메뉴 건너뛰기




Volumn 163, Issue , 1998, Pages 59-76

IgG-Fc-mediated effector functions: Molecular definition of interaction sites for effector ligands and the role of glycosylation

Author keywords

[No Author keywords available]

Indexed keywords

IMMUNOGLOBULIN FC FRAGMENT; IMMUNOGLOBULIN G;

EID: 0031868555     PISSN: 01052896     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1600-065X.1998.tb01188.x     Document Type: Review
Times cited : (301)

References (93)
  • 2
    • 0001500510 scopus 로고
    • Three-dimensional structure of an intact human immunoglobulin
    • Silverton EW, Navia MA, Davies DR. Three-dimensional structure of an intact human immunoglobulin. Proc Natl Acad Sci USA 1977;74:5140-5144.
    • (1977) Proc Natl Acad Sci USA , vol.74 , pp. 5140-5144
    • Silverton, E.W.1    Navia, M.A.2    Davies, D.R.3
  • 3
    • 0027154092 scopus 로고
    • Three-dimensional structure of a human immunoglobulin with a hinge deletion
    • Guddat LW, Herron JN, Edmundson AB. Three-dimensional structure of a human immunoglobulin with a hinge deletion. Proc Natl Acad Sci USA 1993;90:4271-4275.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 4271-4275
    • Guddat, L.W.1    Herron, J.N.2    Edmundson, A.B.3
  • 4
    • 0028289241 scopus 로고
    • Anatomy of the antibody molecule
    • Padlan EA. Anatomy of the antibody molecule. Mol Immunol 1994;31:169-217.
    • (1994) Mol Immunol , vol.31 , pp. 169-217
    • Padlan, E.A.1
  • 5
    • 0019522383 scopus 로고
    • Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein a from Staphylococcus aureus at 2.9- and 2.8-Å resolution
    • Deisenhofer J. Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9- and 2.8-Å resolution. Biochemistry 1981;20:2361-2370.
    • (1981) Biochemistry , vol.20 , pp. 2361-2370
    • Deisenhofer, J.1
  • 6
    • 0002121160 scopus 로고
    • X-ray diffraction studies of antibody constant regions
    • Metzger H, ed. Washington DC: American Society for Microbiology
    • Padlan EA. X-ray diffraction studies of antibody constant regions. In: Metzger H, ed. Fc receptors and the action of antibodies. Washington DC: American Society for Microbiology; 1990. p. 12-30.
    • (1990) Fc Receptors and the Action of Antibodies , pp. 12-30
    • Padlan, E.A.1
  • 7
    • 0021857415 scopus 로고
    • Immunoglobulin G - Functional sites
    • Burton DR. Immunoglobulin G - functional sites. Mol Immunol 1985;22:161-206.
    • (1985) Mol Immunol , vol.22 , pp. 161-206
    • Burton, D.R.1
  • 8
    • 0026657624 scopus 로고
    • Human antibody effector function
    • Burton DR, Woof JM. Human antibody effector function. Adv Immunol 1992;51:1-84.
    • (1992) Adv Immunol , vol.51 , pp. 1-84
    • Burton, D.R.1    Woof, J.M.2
  • 10
    • 0025007923 scopus 로고
    • Selective IgG subclass deficiency: Quantification and clinical relevance
    • Jefferis R, Kumararatne DS. Selective IgG subclass deficiency: quantification and clinical relevance. Clin Exp Immunol 1990;81:357-368.
    • (1990) Clin Exp Immunol , vol.81 , pp. 357-368
    • Jefferis, R.1    Kumararatne, D.S.2
  • 11
    • 0023265503 scopus 로고
    • The solution conformations of the subclasses of human IgG deduced from sedimentation and small-angle x-ray-scattering studies
    • Gregory L, et al. The solution conformations of the subclasses of human IgG deduced from sedimentation and small-angle x-ray-scattering studies. Mol Immunol 1987;24:821-829.
    • (1987) Mol Immunol , vol.24 , pp. 821-829
    • Gregory, L.1
  • 13
    • 0028330521 scopus 로고
    • Local and transmitted conformational changes on complexation of an anti-sweetener Fab
    • Guddat LW, Shan L, Anchin JM, Linthicum DS, Edmundson AB. Local and transmitted conformational changes on complexation of an anti-sweetener Fab. J Mol Biol 1994;236:247-274.
    • (1994) J Mol Biol , vol.236 , pp. 247-274
    • Guddat, L.W.1    Shan, L.2    Anchin, J.M.3    Linthicum, D.S.4    Edmundson, A.B.5
  • 14
    • 0031252319 scopus 로고    scopus 로고
    • Domain-switched mouse IgM/IgG2b hybrids indicate individual roles for Cμ2, Cμ3, and Cμ4 domains in the regulation of the interaction of IgM with complement C1q
    • Chen FH, Arya SK, Rinfret A, Isenman DE, Shulman MJ, Painter RH. Domain-switched mouse IgM/IgG2b hybrids indicate individual roles for Cμ2, Cμ3, and Cμ4 domains in the regulation of the interaction of IgM with complement C1q. J Immunol 1997;159:3354-3363.
