메뉴 건너뛰기




Volumn 5, Issue OCT, 2014, Pages

IgG subclasses and allotypes: From structure to effector functions

Author keywords

Fc receptors; Genetic; Glycosylation; IgG; Immunoglobulin G; Neonatal Fc receptor; Polymorphism

Indexed keywords

CD16 ANTIGEN; CD209 ANTIGEN; COMPLEMENT COMPONENT C1Q; FC RECEPTOR; FC RECEPTOR IIA; FC RECEPTOR IIB; FC RECEPTOR LIKE PROTEIN; IMMUNOGLOBULIN ALLOTYPE; IMMUNOGLOBULIN F(AB) FRAGMENT; IMMUNOGLOBULIN FC FRAGMENT; IMMUNOGLOBULIN G; IMMUNOGLOBULIN G1; IMMUNOGLOBULIN G2; IMMUNOGLOBULIN G3; IMMUNOGLOBULIN G4; IMMUNOGLOBULIN SUBCLASS; PROTEIN; TRIPARTITE MOTIF CONTAINING PROTEIN 21; UNCLASSIFIED DRUG;

EID: 84918825382     PISSN: None     EISSN: 16643224     Source Type: Journal    
DOI: 10.3389/fimmu.2014.00520     Document Type: Article
Times cited : (1802)

