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Volumn 407, Issue 1, 2015, Pages 79-94

Post-translational structural modifications of immunoglobulin G and their effect on biological activity

Author keywords

Bioprocess; Effector function; IgG; Monoclonal antibodies; Post translational modifications

Indexed keywords

BIOACTIVITY; CHEMICAL DETECTION; MOLECULES; MONOCLONAL ANTIBODIES; PROTEINS; SURFACE PLASMON RESONANCE;

EID: 84926684939     PISSN: 16182642     EISSN: 16182650     Source Type: Journal    
DOI: 10.1007/s00216-014-8108-x     Document Type: Review
Times cited : (74)

References (183)
  • 1
    • 60849128549 scopus 로고    scopus 로고
    • Monoclonal antibodies as innovative therapeutics
    • Reichert JM (2008) Monoclonal antibodies as innovative therapeutics. Curr Pharm Biotechnol 9:423-430
    • (2008) Curr Pharm Biotechnol , vol.9 , pp. 423-430
    • Reichert, J.M.1
  • 2
    • 0015327927 scopus 로고
    • The catabolism of human G immunoglobulins of different heavy chain subclasses. 3. The catabolism of heavy chain disease proteins and of Fc fragments of myeloma proteins
    • Spiegelberg HL, Fishkin BG (1972) The catabolism of human G immunoglobulins of different heavy chain subclasses. 3. The catabolism of heavy chain disease proteins and of Fc fragments of myeloma proteins. Clin Exp Immunol 10:599-607
    • (1972) Clin Exp Immunol , vol.10 , pp. 599-607
    • Spiegelberg, H.L.1    Fishkin, B.G.2
  • 3
    • 77953681422 scopus 로고    scopus 로고
    • Stability of IgG isotypes in serum
    • Correia IR (2010) Stability of IgG isotypes in serum. MAbs 2:221-232
    • (2010) MAbs , vol.2 , pp. 221-232
    • Correia, I.R.1
  • 4
    • 37549036732 scopus 로고    scopus 로고
    • Fcγ receptors as regulators of immune responses
    • Nimmerjahn F, Ravtech JV (2008) Fcγ receptors as regulators of immune responses. Nat Rev Immunol 8:34-47
    • (2008) Nat Rev Immunol , vol.8 , pp. 34-47
    • Nimmerjahn, F.1    Ravtech, J.V.2
  • 5
    • 34548229364 scopus 로고    scopus 로고
    • FcRn: The neonatal Fc receptor comes of age
    • Roopenian DC, Akilesh S (2007) FcRn: the neonatal Fc receptor comes of age. Nat Rev Immunol 7:715-725
    • (2007) Nat Rev Immunol , vol.7 , pp. 715-725
    • Roopenian, D.C.1    Akilesh, S.2
  • 6
    • 0034042660 scopus 로고    scopus 로고
    • Multiple roles for the major histocompatibility complex class I- related receptor FcRn
    • Ghetie V, Ward ES (2000) Multiple roles for the major histocompatibility complex class I- related receptor FcRn. Annu Rev Immunol 18:739-766
    • (2000) Annu Rev Immunol , vol.18 , pp. 739-766
    • Ghetie, V.1    Ward, E.S.2
  • 7
    • 15244351004 scopus 로고    scopus 로고
    • Overview of monoclonal antibodies in cancer therapy: Present and promise
    • Stern M, Herrmann R (2005) Overview of monoclonal antibodies in cancer therapy: present and promise. Crit Rev Oncol Hematol 54: 11-29
    • (2005) Crit Rev Oncol Hematol , vol.54 , pp. 11-29
    • Stern, M.1    Herrmann, R.2
  • 8
    • 0041829306 scopus 로고    scopus 로고
    • Current methods for the generation of human antibodies for the treatment of autoimmune diseases
    • Osbourn J, Jermutus L, Duncan A (2003) Current methods for the generation of human antibodies for the treatment of autoimmune diseases. Drug Discov Today 8:845-851
    • (2003) Drug Discov Today , vol.8 , pp. 845-851
    • Osbourn, J.1    Jermutus, L.2    Duncan, A.3
  • 9
    • 68749110765 scopus 로고    scopus 로고
    • Optimal and consistent protein glycosylation in mammalian cell culture
    • Hossler P, Khattak SF, Li ZJ (2009) Optimal and consistent protein glycosylation in mammalian cell culture. Glycobiology 19:936-949
    • (2009) Glycobiology , vol.19 , pp. 936-949
    • Hossler, P.1    Khattak, S.F.2    Li, Z.J.3
  • 10
    • 80051711268 scopus 로고    scopus 로고
    • Industry and regulatory experience of the glycosylation of monoclonal antibodies
    • Read EK, Park JT, Brorson KA (2011) Industry and regulatory experience of the glycosylation of monoclonal antibodies. Biotechnol Appl Biochem 58:213-219
    • (2011) Biotechnol Appl Biochem , vol.58 , pp. 213-219
    • Read, E.K.1    Park, J.T.2    Brorson, K.A.3
  • 11
  • 12
    • 1542291118 scopus 로고    scopus 로고
    • Post-translational modification of therapeutic proteins in plants
    • Gomord V, Faye L (2004) Post-translational modification of therapeutic proteins in plants. Curr Opin Plant Biol 7:171-181
    • (2004) Curr Opin Plant Biol , vol.7 , pp. 171-181
    • Gomord, V.1    Faye, L.2
  • 13
    • 0014823629 scopus 로고
    • Attachment of carbohydrate to the variable region of myeloma immunoglobulin light chains
    • Sox HC Jr, Hood L (1970) Attachment of carbohydrate to the variable region of myeloma immunoglobulin light chains. Proc Natl Acad Sci U S A 66:975-982
    • (1970) Proc Natl Acad Sci U S A , vol.66 , pp. 975-982
    • Sox, H.C.1    Hood, L.2
  • 14
    • 0014944053 scopus 로고
    • Localization of the carbohydrate within the variable region of light and heavy chains of human γg myeloma proteins
    • Spiegelberg HL, Abel CA, Fishkin BG, Grey HM (1970) Localization of the carbohydrate within the variable region of light and heavy chains of human γG myeloma proteins. Biochemistry 9: 4217-4223
    • (1970) Biochemistry , vol.9 , pp. 4217-4223
    • Spiegelberg, H.L.1    Abel, C.A.2    Fishkin, B.G.3    Grey, H.M.4
  • 15
    • 33646093725 scopus 로고    scopus 로고
    • Differential glycosylation of polyclonal IgG, IgG-Fc, and IgG-Fab isolated from the sera of patients with ANCA-associated systemic vasculitis
    • Holland M, Yagi H, Takahashi N, Kato K, Savage COS, Goodall DM, Jefferis R (2006) Differential glycosylation of polyclonal IgG, IgG-Fc, and IgG-Fab isolated from the sera of patients with ANCA-associated systemic vasculitis. Biochim Biophys Acta Gen Subj 1760:669-677
    • (2006) Biochim Biophys Acta Gen Subj , vol.1760 , pp. 669-677
    • Holland, M.1    Yagi, H.2    Takahashi, N.3    Kato, K.4    Savage, C.O.S.5    Goodall, D.M.6    Jefferis, R.7
  • 16
    • 0025909201 scopus 로고
    • Antibody variable region glycosylation: Position effects on antigen binding and carbohydrate structure
    • Wright A, Tao MH, Kabat EA, Morrison SL (1991) Antibody variable region glycosylation: position effects on antigen binding and carbohydrate structure. EMBO J 10:2717-2723
    • (1991) EMBO J , vol.10 , pp. 2717-2723
    • Wright, A.1    Tao, M.H.2    Kabat, E.A.3    Morrison, S.L.4
  • 17
    • 0023819528 scopus 로고
    • Glycosylation of a VH residue of a monoclonal antibody against alpha (1-6) dextran increases its affinity for antigen
    • Wallick SC, Kabat EA, Morrison SL (1988) Glycosylation of a VH residue of a monoclonal antibody against alpha (1-6) dextran increases its affinity for antigen. J Exp Med 168:1099-1109
    • (1988) J Exp Med , vol.168 , pp. 1099-1109
    • Wallick, S.C.1    Kabat, E.A.2    Morrison, S.L.3
  • 19
    • 34548409568 scopus 로고    scopus 로고
    • Contrasting glycosylation profiles between Fab and Fc of a human IgG protein studied by electrospray ionization mass spectrometry
    • Mimura Y, Ashton PR, Takahashi N, Harvey DJ, Jefferis R (2007) Contrasting glycosylation profiles between Fab and Fc of a human IgG protein studied by electrospray ionization mass spectrometry. J Immunol Methods 326:116-126
