메뉴 건너뛰기




Volumn 1253, Issue 1, 2012, Pages 170-180

Novel roles for the IgG Fc glycan

Author keywords

Autoimmune disease; DC SIGN; Fc receptor; Inflammation; Sialylation

Indexed keywords

ASPARAGINE; AUTOANTIGEN; CD209 ANTIGEN; CYTOKINE; FC RECEPTOR; GLYCAN; IMMUNOGLOBULIN; IMMUNOGLOBULIN FC FRAGMENT; IMMUNOGLOBULIN G; IMMUNOGLOBULIN G ANTIBODY; IMMUNOGLOBULIN G FC GLYCAN; MONOSACCHARIDE; UNCLASSIFIED DRUG;

EID: 84860235393     PISSN: 00778923     EISSN: 17496632     Source Type: Book Series    
DOI: 10.1111/j.1749-6632.2011.06305.x     Document Type: Article
Times cited : (158)

References (96)
  • 1
    • 0026264771 scopus 로고
    • The mechanism of diphtheria immunity and tetanus immunity in animals. 1890
    • 9-20
    • von Behring, E. & S. Kitasato. 1991. The mechanism of diphtheria immunity and tetanus immunity in animals. 1890. Mol. Immunol. 28: 1317, 9-20.
    • (1991) Mol. Immunol. , vol.28 , pp. 1317
    • von Behring, E.1    Kitasato, S.2
  • 2
    • 70449144883 scopus 로고
    • Observation of a temporary exception to Ehrlich's rule of horror autotoxicus in idiopathic hemolytic anemia (presence of a specific auto-Rh-antibody (D) in a case of acquired hemolytic anemia during a crisis and its disappearance during hormonal therapy
    • Speiser, P. 1957. Observation of a temporary exception to Ehrlich's rule of horror autotoxicus in idiopathic hemolytic anemia (presence of a specific auto-Rh-antibody (D) in a case of acquired hemolytic anemia during a crisis and its disappearance during hormonal therapy. Wien. Klin. Wochenschr. 69: 149-154.
    • (1957) Wien. Klin. Wochenschr. , vol.69 , pp. 149-154
    • Speiser, P.1
  • 3
    • 77951529848 scopus 로고    scopus 로고
    • Therapeutic antibodies for autoimmunity and inflammation
    • Chan, A.C. & P.J. Carter. 2010. Therapeutic antibodies for autoimmunity and inflammation. Nat. Rev. Immunol. 10: 301-316.
    • (2010) Nat. Rev. Immunol. , vol.10 , pp. 301-316
    • Chan, A.C.1    Carter, P.J.2
  • 4
    • 77951586447 scopus 로고    scopus 로고
    • Strategies and challenges for the next generation of therapeutic antibodies
    • Beck, A., T. Wurch, C. Bailly & N. Corvaia. 2010. Strategies and challenges for the next generation of therapeutic antibodies. Nat. Rev. Immunol. 10: 345-352.
    • (2010) Nat. Rev. Immunol. , vol.10 , pp. 345-352
    • Beck, A.1    Wurch, T.2    Bailly, C.3    Corvaia, N.4
  • 5
    • 0028143211 scopus 로고
    • Randomised double-blind comparison of chimeric monoclonal antibody to tumour necrosis factor alpha (cA2) versus placebo in rheumatoid arthritis
    • Elliott, M.J., R.N. Maini, M. Feldmann, et al. 1994. Randomised double-blind comparison of chimeric monoclonal antibody to tumour necrosis factor alpha (cA2) versus placebo in rheumatoid arthritis. Lancet 344: 1105-1110.
    • (1994) Lancet , vol.344 , pp. 1105-1110
    • Elliott, M.J.1    Maini, R.N.2    Feldmann, M.3
  • 6
    • 0029050742 scopus 로고
    • Treatment of Crohn's disease with anti-tumor necrosis factor chimeric monoclonal antibody (cA2)
    • van Dullemen, H.M., S.J. van Deventer, D.W. Hommes, et al. 1995. Treatment of Crohn's disease with anti-tumor necrosis factor chimeric monoclonal antibody (cA2). Gastroenterology 109: 129-135.
    • (1995) Gastroenterology , vol.109 , pp. 129-135
    • van Dullemen, H.M.1    van Deventer, S.J.2    Hommes, D.W.3
  • 7
    • 17144455839 scopus 로고    scopus 로고
    • IDEC-C2B8: results of a phase I multiple-dose trial in patients with relapsed non-Hodgkin's lymphoma
    • Maloney, D.G., A.J. Grillo-Lopez, D.J. Bodkin, et al. 1997. IDEC-C2B8: results of a phase I multiple-dose trial in patients with relapsed non-Hodgkin's lymphoma. J. Clin. Oncol. 15: 3266-3274.
    • (1997) J. Clin. Oncol. , vol.15 , pp. 3266-3274
    • Maloney, D.G.1    Grillo-Lopez, A.J.2    Bodkin, D.J.3
  • 8
    • 1842368507 scopus 로고    scopus 로고
    • IDEC-C2B8 (Rituximab) anti-CD20 monoclonal antibody therapy in patients with relapsed low-grade non-Hodgkin's lymphoma
    • Maloney, D.G., A.J. Grillo-Lopez, C.A. White, et al. 1997. IDEC-C2B8 (Rituximab) anti-CD20 monoclonal antibody therapy in patients with relapsed low-grade non-Hodgkin's lymphoma. Blood 90: 2188-2195.
    • (1997) Blood , vol.90 , pp. 2188-2195
    • Maloney, D.G.1    Grillo-Lopez, A.J.2    White, C.A.3
  • 9
    • 0024478054 scopus 로고
    • p185HER2 monoclonal antibody has antiproliferative effects in vitro and sensitizes human breast tumor cells to tumor necrosis factor
    • Hudziak, R.M., G.D. Lewis, M. Winget, et al. 1989. p185HER2 monoclonal antibody has antiproliferative effects in vitro and sensitizes human breast tumor cells to tumor necrosis factor. Mol. Cell. Biol. 9: 1165-1172.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 1165-1172
    • Hudziak, R.M.1    Lewis, G.D.2    Winget, M.3
  • 10
    • 0032600294 scopus 로고    scopus 로고
    • Drug update. Trastuzumab: anti-HER2 antibody for treatment of metastatic breast cancer
    • Wong, W.M. 1999. Drug update. Trastuzumab: anti-HER2 antibody for treatment of metastatic breast cancer. Cancer. Pract. 7: 48-50.
