메뉴 건너뛰기




Volumn 1860, Issue 8, 2016, Pages 1655-1668

Immune recruitment or suppression by glycan engineering of endogenous and therapeutic antibodies

Author keywords

Antibody; Effector function; Glycan; Glycosylation; Structure; Therapeutic antibodies

Indexed keywords

1 DEOXYNOJIRIMYCIN; ANTIBODY; CASTANOSPERMINE; CD209 ANTIGEN; FC RECEPTOR; GLYCAN; GRANULOCYTE MACROPHAGE COLONY STIMULATING FACTOR; IMMUNOGLOBULIN; IMMUNOGLOBULIN G ANTIBODY; KIFUNENSINE; MOGAMULIZUMAB; MONOCLONAL ANTIBODY; OBINUTUZUMAB; RECOMBINANT PROTEIN; RITUXIMAB; TRASTUZUMAB; IMMUNOGLOBULIN FC FRAGMENT; IMMUNOGLOBULIN G; POLYSACCHARIDE;

EID: 84973659190     PISSN: 03044165     EISSN: 18728006     Source Type: Journal    
DOI: 10.1016/j.bbagen.2016.04.016     Document Type: Article
Times cited : (44)

References (285)
  • 1
    • 34247122497 scopus 로고    scopus 로고
    • The impact of glycosylation on the biological function and structure of human immunoglobulins
    • J.N. Arnold, M.R. Wormald, R.B. Sim, P.M. Rudd, and R.A. Dwek The impact of glycosylation on the biological function and structure of human immunoglobulins Annu. Rev. Immunol. 25 2007 21 50
    • (2007) Annu. Rev. Immunol. , vol.25 , pp. 21-50
    • Arnold, J.N.1    Wormald, M.R.2    Sim, R.B.3    Rudd, P.M.4    Dwek, R.A.5
  • 2
    • 0037264969 scopus 로고    scopus 로고
    • Therapeutic antibodies for human diseases at the dawn of the twenty-first century
    • O.H. Brekke, and I. Sandlie Therapeutic antibodies for human diseases at the dawn of the twenty-first century Nat. Rev. Drug Discov. 2 2003 52 62
    • (2003) Nat. Rev. Drug Discov. , vol.2 , pp. 52-62
    • Brekke, O.H.1    Sandlie, I.2
  • 3
    • 61649087668 scopus 로고    scopus 로고
    • Glycosylation as a strategy to improve antibody-based therapeutics
    • R. Jefferis Glycosylation as a strategy to improve antibody-based therapeutics Nat. Rev. Drug Discov. 8 2009 226 234
    • (2009) Nat. Rev. Drug Discov. , vol.8 , pp. 226-234
    • Jefferis, R.1
  • 4
    • 84892754407 scopus 로고    scopus 로고
    • Emerging principles for the therapeutic exploitation of glycosylation
    • M. Dalziel, M. Crispin, C.N. Scanlan, N. Zitzmann, and R.A. Dwek Emerging principles for the therapeutic exploitation of glycosylation Science 343 2014 1235681
    • (2014) Science , vol.343 , pp. 1235681
    • Dalziel, M.1    Crispin, M.2    Scanlan, C.N.3    Zitzmann, N.4    Dwek, R.A.5
  • 5
    • 0037178791 scopus 로고    scopus 로고
    • Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human FcγRIII and antibody-dependent cellular toxicity
    • R.L. Shields, J. Lai, R. Keck, L.Y. O'Connell, K. Hong, Y.G. Meng, S.H.A. Weikert, and L.G. Presta Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human FcγRIII and antibody-dependent cellular toxicity J. Biol. Chem. 277 2002 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.A.7    Presta, L.G.8
  • 6
    • 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
    • T. Shinkawa, K. Nakamura, N. Yamane, E. Shoji-Hosaka, Y. Kanda, M. Sakurada, K. Uchida, H. Anazawa, M. Satoh, M. Yamasaki, N. Hanai, and K. Shitara 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 2003 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
  • 8
    • 33646740982 scopus 로고    scopus 로고
    • Nonfucosylated therapeutic IgG1 antibody can evade the inhibitory effect of serum immunoglobulin G on antibody-dependent cellular cytotoxicity through its high binding to FcγRIIIa
    • S. Iida, H. Misaka, M. Inoue, M. Shibata, R. Nakano, N. Yamane-Ohnuki, M. Wakitani, K. Yano, K. Shitara, and M. Satoh Nonfucosylated therapeutic IgG1 antibody can evade the inhibitory effect of serum immunoglobulin G on antibody-dependent cellular cytotoxicity through its high binding to FcγRIIIa Clin. Cancer Res. 12 2006 2879 2887
    • (2006) Clin. Cancer Res. , vol.12 , pp. 2879-2887
    • Iida, S.1    Misaka, H.2    Inoue, M.3    Shibata, M.4    Nakano, R.5    Yamane-Ohnuki, N.6    Wakitani, M.7    Yano, K.8    Shitara, K.9    Satoh, M.10
  • 10
    • 33746888249 scopus 로고    scopus 로고
    • Anti-inflammatory activity of immunoglobulin G resulting from Fc sialylation
    • Y. Kaneko, F. Nimmerjahn, and J.V. Ravetch Anti-inflammatory activity of immunoglobulin G resulting from Fc sialylation Science 313 2006 670 673
    • (2006) Science , vol.313 , pp. 670-673
    • Kaneko, Y.1    Nimmerjahn, F.2    Ravetch, J.V.3
  • 12
    • 84899573297 scopus 로고    scopus 로고
    • Broad requirement for terminal sialic acid residues and FcγRIIB for the preventive and therapeutic activity of intravenous immunoglobulins in vivo
    • I. Schwab, S. Mihai, M. Seeling, M. Kasperkiewicz, R.J. Ludwig, and F. Nimmerjahn Broad requirement for terminal sialic acid residues and FcγRIIB for the preventive and therapeutic activity of intravenous immunoglobulins in vivo Eur. J. Immunol. 44 2014 1444 1453
    • (2014) Eur. J. Immunol. , vol.44 , pp. 1444-1453
    • Schwab, I.1    Mihai, S.2    Seeling, M.3    Kasperkiewicz, M.4    Ludwig, R.J.5    Nimmerjahn, F.6
  • 13
    • 0020977127 scopus 로고
    • Structural basis of antibody function
    • D.R. Davies, and H. Metzger Structural basis of antibody function Annu. Rev. Immunol. 1 1983 87 117
    • (1983) Annu. Rev. Immunol. , vol.1 , pp. 87-117
    • Davies, D.R.1    Metzger, H.2
  • 14
    • 0028289241 scopus 로고
    • Anatomy of the antibody molecule
    • E.A. Padlan Anatomy of the antibody molecule Mol. Immunol. 31 1994 169 217
    • (1994) Mol. Immunol. , vol.31 , pp. 169-217
    • Padlan, E.A.1
  • 15
    • 77953760056 scopus 로고    scopus 로고
    • Antibody-mediated modulation of immune responses
    • F. Nimmerjahn, and J.V. Ravetch Antibody-mediated modulation of immune responses Immunol. Rev. 236 2010 265 275
    • (2010) Immunol. Rev. , vol.236 , pp. 265-275
    • Nimmerjahn, F.1    Ravetch, J.V.2
  • 16
    • 0023679664 scopus 로고
    • IgG subclasses: A historical perspective
    • P.H. Schur IgG subclasses: a historical perspective Monogr. Allergy 23 1988 1 11
    • (1988) Monogr. Allergy , vol.23 , pp. 1-11
    • Schur, P.H.1
  • 17
    • 0023765625 scopus 로고
    • Human monoclonal IgG isotypes differ in complement activating function at the level of C4 as well as C1q
    • C.I. Bindon, G. Hale, M. Brüggemann, and H. Waldmann Human monoclonal IgG isotypes differ in complement activating function at the level of C4 as well as C1q J. Exp. Med. 168 1988 127 142
    • (1988) J. Exp. Med. , vol.168 , pp. 127-142
    • Bindon, C.I.1    Hale, G.2    Brüggemann, M.3    Waldmann, H.4
  • 18
    • 0017102773 scopus 로고
    • Ultracentifuge studies of the binding of IgG of different subclasses to the Clq subunit of the first component of complement
    • V.N. Schumaker, M.A. Calcott, H.L. Spiegelberg, and H.J. Muller-Eberhard Ultracentifuge studies of the binding of IgG of different subclasses to the Clq subunit of the first component of complement Biochemistry 15 1976 5175 5181
    • (1976) Biochemistry , vol.15 , pp. 5175-5181
    • Schumaker, V.N.1    Calcott, M.A.2    Spiegelberg, H.L.3    Muller-Eberhard, H.J.4
  • 19
    • 0027213573 scopus 로고
    • Structural features of human immunoglobulin G that determine isotype-specific differences in complement activation
    • M.H. Tao, R.I. Smith, and S.L. Morrison Structural features of human immunoglobulin G that determine isotype-specific differences in complement activation J. Exp. Med. 178 1993 661 667
    • (1993) J. Exp. Med. , vol.178 , pp. 661-667
    • Tao, M.H.1    Smith, R.I.2    Morrison, S.L.3
  • 20
    • 65549114676 scopus 로고    scopus 로고
    • Specificity and affinity of human Fcγ receptors and their polymorphic variants for human IgG subclasses
    • P. Bruhns, B. Iannascoli, P. England, D.A. Mancardi, N. Fernandez, S. Jorieux, and M. Daëron Specificity and affinity of human Fcγ receptors and their polymorphic variants for human IgG subclasses Blood 113 2009 3716 3725
    • (2009) Blood , vol.113 , pp. 3716-3725
    • Bruhns, P.1    Iannascoli, B.2    England, P.3    Mancardi, D.A.4    Fernandez, N.5    Jorieux, S.6    Daëron, M.7
  • 21
    • 0022487963 scopus 로고
    • Aspects of the molecular structure of IgG subclasses
    • D.R. Burton, L. Gregory, and R. Jefferis Aspects of the molecular structure of IgG subclasses Monogr. Allergy 19 1986 7 35
    • (1986) Monogr. Allergy , vol.19 , pp. 7-35
    • Burton, D.R.1    Gregory, L.2    Jefferis, R.3
  • 23
    • 0019522383 scopus 로고
    • Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9- and 2.8-A resolution
    • J. Deisenhofer Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9- and 2.8-A resolution Biochemistry 20 1981 2361 2370
    • (1981) Biochemistry , vol.20 , pp. 2361-2370
    • Deisenhofer, J.1
  • 24
    • 84945265000 scopus 로고    scopus 로고
    • TRIM21: A cytosolic Fc receptor with broad antibody isotype specificity
    • S. Foss, R. Watkinson, I. Sandlie, L.C. James, and J.T. Andersen TRIM21: a cytosolic Fc receptor with broad antibody isotype specificity Immunol. Rev. 268 2015 328 339
    • (2015) Immunol. Rev. , vol.268 , pp. 328-339
    • Foss, S.1    Watkinson, R.2    Sandlie, I.3    James, L.C.4    Andersen, J.T.5
  • 25
    • 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
    • R.L. Shields, A.K. Namenuk, K. Hong, Y.G. Meng, J. Rae, J. Briggs, D. Xie, J. Lai, A. Stadlen, B. Li, J.A. Fox, and L.G. Presta 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 2001 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
    • 0023897194 scopus 로고
    • The binding site for C1q on IgG
    • A.R. Duncan, and G. Winter The binding site for C1q on IgG Nature 332 1988 738 740
    • (1988) Nature , vol.332 , pp. 738-740
    • Duncan, A.R.1    Winter, G.2
  • 27
    • 0034681465 scopus 로고    scopus 로고
    • Convergent solutions to binding at a protein-protein interface
    • W.L. DeLano, M.H. Ultsch, A.M. de Vos, and J.A. Wells Convergent solutions to binding at a protein-protein interface Science 287 2000 1279 1283
    • (2000) Science , vol.287 , pp. 1279-1283
    • DeLano, W.L.1    Ultsch, M.H.2    De Vos, A.M.3    Wells, J.A.4
  • 28
    • 0021891884 scopus 로고
    • Assembly of asparagine-linked oligosaccharides
    • R. Kornfeld, and S. Kornfeld Assembly of asparagine-linked oligosaccharides Annu. Rev. Biochem. 54 1985 631 664
    • (1985) Annu. Rev. Biochem. , vol.54 , pp. 631-664
    • Kornfeld, R.1    Kornfeld, S.2
  • 32
    • 0035979377 scopus 로고    scopus 로고
    • Glycoengineering of therapeutic glycoproteins: In vitro galactosylation and sialylation of glycoproteins with terminal N-acetylglucosamine and galactose residues
    • T.S. Raju, J.B. Briggs, S.M. Chamow, M.E. Winkler, and A.J.S. Jones Glycoengineering of therapeutic glycoproteins: in vitro galactosylation and sialylation of glycoproteins with terminal N-acetylglucosamine and galactose residues Biochemistry 40 2001 8868 8876
    • (2001) Biochemistry , vol.40 , pp. 8868-8876
    • Raju, T.S.1    Briggs, J.B.2    Chamow, S.M.3    Winkler, M.E.4    Jones, A.J.S.5
  • 34
    • 13544276336 scopus 로고    scopus 로고
    • Glycosylation of recombinant antibody therapeutics
    • R. Jefferis Glycosylation of recombinant antibody therapeutics Biotechnol. Prog. 21 2005 11 16
    • (2005) Biotechnol. Prog. , vol.21 , pp. 11-16
    • Jefferis, R.1
  • 35
    • 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 N-glycans from IgG
    • D.J. Harvey, M. Crispin, C. Scanlan, B.B. Singer, L. Lucka, V.T. Chang, C.M. Radcliffe, S. Thobhani, C.T. Yuen, and P.M. Rudd 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 N-glycans from IgG Rapid Commun. Mass Spectrom. 22 2008 1047 1052
    • (2008) Rapid Commun. Mass Spectrom. , vol.22 , pp. 1047-1052
    • Harvey, D.J.1    Crispin, M.2    Scanlan, C.3    Singer, B.B.4    Lucka, L.5    Chang, V.T.6    Radcliffe, C.M.7    Thobhani, S.8    Yuen, C.T.9    Rudd, P.M.10
