메뉴 건너뛰기




Volumn , Issue , 2009, Pages 79-108

Antibody Glycosylation

Author keywords

Antibodies; Glycosylation; Human IgG; IgG Fc; Translational medicine

Indexed keywords


EID: 81355139831     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9783527626601.ch4     Document Type: Chapter
Times cited : (2)

References (148)
  • 1
    • 27144457668 scopus 로고    scopus 로고
    • Upping the ante on antibodies
    • Baker, M. (2005) Upping the ante on antibodies. Nature Biotechnology, 23, 1065-1072.
    • (2005) Nature Biotechnology , vol.23 , pp. 1065-1072
    • Baker, M.1
  • 2
    • 27144457667 scopus 로고    scopus 로고
    • Monoclonal antibody successes in the clinic
    • Reichert, J.M. et al. (2005) Monoclonal antibody successes in the clinic. Nature Biotechnology, 23, 1073-1078.
    • (2005) Nature Biotechnology , vol.23 , pp. 1073-1078
    • Reichert, J.M.1
  • 3
    • 33646352962 scopus 로고    scopus 로고
    • Potent antibody therapeutics by design
    • Carter, P.J. (2006) Potent antibody therapeutics by design. Nature Reviews, 6, 343-357.
    • (2006) Nature Reviews , vol.6 , pp. 343-357
    • Carter, P.J.1
  • 4
    • 33750835115 scopus 로고    scopus 로고
    • Nonfucosylated therapeutic antibodies as next-generation therapeutic antibodies
    • Satoh, M., Iida, S., Shitara, K. (2006) Nonfucosylated therapeutic antibodies as next-generation therapeutic antibodies. Expert Opinion on Biological Therapy, 6, 1161-1173.
    • (2006) Expert Opinion on Biological Therapy , vol.6 , pp. 1161-1173
    • Satoh, M.1    Iida, S.2    Shitara, K.3
  • 5
    • 34548841437 scopus 로고    scopus 로고
    • Biotechs go generic: the same but different
    • Ledford, H. (2007) Biotechs go generic: the same but different. Nature, 449, 274-276.
    • (2007) Nature , vol.449 , pp. 274-276
    • Ledford, H.1
  • 6
    • 34447503942 scopus 로고    scopus 로고
    • The FDA's assessment of follow-on protein products: a historical perspective. Nature Reviews
    • Woodcock, J. et al. (2007) The FDA's assessment of follow-on protein products: a historical perspective. Nature Reviews. Drug Discovery, 6, 437-442.
    • (2007) Drug Discovery , vol.6 , pp. 437-442
    • Woodcock, J.1
  • 8
    • 40849137603 scopus 로고    scopus 로고
    • Glycan arrays: biological and medical applications
    • Liang, P.H. et al. (2008) Glycan arrays: biological and medical applications. Current Opinion in Chemical Biology, 12, 86-92.
    • (2008) Current Opinion in Chemical Biology , vol.12 , pp. 86-92
    • Liang, P.H.1
  • 9
    • 33745381312 scopus 로고    scopus 로고
    • Genetic defects in the human glycome. Nature Reviews
    • Freeze, H.H. (2007) Genetic defects in the human glycome. Nature Reviews.Genetics, 7, 537-551.
    • (2007) Genetics , vol.7 , pp. 537-551
    • Freeze, H.H.1
  • 10
    • 13544276336 scopus 로고    scopus 로고
    • Glycosylation of recombinant antibody therapeutics
    • Jefferis, R. (2005) Glycosylation of recombinant antibody therapeutics. Biotechnology Progress, 21, 11-16.
    • (2005) Biotechnology Progress , vol.21 , pp. 11-16
    • Jefferis, R.1
  • 11
    • 34748865088 scopus 로고    scopus 로고
    • Antibody therapeutics: isotype and glycoform selection
    • Jefferis, R. (2007) Antibody therapeutics: isotype and glycoform selection. Expert Opinion on Biological Therapy, 7, 1401-1413.
    • (2007) Expert Opinion on Biological Therapy , vol.7 , pp. 1401-1413
    • Jefferis, R.1
  • 12
    • 37549057294 scopus 로고    scopus 로고
    • N-Glycomic changes in serum proteins during human aging
    • Vanhooren, V. et al. (2007) N-Glycomic changes in serum proteins during human aging. Rejuvenation Research, 10, 521-531.
    • (2007) Rejuvenation Research , vol.10 , pp. 521-531
    • Vanhooren, V.1
  • 13
    • 32544455861 scopus 로고    scopus 로고
    • The pivotal nature of sugars in normal physiology and disease
    • Alavi, A. and Axford, J.S. (2006) The pivotal nature of sugars in normal physiology and disease. Wiener Medizinische Wochenschrift, 156, 19-33.
    • (2006) Wiener Medizinische Wochenschrift , vol.156 , pp. 19-33
    • Alavi, A.1    Axford, J.S.2
  • 14
    • 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. et al. (2006) Differential glycosylation of polyclonal IgG, IgG-Fc and IgG-Fab isolated from the sera of patients with ANCA associated systemic vasculitis. Biochimica et Biophysica Acta, 1760, 669-677.
    • (2006) Biochimica et Biophysica Acta , vol.1760 , pp. 669-677
    • Holland, M.1
  • 15
    • 23044510944 scopus 로고    scopus 로고
    • Activated human PMN synthesize and release a strongly fucosylated glycoform of {alpha}1-acid glycoprotein, which is transiently deposited in human myocardial infarction
    • Poland, D.C. et al. (2005) Activated human PMN synthesize and release a strongly fucosylated glycoform of {alpha}1-acid glycoprotein, which is transiently deposited in human myocardial infarction. Journal of Leukocyte Biology, 78, 453-461.
    • (2005) Journal of Leukocyte Biology , vol.78 , pp. 453-461
    • Poland, D.C.1
  • 16
    • 7044231536 scopus 로고    scopus 로고
    • Drug-induced and antibody-mediated pure red cell aplasia: a review of literature and current knowledge
    • Smalling, R. et al. (2004) Drug-induced and antibody-mediated pure red cell aplasia: a review of literature and current knowledge. Biotechnology Annual Review, 10, 37-50.
    • (2004) Biotechnology Annual Review , vol.10 , pp. 37-50
    • Smalling, R.1
  • 17
    • 25444435396 scopus 로고    scopus 로고
    • Glycoengineering: the effect of glycosylation on the properties of therapeutic proteins
    • Sinclair, A.M. and Elloitt, S. (2005) Glycoengineering: the effect of glycosylation on the properties of therapeutic proteins. Journal of Pharmaceutical Sciences, 94, 1626-1635.
    • (2005) Journal of Pharmaceutical Sciences , vol.94 , pp. 1626-1635
    • Sinclair, A.M.1    Elloitt, S.2
  • 18
    • 33749860977 scopus 로고    scopus 로고
    • Posttranslational modifications in the context of therapeutic proteins
    • Walsh, G. and Jefferis, R. (2006) Posttranslational modifications in the context of therapeutic proteins. Nature Biotechnology, 24, 1241-1252.
    • (2006) Nature Biotechnology , vol.24 , pp. 1241-1252
    • Walsh, G.1    Jefferis, R.2
  • 19
    • 0034050074 scopus 로고    scopus 로고
    • Species-specific variation in glycosylation of IgG: evidence for the species-specific sialylation and branch-specific galactosylation and importance for engineering recombinant glycoprotein therapeutics
    • Raju, T.S. et al. (2000) Species-specific variation in glycosylation of IgG: evidence for the species-specific sialylation and branch-specific galactosylation and importance for engineering recombinant glycoprotein therapeutics. Glycobiology, 10, 477-486.
    • (2000) Glycobiology , vol.10 , pp. 477-486
    • Raju, T.S.1
  • 20
    • 0033863867 scopus 로고    scopus 로고
    • Recombinant glycodelin carrying the same type of glycan structures as contraceptive glycodelin-A can be produced in human kidney 293 cells but not in Chinese hamster ovary cells
    • Van den Nieuwenhof, I.M. et al. (2000) Recombinant glycodelin carrying the same type of glycan structures as contraceptive glycodelin-A can be produced in human kidney 293 cells but not in Chinese hamster ovary cells. European Journal of Biochemistry, 267, 4753-4762.