    • (1999) Cancer. Pract. , vol.7 , pp. 48-50
    • Wong, W.M.1
  • 11
    • 0017152608 scopus 로고
    • Crystallographic structure studies of an IgG molecule and an Fc fragment
    • Huber, R., J. Deisenhofer, P.M. Colman, et al. 1976. Crystallographic structure studies of an IgG molecule and an Fc fragment. Nature 264: 415-420.
    • (1976) Nature , vol.264 , pp. 415-420
    • Huber, R.1    Deisenhofer, J.2    Colman, P.M.3
  • 12
    • 0016420497 scopus 로고
    • Structure and function of immunoglobulins
    • Franklin, E.C. 1975. Structure and function of immunoglobulins. Acta Endocrinol. Suppl. 194: 77-95.
    • (1975) Acta Endocrinol. Suppl. , vol.194 , pp. 77-95
    • Franklin, E.C.1
  • 13
    • 30444461383 scopus 로고    scopus 로고
    • Fcgamma receptors: old friends and new family members
    • Nimmerjahn, F. & J.V. Ravetch. 2006. Fcgamma receptors: old friends and new family members. Immunity 24: 19-28.
    • (2006) Immunity , vol.24 , pp. 19-28
    • Nimmerjahn, F.1    Ravetch, J.V.2
  • 15
    • 37549036732 scopus 로고    scopus 로고
    • Fcgamma receptors as regulators of immune responses
    • Nimmerjahn, F. & J.V. Ravetch. 2008. Fcgamma receptors as regulators of immune responses. Nat. Rev. Immunol. 8: 34-47.
    • (2008) Nat. Rev. Immunol. , vol.8 , pp. 34-47
    • Nimmerjahn, F.1    Ravetch, J.V.2
  • 17
    • 58149527503 scopus 로고    scopus 로고
    • Fc receptors and their role in immune regulation and inflammation
    • W.E. Paul, Ed.:. Lippincott Williams and Wilkins. Philadelphia
    • Ravetch, J.V. & F. Nimmerjahn. 2007. Fc receptors and their role in immune regulation and inflammation. In Fundamental Immunology. W.E. Paul, Ed.: 684-705. Lippincott Williams and Wilkins. Philadelphia.
    • (2007) Fundamental Immunology , pp. 684-705
    • Ravetch, J.V.1    Nimmerjahn, F.2
  • 18
    • 34247122497 scopus 로고    scopus 로고
    • The impact of glycosylation on the biological function and structure of human immunoglobulins
    • Arnold, J.N., M.R. Wormald, R.B. Sim, et al. 2007. The impact of glycosylation on the biological function and structure of human immunoglobulins. Annu. Rev. Immunol. 25: 21-50.
    • (2007) Annu. Rev. Immunol. , vol.25 , pp. 21-50
    • Arnold, J.N.1    Wormald, M.R.2    Sim, R.B.3
  • 19
    • 33746888249 scopus 로고    scopus 로고
    • Anti-inflammatory activity of immunoglobulin G resulting from Fc sialylation
    • Kaneko, Y., F. Nimmerjahn & J.V. Ravetch. 2006. Anti-inflammatory activity of immunoglobulin G resulting from Fc sialylation. Science 313: 670-673.
    • (2006) Science , vol.313 , pp. 670-673
    • Kaneko, Y.1    Nimmerjahn, F.2    Ravetch, J.V.3
  • 20
    • 67651149465 scopus 로고    scopus 로고
    • Structure of the murine unglycosylated IgG1 Fc fragment
    • Feige, M.J., S. Nath, S.R. Catharino, et al. 2009. Structure of the murine unglycosylated IgG1 Fc fragment. J. Mol. Biol. 391: 599-608.
    • (2009) J. Mol. Biol. , vol.391 , pp. 599-608
    • Feige, M.J.1    Nath, S.2    Catharino, S.R.3
  • 21
    • 58149510052 scopus 로고    scopus 로고
    • Aglycosylated immunoglobulin G1 variants productively engage activating Fc receptors
    • Sazinsky, S.L., R.G. Ott, N.W. Silver, et al. 2008. Aglycosylated immunoglobulin G1 variants productively engage activating Fc receptors. Proc. Natl. Acad. Sci. USA 105: 20167-20172.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 20167-20172
    • Sazinsky, S.L.1    Ott, R.G.2    Silver, N.W.3
  • 23
    • 0033427574 scopus 로고    scopus 로고
    • Fucosylation of IgG heavy chains is increased in rheumatoid arthritis
    • Gornik, I., G. Maravic, J. Dumic, et al. 1999. Fucosylation of IgG heavy chains is increased in rheumatoid arthritis. Clin. Biochem. 32: 605-608.
    • (1999) Clin. Biochem. , vol.32 , pp. 605-608
    • Gornik, I.1    Maravic, G.2    Dumic, J.3
  • 24
    • 34249989775 scopus 로고    scopus 로고
    • Detection of altered N-glycan profiles in whole serum from rheumatoid arthritis patients
    • Nakagawa, H., M. Hato, Y. Takegawa, et al. 2007. Detection of altered N-glycan profiles in whole serum from rheumatoid arthritis patients. J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. 853: 133-137.
    • (2007) J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. , vol.853 , pp. 133-137
    • Nakagawa, H.1    Hato, M.2    Takegawa, Y.3
  • 25
    • 11844287660 scopus 로고    scopus 로고
    • Repeated immunization induces the increase in fucose content on antigen-specific IgG N-linked oligosaccharides
    • Guo, N., Y. Liu, Y. Masuda, et al. 2005. Repeated immunization induces the increase in fucose content on antigen-specific IgG N-linked oligosaccharides. Clin. Biochem. 38: 149-153.