    • (1997) J Immunol , vol.159 , pp. 3354-3363
    • Chen, F.H.1    Arya, S.K.2    Rinfret, A.3    Isenman, D.E.4    Shulman, M.J.5    Painter, R.H.6
  • 15
    • 0019119230 scopus 로고
    • Crystallographic refinement and atomic models of the intact immunoglobulin molecule Kol and its antigen-binding fragment at 3.0 Å and 1.0 Å resolution
    • Marquart M, Deisenhofer J, Huber R, Palm W. Crystallographic refinement and atomic models of the intact immunoglobulin molecule Kol and its antigen-binding fragment at 3.0 Å and 1.0 Å resolution. J Mol Biol 1980;141:369-391.
    • (1980) J Mol Biol , vol.141 , pp. 369-391
    • Marquart, M.1    Deisenhofer, J.2    Huber, R.3    Palm, W.4
  • 16
    • 0027294016 scopus 로고
    • Activation of complement by an IgG molecule without a genetic hinge
    • retracted in Nature 1996;383:103
    • Brekke OH, Michaelsen TE, Sandlie R, Sandlie I. Activation of complement by an IgG molecule without a genetic hinge [retracted in Nature 1996;383:103]. Nature 1993;363:628.
    • (1993) Nature , vol.363 , pp. 628
    • Brekke, O.H.1    Michaelsen, T.E.2    Sandlie, R.3    Sandlie, I.4
  • 17
    • 0031568069 scopus 로고    scopus 로고
    • The hinge as a spacer contributes to covalent assembly and is required for function of IgG
    • Coloma MJ, Trinh KR, Wims LA, Morrison SL. The hinge as a spacer contributes to covalent assembly and is required for function of IgG. J Immunol 1997;158:733-740.
    • (1997) J Immunol , vol.158 , pp. 733-740
    • Coloma, M.J.1    Trinh, K.R.2    Wims, L.A.3    Morrison, S.L.4
  • 18
    • 0017252923 scopus 로고
    • Crystallographic structural studies of a human Fc fragment. I. An electron density map at 4 Å resolution and a partial model
    • Deisenhofer J, Colman PM, Huber R, Haupt H, Schwick G. Crystallographic structural studies of a human Fc fragment. I. An electron density map at 4 Å resolution and a partial model. Hoppe Seylers Z Physiol Chem 1976;357: 435-445.
    • (1976) Hoppe Seylers Z Physiol Chem , vol.357 , pp. 435-445
    • Deisenhofer, J.1    Colman, P.M.2    Huber, R.3    Haupt, H.4    Schwick, G.5
  • 19
    • 0017194137 scopus 로고
    • Crystallographic structural studies of a human Fc fragment. II. a complete model based on a Fourier map at 3.5 Å resolution
    • Deisenhofer J, Colman PM, Epp O, Huber R. Crystallographic structural studies of a human Fc fragment. II. A complete model based on a Fourier map at 3.5 Å resolution. Hoppe Seylers Z Physiol Chem 1976;357: 1421-1434.
    • (1976) Hoppe Seylers Z Physiol Chem , vol.357 , pp. 1421-1434
    • Deisenhofer, J.1    Colman, P.M.2    Epp, O.3    Huber, R.4
  • 20
    • 0026050344 scopus 로고
    • Human FcγRI and FcγRII interact with distinct but overlapping sites on human IgG
    • Lund J, et al. Human FcγRI and FcγRII interact with distinct but overlapping sites on human IgG. J Immunol 1991;147:2657-2662.
    • (1991) J Immunol , vol.147 , pp. 2657-2662
    • Lund, J.1
  • 21
    • 0029644247 scopus 로고
    • Crystal structure of the C2 fragment of streptococcal protein G in complex with the Fc domain of human IgG
    • Sauer-Eriksson AE, Kleywegt GJ, Uhl M, Jones TA. Crystal structure of the C2 fragment of streptococcal protein G in complex with the Fc domain of human IgG. Structure 1995;3:265-278.
    • (1995) Structure , vol.3 , pp. 265-278
    • Sauer-Eriksson, A.E.1    Kleywegt, G.J.2    Uhl, M.3    Jones, T.A.4
  • 22
    • 9344248427 scopus 로고    scopus 로고
    • Crystallization of a complex between the Fab fragment of a human immunoglobulin M (IgM) rheumatoid factor (RF-AN) and the Fc fragment of human IgG4
    • Sohi MK, et al. Crystallization of a complex between the Fab fragment of a human immunoglobulin M (IgM) rheumatoid factor (RF-AN) and the Fc fragment of human IgG4. Immunology 1996;88:636-641.