    • (2000) European Journal of Biochemistry , vol.267 , pp. 4753-4762
    • Van Den Nieuwenhof, I.M.1
  • 21
    • 34548615130 scopus 로고    scopus 로고
    • Pharming and transgenic plants
    • Lienard, D. et al. (2007) Pharming and transgenic plants. Biotechnology Annual Review, 13, 115-1147.
    • (2007) Biotechnology Annual Review , vol.13 , pp. 115-1147
    • Lienard, D.1
  • 23
    • 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. et al. (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. Analytical Biochemistry, 373, 179-191.
    • (2008) Analytical Biochemistry , vol.373 , pp. 179-191
    • Quan, C.1
  • 24
    • 33644619972 scopus 로고    scopus 로고
    • Heterogeneity of recombinant antibodies: linking structure to function
    • Harris, R.J. (2005) Heterogeneity of recombinant antibodies: linking structure to function. Developmental Biology, 122, 117-127.
    • (2005) Developmental Biology , vol.122 , pp. 117-127
    • Harris, R.J.1
  • 26
    • 1142298744 scopus 로고    scopus 로고
    • Human antibody-Fc receptor interactions illuminated by crystal structures. Nature Reviews
    • Woof, J.M. and Burton, D.R. (2004) Human antibody-Fc receptor interactions illuminated by crystal structures. Nature Reviews. Immunology, 4, 89-99.
    • (2004) Immunology , vol.4 , pp. 89-99
    • Woof, J.M.1    Burton, D.R.2
  • 27
    • 1142286441 scopus 로고    scopus 로고
    • Interactions of immunoglobulins outside the antigen-combining site
    • Nezlin, R. and Ghetie, V. (2004) Interactions of immunoglobulins outside the antigen-combining site. Advances in Immunology, 82, 155-215.
    • (2004) Advances in Immunology , vol.82 , pp. 155-215
    • Nezlin, R.1    Ghetie, V.2
  • 28
    • 34247122497 scopus 로고    scopus 로고
    • The impact of glycosylation on the biological function and structure of human immunoglobulins
    • Arnold, J.N. et al. (2007) The impact of glycosylation on the biological function and structure of human immunoglobulins. Annual Review of Immunology, 25, 21-50.
    • (2007) Annual Review of Immunology , vol.25 , pp. 21-50
    • Arnold, J.N.1
  • 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-Å resolution
    • Deisenhofer, J. (1981) 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-Å resolution. Biochemistry, 20, 2361-2370.
    • (1981) Biochemistry , vol.20 , pp. 2361-2370
    • Deisenhofer, J.1
  • 30
    • 0031823336 scopus 로고    scopus 로고
    • Quantitation of human IgG glycoforms isolated from rheumatoid sera: A critical evaluation of chromatographic methods
    • Routier, F.H. et al. (1998) Quantitation of human IgG glycoforms isolated from rheumatoid sera: A critical evaluation of chromatographic methods. Journal of Immunological Methods, 213, 113-130.
    • (1998) Journal of Immunological Methods , vol.213 , pp. 113-130
    • Routier, F.H.1
  • 31
    • 0034685691 scopus 로고    scopus 로고
    • Pairing of oligosaccharides in the Fc region of immunoglobulin G
    • Masuda, K. et al. (2000) Pairing of oligosaccharides in the Fc region of immunoglobulin G. FEBS Letters, 473, 349-357.
    • (2000) FEBS Letters , vol.473 , pp. 349-357
    • Masuda, K.1
  • 32
    • 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. et al. (2007) Contrasting glycosylation profiles between Fab and Fc of a human IgG protein studied by electrospray ionization mass spectrometry. Journal of Immunological Methods, 326, 116-126.
    • (2007) Journal of Immunological Methods , vol.326 , pp. 116-126
    • Mimura, Y.1
  • 33
    • 84889444554 scopus 로고    scopus 로고
    • Accessed January 5th
    • http://glycomics.scripps.edu/CFGnomenclature.pdf. Accessed January 5th 2009.
    • (2009)
  • 35
    • 84889335228 scopus 로고    scopus 로고
    • Accessed January 5th
    • http://www.functionalglycomics.org. Accessed January 5th 2009.
    • (2009)
  • 36
    • 84889301878 scopus 로고    scopus 로고
    • Accessed January 5th
    • www.proglycan.com. Accessed January 5th 2009.
    • (2009)
  • 37
    • 0030996004 scopus 로고    scopus 로고
    • Structural changes of immunoglobulin G oligosaccharides with age in healthy human serum
    • Yamada, E. et al. (1997) Structural changes of immunoglobulin G oligosaccharides with age in healthy human serum. Glycoconjugate Journal, 14, 401-405.
    • (1997) Glycoconjugate Journal , vol.14 , pp. 401-405
    • Yamada, E.1
  • 38
    • 0029185950 scopus 로고
    • Short communication: Selective transport of maternal IgG to the foetus
    • Williams, P.J., Arkwright, P.D. and Rudd, P.M. (1995) Short communication: Selective transport of maternal IgG to the foetus. Placenta, 16, 749-756.
    • (1995) Placenta , vol.16 , pp. 749-756
    • Williams, P.J.1    Arkwright, P.D.2    Rudd, P.M.3
  • 39
    • 0030434866 scopus 로고    scopus 로고
    • Glycosylation and placental transport of immunoglobulin G
    • Kibe, T. et al. (1996) Glycosylation and placental transport of immunoglobulin G. Journal of Clinical Biochemistry and Nutrition, 21, 57-63.
    • (1996) Journal of Clinical Biochemistry and Nutrition , vol.21 , pp. 57-63
    • Kibe, T.1
  • 40
    • 33646172632 scopus 로고    scopus 로고
    • The carbohydrate at FcgammaRIIIa Asn-162. An element required for high affinity binding to nonfucosylated IgG glycoforms
    • Ferrara, C. et al. (2006) The carbohydrate at FcgammaRIIIa Asn-162. An element required for high affinity binding to nonfucosylated IgG glycoforms. The Journal of Biological Chemistry, 281, 5032-5036.
    • (2006) The Journal of Biological Chemistry , vol.281 , pp. 5032-5036
    • Ferrara, C.1
  • 41
    • 0030755924 scopus 로고    scopus 로고
    • Glycosylation of antibody molecules in multiple myeloma
    • Farooq, M. et al. (1997) Glycosylation of antibody molecules in multiple myeloma. Glycoconjugate Journal, 14, 489-492.
    • (1997) Glycoconjugate Journal , vol.14 , pp. 489-492
    • Farooq, M.1
  • 42
    • 0030470557 scopus 로고    scopus 로고
    • Multiple interactions of IgG with its core oligosaccharide can modulate recognition by complement and human FcgRI and influence the synthesis of its oligosaccharide chains
    • Lund, J. et al. (1996) Multiple interactions of IgG with its core oligosaccharide can modulate recognition by complement and human FcgRI and influence the synthesis of its oligosaccharide chains. Journal of Immunology, 157, 4963-4969.
    • (1996) Journal of Immunology , vol.157 , pp. 4963-4969
    • Lund, J.1
  • 43
    • 0034691322 scopus 로고    scopus 로고
    • The 3.2-A crystal structure of the human IgG1 Fc-FcgRIII complex
    • Sondermann, P. et al. (2000) The 3.2-A crystal structure of the human IgG1 Fc-FcgRIII complex. Nature, 406, 267-273.
    • (2000) Nature , vol.406 , pp. 267-273
    • Sondermann, P.1
  • 44
    • 0035844212 scopus 로고    scopus 로고
    • The structure of human type FcgIII receptor in complex with Fc
    • Radaev, S. et al. (2001) The structure of human type FcgIII receptor in complex with Fc. The Journal of Biological Chemistry, 276, 16469-16477.