    • (2005) Clin. Biochem. , vol.38 , pp. 149-153
    • Guo, N.1    Liu, Y.2    Masuda, Y.3
  • 26
    • 79961233787 scopus 로고    scopus 로고
    • Unique carbohydrate-carbohydrate interactions are required for high affinity binding between Fc{gamma}RIII and antibodies lacking core fucose
    • Ferrara, C., S. Grau, C. Jager, et al. 2011. Unique carbohydrate-carbohydrate interactions are required for high affinity binding between Fc{gamma}RIII and antibodies lacking core fucose. Proc. Natl. Acad. Sci. USA 108: 12669-12674.
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 12669-12674
    • Ferrara, C.1    Grau, S.2    Jager, C.3
  • 27
    • 33646172632 scopus 로고    scopus 로고
    • The carbohydrate at FcgammaRIIIa Asn-162. An element required for high affinity binding to non-fucosylated IgG glycoforms
    • Ferrara, C., F. Stuart, P. Sondermann, et al. 2006. The carbohydrate at FcgammaRIIIa Asn-162. An element required for high affinity binding to non-fucosylated IgG glycoforms. J. Biol. Chem. 281: 5032-5036.
    • (2006) J. Biol. Chem. , vol.281 , pp. 5032-5036
    • Ferrara, C.1    Stuart, F.2    Sondermann, P.3
  • 28
    • 0037178791 scopus 로고    scopus 로고
    • Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human Fcgamma RIII and antibody-dependent cellular toxicity
    • Shields, R.L., J. Lai, R. Keck, et al. 2002. Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human Fcgamma RIII and antibody-dependent cellular toxicity. J. Biol. Chem. 277: 26733-26740.
    • (2002) J. Biol. Chem. , vol.277 , pp. 26733-26740
    • Shields, R.L.1    Lai, J.2    Keck, R.3
  • 29
    • 0037474276 scopus 로고    scopus 로고
    • The absence of fucose but not the presence of galactose or bisecting N-acetylglucosamine of human IgG1 complex-type oligosaccharides shows the critical role of enhancing antibody-dependent cellular cytotoxicity
    • Shinkawa, T., K. Nakamura, N. Yamane, et al. 2003. The absence of fucose but not the presence of galactose or bisecting N-acetylglucosamine of human IgG1 complex-type oligosaccharides shows the critical role of enhancing antibody-dependent cellular cytotoxicity. J. Biol. Chem. 278: 3466-3473.
    • (2003) J. Biol. Chem. , vol.278 , pp. 3466-3473
    • Shinkawa, T.1    Nakamura, K.2    Yamane, N.3
  • 30
    • 34250682223 scopus 로고    scopus 로고
    • Enhanced Fc-dependent cellular cytotoxicity of Fc fusion proteins derived from TNF receptor II and LFA-3 by fucose removal from Asn-linked oligosaccharides
    • Shoji-Hosaka, E., Y. Kobayashi, M. Wakitani, et al. 2006. Enhanced Fc-dependent cellular cytotoxicity of Fc fusion proteins derived from TNF receptor II and LFA-3 by fucose removal from Asn-linked oligosaccharides. J. Biochem. 140: 777-783.
    • (2006) J. Biochem. , vol.140 , pp. 777-783
    • Shoji-Hosaka, E.1    Kobayashi, Y.2    Wakitani, M.3
  • 31
    • 28444437100 scopus 로고    scopus 로고
    • Fucose removal from complex-type oligosaccharide enhances the antibody-dependent cellular cytotoxicity of single-gene-encoded antibody comprising a single-chain antibody linked the antibody constant region
    • Natsume, A., M. Wakitani, N. Yamane-Ohnuki, et al. 2005. Fucose removal from complex-type oligosaccharide enhances the antibody-dependent cellular cytotoxicity of single-gene-encoded antibody comprising a single-chain antibody linked the antibody constant region. J. Immunol. Methods 306: 93-103.
    • (2005) J. Immunol. Methods , vol.306 , pp. 93-103
    • Natsume, A.1    Wakitani, M.2    Yamane-Ohnuki, N.3
  • 32
    • 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
    • Davies, J., L. Jiang, L.Z. Pan, et al. 2001. Expression of GnTIII in a recombinant anti-CD20 CHO production cell line: expression of antibodies with altered glycoforms leads to an increase in ADCC through higher affinity for FC gamma RIII. Biotechnol. Bioeng. 74: 288-294.
    • (2001) Biotechnol. Bioeng. , vol.74 , pp. 288-294
    • Davies, J.1    Jiang, L.2    Pan, L.Z.3
  • 33
    • 79953877355 scopus 로고    scopus 로고
    • IgG fc N-glycosylation changes in Lambert-Eaton myasthenic syndrome and myasthenia gravis
    • Selman, M.H., E.H. Niks, M.J. Titulaer, et al. 2011. IgG fc N-glycosylation changes in Lambert-Eaton myasthenic syndrome and myasthenia gravis. J. Proteome Res. 10: 143-152.
    • (2011) J. Proteome Res. , vol.10 , pp. 143-152
    • Selman, M.H.1    Niks, E.H.2    Titulaer, M.J.3
  • 34
    • 33751253486 scopus 로고    scopus 로고
    • Higher levels of sialylated Fc glycans in immunoglobulin G molecules can adversely impact functionality
    • Scallon, B.J., S.H. Tam, S.G. McCarthy, et al. 2007. Higher levels of sialylated Fc glycans in immunoglobulin G molecules can adversely impact functionality. Mol. Immunol. 44: 1524-1534.
    • (2007) Mol. Immunol. , vol.44 , pp. 1524-1534
    • Scallon, B.J.1    Tam, S.H.2    McCarthy, S.G.3
  • 35
    • 42349085035 scopus 로고    scopus 로고
    • Recapitulation of IVIG anti-inflammatory activity with a recombinant IgG Fc
    • Anthony, R.M., F. Nimmerjahn, D.J. Ashline, et al. 2008. Recapitulation of IVIG anti-inflammatory activity with a recombinant IgG Fc. Science 320: 373-376.