    • (1996) Immunology , vol.88 , pp. 636-641
    • Sohi, M.K.1
  • 23
    • 0030938368 scopus 로고    scopus 로고
    • Structure of human IgM rheumatoid factor Fab bound to its autoantigen IgG Fc reveals a novel topology of antibody-antigen interaction
    • Corper AL, et al. Structure of human IgM rheumatoid factor Fab bound to its autoantigen IgG Fc reveals a novel topology of antibody-antigen interaction. Nat Struct Biol 1997;4:374-381.
    • (1997) Nat Struct Biol , vol.4 , pp. 374-381
    • Corper, A.L.1
  • 24
    • 0028089908 scopus 로고
    • Crystal structure of the complex of rat neonatal Fc receptor with Fc
    • Burmeister WP, Huber AH, Bjorkman PJ. Crystal structure of the complex of rat neonatal Fc receptor with Fc. Nature 1994;372:379-383.
    • (1994) Nature , vol.372 , pp. 379-383
    • Burmeister, W.P.1    Huber, A.H.2    Bjorkman, P.J.3
  • 26
    • 0030937062 scopus 로고    scopus 로고
    • Glycosylation: Heterogeneity and the 3D structure of proteins
    • Rudd PM, Dwek RA. Glycosylation: heterogeneity and the 3D structure of proteins. Crit Rev Biochem Mol Biol 1997;32: 1-100.
    • (1997) Crit Rev Biochem Mol Biol , vol.32 , pp. 1-100
    • Rudd, P.M.1    Dwek, R.A.2
  • 27
    • 0025290953 scopus 로고
    • A comparative study of the N-linked oligosaccharide structures of human IgG subclass proteins
    • Jefferis R, et al. A comparative study of the N-linked oligosaccharide structures of human IgG subclass proteins. Biochem J 1990;268:529-537.
    • (1990) Biochem J , vol.268 , pp. 529-537
    • Jefferis, R.1
  • 28
    • 17344371900 scopus 로고    scopus 로고
    • Quantitation of human IgG glycoforms isolated from rheumatoid sera: A critical evaluation of chromatographic methods
    • In press
    • Routier FH, et al. Quantitation of human IgG glycoforms isolated from rheumatoid sera: a critical evaluation of chromatographic methods. J Immunol Methods 1998 (In press).
    • (1998) J Immunol Methods
    • Routier, F.H.1
  • 29
    • 0024544730 scopus 로고
    • Aglycosylation of human IgG1 and IgG3 monoclonal antibodies can eliminate recognition by human cells expressing FcγRI and/or FcγRII receptors
    • Walker MR, Lund J, Thompson KM, Jefferis R. Aglycosylation of human IgG1 and IgG3 monoclonal antibodies can eliminate recognition by human cells expressing FcγRI and/or FcγRII receptors. Biochem J 1989;259:347-353.
    • (1989) Biochem J , vol.259 , pp. 347-353
    • Walker, M.R.1    Lund, J.2    Thompson, K.M.3    Jefferis, R.4
  • 30
    • 0027450137 scopus 로고
    • Aglycosylated chimeric human IgG3 can trigger the human phagocyte respiratory burst
    • Pound JD, Lund J, Jefferis R. Aglycosylated chimeric human IgG3 can trigger the human phagocyte respiratory burst. Mol Immunol 1993;30:233-241.
    • (1993) Mol Immunol , vol.30 , pp. 233-241
    • Pound, J.D.1    Lund, J.2    Jefferis, R.3
  • 31
    • 0030470557 scopus 로고    scopus 로고
    • Multiple interactions of IgG with its core oligosaccharide can modulate recognition by complement and human Fcy receptor I and influence the synthesis of its oligosaccharide chains
    • Lund J, Takahashi N, Pound JD, Goodall M, Jefferis R. Multiple interactions of IgG with its core oligosaccharide can modulate recognition by complement and human Fcy receptor I and influence the synthesis of its oligosaccharide chains. J Immunol 1996;157:4963-4969.
    • (1996) J Immunol , vol.157 , pp. 4963-4969
    • Lund, J.1    Takahashi, N.2    Pound, J.D.3    Goodall, M.4    Jefferis, R.5
  • 32
    • 0028830782 scopus 로고
    • Oligosaccharide protein interactions in IgG can modulate recognition by Fcy receptors
    • Lund J, Takahashi N, Pound JD, Goodall M, Nakagawa H, Jefferis R. Oligosaccharide protein interactions in IgG can modulate recognition by Fcy receptors. FASEB J 1995;9:115-119.
    • (1995) FASEB J , vol.9 , pp. 115-119
    • Lund, J.1    Takahashi, N.2    Pound, J.D.3    Goodall, M.4    Nakagawa, H.5    Jefferis, R.6
  • 33
    • 0031015976 scopus 로고    scopus 로고
    • Glycosylation of antibody molecules: Structural and functional significance
    • Jefferis R. Lund J. Glycosylation of antibody molecules: structural and functional significance. Chem Immunol 1997;65:111-128.