    • (2001) The Journal of Biological Chemistry , vol.276 , pp. 16469-16477
    • Radaev, S.1
  • 45
    • 0002121160 scopus 로고
    • Fc Receptors and the Action of Antibodies
    • ed. H. Metzger, American Society for Microbiology, Washington D.C
    • Padlan, E.A. (1990) Fc Receptors and the Action of Antibodies (ed. H. Metzger), American Society for Microbiology, Washington D.C., pp. 12-30.
    • (1990) , pp. 12-30
    • Padlan, E.A.1
  • 46
    • 0014513216 scopus 로고
    • The covalent structure of an entire IgG molecule
    • Proceedings of the National Academy of Sciences of the, United States of America
    • Edelman, G.M. et al. (1969) The covalent structure of an entire IgG molecule. Proceedings of the National Academy of Sciences of the, United States of America 63, 78-85.
    • (1969) , vol.63 , pp. 78-85
    • Edelman, G.M.1
  • 47
    • 0035081693 scopus 로고    scopus 로고
    • The influence of glycosylation on the thermal stability and effector function expression of human IgG1-Fc: properties of a series of truncated glycoforms
    • Mimura, Y. et al. (2000) The influence of glycosylation on the thermal stability and effector function expression of human IgG1-Fc: properties of a series of truncated glycoforms. Molecular Immunology, 37, 697-706.
    • (2000) Molecular Immunology , vol.37 , pp. 697-706
    • Mimura, Y.1
  • 48
    • 0035824579 scopus 로고    scopus 로고
    • The role of oligosaccharide residues of IgG1-Fc in FcgIIb binding
    • Mimura, Y. et al. (2001) The role of oligosaccharide residues of IgG1-Fc in FcgIIb binding. The Journal of Biological Chemistry, 276, 45539-45547.
    • (2001) The Journal of Biological Chemistry , vol.276 , pp. 45539-45547
    • Mimura, Y.1
  • 49
    • 0037474543 scopus 로고    scopus 로고
    • Structural analysis of human IgG glycoforms reveals a correlation between oligosaccharide content, structural integrity and Fcgreceptor affinity
    • Krapp, S. et al. (2003) Structural analysis of human IgG glycoforms reveals a correlation between oligosaccharide content, structural integrity and Fcgreceptor affinity. Journal of Molecular Biology, 325, 979-989.
    • (2003) Journal of Molecular Biology , vol.325 , pp. 979-989
    • Krapp, S.1
  • 50
    • 33646105366 scopus 로고    scopus 로고
    • Glycoformdependent conformational alteration of the Fc region of human immunoglobulin G1 as revealed by NMR spectroscopy
    • Yamaguchi, Y. et al. (2006) Glycoformdependent conformational alteration of the Fc region of human immunoglobulin G1 as revealed by NMR spectroscopy. Biochimica et Biophysica Acta, 1760, 693-700.
    • (2006) Biochimica et Biophysica Acta , vol.1760 , pp. 693-700
    • Yamaguchi, Y.1
  • 51
    • 39149106011 scopus 로고    scopus 로고
    • Structural characterization of a mutated, ADCCenhanced human Fc fragment
    • Oganesyan, V. et al. (2008) Structural characterization of a mutated, ADCCenhanced human Fc fragment. Molecular Immunology, 45, 1872-1882.
    • (2008) Molecular Immunology , vol.45 , pp. 1872-1882
    • Oganesyan, V.1
  • 52
    • 35548955496 scopus 로고    scopus 로고
    • Fcreceptors as regulators of immunity
    • Nimmerjahn, F. and Ravetch, J. (2007) Fcreceptors as regulators of immunity. Advances in Immunology, 96, 179-204.
    • (2007) Advances in Immunology , vol.96 , pp. 179-204
    • Nimmerjahn, F.1    Ravetch, J.2
  • 53
    • 37549036732 scopus 로고    scopus 로고
    • Fcgamma receptors as regulators of immune responses. Nature Reviews
    • Nimmerjahn, F. and Ravetch, J. (2008) Fcgamma receptors as regulators of immune responses. Nature Reviews. Immunology, 8, 34-47.
    • (2008) Immunology , vol.8 , pp. 34-47
    • Nimmerjahn, F.1    Ravetch, J.2
  • 54
    • 0031572518 scopus 로고    scopus 로고
    • Cell type-specific glycoforms of Fcgamma RIIIa (CD16): differential ligand binding
    • Edberg, J.C. and Kimberly, R.P. (1997) Cell type-specific glycoforms of Fcgamma RIIIa (CD16): differential ligand binding. Journal of Immunology, 159, 3849-3857.
    • (1997) Journal of Immunology , vol.159 , pp. 3849-3857
    • Edberg, J.C.1    Kimberly, R.P.2
  • 55
    • 0242551825 scopus 로고    scopus 로고
    • Glycosylation of FcgammaRIII in N163 as mechanism of regulating receptor affinity
    • Drescher, B., Witte, T., Schmidt, R.E. (2003) Glycosylation of FcgammaRIII in N163 as mechanism of regulating receptor affinity. Immunology, 110, 335-340.
    • (2003) Immunology , vol.110 , pp. 335-340
    • Drescher, B.1    Witte, T.2    Schmidt, R.E.3
  • 56
    • 0028962403 scopus 로고
    • Glycosylation changes of IgG associated with rheumatoid arthritis can activate complement via the mannose-binding protein
    • Malhotra, R. et al. (1995) Glycosylation changes of IgG associated with rheumatoid arthritis can activate complement via the mannose-binding protein. Nature Medicine, 1, 237-243.
    • (1995) Nature Medicine , vol.1 , pp. 237-243
    • Malhotra, R.1
  • 57
    • 0030723080 scopus 로고    scopus 로고
    • Remodelling the oligosaccharide of human IgG antibodies: effects on biological activities
    • Abadeh, S. et al. (1997) Remodelling the oligosaccharide of human IgG antibodies: effects on biological activities. Biochemical Society Transactions, 25, S661.
    • (1997) Biochemical Society Transactions , vol.25
    • Abadeh, S.1
  • 58
    • 0032055988 scopus 로고    scopus 로고
    • Effect of C2-associated carbohydrate structure on Ig effector function: studies with chimeric mouse-human IgG1 antibodies in glycosylation mutants of Chinese hamster ovary cells
    • Wright, A. and Morrison, S.L. (1998) Effect of C2-associated carbohydrate structure on Ig effector function: studies with chimeric mouse-human IgG1 antibodies in glycosylation mutants of Chinese hamster ovary cells. Journal of Immunology, 160, 3393-3402.
    • (1998) Journal of Immunology , vol.160 , pp. 3393-3402
    • Wright, A.1    Morrison, S.L.2
  • 59
    • 23844468114 scopus 로고    scopus 로고
    • Human serum IgM glycosylation: identification of glycoforms that can bind to mannanbinding lectin
    • Arnold, J.N. et al. (2005) Human serum IgM glycosylation: identification of glycoforms that can bind to mannanbinding lectin. The Journal of Biological Chemistry, 280, 29080-29087.
    • (2005) The Journal of Biological Chemistry , vol.280 , pp. 29080-29087
    • Arnold, J.N.1
  • 60
    • 33746214786 scopus 로고    scopus 로고
    • Degalactosylated and/or denatured IgA, but not native IgA in any form, bind to mannose-binding lectin
    • Terai, I. et al. (2006) Degalactosylated and/or denatured IgA, but not native IgA in any form, bind to mannose-binding lectin. Journal of Immunology, 177, 1737-1745.
    • (2006) Journal of Immunology , vol.177 , pp. 1737-1745
    • Terai, I.1
  • 61
    • 0033571091 scopus 로고    scopus 로고
    • Binding and uptake of agalactosyl IgG by mannose receptor on macrophages and dendritic cells
    • Dong, X., Storkus, W.J., Salter, R.D. (1999) Binding and uptake of agalactosyl IgG by mannose receptor on macrophages and dendritic cells. Journal of Immunology, 163, 5427-5434.