    • (2008) Science , vol.320 , pp. 373-376
    • Anthony, R.M.1    Nimmerjahn, F.2    Ashline, D.J.3
  • 36
    • 33645080442 scopus 로고    scopus 로고
    • Pathology and protection in nephrotoxic nephritis is determined by selective engagement of specific Fc receptors
    • Kaneko, Y., F. Nimmerjahn, M.P. Madaio, & J.V. Ravetch. 2006. Pathology and protection in nephrotoxic nephritis is determined by selective engagement of specific Fc receptors. J. Exp. Med. 203: 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
  • 37
    • 79959817309 scopus 로고    scopus 로고
    • Sialylation levels of anti-proteinase 3 antibodies are associated with the activity of granulomatosis with polyangiitis (Wegener's)
    • Espy, C., W. Morelle, N. Kavian, et al. 2011. Sialylation levels of anti-proteinase 3 antibodies are associated with the activity of granulomatosis with polyangiitis (Wegener's). Arthritis Rheum 63: 2105-2115.
    • (2011) Arthritis Rheum , vol.63 , pp. 2105-2115
    • Espy, C.1    Morelle, W.2    Kavian, N.3
  • 38
    • 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
    • van de Geijn, F.E., M. Wuhrer, M.H. Selman, et al. 2009. 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: R193.
    • (2009) Arthritis Res. Ther. , vol.11
    • van de Geijn, F.E.1    Wuhrer, M.2    Selman, M.H.3
  • 39
    • 34347235526 scopus 로고    scopus 로고
    • Agalactosylated IgG antibodies depend on cellular Fc receptors for in vivo activity
    • Nimmerjahn, F., R.M. Anthony & J.V. Ravetch. 2007. Agalactosylated IgG antibodies depend on cellular Fc receptors for in vivo activity. Proc. Natl. Acad. Sci. USA 104: 8433-8437.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 8433-8437
    • Nimmerjahn, F.1    Anthony, R.M.2    Ravetch, J.V.3
  • 40
    • 0019463420 scopus 로고
    • High-dose intravenous gammaglobulin for idiopathic thrombocytopenic purpura in childhood
    • Imbach, P., S. Barandun, V. d'Apuzzo, et al. 1981. High-dose intravenous gammaglobulin for idiopathic thrombocytopenic purpura in childhood. Lancet 1: 1228-1231.
    • (1981) Lancet , vol.1 , pp. 1228-1231
    • Imbach, P.1    Barandun, S.2    d'Apuzzo, V.3
  • 41
    • 0027504398 scopus 로고
    • Infusion of Fc gamma fragments for treatment of children with acute immune thrombocytopenic purpura
    • Debre, M., M.C. Bonnet, W.H. Fridman, et al. 1993. Infusion of Fc gamma fragments for treatment of children with acute immune thrombocytopenic purpura. Lancet 342: 945-949.
    • (1993) Lancet , vol.342 , pp. 945-949
    • Debre, M.1    Bonnet, M.C.2    Fridman, W.H.3
  • 42
    • 33846423857 scopus 로고    scopus 로고
    • The antiinflammatory activity of IgG: the intravenous IgG paradox
    • Nimmerjahn, F. & J.V. Ravetch. 2007. The antiinflammatory activity of IgG: the intravenous IgG paradox. J. Exp. Med. 204: 11-15.
    • (2007) J. Exp. Med. , vol.204 , pp. 11-15
    • Nimmerjahn, F.1    Ravetch, J.V.2
  • 43
    • 42649089750 scopus 로고    scopus 로고
    • Anti-inflammatory actions of intravenous immunoglobulin
    • Nimmerjahn, F. & J.V. Ravetch. 2008. Anti-inflammatory actions of intravenous immunoglobulin. Annu. Rev. Immunol. 26: 513-533.
    • (2008) Annu. Rev. Immunol. , vol.26 , pp. 513-533
    • Nimmerjahn, F.1    Ravetch, J.V.2
  • 44
    • 0033118675 scopus 로고    scopus 로고
    • From systemic T cell self-reactivity to organ-specific autoimmune disease via immunoglobulins
    • Korganow, A.S., H. Ji, S. Mangialaio, et al. 1999. From systemic T cell self-reactivity to organ-specific autoimmune disease via immunoglobulins. Immunity 10: 451-461.
    • (1999) Immunity , vol.10 , pp. 451-461
    • Korganow, A.S.1    Ji, H.2    Mangialaio, S.3
  • 45
    • 0035910392 scopus 로고    scopus 로고
    • Anti-inflammatory activity of IVIG mediated through the inhibitory Fc receptor
    • Samuelsson, A., T.L. Towers, & J.V. Ravetch. 2001. Anti-inflammatory activity of IVIG mediated through the inhibitory Fc receptor. Science 291: 484-486.
    • (2001) Science , vol.291 , pp. 484-486
    • Samuelsson, A.1    Towers, T.L.2    Ravetch, J.V.3
  • 46
    • 0038494827 scopus 로고    scopus 로고
    • IVIg-mediated amelioration of murine ITP via FcgammaRIIB is independent of SHIP1, SHP-1, and Btk activity
    • Crow, A.R., S. Song, J. Freedman, et al. 2003. IVIg-mediated amelioration of murine ITP via FcgammaRIIB is independent of SHIP1, SHP-1, and Btk activity. Blood 102: 558-560.
    • (2003) Blood , vol.102 , pp. 558-560
    • Crow, A.R.1    Song, S.2    Freedman, J.3
  • 47
    • 0345382854 scopus 로고    scopus 로고
    • IVIG induces dose-dependent amelioration of ITP in rodent models
    • Crow, A.R., S. Song, J.W. Semple, et al. 2003. IVIG induces dose-dependent amelioration of ITP in rodent models. Blood 101: 1658-1659.
    • (2003) Blood , vol.101 , pp. 1658-1659
    • Crow, A.R.1    Song, S.2    Semple, J.W.3
  • 48
    • 77956185954 scopus 로고    scopus 로고
    • A novel role for the IgG Fc glycan: the anti-inflammatory activity of sialylated IgG Fcs
    • Anthony, R.M. & J.V. Ravetch. 2010. A novel role for the IgG Fc glycan: the anti-inflammatory activity of sialylated IgG Fcs. J. Clin. Immunol. 30 Suppl 1: S9-S14.
    • (2010) J. Clin. Immunol. , vol.30 , Issue.SUPPL. 1
    • Anthony, R.M.1    Ravetch, J.V.2
  • 49
    • 78751608551 scopus 로고    scopus 로고
    • The role of differential IgG glycosylation in the interaction of antibodies with FcgammaRs in vivo
    • Anthony, R.M. & F. Nimmerjahn. 2011. The role of differential IgG glycosylation in the interaction of antibodies with FcgammaRs in vivo. Curr. Opin. Organ Transplant. 16: 7-14.