    • (1997) Chem Immunol , vol.65 , pp. 111-128
    • Jefferis, R.1    Lund, J.2
  • 34
    • 0031033895 scopus 로고    scopus 로고
    • Effect of glycosylation on antibody function: Implications for genetic engineering
    • Wright A, Morrison SL. Effect of glycosylation on antibody function: implications for genetic engineering. Trends Biotech 1997;15:26-32.
    • (1997) Trends Biotech , vol.15 , pp. 26-32
    • Wright, A.1    Morrison, S.L.2
  • 36
    • 0030723080 scopus 로고    scopus 로고
    • Remodelling the oligosaccharide of human IgG antibodies: Effects on biological activities
    • Abadeh S, Church S, Dong S, Lund J, Goodall M, Jefferis R. Remodelling the oligosaccharide of human IgG antibodies: effects on biological activities. Biochem Soc Trans 1997;25:S661.
    • (1997) Biochem Soc Trans , vol.25
    • Abadeh, S.1    Church, S.2    Dong, S.3    Lund, J.4    Goodall, M.5    Jefferis, R.6
  • 37
    • 0029914789 scopus 로고    scopus 로고
    • Agalactosyl IgG [Gal(0)] - An analysis of its clinical utility in the long term follow up of patients with rheumatoid arthritis
    • Bodman-Smith K, Sumar N, Sinclair H, Roitt I, Isenberg D, Young A. Agalactosyl IgG [Gal(0)] - an analysis of its clinical utility in the long term follow up of patients with rheumatoid arthritis. Br J Rheumatol 1996;35:1063-1066.
    • (1996) Br J Rheumatol , vol.35 , pp. 1063-1066
    • Bodman-Smith, K.1    Sumar, N.2    Sinclair, H.3    Roitt, I.4    Isenberg, D.5    Young, A.6
  • 38
    • 0028224656 scopus 로고
    • Glycosylation of recombinant proteins: Problems and prospects
    • Jenkins N, Curling E. Glycosylation of recombinant proteins: problems and prospects. Enzyme Micro Technol 1995;16: 354-364.
    • (1995) Enzyme Micro Technol , vol.16 , pp. 354-364
    • Jenkins, N.1    Curling, E.2
  • 39
  • 40
    • 0020738965 scopus 로고
    • The 3-dimensional structure of the carbohydrate within the Fc fragment of immunoglobulin G
    • Sutton BJ, Phillips DC. The 3-dimensional structure of the carbohydrate within the Fc fragment of immunoglobulin G. Biochem Soc Trans 1983;11:130-132.
    • (1983) Biochem Soc Trans , vol.11 , pp. 130-132
    • Sutton, B.J.1    Phillips, D.C.2
  • 41
    • 0028920695 scopus 로고
    • Recognition sites on human IgG for Fcγ receptors - The role of glycosylation
    • Jefferis R, Lund J, Goodall M. Recognition sites on human IgG for Fcγ receptors - the role of glycosylation. Immunol Lett 1995;44:111-117.
    • (1995) Immunol Lett , vol.44 , pp. 111-117
    • Jefferis, R.1    Lund, J.2    Goodall, M.3
  • 42
    • 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
    • Wormald MR, Rudd PM, Harvey DJ, Chang SC, Scragg IG, Dwek RA. Variations in oligosaccharide-protein interactions in immunoglobulin G determine the site-specific glycosylation profiles and modulate the dynamic motion of the Fc oligosaccharides. Biochemistry 1997;36:1370-1380.
    • (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
  • 43
    • 0028169708 scopus 로고
    • A novel C-13 isotopic labeling strategy for probing the structure and dynamics of glycan chains in situ on glycoproteins
    • Gilhespy-Muskett AM, Partridge J, Jefferis R, Homans SW. A novel C-13 isotopic labeling strategy for probing the structure and dynamics of glycan chains in situ on glycoproteins. Glycobiology 1994;4:485-489.
    • (1994) Glycobiology , vol.4 , pp. 485-489
    • Gilhespy-Muskett, A.M.1    Partridge, J.2    Jefferis, R.3    Homans, S.W.4
  • 44
    • 0025339176 scopus 로고
    • Proton nuclear magnetic resonance studies of the structure of the Fc fragment of human immunoglobulin G1 - Comparisons of native and recombinant proteins
    • Matsuda H, et al. Proton nuclear magnetic resonance studies of the structure of the Fc fragment of human immunoglobulin G1 - comparisons of native and recombinant proteins. Mol Immunol 1990;27:571-579.
    • (1990) Mol Immunol , vol.27 , pp. 571-579
    • Matsuda, H.1
  • 45
    • 0025086946 scopus 로고
    • A protein structural change in aglycosylated IgG3 correlates with loss of huFcγRI and huFcγRIII binding and/or activation
    • Lund J, Tanaka T, Takahashi N, Sarmay G, Arata Y, Jefferis R. A protein structural change in aglycosylated IgG3 correlates with loss of huFcγRI and huFcγRIII binding and/or activation. Mol Immunol 1990;27:1145-1153.