  • 38
    • 0029962752 scopus 로고    scopus 로고
    • Site-specific glycosylation of human immunoglobulin G is altered in four rheumatoid arthritis patients
    • A. Youings, S.C. Chang, R.A. Dwek, and I.G. Scragg Site-specific glycosylation of human immunoglobulin G is altered in four rheumatoid arthritis patients Biochem. J. 314 1996 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
  • 39
    • 0031028909 scopus 로고    scopus 로고
    • Variations in oligosaccharide - Protein interactions in immunoglobulin G determine the site-specific glycosylation profiles and modulate the dynamic motion of the Fc oligosaccharides
    • M.R. Wormald, P.M. Rudd, D.J. Harvey, S.-C. Chang, I.G. Scragg, and R.A. Dwek Variations in oligosaccharide - protein interactions in immunoglobulin G determine the site-specific glycosylation profiles and modulate the dynamic motion of the Fc oligosaccharides Biochemistry 36 1997 1370 1380
    • (1997) Biochemistry , vol.36 , pp. 1370-1380
    • Wormald, M.R.1    Rudd, P.M.2    Harvey, D.J.3    Chang, S.-C.4    Scragg, I.G.5    Dwek, R.A.6
  • 40
    • 0034095724 scopus 로고    scopus 로고
    • Effect of somatic hypermutation on potential N-glycosylation sites in human immunoglobulin heavy chain variable regions
    • D. Dunn-Walters, L. Boursier, and J. Spencer Effect of somatic hypermutation on potential N-glycosylation sites in human immunoglobulin heavy chain variable regions Mol. Immunol. 37 2000 107 113
    • (2000) Mol. Immunol. , vol.37 , pp. 107-113
    • Dunn-Walters, D.1    Boursier, L.2    Spencer, J.3
  • 41
    • 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
    • M. Holland, H. Yagi, N. Takahashi, K. Kato, C.O.S. Savage, D.M. Goodall, and R. Jefferis Differential glycosylation of polyclonal IgG, IgG-Fc and IgG-Fab isolated from the sera of patients with ANCA-associated systemic vasculitis Biochim. Biophys. Acta 1760 2006 669 677
    • (2006) Biochim. Biophys. Acta , 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
  • 42
    • 34748865088 scopus 로고    scopus 로고
    • Antibody therapeutics: Isotype and glycoform selection
    • R. Jefferis Antibody therapeutics: isotype and glycoform selection Expert. Opin. Biol. Ther. 7 2007 1401 1413
    • (2007) Expert. Opin. Biol. Ther. , vol.7 , pp. 1401-1413
    • Jefferis, R.1
  • 43
    • 84929587129 scopus 로고    scopus 로고
    • A perspective on the structure and receptor binding properties of immunoglobulin G Fc
    • Q.M. Hanson, and A.W. Barb A perspective on the structure and receptor binding properties of immunoglobulin G Fc Biochemistry 54 2015 2931 2942
    • (2015) Biochemistry , vol.54 , pp. 2931-2942
    • Hanson, Q.M.1    Barb, A.W.2
  • 45
    • 84884309807 scopus 로고    scopus 로고
    • Crystal structure of sialylated IgG Fc: Implications for the mechanism of intravenous immunoglobulin therapy
    • M. Crispin, X. Yu, and T.A. Bowden Crystal structure of sialylated IgG Fc: implications for the mechanism of intravenous immunoglobulin therapy Proc. Natl. Acad. Sci. U. S. A. 110 2013 E3544 E3546
    • (2013) Proc. Natl. Acad. Sci. U. S. A. , vol.110 , pp. E3544-E3546
    • Crispin, M.1    Yu, X.2    Bowden, T.A.3
  • 46
    • 0037474543 scopus 로고    scopus 로고
    • Structural analysis of human IgG-Fc glycoforms reveals a correlation between glycosylation and structural integrity
    • S. Krapp, Y. Mimura, R. Jefferis, R. Huber, and P. Sondermann Structural analysis of human IgG-Fc glycoforms reveals a correlation between glycosylation and structural integrity J. Mol. Biol. 325 2003 979 989
    • (2003) J. Mol. Biol. , vol.325 , pp. 979-989
    • Krapp, S.1    Mimura, Y.2    Jefferis, R.3    Huber, R.4    Sondermann, P.5
  • 48
    • 72649088522 scopus 로고    scopus 로고
    • Identification of high-mannose and multiantennary complex-type N-linked glycans containing alpha-galactose epitopes from nurse shark IgM heavy chain
    • D.J. Harvey, M. Crispin, B.E. Moffatt, S.L. Smith, R.B. Sim, P.M. Rudd, and R.A. Dwek Identification of high-mannose and multiantennary complex-type N-linked glycans containing alpha-galactose epitopes from nurse shark IgM heavy chain Glycoconj. J. 26 2009 1055 1064
    • (2009) Glycoconj. J. , vol.26 , pp. 1055-1064
    • Harvey, D.J.1    Crispin, M.2    Moffatt, B.E.3    Smith, S.L.4    Sim, R.B.5    Rudd, P.M.6    Dwek, R.A.7
  • 50
    • 79951838374 scopus 로고    scopus 로고
    • NMR analysis demonstrates immunoglobulin G N-glycans are accessible and dynamic
    • A.W. Barb, and J.H. Prestegard NMR analysis demonstrates immunoglobulin G N-glycans are accessible and dynamic Nat. Chem. Biol. 7 2011 147 153
    • (2011) Nat. Chem. Biol. , vol.7 , pp. 147-153
    • Barb, A.W.1    Prestegard, J.H.2
  • 52
    • 84884344335 scopus 로고    scopus 로고
    • Reply to Crispin et al.: Molecular model that accounts for the biological and physical properties of sialylated fc
    • P. Sondermann, A. Pincetic, J. Maamary, K. Lammens, and J.V. Ravetch Reply to Crispin et al.: molecular model that accounts for the biological and physical properties of sialylated fc Proc. Natl. Acad. Sci. U. S. A. 110 2013 E3547
    • (2013) Proc. Natl. Acad. Sci. U. S. A. , vol.110 , pp. E3547
    • Sondermann, P.1    Pincetic, A.2    Maamary, J.3    Lammens, K.4    Ravetch, J.V.5
  • 54
    • 84861883015 scopus 로고    scopus 로고
    • NMR characterization of immunoglobulin G Fc glycan motion on enzymatic sialylation
    • A.W. Barb, L. Meng, Z. Gao, R.W. Johnson, K.W. Moremen, and J.H. Prestegard NMR characterization of immunoglobulin G Fc glycan motion on enzymatic sialylation Biochemistry 51 2012 4618 4626
    • (2012) Biochemistry , vol.51 , pp. 4618-4626
    • Barb, A.W.1    Meng, L.2    Gao, Z.3    Johnson, R.W.4    Moremen, K.W.5    Prestegard, J.H.6
  • 56
    • 84958811707 scopus 로고    scopus 로고
    • Effect of Fc-glycan structure on the conformational stability of IgG revealed by hydrogen/deuterium exchange and limited proteolysis
    • J. Fang, J. Richardson, Z. Du, and Z. Zhang Effect of Fc-glycan structure on the conformational stability of IgG revealed by hydrogen/deuterium exchange and limited proteolysis Biochemistry 55 2016 860 868
    • (2016) Biochemistry , vol.55 , pp. 860-868
    • Fang, J.1    Richardson, J.2    Du, Z.3    Zhang, Z.4
  • 57
    • 62649171202 scopus 로고    scopus 로고
    • Emerging methods for the production of homogeneous human glycoproteins
    • J.R. Rich, and S.G. Withers Emerging methods for the production of homogeneous human glycoproteins Nat. Chem. Biol. 5 2009 206 215
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 206-215
    • Rich, J.R.1    Withers, S.G.2
  • 58
    • 84862908666 scopus 로고    scopus 로고
    • Emerging technologies for making glycan-defined glycoproteins
    • L.-X. Wang, and J.V. Lomino Emerging technologies for making glycan-defined glycoproteins ACS Chem. Biol. 7 2012 110 122
    • (2012) ACS Chem. Biol. , vol.7 , pp. 110-122
    • Wang, L.-X.1    Lomino, J.V.2
  • 59
    • 33750835115 scopus 로고    scopus 로고
    • Non-fucosylated therapeutic antibodies as next-generation therapeutic antibodies
    • M. Satoh, S. Iida, and K. Shitara Non-fucosylated therapeutic antibodies as next-generation therapeutic antibodies Expert. Opin. Biol. Ther. 6 2006 1161 1173
    • (2006) Expert. Opin. Biol. Ther. , vol.6 , pp. 1161-1173
    • Satoh, M.1    Iida, S.2    Shitara, K.3
  • 65
    • 84863470971 scopus 로고    scopus 로고
    • Marketing approval of mogamulizumab: A triumph for glyco-engineering
    • A. Beck, and J.M. Reichert Marketing approval of mogamulizumab: a triumph for glyco-engineering mAbs 4 2012 419 425
    • (2012) MAbs , Issue.4 , pp. 419-425
    • Beck, A.1    Reichert, J.M.2
  • 66
    • 0038495798 scopus 로고    scopus 로고
    • Fucose: Biosynthesis and biological function in mammals
    • D.J. Becker, and J.B. Lowe Fucose: biosynthesis and biological function in mammals Glycobiology 13 2003 41R 53R
    • (2003) Glycobiology , vol.13 , pp. 41R-53R
    • Becker, D.J.1    Lowe, J.B.2
  • 67
    • 34250369571 scopus 로고    scopus 로고
    • Establishment of a GDP-mannose 4,6-dehydratase (GMD) knockout host cell line: A new strategy for generating completely non-fucosylated recombinant therapeutics
    • Y. Kanda, H. Imai-Nishiya, R. Kuni-Kamochi, K. Mori, M. Inoue, K. Kitajima-Miyama, A. Okazaki, S. Iida, K. Shitara, and M. Satoh Establishment of a GDP-mannose 4,6-dehydratase (GMD) knockout host cell line: a new strategy for generating completely non-fucosylated recombinant therapeutics J. Biotechnol. 130 2007 300 310
    • (2007) J. Biotechnol. , vol.130 , pp. 300-310
    • Kanda, Y.1    Imai-Nishiya, H.2    Kuni-Kamochi, R.3    Mori, K.4    Inoue, M.5    Kitajima-Miyama, K.6    Okazaki, A.7    Iida, S.8    Shitara, K.9    Satoh, M.10
  • 68
    • 38649143213 scopus 로고    scopus 로고
    • Double knockdown of alpha1,6-fucosyltransferase (FUT8) and GDP-mannose 4,6-dehydratase (GMD) in antibody-producing cells: A new strategy for generating fully non-fucosylated therapeutic antibodies with enhanced ADCC
    • H. Imai-Nishiya, K. Mori, M. Inoue, M. Wakitani, S. Iida, K. Shitara, and M. Satoh Double knockdown of alpha1,6-fucosyltransferase (FUT8) and GDP-mannose 4,6-dehydratase (GMD) in antibody-producing cells: a new strategy for generating fully non-fucosylated therapeutic antibodies with enhanced ADCC BMC Biotechnol. 7 2007 84
    • (2007) BMC Biotechnol. , vol.7 , pp. 84
    • Imai-Nishiya, H.1    Mori, K.2    Inoue, M.3    Wakitani, M.4    Iida, S.5    Shitara, K.6    Satoh, M.7
  • 69
    • 0033044588 scopus 로고    scopus 로고
    • Engineered glycoforms of an antineuroblastoma IgG1 with optimized antibody-dependent cellular cytotoxic activity
    • P. Umana, J. Jean-Mairet, R. Moudry, H. Amstutz, and J.E. Bailey Engineered glycoforms of an antineuroblastoma IgG1 with optimized antibody-dependent cellular cytotoxic activity Nat. Biotechnol. 17 1999 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
  • 71
    • 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-N-acetylglucosaminyltransferase III and Golgi α-mannosidase II
    • C. Ferrara, P. Brünker, T. Suter, S. Moser, U. Püntener, and P. Umaña Modulation of therapeutic antibody effector functions by glycosylation engineering: influence of Golgi enzyme localization domain and co-expression of heterologous β1, 4-N-acetylglucosaminyltransferase III and Golgi α-mannosidase II Biotechnol. Bioeng. 93 2006 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
  • 72
    • 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 FC gamma RIII
    • J. Davies, L. Jiang, L.Z. Pan, M.J. LaBarre, D. Anderson, and M. Reff 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 FC gamma RIII Biotechnol. Bioeng. 74 2001 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
  • 73
    • 84906092974 scopus 로고    scopus 로고
    • Obinutuzumab: A new class of anti-CD20 monoclonal antibody
    • A.L. Gagez, and G. Cartron Obinutuzumab: a new class of anti-CD20 monoclonal antibody Curr. Opin. Oncol. 26 2014 484 491
    • (2014) Curr. Opin. Oncol. , vol.26 , pp. 484-491
    • Gagez, A.L.1    Cartron, G.2
  • 77
    • 0037109074 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: High-level expression of rhodopsin with restricted and homogeneous N-glycosylation by a tetracycline-inducible N-acetylglucosaminyltransferase I-negative HEK293S stable mammalian cell line
    • P.J. Reeves, N. Callewaert, R. Contreras, and H.G. Khorana Structure and function in rhodopsin: high-level expression of rhodopsin with restricted and homogeneous N-glycosylation by a tetracycline-inducible N-acetylglucosaminyltransferase I-negative HEK293S stable mammalian cell line Proc. Natl. Acad. Sci. 99 2002 13419 13424