    • (2011) Curr. Opin. Organ Transplant. , vol.16 , pp. 7-14
    • Anthony, R.M.1    Nimmerjahn, F.2
  • 50
    • 63849187507 scopus 로고    scopus 로고
    • Impaired inhibitory Fcgamma receptor IIB expression on B cells in chronic inflammatory demyelinating polyneuropathy
    • Tackenberg, B., I. Jelcic, A. Baerenwaldt, et al. 2009. Impaired inhibitory Fcgamma receptor IIB expression on B cells in chronic inflammatory demyelinating polyneuropathy. Proc. Natl. Acad. Sci. USA 106: 4788-4792.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 4788-4792
    • Tackenberg, B.1    Jelcic, I.2    Baerenwaldt, A.3
  • 51
    • 77956182458 scopus 로고    scopus 로고
    • Mechanisms of IVIG efficacy in chronic inflammatory demyelinating polyneuropathy
    • Tackenberg, B., F. Nimmerjahn & J.D. Lunemann. 2010. Mechanisms of IVIG efficacy in chronic inflammatory demyelinating polyneuropathy. J. Clin. Immunol. 30 Suppl 1: S65-S69.
    • (2010) J. Clin. Immunol. , vol.30 , Issue.SUPPL. 1
    • Tackenberg, B.1    Nimmerjahn, F.2    Lunemann, J.D.3
  • 52
    • 0037399064 scopus 로고    scopus 로고
    • Colony-stimulating factor-1-dependent macrophages are responsible for IVIG protection in antibody-induced autoimmune disease
    • Bruhns, P., A. Samuelsson, J.W. Pollard & J.V. Ravetch. 2003. Colony-stimulating factor-1-dependent macrophages are responsible for IVIG protection in antibody-induced autoimmune disease. Immunity 18: 573-581.
    • (2003) Immunity , vol.18 , pp. 573-581
    • Bruhns, P.1    Samuelsson, A.2    Pollard, J.W.3    Ravetch, J.V.4
  • 53
    • 58149378347 scopus 로고    scopus 로고
    • Identification of a receptor required for the anti-inflammatory activity of IVIG
    • Anthony, R.M., F. Wermeling, M.C. Karlsson & J.V. Ravetch. 2008. Identification of a receptor required for the anti-inflammatory activity of IVIG. Proc. Natl. Acad. Sci. USA 105: 19571-19578.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 19571-19578
    • Anthony, R.M.1    Wermeling, F.2    Karlsson, M.C.3    Ravetch, J.V.4
  • 54
    • 0026585781 scopus 로고
    • RAG-1-deficient mice have no mature B and T lymphocytes
    • Mombaerts, P., J. Iacomini, R.S. Johnson, et al. 1992. RAG-1-deficient mice have no mature B and T lymphocytes. Cell 68: 869-877.
    • (1992) Cell , vol.68 , pp. 869-877
    • Mombaerts, P.1    Iacomini, J.2    Johnson, R.S.3
  • 55
    • 23444437972 scopus 로고    scopus 로고
    • Structure and function of the spleen
    • Mebius, R.E. & G. Kraal. 2005. Structure and function of the spleen. Nat. Rev. Immunol. 5: 606-616.
    • (2005) Nat. Rev. Immunol. , vol.5 , pp. 606-616
    • Mebius, R.E.1    Kraal, G.2
  • 56
    • 33745980209 scopus 로고    scopus 로고
    • New insights into the cell biology of the marginal zone of the spleen
    • Kraal, G. & R. Mebius. 2006. New insights into the cell biology of the marginal zone of the spleen. Int. Rev. Cytol. 250: 175-215.
    • (2006) Int. Rev. Cytol. , vol.250 , pp. 175-215
    • Kraal, G.1    Mebius, R.2
  • 57
    • 15444368037 scopus 로고    scopus 로고
    • Development and function of the splenic marginal zone
    • Mebius, R.E., M.A. Nolte & G. Kraal. 2004. Development and function of the splenic marginal zone. Crit. Rev. Immunol. 24: 449-464.
    • (2004) Crit. Rev. Immunol. , vol.24 , pp. 449-464
    • Mebius, R.E.1    Nolte, M.A.2    Kraal, G.3
  • 58
    • 21644463169 scopus 로고    scopus 로고
    • Siglecs in innate immunity
    • Crocker, P.R. 2005. Siglecs in innate immunity. Curr. Opin. Pharmacol. 5: 431-437.
    • (2005) Curr. Opin. Pharmacol. , vol.5 , pp. 431-437
    • Crocker, P.R.1
  • 59
    • 0025780182 scopus 로고
    • Purification and properties of sialoadhesin, a sialic acid-binding receptor of murine tissue macrophages
    • Crocker, P.R., S. Kelm, C. Dubois, et al. 1991. Purification and properties of sialoadhesin, a sialic acid-binding receptor of murine tissue macrophages. Embo. J. 10: 1661-1669.
    • (1991) Embo. J. , vol.10 , pp. 1661-1669
    • Crocker, P.R.1    Kelm, S.2    Dubois, C.3
  • 61
    • 0034913685 scopus 로고    scopus 로고
    • Siglecs, sialic acids and innate immunity
    • Crocker, P.R. & A. Varki. 2001. Siglecs, sialic acids and innate immunity. Trends Immunol. 22: 337-342.
    • (2001) Trends Immunol. , vol.22 , pp. 337-342
    • Crocker, P.R.1    Varki, A.2
  • 62
    • 0025125616 scopus 로고
    • Ultrastructural localization of a macrophage-restricted sialic acid binding hemagglutinin, SER, in macrophage-hematopoietic cell clusters
    • Crocker, P.R., Z. Werb, S. Gordon, et al. 1990. Ultrastructural localization of a macrophage-restricted sialic acid binding hemagglutinin, SER, in macrophage-hematopoietic cell clusters. Blood 76: 1131-1138.