    • (1990) Mol Immunol , vol.27 , pp. 1145-1153
    • Lund, J.1    Tanaka, T.2    Takahashi, N.3    Sarmay, G.4    Arata, Y.5    Jefferis, R.6
  • 46
    • 0002365025 scopus 로고    scopus 로고
    • Differences in thermodynamic parameters for the co-operative structures within glycosylated and aglycosylated mouse IgG2b
    • Chowdhry B, Ladbury J, eds. London: Wiley
    • Tishchenko V, Lund J, Goodall M, Jefferis R. Differences in thermodynamic parameters for the co-operative structures within glycosylated and aglycosylated mouse IgG2b. In: Chowdhry B, Ladbury J, eds. Applications of biocalorimetry. London: Wiley; 1998. p. 267-275.
    • (1998) Applications of Biocalorimetry , pp. 267-275
    • Tishchenko, V.1    Lund, J.2    Goodall, M.3    Jefferis, R.4
  • 47
    • 0024424859 scopus 로고
    • The IgG subclass pattern of complement activation depends on epitope density and antibody and complement concentration
    • Garred P, Michaelsen TE, Aase A. The IgG subclass pattern of complement activation depends on epitope density and antibody and complement concentration. Scand J Immunol 1989;30:379-382.
    • (1989) Scand J Immunol , vol.30 , pp. 379-382
    • Garred, P.1    Michaelsen, T.E.2    Aase, A.3
  • 48
    • 0030657786 scopus 로고    scopus 로고
    • Neutrophil Fc gamma and complement receptors involved in binding soluble IgG immune complexes and in specific granule release induced by soluble IgG immune complexes
    • Voice JK, Lachmann PJ. Neutrophil Fc gamma and complement receptors involved in binding soluble IgG immune complexes and in specific granule release induced by soluble IgG immune complexes. Eur J Immunol 1997;27:2514-2523.
    • (1997) Eur J Immunol , vol.27 , pp. 2514-2523
    • Voice, J.K.1    Lachmann, P.J.2
  • 51
    • 0030929805 scopus 로고    scopus 로고
    • Fc receptor biology
    • Daeron M. Fc receptor biology. Annu Rev Immunol 1997;15:203-234.
    • (1997) Annu Rev Immunol , vol.15 , pp. 203-234
    • Daeron, M.1
  • 52
    • 0028130057 scopus 로고
    • Fc receptors: Rubor redux
    • Ravetch JV. Fc receptors: rubor redux. Cell 1994;78:553-560.
    • (1994) Cell , vol.78 , pp. 553-560
    • Ravetch, J.V.1
  • 53
    • 0028179557 scopus 로고
    • 2, CD11b/CD18) and FcγRIII cooperate in generation of a neutrophil respiratory burst - Requirement for FcγRII and tyrosine phosphorylation
    • 2, CD11b/CD18) and FcγRIII cooperate in generation of a neutrophil respiratory burst - requirement for FcγRII and tyrosine phosphorylation. J Cell Biol 1994;125:1407-1416.
    • (1994) J Cell Biol , vol.125 , pp. 1407-1416
    • Zhou, M.J.1    Brown, E.J.2
  • 55
    • 0023933120 scopus 로고
    • Localization of the binding site for the human high affinity Fc receptor on IgG
    • Duncan AR, Woof JM, Partridge LJ, Burton DR, Winter G. Localization of the binding site for the human high affinity Fc receptor on IgG. Nature 1988;332:563-564.
    • (1988) Nature , vol.332 , pp. 563-564
    • Duncan, A.R.1    Woof, J.M.2    Partridge, L.J.3    Burton, D.R.4    Winter, G.5
  • 56
    • 0025762394 scopus 로고
    • The binding affinity of human IgG for its high affinity Fc receptor is determined by multiple amino acids in the CH2 domain and is modulated by the hinge region
    • Canfield SM, Morrison SL. The binding affinity of human IgG for its high affinity Fc receptor is determined by multiple amino acids in the CH2 domain and is modulated by the hinge region. J Exp Med 1991;173:1483-1491.
    • (1991) J Exp Med , vol.173 , pp. 1483-1491
    • Canfield, S.M.1    Morrison, S.L.2
  • 57
    • 0026507779 scopus 로고
    • Mapping and comparison of the interaction sites on the Fc region of IgG responsible for triggering antibody dependent cellular cytotoxicity (ADCC) through different types of human Fcγ receptor
    • Sarmay G, Lund J, Rozsnyay Z, Gergely J, Jefferis R. Mapping and comparison of the interaction sites on the Fc region of IgG responsible for triggering antibody dependent cellular cytotoxicity (ADCC) through different types of human Fcγ receptor. Mol Immunol 1992;29:633-639.
