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Volumn 25, Issue , 2007, Pages 21-50

The impact of glycosylation on the biological function and structure of human immunoglobulins

Author keywords

Fc receptors; Glycoforms; Mannan binding lectin; Rheumatoid arthritis

Indexed keywords

ALEMTUZUMAB; ASPARAGINE LINKED OLIGOSACCHARIDE; EPITOPE; GALECTIN 3; GLYCAN; GLYCOPROTEIN; GLYCOPROTEIN GP 120; IMMUNOGLOBULIN; IMMUNOGLOBULIN A; IMMUNOGLOBULIN A1; IMMUNOGLOBULIN A2; IMMUNOGLOBULIN D; IMMUNOGLOBULIN E; IMMUNOGLOBULIN G1; IMMUNOGLOBULIN M; LECTIN; OLIGOSACCHARIDE; SUGAR;

EID: 34247122497     PISSN: 07320582     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.immunol.25.022106.141702     Document Type: Review
Times cited : (1094)

References (143)
  • 2
    • 0017334109 scopus 로고
    • Structure of an antibody combining site by magnetic resonance
    • Dwek RA, Wain-Hobson S, Dower S, Gettins P, Sutton B, et al. 1977. Structure of an antibody combining site by magnetic resonance. Nature 266:31-37
    • (1977) Nature , vol.266 , pp. 31-37
    • Dwek, R.A.1    Wain-Hobson, S.2    Dower, S.3    Gettins, P.4    Sutton, B.5
  • 3
    • 0028946013 scopus 로고
    • Glycobiology: Towards understanding the function of sugars
    • Dwek RA. 1995. Glycobiology: "towards understanding the function of sugars." Biochem. Soc. Trans. 23:1-25
    • (1995) Biochem. Soc. Trans , vol.23 , pp. 1-25
    • Dwek, R.A.1
  • 4
    • 0019522383 scopus 로고
    • Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9-and 2.8-Å resolution
    • Deisenhofer J. 1981. Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9-and 2.8-Å resolution. Biochemistry 20:2361-70
    • (1981) Biochemistry , vol.20 , pp. 2361-2370
    • Deisenhofer, J.1
  • 5
    • 0022414766 scopus 로고
    • Association of rheumatoid arthritis and primary osteoarthritis with changes in the glycosylation pattern of total serum IgG
    • Parekh RB, Dwek RA, Sutton BJ, Fernandes DL, Leung A, et al. 1985. Association of rheumatoid arthritis and primary osteoarthritis with changes in the glycosylation pattern of total serum IgG. Nature 316:452-57
    • (1985) Nature , vol.316 , pp. 452-457
    • Parekh, R.B.1    Dwek, R.A.2    Sutton, B.J.3    Fernandes, D.L.4    Leung, A.5
  • 6
    • 0028962403 scopus 로고
    • Glycosylation changes of IgG associated with rheumatoid arthritis can activate complement via the mannose-binding protein
    • Malhotra R, Wormald MR, Rudd PM, Fischer PB, Dwek RA, Sim RB. 1995. Glycosylation changes of IgG associated with rheumatoid arthritis can activate complement via the mannose-binding protein. Nat. Med. 1:237-43
    • (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
  • 11
    • 18244422922 scopus 로고    scopus 로고
    • The broadly neutralizing anti-human immunodeficiency virus type 1 antibody 2G12 recognizes a cluster of alpha1→2 mannose residues on the outer face of gp120
    • Scanlan CN, Pantophlet R, Wormald MR, Ollmann Saphire E, Stanfield R, et al. 2002. The broadly neutralizing anti-human immunodeficiency virus type 1 antibody 2G12 recognizes a cluster of alpha1→2 mannose residues on the outer face of gp120. J. Virol. 76:7306-21
    • (2002) J. Virol , vol.76 , pp. 7306-7321
    • Scanlan, C.N.1    Pantophlet, R.2    Wormald, M.R.3    Ollmann Saphire, E.4    Stanfield, R.5
  • 12
    • 12444291017 scopus 로고    scopus 로고
    • Antibody domain exchange is an immunological solution to carbohydrate cluster recognition
    • Calarese DA, Scanlan CN, Zwick MB, Deechongkit S, Mimura Y, et al. 2003. Antibody domain exchange is an immunological solution to carbohydrate cluster recognition. Science 300:2065-71
    • (2003) Science , vol.300 , pp. 2065-2071
    • Calarese, D.A.1    Scanlan, C.N.2    Zwick, M.B.3    Deechongkit, S.4    Mimura, Y.5
  • 14
    • 0018654090 scopus 로고
    • Three-dimensional structure of immunoglobulins
    • Amzel LM, Poljak RJ. 1979. Three-dimensional structure of immunoglobulins. Annu. Rev. Biochem. 48:961-97
    • (1979) Annu. Rev. Biochem , vol.48 , pp. 961-997
    • Amzel, L.M.1    Poljak, R.J.2
  • 15
    • 0035081693 scopus 로고    scopus 로고
    • The influence of glycosylation on the thermal stability and effector function expression of human IgG1-Fc: Properties of a series of truncated glycoforms
    • Mimura Y, Church S, Ghirlando R, Ashton PR, Dong S, et al. 2000. The influence of glycosylation on the thermal stability and effector function expression of human IgG1-Fc: properties of a series of truncated glycoforms. Mol. Immunol. 37:697-706
    • (2000) Mol. Immunol , vol.37 , pp. 697-706
    • Mimura, Y.1    Church, S.2    Ghirlando, R.3    Ashton, P.R.4    Dong, S.5
  • 16
    • 0037047377 scopus 로고    scopus 로고
    • The role of constant region carbohydrate in the assembly and secretion of human IgD and IgA1
    • Gala FA, Morrison SL. 2002. The role of constant region carbohydrate in the assembly and secretion of human IgD and IgA1. J. Biol. Chem. 277:29005-11
    • (2002) J. Biol. Chem , vol.277 , pp. 29005-29011
    • Gala, F.A.1    Morrison, S.L.2
  • 17
  • 18
    • 0033571091 scopus 로고    scopus 로고
    • Binding and uptake of agalactosyl IgG by mannose receptor on macrophages and dendritic cells
    • Dong X, Storkus WJ, Salter RD. 1999. Binding and uptake of agalactosyl IgG by mannose receptor on macrophages and dendritic cells. J. Immunol. 163:5427-34
    • (1999) J. Immunol , vol.163 , pp. 5427-5434
    • Dong, X.1    Storkus, W.J.2    Salter, R.D.3
  • 19
    • 0020738965 scopus 로고
    • The three-dimensional structure of the carbohydrate within the Fc fragment of immunoglobulin G
    • Sutton BJ, Phillips DC. 1983. The three-dimensional structure of the carbohydrate within the Fc fragment of immunoglobulin G. Biochem. Soc. Trans. 11(Pt. 2):130-32
    • (1983) Biochem. Soc. Trans , vol.11 , Issue.PART. 2 , pp. 130-132
    • Sutton, B.J.1    Phillips, D.C.2
  • 21
    • 10744225031 scopus 로고    scopus 로고
    • Detailed glycan analysis of serum glycoproteins of patients with congenital disorders of glycosylation indicates the specific defective glycan processing step and provides an insight into pathogenesis
    • Butler M, Quelhas D, Critchley AJ, Carchon H, Hebestreit HF, et al. 2003. Detailed glycan analysis of serum glycoproteins of patients with congenital disorders of glycosylation indicates the specific defective glycan processing step and provides an insight into pathogenesis. Glycobiology 13:601-22
    • (2003) Glycobiology , vol.13 , pp. 601-622
    • Butler, M.1    Quelhas, D.2    Critchley, A.J.3    Carchon, H.4    Hebestreit, H.F.5
  • 22
    • 0025290953 scopus 로고
    • A comparative study of the N-linked oligosaccharide structures of human IgG subclass proteins