    • (1990) Blood , vol.76 , pp. 1131-1138
    • Crocker, P.R.1    Werb, Z.2    Gordon, S.3
  • 63
    • 29144509535 scopus 로고    scopus 로고
    • Defective microarchitecture of the spleen marginal zone and impaired response to a thymus-independent type 2 antigen in mice lacking scavenger receptors MARCO and SR-A
    • Chen, Y., T. Pikkarainen, O. Elomaa, et al. 2005. Defective microarchitecture of the spleen marginal zone and impaired response to a thymus-independent type 2 antigen in mice lacking scavenger receptors MARCO and SR-A. J. Immunol. 175: 8173-8180.
    • (2005) J. Immunol. , vol.175 , pp. 8173-8180
    • Chen, Y.1    Pikkarainen, T.2    Elomaa, O.3
  • 64
    • 0042161816 scopus 로고    scopus 로고
    • Macrophages control the retention and trafficking of B lymphocytes in the splenic marginal zone
    • Karlsson, M.C., R. Guinamard, S. Bolland, et al. 2003. Macrophages control the retention and trafficking of B lymphocytes in the splenic marginal zone. J. Exp. Med. 198: 333-340.
    • (2003) J. Exp. Med. , vol.198 , pp. 333-340
    • Karlsson, M.C.1    Guinamard, R.2    Bolland, S.3
  • 65
    • 0033519286 scopus 로고    scopus 로고
    • Role of the scavenger receptor MARCO in alveolar macrophage binding of unopsonized environmental particles
    • Palecanda, A., J. Paulauskis, E. Al-Mutairi, et al. 1999. Role of the scavenger receptor MARCO in alveolar macrophage binding of unopsonized environmental particles. J. Exp. Med. 189: 1497-1506.
    • (1999) J. Exp. Med. , vol.189 , pp. 1497-1506
    • Palecanda, A.1    Paulauskis, J.2    Al-Mutairi, E.3
  • 66
    • 0344428149 scopus 로고    scopus 로고
    • Regulation and functional involvement of macrophage scavenger receptor MARCO in clearance of bacteria in vivo
    • van der Laan, L.J., E.A. Dopp, R. Haworth, et al. 1999. Regulation and functional involvement of macrophage scavenger receptor MARCO in clearance of bacteria in vivo. J. Immunol. 162: 939-947.
    • (1999) J. Immunol. , vol.162 , pp. 939-947
    • van der Laan, L.J.1    Dopp, E.A.2    Haworth, R.3
  • 67
    • 2942720454 scopus 로고    scopus 로고
    • High and low affinity carbohydrate ligands revealed for murine SIGN-R1 by carbohydrate array and cell binding approaches, and differing specificities for SIGN-R3 and langerin
    • Galustian, C., C.G. Park, W. Chai, et al. 2004. High and low affinity carbohydrate ligands revealed for murine SIGN-R1 by carbohydrate array and cell binding approaches, and differing specificities for SIGN-R3 and langerin. Int. Immunol. 16: 853-866.
    • (2004) Int. Immunol. , vol.16 , pp. 853-866
    • Galustian, C.1    Park, C.G.2    Chai, W.3
  • 68
    • 33646005763 scopus 로고    scopus 로고
    • A dominant complement fixation pathway for pneumococcal polysaccharides initiated by SIGN-R1 interacting with C1q
    • Kang, Y.S., Y. Do, H.K. Lee, et al. 2006. A dominant complement fixation pathway for pneumococcal polysaccharides initiated by SIGN-R1 interacting with C1q. Cell 125: 47-58.
    • (2006) Cell , vol.125 , pp. 47-58
    • Kang, Y.S.1    Do, Y.2    Lee, H.K.3
  • 69
    • 9144229622 scopus 로고    scopus 로고
    • The C-type lectin SIGN-R1 mediates uptake of the capsular polysaccharide of Streptococcus pneumoniae in the marginal zone of mouse spleen
    • Kang, Y.S., J.Y. Kim, S.A. Bruening, et al. 2004. The C-type lectin SIGN-R1 mediates uptake of the capsular polysaccharide of Streptococcus pneumoniae in the marginal zone of mouse spleen. Proc. Natl. Acad. Sci. USA 101: 215-220.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 215-220
    • Kang, Y.S.1    Kim, J.Y.2    Bruening, S.A.3
  • 70
    • 12244283114 scopus 로고    scopus 로고
    • SIGN-R1, a novel C-type lectin expressed by marginal zone macrophages in spleen, mediates uptake of the polysaccharide dextran
    • Kang, Y.S., S. Yamazaki, T. Iyoda, et al. 2003. SIGN-R1, a novel C-type lectin expressed by marginal zone macrophages in spleen, mediates uptake of the polysaccharide dextran. Int. Immunol. 15: 177-186.
    • (2003) Int. Immunol. , vol.15 , pp. 177-186
    • Kang, Y.S.1    Yamazaki, S.2    Iyoda, T.3
  • 71
    • 10644225200 scopus 로고    scopus 로고
    • SIGN-R1 contributes to protection against lethal pneumococcal infection in mice
    • Lanoue, A., M.R. Clatworthy, P. Smith, et al. 2004. SIGN-R1 contributes to protection against lethal pneumococcal infection in mice. J. Exp. Med. 200: 1383-1393.
    • (2004) J. Exp. Med. , vol.200 , pp. 1383-1393
    • Lanoue, A.1    Clatworthy, M.R.2    Smith, P.3
  • 72
    • 0037108432 scopus 로고    scopus 로고
    • Marginal zone macrophages express a murine homologue of DC-SIGN that captures blood-borne antigens in vivo
    • Geijtenbeek, T.B., P.C. Groot, M.A. Nolte, et al. 2002. Marginal zone macrophages express a murine homologue of DC-SIGN that captures blood-borne antigens in vivo. Blood 100: 2908-2916.
    • (2002) Blood , vol.100 , pp. 2908-2916
    • Geijtenbeek, T.B.1    Groot, P.C.2    Nolte, M.A.3
  • 73
    • 0034772132 scopus 로고    scopus 로고
    • Five mouse homologues of the human dendritic cell C-type lectin, DC-SIGN
    • Park, C.G., K. Takahara, E. Umemoto, et al. 2001. Five mouse homologues of the human dendritic cell C-type lectin, DC-SIGN. Int. Immunol. 13: 1283-1290.