    • (1992) Mol Immunol , vol.29 , pp. 633-639
    • Sarmay, G.1    Lund, J.2    Rozsnyay, Z.3    Gergely, J.4    Jefferis, R.5
  • 58
    • 0026567110 scopus 로고
    • Multiple binding sites on the CH2 domain of IgG for mouse FcγRII
    • Lund J, et al. Multiple binding sites on the CH2 domain of IgG for mouse FcγRII. Mol Immunol 1992;29:53-59.
    • (1992) Mol Immunol , vol.29 , pp. 53-59
    • Lund, J.1
  • 59
    • 0023123134 scopus 로고
    • Structural polymorphism of the human monocyte 40 kilodalton Fc receptor for IgG
    • Anderson CL, Ryan DH, Looney RJ, Leary PC. Structural polymorphism of the human monocyte 40 kilodalton Fc receptor for IgG. J Immunol 1987;138:2254-2256.
    • (1987) J Immunol , vol.138 , pp. 2254-2256
    • Anderson, C.L.1    Ryan, D.H.2    Looney, R.J.3    Leary, P.C.4
  • 60
    • 0025357684 scopus 로고
    • The monoclonal antibody 41H16 detects the leu-4 responder form of human FcγRII
    • Gosselin EJ, Brown MF, Anderson CL, Zipf TF, Guyre PM. The monoclonal antibody 41H16 detects the leu-4 responder form of human FcγRII. J Immunol 1990;144:1817-1822.
    • (1990) J Immunol , vol.144 , pp. 1817-1822
    • Gosselin, E.J.1    Brown, M.F.2    Anderson, C.L.3    Zipf, T.F.4    Guyre, P.M.5
  • 61
    • 0021934458 scopus 로고
    • Mapping the functional topography of Fcγ with monoclonal antibodies - Localization of epitopes interacting with the binding sites of Fc receptor on human K cells
    • Sarmay G, Jefferis R, Klein E, Benczur M, Gergely J. Mapping the functional topography of Fcγ with monoclonal antibodies - localization of epitopes interacting with the binding sites of Fc receptor on human K cells. Eur J Immunol 1985;15:1037-1042.
    • (1985) Eur J Immunol , vol.15 , pp. 1037-1042
    • Sarmay, G.1    Jefferis, R.2    Klein, E.3    Benczur, M.4    Gergely, J.5
  • 62
    • 0028670916 scopus 로고
    • Galactosylation of human IgG anti-D produced by EBV-transformed B lymphoblastoid cell lines is dependent on culture method and affects Fc receptor mediated functional activity
    • Kumpel BM, Rademacher TW, Rook GAW, Williams PJ, Wilson IBH. Galactosylation of human IgG anti-D produced by EBV-transformed B lymphoblastoid cell lines is dependent on culture method and affects Fc receptor mediated functional activity. Hum Antibodies Hybridomas 1994;5: 143-151.
    • (1994) Hum Antibodies Hybridomas , vol.5 , pp. 143-151
    • Kumpel, B.M.1    Rademacher, T.W.2    Rook, G.A.W.3    Williams, P.J.4    Wilson, I.B.H.5
  • 65
    • 0028169439 scopus 로고
    • Effect of altered CH2 associated carbohydrate structure on the functional properties and in vivo fate of chimeric mouse-human immunoglobulin G1
    • Wright A, Morrison SL. Effect of altered CH2 associated carbohydrate structure on the functional properties and in vivo fate of chimeric mouse-human immunoglobulin G1. J Exp Med 1994;180:1087-1096.
    • (1994) J Exp Med , vol.180 , pp. 1087-1096
    • Wright, A.1    Morrison, S.L.2
  • 66
    • 0024529856 scopus 로고
    • An Fc receptor structurally related to MHC class I antigens
    • Simister NE, Mostov KE. An Fc receptor structurally related to MHC class I antigens. Nature 1989;337:184-187.
    • (1989) Nature , vol.337 , pp. 184-187
    • Simister, N.E.1    Mostov, K.E.2
  • 67
    • 0029731813 scopus 로고    scopus 로고
    • Fc receptors and their interactions with immunoglobulins
    • Raghavan M, Bjorkman PJ. Fc receptors and their interactions with immunoglobulins. Annu Rev Cell Dev Biol 1996;12:181-220.
    • (1996) Annu Rev Cell Dev Biol , vol.12 , pp. 181-220
    • Raghavan, M.1    Bjorkman, P.J.2
  • 68
    • 0028061347 scopus 로고
    • A major histocompatibility complex class I-like Fc receptor cloned from human placenta - Possible role in transfer of immunoglobulin G from mother to fetus
    • Story CM, Mikulska JE, Simister NE. A major histocompatibility complex class I-like Fc receptor cloned from human placenta - possible role in transfer of immunoglobulin G from mother to fetus. J Exp Med 1994;180:2377-2381.