    • (2002) Proc. Natl. Acad. Sci. , vol.99 , pp. 13419-13424
    • Reeves, P.J.1    Callewaert, N.2    Contreras, R.3    Khorana, H.G.4
  • 79
    • 0032959440 scopus 로고    scopus 로고
    • Overview of N- and O-linked oligosaccharide structures found in various yeast species
    • T.R. Gemmill, and R.B. Trimble Overview of N- and O-linked oligosaccharide structures found in various yeast species Biochim. Biophys. Acta Gen. Subj. 1426 1999 227 237
    • (1999) Biochim. Biophys. Acta Gen. Subj. , vol.1426 , pp. 227-237
    • Gemmill, T.R.1    Trimble, R.B.2
  • 80
    • 84973626000 scopus 로고    scopus 로고
    • 4.32 - Glycoengineering: Recombinant glycoproteins
    • H. Kamerling, Elsevier Oxford
    • M.J. Betenbaugh, N. Tomiya, and S. Narang 4.32 - glycoengineering: recombinant glycoproteins H. Kamerling, Comprehensive Glycoscience 2007 Elsevier Oxford 607 642
    • (2007) Comprehensive Glycoscience , pp. 607-642
    • Betenbaugh, M.J.1    Tomiya, N.2    Narang, S.3
  • 81
    • 36549015182 scopus 로고    scopus 로고
    • Production of humanized glycoproteins in bacteria and yeasts
    • Y. Chiba, and Y. Jigami Production of humanized glycoproteins in bacteria and yeasts Curr. Opin. Chem. Biol. 11 2007 670 676
    • (2007) Curr. Opin. Chem. Biol. , vol.11 , pp. 670-676
    • Chiba, Y.1    Jigami, Y.2
  • 89
    • 61449242817 scopus 로고    scopus 로고
    • Engineering complex-type N-glycosylation in Pichia pastoris using GlycoSwitch technology
    • P.P. Jacobs, S. Geysens, W. Vervecken, R. Contreras, and N. Callewaert Engineering complex-type N-glycosylation in Pichia pastoris using GlycoSwitch technology Nat. Protoc. 4 2008 58 70
    • (2008) Nat. Protoc. , vol.4 , pp. 58-70
    • Jacobs, P.P.1    Geysens, S.2    Vervecken, W.3    Contreras, R.4    Callewaert, N.5
  • 96
    • 46549088526 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis of glycopeptides and glycoproteins through endoglycosidase-catalyzed transglycosylation
    • L.-X. Wang Chemoenzymatic synthesis of glycopeptides and glycoproteins through endoglycosidase-catalyzed transglycosylation Carbohydr. Res. 343 2008 1509 1522
    • (2008) Carbohydr. Res. , vol.343 , pp. 1509-1522
    • Wang, L.-X.1
  • 97
    • 22144450662 scopus 로고    scopus 로고
    • Highly efficient endoglycosidase-catalyzed synthesis of glycopeptides using oligosaccharide oxazolines as donor substrates
    • B. Li, Y. Zeng, S. Hauser, H. Song, and L.-X. Wang Highly efficient endoglycosidase-catalyzed synthesis of glycopeptides using oligosaccharide oxazolines as donor substrates J. Am. Chem. Soc. 127 2005 9692 9693
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 9692-9693
    • Li, B.1    Zeng, Y.2    Hauser, S.3    Song, H.4    Wang, L.-X.5
  • 98
    • 33746608497 scopus 로고    scopus 로고
    • A highly efficient chemoenzymatic approach toward glycoprotein synthesis
    • B. Li, H. Song, S. Hauser, and L.-X. Wang A highly efficient chemoenzymatic approach toward glycoprotein synthesis Org. Lett. 8 2006 3081 3084
    • (2006) Org. Lett. , vol.8 , pp. 3081-3084
    • Li, B.1    Song, H.2    Hauser, S.3    Wang, L.-X.4
  • 100
    • 84864238717 scopus 로고    scopus 로고
    • Chemoenzymatic glycoengineering of intact IgG antibodies for gain of functions
    • W. Huang, J. Giddens, S.-Q. Fan, C. Toonstra, and L.-X. Wang Chemoenzymatic glycoengineering of intact IgG antibodies for gain of functions J. Am. Chem. Soc. 134 2012 12308 12318
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 12308-12318
    • Huang, W.1    Giddens, J.2    Fan, S.-Q.3    Toonstra, C.4    Wang, L.-X.5
  • 101
    • 41949130819 scopus 로고    scopus 로고
    • Mutants of mucor hiemalis endo-β-N-acetylglucosaminidase show enhanced transglycosylation and glycosynthase-like activities
    • M. Umekawa, W. Huang, B. Li, K. Fujita, H. Ashida, L.-X. Wang, and K. Yamamoto Mutants of mucor hiemalis endo-β-N-acetylglucosaminidase show enhanced transglycosylation and glycosynthase-like activities J. Biol. Chem. 283 2008 4469 4479
    • (2008) J. Biol. Chem. , vol.283 , pp. 4469-4479
    • Umekawa, M.1    Huang, W.2    Li, B.3    Fujita, K.4    Ashida, H.5    Wang, L.-X.6    Yamamoto, K.7
  • 102
    • 67749122310 scopus 로고    scopus 로고
    • Glycosynthases enable a highly efficient chemoenzymatic synthesis of N-glycoproteins carrying intact natural N-glycans
    • W. Huang, C. Li, B. Li, M. Umekawa, K. Yamamoto, X. Zhang, and L.-X. Wang Glycosynthases enable a highly efficient chemoenzymatic synthesis of N-glycoproteins carrying intact natural N-glycans J. Am. Chem. Soc. 131 2009 2214 2223
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 2214-2223
    • Huang, W.1    Li, C.2    Li, B.3    Umekawa, M.4    Yamamoto, K.5    Zhang, X.6    Wang, L.-X.7
  • 104
    • 52949115690 scopus 로고    scopus 로고
    • Glycoengineering of human IgG1-Fc through combined yeast expression and in vitro chemoenzymatic glycosylation
    • Y. Wei, C. Li, W. Huang, B. Li, S. Strome, and L.-X. Wang Glycoengineering of human IgG1-Fc through combined yeast expression and in vitro chemoenzymatic glycosylation Biochemistry 47 2008 10294 10304
    • (2008) Biochemistry , vol.47 , pp. 10294-10304
    • Wei, Y.1    Li, C.2    Huang, W.3    Li, B.4    Strome, S.5    Wang, L.-X.6
  • 105
    • 83055166012 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis and Fcγ receptor binding of homogeneous glycoforms of antibody Fc domain. Presence of a bisecting sugar moiety enhances the affinity of Fc to FcγIIIa receptor
    • G. Zou, H. Ochiai, W. Huang, Q. Yang, C. Li, and L.-X. Wang Chemoenzymatic synthesis and Fcγ receptor binding of homogeneous glycoforms of antibody Fc domain. Presence of a bisecting sugar moiety enhances the affinity of Fc to FcγIIIa receptor J. Am. Chem. Soc. 133 2011 18975 18991
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 18975-18991
    • Zou, G.1    Ochiai, H.2    Huang, W.3    Yang, Q.4    Li, C.5    Wang, L.-X.6
  • 107
    • 84957369935 scopus 로고    scopus 로고
    • Chemoenzymatic glyco-engineering of monoclonal antibodies
    • A. Castilho, Springer New York
    • J. Giddens, and L.-X. Wang Chemoenzymatic glyco-engineering of monoclonal antibodies A. Castilho, Glyco-Engineering 1321 2015 Springer New York 375 387
    • (2015) Glyco-Engineering , vol.1321 , pp. 375-387
    • Giddens, J.1    Wang, L.-X.2
  • 108
    • 28444495153 scopus 로고    scopus 로고
    • IgG subclass-independent improvement of antibody-dependent cellular cytotoxicity by fucose removal from Asn297-linked oligosaccharides
    • R. Niwa, A. Natsume, A. Uehara, M. Wakitani, S. Iida, K. Uchida, M. Satoh, and K. Shitara IgG subclass-independent improvement of antibody-dependent cellular cytotoxicity by fucose removal from Asn297-linked oligosaccharides J. Immunol. Methods 306 2005 151 160
    • (2005) J. Immunol. Methods , vol.306 , pp. 151-160
    • Niwa, R.1    Natsume, A.2    Uehara, A.3    Wakitani, M.4    Iida, S.5    Uchida, K.6    Satoh, M.7    Shitara, K.8
  • 109
    • 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
    • A. Natsume, M. Wakitani, N. Yamane-Ohnuki, E. Shoji-Hosaka, R. Niwa, K. Uchida, M. Satoh, and K. Shitara 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 J. Immunol. Methods 306 2005 93 103
    • (2005) J. Immunol. Methods , vol.306 , pp. 93-103
    • Natsume, A.1    Wakitani, M.2    Yamane-Ohnuki, N.3    Shoji-Hosaka, E.4    Niwa, R.5    Uchida, K.6    Satoh, M.7    Shitara, K.8
  • 110
    • 16844381436 scopus 로고    scopus 로고
    • Enhanced natural killer cell binding and activation by low-fucose igg1 antibody results in potent antibody-dependent cellular cytotoxicity induction at lower antigen density
    • R. Niwa, M. Sakurada, Y. Kobayashi, A. Uehara, K. Matsushima, R. Ueda, K. Nakamura, and K. Shitara Enhanced natural killer cell binding and activation by low-fucose igg1 antibody results in potent antibody-dependent cellular cytotoxicity induction at lower antigen density Clin. Cancer Res. 11 2005 2327 2336
    • (2005) Clin. Cancer Res. , vol.11 , pp. 2327-2336
    • Niwa, R.1    Sakurada, M.2    Kobayashi, Y.3    Uehara, A.4    Matsushima, K.5    Ueda, R.6    Nakamura, K.7    Shitara, K.8
  • 111
    • 34247215987 scopus 로고    scopus 로고
    • Enhanced binding affinity for FcγRIIIa of fucose-negative antibody is sufficient to induce maximal antibody-dependent cellular cytotoxicity
    • K. Masuda, T. Kubota, E. Kaneko, S. Iida, M. Wakitani, Y. Kobayashi-Natsume, A. Kubota, K. Shitara, and K. Nakamura Enhanced binding affinity for FcγRIIIa of fucose-negative antibody is sufficient to induce maximal antibody-dependent cellular cytotoxicity Mol. Immunol. 44 2007 3122 3131
    • (2007) Mol. Immunol. , vol.44 , pp. 3122-3131
    • Masuda, K.1    Kubota, T.2    Kaneko, E.3    Iida, S.4    Wakitani, M.5    Kobayashi-Natsume, Y.6    Kubota, A.7    Shitara, K.8    Nakamura, K.9
  • 112
    • 0036464719 scopus 로고    scopus 로고
    • Therapeutic activity of humanized anti-CD20 monoclonal antibody and polymorphism in IgG Fc receptor FcγRIIIa gene
    • G. Cartron, L. Dacheux, G. Salles, P. Solal-Celigny, P. Bardos, P. Colombat, and H. Watier Therapeutic activity of humanized anti-CD20 monoclonal antibody and polymorphism in IgG Fc receptor FcγRIIIa gene Blood 99 2002 754 758
    • (2002) Blood , vol.99 , pp. 754-758
    • Cartron, G.1    Dacheux, L.2    Salles, G.3    Solal-Celigny, P.4    Bardos, P.5    Colombat, P.6    Watier, H.7
  • 113
    • 0642373290 scopus 로고    scopus 로고
    • Two immunoglobulin G fragment C receptor polymorphisms independently predict response to rituximab in patients with follicular lymphoma
    • W.-K. Weng, and R. Levy Two immunoglobulin G fragment C receptor polymorphisms independently predict response to rituximab in patients with follicular lymphoma J. Clin. Oncol. 21 2003 3940 3947
    • (2003) J. Clin. Oncol. , vol.21 , pp. 3940-3947
    • Weng, W.-K.1    Levy, R.2
  • 114
    • 3042743884 scopus 로고    scopus 로고
    • Rituximab-dependent cytotoxicity by natural killer cells: Influence of FCGR3A polymorphism on the concentration-effect relationship
    • S. Dall'Ozzo, S. Tartas, G. Paintaud, G. Cartron, P. Colombat, P. Bardos, H. Watier, and G. Thibault Rituximab-dependent cytotoxicity by natural killer cells: influence of FCGR3A polymorphism on the concentration-effect relationship Cancer Res. 64 2004 4664 4669
    • (2004) Cancer Res. , vol.64 , pp. 4664-4669
    • Dall'Ozzo, S.1    Tartas, S.2    Paintaud, G.3    Cartron, G.4    Colombat, P.5    Bardos, P.6    Watier, H.7    Thibault, G.8
  • 116
    • 12144289636 scopus 로고    scopus 로고
    • Defucosylated chimeric anti-CC chemokine receptor 4 IgG1 with enhanced antibody-dependent cellular cytotoxicity shows potent therapeutic activity to T-cell leukemia and lymphoma
    • R. Niwa, E. Shoji-Hosaka, M. Sakurada, T. Shinkawa, K. Uchida, K. Nakamura, K. Matsushima, R. Ueda, N. Hanai, and K. Shitara Defucosylated chimeric anti-CC chemokine receptor 4 IgG1 with enhanced antibody-dependent cellular cytotoxicity shows potent therapeutic activity to T-cell leukemia and lymphoma Cancer Res. 64 2004 2127 2133
    • (2004) Cancer Res. , vol.64 , pp. 2127-2133
    • Niwa, R.1    Shoji-Hosaka, E.2    Sakurada, M.3    Shinkawa, T.4    Uchida, K.5    Nakamura, K.6    Matsushima, K.7    Ueda, R.8    Hanai, N.9    Shitara, K.10
  • 117
    • 79953183947 scopus 로고    scopus 로고
    • Mechanism of action of type II, glycoengineered, anti-CD20 monoclonal antibody GA101 in B-chronic lymphocytic leukemia whole blood assays in comparison with rituximab and alemtuzumab
    • L. Bologna, E. Gotti, M. Manganini, A. Rambaldi, T. Intermesoli, M. Introna, and J. Golay Mechanism of action of type II, glycoengineered, anti-CD20 monoclonal antibody GA101 in B-chronic lymphocytic leukemia whole blood assays in comparison with rituximab and alemtuzumab J. Immunol. 186 2011 3762 3769