    • (1999) Journal of Immunology , vol.163 , pp. 5427-5434
    • Dong, X.1    Storkus, W.J.2    Salter, R.D.3
  • 62
    • 0034495971 scopus 로고    scopus 로고
    • In vivo trafficking and catabolism of IgG1 antibodies with Fc associated carbohydrates of differing structure
    • Wright, A. et al. (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
  • 63
    • 0024424859 scopus 로고
    • The IgG subclass pattern of complement activation depends on epitope density and antibody and complement concentration
    • Garred, P., Michaesen, T.E., Aase, A. (1989) The IgG subclass pattern of complement activation depends on epitope density and antibody and complement concentration. Scandinavian Journal of Immunology, 30, 379-382.
    • (1989) Scandinavian Journal of Immunology , vol.30 , pp. 379-382
    • Garred, P.1    Michaesen, T.E.2    Aase, A.3
  • 64
    • 0025732287 scopus 로고
    • The effect of antibody isotype and antigenic epitope density on the complement-fixing activity of immune complexes: a systematic study using chimaeric anti-NIP antibodies with human Fc regions
    • Lucisano Valim, Y.M. and Lachmann, P.J. (1991) The effect of antibody isotype and antigenic epitope density on the complement-fixing activity of immune complexes: a systematic study using chimaeric anti-NIP antibodies with human Fc regions. Clinical and Experimental Immunology, 84, 1-8.
    • (1991) Clinical and Experimental Immunology , vol.84 , pp. 1-8
    • Lucisano Valim, Y.M.1    Lachmann, P.J.2
  • 65
    • 0030657786 scopus 로고    scopus 로고
    • Neutrophil Fc gamma and complement receptors involved in binding soluble IgG immune complexes and in specific granule release induced by soluble IgG immune complexes
    • Voice, J.K. and Lachmann, P.J. (1997) Neutrophil Fc gamma and complement receptors involved in binding soluble IgG immune complexes and in specific granule release induced by soluble IgG immune complexes. European Journal of Immunology, 27, 2514-2523.
    • (1997) European Journal of Immunology , vol.27 , pp. 2514-2523
    • Voice, J.K.1    Lachmann, P.J.2
  • 66
    • 0036671324 scopus 로고    scopus 로고
    • The contrasting IgG-binding interactions of human and herpes simplex virus Fc receptors
    • Armour, K.L. et al. (2002) The contrasting IgG-binding interactions of human and herpes simplex virus Fc receptors. Biochemical Society Transactions, 30, 495-500.
    • (2002) Biochemical Society Transactions , vol.30 , pp. 495-500
    • Armour, K.L.1
  • 67
    • 35348875440 scopus 로고    scopus 로고
    • Endoglycosidase treatment abrogates IgG arthritogenicity: importance of IgG glycosylation in arthritis
    • Nandakumar, K.S. et al. (2007) Endoglycosidase treatment abrogates IgG arthritogenicity: importance of IgG glycosylation in arthritis. European Journal of Immunology, 37, 2973-2982.
    • (2007) European Journal of Immunology , vol.37 , pp. 2973-2982
    • Nandakumar, K.S.1
  • 68
    • 0024438061 scopus 로고
    • Studies of aglycosylated chimeric mousehuman IgG. Role of carbohydrate in the structure and effector functions mediated by the human IgG constant region
    • Tao, M.H. and Morrison, S.L. (1989) Studies of aglycosylated chimeric mousehuman IgG. Role of carbohydrate in the structure and effector functions mediated by the human IgG constant region. Journal of Immunology, 143, 2595.
    • (1989) Journal of Immunology , vol.143 , pp. 2595
    • Tao, M.H.1    Morrison, S.L.2
  • 69
    • 0027414763 scopus 로고
    • Aglycosylated chimeric human IgG3 can trigger the human phagocyte respiratory burst
    • Pound, J.D., Lund, J., Jefferis, R. (1993) Aglycosylated chimeric human IgG3 can trigger the human phagocyte respiratory burst. Molecular Immunology, 30, 469-478.
    • (1993) Molecular Immunology , vol.30 , pp. 469-478
    • Pound, J.D.1    Lund, J.2    Jefferis, R.3
  • 70
    • 0026050344 scopus 로고
    • Human FcgRI and FcgRII interact with distinct but overlapping sites on human IgG
    • Lund, J. et al. (1991) Human FcgRI and FcgRII interact with distinct but overlapping sites on human IgG. Journal of Immunology, 147, 2657-2662.
    • (1991) Journal of Immunology , vol.147 , pp. 2657-2662
    • Lund, J.1
  • 71
    • 0026507779 scopus 로고
    • Mapping and comparison of the interaction sites on the Fc region of IgG responsible for triggering antibody dependent cellular cytotoxicity (ADCC) through different types of Fcg receptor
    • Sarmay, G. et al. (1992) Mapping and comparison of the interaction sites on the Fc region of IgG responsible for triggering antibody dependent cellular cytotoxicity (ADCC) through different types of Fcg receptor. Molecular Immunology, 29, 633-639.
    • (1992) Molecular Immunology , vol.29 , pp. 633-639
    • Sarmay, G.1
  • 72
    • 0035794194 scopus 로고    scopus 로고
    • High resolution mapping of the binding site on human IgG1 for FcgRI, FcgRII, FcgRIII, and FcRn and design of IgG1 variants with improved binding to the FcgR
    • Shields, R.L. et al. (2001) High resolution mapping of the binding site on human IgG1 for FcgRI, FcgRII, FcgRIII, and FcRn and design of IgG1 variants with improved binding to the FcgR. The Journal of Biological Chemistry, 276, 6591-6604.
    • (2001) The Journal of Biological Chemistry , vol.276 , pp. 6591-6604
    • Shields, R.L.1
  • 73
    • 35748949531 scopus 로고    scopus 로고
    • Optimizing engagement of the immune system by anti-tumor antibodies: an engineer's perspective
    • Desjarlais, J.R. et al. (2007) Optimizing engagement of the immune system by anti-tumor antibodies: an engineer's perspective. Drug Discovery Today, 12, 898-910.
    • (2007) Drug Discovery Today , vol.12 , pp. 898-910
    • Desjarlais, J.R.1
  • 74
    • 0036010538 scopus 로고    scopus 로고
    • Recognition of immunoglobulins by Fcgamma receptors
    • Radaev, S. and Sun, P. (2002) Recognition of immunoglobulins by Fcgamma receptors. Molecular Immunology, 38, 1073-1083.
    • (2002) Molecular Immunology , vol.38 , pp. 1073-1083
    • Radaev, S.1    Sun, P.2
  • 75
    • 0029644247 scopus 로고
    • Crystal structure of the C2 fragment of streptococcal protein G in complex with the Fc domain of human IgG
    • Sauer-Eriksson, A.E. et al. (1995) Crystal structure of the C2 fragment of streptococcal protein G in complex with the Fc domain of human IgG. Structure, 3, 265-278.
    • (1995) Structure , vol.3 , pp. 265-278
    • Sauer-Eriksson, A.E.1
  • 76
    • 0030938368 scopus 로고    scopus 로고
    • Structure of human IgM rheumatoid factor Fab bound to its autoantigen IgG Fc reveals a novel topology of antibody-antigen interaction
    • Corper, A.L. et al. (1997) Structure of human IgM rheumatoid factor Fab bound to its autoantigen IgG Fc reveals a novel topology of antibody-antigen interaction. Nature Structural Biology, 4, 374-381.
    • (1997) Nature Structural Biology , vol.4 , pp. 374-381
    • Corper, A.L.1
  • 77
    • 0000146003 scopus 로고
    • A theoretical model of gammaglobulin catabolism
    • Brambell, F.W.R., Hemmings, W.A. and Morris, I.G. (1964) A theoretical model of gammaglobulin catabolism. Nature, 203, 1352-1355.
    • (1964) Nature , vol.203 , pp. 1352-1355
    • Brambell, F.W.R.1    Hemmings, W.A.2    Morris, I.G.3
  • 78
    • 34447296997 scopus 로고    scopus 로고
    • Selective clearance of glycoforms of a complex glycoprotein pharmaceutical caused by terminal Nacetylglucosamine is similar in humans and cynomolgus monkeys
    • Jones, A.J. et al. (2007) Selective clearance of glycoforms of a complex glycoprotein pharmaceutical caused by terminal Nacetylglucosamine is similar in humans and cynomolgus monkeys. Glycobiology, 17, 529-540.