    • Jefferis R, Lund J, Mizutani H, Nakagawa H, Kawazoe Y, et al. 1990. A comparative study of the N-linked oligosaccharide structures of human IgG subclass proteins. Biochem. J. 268:529-37
    • (1990) Biochem. J , vol.268 , pp. 529-537
    • Jefferis, R.1    Lund, J.2    Mizutani, H.3    Nakagawa, H.4    Kawazoe, Y.5
  • 23
    • 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, et al. 1997. Variations in oligosaccharide-protein interactions in immunoglobulin G determine the site-specific glycosylation profiles and modulate the dynamic motion of the Fc oligosaccharides. Biochemistry 36:1370-80
    • (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
  • 24
    • 0023912648 scopus 로고
    • Age-related galactosylation of the N-linked oligosaccharides of human serum IgG
    • Parekh R, Roitt I, Isenberg D, Dwek R, Rademacher T. 1988. Age-related galactosylation of the N-linked oligosaccharides of human serum IgG. J. Exp. Med. 167:1731-36
    • (1988) J. Exp. Med , vol.167 , pp. 1731-1736
    • Parekh, R.1    Roitt, I.2    Isenberg, D.3    Dwek, R.4    Rademacher, T.5
  • 25
    • 0011655887 scopus 로고
    • Magnetic resonance studies on antibody combining sites
    • Dwek RA, Leatherbarrow RJ. 1983. Magnetic resonance studies on antibody combining sites. Period. Biol. 85 (Suppl. 2):21-29
    • (1983) Period. Biol , vol.85 , Issue.SUPPL. 2 , pp. 21-29
    • Dwek, R.A.1    Leatherbarrow, R.J.2
  • 26
    • 0021041854 scopus 로고
    • Biological significance of carbohydrate chains on monoclonal antibodies
    • Padlan EA. 1991. Biological significance of carbohydrate chains on monoclonal antibodies. Proc. Natl. Acad. Sci. USA 80:6632-36
    • (1991) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 6632-6636
    • Padlan, E.A.1
  • 27
    • 0037474543 scopus 로고    scopus 로고
    • Structural analysis of human IgG-Fc glycoforms reveals a correlation between glycosylation and structural integrity
    • Krapp S, Mimura Y, Jefferis R, Huber R, Sondermann P. 2003. Structural analysis of human IgG-Fc glycoforms reveals a correlation between glycosylation and structural integrity. J. Mol. Biol. 325:979-89
    • (2003) J. Mol. Biol , vol.325 , pp. 979-989
    • Krapp, S.1    Mimura, Y.2    Jefferis, R.3    Huber, R.4    Sondermann, P.5
  • 28
    • 0030470557 scopus 로고    scopus 로고
    • Multiple interactions of IgG with its core oligosaccharide can modulate recognition by complement and human Fc gamma receptor I and influence the synthesis of its oligosaccharide chains
    • Lund J, Takahashi N, Pound JD, Goodall M, Jefferis R. 1996. Multiple interactions of IgG with its core oligosaccharide can modulate recognition by complement and human Fc gamma receptor I and influence the synthesis of its oligosaccharide chains. J. Immunol. 157:4963-69
    • (1996) J. Immunol , vol.157 , pp. 4963-4969
    • Lund, J.1    Takahashi, N.2    Pound, J.D.3    Goodall, M.4    Jefferis, R.5
  • 29
    • 0018199718 scopus 로고
    • Structure-function relationships in human immunoglobulin E
    • Dorrington KJ, Bennich HH. 1978. Structure-function relationships in human immunoglobulin E. Immunol. Rev. 41:3-25
    • (1978) Immunol. Rev , vol.41 , pp. 3-25
    • Dorrington, K.J.1    Bennich, H.H.2
  • 30
    • 0016382122 scopus 로고
    • Structure of the carbohydrate units of IgE immunoglobulin. II. Sequence of the sialic acid-containing glycopeptides
    • Baenziger J, Kornfeld S, Kochwa S. 1974. Structure of the carbohydrate units of IgE immunoglobulin. II. Sequence of the sialic acid-containing glycopeptides. J. Biol. Chem. 249:1897-903
    • (1974) J. Biol. Chem , vol.249 , pp. 1897-1903
    • Baenziger, J.1    Kornfeld, S.2    Kochwa, S.3
  • 31
    • 0016382380 scopus 로고
    • Structure of the carbohydrate units of IgE immunoglobulin. I. Over-all composition, glycopeptide isolation, and structure of the high mannose oligosaccharide unit
    • Baenziger J, Kornfeld S, Kochwa S. 1974. Structure of the carbohydrate units of IgE immunoglobulin. I. Over-all composition, glycopeptide isolation, and structure of the high mannose oligosaccharide unit. J. Biol. Chem. 249:1889-96
    • (1974) J. Biol. Chem , vol.249 , pp. 1889-1896
    • Baenziger, J.1    Kornfeld, S.2    Kochwa, S.3
  • 32
    • 9144261693 scopus 로고    scopus 로고
    • The glycosylation of human serum IgD and IgE and the accessibility of identified oligomannose structures for interaction with mannan-binding lectin
    • Arnold JN, Radcliffe CM, Wormald MR, Royle L, Harvey DJ, et al. 2004. The glycosylation of human serum IgD and IgE and the accessibility of identified oligomannose structures for interaction with mannan-binding lectin. J. Immunol. 173:6831-40
    • (2004) J. Immunol , vol.173 , pp. 6831-6840
    • Arnold, J.N.1    Radcliffe, C.M.2    Wormald, M.R.3    Royle, L.4    Harvey, D.J.5
  • 33
    • 0027508083 scopus 로고
    • S-type mammalian lectins in allergic inflammation
    • Liu FT. 1993. S-type mammalian lectins in allergic inflammation. Immunol. Today 14:486-90
    • (1993) Immunol. Today , vol.14 , pp. 486-490
    • Liu, F.T.1
  • 34
    • 4744345820 scopus 로고    scopus 로고
    • IgA function - variations on a theme
    • Woof JM, Kerr MA. 2004. IgA function - variations on a theme. Immunology 113:175-77
    • (2004) Immunology , vol.113 , pp. 175-177
    • Woof, J.M.1    Kerr, M.A.2
  • 35
    • 0025007135 scopus 로고
    • The structure and function of human IgA
    • Kerr MA. 1990. The structure and function of human IgA. Biochem. J. 271:285-96
    • (1990) Biochem. J , vol.271 , pp. 285-296
    • Kerr, M.A.1
  • 38
    • 0028280439 scopus 로고
    • Structural analysis of the N-glycans from human immunoglobulin A1: Comparison of normal human serum immunoglobulin A1 with that isolated from patients with rheumatoid arthritis
    • Field MC, Amatayakul-Chantler S, Rademacher TW, Rudd PM, Dwek RA. 1994. Structural analysis of the N-glycans from human immunoglobulin A1: comparison of normal human serum immunoglobulin A1 with that isolated from patients with rheumatoid arthritis. Biochem. J. 299(Pt. 1):261-75
    • (1994) Biochem. J , vol.299 , Issue.PART. 1 , pp. 261-275
    • Field, M.C.1    Amatayakul-Chantler, S.2    Rademacher, T.W.3    Rudd, P.M.4    Dwek, R.A.5
  • 39
    • 0031915973 scopus 로고    scopus 로고
    • The glycosylation and structure of human serum IgA1, Fab, and Fc regions and the role of N-glycosylation on Fc alpha receptor interactions
    • Mattu TS, Pleass RJ, Willis AC, Kilian M, Wormald MR, et al. 1998. The glycosylation and structure of human serum IgA1, Fab, and Fc regions and the role of N-glycosylation on Fc alpha receptor interactions. J. Biol. Chem. 273:2260-72