    • (2007) J Immunol Methods , vol.326 , pp. 116-126
    • Mimura, Y.1    Ashton, P.R.2    Takahashi, N.3    Harvey, D.J.4    Jefferis, R.5
  • 20
    • 0037474543 scopus 로고    scopus 로고
    • Structural analysis of human IgG-Fc glycoforms reveals a correlation between glycosylation and structural integrity
    • Krapp S, Mimura Y, Jefferis R, Huber R, Sondermann P (2003) Structural analysis of human IgG-Fc glycoforms reveals a correlation between glycosylation and structural integrity. JMol Biol 979-989
    • (2003) JMol Biol , pp. 979-989
    • Krapp, S.1    Mimura, Y.2    Jefferis, R.3    Huber, R.4    Sondermann, P.5
  • 21
    • 0034691322 scopus 로고    scopus 로고
    • The 3.2- angst. Crystal structure of the human IgG1 Fc fragment- Fc[gamma]RIII complex
    • Sondermann P, Huber R, Oosthuizen V, Jacob U (2000) The 3.2- angst. Crystal structure of the human IgG1 Fc fragment- Fc[gamma]RIII complex. Nature 406:267-273
    • (2000) Nature , vol.406 , pp. 267-273
    • Sondermann, P.1    Huber, R.2    Oosthuizen, V.3    Jacob, U.4
  • 23
    • 0035794194 scopus 로고    scopus 로고
    • High resolution mapping of the binding site on human IgG1 for FcγRI, FcγRII, FcγRIII, and FcRn and design of IgG1 variants with improved binding to the FcγR
    • Shields RL, Namenuk AK, Hong K, Meng YG, Rae J, Briggs J, Xie D, Lai J, Stadlen A, Li B, Fox JA, Presta LG (2001) High resolution mapping of the binding site on human IgG1 for FcγRI, FcγRII, FcγRIII, and FcRn and design of IgG1 variants with improved binding to the FcγR. J Biol Chem 276:6591-6604
    • (2001) J Biol Chem , vol.276 , pp. 6591-6604
    • Shields, R.L.1    Namenuk, A.K.2    Hong, K.3    Meng, Y.G.4    Rae, J.5    Briggs, J.6    Xie, D.7    Lai, J.8    Stadlen, A.9    Li, B.10    Fox, J.A.11    Presta, L.G.12
  • 26
    • 0021866261 scopus 로고
    • Effector functions of amonoclonal aglycosylatedmouse IgG2a: Binding and activation of complement component C1 and interaction with human monocyte Fc receptor
    • Leatherbarrow RJ, Rademacher TW, Dwek RA, Woof JM, Clark A, Burton DR, Richardson N, Feinstein A (1985) Effector functions of amonoclonal aglycosylatedmouse IgG2a: binding and activation of complement component C1 and interaction with human monocyte Fc receptor. Mol Immunol 22:407-415
    • (1985) Mol Immunol , vol.22 , pp. 407-415
    • Leatherbarrow, R.J.1    Rademacher, T.W.2    Dwek, R.A.3    Woof, J.M.4    Clark, A.5    Burton, D.R.6    Richardson, N.7    Feinstein, A.8
  • 28
    • 79951838374 scopus 로고    scopus 로고
    • NMR analysis demonstrates immunoglobulin G N-glycans are accessible and dynamic
    • Barb AW, Prestegard JH (2011) NMR analysis demonstrates immunoglobulin G N-glycans are accessible and dynamic. Nat Chem Biol 7:147-153
    • (2011) Nat Chem Biol , vol.7 , pp. 147-153
    • Barb, A.W.1    Prestegard, J.H.2
  • 30
    • 80053941908 scopus 로고    scopus 로고
    • Glycosylation profiles of therapeutic antibody pharmaceuticals
    • Wacker C, Berger CN, Girard P, Meier R (2011) Glycosylation profiles of therapeutic antibody pharmaceuticals. Eur J Pharm Biopharm 79:503-507
    • (2011) Eur J Pharm Biopharm , vol.79 , pp. 503-507
    • Wacker, C.1    Berger, C.N.2    Girard, P.3    Meier, R.4
  • 32
    • 0032055988 scopus 로고    scopus 로고
    • Effect of C2-associated carbohydrate structure on Ig effector function: Studies with chimeric mousehuman IgG1 antibodies in glycosylation mutants of Chinese hamster ovary cells
    • Wright A, Morrison SL (1998) Effect of C2-associated carbohydrate structure on Ig effector function: studies with chimeric mousehuman IgG1 antibodies in glycosylation mutants of Chinese hamster ovary cells. J Immunol 160:3393-3402
    • (1998) J Immunol , vol.160 , pp. 3393-3402
    • Wright, A.1    Morrison, S.L.2
  • 33
    • 0037178791 scopus 로고    scopus 로고
    • Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human Fcγ RIII and antibody-dependent cellular toxicity
    • Shields RL, Lai J, Keck R, O'Connell LY, Hong K, Meng YG, Weikert SH, Presta LG (2002) Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human Fcγ RIII and antibody-dependent cellular toxicity. J Biol Chem 277: 26733-26740
    • (2002) J Biol Chem , vol.277 , pp. 26733-26740
    • Shields, R.L.1    Lai, J.2    Keck, R.3    O'Connell, L.Y.4    Hong, K.5    Meng, Y.G.6    Weikert, S.H.7    Presta, L.G.8
  • 34
    • 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
    • Shinkawa T, Nakamura K, Yamane N, Shoji-Hosaka E, Kanda Y, Sakurada M, Uchida K, Anazawa H, Satoh M, Yamasaki M, Hanai N, Shitara K (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
    • (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    Uchida, K.7    Anazawa, H.8    Satoh, M.9    Yamasaki, M.10    Hanai, N.11    Shitara, K.12
  • 37
    • 0029558207 scopus 로고
    • The effect of the removal of sialic acid, galactose and total carbohydrate on the functional activity of Campath-1H
    • Boyd PN, Lines AC, Patel AK (1995) The effect of the removal of sialic acid, galactose and total carbohydrate on the functional activity of Campath-1H. Mol Immunol 32:1311-1318
    • (1995) Mol Immunol , vol.32 , pp. 1311-1318
    • Boyd, P.N.1    Lines, A.C.2    Patel, A.K.3
  • 38
    • 28844463354 scopus 로고    scopus 로고
    • Control of recombinant monoclonal antibody effector functions by Fc N-glycan remodeling in vitro
    • Hodoniczky J, Zheng YZ, JamesDC (2005) Control of recombinant monoclonal antibody effector functions by Fc N-glycan remodeling in vitro. Biotechnol Prog 21:1644-1652
    • (2005) Biotechnol Prog , vol.21 , pp. 1644-1652
    • Hodoniczky, J.1    Zheng, Y.Z.2    James, D.C.3
  • 41
    • 42649089750 scopus 로고    scopus 로고
    • Anti-inflammatory actions of intravenous immunoglobulin
    • Nimmerjahn F, Ravetch JV (2008) Anti-inflammatory actions of intravenous immunoglobulin. Annu Rev Immunol 26:513-533
    • (2008) Annu Rev Immunol , vol.26 , pp. 513-533
    • Nimmerjahn, F.1    Ravetch, J.V.2
  • 42
    • 33846423857 scopus 로고    scopus 로고
    • The anti-inflammatory activity of IgG: The intravenous IgG paradox
    • Nimmerjahn F, Ravetch JV (2007) The anti-inflammatory activity of IgG: the intravenous IgG paradox. J Exp Med 204:11-15
    • (2007) J Exp Med , vol.204 , pp. 11-15
    • Nimmerjahn, F.1    Ravetch, J.V.2
  • 43
    • 58149378347 scopus 로고    scopus 로고
    • Identification of a receptor required for the anti-inflammatory activity of IVIG
    • Anthony RM, Wermeling F, Karlsson MC, Ravetch JV (2008) Identification of a receptor required for the anti-inflammatory activity of IVIG. Proc Natl Acad Sci U S A 105:19571-19578
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 19571-19578
    • Anthony, R.M.1    Wermeling, F.2    Karlsson, M.C.3    Ravetch, J.V.4
  • 44
    • 0017665490 scopus 로고
    • Antigen of "serum sickness" type of heterophile antibodies in human sera: Identification as gangliosides with N-glycolylneuraminic acid
    • Higashi H, NaikiM, Matuo S, OkouchiK (1977)Antigen of "serum sickness" type of heterophile antibodies in human sera: identification as gangliosides with N-glycolylneuraminic acid. Biochem Biophys Res Commun 79:388-395
    • (1977) Biochem Biophys Res Commun , vol.79 , pp. 388-395
    • Higashi, H.1    Naiki, M.2    Matuo, S.3    Okouchi, K.4
  • 45
    • 0018152253 scopus 로고