References (216)
  • 2
    • 65549114676 scopus 로고    scopus 로고
    • Specificity and affinity of human Fcgamma receptors and their polymorphic variants for human IgG subclasses
    • Bruhns P, Iannascoli B, England P, Mancardi DA, Fernandez N, Jorieux S, et al. Specificity and affinity of human Fcgamma receptors and their polymorphic variants for human IgG subclasses. Blood (2009) 113(16):3716-25. doi:10.1182/blood-2008-09-179754
    • (2009) Blood , vol.113 , Issue.16 , pp. 3716-3725
    • Bruhns, P.1    Iannascoli, B.2    England, P.3    Mancardi, D.A.4    Fernandez, N.5    Jorieux, S.6
  • 3
    • 0034501119 scopus 로고    scopus 로고
    • Molecular basis of IgG subclass deficiency
    • Pan Q, Hammarstrom L. Molecular basis of IgG subclass deficiency. Immunol Rev (2000) 178:99-110. doi:10.1034/j.1600-065X.2000.17815.x
    • (2000) Immunol Rev , vol.178 , pp. 99-110
    • Pan, Q.1    Hammarstrom, L.2
  • 5
    • 84860292969 scopus 로고    scopus 로고
    • BCR-signalling synergizes with TLR-signalling for induction of AID and immunoglobulin class-switching through the non-canonical NF-kappaB pathway
    • Pone EJ, Zhang J, Mai T, White CA, Li G, Sakakura JK, et al. BCR-signalling synergizes with TLR-signalling for induction of AID and immunoglobulin class-switching through the non-canonical NF-kappaB pathway. Nat Commun (2012) 3:767. doi:10.1038/ncomms1769
    • (2012) Nat Commun , vol.3 , pp. 767
    • Pone, E.J.1    Zhang, J.2    Mai, T.3    White, C.A.4    Li, G.5    Sakakura, J.K.6
  • 6
    • 77950967415 scopus 로고    scopus 로고
    • Toll-like receptors and B-cell receptors synergize to induce immunoglobulin class-switch DNA recombination: relevance to microbial antibody responses
    • Pone EJ, Zan H, Zhang J, Al-Qahtani A, Xu Z, Casali P. Toll-like receptors and B-cell receptors synergize to induce immunoglobulin class-switch DNA recombination: relevance to microbial antibody responses. Crit Rev Immunol (2010) 30(1):1-29. doi:10.1615/CritRevImmunol.v30.i1.10
    • (2010) Crit Rev Immunol , vol.30 , Issue.1 , pp. 1-29
    • Pone, E.J.1    Zan, H.2    Zhang, J.3    Al-Qahtani, A.4    Xu, Z.5    Casali, P.6
  • 7
    • 80052171651 scopus 로고    scopus 로고
    • Human memory B cells originate from three distinct germinal center-dependent and -independent maturation pathways
    • Berkowska MA, Driessen GJ, Bikos V, Grosserichter-Wagener C, Stamatopoulos K, Cerutti A, et al. Human memory B cells originate from three distinct germinal center-dependent and -independent maturation pathways. Blood (2011) 118(8):2150-8. doi:10.1182/blood-2011-04-345579
    • (2011) Blood , vol.118 , Issue.8 , pp. 2150-2158
    • Berkowska, M.A.1    Driessen, G.J.2    Bikos, V.3    Grosserichter-Wagener, C.4    Stamatopoulos, K.5    Cerutti, A.6
  • 9
    • 0025041444 scopus 로고
    • IgG subclass distribution of antibodies to bacterial and viral antigens.
    • Ferrante A, Beard LJ, Feldman RG. IgG subclass distribution of antibodies to bacterial and viral antigens. Pediatr Infect Dis J (1990) 9(8 Suppl):S16-24. doi:10.1097/00006454-199008001-00004
    • (1990) Pediatr Infect Dis J , vol.9 , Issue.8 SUPPL , pp. S16-S24
    • Ferrante, A.1    Beard, L.J.2    Feldman, R.G.3
  • 10
    • 0025007923 scopus 로고
    • Selective IgG subclass deficiency: quantification and clinical relevance
    • Jefferis R, Kumararatne DS. Selective IgG subclass deficiency: quantification and clinical relevance. Clin Exp Immunol (1990) 81(3):357-67. doi:10.1111/j.1365-2249.1990.tb05339.x
    • (1990) Clin Exp Immunol , vol.81 , Issue.3 , pp. 357-367
    • Jefferis, R.1    Kumararatne, D.S.2
  • 11
    • 0018950766 scopus 로고
    • Correlation between serum IgG-2 concentrations and the antibody response to bacterial polysaccharide antigens