    • (1994) J Exp Med , vol.180 , pp. 2377-2381
    • Story, C.M.1    Mikulska, J.E.2    Simister, N.E.3
  • 69
    • 0029947639 scopus 로고    scopus 로고
    • Colocalization of the neonatal Fcy receptor and IgG in human placental term syncytiotrophoblasts
    • Kristoffersen EK, Matre R. Colocalization of the neonatal Fcy receptor and IgG in human placental term syncytiotrophoblasts. Eur J Immunol 1996;26:1668-1671.
    • (1996) Eur J Immunol , vol.26 , pp. 1668-1671
    • Kristoffersen, E.K.1    Matre, R.2
  • 70
    • 0029185950 scopus 로고
    • Short communication. Selective placental transport of maternal IgG to the fetus
    • Williams PJ, et al. Short communication. Selective placental transport of maternal IgG to the fetus. Placenta 1995;16:749-756.
    • (1995) Placenta , vol.16 , pp. 749-756
    • Williams, P.J.1
  • 71
    • 0030434866 scopus 로고    scopus 로고
    • Glycosylation and placental transport of immunoglobulin G
    • Kibe T, et al. Glycosylation and placental transport of immunoglobulin G. J Clin Biochem Nutr 1996;21:57-63.
    • (1996) J Clin Biochem Nutr , vol.21 , pp. 57-63
    • Kibe, T.1
  • 74
    • 0029891262 scopus 로고    scopus 로고
    • 2 microglobulin-containing neonatal intestinal transport receptor
    • 2 microglobulin-containing neonatal intestinal transport receptor. Proc Natl Acad Sci USA 1996;93:5512-5516.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 5512-5516
    • Junghans, R.P.1    Anderson, C.L.2
  • 75
    • 0031449358 scopus 로고    scopus 로고
    • FcRn: The MHC class I-related receptor that is more than an IgG transporter
    • Ghetie V, Ward ES. FcRn: the MHC class I-related receptor that is more than an IgG transporter. Immunol Today 1997;18:592-598.
    • (1997) Immunol Today , vol.18 , pp. 592-598
    • Ghetie, V.1    Ward, E.S.2
  • 76
    • 0030796064 scopus 로고    scopus 로고
    • Increasing the serum persistence of an IgG fragment by random mutagenesis
    • Ghetie V, et al. Increasing the serum persistence of an IgG fragment by random mutagenesis. Nat Biotechnol 1997;15:637-640.
    • (1997) Nat Biotechnol , vol.15 , pp. 637-640
    • Ghetie, V.1
  • 77
    • 0000146003 scopus 로고
    • A theoretical model of gammaglobulin catabolism
    • Brambell FWR, Hemmings WA, Morris IG. A theoretical model of gammaglobulin catabolism. Nature 1964;203:1352-1355.
    • (1964) Nature , vol.203 , pp. 1352-1355
    • Brambell, F.W.R.1    Hemmings, W.A.2    Morris, I.G.3
  • 78
    • 0015327927 scopus 로고
    • The catabolism of human G immunoglobulins of different heavy chain subclasses. 3. The catabolism of heavy chain disease proteins and of Fc fragments of myeloma proteins
    • Spiegelberg HL, Fishkin BG. The catabolism of human G immunoglobulins of different heavy chain subclasses. 3. The catabolism of heavy chain disease proteins and of Fc fragments of myeloma proteins. Clin Exp Immunol 1972;10:599-607.
    • (1972) Clin Exp Immunol , vol.10 , pp. 599-607
    • Spiegelberg, H.L.1    Fishkin, B.G.2
  • 79
    • 0026512163 scopus 로고
    • Recombinant mouse monoclonal antibodies with single amino acid substitutions affecting C1q and high affinity Fc receptor binding have identical serum half-lives in the Balb/c mouse
    • Wawrzynczak EJ, Denham S, Parnell GD, Cumber AJ, Jones PT, Winter G. Recombinant mouse monoclonal antibodies with single amino acid substitutions affecting C1q and high affinity Fc receptor binding have identical serum half-lives in the Balb/c mouse. Mol Immunol 1992;29:221-227.
    • (1992) Mol Immunol , vol.29 , pp. 221-227
    • Wawrzynczak, E.J.1    Denham, S.2    Parnell, G.D.3    Cumber, A.J.4    Jones, P.T.5    Winter, G.6
  • 80
    • 0028220297 scopus 로고
    • Identifying amino acid residues that influence plasma clearance of murine IgG1 fragments by site-directed mutagenesis
    • Kim JK, Tsen MF, Ghetie V, Ward ES. Identifying amino acid residues that influence plasma clearance of murine IgG1 fragments by site-directed mutagenesis. Eur J Immunol 1994;24:542-548.