    • (2011) J. Immunol. , vol.186 , pp. 3762-3769
    • Bologna, L.1    Gotti, E.2    Manganini, M.3    Rambaldi, A.4    Intermesoli, T.5    Introna, M.6    Golay, J.7
  • 124
    • 0028234702 scopus 로고
    • Fanger, Role of Fc gamma receptors in cancer and infectious disease
    • A.L. Wallace, and M.W. Howell Fanger, Role of Fc gamma receptors in cancer and infectious disease Journal of Leukocyte Biology 55 1994 816 826
    • (1994) Journal of Leukocyte Biology , vol.55 , pp. 816-826
    • Wallace, A.L.1    Howell, M.W.2
  • 125
    • 3042743884 scopus 로고    scopus 로고
    • Rituximab-dependent cytotoxicity by natural killer cells: Influence of FCGR3A polymorphism on the concentration-ffect relationship
    • S. Dall'Ozzo, S. Tartas, G. Paintaud, G. Cartron, P. Colombat, P. Bardos, H. Watier, and G. Thibault Rituximab-dependent cytotoxicity by natural killer cells: influence of FCGR3A polymorphism on the concentration-ffect relationship Cancer Res. 64 2004 4664 4669
    • (2004) Cancer Res. , vol.64 , pp. 4664-4669
    • Dall'Ozzo, S.1    Tartas, S.2    Paintaud, G.3    Cartron, G.4    Colombat, P.5    Bardos, P.6    Watier, H.7    Thibault, G.8
  • 126
    • 11144256170 scopus 로고    scopus 로고
    • Anatomy of a murder - Signal transduction pathways leading to activation of natural killer cells
    • S. Zompi, and F. Colucci Anatomy of a murder - signal transduction pathways leading to activation of natural killer cells Immunol. Lett. 97 2005 31 39
    • (2005) Immunol. Lett. , vol.97 , pp. 31-39
    • Zompi, S.1    Colucci, F.2
  • 127
    • 0030584826 scopus 로고    scopus 로고
    • Fc receptor-induced expression of Fas ligand on activated NK cells facilitates cell-mediated cytotoxicity and subsequent autocrine NK cell apoptosis
    • C.M. Eischen, J.D. Schilling, D.H. Lynch, P.H. Krammer, and P.J. Leibson Fc receptor-induced expression of Fas ligand on activated NK cells facilitates cell-mediated cytotoxicity and subsequent autocrine NK cell apoptosis J. Immunol. 156 1996 2693 2699
    • (1996) J. Immunol. , vol.156 , pp. 2693-2699
    • Eischen, C.M.1    Schilling, J.D.2    Lynch, D.H.3    Krammer, P.H.4    Leibson, P.J.5
  • 128
    • 0019480946 scopus 로고
    • Monocyte-mediated antibody-dependent cell-mediated cytotoxicity: The role of the metabolic burst
    • C. Koller, and A. LoBuglio Monocyte-mediated antibody-dependent cell-mediated cytotoxicity: the role of the metabolic burst Blood 58 1981 293 299
    • (1981) Blood , vol.58 , pp. 293-299
    • Koller, C.1    LoBuglio, A.2
  • 129
    • 84858863479 scopus 로고    scopus 로고
    • Both activating and inhibitory Fc gamma receptors mediate rituximab-induced trogocytosis of CD20 in mice
    • P. Boross, J.H.M. Jansen, A. Pastula, C.E. van der Poel, and J.H.W. Leusen Both activating and inhibitory Fc gamma receptors mediate rituximab-induced trogocytosis of CD20 in mice Immunol. Lett. 143 2012 44 52
    • (2012) Immunol. Lett. , vol.143 , pp. 44-52
    • Boross, P.1    Jansen, J.H.M.2    Pastula, A.3    Van Der Poel, C.E.4    Leusen, J.H.W.5
  • 131
    • 30344434022 scopus 로고    scopus 로고
    • High concentrations of therapeutic IgG1 antibodies are needed to compensate for inhibition of antibody-dependent cellular cytotoxicity by excess endogenous immunoglobulin G
    • S. Preithner, S. Elm, S. Lippold, M. Locher, A. Wolf, A.J.Dd. Silva, P.A. Baeuerle, and N.S. Prang High concentrations of therapeutic IgG1 antibodies are needed to compensate for inhibition of antibody-dependent cellular cytotoxicity by excess endogenous immunoglobulin G Mol. Immunol. 43 2006 1183 1193
    • (2006) Mol. Immunol. , vol.43 , pp. 1183-1193
    • Preithner, S.1    Elm, S.2    Lippold, S.3    Locher, M.4    Wolf, A.5    Silva, A.J.Dd.6    Baeuerle, P.A.7    Prang, N.S.8
  • 132
    • 3042606229 scopus 로고    scopus 로고
    • Rituximab-mediated depletion of cynomolgus monkey B cells in vitro in different matrices: Possible inhibitory effect of IgG
    • Y. Vugmeyster, and K. Howell Rituximab-mediated depletion of cynomolgus monkey B cells in vitro in different matrices: possible inhibitory effect of IgG Int. Immunopharmacol. 4 2004 1117 1124
    • (2004) Int. Immunopharmacol. , vol.4 , pp. 1117-1124
    • Vugmeyster, Y.1    Howell, K.2
  • 133
    • 61849148375 scopus 로고    scopus 로고
    • Two mechanisms of the enhanced antibody-dependent cellular cytotoxicity (ADCC) efficacy of non-fucosylated therapeutic antibodies in human blood
    • S. Iida, R. Kuni-Kamochi, K. Mori, H. Misaka, M. Inoue, A. Okazaki, K. Shitara, and M. Satoh Two mechanisms of the enhanced antibody-dependent cellular cytotoxicity (ADCC) efficacy of non-fucosylated therapeutic antibodies in human blood BMC Cancer 9 2009 1 12
    • (2009) BMC Cancer , vol.9 , pp. 1-12
    • Iida, S.1    Kuni-Kamochi, R.2    Mori, K.3    Misaka, H.4    Inoue, M.5    Okazaki, A.6    Shitara, K.7    Satoh, M.8
  • 134
    • 33751322142 scopus 로고    scopus 로고
    • Compensation of endogenous IgG mediated inhibition of antibody-dependent cellular cytotoxicity by glyco-engineering of therapeutic antibodies
    • A. Nechansky, M. Schuster, W. Jost, P. Siegl, S. Wiederkum, G. Gorr, and R. Kircheis Compensation of endogenous IgG mediated inhibition of antibody-dependent cellular cytotoxicity by glyco-engineering of therapeutic antibodies Mol. Immunol. 44 2007 1815 1817
    • (2007) Mol. Immunol. , vol.44 , pp. 1815-1817
    • Nechansky, A.1    Schuster, M.2    Jost, W.3    Siegl, P.4    Wiederkum, S.5    Gorr, G.6    Kircheis, R.7
  • 135
    • 30344434022 scopus 로고    scopus 로고
    • High concentrations of therapeutic IgG1 antibodies are needed to compensate for inhibition of antibody-dependent cellular cytotoxicity by excess endogenous immunoglobulin G
    • S. Preithner, S. Elm, S. Lippold, M. Locher, A. Wolf, A.J. da Silva, P.A. Baeuerle, and N.S. Prang High concentrations of therapeutic IgG1 antibodies are needed to compensate for inhibition of antibody-dependent cellular cytotoxicity by excess endogenous immunoglobulin G Mol. Immunol. 43 2006 1183 1193
    • (2006) Mol. Immunol. , vol.43 , pp. 1183-1193
    • Preithner, S.1    Elm, S.2    Lippold, S.3    Locher, M.4    Wolf, A.5    Da Silva, A.J.6    Baeuerle, P.A.7    Prang, N.S.8
  • 136
    • 0022005365 scopus 로고
    • The concentration of IgG in the serum is a major determinant of Fc-dependent reticuloendothelial function
    • J.G. Kelton, J. Singer, C. Rodger, J. Gauldie, P. Horsewood, and P. Dent The concentration of IgG in the serum is a major determinant of Fc-dependent reticuloendothelial function Blood 66 1985 490 495
    • (1985) Blood , vol.66 , pp. 490-495
    • Kelton, J.G.1    Singer, J.2    Rodger, C.3    Gauldie, J.4    Horsewood, P.5    Dent, P.6
  • 138
    • 84922807192 scopus 로고    scopus 로고
    • The current status and prospects of antibody engineering for therapeutic use: Focus on glycoengineering technology
    • R. Niwa, and M. Satoh The current status and prospects of antibody engineering for therapeutic use: focus on glycoengineering technology J. Pharm. Sci. 104 2015 930 941
    • (2015) J. Pharm. Sci. , vol.104 , pp. 930-941
    • Niwa, R.1    Satoh, M.2
  • 139
    • 59749104215 scopus 로고    scopus 로고
    • Nonfucosylated rituximab potentiates human neutrophil phagocytosis through its high binding for FcγRIIIb and MHC class II expression on the phagocytotic neutrophils
    • M. Shibata-Koyama, S. Iida, H. Misaka, K. Mori, K. Yano, K. Shitara, and M. Satoh Nonfucosylated rituximab potentiates human neutrophil phagocytosis through its high binding for FcγRIIIb and MHC class II expression on the phagocytotic neutrophils Exp. Hematol. 37 2009 309 321
    • (2009) Exp. Hematol. , vol.37 , pp. 309-321
    • Shibata-Koyama, M.1    Iida, S.2    Misaka, H.3    Mori, K.4    Yano, K.5    Shitara, K.6    Satoh, M.7
  • 140
    • 79953736960 scopus 로고    scopus 로고
    • The broadly neutralizing HIV-1 IgG 2F5 elicits gp41-specific antibody-dependent cell cytotoxicity in a FcgammaRI-dependent manner
    • D. Tudor, and M. Bomsel The broadly neutralizing HIV-1 IgG 2F5 elicits gp41-specific antibody-dependent cell cytotoxicity in a FcgammaRI-dependent manner AIDS (London, England) 25 2011 751 759
    • (2011) AIDS (London, England) , vol.25 , pp. 751-759
    • Tudor, D.1    Bomsel, M.2
  • 141
    • 0034076307 scopus 로고    scopus 로고
    • Inhibitory Fc receptors modulate in vivo cytoxicity against tumor targets
    • R.A. Clynes, T.L. Towers, L.G. Presta, and J.V. Ravetch Inhibitory Fc receptors modulate in vivo cytoxicity against tumor targets Nat. Med. 6 2000 443 446
    • (2000) Nat. Med. , vol.6 , pp. 443-446
    • Clynes, R.A.1    Towers, T.L.2    Presta, L.G.3    Ravetch, J.V.4
  • 142
    • 51649123832 scopus 로고    scopus 로고
    • Lymphoma depletion during CD20 immunotherapy in mice is mediated by macrophage FcγRI, FcγRIII, and FcγRIV
    • V. Minard-Colin, Y. Xiu, J.C. Poe, M. Horikawa, C.M. Magro, Y. Hamaguchi, K.M. Haas, and T.F. Tedder Lymphoma depletion during CD20 immunotherapy in mice is mediated by macrophage FcγRI, FcγRIII, and FcγRIV Blood 112 2008 1205 1213
    • (2008) Blood , vol.112 , pp. 1205-1213
    • Minard-Colin, V.1    Xiu, Y.2    Poe, J.C.3    Horikawa, M.4    Magro, C.M.5    Hamaguchi, Y.6    Haas, K.M.7    Tedder, T.F.8
  • 144
    • 31544442680 scopus 로고    scopus 로고
    • Pathogenic autoantibodies: Emerging insights into tissue injury
    • P.-L. Lim, and M. Zouali Pathogenic autoantibodies: emerging insights into tissue injury Immunol. Lett. 103 2006 17 26
    • (2006) Immunol. Lett. , vol.103 , pp. 17-26
    • Lim, P.-L.1    Zouali, M.2
  • 145
    • 2342523339 scopus 로고    scopus 로고
    • Autoantibodies as predictors of disease
    • R.H. Scofield Autoantibodies as predictors of disease Lancet 363 2004 1544 1546
    • (2004) Lancet , vol.363 , pp. 1544-1546
    • Scofield, R.H.1
  • 146
    • 38149006291 scopus 로고    scopus 로고
    • Arthritogenic antibodies specific for a major type II collagen triple-helical epitope bind and destabilize cartilage independent of inflammation
    • K.S. Nandakumar, E. Bajtner, L. Hill, B. Böhm, M.J. Rowley, H. Burkhardt, and R. Holmdahl Arthritogenic antibodies specific for a major type II collagen triple-helical epitope bind and destabilize cartilage independent of inflammation Arthritis Rheum. 58 2008 184 196
    • (2008) Arthritis Rheum. , vol.58 , pp. 184-196
    • Nandakumar, K.S.1    Bajtner, E.2    Hill, L.3    Böhm, B.4    Rowley, M.J.5    Burkhardt, H.6    Holmdahl, R.7
  • 148
    • 28444460336 scopus 로고    scopus 로고
    • Mechanisms of blister induction by autoantibodies
    • C. Sitaru, and D. Zillikens Mechanisms of blister induction by autoantibodies Exp. Dermatol. 14 2005 861 875
    • (2005) Exp. Dermatol. , vol.14 , pp. 861-875
    • Sitaru, C.1    Zillikens, D.2
  • 149
    • 34248150428 scopus 로고    scopus 로고
    • The relevance of the IgG subclass of autoantibodies for blister induction in autoimmune bullous skin diseases
    • C. Sitaru, S. Mihai, and D. Zillikens The relevance of the IgG subclass of autoantibodies for blister induction in autoimmune bullous skin diseases Arch. Dermatol. Res. 299 2007 1 8
    • (2007) Arch. Dermatol. Res. , vol.299 , pp. 1-8
    • Sitaru, C.1    Mihai, S.2    Zillikens, D.3
  • 150
    • 25844480988 scopus 로고    scopus 로고
    • Antibody-mediated organ-allograft rejection
    • R.B. Colvin, and R.N. Smith Antibody-mediated organ-allograft rejection Nat. Rev. Immunol. 5 2005 807 817
    • (2005) Nat. Rev. Immunol. , vol.5 , pp. 807-817
    • Colvin, R.B.1    Smith, R.N.2
  • 151
    • 69949159693 scopus 로고    scopus 로고
    • Sugar-free antibodies - The bacterial solution to autoimmunity?