    • Characterization of the Hanganutziu-Deicher (serum-sickness) antigen as gangliosides containing N-glycolylneuraminic acid
    • Merrick JM, Zadarlik K, Milgrom F (1978) Characterization of the Hanganutziu-Deicher (serum-sickness) antigen as gangliosides containing N-glycolylneuraminic acid. Int Arch Allergy Appl Immunol 57:477-580
    • (1978) Int Arch Allergy Appl Immunol , vol.57 , pp. 477-580
    • Merrick, J.M.1    Zadarlik, K.2    Milgrom, F.3
  • 46
    • 77955436442 scopus 로고    scopus 로고
    • Implications of the presence of N-glycolylneuraminic acid in recombinant therapeutic glycoproteins
    • Ghaderi D, Taylor RE, Padler-Karavani V, Diaz S, Varki A (2010) Implications of the presence of N-glycolylneuraminic acid in recombinant therapeutic glycoproteins. Nat Biotechnol 28:863-867
    • (2010) Nat Biotechnol , vol.28 , pp. 863-867
    • Ghaderi, D.1    Taylor, R.E.2    Padler-Karavani, V.3    Diaz, S.4    Varki, A.5
  • 47
    • 0034495971 scopus 로고    scopus 로고
    • In vivo trafficking and catabolism of igG1 antibodies with Fc associated carbohydrates of differing structure
    • Wright A, Sato Y, Okada T, Chang KH, Endo T, Morrison SL (2000) In vivo trafficking and catabolism of IgG1 antibodies with Fc associated carbohydrates of differing structure. Glycobiology 10: 1347-1355
    • (2000) Glycobiology , vol.10 , pp. 1347-1355
    • Wright, A.1    Sato, Y.2    Okada, T.3    Chang, K.H.4    Endo, T.5    Morrison, S.L.6
  • 48
    • 84863440630 scopus 로고    scopus 로고
    • Production, characterization, and pharmacokinetic properties of antibodies with N-linked mannose-5 glycans
    • Landes Bioscience
    • YuM, Brown D, Reed C, Chung S, Lutman J, Stefanich E, Wong A, Stephan J-P, Bayer R (2012) Production, characterization, and pharmacokinetic properties of antibodies with N-linked mannose-5 glycans. mAbs 4(4):475-487, Landes Bioscience
    • (2012) MAbs , vol.4 , Issue.4 , pp. 475-487
    • Yum Brown, D.1    Reed, C.2    Chung, S.3    Lutman, J.4    Stefanich, E.5    Wong, A.6    Stephan, J.-P.7    Bayer, R.8
  • 49
    • 0033044588 scopus 로고    scopus 로고
    • Engineered glycoforms of an antineuroblastoma IgG1 with optimized antibody-dependent cellular cytotoxic activity
    • Umana P, Jean-Mairet J, Moudry R, Amstutz H, Bailey JE (1999) Engineered glycoforms of an antineuroblastoma IgG1 with optimized antibody-dependent cellular cytotoxic activity. Nat Biotechnol 17:176-180
    • (1999) Nat Biotechnol , vol.17 , pp. 176-180
    • Umana, P.1    Jean-Mairet, J.2    Moudry, R.3    Amstutz, H.4    Bailey, J.E.5
  • 50
    • 33646070900 scopus 로고    scopus 로고
    • Modulation of therapeutic antibody effector functions by glycosylation engineering: Influence of Golgi enzyme localization domain and co-expression of heterologous β1, 4-Nacetylglucosaminyltransferase III and Golgi α-mannosidase II
    • Ferrara C, Brünker P, Suter T, Moser S, Püntener U, Umaña P (2006) Modulation of therapeutic antibody effector functions by glycosylation engineering: influence of Golgi enzyme localization domain and co-expression of heterologous β1, 4-Nacetylglucosaminyltransferase III and Golgi α-mannosidase II. Biotechnol Bioeng 93:851-861
    • (2006) Biotechnol Bioeng , vol.93 , pp. 851-861
    • Ferrara, C.1    Brünker, P.2    Suter, T.3    Moser, S.4    Püntener, U.5    Umaña, P.6
  • 51
    • 23844433927 scopus 로고    scopus 로고
    • Animal cell cultures: Recent achievements and perspectives in the production of biopharmaceuticals
    • Butler M (2005) Animal cell cultures: recent achievements and perspectives in the production of biopharmaceuticals. Appl Microbiol Biotechnol 68:283-291
    • (2005) Appl Microbiol Biotechnol , vol.68 , pp. 283-291
    • Butler, M.1
  • 52
    • 84879259694 scopus 로고    scopus 로고
    • Fermentanomics informed amino acid supplementation of an antibody producing mammalian cell culture
    • Read EK, Bradley SA, Smitka TA, Agarabi CD, Lute SC, Brorson KA (2013) Fermentanomics informed amino acid supplementation of an antibody producing mammalian cell culture. Biotechnol Prog 29:745-753
    • (2013) Biotechnol Prog , vol.29 , pp. 745-753
    • Read, E.K.1    Bradley, S.A.2    Smitka, T.A.3    Agarabi, C.D.4    Lute, S.C.5    Brorson, K.A.6
  • 54
    • 84865578480 scopus 로고    scopus 로고
    • Glycoprotein analysis using mass spectrometry: Unraveling the layers of complexity
    • Schiel JE (2012) Glycoprotein analysis using mass spectrometry: unraveling the layers of complexity. Anal Bioanal Chem 404:1141-1149
    • (2012) Anal Bioanal Chem , vol.404 , pp. 1141-1149
    • Schiel, J.E.1
  • 55
    • 77952820391 scopus 로고    scopus 로고
    • A multi-method approach toward de novo glycan characterization: A Man-5 case study
    • Prien JM, Prater BD, Cockrill SL (2010) A multi-method approach toward de novo glycan characterization: a Man-5 case study. Glycobiology 20:629-647
    • (2010) Glycobiology , vol.20 , pp. 629-647
    • Prien, J.M.1    Prater, B.D.2    Cockrill, S.L.3
  • 58
    • 77955412238 scopus 로고    scopus 로고
    • Posttranslational modifications differentially affect IgG1 conformation and receptor binding
    • Houde D, Peng Y, Berkowitz SA, Engen JR (2010) Posttranslational modifications differentially affect IgG1 conformation and receptor binding. Mol Cell Proteomics 9:1716-1728
    • (2010) Mol Cell Proteomics , vol.9 , pp. 1716-1728
    • Houde, D.1    Peng, Y.2    Berkowitz, S.A.3    Engen, J.R.4
  • 59
    • 33646172632 scopus 로고    scopus 로고
    • Thecarbohydrate at FcγRIIIa Asn-162: An element required for high affinity binding to non-fucosylated IgG glycoforms
    • Ferrara C, Stuart F, Sondermann P, Brünker P, Umaña P (2006) Thecarbohydrate at FcγRIIIa Asn-162: an element required for high affinity binding to non-fucosylated IgG glycoforms. J Biol Chem 281:5032-5036
    • (2006) J Biol Chem , vol.281 , pp. 5032-5036
    • Ferrara, C.1    Stuart, F.2    Sondermann, P.3    Brünker, P.4    Umaña, P.5
  • 61
    • 84863470971 scopus 로고    scopus 로고
    • Marketing approval of mogamulizumab: A triumph for glyco-engineering, mAbs
    • 1012
    • Beck A, Reichert JM (1012) Marketing approval of mogamulizumab: a triumph for glyco-engineering, mAbs. Landes Bioscience: pp 419-425
    • Landes Bioscience , pp. 419-425
    • Beck, A.1    Reichert, J.M.2
  • 62
    • 0028962403 scopus 로고
    • Glycosylation changes of IgG associated with rheumatoid arthritis can activate complement via the mannose-binding protein
    • Malhotra R, Wormald MR, Rudd PM, Fischer PB, Dwek RA, Sim RB (1995) Glycosylation changes of IgG associated with rheumatoid arthritis can activate complement via the mannose-binding protein. Nat Med 1:237-243
    • (1995) Nat Med , vol.1 , pp. 237-243
    • Malhotra, R.1    Wormald, M.R.2    Rudd, P.M.3    Fischer, P.B.4    Dwek, R.A.5    Sim, R.B.6
  • 65
    • 0029962752 scopus 로고    scopus 로고
    • Site-specific glycosylation of human immunoglobulin G is altered in four rheumatoid arthritis patients
    • Youings A, Chang SC, Dwek RA, Scragg IG (1996) Site-specific glycosylation of human immunoglobulin G is altered in four rheumatoid arthritis patients. Biochem J 314(Pt 2):621-630
    • (1996) Biochem J , vol.314 , pp. 621-630
    • Youings, A.1    Chang, S.C.2    Dwek, R.A.3    Scragg, I.G.4
  • 68
    • 33746888249 scopus 로고    scopus 로고
    • Anti-inflammatory activity of immunoglobulin G resulting from Fc sialylation