    • (1998) J. Biol. Chem , vol.273 , pp. 2260-2272
    • Mattu, T.S.1    Pleass, R.J.2    Willis, A.C.3    Kilian, M.4    Wormald, M.R.5
  • 40
    • 0016293141 scopus 로고
    • Structure of the carbohydrate units of IgA1 immunoglobulin. I. Composition, glycopeptide isolation, and structure of the asparagine-linked oligosaccharide units
    • Baenziger J, Kornfeld S. 1974. Structure of the carbohydrate units of IgA1 immunoglobulin. I. Composition, glycopeptide isolation, and structure of the asparagine-linked oligosaccharide units. J. Biol. Chem. 249:7260-69
    • (1974) J. Biol. Chem , vol.249 , pp. 7260-7269
    • Baenziger, J.1    Kornfeld, S.2
  • 41
    • 0028114209 scopus 로고
    • Carbohydrate heterogeneity of human myeloma proteins of the IgA1 and IgA2 subclasses
    • Endo T, Mestecky J, Kulhavy R, Kobata A. 1994. Carbohydrate heterogeneity of human myeloma proteins of the IgA1 and IgA2 subclasses. Mol. Immunol. 31:1415-22
    • (1994) Mol. Immunol , vol.31 , pp. 1415-1422
    • Endo, T.1    Mestecky, J.2    Kulhavy, R.3    Kobata, A.4
  • 43
    • 0028998769 scopus 로고
    • The asialoglycoprotein receptor: Relationships between structure, function, and expression
    • Stockert RJ. 1995. The asialoglycoprotein receptor: relationships between structure, function, and expression. Physiol. Rev. 75:591-6 09
    • (1995) Physiol. Rev , vol.75 , Issue.591-596 , pp. 09
    • Stockert, R.J.1
  • 44
    • 0035500293 scopus 로고    scopus 로고
    • Johansen FE, Braathen R, Brandtzaeg P. 2001. The J chain is essential for polymeric Ig receptor-mediated epithelial transport of IgA. J. Immunol. 167:5185-92
    • Johansen FE, Braathen R, Brandtzaeg P. 2001. The J chain is essential for polymeric Ig receptor-mediated epithelial transport of IgA. J. Immunol. 167:5185-92
  • 45
    • 0038165519 scopus 로고    scopus 로고
    • Secretory IgA N- and O-glycans provide a link between the innate and adaptive immune systems
    • Royle L, Roos A, Harvey DJ, Wormald MR, van Gijlswijk-Janssen D, et al. 2003. Secretory IgA N- and O-glycans provide a link between the innate and adaptive immune systems. J. Biol. Chem. 278:20140-53
    • (2003) J. Biol. Chem , vol.278 , pp. 20140-20153
    • Royle, L.1    Roos, A.2    Harvey, D.J.3    Wormald, M.R.4    van Gijlswijk-Janssen, D.5
  • 46
    • 0032526642 scopus 로고    scopus 로고
    • Wiersma EJ, Collins C, Fazel S, Shulman MJ. 1998. Structural and functional analysis of J chain-deficient IgM. J. Immunol. 160:5979-89
    • Wiersma EJ, Collins C, Fazel S, Shulman MJ. 1998. Structural and functional analysis of J chain-deficient IgM. J. Immunol. 160:5979-89
  • 48
    • 0030861590 scopus 로고    scopus 로고
    • Interaction of antigens and antibodies at mucosal surfaces
    • Lamm ME. 1997. Interaction of antigens and antibodies at mucosal surfaces. Annu. Rev. Microbiol. 51:311-40
    • (1997) Annu. Rev. Microbiol , vol.51 , pp. 311-340
    • Lamm, M.E.1
  • 49
    • 2442649014 scopus 로고    scopus 로고
    • Oligosaccharide side chains on human secretory IgA serve as receptors for ricin
    • Mantis NJ, Farrant SA, Mehta S. 2004. Oligosaccharide side chains on human secretory IgA serve as receptors for ricin. J. Immunol. 172:6838-45
    • (2004) J. Immunol , vol.172 , pp. 6838-6845
    • Mantis, N.J.1    Farrant, S.A.2    Mehta, S.3
  • 50
    • 0031824084 scopus 로고    scopus 로고
    • Fab-independent antiadhesion effects of secretory immunoglobulin A on S-fimbriated Escherichia coli are mediated by sialyloligosaccharides
    • Schroten H, Stapper C, Plogmann R, Kohler H, Hacker J, Hanisch FG. 1998. Fab-independent antiadhesion effects of secretory immunoglobulin A on S-fimbriated Escherichia coli are mediated by sialyloligosaccharides. Infect. Immun. 66:3971-73
    • (1998) Infect. Immun , vol.66 , pp. 3971-3973
    • Schroten, H.1    Stapper, C.2    Plogmann, R.3    Kohler, H.4    Hacker, J.5    Hanisch, F.G.6
  • 51
    • 0025111615 scopus 로고
    • Secretory immunoglobulin A carries oligosaccharide receptors for Escherichia coli type 1 fimbrial lectin
    • Wold AE, Mestecky J, Tomana M, Kobata A, Ohbayashi H, et al. 1990. Secretory immunoglobulin A carries oligosaccharide receptors for Escherichia coli type 1 fimbrial lectin. Infect. Immun. 58:3073-77
    • (1990) Infect. Immun , vol.58 , pp. 3073-3077
    • Wold, A.E.1    Mestecky, J.2    Tomana, M.3    Kobata, A.4    Ohbayashi, H.5
  • 52
    • 18544412344 scopus 로고    scopus 로고
    • Krugmann S, Pleass RJ, Atkin JD, Woof JM. 1997. Mutagenesis of J chain residues critical for IgA dimer assembly. Biochem. Soc. Trans. 25:323
    • Krugmann S, Pleass RJ, Atkin JD, Woof JM. 1997. Mutagenesis of J chain residues critical for IgA dimer assembly. Biochem. Soc. Trans. 25:323
  • 53
    • 0027512558 scopus 로고
    • An in vitro adherence assay reveals that Helicobacter pylori exhibits cell lineage-specific tropism in the human gastric epithelium
    • Falk P, Roth KA, Boren T, Westblom TU, Gordon JI, Normark S. 1993. An in vitro adherence assay reveals that Helicobacter pylori exhibits cell lineage-specific tropism in the human gastric epithelium. Proc. Natl. Acad. Sci. USA 90:2035-39
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2035-2039
    • Falk, P.1    Roth, K.A.2    Boren, T.3    Westblom, T.U.4    Gordon, J.I.5    Normark, S.6
  • 54
    • 0027749278 scopus 로고
    • Attachment of Helicobacter pylori to human gastric epithelium mediated by blood group antigens
    • Boren T, Falk P, Roth KA, Larson G, Normark S. 1993. Attachment of Helicobacter pylori to human gastric epithelium mediated by blood group antigens. Science 262:1892-95
    • (1993) Science , vol.262 , pp. 1892-1895
    • Boren, T.1    Falk, P.2    Roth, K.A.3    Larson, G.4    Normark, S.5
  • 57
    • 25144489575 scopus 로고    scopus 로고
    • Semi-extended solution structure of human myeloma immunoglobulin D determined by constrained X-ray scattering
    • Sun Z, Almogren A, Furtado PB, Chowdhury B, Kerr MA, Perkins SJ. 2005. Semi-extended solution structure of human myeloma immunoglobulin D determined by constrained X-ray scattering. J. Mol. Biol. 353:155-73
    • (2005) J. Mol. Biol , vol.353 , pp. 155-173
    • Sun, Z.1    Almogren, A.2    Furtado, P.B.3    Chowdhury, B.4    Kerr, M.A.5    Perkins, S.J.6
  • 59
    • 0020544578 scopus 로고
    • Structures of the oligosaccharides present at the three asparagine-linked glycosylation sites of human IgD
    • Mellis SJ, Baenziger JU. 1983. Structures of the oligosaccharides present at the three asparagine-linked glycosylation sites of human IgD. J. Biol. Chem. 258:11546-56
    • (1983) J. Biol. Chem , vol.258 , pp. 11546-11556
