22123055; http://dx.doi. org/10.4161/mabs.3.6.18123
    • (2011) MAbs , vol.3 , pp. 546-557
    • Moore, G.L.1    Bautista, C.2    Pong, E.3    Nguyen, D.H.4    Jacinto, J.5    Eivazi, A.6
  • 22
    • 11844291300 scopus 로고    scopus 로고
    • Protein aggregation and its inhibition in biopharmaceutics
    • PMID:15652195
    • Wang W. Protein aggregation and its inhibition in biopharmaceutics. Int J Pharm 2005; 289:1-30; PMID:15652195; http://dx.doi.org/10.1016/j. ijpharm.2004.11.014
    • (2005) Int J Pharm , vol.289 , pp. 1-30
    • Wang, W.1
  • 23
    • 50249132634 scopus 로고    scopus 로고
    • Antibody therapeutics, antibody engineering, and the merits of protein stability
    • PMID:18729019
    • Demarest SJ, Glaser SM. Antibody therapeutics, antibody engineering, and the merits of protein stability. Curr Opin Drug Discov Devel 2008; 11:675-87; PMID:18729019
    • (2008) Curr Opin Drug Discov Devel , vol.11 , pp. 675-687
    • Demarest, S.J.1    Glaser, S.M.2
  • 24
    • 84883892486 scopus 로고    scopus 로고
    • Using differential scanning calorimetry in understanding the correlation between thermal stability and protein stability: A case study
    • Wen J, Jiang Y, Hymes K, Gong K, Nahri L. Using Differential Scanning Calorimetry in Understanding the Correlation Between Thermal Stability and Protein Stability: A Case Study. Microcal Application Note, 2011.
    • (2011) Microcal Application Note
    • Wen, J.1    Jiang, Y.2    Hymes, K.3    Gong, K.4    Nahri, L.5
  • 25
    • 84863045993 scopus 로고    scopus 로고
    • Disulfide bond structures of IgG molecules: Structural variations, chemical modifications and possible impacts to stability and biological function
    • PMID:22327427
    • Liu H, May K. Disulfide bond structures of IgG molecules: structural variations, chemical modifications and possible impacts to stability and biological function. MAbs 2012; 4:17-23; PMID:22327427; http://dx.doi.org/10. 4161/mabs.4.1.18347
    • (2012) MAbs , vol.4 , pp. 17-23
    • Liu, H.1    May, K.2
  • 26
    • 84883856643 scopus 로고    scopus 로고
    • Developability studies before initiation of process development: Improving manufacturability of monoclonal antibodies
    • Yang X, Xu W, Dukleska S, Benchaar B, Mengisen S, Antochshuk V, et al. Developability studies before initiation of process development: Improving manufacturability of monoclonal antibodies. MAbs 2013; 5:787-94; http://dx.doi.org/10.4161/mabs.25269.
    • (2013) MAbs , vol.5 , pp. 787-794
    • Yang, X.1    Xu, W.2    Dukleska, S.3    Benchaar, B.4    Mengisen, S.5    Antochshuk, V.6
  • 27
    • 84876563164 scopus 로고    scopus 로고
    • Engineering a therapeutic IgG molecule to address cysteinylation, aggregation and enhance thermal stability and expression
    • PMID:23412563
    • Buchanan A, Clementel V, Woods R, Harn N, Bowen MA, Mo W, et al. Engineering a therapeutic IgG molecule to address cysteinylation, aggregation and enhance thermal stability and expression. MAbs 2013; 5:255-62; PMID:23412563; http://dx.doi. org/10.4161/mabs.23392
    • (2013) MAbs , vol.5 , pp. 255-262
    • Buchanan, A.1    Clementel, V.2    Woods, R.3    Harn, N.4    Bowen, M.A.5    Mo, W.6
  • 28
    • 24644472964 scopus 로고    scopus 로고
    • Specificity versus stability in computational protein design
    • PMID:16129838
    • Bolon DN, Grant RA, Baker TA, Sauer RT. Specificity versus stability in computational protein design. Proc Natl Acad Sci U S A 2005; 102:12724-9; PMID:16129838; http://dx.doi.org/10.1073/pnas.0506124102
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 12724-12729
    • Bolon, D.N.1    Grant, R.A.2    Baker, T.A.3    Sauer, R.T.4
  • 29
    • 0019522383 scopus 로고
    • Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9- and 2.8-A resolution?