    • Kaneko Y, Nimmerjahn F, Ravetch JV (2006) Anti-inflammatory activity of immunoglobulin G resulting from Fc sialylation. Science 313:670-673
    • (2006) Science , vol.313 , pp. 670-673
    • Kaneko, Y.1    Nimmerjahn, F.2    Ravetch, J.V.3
  • 69
    • 34347235526 scopus 로고    scopus 로고
    • Agalactosylated IgG antibodies depend on cellular Fc receptors for in vivo activity
    • Nimmerjahn F, Anthony RM, Ravetch JV (2007) Agalactosylated IgG antibodies depend on cellular Fc receptors for in vivo activity. Proc Natl Acad Sci U S A 104:8433-8437
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 8433-8437
    • Nimmerjahn, F.1    Anthony, R.M.2    Ravetch, J.V.3
  • 70
    • 0034690723 scopus 로고    scopus 로고
    • Effects of ammonia on CHO cell growth, erythropoietin production, and glycosylation
    • YangM, ButlerM(2000) Effects of ammonia on CHO cell growth, erythropoietin production, and glycosylation. Biotechnol Bioeng 68:370-380
    • (2000) Biotechnol Bioeng , vol.68 , pp. 370-380
    • Yang, M.1    Butler, M.2
  • 71
    • 0034691229 scopus 로고    scopus 로고
    • Ammonium alters N-glycan structures of recombinant TNFR-IgG: Degradative versus biosynthetic mechanisms
    • Gawlitzek M, Ryll T, Lofgren J, Sliwkowski MB (2000) Ammonium alters N-glycan structures of recombinant TNFR-IgG: degradative versus biosynthetic mechanisms. Biotechnol Bioeng 68:637-646
    • (2000) Biotechnol Bioeng , vol.68 , pp. 637-646
    • Gawlitzek, M.1    Ryll, T.2    Lofgren, J.3    Sliwkowski, M.B.4
  • 72
    • 77953666582 scopus 로고    scopus 로고
    • Differences in N-glycan structures found on recombinant IgA1 and IgA2 produced in murine myeloma and CHO cell lines
    • Yoo EM, Yu LJ, Wims LA, Goldberg D, Morrison SL (2010) Differences in N-glycan structures found on recombinant IgA1 and IgA2 produced in murine myeloma and CHO cell lines. MAbs 2:320-334
    • (2010) MAbs , vol.2 , pp. 320-334
    • Yoo, E.M.1    Yu, L.J.2    Wims, L.A.3    Goldberg, D.4    Morrison, S.L.5
  • 73
    • 0022260876 scopus 로고
    • Human natural anti-α-galactosyl IgG. II. The specific recognition of alpha (1-3)-linked galactose residues
    • Galili U, Macher BA, Buehler J, Shohet SB (1985) Human natural anti-α-galactosyl IgG. II. The specific recognition of alpha (1-3)-linked galactose residues. J Exp Med 162:573-582
    • (1985) J Exp Med , vol.162 , pp. 573-582
    • Galili, U.1    Macher, B.A.2    Buehler, J.3    Shohet, S.B.4
  • 74
    • 0021678856 scopus 로고
    • A unique natural human IgG antibody with anti-α-galactosyl specificity
    • Galili U, Rachmilewitz EA, Peleg A, Flechner I (1984) A unique natural human IgG antibody with anti-α-galactosyl specificity. J Exp Med 160:1519-1531
    • (1984) J Exp Med , vol.160 , pp. 1519-1531
    • Galili, U.1    Rachmilewitz, E.A.2    Peleg, A.3    Flechner, I.4
  • 75
    • 0024306541 scopus 로고
    • Reactivity of human anti-α-galactosyl IgG antibody with α(1-> 3)-linked galactosyl epitopes exposed on basement membranes and on glomerular epithelial cells: An in vitro and in vivo study in the mouse
    • Vecchi ML, Davin JC, Castronovo V, Foidart JM, Malaise M, Foidart JB, Dechene C, Sangiorgi GB, Mahieu P (1989) Reactivity of human anti-α-galactosyl IgG antibody with α(1-> 3)-linked galactosyl epitopes exposed on basement membranes and on glomerular epithelial cells: an in vitro and in vivo study in the mouse. Clin Exp Immunol 78:271-277
    • (1989) Clin Exp Immunol , vol.78 , pp. 271-277
    • Vecchi, M.L.1    Davin, J.C.2    Castronovo, V.3    Foidart, J.M.4    Malaise, M.5    Foidart, J.B.6    Dechene, C.7    Sangiorgi, G.B.8    Mahieu, P.9
  • 76
    • 79953646035 scopus 로고    scopus 로고
    • Impaired allergy diagnostics among parasite-infected patients caused by IgE antibodies to the carbohydrate epitope galactose-α1, 3-galactose
    • Arkestal K, Sibanda E, Thors C, Troye-Blomberg M, Mduluza T, Valenta R, Gronlund H, van Hage M (2011) Impaired allergy diagnostics among parasite-infected patients caused by IgE antibodies to the carbohydrate epitope galactose-α1, 3-galactose. J Allergy Clin Immunol 127:1024-1028
    • (2011) J Allergy Clin Immunol , vol.127 , pp. 1024-1028
    • Arkestal, K.1    Sibanda, E.2    Thors, C.3    Troye-Blomberg, M.4    Mduluza, T.5    Valenta, R.6    Gronlund, H.7    Van Hage, M.8
  • 80
    • 0037384789 scopus 로고    scopus 로고
    • Darbepoetin-α has a longer circulating half-life and greater in vivo potency than recombinant human erythropoietin
    • Egrie JC, Dwyer E, Browne JK, Hitz A, Lykos MA (2003) Darbepoetin-α has a longer circulating half-life and greater in vivo potency than recombinant human erythropoietin. Exp Hematol 31: 290-299
    • (2003) Exp Hematol , vol.31 , pp. 290-299
    • Egrie, J.C.1    Dwyer, E.2    Browne, J.K.3    Hitz, A.4    Lykos, M.A.5
  • 81
    • 77956873702 scopus 로고    scopus 로고
    • Pharmacokinetic, pharmacodynamic, and immunogenicity comparability assessment strategies for monoclonal antibodies
    • Putnam WS, Prabhu S, Zheng Y, Subramanyam M, Wang YM (2010) Pharmacokinetic, pharmacodynamic, and immunogenicity comparability assessment strategies for monoclonal antibodies. Trends Biotechnol 28:509-516
    • (2010) Trends Biotechnol , vol.28 , pp. 509-516
    • Putnam, W.S.1    Prabhu, S.2    Zheng, Y.3    Subramanyam, M.4    Wang, Y.M.5
  • 82
    • 53049100695 scopus 로고    scopus 로고
    • Diversity in specificity, abundance, and composition of anti-Neu5Gc antibodies in normal humans: Potential implications for disease
    • Padler-Karavani V, Yu H, Cao H, Chokhawala H, Karp F, Varki N, Chen X, Varki A (2008) Diversity in specificity, abundance, and composition of anti-Neu5Gc antibodies in normal humans: potential implications for disease. Glycobiology 18:818-830
    • (2008) Glycobiology , vol.18 , pp. 818-830
    • Padler-Karavani, V.1    Yu, H.2    Cao, H.3    Chokhawala, H.4    Karp, F.5    Varki, N.6    Chen, X.7    Varki, A.8
  • 83
    • 0034281427 scopus 로고    scopus 로고
    • Effect of ammonia on the glycosylation of human recombinant erythropoietin in culture
    • YangM, ButlerM(2000) Effect of ammonia on the glycosylation of human recombinant erythropoietin in culture. Biotechnol Prog 16: 751-759
    • (2000) Biotechnol Prog , vol.16 , pp. 751-759
    • Yang, M.1    Butler, M.2
  • 84
    • 14744285958 scopus 로고
    • Culture pH affects expression rates and glycosylation of recombinant mouse placental lactogen proteins by Chinese hamster ovary (CHO) cells
    • Borys MC, Linzer DI, Papoutsakis ET (1993) Culture pH affects expression rates and glycosylation of recombinant mouse placental lactogen proteins by Chinese hamster ovary (CHO) cells. Biotechnology (NY) 11:720-724
    • (1993) Biotechnology (NY) , vol.11 , pp. 720-724
    • Borys, M.C.1    Linzer, D.I.2    Papoutsakis, E.T.3
  • 85
    • 77953618368 scopus 로고    scopus 로고
    • Naturally occurring glycan forms of human immunoglobulins G1 and G2
    • Flynn GC, Chen X, Liu YD, Shah B, Zhang Z (2010) Naturally occurring glycan forms of human immunoglobulins G1 and G2. Mol Immunol 47:2074-2082
    • (2010) Mol Immunol , vol.47 , pp. 2074-2082
    • Flynn, G.C.1    Chen, X.2    Liu, Y.D.3    Shah, B.4    Zhang, Z.5
  • 86
    • 79958837668 scopus 로고    scopus 로고
    • High-mannose glycans on the Fc region of therapeutic IgG antibodies increase serum clearance in humans