    • Mellis, S.J.1    Baenziger, J.U.2
  • 60
    • 0032502282 scopus 로고    scopus 로고
    • Oligosaccharide binding characteristics of the molecular chaperones calnexin and calreticulin
    • Vassilakos A, Michalak M, Lehrman MA, Wlliams DB. 1998. Oligosaccharide binding characteristics of the molecular chaperones calnexin and calreticulin. Biochemistry 37:3480-90
    • (1998) Biochemistry , vol.37 , pp. 3480-3490
    • Vassilakos, A.1    Michalak, M.2    Lehrman, M.A.3    Wlliams, D.B.4
  • 61
  • 62
    • 0033521072 scopus 로고    scopus 로고
    • Setting the standards: Quality control in the secretory pathway
    • Ellgaard L, Molinari M, Helenius A. 1999. Setting the standards: quality control in the secretory pathway. Science 286:1882-88
    • (1999) Science , vol.286 , pp. 1882-1888
    • Ellgaard, L.1    Molinari, M.2    Helenius, A.3
  • 64
    • 2442487932 scopus 로고    scopus 로고
    • Monoglucosylated glycans in the secreted human complement component C3: Implications for protein biosynthesis and structure
    • Crispin MD, Ritchie GE, Critchley AJ, Morgan BP, Wilson IA, et al. 2004. Monoglucosylated glycans in the secreted human complement component C3: implications for protein biosynthesis and structure. FEBS Lett. 566:270-74
    • (2004) FEBS Lett , vol.566 , pp. 270-274
    • Crispin, M.D.1    Ritchie, G.E.2    Critchley, A.J.3    Morgan, B.P.4    Wilson, I.A.5
  • 65
    • 0025782587 scopus 로고
    • The conformational effects of N-glycosylation on the tailpiece from serum IgM
    • Wormald MR, Wooten EW, Bazzo R, Edge CJ, Feinstein A, et al. 1991. The conformational effects of N-glycosylation on the tailpiece from serum IgM. Eur. J. Biochem198:131-39
    • (1991) Eur. J. Biochem , vol.198 , pp. 131-139
    • Wormald, M.R.1    Wooten, E.W.2    Bazzo, R.3    Edge, C.J.4    Feinstein, A.5
  • 66
    • 0022512382 scopus 로고
    • Aregion of the immunoglobulin-mu heavy chain necessary for forming pentameric IgM
    • Baker MD, Wu GE, Toone WM, Murialdo H, Davis AC, Shulman MJ. 1986. Aregion of the immunoglobulin-mu heavy chain necessary for forming pentameric IgM. J. Immunol. 137:1724-28
    • (1986) J. Immunol , vol.137 , pp. 1724-1728
    • Baker, M.D.1    Wu, G.E.2    Toone, W.M.3    Murialdo, H.4    Davis, A.C.5    Shulman, M.J.6
  • 67
    • 23844468114 scopus 로고    scopus 로고
    • Human serum IgM glycosylation: Identification of glycoforms that can bind to mannan-binding lectin
    • Arnold JN, Wormald MR, Suter DM, Radcliffe CM, Harvey DJ, et al. 2005. Human serum IgM glycosylation: identification of glycoforms that can bind to mannan-binding lectin. J. Biol. Chem. 280:29080-87
    • (2005) J. Biol. Chem , vol.280 , pp. 29080-29087
    • Arnold, J.N.1    Wormald, M.R.2    Suter, D.M.3    Radcliffe, C.M.4    Harvey, D.J.5
  • 68
    • 0018395656 scopus 로고
    • Structure of the high mannose oligosaccharides of a human IgM myeloma protein. II. The minor oligosaccharides of high mannose glycopeptide
    • Chapman A, Kornfeld R. 1979. Structure of the high mannose oligosaccharides of a human IgM myeloma protein. II. The minor oligosaccharides of high mannose glycopeptide. J. Biol. Chem. 254:824-28
    • (1979) J. Biol. Chem , vol.254 , pp. 824-828
    • Chapman, A.1    Kornfeld, R.2
  • 69
    • 0018757886 scopus 로고
    • Structure of the high mannose oligosaccharides of a human IgM myeloma protein. I. The major oligosaccharides of the two high mannose glycopeptides
    • Chapman A, Kornfeld R. 1979. Structure of the high mannose oligosaccharides of a human IgM myeloma protein. I. The major oligosaccharides of the two high mannose glycopeptides. J. Biol. Chem. 254:816-23
    • (1979) J. Biol. Chem , vol.254 , pp. 816-823
    • Chapman, A.1    Kornfeld, R.2
  • 70
    • 0028952933 scopus 로고
    • Characterization of the glycosylation of a human IgM produced by a human-mouse hybridoma
    • Monica TJ, Williams SB, Goochee CF, Maiorella BL. 1995. Characterization of the glycosylation of a human IgM produced by a human-mouse hybridoma. Glycobiology 5:175-85
    • (1995) Glycobiology , vol.5 , pp. 175-185
    • Monica, T.J.1    Williams, S.B.2    Goochee, C.F.3    Maiorella, B.L.4
  • 71
    • 0018642542 scopus 로고
    • Phylogeny of the rabbit gamma-chain determinants: A d12-like antigenic determinant in Pronolagus rupestris
    • Hamers-Casterman C, Wittouck E, van der Loo W, Hamers R. 1979. Phylogeny of the rabbit gamma-chain determinants: a d12-like antigenic determinant in Pronolagus rupestris. J. Immunogenet. 6:373-81
    • (1979) J. Immunogenet , vol.6 , pp. 373-381
    • Hamers-Casterman, C.1    Wittouck, E.2    van der Loo, W.3    Hamers, R.4
  • 72
    • 0020634270 scopus 로고
    • Structures of the O-glycosidically linked oligosaccharides of human IgD
    • Mellis SJ, Baenziger JU. 1983. Structures of the O-glycosidically linked oligosaccharides of human IgD. J. Biol. Chem. 258:11557-63
    • (1983) J. Biol. Chem , vol.258 , pp. 11557-11563
    • Mellis, S.J.1    Baenziger, J.U.2
  • 73
    • 0016270014 scopus 로고
    • Structure of the carbohydrate units of IgA1 immunoglobulin. II. Structure of the O-glycosidically linked oligosaccharide units
    • Baenziger J, Kornfeld S. 1974. Structure of the carbohydrate units of IgA1 immunoglobulin. II. Structure of the O-glycosidically linked oligosaccharide units. J. Biol. Chem. 249:7270-81
    • (1974) J. Biol. Chem , vol.249 , pp. 7270-7281
    • Baenziger, J.1    Kornfeld, S.2
  • 74
    • 4444307298 scopus 로고    scopus 로고
    • Human serum IgA1 is substituted with up to six O-glycans as shown by matrix assisted laser desorption ionisation time-of-flight mass spectrometry
    • Tarelli E, Smith AC, Hendry BM, Challacombe SJ, Pouria S. 2004. Human serum IgA1 is substituted with up to six O-glycans as shown by matrix assisted laser desorption ionisation time-of-flight mass spectrometry. Carbohydr. Res. 339:2329-35
    • (2004) Carbohydr. Res , vol.339 , pp. 2329-2335
    • Tarelli, E.1    Smith, A.C.2    Hendry, B.M.3    Challacombe, S.J.4    Pouria, S.5
  • 75
    • 0030014069 scopus 로고    scopus 로고
    • Biological significance of IgA1 proteases in bacterial colonization and pathogenesis: Critical evaluation of experimental evidence
    • Kilian M, Reinholdt J, Lomholt H, Poulsen K, Frandsen EV. 1996. Biological significance of IgA1 proteases in bacterial colonization and pathogenesis: critical evaluation of experimental evidence. Apmis 104:321-38
    • (1996) Apmis , vol.104 , pp. 321-338
    • Kilian, M.1    Reinholdt, J.2    Lomholt, H.3    Poulsen, K.4    Frandsen, E.V.5
  • 76
    • 0025270701 scopus 로고
    • Molecular aspects of immunoglobulin A1 degradation by oral streptococci