    • PMID:7236608
    • Deisenhofer J. Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9- and 2.8-A resolution. Biochemistry 1981; 20:2361-70; PMID:7236608; http://dx.doi. org/10.1021/bi00512a001
    • (1981) Biochemistry , vol.20 , pp. 2361-2370
    • Deisenhofer, J.1
  • 30
    • 0032581013 scopus 로고    scopus 로고
    • Contribution of domain interface residues to the stability of antibody CH3 domain homodimers
    • PMID:9649307
    • Dall'Acqua W, Simon AL, Mulkerrin MG, Carter P. Contribution of domain interface residues to the stability of antibody CH3 domain homodimers. Biochemistry 1998; 37:9266-73; PMID:9649307; http://dx.doi.org/10.1021/bi980270i
    • (1998) Biochemistry , vol.37 , pp. 9266-9273
    • Dall'Acqua, W.1    Simon, A.L.2    Mulkerrin, M.G.3    Carter, P.4
  • 31
    • 33748518255 scopus 로고    scopus 로고
    • Comparison of multiple Amber force fields and development of improved protein backbone parameters
    • PMID:16981200
    • Hornak V, Abel R, Okur A, Strockbine B, Roitberg A, Simmerling C. Comparison of multiple Amber force fields and development of improved protein backbone parameters. Proteins 2006; 65:712-25; PMID:16981200; http://dx.doi.org/10.1002/prot.21123
    • (2006) Proteins , vol.65 , pp. 712-725
    • Hornak, V.1    Abel, R.2    Okur, A.3    Strockbine, B.4    Roitberg, A.5    Simmerling, C.6
  • 32
    • 0000043930 scopus 로고    scopus 로고
    • Solvation Free Energy of Biomacromolecules: Parameters for a Modified Generalized Born Model Consistent with the AMBER Force Field
    • Jayaram B, Sprous D, Beveridge DL. Solvation Free Energy of Biomacromolecules: Parameters for a Modified Generalized Born Model Consistent with the AMBER Force Field. J Phys Chem B 1998; 102:9571-6; http://dx.doi.org/ 10.1021/jp982007x
    • (1998) J Phys Chem B , vol.102 , pp. 9571-9576
    • Jayaram, B.1    Sprous, D.2    Beveridge, D.L.3
  • 33
    • 0030968991 scopus 로고    scopus 로고
    • Empirical potentials and functions for protein folding and binding
    • PMID:9094333
    • Vajda S, Sippl M, Novotny J. Empirical potentials and functions for protein folding and binding. Curr Opin Struct Biol 1997; 7:222-8; PMID:9094333; http://dx.doi.org/10.1016/S0959-440X(97)80029-2
    • (1997) Curr Opin Struct Biol , vol.7 , pp. 222-228
    • Vajda, S.1    Sippl, M.2    Novotny, J.3
  • 34
    • 0035838974 scopus 로고    scopus 로고
    • Extending the accuracy limits of prediction for side-chain conformations
    • PMID:11478870
    • Xiang Z, Honig B. Extending the accuracy limits of prediction for side-chain conformations. J Mol Biol 2001; 311:421-30; PMID:11478870; http://dx.doi. org/10.1006/jmbi.2001.4865
    • (2001) J Mol Biol , vol.311 , pp. 421-430
    • Xiang, Z.1    Honig, B.2
  • 35
    • 32044456003 scopus 로고    scopus 로고
    • The backrub motion: How protein backbone shrugs when a sidechain dances
    • PMID:16472746
    • rd, Richardson DC, Richardson JS. The backrub motion: how protein backbone shrugs when a sidechain dances. Structure 2006; 14:265-74; PMID:16472746; http://dx.doi. org/10.1016/j.str.2005.10.007
    • (2006) Structure , vol.14 , pp. 265-274
    • Davis, I.W.1    Arendall III, W.B.2    Richardson, D.C.3    Richardson, J.S.4
  • 36
    • 63749128279 scopus 로고    scopus 로고
    • Reducing risk, improving outcomes: Bioengineering less immunogenic protein therapeutics
    • PMID:19269256
    • De Groot AS, Martin W. Reducing risk, improving outcomes: bioengineering less immunogenic protein therapeutics. Clin Immunol 2009; 131:189-201; PMID:19269256; http://dx.doi.org/10.1016/j. clim.2009.01.009
    • (2009) Clin Immunol , vol.131 , pp. 189-201
    • De Groot, A.S.1    Martin, W.2
  • 37
    • 75149152376 scopus 로고    scopus 로고
    • Prediction of immunogenicity of therapeutic proteins: Validity of computational tools
    • PMID:20055528
    • Bryson CJ, Jones TD, Baker MP. Prediction of immunogenicity of therapeutic proteins: validity of computational tools. Bio Drugs 2010; 24:1-8; PMID:20055528; http://dx.doi.org/10.2165/11318560-000000000-00000
    • (2010) Bio Drugs , vol.24 , pp. 1-8
    • Bryson, C.J.1    Jones, T.D.2    Baker, M.P.3
  • 38