    • (2001) Int. Immunol. , vol.13 , pp. 1283-1290
    • Park, C.G.1    Takahara, K.2    Umemoto, E.3
  • 74
    • 33846872115 scopus 로고    scopus 로고
    • Mice lacking SIGNR1 have stronger T helper 1 responses to mycobacterium tuberculosis
    • Wieland, C.W., E.A. Koppel, J. den Dunnen, et al. 2007. Mice lacking SIGNR1 have stronger T helper 1 responses to mycobacterium tuberculosis. Microbes. Infect. 9: 134-141.
    • (2007) Microbes. Infect. , vol.9 , pp. 134-141
    • Wieland, C.W.1    Koppel, E.A.2    den Dunnen, J.3
  • 75
    • 0034598905 scopus 로고    scopus 로고
    • DC-SIGN, a dendritic cell-specific HIV-1-binding protein that enhances trans-infection of T cells
    • Geijtenbeek, T.B., D.S. Kwon, R. Torensma, et al. 2000. DC-SIGN, a dendritic cell-specific HIV-1-binding protein that enhances trans-infection of T cells. Cell 100: 587-597.
    • (2000) Cell , vol.100 , pp. 587-597
    • Geijtenbeek, T.B.1    Kwon, D.S.2    Torensma, R.3
  • 76
    • 0034598934 scopus 로고    scopus 로고
    • Identification of DC-SIGN, a novel dendritic cell-specific ICAM-3 receptor that supports primary immune responses
    • Geijtenbeek, T.B., R. Torensma, S.J. van Vliet, et al. 2000. Identification of DC-SIGN, a novel dendritic cell-specific ICAM-3 receptor that supports primary immune responses. Cell 100: 575-585.
    • (2000) Cell , vol.100 , pp. 575-585
    • Geijtenbeek, T.B.1    Torensma, R.2    van Vliet, S.J.3
  • 77
    • 0037192786 scopus 로고    scopus 로고
    • Identification of different binding sites in the dendritic cell-specific receptor DC-SIGN for intercellular adhesion molecule 3 and HIV-1
    • Geijtenbeek, T.B., G.C. van Duijnhoven, S.J. van Vliet, et al. 2002. Identification of different binding sites in the dendritic cell-specific receptor DC-SIGN for intercellular adhesion molecule 3 and HIV-1. J. Biol. Chem. 277: 11314-11320.
    • (2002) J. Biol. Chem. , vol.277 , pp. 11314-11320
    • Geijtenbeek, T.B.1    van Duijnhoven, G.C.2    van Vliet, S.J.3
  • 78
    • 0037237593 scopus 로고    scopus 로고
    • Mycobacteria target DC-SIGN to suppress dendritic cell function
    • Geijtenbeek, T.B., S.J. Van Vliet, E.A. Koppel, et al. 2003. Mycobacteria target DC-SIGN to suppress dendritic cell function. J. Exp. Med. 197: 7-17.
    • (2003) J. Exp. Med. , vol.197 , pp. 7-17
    • Geijtenbeek, T.B.1    Van Vliet, S.J.2    Koppel, E.A.3
  • 79
    • 70349201241 scopus 로고    scopus 로고
    • Carbohydrate-specific signaling through the DC-SIGN signalosome tailors immunity to mycobacterium tuberculosis, HIV-1 and Helicobacter pylori
    • Gringhuis, S.I., J. den Dunnen, M. Litjens, et al. 2009. Carbohydrate-specific signaling through the DC-SIGN signalosome tailors immunity to mycobacterium tuberculosis, HIV-1 and Helicobacter pylori. Nat. Immunol. 10: 1081-1088.
    • (2009) Nat. Immunol. , vol.10 , pp. 1081-1088
    • Gringhuis, S.I.1    den Dunnen, J.2    Litjens, M.3
  • 80
    • 34248544993 scopus 로고    scopus 로고
    • C-type lectin DC-SIGN modulates Toll-like receptor signaling via Raf-1 kinase-dependent acetylation of transcription factor NF-kappaB
    • Gringhuis, S.I., J. den Dunnen, M. Litjens, et al. 2007. C-type lectin DC-SIGN modulates Toll-like receptor signaling via Raf-1 kinase-dependent acetylation of transcription factor NF-kappaB. Immunity 26: 605-616.
    • (2007) Immunity , vol.26 , pp. 605-616
    • Gringhuis, S.I.1    den Dunnen, J.2    Litjens, M.3
  • 81
    • 13844322103 scopus 로고    scopus 로고
    • Distinct functions of DC-SIGN and its homologues L-SIGN (DC-SIGNR) and mSIGNR1 in pathogen recognition and immune regulation
    • Koppel, E.A., K.P. van Gisbergen, T.B. Geijtenbeek & Y. van Kooyk. 2005. Distinct functions of DC-SIGN and its homologues L-SIGN (DC-SIGNR) and mSIGNR1 in pathogen recognition and immune regulation. Cell. Microbiol. 7: 157-165.
    • (2005) Cell. Microbiol. , vol.7 , pp. 157-165
    • Koppel, E.A.1    van Gisbergen, K.P.2    Geijtenbeek, T.B.3    van Kooyk, Y.4
  • 82
    • 0037240748 scopus 로고    scopus 로고
    • DC-SIGN is the major mycobacterium tuberculosis receptor on human dendritic cells
    • Tailleux, L., O. Schwartz, J.L. Herrmann, et al. 2003. DC-SIGN is the major mycobacterium tuberculosis receptor on human dendritic cells. J. Exp. Med. 197: 121-127.
    • (2003) J. Exp. Med. , vol.197 , pp. 121-127
    • Tailleux, L.1    Schwartz, O.2    Herrmann, J.L.3
  • 83
  • 84
    • 33750498126 scopus 로고    scopus 로고
    • Specificity of DC-SIGN for mannose- and fucose-containing glycans
    • van Liempt, E., C.M. Bank, P. Mehta, et al. 2006. Specificity of DC-SIGN for mannose- and fucose-containing glycans. FEBS Lett. 580: 6123-6131.