    • M. Allhorn, and M. Collin Sugar-free antibodies - the bacterial solution to autoimmunity? Ann. N. Y. Acad. Sci. 1173 2009 664 669
    • (2009) Ann. N. Y. Acad. Sci. , vol.1173 , pp. 664-669
    • Allhorn, M.1    Collin, M.2
  • 152
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • J. Hardy, and D.J. Selkoe The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics Science 297 2002 353 356
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 159
    • 33745001453 scopus 로고    scopus 로고
    • Deglycosylated anti-amyloid-β antibodies eliminate cognitive deficits and reduce parenchymal amyloid with minimal vascular consequences in aged amyloid precursor protein transgenic mice
    • D.M. Wilcock, J. Alamed, P.E. Gottschall, J. Grimm, A. Rosenthal, J. Pons, V. Ronan, K. Symmonds, M.N. Gordon, and D. Morgan Deglycosylated anti-amyloid-β antibodies eliminate cognitive deficits and reduce parenchymal amyloid with minimal vascular consequences in aged amyloid precursor protein transgenic mice J. Neurosci. 26 2006 5340 5346
    • (2006) J. Neurosci. , vol.26 , pp. 5340-5346
    • Wilcock, D.M.1    Alamed, J.2    Gottschall, P.E.3    Grimm, J.4    Rosenthal, A.5    Pons, J.6    Ronan, V.7    Symmonds, K.8    Gordon, M.N.9    Morgan, D.10
  • 161
    • 27144450504 scopus 로고    scopus 로고
    • Deglycosylation of anti-ß amyloid antibodies inhibits microglia activation in BV-2 cellular model
    • S. Rebe, and B. Solomon Deglycosylation of anti-ß amyloid antibodies inhibits microglia activation in BV-2 cellular model Am. J. Alzheimers Dis. Other Demen. 20 2005 303 313
    • (2005) Am. J. Alzheimers Dis. Other Demen. , vol.20 , pp. 303-313
    • Rebe, S.1    Solomon, B.2
  • 162
    • 33745111586 scopus 로고    scopus 로고
    • Intracranial administration of deglycosylated C-terminal-specific anti-Abeta antibody efficiently clears amyloid plaques without activating microglia in amyloid-depositing transgenic mice
    • N. Carty, D. Wilcock, A. Rosenthal, J. Grimm, J. Pons, V. Ronan, P. Gottschall, M. Gordon, and D. Morgan Intracranial administration of deglycosylated C-terminal-specific anti-Abeta antibody efficiently clears amyloid plaques without activating microglia in amyloid-depositing transgenic mice J. Neuroinflammation 3 2006 11
    • (2006) J. Neuroinflammation , vol.3 , pp. 11
    • Carty, N.1    Wilcock, D.2    Rosenthal, A.3    Grimm, J.4    Pons, J.5    Ronan, V.6    Gottschall, P.7    Gordon, M.8    Morgan, D.9
  • 163
    • 84873406959 scopus 로고    scopus 로고
    • Enzymatic deglycosylation converts pathogenic neuromyelitis optica anti-aquaporin-4 immunoglobulin G into therapeutic antibody
    • L. Tradtrantip, J. Ratelade, H. Zhang, and A.S. Verkman Enzymatic deglycosylation converts pathogenic neuromyelitis optica anti-aquaporin-4 immunoglobulin G into therapeutic antibody Ann. Neurol. 73 2013 77 85
    • (2013) Ann. Neurol. , vol.73 , pp. 77-85
    • Tradtrantip, L.1    Ratelade, J.2    Zhang, H.3    Verkman, A.S.4
  • 164
    • 84879304669 scopus 로고    scopus 로고
    • Inhibition of HPA-1a alloantibody-mediated platelet destruction by a deglycosylated anti-HPA-1a monoclonal antibody in mice: Toward targeted treatment of fetal-alloimmune thrombocytopenia
    • T. Bakchoul, A. Greinacher, U.J. Sachs, A. Krautwurst, H. Renz, H. Harb, G. Bein, P.J. Newman, and S. Santoso Inhibition of HPA-1a alloantibody-mediated platelet destruction by a deglycosylated anti-HPA-1a monoclonal antibody in mice: toward targeted treatment of fetal-alloimmune thrombocytopenia Blood 122 2013 321 327
    • (2013) Blood , vol.122 , pp. 321-327
    • Bakchoul, T.1    Greinacher, A.2    Sachs, U.J.3    Krautwurst, A.4    Renz, H.5    Harb, H.6    Bein, G.7    Newman, P.J.8    Santoso, S.9
  • 165
    • 54449089342 scopus 로고    scopus 로고
    • In vivo enzymatic modulation of IgG glycosylation inhibits autoimmune disease in an IgG subclass-dependent manner
    • H. Albert, M. Collin, D. Dudziak, J.V. Ravetch, and F. Nimmerjahn In vivo enzymatic modulation of IgG glycosylation inhibits autoimmune disease in an IgG subclass-dependent manner Proc. Natl. Acad. Sci. 105 2008 15005 15009
    • (2008) Proc. Natl. Acad. Sci. , vol.105 , pp. 15005-15009
    • Albert, H.1    Collin, M.2    Dudziak, D.3    Ravetch, J.V.4    Nimmerjahn, F.5
  • 168
    • 84864484027 scopus 로고    scopus 로고
    • IgG glycan hydrolysis by endoglycosidase S diminishes the proinflammatory properties of immune complexes from patients with systemic lupus erythematosus: A possible new treatment?
    • C. Lood, M. Allhorn, R. Lood, B. Gullstrand, A.I. Olin, L. Rönnblom, L. Truedsson, M. Collin, and A.A. Bengtsson IgG glycan hydrolysis by endoglycosidase S diminishes the proinflammatory properties of immune complexes from patients with systemic lupus erythematosus: a possible new treatment? Arthritis Rheum. 64 2012 2698 2706
    • (2012) Arthritis Rheum. , vol.64 , pp. 2698-2706
    • Lood, C.1    Allhorn, M.2    Lood, R.3    Gullstrand, B.4    Olin, A.I.5    Rönnblom, L.6    Truedsson, L.7    Collin, M.8    Bengtsson, A.A.9
  • 170
    • 0038782015 scopus 로고    scopus 로고
    • Extracellular enzymes with immunomodulating activities: Variations on a theme in Streptococcus pyogenes
    • M. Collin, and A. Olsén Extracellular enzymes with immunomodulating activities: variations on a theme in Streptococcus pyogenes Infect. Immun. 71 2003 2983 2992
    • (2003) Infect. Immun. , vol.71 , pp. 2983-2992
    • Collin, M.1    Olsén, A.2
  • 171
    • 84861804997 scopus 로고    scopus 로고
    • Selective deactivation of serum IgG: A general strategy for the enhancement of monoclonal antibody receptor interactions
    • K. Baruah, T.A. Bowden, B.A. Krishna, R.A. Dwek, M. Crispin, and C.N. Scanlan Selective deactivation of serum IgG: a general strategy for the enhancement of monoclonal antibody receptor interactions J. Mol. Biol. 420 2012 1 7
    • (2012) J. Mol. Biol. , vol.420 , pp. 1-7
    • Baruah, K.1    Bowden, T.A.2    Krishna, B.A.3    Dwek, R.A.4    Crispin, M.5    Scanlan, C.N.6
  • 172
    • 84857792795 scopus 로고    scopus 로고
    • Bacterial hydrolysis of host glycoproteins - Powerful protein modification and efficient nutrient acquisition
    • J. Garbe, and M. Collin Bacterial hydrolysis of host glycoproteins - powerful protein modification and efficient nutrient acquisition J. Innate Immun. 4 2012 121 131
    • (2012) J. Innate Immun. , vol.4 , pp. 121-131
    • Garbe, J.1    Collin, M.2
  • 174
    • 79957456998 scopus 로고    scopus 로고
    • Study of the IgG endoglycosidase EndoS in group A streptococcal phagocyte resistance and virulence
    • J. Sjögren, C.Y. Okumura, M. Collin, V. Nizet, and A. Hollands Study of the IgG endoglycosidase EndoS in group A streptococcal phagocyte resistance and virulence BMC Microbiol. 11 2011 1 7
    • (2011) BMC Microbiol. , vol.11 , pp. 1-7
    • Sjögren, J.1    Okumura, C.Y.2    Collin, M.3    Nizet, V.4    Hollands, A.5
  • 175
    • 41949141128 scopus 로고    scopus 로고
    • IgG glycan hydrolysis by a bacterial enzyme as a therapy against autoimmune conditions
    • M. Collin, O. Shannon, and L. Björck IgG glycan hydrolysis by a bacterial enzyme as a therapy against autoimmune conditions Proc. Natl. Acad. Sci. 105 2008 4265 4270
    • (2008) Proc. Natl. Acad. Sci. , vol.105 , pp. 4265-4270
    • Collin, M.1    Shannon, O.2    Björck, L.3
  • 178
    • 0037330259 scopus 로고    scopus 로고
    • IdeS and SpeB: Immunoglobulin-degrading cysteine proteinases of Streptococcus pyogenes
    • U. von Pawel-Rammingen, and L. Björck IdeS and SpeB: immunoglobulin-degrading cysteine proteinases of Streptococcus pyogenes Curr. Opin. Microbiol. 6 2003 50 55
    • (2003) Curr. Opin. Microbiol. , vol.6 , pp. 50-55
    • Von Pawel-Rammingen, U.1    Björck, L.2
  • 179
    • 84884230691 scopus 로고    scopus 로고
    • EndoS2 is a unique and conserved enzyme of serotype M49 group A Streptococcus that hydrolyses N-linked glycans on IgG and alpha1-acid glycoprotein
    • J. Sjogren, W.B. Struwe, E.F. Cosgrave, P.M. Rudd, M. Stervander, M. Allhorn, A. Hollands, V. Nizet, and M. Collin EndoS2 is a unique and conserved enzyme of serotype M49 group A Streptococcus that hydrolyses N-linked glycans on IgG and alpha1-acid glycoprotein Biochem. J. 455 2013 107 118
    • (2013) Biochem. J. , vol.455 , pp. 107-118
    • Sjogren, J.1    Struwe, W.B.2    Cosgrave, E.F.3    Rudd, P.M.4    Stervander, M.5    Allhorn, M.6    Hollands, A.7    Nizet, V.8    Collin, M.9
  • 180
    • 33845590523 scopus 로고    scopus 로고
    • Comparison of biological activity among nonfucosylated therapeutic IgG1 antibodies with three different N-linked Fc oligosaccharides: The high-mannose, hybrid, and complex types
    • Y. Kanda, T. Yamada, K. Mori, A. Okazaki, M. Inoue, K. Kitajima-Miyama, R. Kuni-Kamochi, R. Nakano, K. Yano, S. Kakita, K. Shitara, and M. Satoh Comparison of biological activity among nonfucosylated therapeutic IgG1 antibodies with three different N-linked Fc oligosaccharides: the high-mannose, hybrid, and complex types Glycobiology 17 2007 104 118
    • (2007) Glycobiology , vol.17 , pp. 104-118
    • Kanda, Y.1    Yamada, T.2    Mori, K.3    Okazaki, A.4    Inoue, M.5    Kitajima-Miyama, K.6    Kuni-Kamochi, R.7    Nakano, R.8    Yano, K.9    Kakita, S.10    Shitara, K.11    Satoh, M.12
  • 181
    • 38449115463 scopus 로고    scopus 로고
    • Development of a simple and rapid method for producing non-fucosylated oligomannose containing antibodies with increased effector function
    • Q. Zhou, S. Shankara, A. Roy, H. Qiu, S. Estes, A. McVie-Wylie, K. Culm-Merdek, A. Park, C. Pan, and T. Edmunds Development of a simple and rapid method for producing non-fucosylated oligomannose containing antibodies with increased effector function Biotechnol. Bioeng. 99 2008 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
  • 183
    • 33644619972 scopus 로고    scopus 로고
    • Heterogeneity of recombinant antibodies: Linking structure to function
    • R.J. Harris Heterogeneity of recombinant antibodies: linking structure to function Dev. Biol. 122 2005 117 127
    • (2005) Dev. Biol. , vol.122 , pp. 117-127
    • Harris, R.J.1
  • 184
    • 79958837668 scopus 로고    scopus 로고
    • High-mannose glycans on the Fc region of therapeutic IgG antibodies increase serum clearance in humans
    • A.M. Goetze, Y.D. Liu, Z. Zhang, B. Shah, E. Lee, P.V. Bondarenko, and G.C. Flynn High-mannose glycans on the Fc region of therapeutic IgG antibodies increase serum clearance in humans Glycobiology 21 2011 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
  • 186
    • 33644530355 scopus 로고    scopus 로고
    • Differences between IGIV products: Impact on clinical outcome
    • E.W. Gelfand Differences between IGIV products: impact on clinical outcome Int. Immunopharmacol. 6 2006 592 599
    • (2006) Int. Immunopharmacol. , vol.6 , pp. 592-599
    • Gelfand, E.W.1
  • 187
    • 34248576453 scopus 로고    scopus 로고
    • Efficacy of various intravenous immunoglobulin therapy protocols in autoimmune and chronic inflammatory disorders
    • H.M. Gürcan, and A.R. Ahmed Efficacy of various intravenous immunoglobulin therapy protocols in autoimmune and chronic inflammatory disorders Ann. Pharmacother. 41 2007 812 823
    • (2007) Ann. Pharmacother. , vol.41 , pp. 812-823
    • Gürcan, H.M.1    Ahmed, A.R.2
  • 188
    • 42649089750 scopus 로고    scopus 로고
    • Anti-inflammatory actions of intravenous immunoglobulin
    • F. Nimmerjahn, and J.V. Ravetch Anti-inflammatory actions of intravenous immunoglobulin Annu. Rev. Immunol. 26 2008 513 533
    • (2008) Annu. Rev. Immunol. , vol.26 , pp. 513-533
    • Nimmerjahn, F.1    Ravetch, J.V.2
  • 190
    • 79551488012 scopus 로고    scopus 로고
    • The IgG molecule as a biological immune response modifier: Mechanisms of action of intravenous immune serum globulin in autoimmune and inflammatory disorders
    • M. Ballow The IgG molecule as a biological immune response modifier: mechanisms of action of intravenous immune serum globulin in autoimmune and inflammatory disorders J. Allergy Clin. Immunol. 127 2011 315 323
    • (2011) J. Allergy Clin. Immunol. , vol.127 , pp. 315-323
    • Ballow, M.1
  • 191
    • 84875410765 scopus 로고    scopus 로고
    • Intravenous immunoglobulin therapy: How does IgG modulate the immune system?