    • Goetze AM, Liu YD, Zhang Z, Shah B, Lee E, Bondarenko PV, Flynn GC (2011) High-mannose glycans on the Fc region of therapeutic IgG antibodies increase serum clearance in humans. Glycobiology 21:949-959
    • (2011) Glycobiology , vol.21 , pp. 949-959
    • Goetze, A.M.1    Liu, Y.D.2    Zhang, Z.3    Shah, B.4    Lee, E.5    Bondarenko, P.V.6    Flynn, G.C.7
  • 87
    • 58949086663 scopus 로고    scopus 로고
    • The effect of Fc glycan forms on human IgG2 antibody clearance in humans
    • Chen X, LiuYD, Flynn GC (2009) The effect of Fc glycan forms on human IgG2 antibody clearance in humans. Glycobiology 19:240-249
    • (2009) Glycobiology , vol.19 , pp. 240-249
    • Chen, X.1    Liu, Y.D.2    Flynn, G.C.3
  • 88
    • 38449115463 scopus 로고    scopus 로고
    • Development of a simple and rapid method for producing non-fucosylated oligomannose containing antibodies with increased effector function
    • Zhou Q, Shankara S, Roy A, Qiu H, Estes S, McVie-Wylie A, Culm-Merdek K, Park A, Pan C, Edmunds T (2008) Development of a simple and rapid method for producing non-fucosylated oligomannose containing antibodies with increased effector function. Biotechnol Bioeng 99:652-665
    • (2008) Biotechnol Bioeng , vol.99 , pp. 652-665
    • Zhou, Q.1    Shankara, S.2    Roy, A.3    Qiu, H.4    Estes, S.5    McVie-Wylie, A.6    Culm-Merdek, K.7    Park, A.8    Pan, C.9    Edmunds, T.10
  • 89
    • 80051798475 scopus 로고    scopus 로고
    • Effects of cell culture conditions on antibody N-linked glycosylation-what affects high mannose 5 glycoform
    • Pacis E, Yu M, Autsen J, Bayer R, Li F (2011) Effects of cell culture conditions on antibody N-linked glycosylation-what affects high mannose 5 glycoform. Biotechnol Bioeng 108(10):2348-2358
    • (2011) Biotechnol Bioeng , vol.108 , Issue.10 , pp. 2348-2358
    • Pacis, E.1    Yu, M.2    Autsen, J.3    Bayer, R.4    Li, F.5
  • 90
    • 0035921175 scopus 로고    scopus 로고
    • Expression of GnTIII in a recombinant anti-CD20 CHO production cell line: Expression of antibodies with altered glycoforms leads to an increase in ADCC through higher affinity for FCγRIII
    • Davies J, Jiang L, Pan L-Z, LaBarre MJ, Anderson D, Reff M (2001) Expression of GnTIII in a recombinant anti-CD20 CHO production cell line: expression of antibodies with altered glycoforms leads to an increase in ADCC through higher affinity for FCγRIII. Biotechnol Bioeng 74:288-294
    • (2001) Biotechnol Bioeng , vol.74 , pp. 288-294
    • Davies, J.1    Jiang, L.2    Pan, L.-Z.3    Labarre, M.J.4    Anderson, D.5    Reff, M.6
  • 91
    • 0021749885 scopus 로고
    • A dominant mutation to ricin resistance in Chinese hamster ovary cells induces UDP-GlcNAc:glycopeptide beta-4-N-acetylglucosaminyltransferase III activity
    • Campbell C, Stanley P (1984) A dominant mutation to ricin resistance in Chinese hamster ovary cells induces UDP-GlcNAc:glycopeptide beta-4-N-acetylglucosaminyltransferase III activity. J Biol Chem 259:13370-13378
    • (1984) J Biol Chem , vol.259 , pp. 13370-13378
    • Campbell, C.1    Stanley, P.2
  • 92
  • 94
    • 79960137705 scopus 로고    scopus 로고
    • Isolation and characterization of therapeutic antibody charge variants using cation exchange displacement chromatography
    • Zhang T, Bourret J, Cano T (2011) Isolation and characterization of therapeutic antibody charge variants using cation exchange displacement chromatography. J Chromatogr A 1218:5079-5086
    • (2011) J Chromatogr A , vol.1218 , pp. 5079-5086
    • Zhang, T.1    Bourret, J.2    Cano, T.3
  • 96
    • 84881369909 scopus 로고    scopus 로고
    • Topdown MS for rapid methionine oxidation site assignment in filgrastim
    • Holzmann J, Hausberger A, Rupprechter A, Toll H (2013) Topdown MS for rapid methionine oxidation site assignment in filgrastim. Anal Bioanal Chem 405:6667-6674
    • (2013) Anal Bioanal Chem , vol.405 , pp. 6667-6674
    • Holzmann, J.1    Hausberger, A.2    Rupprechter, A.3    Toll, H.4
  • 97
    • 64549163344 scopus 로고    scopus 로고
    • Mass spectrometric analysis of innovator, counterfeit, and follow-on recombinant human growth hormone
    • Jiang H, Wu SL, Karger BL, Hancock WS (2009) Mass spectrometric analysis of innovator, counterfeit, and follow-on recombinant human growth hormone. Biotechnol Prog 25:207-218
    • (2009) Biotechnol Prog , vol.25 , pp. 207-218
    • Jiang, H.1    Wu, S.L.2    Karger, B.L.3    Hancock, W.S.4
  • 98
    • 33750910358 scopus 로고    scopus 로고
    • Changes in avidity and specificity of IgG during electro-oxidation Relevance of binding of antibodies to β2-GPI
    • Božič B, Čučnik S, Kveder T, Rozman B (2006) Changes in avidity and specificity of IgG during electro-oxidation. Relevance of binding of antibodies to β2-GPI. Autoimmun Rev 6:28-32
    • (2006) Autoimmun Rev , vol.6 , pp. 28-32
    • Božič, B.1    Čučnik, S.2    Kveder, T.3    Rozman, B.4
  • 101
    • 34848814407 scopus 로고    scopus 로고
    • Structural effect of deglycosylation and methionine oxidation on a recombinant monoclonal antibody
    • Liu H, Gaza-Bulseco G, Xiang T, Chumsae C (2008) Structural effect of deglycosylation and methionine oxidation on a recombinant monoclonal antibody. Mol Immunol 45:701-708
    • (2008) Mol Immunol , vol.45 , pp. 701-708
    • Liu, H.1    Gaza-Bulseco, G.2    Xiang, T.3    Chumsae, C.4
  • 102
    • 77950236865 scopus 로고    scopus 로고
    • Conformational changes in oxidatively stressed monoclonal antibodies studied by hydrogen exchange mass spectrometry
    • Burkitt W, Domann P, O'Connor G (2010) Conformational changes in oxidatively stressed monoclonal antibodies studied by hydrogen exchange mass spectrometry. Protein Sci 19:826-835
    • (2010) Protein Sci , vol.19 , pp. 826-835
    • Burkitt, W.1    Domann, P.2    O'Connor, G.3
  • 103
    • 59949104434 scopus 로고    scopus 로고
    • Methionine oxidation in human IgG2 Fc decreases binding affinities to protein A and FcRn
    • Pan H, Chen K, Chu L, Kinderman F, Apostol I, Huang G (2009) Methionine oxidation in human IgG2 Fc decreases binding affinities to protein A and FcRn. Protein Sci 18:424-433
    • (2009) Protein Sci , vol.18 , pp. 424-433
    • Pan, H.1    Chen, K.2    Chu, L.3    Kinderman, F.4    Apostol, I.5    Huang, G.6
  • 104
    • 45849089529 scopus 로고    scopus 로고
    • Effect of methionine oxidation of a recombinant monoclonal antibody on the binding affinity to protein A and protein G
    • Gaza-Bulseco G, Faldu S, Hurkmans K, Chumsae C, Liu H (2008) Effect of methionine oxidation of a recombinant monoclonal antibody on the binding affinity to protein A and protein G. J Chromatogr B Anal Technol Biomed Life Sci 870:55-62
    • (2008) J Chromatogr B Anal Technol Biomed Life Sci , vol.870 , pp. 55-62
    • Gaza-Bulseco, G.1    Faldu, S.2    Hurkmans, K.3    Chumsae, C.4    Liu, H.5
  • 105
    • 33749057744 scopus 로고    scopus 로고
    • Protein aggregation and bioprocessing
    • Cromwell ME, Hilario E, Jacobson F (2006) Protein aggregation and bioprocessing. AAPS J 8:E572-E579
    • (2006) AAPS J , vol.8 , pp. E572-E579
    • Cromwell, M.E.1    Hilario, E.2    Jacobson, F.3
  • 107
    • 85027940300 scopus 로고    scopus 로고
    • Characterization of therapeutic monoclonal antibodies reveals differences between in vitro and in vivo time-course studies