    • (2007) Glycobiology , vol.17 , pp. 529-540
    • Jones, A.J.1
  • 79
    • 43149096504 scopus 로고    scopus 로고
    • N-glycosylation as novel strategy to improve pharmacokinetic properties of bispecific single-chain diabodies
    • Stork, R. et al. (2008) N-glycosylation as novel strategy to improve pharmacokinetic properties of bispecific single-chain diabodies. The Journal of Biological Chemistry, 283, 7804-7812.
    • (2008) The Journal of Biological Chemistry , vol.283 , pp. 7804-7812
    • Stork, R.1
  • 80
    • 29644434678 scopus 로고    scopus 로고
    • An engineered human IgG1 antibody with longer serum half-life
    • Hinton, P.R. et al. (2006) An engineered human IgG1 antibody with longer serum half-life. Journal of Immunology, 176, 346-356.
    • (2006) Journal of Immunology , vol.176 , pp. 346-356
    • Hinton, P.R.1
  • 81
    • 33750699277 scopus 로고    scopus 로고
    • Pulmonary administration of therapeutic proteins using an immunoglobulin transport pathway
    • Bitonti, A.J. and Dumont, J.A. (2006) Pulmonary administration of therapeutic proteins using an immunoglobulin transport pathway. Advanced Drug Delivery Reviews, 58, 1106-1118.
    • (2006) Advanced Drug Delivery Reviews , vol.58 , pp. 1106-1118
    • Bitonti, A.J.1    Dumont, J.A.2
  • 82
    • 0022414766 scopus 로고
    • Association of rheumatoid arthritis and primary osteoarthritis with changes in the glycosylation pattern of total serum IgG
    • Parekh, R.B. et al. (1985) Association of rheumatoid arthritis and primary osteoarthritis with changes in the glycosylation pattern of total serum IgG. Nature, 316, 452-457.
    • (1985) Nature , vol.316 , pp. 452-457
    • Parekh, R.B.1
  • 83
    • 0346218144 scopus 로고    scopus 로고
    • Rheumatic disease differentiation using immunoglobulin G sugar printing by high density electrophoresis
    • Axford, J.S. et al. (2003) Rheumatic disease differentiation using immunoglobulin G sugar printing by high density electrophoresis. The Journal of Rheumatology, 12, 2540-2546.
    • (2003) The Journal of Rheumatology , vol.12 , pp. 2540-2546
    • Axford, J.S.1
  • 84
    • 0344542074 scopus 로고    scopus 로고
    • Fucosylation and galactosylation of IgG heavy chains differ between acute and remission phases of juvenile chronic arthritis
    • Flogel, M. et al. (1998) Fucosylation and galactosylation of IgG heavy chains differ between acute and remission phases of juvenile chronic arthritis. Clinical Chemistry and Laboratory Medicine, 36, 99-102.
    • (1998) Clinical Chemistry and Laboratory Medicine , vol.36 , pp. 99-102
    • Flogel, M.1
  • 85
    • 0028006394 scopus 로고
    • Deficient galactosylation of serum IgG in inflammatory bowel disease: correlation with disease activity
    • Go, M.F., Schrohenloher, R.E., and Tomana, M. (1994) Deficient galactosylation of serum IgG in inflammatory bowel disease: correlation with disease activity. Journal of Clinical Gastroenterology, 18, 86-87.
    • (1994) Journal of Clinical Gastroenterology , vol.18 , pp. 86-87
    • Go, M.F.1    Schrohenloher, R.E.2    Tomana, M.3
  • 86
    • 0036379420 scopus 로고    scopus 로고
    • Hypogalactosylation of serum IgG in patients with ANCA-associated systemic vasculitis
    • Holland, M. et al. (2002) Hypogalactosylation of serum IgG in patients with ANCA-associated systemic vasculitis. Clinical and Experimental Immunology, 29, 183-190.
    • (2002) Clinical and Experimental Immunology , vol.29 , pp. 183-190
    • Holland, M.1
  • 88
    • 32944461195 scopus 로고    scopus 로고
    • Heterogeneity of IgG glycosylation in adult periodontal disease
    • Novak, J. et al. (2005) Heterogeneity of IgG glycosylation in adult periodontal disease. Journal of Dental Research, 84, 897-901.
    • (2005) Journal of Dental Research , vol.84 , pp. 897-901
    • Novak, J.1
  • 89
    • 0019934863 scopus 로고
    • Structural and numerical variations of the carbohydrate moiety of immunoglobulin G
    • Mizouchi, T. et al. (1982) Structural and numerical variations of the carbohydrate moiety of immunoglobulin G. Journal of Immunology, 129, 2016-2020.
    • (1982) Journal of Immunology , vol.129 , pp. 2016-2020
    • Mizouchi, T.1
  • 90
    • 33746888249 scopus 로고    scopus 로고
    • Anti-inflammatory activity of immunoglobulin G resulting from Fc sialylation
    • Kaneko, Y., Nimmerjahn, F. and Ravetch, J. (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.3
  • 91
    • 33749850937 scopus 로고    scopus 로고
    • A sugar switch for antiinflammatory antibodies
    • Jefferis, R. (2006) A sugar switch for antiinflammatory antibodies. Nature Biotechnology, 24, 1230-1231.
    • (2006) Nature Biotechnology , vol.24 , pp. 1230-1231
    • Jefferis, R.1
  • 92
    • 33751253486 scopus 로고    scopus 로고
    • Higher levels of sialylated Fc glycans in immunoglobulin G molecules can adversely impact functionality
    • Scallon, B. et al. (2007) Higher levels of sialylated Fc glycans in immunoglobulin G molecules can adversely impact functionality. Molecular Immunology, 44, 1524-1534.
    • (2007) Molecular Immunology , vol.44 , pp. 1524-1534
    • Scallon, B.1
  • 93
    • 31844447560 scopus 로고    scopus 로고
    • Impact of variable domain glycosylation on antibody clearance: An LC/MS characterization
    • Huang, L. et al. (2006) Impact of variable domain glycosylation on antibody clearance: An LC/MS characterization. Analytical Biochemistry, 349, 197-207.
    • (2006) Analytical Biochemistry , vol.349 , pp. 197-207
    • Huang, L.1
  • 94
    • 33947688082 scopus 로고    scopus 로고
    • Structural characterization of N-linked oligosaccharides on monoclonal antibody cetuximab by the combination of orthogonal matrix-assisted laser desorption/ionization hybrid quadrupole-quadrupole time-of-flight tandem mass spectrometry and sequential enzymatic digestion
    • Qian, J. et al. (2007) Structural characterization of N-linked oligosaccharides on monoclonal antibody cetuximab by the combination of orthogonal matrix-assisted laser desorption/ionization hybrid quadrupole-quadrupole time-of-flight tandem mass spectrometry and sequential enzymatic digestion. Analytical Biochemistry, 364, 8-18.
    • (2007) Analytical Biochemistry , vol.364 , pp. 8-18
    • Qian, J.1
  • 96
    • 33947611087 scopus 로고    scopus 로고
    • Glycosylation of therapeutic proteins in different production systems
    • (Oslo, Norway: 1992) Supplement
    • Werner, R.G., Kopp, K., Schleuter, M. (2007) Glycosylation of therapeutic proteins in different production systems. Acta Paediatrica (Oslo, Norway: 1992) Supplement, 96, 17-22.
    • (2007) Acta Paediatrica , vol.96 , pp. 17-22
    • Werner, R.G.1    Kopp, K.2    Schleuter, M.3
  • 97
    • 0035977068 scopus 로고    scopus 로고
    • The human low affinity Fcgamma receptors IIa, IIb, and III bind IgG with fast kinetics and distinct thermodynamic properties
    • Maenaka, K. et al. (2001) The human low affinity Fcgamma receptors IIa, IIb, and III bind IgG with fast kinetics and distinct thermodynamic properties. The Journal of Biological Chemistry, 276, 44898-44904.