    • Siber GR, Schur PH, Aisenberg AC, Weitzman SA, Schiffman G. Correlation between serum IgG-2 concentrations and the antibody response to bacterial polysaccharide antigens. N Engl J Med (1980) 303(4):178-82. doi:10.1056/NEJM198007243030402
    • (1980) N Engl J Med , vol.303 , Issue.4 , pp. 178-182
    • Siber, G.R.1    Schur, P.H.2    Aisenberg, A.C.3    Weitzman, S.A.4    Schiffman, G.5
  • 12
    • 0022645912 scopus 로고
    • IgG2 subclass restriction of antibody to pneumococcal polysaccharides
    • Barrett DJ, Ayoub EM. IgG2 subclass restriction of antibody to pneumococcal polysaccharides. Clin Exp Immunol (1986) 63(1):127-34.
    • (1986) Clin Exp Immunol , vol.63 , Issue.1 , pp. 127-134
    • Barrett, D.J.1    Ayoub, E.M.2
  • 13
    • 0037341292 scopus 로고    scopus 로고
    • Levels of antibodies specific to tetanus toxoid, Haemophilus influenzae type b, and pneumococcal capsular polysaccharide in healthy children and adults
    • Schauer U, Stemberg F, Rieger CH, Buttner W, Borte M, Schubert S, et al. Levels of antibodies specific to tetanus toxoid, Haemophilus influenzae type b, and pneumococcal capsular polysaccharide in healthy children and adults. Clin Diagn Lab Immunol (2003) 10(2):202-7. doi:10.1128/CDLI.10.2.202-207.2003
    • (2003) Clin Diagn Lab Immunol , vol.10 , Issue.2 , pp. 202-207
    • Schauer, U.1    Stemberg, F.2    Rieger, C.H.3    Buttner, W.4    Borte, M.5    Schubert, S.6
  • 14
    • 0020673999 scopus 로고
    • IgG2 deficiency in a healthy blood donor Concomitant lack of IgG2, IgA and IgE immunoglobulins and specific anti-carbohydrate antibodies
    • Hammarstrom L, Smith CI. IgG2 deficiency in a healthy blood donor. Concomitant lack of IgG2, IgA and IgE immunoglobulins and specific anti-carbohydrate antibodies. Clin Exp Immunol (1983) 51(3):600-4.
    • (1983) Clin Exp Immunol , vol.51 , Issue.3 , pp. 600-604
    • Hammarstrom, L.1    Smith, C.I.2
  • 15
    • 0023515460 scopus 로고
    • Subclass restriction pattern of antigen-specific antibodies in donors with defective expression of IgG or IgA subclass heavy chain constant region genes
    • Hammarstrom L, Carbonara AO, DeMarchi M, Lefranc G, Moller G, Smith CI, et al. Subclass restriction pattern of antigen-specific antibodies in donors with defective expression of IgG or IgA subclass heavy chain constant region genes. Clin Immunol Immunopathol (1987) 45(3):461-70. doi:10.1016/0090-1229(87)90097-3
    • (1987) Clin Immunol Immunopathol , vol.45 , Issue.3 , pp. 461-470
    • Hammarstrom, L.1    Carbonara, A.O.2    DeMarchi, M.3    Lefranc, G.4    Moller, G.5    Smith, C.I.6
  • 16
    • 0026462066 scopus 로고
    • IgG subclass deficiencies and recurrent pyogenic infections, unresponsiveness against bacterial polysaccharide antigens
    • Kuijpers TW, Weening RS, Out TA. IgG subclass deficiencies and recurrent pyogenic infections, unresponsiveness against bacterial polysaccharide antigens. Allergol Immunopathol (Madr) (1992) 20(1):28-34.
    • (1992) Allergol Immunopathol (Madr) , vol.20 , Issue.1 , pp. 28-34
    • Kuijpers, T.W.1    Weening, R.S.2    Out, T.A.3
  • 17
    • 34047158146 scopus 로고    scopus 로고
    • The clinical significance of immunoglobulin A deficiency.
    • Latiff AH, Kerr MA. The clinical significance of immunoglobulin A deficiency. Ann Clin Biochem (2007) 44(Pt 2):131-9. doi:10.1258/000456307780117993
    • (2007) Ann Clin Biochem , vol.44 , pp. 131-139
    • Latiff, A.H.1    Kerr, M.A.2
  • 18
    • 67649212162 scopus 로고    scopus 로고
    • Intravenous immunoglobulin contains a broad repertoire of anticarbohydrate antibodies that is not restricted to the IgG2 subclass
    • von Gunten S, Smith DF, Cummings RD, Riedel S, Miescher S, Schaub A, et al. Intravenous immunoglobulin contains a broad repertoire of anticarbohydrate antibodies that is not restricted to the IgG2 subclass. J Allergy Clin Immunol (2009) 123(6):1268-76. doi:10.1016/j.jaci.2009.03.013