    • Yin S, Pastuskovas C, Khawli L, Stults J (2013) Characterization of therapeutic monoclonal antibodies reveals differences between in vitro and in vivo time-course studies. Pharm Res 30:167-178
    • (2013) Pharm Res , vol.30 , pp. 167-178
    • Yin, S.1    Pastuskovas, C.2    Khawli, L.3    Stults, J.4
  • 108
    • 34247346055 scopus 로고    scopus 로고
    • Comparison of methionine oxidation in thermal stability and chemically stressed samples of a fully human monoclonal antibody
    • Chumsae C, Gaza-Bulseco G, Sun J, Liu H (2007) Comparison of methionine oxidation in thermal stability and chemically stressed samples of a fully human monoclonal antibody. J Chromatogr B Anal Technol Biomed Life Sci 850:285-294
    • (2007) J Chromatogr B Anal Technol Biomed Life Sci , vol.850 , pp. 285-294
    • Chumsae, C.1    Gaza-Bulseco, G.2    Sun, J.3    Liu, H.4
  • 109
    • 60649093469 scopus 로고    scopus 로고
    • Mass spectrometry analysis of photo-induced methionine oxidation of a recombinant human monoclonal antibody
    • Liu H, Gaza-Bulseco G, Zhou L (2009) Mass spectrometry analysis of photo-induced methionine oxidation of a recombinant human monoclonal antibody. J Am Soc Mass Spectrom 20:525-528
    • (2009) J Am Soc Mass Spectrom , vol.20 , pp. 525-528
    • Liu, H.1    Gaza-Bulseco, G.2    Zhou, L.3
  • 110
    • 60849102492 scopus 로고    scopus 로고
    • Heterogeneity of monoclonal antibodies revealed by charge-sensitive methods
    • Vlasak J, Ionescu R (2008) Heterogeneity of monoclonal antibodies revealed by charge-sensitive methods. Curr Pharm Biotechnol 9: 468-481
    • (2008) Curr Pharm Biotechnol , vol.9 , pp. 468-481
    • Vlasak, J.1    Ionescu, R.2
  • 111
    • 84893821087 scopus 로고    scopus 로고
    • Accurate identification of deamidated peptides in global proteomics using a quadrupole orbitrap mass spectrometer
    • Nepomuceno AI, Gibson RJ, Randall SM, Muddiman DC (2014) Accurate identification of deamidated peptides in global proteomics using a quadrupole orbitrap mass spectrometer. J Proteome Res 13: 777-785
    • (2014) J Proteome Res , vol.13 , pp. 777-785
    • Nepomuceno, A.I.1    Gibson, R.J.2    Randall, S.M.3    Muddiman, D.C.4
  • 113
    • 24944512327 scopus 로고    scopus 로고
    • Identification and characterization of deamidation sites in the conserved regions of human immunoglobulin-γ antibodies
    • Chelius D, Rehder DS, Bondarenko PV (2005) Identification and characterization of deamidation sites in the conserved regions of human immunoglobulin-γ antibodies. Anal Chem 77:6004-6011
    • (2005) Anal Chem , vol.77 , pp. 6004-6011
    • Chelius, D.1    Rehder, D.S.2    Bondarenko, P.V.3
  • 114
    • 46349085153 scopus 로고    scopus 로고
    • Post-translational modifications of recombinant proteins: Significance for biopharmaceuticals
    • Jenkins N, Murphy L, Tyther R (2008) Post-translational modifications of recombinant proteins: significance for biopharmaceuticals. Mol Biotechnol 39:113-118
    • (2008) Mol Biotechnol , vol.39 , pp. 113-118
    • Jenkins, N.1    Murphy, L.2    Tyther, R.3
  • 115
    • 69649088633 scopus 로고    scopus 로고
    • Human antibody Fc deamidation in vivo
    • Liu YD, van Enk JZ, Flynn GC (2009) Human antibody Fc deamidation in vivo. Biologicals 37:313-322
    • (2009) Biologicals , vol.37 , pp. 313-322
    • Liu, Y.D.1    Van Enk, J.Z.2    Flynn, G.C.3
  • 117
    • 77958584087 scopus 로고    scopus 로고
    • Assessing monoclonal antibody product quality attribute criticality through clinical studies
    • Goetze AM, Schenauer MR, Flynn GC (2010) Assessing monoclonal antibody product quality attribute criticality through clinical studies. MAbs 2:500-507
    • (2010) MAbs , vol.2 , pp. 500-507
    • Goetze, A.M.1    Schenauer, M.R.2    Flynn, G.C.3
  • 118
    • 84863045993 scopus 로고    scopus 로고
    • Disulfide bond structures of IgG molecules: Structural variations, chemical modifications, and possible impacts to stability and biological function
    • Liu H, May K (2012) Disulfide bond structures of IgG molecules: structural variations, chemical modifications, and possible impacts to stability and biological function. MAbs 4:17-23
    • (2012) MAbs , vol.4 , pp. 17-23
    • Liu, H.1    May, K.2
  • 121
    • 0036901746 scopus 로고    scopus 로고
    • Complete disulfide bond assignment of a recombinant immunoglobulin G4 monoclonal antibody
    • Zhang W, Marzilli LA, Rouse JC, Czupryn MJ (2002) Complete disulfide bond assignment of a recombinant immunoglobulin G4 monoclonal antibody. Anal Biochem 311:1-9
    • (2002) Anal Biochem , vol.311 , pp. 1-9
    • Zhang, W.1    Marzilli, L.A.2    Rouse, J.C.3    Czupryn, M.J.4
  • 122
    • 33644619972 scopus 로고    scopus 로고
    • Heterogeneity of recombinant antibodies: Linking structure to function
    • Harris RJ (2005) Heterogeneity of recombinant antibodies: linking structure to function. Dev Biol (Basel) 122:117-127
    • (2005) Dev Biol (Basel) , vol.122 , pp. 117-127
    • Harris, R.J.1
  • 126
    • 77449115254 scopus 로고    scopus 로고
    • Protein disulfide isomerase does not control recombinant IgG4 productivity in mammalian cell lines
    • Hayes NV, Smales CM, Klappa P (2010) Protein disulfide isomerase does not control recombinant IgG4 productivity in mammalian cell lines. Biotechnol Bioeng 105:770-779
    • (2010) Biotechnol Bioeng , vol.105 , pp. 770-779
    • Hayes, N.V.1    Smales, C.M.2    Klappa, P.3
  • 128
    • 0034905149 scopus 로고    scopus 로고
    • The interheavy chain disulfide bonds of IgG4 are in equilibrium with intrachain disulfide bonds
    • Schuurman J, Perdok GJ, Gorter AD, Aalberse RC (2001) The interheavy chain disulfide bonds of IgG4 are in equilibrium with intrachain disulfide bonds. Mol Immunol 38:1-8
    • (2001) Mol Immunol , vol.38 , pp. 1-8
    • Schuurman, J.1    Perdok, G.J.2    Gorter, A.D.3    Aalberse, R.C.4
  • 132
    • 84863795910 scopus 로고    scopus 로고
    • Engineering an improved IgG4 molecule with reduced disulfide bond heterogeneity and increased Fab domain thermal stability
    • Peters SJ, Smales CM, Henry AJ, Stephens PE, West S, Humphreys DP (2012) Engineering an improved IgG4 molecule with reduced disulfide bond heterogeneity and increased Fab domain thermal stability. J Biol Chem 287:24525-24533
    • (2012) J Biol Chem , vol.287 , pp. 24525-24533
    • Peters, S.J.1    Smales, C.M.2    Henry, A.J.3    Stephens, P.E.4    West, S.5    Humphreys, D.P.6
  • 134
    • 68049084746 scopus 로고    scopus 로고
    • Evidence for trisulfide bonds in a recombinant variant of a human IgG2 monoclonal antibody
    • Pristatsky P, Cohen SL, Krantz D, Acevedo J, Ionescu R, Vlasak J (2009) Evidence for trisulfide bonds in a recombinant variant of a human IgG2 monoclonal antibody. Anal Chem 81:6148-6155
    • (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
  • 136
    • 34250182367 scopus 로고    scopus 로고
    • Beta-elimination and peptide bond hydrolysis: Two distinct mechanisms of human IgG1 hinge fragmentation upon storage
    • Cohen SL, Price C, Vlasak J (2007) Beta-elimination and peptide bond hydrolysis: two distinct mechanisms of human IgG1 hinge fragmentation upon storage. J Am Chem Soc 129:6976-6977
    • (2007) J Am Chem Soc , vol.129 , pp. 6976-6977
    • Cohen, S.L.1    Price, C.2    Vlasak, J.3
  • 139
    • 77956355090 scopus 로고    scopus 로고