    • (2001) The Journal of Biological Chemistry , vol.276 , pp. 44898-44904
    • Maenaka, K.1
  • 98
    • 0031028909 scopus 로고    scopus 로고
    • Variations in oligosaccharide-protein interactions in immunoglobulin G determine the sitespecific glycosylation profiles and modulate the dynamic motion of the Fc oligosaccharides
    • Wormald, M.R. et al. (1997) Variations in oligosaccharide-protein interactions in immunoglobulin G determine the sitespecific glycosylation profiles and modulate the dynamic motion of the Fc oligosaccharides. Biochemistry, 36, 1370-1380.
    • (1997) Biochemistry , vol.36 , pp. 1370-1380
    • Wormald, M.R.1
  • 99
    • 34547725185 scopus 로고    scopus 로고
    • Efficacy of RhD monoclonal antibodies in clinical trials as replacement therapy for prophylactic anti-D immunoglobulin: more questions than answers
    • Kumpel, B.M. (2007) Efficacy of RhD monoclonal antibodies in clinical trials as replacement therapy for prophylactic anti-D immunoglobulin: more questions than answers. Vox Sanguinis, 93, 99-111.
    • (2007) Vox Sanguinis , vol.93 , pp. 99-111
    • Kumpel, B.M.1
  • 100
    • 0030070215 scopus 로고    scopus 로고
    • On the interaction between agalactosyl IgG and Fc gamma receptors
    • Groenink, J. et al. (1996) On the interaction between agalactosyl IgG and Fc gamma receptors. European Journal of Immunology, 26, 1404-1407.
    • (1996) European Journal of Immunology , vol.26 , pp. 1404-1407
    • Groenink, J.1
  • 101
    • 0029558207 scopus 로고
    • The effect of the removal of sialic acid, galactose and total carbohydrate on the functional activity of Campath-1H
    • Boyd, P.N. et al. (1995) The effect of the removal of sialic acid, galactose and total carbohydrate on the functional activity of Campath-1H. Molecular Immunology, 32, 1311-1318.
    • (1995) Molecular Immunology , vol.32 , pp. 1311-1318
    • Boyd, P.N.1
  • 102
    • 84889485459 scopus 로고    scopus 로고
    • Accessed January 5th
    • http://www.fda.gov/cder/biologics/review/ritugen112697-r2.pdf. Accessed January 5th 2009.
    • (2009)
  • 103
    • 0033978652 scopus 로고    scopus 로고
    • Two edged role of mannose binding lectin in rheumatoid arthritis: a cross sectional study
    • Garred, P. et al. (2000) Two edged role of mannose binding lectin in rheumatoid arthritis: a cross sectional study. The Journal of Rheumatology, 27, 26-34.
    • (2000) The Journal of Rheumatology , vol.27 , pp. 26-34
    • Garred, P.1
  • 104
    • 3242660135 scopus 로고    scopus 로고
    • The potential role of mannan-binding lectin in the clearance of self-components including immune complexes
    • Saevarsdottir, S., Vikingsdottir, T. and Valdimarsson, H. (2004) The potential role of mannan-binding lectin in the clearance of self-components including immune complexes. Scandinavian Journal of Immunology, 60, 23-29.
    • (2004) Scandinavian Journal of Immunology , vol.60 , pp. 23-29
    • Saevarsdottir, S.1    Vikingsdottir, T.2    Valdimarsson, H.3
  • 105
    • 0142011590 scopus 로고    scopus 로고
    • Structure-function analysis of C-type animal lectins
    • Taylor, M.E. and Drickamer, K. (2003) Structure-function analysis of C-type animal lectins. Methods in Enzymology, 363, 3-16.
    • (2003) Methods in Enzymology , vol.363 , pp. 3-16
    • Taylor, M.E.1    Drickamer, K.2
  • 106
    • 4644282738 scopus 로고    scopus 로고
    • The mannose receptor fails to enhance processing and presentation of a glycoprotein antigen in transfected fibroblasts
    • Napper, C.E. and Taylor, M.E. (2004) The mannose receptor fails to enhance processing and presentation of a glycoprotein antigen in transfected fibroblasts. Glycobiology, 14, 7C-12C.
    • (2004) Glycobiology , vol.14
    • Napper, C.E.1    Taylor, M.E.2
  • 107
    • 0141533076 scopus 로고    scopus 로고
    • Levels of complexity in pathogen recognition by C-type lectins
    • Cambi, A. and Figdor, C.G. (2003) Levels of complexity in pathogen recognition by C-type lectins. Current Opinion in Cell Biology, 2003, 15, 539-546.
    • (2003) Current Opinion in Cell Biology , vol.15 , pp. 539-546
    • Cambi, A.1    Figdor, C.G.2
  • 108
    • 0029563888 scopus 로고
    • Glycosylation and biological activity of CAMPATH-1H expressed in different cell lines and grown under different culture conditions
    • Lifely, M.R., Hale, G. and Boyse, S. (1995) Glycosylation and biological activity of CAMPATH-1H expressed in different cell lines and grown under different culture conditions. Glycobiology, 5, 813-822.
    • (1995) Glycobiology , vol.5 , pp. 813-822
    • Lifely, M.R.1    Hale, G.2    Boyse, S.3
  • 109
    • 0033044588 scopus 로고    scopus 로고
    • Engineered glycoforms of an anti-neuroblastoma. IgG1 with optimized antibody-dependent cellular cytotoxic activity
    • Umana, P. et al. (1999) Engineered glycoforms of an anti-neuroblastoma. IgG1 with optimized antibody-dependent cellular cytotoxic activity. Nature Biotechnology, 17, 176-180.
    • (1999) Nature Biotechnology , vol.17 , pp. 176-180
    • Umana, P.1
  • 110
    • 0035921175 scopus 로고    scopus 로고
    • Expression of GTIII in a recombinant anti-CD20 CHO production cell line: expression of antibodies of altered glycoforms leads to an increase in ADCC thro' higher affinity for FcRIII
    • Davies, J. et al. (2001) Expression of GTIII in a recombinant anti-CD20 CHO production cell line: expression of antibodies of altered glycoforms leads to an increase in ADCC thro' higher affinity for FcRIII. Biotechnology and Bioengineering, 74, 288-294.
    • (2001) Biotechnology and Bioengineering , vol.74 , pp. 288-294
    • Davies, J.1
  • 111
    • 0037178791 scopus 로고    scopus 로고
    • Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human FcgRIII and antibody-dependent cellular toxicity
    • Shields, R.L. et al. (2002) Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human FcgRIII and antibody-dependent cellular toxicity. The Journal of Biological Chemistry, 277, 26733-26740.
    • (2002) The Journal of Biological Chemistry , vol.277 , pp. 26733-26740
    • Shields, R.L.1
  • 112
    • 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. et al. (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. The Journal of Biological Chemistry, 278, 3466-3473.
    • (2003) The Journal of Biological Chemistry , vol.278 , pp. 3466-3473
    • Shinkawa, T.1
  • 113
    • 1242317024 scopus 로고    scopus 로고
    • Fucose depletion from human IgG1 oligosaccharide enhances binding enthalpy and association rate between IgG1 and FcgammaRIIIa
    • Okazaki, A. et al. (2004) Fucose depletion from human IgG1 oligosaccharide enhances binding enthalpy and association rate between IgG1 and FcgammaRIIIa. Journal of Molecular Biology, 336, 1239-1249.
    • (2004) Journal of Molecular Biology , vol.336 , pp. 1239-1249
    • Okazaki, A.1
  • 114
    • 33646070900 scopus 로고    scopus 로고
    • Modulation of therapeutic antibody effector functions by glycosylation engineering: influence of Golgi enzyme localization domain and coexpression of heterologous beta1, 4-Nacetylglucosaminyltransferase III and Golgi alpha-mannosidase II
    • Ferrara, C. et al. (2006) Modulation of therapeutic antibody effector functions by glycosylation engineering: influence of Golgi enzyme localization domain and coexpression of heterologous beta1, 4-Nacetylglucosaminyltransferase III and Golgi alpha-mannosidase II. Biotechnology and Bioengineering, 93, 851-861.