    • 43249105327 scopus 로고    scopus 로고
    • Contribution of variable domains to the stability of humanized IgG1 monoclonal antibodies
    • PMID:17721938
    • Ionescu RM, Vlasak J, Price C, Kirchmeier M. Contribution of variable domains to the stability of humanized IgG1 monoclonal antibodies. J Pharm Sci 2008; 97:1414-26; PMID:17721938; http://dx.doi. org/10.1002/jps.21104
    • (2008) J Pharm Sci , vol.97 , pp. 1414-1426
    • Ionescu, R.M.1    Vlasak, J.2    Price, C.3    Kirchmeier, M.4
  • 39
    • 84871295525 scopus 로고    scopus 로고
    • Effect of pH, temperature, and salt on the stability of Escherichia coli- and Chinese hamster ovary cell-derived IgG1 Fc
    • PMID:23078371
    • Li CH, Narhi LO, Wen J, Dimitrova M, Wen ZQ, Li J, et al. Effect of pH, temperature, and salt on the stability of Escherichia coli- and Chinese hamster ovary cell-derived IgG1 Fc. Biochemistry 2012; 51:10056-65; PMID:23078371; http://dx.doi.org/10.1021/bi300702e
    • (2012) Biochemistry , vol.51 , pp. 10056-10065
    • Li, C.H.1    Narhi, L.O.2    Wen, J.3    Dimitrova, M.4    Wen, Z.Q.5    Li, J.6
  • 40
    • 0344255687 scopus 로고    scopus 로고
    • Optimization of the antibody C(H)3 domain by residue frequency analysis of IgG sequences
    • PMID:14659738
    • Demarest SJ, Rogers J, Hansen G. Optimization of the antibody C(H)3 domain by residue frequency analysis of IgG sequences. J Mol Biol 2004; 335:41-8; PMID:14659738; http://dx.doi.org/10.1016/j. jmb.2003.10.040
    • (2004) J Mol Biol , vol.335 , pp. 41-48
    • Demarest, S.J.1    Rogers, J.2    Hansen, G.3
  • 41
    • 33847416982 scopus 로고    scopus 로고
    • A broad range of Fab stabilities within a host of therapeutic IgGs
    • PMID:17321501
    • Garber E, Demarest SJ. A broad range of Fab stabilities within a host of therapeutic IgGs. Biochem Biophys Res Commun 2007; 355:751-7; PMID:17321501; http://dx.doi.org/10.1016/j.bbrc.2007.02.042
    • (2007) Biochem Biophys Res Commun , vol.355 , pp. 751-757
    • Garber, E.1    Demarest, S.J.2
  • 42
    • 7044247460 scopus 로고    scopus 로고
    • Folding mechanism of the CH2 antibody domain
    • PMID:15504405
    • Feige MJ, Walter S, Buchner J. Folding mechanism of the CH2 antibody domain. J Mol Biol 2004; 344:107-18; PMID:15504405; http://dx.doi.org/10.1016/j. jmb.2004.09.033
    • (2004) J Mol Biol , vol.344 , pp. 107-118
    • Feige, M.J.1    Walter, S.2    Buchner, J.3
  • 43
    • 0033569502 scopus 로고    scopus 로고
    • Folding and association of the antibody domain CH3: Prolyl isomerization preceeds dimerization
    • PMID:10512716
    • Thies MJ, Mayer J, Augustine JG, Frederick CA, Lilie H, Buchner J. Folding and association of the antibody domain CH3: prolyl isomerization preceeds dimerization. J Mol Biol 1999; 293:67-79; PMID:10512716; http://dx.doi.org/10.1006/jmbi.1999.3128
    • (1999) J Mol Biol , vol.293 , pp. 67-79
    • Thies, M.J.1    Mayer, J.2    Augustine, J.G.3    Frederick, C.A.4    Lilie, H.5    Buchner, J.6
  • 44
    • 0036301435 scopus 로고    scopus 로고
    • Folding and oxidation of the antibody domain C(H)3
    • PMID:12079363
    • Thies MJ, Talamo F, Mayer M, Bell S, Ruoppolo M, Marino G, et al. Folding and oxidation of the antibody domain C(H)3. J Mol Biol 2002; 319:1267-77; PMID:12079363; http://dx.doi.org/10.1016/S0022-2836(02)00375-3
    • (2002) J Mol Biol , vol.319 , pp. 1267-1277
    • Thies, M.J.1    Talamo, F.2    Mayer, M.3    Bell, S.4    Ruoppolo, M.5    Marino, G.6
  • 45
    • 37548998932 scopus 로고    scopus 로고
    • Contributions of a disulfide bond to the structure, stability, and dimerization of human IgG1 antibody CH3 domain
    • PMID:18156469
    • McAuley A, Jacob J, Kolvenbach CG, Westland K, Lee HJ, Brych SR, et al. Contributions of a disulfide bond to the structure, stability, and dimerization of human IgG1 antibody CH3 domain. Protein Sci 2008; 17:95-106; PMID:18156469; http://dx.doi.org/10.1110/ps.073134408
    • (2008) Protein Sci , vol.17 , pp. 95-106
    • McAuley, A.1    Jacob, J.2    Kolvenbach, C.G.3    Westland, K.4    Lee, H.J.5    Brych, S.R.6
  • 46
    • 79960107245 scopus 로고    scopus 로고
    • Bispecific antibodies and ADCs: Once and future kings?