    • Reinholdt J, Tomana M, Mortensen SB, Kilian M. 1990. Molecular aspects of immunoglobulin A1 degradation by oral streptococci. Infect. Immun. 58:1186-94
    • (1990) Infect. Immun , vol.58 , pp. 1186-1194
    • Reinholdt, J.1    Tomana, M.2    Mortensen, S.B.3    Kilian, M.4
  • 77
    • 0033548612 scopus 로고    scopus 로고
    • The Fab and Fc fragments of IgA1 exhibit a different arrangement from that in IgG: A study by X-ray and neutron solution scattering and homology modelling
    • Boehm MK, Woof JM, Kerr MA, Perkins SJ. 1999. The Fab and Fc fragments of IgA1 exhibit a different arrangement from that in IgG: a study by X-ray and neutron solution scattering and homology modelling. J Mol. Biol. 286:1421-47
    • (1999) J Mol. Biol , vol.286 , pp. 1421-1447
    • Boehm, M.K.1    Woof, J.M.2    Kerr, M.A.3    Perkins, S.J.4
  • 78
    • 0036530010 scopus 로고    scopus 로고
    • Acquisition of potential N-glycosylation sites in the immunoglobulin variable region by somatic mutation is a distinctive feature of follicular lymphoma
    • Zhu D, McCarthy H, Ottensmeier CH, Johnson P, Hamblin TJ, Stevenson FK. 2002. Acquisition of potential N-glycosylation sites in the immunoglobulin variable region by somatic mutation is a distinctive feature of follicular lymphoma. Blood 99:2562-68
    • (2002) Blood , vol.99 , pp. 2562-2568
    • Zhu, D.1    McCarthy, H.2    Ottensmeier, C.H.3    Johnson, P.4    Hamblin, T.J.5    Stevenson, F.K.6
  • 79
    • 0019508130 scopus 로고
    • Structures of sialylated O-glycosidically and N-glycosidically linked oligosaccharides in a monoclonal immunoglobulin light chain
    • Chandrasekaran EV, Mendicino A, Garver FA, Mendicino J. 1981. Structures of sialylated O-glycosidically and N-glycosidically linked oligosaccharides in a monoclonal immunoglobulin light chain. J Biol. Chem. 256:1549-55
    • (1981) J Biol. Chem , vol.256 , pp. 1549-1555
    • Chandrasekaran, E.V.1    Mendicino, A.2    Garver, F.A.3    Mendicino, J.4
  • 80
    • 0023819528 scopus 로고
    • Glycosylation of a VH residue of a monoclonal antibody against α(1→6) dextran increases its affinity for antigen
    • Wallick SC, Kabat EA, Morrison SL. 1988. Glycosylation of a VH residue of a monoclonal antibody against α(1→6) dextran increases its affinity for antigen. J. Exp. Med. 168:1099-09
    • (1988) J. Exp. Med , vol.168 , pp. 1099-1009
    • Wallick, S.C.1    Kabat, E.A.2    Morrison, S.L.3
  • 81
    • 0025909201 scopus 로고
    • Antibody variable region glycosylation: Position effects on antigen binding and carbohydrate structure
    • Wright A, Tao MH, Kabat EA, Morrison SL. 1991. Antibody variable region glycosylation: position effects on antigen binding and carbohydrate structure. EMBO J. 10:2717-23
    • (1991) EMBO J , vol.10 , pp. 2717-2723
    • Wright, A.1    Tao, M.H.2    Kabat, E.A.3    Morrison, S.L.4
  • 82
    • 0022339826 scopus 로고
    • Structures of the sugar chains of rabbit immunoglobulin G: Occurrence of asparagine-linked sugar chains in Fab fragment
    • Taniguchi T, Mizuochi T, Beale M, Dwek RA, Rademacher TW, Kobata A. 1985. Structures of the sugar chains of rabbit immunoglobulin G: occurrence of asparagine-linked sugar chains in Fab fragment. Biochemistry 24:5551-57
    • (1985) Biochemistry , vol.24 , pp. 5551-5557
    • Taniguchi, T.1    Mizuochi, T.2    Beale, M.3    Dwek, R.A.4    Rademacher, T.W.5    Kobata, A.6
  • 83
    • 0029962752 scopus 로고    scopus 로고
    • Site-specific glycosylation of human immunoglobulin G is altered in four rheumatoid arthritis patients
    • Youings A, Chang SC, Dwek RA, Scragg IG. 1996. Site-specific glycosylation of human immunoglobulin G is altered in four rheumatoid arthritis patients. Biochem. J. 314(Pt. 2):621-30
    • (1996) Biochem. J , vol.314 , Issue.PART. 2 , pp. 621-630
    • Youings, A.1    Chang, S.C.2    Dwek, R.A.3    Scragg, I.G.4
  • 84
    • 2142813035 scopus 로고    scopus 로고
    • V region carbohydrate and antibody expression
    • Gala FA, Morrison SL. 2004. V region carbohydrate and antibody expression. J. Immunol. 172:5489-94
    • (2004) J. Immunol , vol.172 , pp. 5489-5494
    • Gala, F.A.1    Morrison, S.L.2
  • 85
    • 34247116573 scopus 로고    scopus 로고
    • Human follicular lymphoma cells contain oligomannose glycans in the antigen-binding site of the B cell receptor
    • In press
    • Radcliffe CM, Arnold JN, Suter DM, Wormald MR, Harvey DJ, et al. 2007. Human follicular lymphoma cells contain oligomannose glycans in the antigen-binding site of the B cell receptor. J. Biol. Chem. In press
    • (2007) J. Biol. Chem
    • Radcliffe, C.M.1    Arnold, J.N.2    Suter, D.M.3    Wormald, M.R.4    Harvey, D.J.5
  • 86
    • 0023338172 scopus 로고
    • Tissue-specific N-glycosylation, site-specific oligosaccharide patterns and lentil lectin recognition of rat Thy-1
    • Parekh RB, Tse AG, Dwek RA, Williams AF, Rademacher TW. 1987. Tissue-specific N-glycosylation, site-specific oligosaccharide patterns and lentil lectin recognition of rat Thy-1. EMBO J. 6:1233-44
    • (1987) EMBO J , vol.6 , pp. 1233-1244
    • Parekh, R.B.1    Tse, A.G.2    Dwek, R.A.3    Williams, A.F.4    Rademacher, T.W.5
  • 87
    • 0030937062 scopus 로고    scopus 로고
    • Glycosylation: Heterogeneity and the 3D structure of proteins
    • Rudd PM, Dwek RA. 1997. Glycosylation: heterogeneity and the 3D structure of proteins. Crit. Rev. Biochem. Mol. Biol. 32:1-100
    • (1997) Crit. Rev. Biochem. Mol. Biol , vol.32 , pp. 1-100
    • Rudd, P.M.1    Dwek, R.A.2
  • 88
    • 0035794194 scopus 로고    scopus 로고
    • High resolution mapping of the binding site on human IgG1 for FcγRI, FcγRII, FcγRIII, and FcRn and design of IgG1 variants with improved binding to the FcγR
    • Shields RL, Namenuk AK, Hong K, Meng YG, Rae J, et al. 2001. High resolution mapping of the binding site on human IgG1 for FcγRI, FcγRII, FcγRIII, and FcRn and design of IgG1 variants with improved binding to the FcγR. J. Biol. Chem. 276:6591-604
    • (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
  • 89
    • 0037013743 scopus 로고    scopus 로고
    • Interaction sites on human IgG-Fc for FcγR: Current models
    • Jefferis R, Lund J. 2002. Interaction sites on human IgG-Fc for FcγR: current models. Immunol. Lett. 82:57-65
    • (2002) Immunol. Lett , vol.82 , pp. 57-65
    • Jefferis, R.1    Lund, J.2
  • 90
    • 1242317024 scopus 로고    scopus 로고
    • Fucose depletion from human IgG1 oligosaccharide enhances binding enthalpy and association rate between IgG1 and FcγRIIIa
    • Okazaki A, Shoji-Hosaka E, Nakamura K, Wakitani M, Uchida K, et al. 2004. Fucose depletion from human IgG1 oligosaccharide enhances binding enthalpy and association rate between IgG1 and FcγRIIIa. J. Mol. Biol. 336:1239-49