    • (2006) Biotechnology and Bioengineering , vol.93 , pp. 851-861
    • Ferrara, C.1
  • 115
    • 28444495153 scopus 로고    scopus 로고
    • IgG subclassindependent improvement of antibodydependent cellular cytotoxicity by fucose removal from Asn297-linked oligosaccharides
    • Niwa, R. et al. (2005) IgG subclassindependent improvement of antibodydependent cellular cytotoxicity by fucose removal from Asn297-linked oligosaccharides. Journal of Immunological Methods, 306, 151-160.
    • (2005) Journal of Immunological Methods , vol.306 , pp. 151-160
    • Niwa, R.1
  • 116
    • 28444437100 scopus 로고    scopus 로고
    • Fucose removal from complex-type oligosaccharide enhances the antibody-dependent cellular cytotoxicity of single-gene-encoded antibody comprising a single-chain antibody linked the antibody constant region
    • Natsume, A. et al. (2005) Fucose removal from complex-type oligosaccharide enhances the antibody-dependent cellular cytotoxicity of single-gene-encoded antibody comprising a single-chain antibody linked the antibody constant region. Journal of Immunological Methods, 306, 93-103.
    • (2005) Journal of Immunological Methods , vol.306 , pp. 93-103
    • Natsume, A.1
  • 117
    • 0035844221 scopus 로고    scopus 로고
    • Recognition of IgG by Fcgamma receptor. The role of Fc glycosylation and the binding of peptide inhibitors
    • Radaev, S. and Sun, P.D. (2001) Recognition of IgG by Fcgamma receptor. The role of Fc glycosylation and the binding of peptide inhibitors. The Journal of Biological Chemistry, 276, 16478-16483.
    • (2001) The Journal of Biological Chemistry , vol.276 , pp. 16478-16483
    • Radaev, S.1    Sun, P.D.2
  • 118
    • 34247854443 scopus 로고    scopus 로고
    • A nonfucosylated anti-HER2 antibody augments antibodydependent cellular cytotoxicity in breast cancer patients
    • Suzuki, E. et al. (2007) A nonfucosylated anti-HER2 antibody augments antibodydependent cellular cytotoxicity in breast cancer patients. Clinical Cancer Research, 13, 1875-1882.
    • (2007) Clinical Cancer Research , vol.13 , pp. 1875-1882
    • Suzuki, E.1
  • 119
    • 0029962752 scopus 로고    scopus 로고
    • Site-specific glycosylation of human immunoglobulin G is altered in four rheumatoid arthritis patients
    • Youings, A. et al. (1996) Site-specific glycosylation of human immunoglobulin G is altered in four rheumatoid arthritis patients. The Biochemical Journal, 314, 621-630.
    • (1996) The Biochemical Journal , vol.314 , pp. 621-630
    • Youings, A.1
  • 120
    • 0034095724 scopus 로고    scopus 로고
    • Effect of somatic hypermutation on potential Nglycosylation sites in human immunoglobulin heavy chain variable regions
    • Dunn-Walters, D.K., Boursier, L. and Spencer, J. (2000) Effect of somatic hypermutation on potential Nglycosylation sites in human immunoglobulin heavy chain variable regions. Molecular Immunology, 37, 107-113.
    • (2000) Molecular Immunology , vol.37 , pp. 107-113
    • Dunn-Walters, D.K.1    Boursier, L.2    Spencer, J.3
  • 121
    • 41549130879 scopus 로고    scopus 로고
    • Differentiation between isomeric triantennary N-linked glycans by negative ion tandem mass spectrometry and confirmation of glycans containing galactose attached to the bisecting (beta1-4-GlcNAc) residue in Nglycans from IgG
    • Harvey, D.J. et al. (2008) Differentiation between isomeric triantennary N-linked glycans by negative ion tandem mass spectrometry and confirmation of glycans containing galactose attached to the bisecting (beta1-4-GlcNAc) residue in Nglycans from IgG. Rapid Communications in Mass Spectrometry, 22, 1047-1052.
    • (2008) Rapid Communications in Mass Spectrometry , vol.22 , pp. 1047-1052
    • Harvey, D.J.1
  • 122
    • 40849142102 scopus 로고    scopus 로고
    • Cetuximabinduced anaphylaxis and IgE specific for galactose-a-1,3-galactose
    • Chung, C.H. et al. (2008) Cetuximabinduced anaphylaxis and IgE specific for galactose-a-1,3-galactose. The New England Journal of Medicine, 358, 1109-1117.
    • (2008) The New England Journal of Medicine , vol.358 , pp. 1109-1117
    • Chung, C.H.1
  • 123
    • 0031033895 scopus 로고    scopus 로고
    • Effect of glycosylation on antibody function: implications for genetic engineering
    • Wright, A. and Morrison, S.L. (1997) Effect of glycosylation on antibody function: implications for genetic engineering. Trends in Biotechnology, 15, 26-32.
    • (1997) Trends in Biotechnology , vol.15 , pp. 26-32
    • Wright, A.1    Morrison, S.L.2
  • 124
    • 2142813035 scopus 로고    scopus 로고
    • V region carbohydrate and antibody expression
    • Gala, F.A. and Morrison, S.L. (2004) V region carbohydrate and antibody expression. Journal of Immunology, 172, 5489-5494.
    • (2004) Journal of Immunology , vol.172 , pp. 5489-5494
    • Gala, F.A.1    Morrison, S.L.2
  • 125
    • 0027434029 scopus 로고
    • Genetically engineered deglycosylation of the variable domain increases the affinity of an anti-CD33 monoclonal antibody
    • Co, M.S. et al. (1993) Genetically engineered deglycosylation of the variable domain increases the affinity of an anti-CD33 monoclonal antibody. Molecular Immunology, 30, 1361-1367.
    • (1993) Molecular Immunology , vol.30 , pp. 1361-1367
    • Co, M.S.1
  • 126
    • 0034328791 scopus 로고    scopus 로고
    • Antigen binding of an ovomucoid-specific antibody is affected by a carbohydrate chain located on the light chain variable region
    • Fujomura, Y. et al. (2004) Antigen binding of an ovomucoid-specific antibody is affected by a carbohydrate chain located on the light chain variable region. Bioscience, Biotechnology, and Biochemistry, 64, 2298-2305.
    • (2004) Bioscience, Biotechnology, and Biochemistry , vol.64 , pp. 2298-2305
    • Fujomura, Y.1
  • 127
    • 0039725069 scopus 로고    scopus 로고
    • Variable domainlinked oligosaccharides of a human monoclonal IgG: structure and influence on antigen binding
    • Leibiger, H. et al. (1999) Variable domainlinked oligosaccharides of a human monoclonal IgG: structure and influence on antigen binding. The Biochemical Journal, 338, (Pt 2) 529-538.
    • (1999) The Biochemical Journal , vol.338 , Issue.PT. 2 , pp. 529-538
    • Leibiger, H.1
  • 128
    • 34247116573 scopus 로고    scopus 로고
    • Human follicular lymphoma cells contain oligomannose glycans in the antigenbinding site of the B-cell receptor
    • Radcliffe, C.M. et al. (2007) Human follicular lymphoma cells contain oligomannose glycans in the antigenbinding site of the B-cell receptor. The Journal of Biological Chemistry, 282, 7405-7415.
    • (2007) The Journal of Biological Chemistry , vol.282 , pp. 7405-7415
    • Radcliffe, C.M.1
  • 129
    • 38949143338 scopus 로고    scopus 로고
    • Remarkable selective glycosylation of the immunoglobulin variable region in follicular lymphoma
    • McCann, K.J. et al. (2008) Remarkable selective glycosylation of the immunoglobulin variable region in follicular lymphoma. Molecular Immunology, 45, 1567-1572.