    • Increased aggregation propensity of IgG2 subclass over IgG1: Role of conformational changes and covalent character in isolated aggregates
    • Franey H, Brych SR, Kolvenbach CG, Rajan RS (2010) Increased aggregation propensity of IgG2 subclass over IgG1: role of conformational changes and covalent character in isolated aggregates. Protein Sci 19:1601-1615
    • (2010) Protein Sci , vol.19 , pp. 1601-1615
    • Franey, H.1    Brych, S.R.2    Kolvenbach, C.G.3    Rajan, R.S.4
  • 140
    • 51249120701 scopus 로고    scopus 로고
    • Free sulfhydryl measurement as an indicator of antibody stability
    • Lacy ER, Baker M, Brigham-Burke M (2008) Free sulfhydryl measurement as an indicator of antibody stability. Anal Biochem 382:66-68
    • (2008) Anal Biochem , vol.382 , pp. 66-68
    • Lacy, E.R.1    Baker, M.2    Brigham-Burke, M.3
  • 141
    • 34047270107 scopus 로고    scopus 로고
    • A role for protein misfolding in immunogenicity of biopharmaceuticals
    • Maas C, Hermeling S, Bouma B, Jiskoot W, Gebbink MFBG (2007) A role for protein misfolding in immunogenicity of biopharmaceuticals. J Biol Chem 282:2229-2236
    • (2007) J Biol Chem , vol.282 , pp. 2229-2236
    • Maas, C.1    Hermeling, S.2    Bouma, B.3    Jiskoot, W.4    Gebbink, M.F.B.G.5
  • 142
    • 33846910013 scopus 로고    scopus 로고
    • Immunoglobulin glycation with fructose: A comparative study
    • Jairajpuri DS, Fatima S, Saleemuddin M (2007) Immunoglobulin glycation with fructose: a comparative study. Clin Chim Acta 378: 86-92
    • (2007) Clin Chim Acta , vol.378 , pp. 86-92
    • Jairajpuri, D.S.1    Fatima, S.2    Saleemuddin, M.3
  • 143
    • 37749041309 scopus 로고    scopus 로고
    • A study in glycation of a therapeutic recombinant humanized monoclonal antibody: Where it is, how it got there, and how it affects charge-based behavior
    • Quan C, Alcala E, Petkovska I, Matthews D, Canova-Davis E, Taticek R, Ma S (2008) A study in glycation of a therapeutic recombinant humanized monoclonal antibody: where it is, how it got there, and how it affects charge-based behavior. Anal Biochem 373:179-191
    • (2008) Anal Biochem , vol.373 , pp. 179-191
    • Quan, C.1    Alcala, E.2    Petkovska, I.3    Matthews, D.4    Canova-Davis, E.5    Taticek, R.6    Ma, S.7
  • 145
    • 0025732948 scopus 로고
    • Role of oxidative stress in development of complications in diabetes
    • Baynes JW (1991) Role of oxidative stress in development of complications in diabetes. Diabetes 40:405-412
    • (1991) Diabetes , vol.40 , pp. 405-412
    • Baynes, J.W.1
  • 146
    • 20044376702 scopus 로고    scopus 로고
    • The pathobiology of diabetic complications: A unifying mechanism
    • Brownlee M (2005) The pathobiology of diabetic complications: a unifying mechanism. Diabetes 54:1615-1625
    • (2005) Diabetes , vol.54 , pp. 1615-1625
    • Brownlee, M.1
  • 147
    • 0034294932 scopus 로고    scopus 로고
    • Glycation as the glucose link to diabetic complications
    • Gugliucci A (2000) Glycation as the glucose link to diabetic complications. J Am Osteopath Assoc 100:621-634
    • (2000) J Am Osteopath Assoc , vol.100 , pp. 621-634
    • Gugliucci, A.1
  • 148
    • 79951973231 scopus 로고    scopus 로고
    • Advanced glycation end-products damaged IgG, a target for circulating autoantibodies in patients with type 1 diabetes mellitus
    • Rasheed Z, Kumar L, Abbas S, Prasad I, Ansari N, Ahmad R (2009) Advanced glycation end-products damaged IgG, a target for circulating autoantibodies in patients with type 1 diabetes mellitus. Open Glycosci 2:1-8
    • (2009) Open Glycosci , vol.2 , pp. 1-8
    • Rasheed, Z.1    Kumar, L.2    Abbas, S.3    Prasad, I.4    Ansari, N.5    Ahmad, R.6
  • 150
    • 84870860517 scopus 로고    scopus 로고
    • Preferential recognition of epitopes on AGE-IgG by the autoantibodies in rheumatoid arthritis patients
    • Ahmad S, Habib S, Moinuddin, Ali A (2013) Preferential recognition of epitopes on AGE-IgG by the autoantibodies in rheumatoid arthritis patients. Hum Immunol 74:23-27
    • (2013) Hum Immunol , vol.74 , pp. 23-27
    • Ahmad, S.1    Habib, S.2    Moinuddin Ali, A.3
  • 151
    • 48249103154 scopus 로고    scopus 로고
    • Advanced glycation end products induce in vitro cross-linking of alpha-synuclein and accelerate the process of intracellular inclusion body formation
    • Shaikh S, Nicholson LF (2008) Advanced glycation end products induce in vitro cross-linking of alpha-synuclein and accelerate the process of intracellular inclusion body formation. J Neurosci Res 86:2071-2082
    • (2008) J Neurosci Res , vol.86 , pp. 2071-2082
    • Shaikh, S.1    Nicholson, L.F.2
  • 152
    • 0027960596 scopus 로고
    • Glycation of monoclonal antibodies impairs their ability to bind antigen
    • Kennedy DM, Skillen AW, Self CH (1994) Glycation of monoclonal antibodies impairs their ability to bind antigen. Clin Exp Immunol 98:245-251
    • (1994) Clin Exp Immunol , vol.98 , pp. 245-251
    • Kennedy, D.M.1    Skillen, A.W.2    Self, C.H.3
  • 153
    • 50349097199 scopus 로고    scopus 로고
    • Glycation during storage and administration of monoclonal antibody formulations
    • Fischer S, Hoernschemeyer J, Mahler H-C (2008) Glycation during storage and administration of monoclonal antibody formulations. Eur J Pharm Biopharm 70:42-50
    • (2008) Eur J Pharm Biopharm , vol.70 , pp. 42-50
    • Fischer, S.1    Hoernschemeyer, J.2    Mahler, H.-C.3
  • 157
    • 0025003795 scopus 로고
    • Effect of nonenzymatic glycation on the structure of immunoglobulin G
    • Dolhofer-Bliesener R, Gerbitz KD (1990) Effect of nonenzymatic glycation on the structure of immunoglobulin G. Biol Chem Hoppe Seyler 371:693-697
    • (1990) Biol Chem Hoppe Seyler , vol.371 , pp. 693-697
    • Dolhofer-Bliesener, R.1    Gerbitz, K.D.2
  • 158
    • 0024382985 scopus 로고
    • Nonenzymic glycation of human immunoglobulins does not impair their immunoreactivity
    • Morin LG, Austin GE, Rodey GE, Johnson JE (1989) Nonenzymic glycation of human immunoglobulins does not impair their immunoreactivity. Clin Chem 35:1039-1042
    • (1989) Clin Chem , vol.35 , pp. 1039-1042
    • Morin, L.G.1    Austin, G.E.2    Rodey, G.E.3    Johnson, J.E.4
  • 159
    • 0021838201 scopus 로고
    • Nonenzymatic glycation of immunoglobulins leads to an impairment of immunoreactivity
    • Dolhofer R, Siess EA, Wieland OH (1985) Nonenzymatic glycation of immunoglobulins leads to an impairment of immunoreactivity. Biol Chem Hoppe Seyler 366:361-366
    • (1985) Biol Chem Hoppe Seyler , vol.366 , pp. 361-366
    • Dolhofer, R.1    Siess, E.A.2    Wieland, O.H.3
  • 160
    • 84863311029 scopus 로고    scopus 로고
    • Immunological studies on glycated human IgG
    • Moinuddin AS, Ali A (2012) Immunological studies on glycated human IgG. Life Sci 90:980-987
    • (2012) Life Sci , vol.90 , pp. 980-987
    • Moinuddin, A.S.1    Ali, A.2
  • 161
    • 84877697551 scopus 로고    scopus 로고
    • Multispecificity of immunoglobulin M Antibodies raised against advanced glycation end products: Involvement of electronegative potential of antigens
    • Chikazawa M, Otaki N, Shibata T, Miyashita H, Kawai Y, Maruyama S, Toyokuni S, Kitaura Y, Matsuda T, Uchida K (2013) Multispecificity of immunoglobulin M Antibodies raised against advanced glycation end products: involvement of electronegative potential of antigens. J Biol Chem 288:13204-13214