    • (2004) J. Mol. Biol , vol.336 , pp. 1239-1249
    • Okazaki, A.1    Shoji-Hosaka, E.2    Nakamura, K.3    Wakitani, M.4    Uchida, K.5
  • 91
    • 33646172632 scopus 로고    scopus 로고
    • The carbohydrate at FcγRIIIa Asn-162. An element required for high affinity binding to non-fucosylated IgG glycoforms
    • Ferrara C, Stuart F, Sondermann P, Brunker P, Umana P. 2006. The carbohydrate at FcγRIIIa Asn-162. An element required for high affinity binding to non-fucosylated IgG glycoforms. J. Biol. Chem. 281:5032-36
    • (2006) J. Biol. Chem , vol.281 , pp. 5032-5036
    • Ferrara, C.1    Stuart, F.2    Sondermann, P.3    Brunker, P.4    Umana, P.5
  • 92
    • 0028129261 scopus 로고
    • A human T-cell receptor recognizes 'O'-linked sugars from the hinge region of human IgA1 and IgD
    • Rudd PM, Fortune F, Patel T, Parekh RB, Dwek RA, Lehner T. 1994. A human T-cell receptor recognizes 'O'-linked sugars from the hinge region of human IgA1 and IgD. Immunology 83:99-106
    • (1994) Immunology , vol.83 , pp. 99-106
    • Rudd, P.M.1    Fortune, F.2    Patel, T.3    Parekh, R.B.4    Dwek, R.A.5    Lehner, T.6
  • 97
    • 0017595157 scopus 로고
    • A subpopulation of normal human peripheral B Iymphcytes that bind IgE
    • Gonzalez-Molina A, Spiegelberg HL. 1977. A subpopulation of normal human peripheral B Iymphcytes that bind IgE. J. Clin. Invest. 59:616-24
    • (1977) J. Clin. Invest , vol.59 , pp. 616-624
    • Gonzalez-Molina, A.1    Spiegelberg, H.L.2
  • 98
    • 0018748142 scopus 로고
    • Lymphocytes bearing Fc receptors for IgE. I. Presence of human and rat T lymphocytes with Fc epsilon receptors
    • Yodoi J, Ishizaka K. 1979. Lymphocytes bearing Fc receptors for IgE. I. Presence of human and rat T lymphocytes with Fc epsilon receptors. J. Immunol. 122:2577-83
    • (1979) J. Immunol , vol.122 , pp. 2577-2583
    • Yodoi, J.1    Ishizaka, K.2
  • 99
    • 0027715015 scopus 로고
    • The human IgE network
    • Sutton BJ, Gould HJ. 1993. The human IgE network. Nature 366:421-28
    • (1993) Nature , vol.366 , pp. 421-428
    • Sutton, B.J.1    Gould, H.J.2
  • 100
    • 0011146968 scopus 로고
    • Binding site for IgE of the human lymphocyte low-affinity Fcereceptor (FcεRII/CD23) is confined to the domain homologous with animal lectins
    • Bettler B, Maier R, Ruegg D, Hofstetter H. 1989. Binding site for IgE of the human lymphocyte low-affinity Fcereceptor (FcεRII/CD23) is confined to the domain homologous with animal lectins. Proc. Natl. Acad. Sci. USA 86:7118-22
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 7118-7122
    • Bettler, B.1    Maier, R.2    Ruegg, D.3    Hofstetter, H.4
  • 102
    • 0025213243 scopus 로고
    • The binding of IgE to murine FcεRII is calcium-dependent but not inhibited by carbohydrate
    • Richards ML, Katz DH. 1990. The binding of IgE to murine FcεRII is calcium-dependent but not inhibited by carbohydrate. J. Immunol. 144:2638-46
    • (1990) J. Immunol , vol.144 , pp. 2638-2646
    • Richards, M.L.1    Katz, D.H.2
  • 103
    • 0345280710 scopus 로고    scopus 로고
    • N-glycosylation influences epitope expression and receptor binding structures in human IgE
    • Bjorklund JE, Karlsson T, Magnusson CG. 1999. N-glycosylation influences epitope expression and receptor binding structures in human IgE. Mol. Immunol. 36:213-21
    • (1999) Mol. Immunol , vol.36 , pp. 213-221
    • Bjorklund, J.E.1    Karlsson, T.2    Magnusson, C.G.3
  • 104
    • 0025022325 scopus 로고
    • Identification and characterization of IgA and Vicia villosa-binding T cell subsets in rheumatoid arthritis
    • Fortune F, Kingston J, Barnes CS, Lehner T. 1990. Identification and characterization of IgA and Vicia villosa-binding T cell subsets in rheumatoid arthritis. Clin. Exp. Immunol. 79:202-8
    • (1990) Clin. Exp. Immunol , vol.79 , pp. 202-208
    • Fortune, F.1    Kingston, J.2    Barnes, C.S.3    Lehner, T.4
  • 105
    • 10744224171 scopus 로고    scopus 로고
    • Glycosylation and size of IgA1 are essential for interaction with mesangial transferrin receptor in IgA nephropathy
    • Moura IC, Arcos-Fajardo M, Sadaka C, Leroy V, Benhamou M, et al. 2004. Glycosylation and size of IgA1 are essential for interaction with mesangial transferrin receptor in IgA nephropathy. J. Am. Soc. Nephrol. 15:622-34
    • (2004) J. Am. Soc. Nephrol , vol.15 , pp. 622-634
    • Moura, I.C.1    Arcos-Fajardo, M.2    Sadaka, C.3    Leroy, V.4    Benhamou, M.5
  • 106
    • 0035920589 scopus 로고    scopus 로고
    • Identification of the transferrin receptor as a novel immunoglobulin (Ig)A1 receptor and its enhanced expression on mesangial cells in IgA nephropathy
    • Moura IC, Centelles MN, Arcos-Fajardo M, Malheiros DM, Collawn JF, et al. 2001. Identification of the transferrin receptor as a novel immunoglobulin (Ig)A1 receptor and its enhanced expression on mesangial cells in IgA nephropathy. J. Exp. Med. 194:417-25
    • (2001) J. Exp. Med , vol.194 , pp. 417-425
    • Moura, I.C.1    Centelles, M.N.2    Arcos-Fajardo, M.3    Malheiros, D.M.4    Collawn, J.F.5
  • 107
    • 0026072580 scopus 로고
    • Changes in IgG glycoform levels are associated with remission of arthritis during pregnancy
    • Rook GA, Steele J, Brealey R, Whyte A, Isenberg D, et al. 1991. Changes in IgG glycoform levels are associated with remission of arthritis during pregnancy. J. Autoimmun. 4:779-94
    • (1991) J. Autoimmun , vol.4 , pp. 779-794
    • Rook, G.A.1    Steele, J.2    Brealey, R.3    Whyte, A.4    Isenberg, D.5
  • 109
    • 0024642881 scopus 로고
    • A comparative analysis of disease-associated changes in the galactosyladon of serum IgG
    • Parekh R, Isenberg D, Rook G, Roitt I, Dwek R, Rademacher T. 1989. A comparative analysis of disease-associated changes in the galactosyladon of serum IgG. J. Autoimmun. 2:101-14
    • (1989) J. Autoimmun , vol.2 , pp. 101-114
    • Parekh, R.1    Isenberg, D.2    Rook, G.3    Roitt, I.4    Dwek, R.5    Rademacher, T.6
  • 110
    • 0031081480 scopus 로고    scopus 로고
    • A detailed lectin analysis of IgG glycosylation, demonstrating disease specific changes in terminal galactose and N-acetylglucosamine
    • Bond A, Alavi A, Axford JS, Bourke BE, Bruckner FE, et al. 1997. A detailed lectin analysis of IgG glycosylation, demonstrating disease specific changes in terminal galactose and N-acetylglucosamine. J. Autoimmun. 10:77-85
    • (1997) J. Autoimmun , vol.10 , pp. 77-85
    • Bond, A.1    Alavi, A.2    Axford, J.S.3    Bourke, B.E.4    Bruckner, F.E.5
  • 111
    • 33750939466 scopus 로고    scopus 로고