    • PMID:21654205
    • Reichert JM. Bispecific antibodies and ADCs: Once and future kings? MAbs 2011; 3:329-30; PMID:21654205; http://dx.doi.org/10.4161/mabs.3.4.16589
    • (2011) MAbs , vol.3 , pp. 329-330
    • Reichert, J.M.1
  • 47
    • 77956637683 scopus 로고    scopus 로고
    • Physicochemical stability of the antibody-drug conjugate Trastuzumab-DM1: Changes due to modification and conjugation processes
    • PMID:20698491
    • Wakankar AA, Feeney MB, Rivera J, Chen Y, Kim M, Sharma VK, et al. Physicochemical stability of the antibody-drug conjugate Trastuzumab-DM1: changes due to modification and conjugation processes. Bioconjug Chem 2010; 21:1588-95; PMID:20698491; http://dx.doi.org/10.1021/bc900434c
    • (2010) Bioconjug Chem , vol.21 , pp. 1588-1595
    • Wakankar, A.A.1    Feeney, M.B.2    Rivera, J.3    Chen, Y.4    Kim, M.5    Sharma, V.K.6
  • 49
    • 47749141082 scopus 로고    scopus 로고
    • Estimation of protein aggregation propensity with a melting point apparatus
    • PMID:18544334
    • Raibekas AA. Estimation of protein aggregation propensity with a melting point apparatus. Anal Biochem 2008; 380:331-2; PMID:18544334; http://dx.doi. org/10.1016/j.ab.2008.05.023
    • (2008) Anal Biochem , vol.380 , pp. 331-332
    • Raibekas, A.A.1
  • 50
    • 84883869187 scopus 로고    scopus 로고
    • LC-MS characterization and purity assessment of a prototype bispecific antibody
    • Woods RJ, Xie M, von Kreudenstein T, Ng G, Dixit SB. LC-MS characterization and purity assessment of a prototype bispecific antibody. MAbs 2013; 5:711-22; http://dx.doi.org/10.4161/mabs.25488.
    • (2013) MAbs , vol.5 , pp. 711-722
    • Woods, R.J.1    Xie, M.2    Von Kreudenstein, T.3    Ng, G.4    Dixit, S.B.5
  • 51
    • 84855862411 scopus 로고    scopus 로고
    • Rapid production of functional proteins of a combinatorial IgG library in CHO cells
    • Girod PA, Le Fourn V. Rapid production of functional proteins of a combinatorial IgG library in CHO cells. Bioprocess Int 2012; 10:58-61
    • (2012) Bioprocess Int , vol.10 , pp. 58-61
    • Girod, P.A.1    Le Fourn, V.2
  • 52
    • 77954953911 scopus 로고    scopus 로고
    • Comparison of humanized IgG and FvFc anti-CD3 monoclonal antibodies expressed in CHO cells
    • PMID:20336495
    • Serpieri F, Inocencio A, de Oliveira JM, Pimenta AA Jr., Garbuio A, Kalil J, et al. Comparison of humanized IgG and FvFc anti-CD3 monoclonal antibodies expressed in CHO cells. Mol Biotechnol 2010; 45:218-25; PMID:20336495; http://dx.doi.org/10.1007/s12033-010-9269-2
    • (2010) Mol Biotechnol , vol.45 , pp. 218-225
    • Serpieri, F.1    Inocencio, A.2    De Oliveira, J.M.3    Pimenta Jr., A.A.4    Garbuio, A.5    Kalil, J.6


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