    • I. Schwab, and F. Nimmerjahn Intravenous immunoglobulin therapy: how does IgG modulate the immune system? Nat. Rev. Immunol. 13 2013 176 189
    • (2013) Nat. Rev. Immunol. , vol.13 , pp. 176-189
    • Schwab, I.1    Nimmerjahn, F.2
  • 192
    • 84901421934 scopus 로고    scopus 로고
    • Fragments of truth: T-cell targets of polyclonal immunoglobulins in autoimmune diseases
    • F. Petta, C. De Luca, M. Triggiani, and V. Casolaro Fragments of truth: T-cell targets of polyclonal immunoglobulins in autoimmune diseases Curr. Opin. Pharmacol. 17 2014 1 11
    • (2014) Curr. Opin. Pharmacol. , vol.17 , pp. 1-11
    • Petta, F.1    De Luca, C.2    Triggiani, M.3    Casolaro, V.4
  • 193
    • 0024836531 scopus 로고
    • Antiidiotypes against autoantibodies in pooled normal human polyspecific Ig
    • F. Rossi, and M.D. Kazatchkine Antiidiotypes against autoantibodies in pooled normal human polyspecific Ig J. Immunol. 143 1989 4104 4109
    • (1989) J. Immunol. , vol.143 , pp. 4104-4109
    • Rossi, F.1    Kazatchkine, M.D.2
  • 195
    • 0347364814 scopus 로고    scopus 로고
    • Concurrent presence of agonistic and antagonistic anti-CD95 autoantibodies in intravenous Ig preparations
    • F. Altznauer, S. von Gunten, P. Späth, and H.-U. Simon Concurrent presence of agonistic and antagonistic anti-CD95 autoantibodies in intravenous Ig preparations J. Allergy Clin. Immunol. 112 2003 1185 1190
    • (2003) J. Allergy Clin. Immunol. , vol.112 , pp. 1185-1190
    • Altznauer, F.1    Von Gunten, S.2    Späth, P.3    Simon, H.-U.4
  • 199
    • 84928963187 scopus 로고    scopus 로고
    • Protection in antibody- and T cell-mediated autoimmune diseases by antiinflammatory IgG Fcs requires type II FcRs
    • B.M. Fiebiger, J. Maamary, A. Pincetic, and J.V. Ravetch Protection in antibody- and T cell-mediated autoimmune diseases by antiinflammatory IgG Fcs requires type II FcRs Proc. Natl. Acad. Sci. 112 2015 E2385 E2394
    • (2015) Proc. Natl. Acad. Sci. , vol.112 , pp. E2385-E2394
    • Fiebiger, B.M.1    Maamary, J.2    Pincetic, A.3    Ravetch, J.V.4
  • 200
    • 84879385142 scopus 로고    scopus 로고
    • Beneficial effect of a multimerized immunoglobulin Fc in an animal model of inflammatory neuropathy (experimental autoimmune neuritis)
    • M. Niknami, M.-X. Wang, T. Nguyen, and J.D. Pollard Beneficial effect of a multimerized immunoglobulin Fc in an animal model of inflammatory neuropathy (experimental autoimmune neuritis) J. Peripher. Nerv. Syst. 18 2013 141 152
    • (2013) J. Peripher. Nerv. Syst. , vol.18 , pp. 141-152
    • Niknami, M.1    Wang, M.-X.2    Nguyen, T.3    Pollard, J.D.4
  • 202
    • 84904320258 scopus 로고    scopus 로고
    • Recombinant IgG2a Fc (M045) multimers effectively suppress experimental autoimmune myasthenia gravis
    • M. Thiruppathi, J.R. Sheng, L. Li, B.S. Prabhakar, and M.N. Meriggioli Recombinant IgG2a Fc (M045) multimers effectively suppress experimental autoimmune myasthenia gravis J. Autoimmun. 52 2014 64 73
    • (2014) J. Autoimmun. , vol.52 , pp. 64-73
    • Thiruppathi, M.1    Sheng, J.R.2    Li, L.3    Prabhakar, B.S.4    Meriggioli, M.N.5
  • 204
    • 33744989699 scopus 로고    scopus 로고
    • Intravenous immunoglobulin ameliorates ITP via activating Fc[gamma] receptors on dendritic cells
    • V. Siragam, A.R. Crow, D. Brinc, S. Song, J. Freedman, and A.H. Lazarus Intravenous immunoglobulin ameliorates ITP via activating Fc[gamma] receptors on dendritic cells Nat. Med. 12 2006 688 692
    • (2006) Nat. Med. , vol.12 , pp. 688-692
    • Siragam, V.1    Crow, A.R.2    Brinc, D.3    Song, S.4    Freedman, J.5    Lazarus, A.H.6
  • 205
    • 33846225960 scopus 로고    scopus 로고
    • FcγRIII-dependent inhibition of interferon-γ responses mediates suppressive effects of intravenous immune globulin
    • K.-H. Park-Min, N.V. Serbina, W. Yang, X. Ma, G. Krystal, B.G. Neel, S.L. Nutt, X. Hu, and L.B. Ivashkiv FcγRIII-dependent inhibition of interferon-γ responses mediates suppressive effects of intravenous immune globulin Immunity 26 2007 67 78
    • (2007) Immunity , vol.26 , pp. 67-78
    • Park-Min, K.-H.1    Serbina, N.V.2    Yang, W.3    Ma, X.4    Krystal, G.5    Neel, B.G.6    Nutt, S.L.7    Hu, X.8    Ivashkiv, L.B.9
  • 206
    • 0035910392 scopus 로고    scopus 로고
    • Anti-inflammatory activity of IVIG mediated through the inhibitory Fc receptor
    • A. Samuelsson, T.L. Towers, and J.V. Ravetch Anti-inflammatory activity of IVIG mediated through the inhibitory Fc receptor Science 291 2001 484 486
    • (2001) Science , vol.291 , pp. 484-486
    • Samuelsson, A.1    Towers, T.L.2    Ravetch, J.V.3
  • 207
    • 34250370468 scopus 로고    scopus 로고
    • Selective blockade of the inhibitory Fcγ receptor (FcγRIIB) in human dendritic cells and monocytes induces a type i interferon response program
    • K.M. Dhodapkar, D. Banerjee, J. Connolly, A. Kukreja, E. Matayeva, M.C. Veri, J.V. Ravetch, R.M. Steinman, and M.V. Dhodapkar Selective blockade of the inhibitory Fcγ receptor (FcγRIIB) in human dendritic cells and monocytes induces a type I interferon response program J. Exp. Med. 204 2007 1359 1369
    • (2007) J. Exp. Med. , vol.204 , pp. 1359-1369
    • Dhodapkar, K.M.1    Banerjee, D.2    Connolly, J.3    Kukreja, A.4    Matayeva, E.5    Veri, M.C.6    Ravetch, J.V.7    Steinman, R.M.8    Dhodapkar, M.V.9
  • 208
    • 12844251399 scopus 로고    scopus 로고
    • Restoration of tolerance in lupus by targeted inhibitory receptor expression
    • T.L. McGaha, B. Sorrentino, and J.V. Ravetch Restoration of tolerance in lupus by targeted inhibitory receptor expression Science 307 2005 590 593
    • (2005) Science , vol.307 , pp. 590-593
    • McGaha, T.L.1    Sorrentino, B.2    Ravetch, J.V.3
  • 209
    • 28544449847 scopus 로고    scopus 로고
    • Divergent immunoglobulin G subclass activity through selective Fc receptor binding
    • F. Nimmerjahn, and J.V. Ravetch Divergent immunoglobulin G subclass activity through selective Fc receptor binding Science 310 2005 1510 1512
    • (2005) Science , vol.310 , pp. 1510-1512
    • Nimmerjahn, F.1    Ravetch, J.V.2
  • 211
    • 0036918050 scopus 로고    scopus 로고
    • Intravenous immunoglobulin mediates an increase in anti-platelet antibody clearance via the FcRn receptor
    • R.J. Hansen, and J.P. Balthasar Intravenous immunoglobulin mediates an increase in anti-platelet antibody clearance via the FcRn receptor Thromb. Haemost. 88 2002 898 899
    • (2002) Thromb. Haemost. , vol.88 , pp. 898-899
    • Hansen, R.J.1    Balthasar, J.P.2
  • 213
    • 77956566546 scopus 로고    scopus 로고
    • IVIg modulates BCR signaling through CD22 and promotes apoptosis in mature human B lymphocytes
    • J.-F. Séïté, D. Cornec, Y. Renaudineau, P. Youinou, R.A. Mageed, and S. Hillion IVIg modulates BCR signaling through CD22 and promotes apoptosis in mature human B lymphocytes Blood 116 2010 1698 1704
    • (2010) Blood , vol.116 , pp. 1698-1704
    • Séïté, J.-F.1    Cornec, D.2    Renaudineau, Y.3    Youinou, P.4    Mageed, R.A.5    Hillion, S.6
  • 214
    • 58149378347 scopus 로고    scopus 로고
    • Identification of a receptor required for the anti-inflammatory activity of IVIG
    • R.M. Anthony, F. Wermeling, M.C.I. Karlsson, and J.V. Ravetch Identification of a receptor required for the anti-inflammatory activity of IVIG Proc. Natl. Acad. Sci. 105 2008 19571 19578
    • (2008) Proc. Natl. Acad. Sci. , vol.105 , pp. 19571-19578
    • Anthony, R.M.1    Wermeling, F.2    Karlsson, M.C.I.3    Ravetch, J.V.4
  • 215
    • 84860257686 scopus 로고    scopus 로고
    • IVIg-mediated amelioration of ITP in mice is dependent on sialic acid and SIGNR1
    • I. Schwab, M. Biburger, G. Krönke, G. Schett, and F. Nimmerjahn IVIg-mediated amelioration of ITP in mice is dependent on sialic acid and SIGNR1 Eur. J. Immunol. 42 2012 826 830
    • (2012) Eur. J. Immunol. , vol.42 , pp. 826-830
    • Schwab, I.1    Biburger, M.2    Krönke, G.3    Schett, G.4    Nimmerjahn, F.5
  • 217
  • 218
    • 84878097614 scopus 로고    scopus 로고
    • Human Fc receptor-like 5 binds intact IgG via mechanisms distinct from those of Fc receptors
    • A. Franco, B. Damdinsuren, T. Ise, J. Dement-Brown, H. Li, S. Nagata, and M. Tolnay Human Fc receptor-like 5 binds intact IgG via mechanisms distinct from those of Fc receptors J. Immunol. 190 2013 5739 5746
    • (2013) J. Immunol. , vol.190 , pp. 5739-5746
    • Franco, A.1    Damdinsuren, B.2    Ise, T.3    Dement-Brown, J.4    Li, H.5    Nagata, S.6    Tolnay, M.7
  • 219
    • 33645080442 scopus 로고    scopus 로고
    • Pathology and protection in nephrotoxic nephritis is determined by selective engagement of specific Fc receptors
    • Y. Kaneko, F. Nimmerjahn, M.P. Madaio, and J.V. Ravetch Pathology and protection in nephrotoxic nephritis is determined by selective engagement of specific Fc receptors J. Exp. Med. 203 2006 789 797
    • (2006) J. Exp. Med. , vol.203 , pp. 789-797
    • Kaneko, Y.1    Nimmerjahn, F.2    Madaio, M.P.3    Ravetch, J.V.4
  • 220
    • 84871276532 scopus 로고    scopus 로고
    • B cells and CD22 are dispensable for the immediate antiinflammatory activity of intravenous immunoglobulins in vivo
    • I. Schwab, M. Seeling, M. Biburger, S. Aschermann, L. Nitschke, and F. Nimmerjahn B cells and CD22 are dispensable for the immediate antiinflammatory activity of intravenous immunoglobulins in vivo Eur. J. Immunol. 42 2012 3302 3309
    • (2012) Eur. J. Immunol. , vol.42 , pp. 3302-3309
    • Schwab, I.1    Seeling, M.2    Biburger, M.3    Aschermann, S.4    Nitschke, L.5    Nimmerjahn, F.6
  • 221
    • 83455195478 scopus 로고    scopus 로고
    • The neonatal Fc receptor (FcRn) is not required for IVIg or anti-CD44 monoclonal antibody-mediated amelioration of murine immune thrombocytopenia
    • A.R. Crow, S.J. Suppa, X. Chen, P.J. Mott, and A.H. Lazarus The neonatal Fc receptor (FcRn) is not required for IVIg or anti-CD44 monoclonal antibody-mediated amelioration of murine immune thrombocytopenia Blood 118 2011 6403 6406
    • (2011) Blood , vol.118 , pp. 6403-6406
    • Crow, A.R.1    Suppa, S.J.2    Chen, X.3    Mott, P.J.4    Lazarus, A.H.5
  • 222
    • 84861858882 scopus 로고    scopus 로고
    • Mouse background and IVIG dosage are critical in establishing the role of inhibitory Fcγ receptor for the amelioration of experimental ITP
    • D. Leontyev, Y. Katsman, and D.R. Branch Mouse background and IVIG dosage are critical in establishing the role of inhibitory Fcγ receptor for the amelioration of experimental ITP Blood 119 2012 5261 5264