    • Glycan analysis of monoclonal antibodies secreted in deposition disorders indicates that subsets of plasma cells differentially process IgG glycans
    • Omtvedt LA, Royle L, Husby G, Sletten K, Radcliffe CM, et al. 2006. Glycan analysis of monoclonal antibodies secreted in deposition disorders indicates that subsets of plasma cells differentially process IgG glycans. Arthritis Rheum. 54:3433-40
    • (2006) Arthritis Rheum , vol.54 , pp. 3433-3440
    • Omtvedt, L.A.1    Royle, L.2    Husby, G.3    Sletten, K.4    Radcliffe, C.M.5
  • 113
    • 0026582182 scopus 로고
    • Changes in normal glycosylation mechanisms in autoimmune rheumatic disease
    • Axford JS, Sumar N, Alavi A, Isenberg DA, Young A, et al. 1992. Changes in normal glycosylation mechanisms in autoimmune rheumatic disease. J. Clin. Invest. 89:1021-31
    • (1992) J. Clin. Invest , vol.89 , pp. 1021-1031
    • Axford, J.S.1    Sumar, N.2    Alavi, A.3    Isenberg, D.A.4    Young, A.5
  • 114
    • 0033978652 scopus 로고    scopus 로고
    • Two edged role of mannose binding lectin in rheumatoid arthritis: A cross sectional study
    • Garred P, Madsen HO, Marquart H, Hansen TM, Sorensen SF, et al. 2000. Two edged role of mannose binding lectin in rheumatoid arthritis: a cross sectional study. J. Rheumatol. 27:26-34
    • (2000) J. Rheumatol , vol.27 , pp. 26-34
    • Garred, P.1    Madsen, H.O.2    Marquart, H.3    Hansen, T.M.4    Sorensen, S.F.5
  • 115
    • 0019203677 scopus 로고
    • Selective deposition of immunoglobulin A1 in immunoglobulin A nephropathy, anaphylactoid purpura nephritis, and systemic lupus erythematosus
    • Conley ME, Cooper MD, Michael AF. 1980. Selective deposition of immunoglobulin A1 in immunoglobulin A nephropathy, anaphylactoid purpura nephritis, and systemic lupus erythematosus. J. Clin. Invest. 66:1432-36
    • (1980) J. Clin. Invest , vol.66 , pp. 1432-1436
    • Conley, M.E.1    Cooper, M.D.2    Michael, A.F.3
  • 116
    • 0035723058 scopus 로고    scopus 로고
    • Mesangial IgA1 in IgA nephropathy exhibits aberrant O-glycosylation: Observations in three patients
    • Allen AC, Bailey EM, Brenchley PE, Buck KS, Barrati J, Feehally J. 2001. Mesangial IgA1 in IgA nephropathy exhibits aberrant O-glycosylation: observations in three patients. Kidney Int. 60:969-73
    • (2001) Kidney Int , vol.60 , pp. 969-973
    • Allen, A.C.1    Bailey, E.M.2    Brenchley, P.E.3    Buck, K.S.4    Barrati, J.5    Feehally, J.6
  • 117
    • 0027355459 scopus 로고
    • Defective galactosylation and clearance of IgA1 molecules as a possible etiopathogenic factor in IgA nephropathy
    • Mestecky J, Tomana M, Crowley-Nowick PA, Moldoveanu Z, Julian BA, Jackson S. 1993. Defective galactosylation and clearance of IgA1 molecules as a possible etiopathogenic factor in IgA nephropathy. Contrib. Nephrol. 104:172-82
    • (1993) Contrib. Nephrol , vol.104 , pp. 172-182
    • Mestecky, J.1    Tomana, M.2    Crowley-Nowick, P.A.3    Moldoveanu, Z.4    Julian, B.A.5    Jackson, S.6
  • 118
    • 0035093693 scopus 로고    scopus 로고
    • Mass spectrometry proves under-O-glycosylation of glomerular IgA1 in IgA nephropathy
    • Hiki Y, Odani H, Takahashi M, Yasuda Y, Nishimoto A, et al. 2001. Mass spectrometry proves under-O-glycosylation of glomerular IgA1 in IgA nephropathy. Kidney Int. 59:1077-85
    • (2001) Kidney Int , vol.59 , pp. 1077-1085
    • Hiki, Y.1    Odani, H.2    Takahashi, M.3    Yasuda, Y.4    Nishimoto, A.5
  • 119
    • 0029182704 scopus 로고
    • Alterations in the IgA carbohydrate chains influence the cellular distribution of IgA1
    • Mestecky J, Hashim OH, Tomana M. 1995. Alterations in the IgA carbohydrate chains influence the cellular distribution of IgA1. Contrib. Nephrol. 111:66-71
    • (1995) Contrib. Nephrol , vol.111 , pp. 66-71
    • Mestecky, J.1    Hashim, O.H.2    Tomana, M.3
  • 120
    • 0030358020 scopus 로고    scopus 로고
    • Association of asialogalactosyl beta 1-3N-acetylgalactosamine on the hinge with a conformational instability of Jacalin-reactive immunoglobulin A1 in immunoglobulin A nephropathy
    • Hiki Y, Iwase H, Kokubo T, Horii A, Tanaka A, et al. 1996. Association of asialogalactosyl beta 1-3N-acetylgalactosamine on the hinge with a conformational instability of Jacalin-reactive immunoglobulin A1 in immunoglobulin A nephropathy. J. Am. Soc. Nephrol. 7:955-60
    • (1996) J. Am. Soc. Nephrol , vol.7 , pp. 955-960
    • Hiki, Y.1    Iwase, H.2    Kokubo, T.3    Horii, A.4    Tanaka, A.5
  • 121
    • 0033663064 scopus 로고    scopus 로고
    • IgA nephropathy: Recent developments
    • Floege J, Feehally J. 2000. IgA nephropathy: recent developments. J. Am. Soc. Nephrol. 11:2395-403
    • (2000) J. Am. Soc. Nephrol , vol.11 , pp. 2395-2403
    • Floege, J.1    Feehally, J.2
  • 122
    • 0034017259 scopus 로고    scopus 로고
    • Increased N-linked glycosylation leading to oversialylation of monomeric immunoglobulin A1 from patients with Sjogren's syndrome
    • Basset C, Durand V, Jamin C, Clement J, Pennec Y, et al. 2000. Increased N-linked glycosylation leading to oversialylation of monomeric immunoglobulin A1 from patients with Sjogren's syndrome. Scand. J. Immunol. 51:300-6
    • (2000) Scand. J. Immunol , vol.51 , pp. 300-306
    • Basset, C.1    Durand, V.2    Jamin, C.3    Clement, J.4    Pennec, Y.5
  • 123
    • 0037279060 scopus 로고    scopus 로고
    • Incidence of potential glycosylation sites in immunoglobulin variable regions distinguishes between subsets of Burkitt's lymphoma and mucosa-associated lymphoid tissue lymphoma
    • Zhu D, Ottensmeier CH, Du MQ, McCarthy H, Stevenson FK. 2003. Incidence of potential glycosylation sites in immunoglobulin variable regions distinguishes between subsets of Burkitt's lymphoma and mucosa-associated lymphoid tissue lymphoma. Br. J. Haematol. 120:217-22
    • (2003) Br. J. Haematol , vol.120 , pp. 217-222
    • Zhu, D.1    Ottensmeier, C.H.2    Du, M.Q.3    McCarthy, H.4    Stevenson, F.K.5
  • 124
    • 0028231880 scopus 로고
    • Structure of a single-chain antibody variable domain (Fv) fragment complexed with a carbohydrate antigen at 1.7-Å resolution
    • Zdanov A, Li Y, Bundle DR, Deng SJ, MacKenzie CR, et al. 1994. Structure of a single-chain antibody variable domain (Fv) fragment complexed with a carbohydrate antigen at 1.7-Å resolution. Proc. Natl. Acad. Sci. USA 91:6423-27
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 6423-6427
    • Zdanov, A.1    Li, Y.2    Bundle, D.R.3    Deng, S.J.4    MacKenzie, C.R.5
  • 125
    • 0028279360 scopus 로고
    • Molecular recognition of a Salmonella trisaccharide epitope by monoclonal antibody Se155-4