    • (1994) Eur J Immunol , vol.24 , pp. 542-548
    • Kim, J.K.1    Tsen, M.F.2    Ghetie, V.3    Ward, E.S.4
  • 81
    • 0023897194 scopus 로고
    • The binding site for C1q on IgG
    • Duncan AR, Winter G. The binding site for C1q on IgG. Nature 1988;332:738-740.
    • (1988) Nature , vol.332 , pp. 738-740
    • Duncan, A.R.1    Winter, G.2
  • 83
    • 0025763066 scopus 로고
    • Aglycosylated chimeric mouse human IgG1 antibody retains some effector function
    • Dorai H, Mueller BM, Reisfeld RA, Gillies SD. Aglycosylated chimeric mouse human IgG1 antibody retains some effector function. Hybridoma 1991;10:211-217.
    • (1991) Hybridoma , vol.10 , pp. 211-217
    • Dorai, H.1    Mueller, B.M.2    Reisfeld, R.A.3    Gillies, S.D.4
  • 84
    • 0024854278 scopus 로고
    • Substitution of asparagine-324 with aspartic-acid in the Fc portion of mouse antibodies reduces their capacity for C1q binding
    • Nose M, Leanderson T. Substitution of asparagine-324 with aspartic-acid in the Fc portion of mouse antibodies reduces their capacity for C1q binding. Eur J Immunol 1989;19:2179-2181.
    • (1989) Eur J Immunol , vol.19 , pp. 2179-2181
    • Nose, M.1    Leanderson, T.2
  • 85
    • 0025371129 scopus 로고
    • Inhibition of processing of asparagine-linked carbohydrate chains on IgG2a by using swainsonine has no influence upon antibody effector functions in vitro
    • Nose M, Heyman B. Inhibition of processing of asparagine-linked carbohydrate chains on IgG2a by using swainsonine has no influence upon antibody effector functions in vitro. J Immunol 1990;145:910-914.
    • (1990) J Immunol , vol.145 , pp. 910-914
    • Nose, M.1    Heyman, B.2
  • 87
    • 0029014041 scopus 로고
    • Rheumatoid factors, B cells and immunoglobulin genes
    • Jefferis R. Rheumatoid factors, B cells and immunoglobulin genes. Br Med Bull 1995;51:312-331.
    • (1995) Br Med Bull , vol.51 , pp. 312-331
    • Jefferis, R.1
  • 88
    • 0021059401 scopus 로고
    • Immunogenic and antigenic epitopes of immunoglobulins. 8. A human monoclonal rheumatoid factor having specificity for a discontinuous epitope determined by histidine arginine interchange as residue-435 of immunoglobulin G
    • Jefferis R, Iskandar M, Jaafar N, Steinitz M. Immunogenic and antigenic epitopes of immunoglobulins. 8. A human monoclonal rheumatoid factor having specificity for a discontinuous epitope determined by histidine arginine interchange as residue-435 of immunoglobulin G. Immunol Lett 1984;7:191-194.
    • (1984) Immunol Lett , vol.7 , pp. 191-194
    • Jefferis, R.1    Iskandar, M.2    Jaafar, N.3    Steinitz, M.4
  • 90
    • 0027940677 scopus 로고
    • Studies of protein A and Herpes simplex virus 1 induced Fcγ-binding specificities - Different binding patterns for IgG3 from Caucasian and oriental subjects
    • Johansson PJH, Ota T, Tsuchiya N, Malone CC, Williams RC. Studies of protein A and Herpes simplex virus 1 induced Fcγ-binding specificities - different binding patterns for IgG3 from Caucasian and oriental subjects. Immunology 1994;83:631-638.
    • (1994) Immunology , vol.83 , pp. 631-638
    • Johansson, P.J.H.1    Ota, T.2    Tsuchiya, N.3    Malone, C.C.4    Williams, R.C.5
  • 91
    • 0021101977 scopus 로고
    • The effect of aglycosylation on the binding of mouse IgG to staphylococcal protein A
    • Leatherbarrow RJ, Dwek RA. The effect of aglycosylation on the binding of mouse IgG to staphylococcal protein A. FEBS Lett 1983;164:227-230.
    • (1983) FEBS Lett , vol.164 , pp. 227-230
    • Leatherbarrow, R.J.1    Dwek, R.A.2
  • 92
    • 0021041854 scopus 로고
    • Biological significance of carbohydrate chains on monoclonal antibodies
    • Nose M, Wigzell H. Biological significance of carbohydrate chains on monoclonal antibodies. Proc Nath Acad Sci USA 1983;80:6632-6636.
    • (1983) Proc Nath Acad Sci USA , vol.80 , pp. 6632-6636
    • Nose, M.1    Wigzell, H.2
  • 93
    • 0029643787 scopus 로고
    • Model for the complex between protein G and an antibody Fc fragment in solution
    • Kato K, et al. Model for the complex between protein G and an antibody Fc fragment in solution. Structure 1995;3:79-85.
    • (1995) Structure , vol.3 , pp. 79-85
    • Kato, K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.