    • (2012) Blood , vol.119 , pp. 5261-5264
    • Leontyev, D.1    Katsman, Y.2    Branch, D.R.3
  • 223
    • 84875749746 scopus 로고    scopus 로고
    • Dissecting the molecular mechanism of IVIg therapy: The interaction between serum IgG and DC-SIGN is independent of antibody glycoform or Fc domain
    • X. Yu, S. Vasiljevic, D.A. Mitchell, M. Crispin, and C.N. Scanlan Dissecting the molecular mechanism of IVIg therapy: the interaction between serum IgG and DC-SIGN is independent of antibody glycoform or Fc domain J. Mol. Biol. 425 2013 1253 1258
    • (2013) J. Mol. Biol. , vol.425 , pp. 1253-1258
    • Yu, X.1    Vasiljevic, S.2    Mitchell, D.A.3    Crispin, M.4    Scanlan, C.N.5
  • 224
    • 0035824446 scopus 로고    scopus 로고
    • Structural basis for selective recognition of oligosaccharides by DC-SIGN and DC-SIGNR
    • H. Feinberg, D.A. Mitchell, K. Drickamer, and W.I. Weis Structural basis for selective recognition of oligosaccharides by DC-SIGN and DC-SIGNR Science 294 2001 2163 2166
    • (2001) Science , vol.294 , pp. 2163-2166
    • Feinberg, H.1    Mitchell, D.A.2    Drickamer, K.3    Weis, W.I.4
  • 226
    • 33748355349 scopus 로고    scopus 로고
    • Reversal of immune thrombocytopenia in mice by cross-linking human immunoglobulin G with a high-affinity monoclonal antibody
    • R. Bazin, R. Lemieux, and T. Tremblay Reversal of immune thrombocytopenia in mice by cross-linking human immunoglobulin G with a high-affinity monoclonal antibody Br. J. Haematol. 135 2006 97 100
    • (2006) Br. J. Haematol. , vol.135 , pp. 97-100
    • Bazin, R.1    Lemieux, R.2    Tremblay, T.3
  • 227
    • 84944684515 scopus 로고    scopus 로고
    • Pathways responsible for human autoantibody and therapeutic intravenous IgG activity in humanized mice
    • I. Schwab, A. Lux, and F. Nimmerjahn Pathways responsible for human autoantibody and therapeutic intravenous IgG activity in humanized mice Cell Rep. 13 2015 610 620
    • (2015) Cell Rep. , vol.13 , pp. 610-620
    • Schwab, I.1    Lux, A.2    Nimmerjahn, F.3
  • 228
    • 0028962403 scopus 로고
    • Glycosylation changes of IgG associated with rheumatoid arthritis can activate complement via the mannose-binding protein
    • R. Malhotra, M.R. Wormald, P.M. Rudd, P.B. Fischer, R.A. Dwek, and R.B. Sim Glycosylation changes of IgG associated with rheumatoid arthritis can activate complement via the mannose-binding protein Nat. Med. 1 1995 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
  • 229
    • 0028244694 scopus 로고
    • Agalactosyl glycoforms of IgG autoantibodies are pathogenic
    • T.W. Rademacher, P. Williams, and R.A. Dwek Agalactosyl glycoforms of IgG autoantibodies are pathogenic Proc. Natl. Acad. Sci. 91 1994 6123 6127
    • (1994) Proc. Natl. Acad. Sci. , vol.91 , pp. 6123-6127
    • Rademacher, T.W.1    Williams, P.2    Dwek, R.A.3
  • 231
    • 77952487132 scopus 로고    scopus 로고
    • Immunoglobulin G galactosylation and sialylation are associated with pregnancy-induced improvement of rheumatoid arthritis and the postpartum flare: Results from a large prospective cohort study
    • F. van de Geijn, M. Wuhrer, M. Selman, S. Willemsen, Y. de Man, A. Deelder, J. Hazes, and R. Dolhain Immunoglobulin G galactosylation and sialylation are associated with pregnancy-induced improvement of rheumatoid arthritis and the postpartum flare: results from a large prospective cohort study Arthritis Res. Ther. 11 2009 R193
    • (2009) Arthritis Res. Ther. , vol.11 , pp. R193
    • Van De Geijn, F.1    Wuhrer, M.2    Selman, M.3    Willemsen, S.4    De Man, Y.5    Deelder, A.6    Hazes, J.7    Dolhain, R.8
  • 235
    • 33751253486 scopus 로고    scopus 로고
    • Higher levels of sialylated Fc glycans in immunoglobulin G molecules can adversely impact functionality
    • B.J. Scallon, S.H. Tam, S.G. McCarthy, A.N. Cai, and T.S. Raju Higher levels of sialylated Fc glycans in immunoglobulin G molecules can adversely impact functionality Mol. Immunol. 44 2007 1524 1534
    • (2007) Mol. Immunol. , vol.44 , pp. 1524-1534
    • Scallon, B.J.1    Tam, S.H.2    McCarthy, S.G.3    Cai, A.N.4    Raju, T.S.5
  • 236
    • 79960046406 scopus 로고    scopus 로고
    • Intravenous gammaglobulin suppresses inflammation through a novel TH2 pathway
    • R.M. Anthony, T. Kobayashi, F. Wermeling, and J.V. Ravetch Intravenous gammaglobulin suppresses inflammation through a novel TH2 pathway Nature 475 2011 110 113
    • (2011) Nature , vol.475 , pp. 110-113
    • Anthony, R.M.1    Kobayashi, T.2    Wermeling, F.3    Ravetch, J.V.4
  • 238
    • 84937572658 scopus 로고    scopus 로고
    • DC-SIGN: The strange case of Dr. Jekyll and Mr. Hyde
    • Juan J. Garcia-Vallejo, and Y. van Kooyk DC-SIGN: the strange case of Dr. Jekyll and Mr. Hyde Immunity 42 2015 983 985
    • (2015) Immunity , vol.42 , pp. 983-985
    • Garcia-Vallejo, J.J.1    Van Kooyk, Y.2
  • 239
    • 0035800757 scopus 로고    scopus 로고
    • A novel mechanism of carbohydrate recognition by the C-type lectins DC-SIGN and DC-SIGNR: Subunit organization and binding to multivalent ligands
    • D.A. Mitchell, A.J. Fadden, and K. Drickamer A novel mechanism of carbohydrate recognition by the C-type lectins DC-SIGN and DC-SIGNR: subunit organization and binding to multivalent ligands J. Biol. Chem. 276 2001 28939 28945
    • (2001) J. Biol. Chem. , vol.276 , pp. 28939-28945
    • Mitchell, D.A.1    Fadden, A.J.2    Drickamer, K.3
  • 240
    • 84907554266 scopus 로고    scopus 로고
    • Structural characterization of the DC-SIGN-LewisX complex
    • K. Pederson, D.A. Mitchell, and J.H. Prestegard Structural characterization of the DC-SIGN-LewisX complex Biochemistry 53 2014 5700 5709
    • (2014) Biochemistry , vol.53 , pp. 5700-5709
    • Pederson, K.1    Mitchell, D.A.2    Prestegard, J.H.3
  • 241
    • 80052310703 scopus 로고    scopus 로고
    • Comparative analysis reveals selective recognition of glycans by the dendritic cell receptors DC-SIGN and Langerin
    • A. Holla, and A. Skerra Comparative analysis reveals selective recognition of glycans by the dendritic cell receptors DC-SIGN and Langerin Protein Eng. Des. Sel. 24 2011 659 669
    • (2011) Protein Eng. Des. Sel. , vol.24 , pp. 659-669
    • Holla, A.1    Skerra, A.2
  • 243
    • 0037474543 scopus 로고    scopus 로고
    • Structural analysis of human IgG-Fc glycoforms reveals a correlation between glycosylation and structural integrity
    • S. Krapp, Y. Mimura, R. Jefferis, R. Huber, and P. Sondermann Structural analysis of human IgG-Fc glycoforms reveals a correlation between glycosylation and structural integrity J. Mol. Biol. 325 2003 979 989
    • (2003) J. Mol. Biol. , vol.325 , pp. 979-989
    • Krapp, S.1    Mimura, Y.2    Jefferis, R.3    Huber, R.4    Sondermann, P.5
  • 246
    • 62549095425 scopus 로고    scopus 로고
    • DC-SIGN and α2,6-sialylated IgG Fc interaction is dispensable for the anti-inflammatory activity of IVIg on human dendritic cells
    • J. Bayry, K. Bansal, M.D. Kazatchkine, and S.V. Kaveri DC-SIGN and α2,6-sialylated IgG Fc interaction is dispensable for the anti-inflammatory activity of IVIg on human dendritic cells Proc. Natl. Acad. Sci. U. S. A. 106 2009 E24
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. E24
    • Bayry, J.1    Bansal, K.2    Kazatchkine, M.D.3    Kaveri, S.V.4
  • 247
    • 79952313700 scopus 로고    scopus 로고
    • Inhibition of differentiation, amplification, and function of human TH17 cells by intravenous immunoglobulin
    • M.S. Maddur, J. Vani, P. Hegde, S. Lacroix-Desmazes, S.V. Kaveri, and J. Bayry Inhibition of differentiation, amplification, and function of human TH17 cells by intravenous immunoglobulin J. Allergy Clin. Immunol. 127 2011 823 830 e827
    • (2011) J. Allergy Clin. Immunol. , vol.127 , pp. 823-830
    • Maddur, M.S.1    Vani, J.2    Hegde, P.3    Lacroix-Desmazes, S.4    Kaveri, S.V.5    Bayry, J.6
  • 248
    • 84886806068 scopus 로고    scopus 로고
    • Intravenous immunoglobulin expands regulatory T cells via induction of cyclooxygenase-2-dependent prostaglandin E2 in human dendritic cells
    • J. Trinath, P. Hegde, M. Sharma, M.S. Maddur, M. Rabin, J.-M. Vallat, L. Magy, K.N. Balaji, S.V. Kaveri, and J. Bayry Intravenous immunoglobulin expands regulatory T cells via induction of cyclooxygenase-2-dependent prostaglandin E2 in human dendritic cells Blood 122 2013 1419 1427
    • (2013) Blood , vol.122 , pp. 1419-1427
    • Trinath, J.1    Hegde, P.2    Sharma, M.3    Maddur, M.S.4    Rabin, M.5    Vallat, J.-M.6    Magy, L.7    Balaji, K.N.8    Kaveri, S.V.9    Bayry, J.10
  • 249
    • 84934289199 scopus 로고    scopus 로고
    • Differences in anti-inflammatory actions of intravenous immunoglobulin between mice and men: More than meets the eye
    • A.S. Tjon, R. van Gent, T.B. Geijtenbeek, and J. Kwekkeboom Differences in anti-inflammatory actions of intravenous immunoglobulin between mice and men: more than meets the eye Front. Immunol. 6 2015 10.3389/fimmu.2015.00197
    • (2015) Front. Immunol. , vol.6
    • Tjon, A.S.1    Van Gent, R.2    Geijtenbeek, T.B.3    Kwekkeboom, J.4
  • 250
    • 84884812281 scopus 로고    scopus 로고
    • The physiological role of DC-SIGN: A tale of mice and men
    • J.J. Garcia-Vallejo, and Y. van Kooyk The physiological role of DC-SIGN: a tale of mice and men Trends Immunol. 34 2013 482 486
    • (2013) Trends Immunol. , vol.34 , pp. 482-486
    • Garcia-Vallejo, J.J.1    Van Kooyk, Y.2
  • 251
    • 33745988599 scopus 로고    scopus 로고
    • Widely divergent biochemical properties of the complete set of mouse DC-SIGN-related proteins
    • A.S. Powlesland, E.M. Ward, S.K. Sadhu, Y. Guo, M.E. Taylor, and K. Drickamer Widely divergent biochemical properties of the complete set of mouse DC-SIGN-related proteins J. Biol. Chem. 281 2006 20440 20449
    • (2006) J. Biol. Chem. , vol.281 , pp. 20440-20449
    • Powlesland, A.S.1    Ward, E.M.2    Sadhu, S.K.3    Guo, Y.4    Taylor, M.E.5    Drickamer, K.6
  • 252
    • 84936871761 scopus 로고    scopus 로고
    • Recent insights into structures and functions of C-type lectins in the immune system
    • K. Drickamer, and M.E. Taylor Recent insights into structures and functions of C-type lectins in the immune system Curr. Opin. Struct. Biol. 34 2015 26 34
    • (2015) Curr. Opin. Struct. Biol. , vol.34 , pp. 26-34
    • Drickamer, K.1    Taylor, M.E.2
  • 255
    • 25444513373 scopus 로고    scopus 로고
    • Dendritic cell-specific intercellular adhesion molecule 3-grabbing nonintegrin/CD209 is abundant on macrophages in the normal human lymph node and is not required for dendritic cell stimulation of the mixed leukocyte reaction