    • Bundle DR, Eichler E, Gidney MA, Meldal M, Ragauskas A, et al. 1994. Molecular recognition of a Salmonella trisaccharide epitope by monoclonal antibody Se155-4. Biochemistry 33:5172-82
    • (1994) Biochemistry , vol.33 , pp. 5172-5182
    • Bundle, D.R.1    Eichler, E.2    Gidney, M.A.3    Meldal, M.4    Ragauskas, A.5
  • 126
    • 0028290382 scopus 로고
    • Quantitative determination of circulating soluble egg antigen in urine and serum of Schistosoma mansoni-infected individuals using a combined two-site enzyme-linked immunosorbent assay
    • Nourel Din MS, Nibbeling R, Rotmans JP, Polderman AM, Krijger FW, Deelder AM. 1994. Quantitative determination of circulating soluble egg antigen in urine and serum of Schistosoma mansoni-infected individuals using a combined two-site enzyme-linked immunosorbent assay. Am. J. Trop. Med. Hyg. 50:585-94
    • (1994) Am. J. Trop. Med. Hyg , vol.50 , pp. 585-594
    • Nourel Din, M.S.1    Nibbeling, R.2    Rotmans, J.P.3    Polderman, A.M.4    Krijger, F.W.5    Deelder, A.M.6
  • 127
    • 9244257329 scopus 로고    scopus 로고
    • Antigenicity and immunogenicity of a synthetic oligosaccharide-protein conjugate vaccine against Haemophilus influenzae type b
    • Fernandez-Santana V, Cardoso F, Rodriguez A, Carmenate T, Pena L, et al. 2004. Antigenicity and immunogenicity of a synthetic oligosaccharide-protein conjugate vaccine against Haemophilus influenzae type b. Infect. Immun. 12:7115-23
    • (2004) Infect. Immun , vol.12 , pp. 7115-7123
    • Fernandez-Santana, V.1    Cardoso, F.2    Rodriguez, A.3    Carmenate, T.4    Pena, L.5
  • 128
    • 9044241681 scopus 로고    scopus 로고
    • Human monoclonal antibody 2G12 defines a distinctive neutralization epitope on the gp120 glycoprotein of human immunodeficiency virus type 1
    • Trkola A, Purtscher M, Muster T, Ballaun C, Buchacher A, et al. 1996. Human monoclonal antibody 2G12 defines a distinctive neutralization epitope on the gp120 glycoprotein of human immunodeficiency virus type 1. J. Virol. 70:1100-8
    • (1996) J. Virol , vol.70 , pp. 1100-1108
    • Trkola, A.1    Purtscher, M.2    Muster, T.3    Ballaun, C.4    Buchacher, A.5
  • 129
    • 0033044588 scopus 로고    scopus 로고
    • Engineered glycoforms of an antineuroblastoma IgG1 with optimized antibody-dependent cellular cytotoxic activity
    • Umana P, JeaN-Mairet J, Moudry R, Amstutz H, Bailey JE. 1999. Engineered glycoforms of an antineuroblastoma IgG1 with optimized antibody-dependent cellular cytotoxic activity. Nat. Biotechnol. 17:176-80
    • (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
  • 130
    • 0029563888 scopus 로고
    • Glycosylation and biological activity of CAMPATH-1H expressed in different cell lines and grown under different culture conditions
    • Lifely MR, Hale C, Boyce S, Keen MJ, Phillips J. 1995. Glycosylation and biological activity of CAMPATH-1H expressed in different cell lines and grown under different culture conditions. Glycobiology 5:813-22
    • (1995) Glycobiology , vol.5 , pp. 813-822
    • Lifely, M.R.1    Hale, C.2    Boyce, S.3    Keen, M.J.4    Phillips, J.5
  • 132
    • 0027458717 scopus 로고
    • The generation of a humanized, non-mitogenic CD3 monoclonal antibody which retains in vitro immunosuppressive properties
    • Bolt S, Routledge E, Lloyd I, Chatenoud L, Pope H, et al. 1993. The generation of a humanized, non-mitogenic CD3 monoclonal antibody which retains in vitro immunosuppressive properties. Eur. J. Immunol. 23:403-11
    • (1993) Eur. J. Immunol , vol.23 , pp. 403-411
    • Bolt, S.1    Routledge, E.2    Lloyd, I.3    Chatenoud, L.4    Pope, H.5
  • 133
    • 0033572786 scopus 로고    scopus 로고
    • Phase I study of an engineered aglycosylated humanized CD3 antibody in renal transplant rejection
    • Friend PJ, Hale G, Chatenoud L, Rebello P, Bradley J, et al. 1999. Phase I study of an engineered aglycosylated humanized CD3 antibody in renal transplant rejection. Transplantation 68:1632-37
    • (1999) Transplantation , vol.68 , pp. 1632-1637
    • Friend, P.J.1    Hale, G.2    Chatenoud, L.3    Rebello, P.4    Bradley, J.5
  • 135
    • 0036901079 scopus 로고    scopus 로고
    • Monoclonal antibody manufacturing in transgenic plants - myths and realities
    • Hood EE, Woodard SL, Horn ME. 2002. Monoclonal antibody manufacturing in transgenic plants - myths and realities. Curr. Opin. Biotechnol. 13:630-35
    • (2002) Curr. Opin. Biotechnol , vol.13 , pp. 630-635
    • Hood, E.E.1    Woodard, S.L.2    Horn, M.E.3
  • 136
  • 137
    • 14744277420 scopus 로고    scopus 로고
    • Bioprospecting in plants for engineered proteins
    • Joshi L, Lopez LC. 2005. Bioprospecting in plants for engineered proteins. Curr. Opin. Plant. Biol. 8:223-26
    • (2005) Curr. Opin. Plant. Biol , vol.8 , pp. 223-226
    • Joshi, L.1    Lopez, L.C.2
  • 139
    • 0025321903 scopus 로고
    • Crystal structures of an antibody to a peptide and its complex with peptide antigen at 2.8 Å
    • Stanfield RL, Fieser TM, Lerner RA, Wilson IA. 1990. Crystal structures of an antibody to a peptide and its complex with peptide antigen at 2.8 Å. Science 248:712-19
    • (1990) Science , vol.248 , pp. 712-719
    • Stanfield, R.L.1    Fieser, T.M.2    Lerner, R.A.3    Wilson, I.A.4
  • 140
    • 0036308980 scopus 로고    scopus 로고
    • The crystal structure of IgE Fc reveals an asymmetrically bent conformation
    • Wan T, Beavil RL, Fabiane SM, Beavil AJ, Sohi MK, et al. 2002. The crystal structure of IgE Fc reveals an asymmetrically bent conformation. Nat. Immunol. 3:681-86
    • (2002) Nat. Immunol , vol.3 , pp. 681-686
    • Wan, T.1    Beavil, R.L.2    Fabiane, S.M.3    Beavil, A.J.4    Sohi, M.K.5
  • 141
    • 0034691520 scopus 로고    scopus 로고
    • Structure of the Fc fragment of human IgE bound to its high-affinity receptor FcεRIα
    • Garman SC, Wurzburg BA, Tarchevskaya SS, Kinet JP, Jardetzky TS. 2000. Structure of the Fc fragment of human IgE bound to its high-affinity receptor FcεRIα. Nature 406:259-66
    • (2000) Nature , vol.406 , pp. 259-266
    • Garman, S.C.1    Wurzburg, B.A.2    Tarchevskaya, S.S.3    Kinet, J.P.4    Jardetzky, T.S.5
  • 142
    • 0030571019 scopus 로고    scopus 로고
    • A rapid high-resolution high-performance liquid chromatographic method for separating glycan mixtures and analyzing oligosaccharide profiles
    • Guile GR, Rudd PM, Wing DR, Prime SB, Dwek RA. 1996. A rapid high-resolution high-performance liquid chromatographic method for separating glycan mixtures and analyzing oligosaccharide profiles. Anal. Biochem. 240:210-26
    • (1996) Anal. Biochem , vol.240 , pp. 210-226
    • Guile, G.R.1    Rudd, P.M.2    Wing, D.R.3    Prime, S.B.4    Dwek, R.A.5


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