    • (2006) FEBS Lett. , vol.580 , pp. 6123-6131
    • van Liempt, E.1    Bank, C.M.2    Mehta, P.3
  • 85
    • 79960046406 scopus 로고    scopus 로고
    • Intravenous gammaglobulin suppresses inflammation through a novel T(H)2 pathway
    • Anthony, R.M., T. Kobayashi, F. Wermeling & J.V. Ravetch. 2011. Intravenous gammaglobulin suppresses inflammation through a novel T(H)2 pathway. Nature 475: 110-113.
    • (2011) Nature , vol.475 , pp. 110-113
    • Anthony, R.M.1    Kobayashi, T.2    Wermeling, F.3    Ravetch, J.V.4
  • 86
    • 45549105692 scopus 로고    scopus 로고
    • Decreased pathology and prolonged survival of human DC-SIGN transgenic mice during mycobacterial infection
    • Schaefer, M., N. Reiling, C. Fessler, et al. 2008. Decreased pathology and prolonged survival of human DC-SIGN transgenic mice during mycobacterial infection. J. Immunol. 180: 6836-6845.
    • (2008) J. Immunol. , vol.180 , pp. 6836-6845
    • Schaefer, M.1    Reiling, N.2    Fessler, C.3
  • 87
    • 77951817855 scopus 로고    scopus 로고
    • Nuocytes represent a new innate effector leukocyte that mediates type-2 immunity
    • Neill, D.R., S.H. Wong, A. Bellosi, et al. 2010. Nuocytes represent a new innate effector leukocyte that mediates type-2 immunity. Nature 464: 1367-1370.
    • (2010) Nature , vol.464 , pp. 1367-1370
    • Neill, D.R.1    Wong, S.H.2    Bellosi, A.3
  • 88
    • 79955757689 scopus 로고    scopus 로고
    • Fc-glycosylation of IgG1 is modulated by B-cell stimuli
    • M110 004655-1-M110 004655-12
    • Wang, J., C.I. Balog, K. Stavenhagen, et al. 2011. Fc-glycosylation of IgG1 is modulated by B-cell stimuli. Mol. Cell. Proteomics 10: M110 004655-1-M110 004655-12.
    • (2011) Mol. Cell. Proteomics , vol.10
    • Wang, J.1    Balog, C.I.2    Stavenhagen, K.3
  • 89
    • 0031225688 scopus 로고    scopus 로고
    • The glycosylation of IgA produced by murine B cells is altered by Th2 cytokines
    • Chintalacharuvu, S.R. & S.N. Emancipator. 1997. The glycosylation of IgA produced by murine B cells is altered by Th2 cytokines. J. Immunol. 159: 2327-2333.
    • (1997) J. Immunol. , vol.159 , pp. 2327-2333
    • Chintalacharuvu, S.R.1    Emancipator, S.N.2
  • 90
    • 0036327185 scopus 로고    scopus 로고
    • Human antibodies against amyloid beta peptide: a potential treatment for Alzheimer's disease
    • Dodel, R., H. Hampel, C. Depboylu, et al. 2002. Human antibodies against amyloid beta peptide: a potential treatment for Alzheimer's disease. Ann. Neurol. 52: 253-256.
    • (2002) Ann. Neurol. , vol.52 , pp. 253-256
    • Dodel, R.1    Hampel, H.2    Depboylu, C.3
  • 91
    • 77949300796 scopus 로고    scopus 로고
    • 11C-PiB PET assessment of change in fibrillar amyloid-beta load in patients with Alzheimer's disease treated with bapineuzumab: a phase 2, double-blind, placebo-controlled, ascending-dose study
    • Rinne, J.O., D.J. Brooks, M.N. Rossor, et al. 2010. 11C-PiB PET assessment of change in fibrillar amyloid-beta load in patients with Alzheimer's disease treated with bapineuzumab: a phase 2, double-blind, placebo-controlled, ascending-dose study. Lancet Neurol. 9: 363-372.
    • (2010) Lancet Neurol. , vol.9 , pp. 363-372
    • Rinne, J.O.1    Brooks, D.J.2    Rossor, M.N.3
  • 92
    • 68949169046 scopus 로고    scopus 로고
    • IV immunoglobulin is associated with a reduced risk of Alzheimer disease and related disorders
    • Fillit, H., G. Hess, J. Hill, et al. 2009. IV immunoglobulin is associated with a reduced risk of Alzheimer disease and related disorders. Neurology 73: 180-185.
    • (2009) Neurology , vol.73 , pp. 180-185
    • Fillit, H.1    Hess, G.2    Hill, J.3
  • 93
    • 70049083865 scopus 로고    scopus 로고
    • 18-month study of intravenous immunoglobulin for treatment of mild Alzheimer disease
    • Relkin, N.R., P. Szabo, B. Adamiak, et al. 2009. 18-month study of intravenous immunoglobulin for treatment of mild Alzheimer disease. Neurobiol. Aging 30: 1728-1736.
    • (2009) Neurobiol. Aging , vol.30 , pp. 1728-1736
    • Relkin, N.R.1    Szabo, P.2    Adamiak, B.3
  • 94
    • 8844256204 scopus 로고    scopus 로고
    • Intravenous immunoglobulins for Alzheimer's disease
    • Fillit, H. 2004. Intravenous immunoglobulins for Alzheimer's disease. Lancet Neurol. 3: 704.
    • (2004) Lancet Neurol. , vol.3 , pp. 704
    • Fillit, H.1
  • 95
    • 4644337032 scopus 로고    scopus 로고
    • Intravenous immunoglobulins: a treatment for Alzheimer's disease?
    • Hack, C.E. & P. Scheltens. 2004. Intravenous immunoglobulins: a treatment for Alzheimer's disease? J. Neurol. Neurosurg. Psychiatr. 75: 1374-1375.
    • (2004) J. Neurol. Neurosurg. Psychiatr. , vol.75 , pp. 1374-1375
    • Hack, C.E.1    Scheltens, P.2
  • 96
    • 17944380435 scopus 로고    scopus 로고
    • Crystal structure of a neutralizing human IGG against HIV-1: a template for vaccine design
    • Saphire, E.O., P.W. Parren, R. Pantophlet, et al. 2001. Crystal structure of a neutralizing human IGG against HIV-1: a template for vaccine design. Science 293: 1155-1159.
    • (2001) Science , vol.293 , pp. 1155-1159
    • Saphire, E.O.1    Parren, P.W.2    Pantophlet, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.