    • (2013) J Biol Chem , vol.288 , pp. 13204-13214
    • Chikazawa, M.1    Otaki, N.2    Shibata, T.3    Miyashita, H.4    Kawai, Y.5    Maruyama, S.6    Toyokuni, S.7    Kitaura, Y.8    Matsuda, T.9    Uchida, K.10
  • 162
    • 84855882002 scopus 로고    scopus 로고
    • Physicochemical studies on glycation-induced structural changes in human IgG
    • Moinuddin AS, Khan RH, Ali A (2012) Physicochemical studies on glycation-induced structural changes in human IgG. IUBMB Life 64:151-156
    • (2012) IUBMB Life , vol.64 , pp. 151-156
    • Moinuddin, A.S.1    Khan, R.H.2    Ali, A.3
  • 163
    • 84862212634 scopus 로고    scopus 로고
    • Quality attributes of recombinant therapeutic proteins: An assessment of impact on safety and efficacy as part of a quality by design development approach
    • Eon-Duval A, Broly H, Gleixner R (2012) Quality attributes of recombinant therapeutic proteins: an assessment of impact on safety and efficacy as part of a quality by design development approach. Biotechnol Prog 28:608-622
    • (2012) Biotechnol Prog , vol.28 , pp. 608-622
    • Eon-Duval, A.1    Broly, H.2    Gleixner, R.3
  • 164
    • 84861842454 scopus 로고    scopus 로고
    • Biosimilar, biobetter, and next generation antibody characterization by mass spectrometry
    • Beck A, Sanglier-Cianferani S, Van DorsselaerA (2012) Biosimilar, biobetter, and next generation antibody characterization by mass spectrometry. Anal Chem 84:4637-4646
    • (2012) Anal Chem , vol.84 , pp. 4637-4646
    • Beck, A.1    Sanglier-Cianferani, S.2    Van Dorsselaer, A.3
  • 166
    • 84876703111 scopus 로고    scopus 로고
    • Structural comparison of two anti-CD20 monoclonal antibody drug products using middle-down mass spectrometry
    • Wang B, Gucinski AC, Keire DA, Buhse LF, Boyne MT II (2013) Structural comparison of two anti-CD20 monoclonal antibody drug products using middle-down mass spectrometry. Analyst 138: 3058-3065
    • (2013) Analyst , vol.138 , pp. 3058-3065
    • Wang, B.1    Gucinski, A.C.2    Keire, D.A.3    Buhse, L.F.4    Boyne, M.T.5
  • 167
    • 29144436001 scopus 로고    scopus 로고
    • Analysis of recombinant monoclonal antibody isoforms by electrospray ionization mass spectrometry as a strategy for streamlining characterization of recombinant monoclonal antibody charge heterogeneity
    • Lyubarskaya Y, Houde D, Woodard J, Murphy D, Mhatre R (2006) Analysis of recombinant monoclonal antibody isoforms by electrospray ionization mass spectrometry as a strategy for streamlining characterization of recombinant monoclonal antibody charge heterogeneity. Anal Biochem 348:24-39
    • (2006) Anal Biochem , vol.348 , pp. 24-39
    • Lyubarskaya, Y.1    Houde, D.2    Woodard, J.3    Murphy, D.4    Mhatre, R.5
  • 169
    • 78650214185 scopus 로고    scopus 로고
    • C-terminal lysine processing of human immunoglobulin G2 heavy chain in vivo
    • Cai B, Pan H, Flynn GC (2011) C-terminal lysine processing of human immunoglobulin G2 heavy chain in vivo. Biotechnol Bioeng 108:404-412
    • (2011) Biotechnol Bioeng , vol.108 , pp. 404-412
    • Cai, B.1    Pan, H.2    Flynn, G.C.3
  • 170
    • 48649090322 scopus 로고    scopus 로고
    • Cterminal lysine variants in fully human monoclonal antibodies: Investigation of test methods and possible causes
    • Dick LW Jr, Qiu D, Mahon D, Adamo M, Cheng KC (2008) Cterminal lysine variants in fully human monoclonal antibodies: investigation of test methods and possible causes. Biotechnol Bioeng 100:1132-1143
    • (2008) Biotechnol Bioeng , vol.100 , pp. 1132-1143
    • Dick, L.W.1    Qiu, D.2    Mahon, D.3    Adamo, M.4    Cheng, K.C.5
  • 172
    • 84883208534 scopus 로고    scopus 로고
    • Quality assurance of monoclonal antibody pharmaceuticals based on their charge variants using microchip isoelectric focusing method
    • KinoshitaM, Nakatsuji Y, Suzuki S, Hayakawa T, Kakehi K (2013) Quality assurance of monoclonal antibody pharmaceuticals based on their charge variants using microchip isoelectric focusing method. J Chromatogr A 1309:76-83
    • (2013) J Chromatogr A , vol.1309 , pp. 76-83
    • Kinoshita, M.1    Nakatsuji, Y.2    Suzuki, S.3    Hayakawa, T.4    Kakehi, K.5
  • 173
    • 84875371804 scopus 로고    scopus 로고
    • Monoclonal antibody heterogeneity analysis and deamidation monitoring with high-performance cation-exchange chromatofocusing using simple, two component buffer systems
    • Kang X, Kutzko JP, Hayes ML, Frey DD (2013) Monoclonal antibody heterogeneity analysis and deamidation monitoring with high-performance cation-exchange chromatofocusing using simple, two component buffer systems. J Chromatogr A 1283:89-97
    • (2013) J Chromatogr A , vol.1283 , pp. 89-97
    • Kang, X.1    Kutzko, J.P.2    Hayes, M.L.3    Frey, D.D.4
  • 176
    • 29044447751 scopus 로고    scopus 로고
    • Reversed-phase liquid chromatography/mass spectrometry analysis of reduced monoclonal antibodies in pharmaceutics
    • Rehder DS, Dillon TM, Pipes GD, Bondarenko PV (2006) Reversed-phase liquid chromatography/mass spectrometry analysis of reduced monoclonal antibodies in pharmaceutics. J Chromatogr A 1102:164-175
    • (2006) J Chromatogr A , vol.1102 , pp. 164-175
    • Rehder, D.S.1    Dillon, T.M.2    Pipes, G.D.3    Bondarenko, P.V.4
  • 177
    • 79953231678 scopus 로고    scopus 로고
    • N-terminal glutamate to pyroglutamate conversion in vivo for human IgG2 antibodies
    • Liu YD, Goetze AM, Bass RB, Flynn GC (2011) N-terminal glutamate to pyroglutamate conversion in vivo for human IgG2 antibodies. J Biol Chem 286:11211-11217
    • (2011) J Biol Chem , vol.286 , pp. 11211-11217
    • Liu, Y.D.1    Goetze, A.M.2    Bass, R.B.3    Flynn, G.C.4
  • 179
    • 75149132833 scopus 로고    scopus 로고
    • Immunological mechanism underlying the immune response to recombinant human protein therapeutics
    • Sauerborn M, Brinks V, Jiskoot W, Schellekens H (2010) Immunological mechanism underlying the immune response to recombinant human protein therapeutics. Trends Pharmacol Sci 31:53, H 59
    • (2010) Trends Pharmacol Sci , vol.31 , Issue.53 , pp. H59
    • Sauerborn, M.1    Brinks, V.2    Jiskoot, W.3    Schellekens, H.4
  • 180
    • 0030862195 scopus 로고    scopus 로고
    • Vascular leak syndrome: A side effect of immunotherapy
    • Baluna R, Vitetta ES (1997)Vascular leak syndrome: a side effect of immunotherapy. Immunopharmacology 37:117-132
    • (1997) Immunopharmacology , vol.37 , pp. 117-132
    • Baluna, R.1    Vitetta, E.S.2
  • 181
    • 84863025438 scopus 로고    scopus 로고
    • Immunotoxins constructed with chimeric, short-lived anti-CD22 monoclonal antibodies induce less vascular leak without loss of cytotoxicity
    • Liu XY, Pop LM, Schindler J, Vitetta ES (2012) Immunotoxins constructed with chimeric, short-lived anti-CD22 monoclonal antibodies induce less vascular leak without loss of cytotoxicity. MAbs 4:57-68
    • (2012) MAbs , vol.4 , pp. 57-68
    • Liu, X.Y.1    Pop, L.M.2    Schindler, J.3    Vitetta, E.S.4
  • 182
    • 17644378667 scopus 로고    scopus 로고
    • Immunogenicity of engineered antibodies
    • Hwang WYK, Foote J (2005) Immunogenicity of engineered antibodies. Methods 36:3-10
    • (2005) Methods , vol.36 , pp. 3-10
    • Hwang, W.Y.K.1    Foote, J.2


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