    • A. Granelli-Piperno, A. Pritsker, M. Pack, I. Shimeliovich, J.F. Arrighi, C.G. Park, C. Trumpfheller, V. Piguet, T.M. Moran, and R.M. Steinman Dendritic cell-specific intercellular adhesion molecule 3-grabbing nonintegrin/CD209 is abundant on macrophages in the normal human lymph node and is not required for dendritic cell stimulation of the mixed leukocyte reaction J. Immunol. 175 2005 4265 4273
    • (2005) J. Immunol. , vol.175 , pp. 4265-4273
    • Granelli-Piperno, A.1    Pritsker, A.2    Pack, M.3    Shimeliovich, I.4    Arrighi, J.F.5    Park, C.G.6    Trumpfheller, C.7    Piguet, V.8    Moran, T.M.9    Steinman, R.M.10
  • 256
    • 0027511875 scopus 로고
    • Natural ligands of the B cell adhesion molecule CD22 beta carry N-linked oligosaccharides with alpha-2,6-linked sialic acids that are required for recognition
    • L.D. Powell, D. Sgroi, E.R. Sjoberg, I. Stamenkovic, and A. Varki Natural ligands of the B cell adhesion molecule CD22 beta carry N-linked oligosaccharides with alpha-2,6-linked sialic acids that are required for recognition J. Biol. Chem. 268 1993 7019 7027
    • (1993) J. Biol. Chem. , vol.268 , pp. 7019-7027
    • Powell, L.D.1    Sgroi, D.2    Sjoberg, E.R.3    Stamenkovic, I.4    Varki, A.5
  • 257
    • 0036462606 scopus 로고    scopus 로고
    • Chemical diversity in the sialic acids and related α-keto acids: An evolutionary perspective
    • T. Angata, and A. Varki Chemical diversity in the sialic acids and related α-keto acids: an evolutionary perspective Chem. Rev. 102 2002 439 470
    • (2002) Chem. Rev. , vol.102 , pp. 439-470
    • Angata, T.1    Varki, A.2
  • 258
    • 0029000263 scopus 로고
    • Molecular cloning of cytidine monophospho-N-acetylneuraminic acid hydroxylase. Regulation of species- and tissue-specific expression of N-glycolylneuraminic acid
    • T. Kawano, S. Koyama, H. Takematsu, Y. Kozutsumi, H. Kawasaki, S. Kawashima, T. Kawasaki, and A. Suzuki Molecular cloning of cytidine monophospho-N-acetylneuraminic acid hydroxylase. Regulation of species- and tissue-specific expression of N-glycolylneuraminic acid J. Biol. Chem. 270 1995 16458 16463
    • (1995) J. Biol. Chem. , vol.270 , pp. 16458-16463
    • Kawano, T.1    Koyama, S.2    Takematsu, H.3    Kozutsumi, Y.4    Kawasaki, H.5    Kawashima, S.6    Kawasaki, T.7    Suzuki, A.8
  • 259
    • 0032546785 scopus 로고    scopus 로고
    • The molecular basis for the absence of N-glycolylneuraminic acid in humans
    • A. Irie, S. Koyama, Y. Kozutsumi, T. Kawasaki, and A. Suzuki The molecular basis for the absence of N-glycolylneuraminic acid in humans J. Biol. Chem. 273 1998 15866 15871
    • (1998) J. Biol. Chem. , vol.273 , pp. 15866-15871
    • Irie, A.1    Koyama, S.2    Kozutsumi, Y.3    Kawasaki, T.4    Suzuki, A.5
  • 263
    • 79952555821 scopus 로고    scopus 로고
    • Survey of immune-related, mannose/fucose-binding C-type lectin receptors reveals widely divergent sugar-binding specificities
    • R.T. Lee, T.L. Hsu, S.K. Huang, S.L. Hsieh, C.H. Wong, and Y.C. Lee Survey of immune-related, mannose/fucose-binding C-type lectin receptors reveals widely divergent sugar-binding specificities Glycobiology 21 2011 512 520
    • (2011) Glycobiology , vol.21 , pp. 512-520
    • Lee, R.T.1    Hsu, T.L.2    Huang, S.K.3    Hsieh, S.L.4    Wong, C.H.5    Lee, Y.C.6
  • 265
    • 0035859830 scopus 로고    scopus 로고
    • Identification of a family of Fc receptor homologs with preferential B cell expression
    • R.S. Davis, Y.H. Wang, H. Kubagawa, and M.D. Cooper Identification of a family of Fc receptor homologs with preferential B cell expression Proc. Natl. Acad. Sci. 98 2001 9772 9777
    • (2001) Proc. Natl. Acad. Sci. , vol.98 , pp. 9772-9777
    • Davis, R.S.1    Wang, Y.H.2    Kubagawa, H.3    Cooper, M.D.4
  • 266
    • 0037089218 scopus 로고    scopus 로고
    • IRTAs: A new family of immunoglobulinlike receptors differentially expressed in B cells
    • I. Miller, G. Hatzivassiliou, G. Cattoretti, C. Mendelsohn, and R. Dalla-Favera IRTAs: a new family of immunoglobulinlike receptors differentially expressed in B cells Blood 99 2002 2662 2669
    • (2002) Blood , vol.99 , pp. 2662-2669
    • Miller, I.1    Hatzivassiliou, G.2    Cattoretti, G.3    Mendelsohn, C.4    Dalla-Favera, R.5
  • 267
    • 34247895443 scopus 로고    scopus 로고
    • Fc receptor-like molecules
    • R.S. Davis Fc receptor-like molecules Annu. Rev. Immunol. 25 2007 525 560
    • (2007) Annu. Rev. Immunol. , vol.25 , pp. 525-560
    • Davis, R.S.1
  • 268
    • 11344249227 scopus 로고    scopus 로고
    • Immunoglobulin superfamily receptor translocation associated 2 protein on lymphoma cell lines and hairy cell leukemia cells detected by novel monoclonal antibodies
    • T. Ise, H. Maeda, K. Santora, L. Xiang, R.J. Kreitman, I. Pastan, and S. Nagata Immunoglobulin superfamily receptor translocation associated 2 protein on lymphoma cell lines and hairy cell leukemia cells detected by novel monoclonal antibodies Clin. Cancer Res. 11 2005 87 96
    • (2005) Clin. Cancer Res. , vol.11 , pp. 87-96
    • Ise, T.1    Maeda, H.2    Santora, K.3    Xiang, L.4    Kreitman, R.J.5    Pastan, I.6    Nagata, S.7
  • 271
    • 84861130144 scopus 로고    scopus 로고
    • Cutting edge: Human FcRL4 and FcRL5 are receptors for IgA and IgG
    • T.J. Wilson, A. Fuchs, and M. Colonna Cutting edge: human FcRL4 and FcRL5 are receptors for IgA and IgG J. Immunol. 188 2012 4741 4745
    • (2012) J. Immunol. , vol.188 , pp. 4741-4745
    • Wilson, T.J.1    Fuchs, A.2    Colonna, M.3
  • 272
    • 84872754818 scopus 로고    scopus 로고
    • Analysis and functional consequences of increased Fab-sialylation of intravenous immunoglobulin (IVIg) after lectin fractionation
    • F. Käsermann, D.J. Boerema, M. Rüegsegger, A. Hofmann, S. Wymann, A.W. Zuercher, and S. Miescher Analysis and functional consequences of increased Fab-sialylation of intravenous immunoglobulin (IVIg) after lectin fractionation PLoS One 7 2012 e37243
    • (2012) PLoS One , vol.7
    • Käsermann, F.1    Boerema, D.J.2    Rüegsegger, M.3    Hofmann, A.4    Wymann, S.5    Zuercher, A.W.6    Miescher, S.7
  • 274
    • 84938244540 scopus 로고    scopus 로고
    • Intravenous IgG (IVIG) and subcutaneous IgG (SCIG) preparations have comparable inhibitory effect on T cell activation, which is not dependent on IgG sialylation, monocytes or B cells
    • A.C. Issekutz, D. Rowter, S. Miescher, and F. Käsermann Intravenous IgG (IVIG) and subcutaneous IgG (SCIG) preparations have comparable inhibitory effect on T cell activation, which is not dependent on IgG sialylation, monocytes or B cells Clin. Immunol. 160 2015 123 132
    • (2015) Clin. Immunol. , vol.160 , pp. 123-132
    • Issekutz, A.C.1    Rowter, D.2    Miescher, S.3    Käsermann, F.4
  • 275
    • 84865030107 scopus 로고    scopus 로고
    • Sialylation-independent mechanism involved in the amelioration of murine immune thrombocytopenia using intravenous gammaglobulin
    • D. Leontyev, Y. Katsman, X.-Z. Ma, S. Miescher, F. Käsermann, and D.R. Branch Sialylation-independent mechanism involved in the amelioration of murine immune thrombocytopenia using intravenous gammaglobulin Transfusion 52 2012 1799 1805
    • (2012) Transfusion , vol.52 , pp. 1799-1805
    • Leontyev, D.1    Katsman, Y.2    Ma, X.-Z.3    Miescher, S.4    Käsermann, F.5    Branch, D.R.6
  • 276
    • 79959555556 scopus 로고    scopus 로고
    • Enrichment of sialylated IgG by lectin fractionation does not enhance the efficacy of immunoglobulin G in a murine model of immune thrombocytopenia
    • T. Guhr, J. Bloem, N.I.L. Derksen, M. Wuhrer, A.H.L. Koenderman, R.C. Aalberse, and T. Rispens Enrichment of sialylated IgG by lectin fractionation does not enhance the efficacy of immunoglobulin G in a murine model of immune thrombocytopenia PLoS One 6 2011 e21246
    • (2011) PLoS One , vol.6
    • Guhr, T.1    Bloem, J.2    Derksen, N.I.L.3    Wuhrer, M.4    Koenderman, A.H.L.5    Aalberse, R.C.6    Rispens, T.7
  • 279
    • 79959850012 scopus 로고    scopus 로고
    • Passively administered pooled human immunoglobulins exert IL-10 dependent anti-inflammatory effects that protect against fatal HSV encephalitis
    • C. Ramakrishna, A.N.S. Newo, Y.-W. Shen, and E. Cantin Passively administered pooled human immunoglobulins exert IL-10 dependent anti-inflammatory effects that protect against fatal HSV encephalitis PLoS Pathog. 7 2011 e1002071
    • (2011) PLoS Pathog. , vol.7
    • Ramakrishna, C.1    Newo, A.N.S.2    Shen, Y.-W.3    Cantin, E.4
  • 280
    • 33947139304 scopus 로고    scopus 로고
    • Shortage of human intravenous immunoglobulin - Reasons and possible solutions
    • J. Bayry, M.D. Kazatchkine, and S.V. Kaveri Shortage of human intravenous immunoglobulin - reasons and possible solutions Nat. Rev. Neurol. 3 2007 120 121
    • (2007) Nat. Rev. Neurol. , vol.3 , pp. 120-121
    • Bayry, J.1    Kazatchkine, M.D.2    Kaveri, S.V.3
  • 283
    • 68549091059 scopus 로고    scopus 로고
    • Proposal for a standard system for drawing structural diagrams of N- and O-linked carbohydrates and related compounds
    • D.J. Harvey, A.H. Merry, L. Royle, M.P. Campbell, R.A. Dwek, and P.M. Rudd Proposal for a standard system for drawing structural diagrams of N- and O-linked carbohydrates and related compounds Proteomics 9 2009 3796 3801
    • (2009) Proteomics , vol.9 , pp. 3796-3801
    • Harvey, D.J.1    Merry, A.H.2    Royle, L.3    Campbell, M.P.4    Dwek, R.A.5    Rudd, P.M.6
  • 284
    • 0343373375 scopus 로고
    • High-resolution 1H nuclear magnetic resonance spectroscopy as a tool in the structural analysis of carbohydrates related to glycoproteins.
    • J.F.G. Vliegenthart, L. Dorland, and H. van Halbeek High-resolution 1H nuclear magnetic resonance spectroscopy as a tool in the structural analysis of carbohydrates related to glycoproteins. Adv. Carbohydr. Chem. Biochem. 41 1983 209 374
    • (1983) Adv. Carbohydr. Chem. Biochem. , vol.41 , pp. 209-374
    • Vliegenthart, J.F.G.1    Dorland, L.2    Van Halbeek, H.3
  • 285
    • 0028829350 scopus 로고
    • Glycobiology: 'The function of sugar in the IgG molecule'
    • R.A. Dwek, A.C. Lellouch, and M.R. Wormald Glycobiology: 'the function of sugar in the IgG molecule' J. Anat. 187 Pt 2 1995 279 292
    • (1995) J. Anat. , vol.187 , pp. 279-292
    • Dwek, R.A.1    Lellouch, A.C.2    Wormald, M.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.