    • (2008) Molecular Immunology , vol.45 , pp. 1567-1572
    • McCann, K.J.1
  • 130
    • 35348827319 scopus 로고    scopus 로고
    • Monoclonal antibody mechanisms of action in cancer
    • Weiner, G.J. (2007) Monoclonal antibody mechanisms of action in cancer. Immunologic Research, 39, 271-278.
    • (2007) Immunologic Research , vol.39 , pp. 271-278
    • Weiner, G.J.1
  • 131
    • 33847399072 scopus 로고    scopus 로고
    • FcgR, the key to optimize therapeutic antibodies?
    • Siberil, S. et al. (2007) FcgR, the key to optimize therapeutic antibodies? Critical Reviews in Oncology/Hematology, 62, 26-33.
    • (2007) Critical Reviews in Oncology/Hematology , vol.62 , pp. 26-33
    • Siberil, S.1
  • 132
    • 35648996524 scopus 로고    scopus 로고
    • Recombinant therapeutic monoclonal antibodies: mechanisms of action in relation to structural and functional duality
    • Congy-Jolivet, N. et al. (2007) Recombinant therapeutic monoclonal antibodies: mechanisms of action in relation to structural and functional duality. Critical Reviews in Oncology/Hematology, 64, 226-233.
    • (2007) Critical Reviews in Oncology/Hematology , vol.64 , pp. 226-233
    • Congy-Jolivet, N.1
  • 133
    • 35649016260 scopus 로고    scopus 로고
    • Updated consensus statement on biological agents for the treatment of rheumatic diseases, 2007
    • Furst, D.E. et al. (2007) Updated consensus statement on biological agents for the treatment of rheumatic diseases, 2007. Annals of the Rheumatic Diseases, 66, (Suppl 3) iii2-iii22.
    • (2007) Annals of the Rheumatic Diseases , vol.66 , Issue.SUPPL. 3 , pp. 32-322
    • Furst, D.E.1
  • 134
    • 4644280717 scopus 로고    scopus 로고
    • Anti-neutrophil cytoplasm antibody IgG subclasses in Wegener's granulomatosis: a possible pathogenic role for the IgG4 subclass
    • Holland, M. et al. (2004) Anti-neutrophil cytoplasm antibody IgG subclasses in Wegener's granulomatosis: a possible pathogenic role for the IgG4 subclass. Clinical and Experimental Immunology, 138, 183-192.
    • (2004) Clinical and Experimental Immunology , vol.138 , pp. 183-192
    • Holland, M.1
  • 135
    • 34548694517 scopus 로고    scopus 로고
    • Anti-inflammatory activity of human IgG4 antibodies by dynamic Fab arm exchange
    • van der Neut Kolfschoten, M. et al. (2007) Anti-inflammatory activity of human IgG4 antibodies by dynamic Fab arm exchange. Science, 317, 1554-1557.
    • (2007) Science , vol.317 , pp. 1554-1557
    • Van Der Neut Kolfschoten, M.1
  • 136
    • 37349089029 scopus 로고    scopus 로고
    • First-in-Man (FIM) clinical trials post-TeGenero: a review of the impact of the TeGenero trial on the design, conduct, and ethics of FIM trials
    • Nada, A. and Somberg, J. (2007) First-in-Man (FIM) clinical trials post-TeGenero: a review of the impact of the TeGenero trial on the design, conduct, and ethics of FIM trials. American Journal of Therapeutics, 14, 594-604.
    • (2007) American Journal of Therapeutics , vol.14 , pp. 594-604
    • Nada, A.1    Somberg, J.2
  • 137
    • 37849022052 scopus 로고    scopus 로고
    • Preparing for first-in-man studies: the challenges for translational immunology post-TGN1412
    • Dayan, C.M. and Wraith, D.C. (2008) Preparing for first-in-man studies: the challenges for translational immunology post-TGN1412. Clinical and Experimental Immunology, 151, 231-234.
    • (2008) Clinical and Experimental Immunology , vol.151 , pp. 231-234
    • Dayan, C.M.1    Wraith, D.C.2
  • 139
    • 33749236399 scopus 로고    scopus 로고
    • Established bioprocesses for producing antibodies as a basis for future planning
    • Farid, S.S. (2006) Established bioprocesses for producing antibodies as a basis for future planning. Advances in Biochemical Engineering/Biotechnology, 101, 1-42.
    • (2006) Advances in Biochemical Engineering/Biotechnology , vol.101 , pp. 1-42
    • Farid, S.S.1
  • 140
    • 15944365883 scopus 로고    scopus 로고
    • A review of human anti-globulin antibody (HAGA, HAMA, HACA, HAHA) responses to monoclonal antibodies. Not four letter words
    • Mirik, G.R. et al. (2004) A review of human anti-globulin antibody (HAGA, HAMA, HACA, HAHA) responses to monoclonal antibodies. Not four letter words. Quarterly Journal of Nuclear Medicine and Molecular, Imaging 48, 251-257.
    • (2004) Quarterly Journal of Nuclear Medicine and Molecular, Imaging , vol.48 , pp. 251-257
    • Mirik, G.R.1
  • 141
    • 33947321425 scopus 로고    scopus 로고
    • Pharma-Planta: road testing the developing regulatory guidelines for plant-made pharmaceuticals
    • Sparrow, P.A. (2007) Pharma-Planta: road testing the developing regulatory guidelines for plant-made pharmaceuticals. Transgenic Research, 16, 147-161.
    • (2007) Transgenic Research , vol.16 , pp. 147-161
    • Sparrow, P.A.1
  • 142
    • 33846126638 scopus 로고    scopus 로고
    • Antibody production with yeasts and filamentous fungi: on the road to large scale?
    • Gasser, B. and Mattanovitch, D. (2007) Antibody production with yeasts and filamentous fungi: on the road to large scale? Biotechnology Letters, 29, 201-212.
    • (2007) Biotechnology Letters , vol.29 , pp. 201-212
    • Gasser, B.1    Mattanovitch, D.2
  • 143
    • 0037344670 scopus 로고    scopus 로고
    • Production of antibodies and antibody fragments in Escherichia coli and a comparison of their functions, uses and modification
    • Humphreys, D.P. (2003) Production of antibodies and antibody fragments in Escherichia coli and a comparison of their functions, uses and modification. Current Opinion in Drug Discovery & Development, 6, 188-196.
    • (2003) Current Opinion in Drug Discovery & Development , vol.6 , pp. 188-196
    • Humphreys, D.P.1
  • 144
    • 33644686538 scopus 로고    scopus 로고
    • The Process Analytical Technology initiative and multivariate process analysis, monitoring and control
    • Kourti, T. (2006) The Process Analytical Technology initiative and multivariate process analysis, monitoring and control. Analytical and Bioanalytical Chemistry, 384, 1043-1048.
    • (2006) Analytical and Bioanalytical Chemistry , vol.384 , pp. 1043-1048
    • Kourti, T.1
  • 145
    • 84889350802 scopus 로고    scopus 로고
    • Accessed January 5th
    • http://www.fda.gov/CDER/GUIDANCE/6419fnl.htm. Accessed January 5th 2009.
    • (2009)
  • 146
    • 84889357267 scopus 로고    scopus 로고
    • Accessed January 5th
    • http://www.percivia.com/index.html. Accessed January 5th 2009.
    • (2009)
  • 147
    • 36149001292 scopus 로고    scopus 로고
    • Glycosylation engineering in yeast: the advent of fully humanized yeast
    • Hamilton, S.R. and Gerngross, T.U. (2007) Glycosylation engineering in yeast: the advent of fully humanized yeast. Current Opinion in Biotechnology, 18, 387-392.
    • (2007) Current Opinion in Biotechnology , vol.18 , pp. 387-392
    • Hamilton, S.R.1    Gerngross, T.U.2
  • 148
    • 33845711353 scopus 로고    scopus 로고
    • Glycan optimization of a human monoclonal antibody in the aquatic plant Lemna minor
    • Cox, K.M. et al. (2006) Glycan optimization of a human monoclonal antibody in the aquatic plant Lemna minor. Nature Biotechnology, 24, 1591-1597.
    • (2006) Nature Biotechnology , vol.24 , pp. 1591-1597
    • Cox, K.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.