    • (2009) J Allergy Clin Immunol , vol.123 , Issue.6 , pp. 1268-1276
    • von Gunten, S.1    Smith, D.F.2    Cummings, R.D.3    Riedel, S.4    Miescher, S.5    Schaub, A.6
  • 19
    • 0031839518 scopus 로고    scopus 로고
    • Isotypes and opsonophagocytosis of pneumococcus type 6B antibodies elicited in infants and adults by an experimental pneumococcus type 6B-tetanus toxoid vaccine
    • Vidarsson G, Sigurdardottir ST, Gudnason T, Kjartansson S, Kristinsson KG, Ingolfsdottir G, et al. Isotypes and opsonophagocytosis of pneumococcus type 6B antibodies elicited in infants and adults by an experimental pneumococcus type 6B-tetanus toxoid vaccine. Infect Immun (1998) 66(6):2866-70.
    • (1998) Infect Immun , vol.66 , Issue.6 , pp. 2866-2870
    • Vidarsson, G.1    Sigurdardottir, S.T.2    Gudnason, T.3    Kjartansson, S.4    Kristinsson, K.G.5    Ingolfsdottir, G.6
  • 20
    • 84455208902 scopus 로고    scopus 로고
    • Competition for FcRn-mediated transport gives rise to short half-life of human IgG3 and offers therapeutic potential
    • Stapleton NM, Andersen JT, Stemerding AM, Bjarnarson SP, Verheul RC, Gerritsen J, et al. Competition for FcRn-mediated transport gives rise to short half-life of human IgG3 and offers therapeutic potential. Nat Commun (2011) 2:599. doi:10.1038/ncomms1608
    • (2011) Nat Commun , vol.2 , pp. 599
    • Stapleton, N.M.1    Andersen, J.T.2    Stemerding, A.M.3    Bjarnarson, S.P.4    Verheul, R.C.5    Gerritsen, J.6
  • 21
    • 0027181387 scopus 로고
    • Low concentrations of Gm allotypic subsets G3 mg and G1 mf in homozygotes and heterozygotes
    • Seppala IJ, Sarvas H, Makela O. Low concentrations of Gm allotypic subsets G3 mg and G1 mf in homozygotes and heterozygotes. J Immunol (1993) 151(5):2529-37.
    • (1993) J Immunol , vol.151 , Issue.5 , pp. 2529-2537
    • Seppala, I.J.1    Sarvas, H.2    Makela, O.3
  • 22
    • 0026505119 scopus 로고
    • Regulation of C gamma 3 expression Role of switch in the allotype-associated variation of human serum IgG3 levels
    • Hassan MS, Islam KB, Hammarstrom L, Smith CI. Regulation of C gamma 3 expression. Role of switch in the allotype-associated variation of human serum IgG3 levels. J Immunol (1992) 148(8):2555-62.
    • (1992) J Immunol , vol.148 , Issue.8 , pp. 2555-2562
    • Hassan, M.S.1    Islam, K.B.2    Hammarstrom, L.3    Smith, C.I.4
  • 23
    • 77953677176 scopus 로고    scopus 로고
    • Cleavage of IgGs by proteases associated with invasive diseases: an evasion tactic against host immunity?
    • Brezski RJ, Jordan RE. Cleavage of IgGs by proteases associated with invasive diseases: an evasion tactic against host immunity? MAbs (2010) 2(3):212-20. doi:10.4161/mabs.2.3.11780
    • (2010) MAbs , vol.2 , Issue.3 , pp. 212-220
    • Brezski, R.J.1    Jordan, R.E.2
  • 24
    • 0021947248 scopus 로고
    • Immunoglobulin subclass (IgG3) restriction of anti-P and anti-Pk antibodies in patients of the rare p blood group
    • Soderstrom T, Enskog A, Samuelsson BE, Cedergren B. Immunoglobulin subclass (IgG3) restriction of anti-P and anti-Pk antibodies in patients of the rare p blood group. J Immunol (1985) 134(1):1-3.
    • (1985) J Immunol , vol.134 , Issue.1 , pp. 1-3
    • Soderstrom, T.1    Enskog, A.2    Samuelsson, B.E.3    Cedergren, B.4
  • 25
    • 0024271472 scopus 로고
    • Maternal antibodies against fetal blood group antigens A or B: lytic activity of IgG subclasses in monocyte-driven cytotoxicity and correlation with ABO haemolytic disease of the newborn
    • Brouwers HA, Overbeeke MA, Ouwehand WH, Keuning K, van Ertbruggen I, van Leeuwen EF, et al. Maternal antibodies against fetal blood group antigens A or B: lytic activity of IgG subclasses in monocyte-driven cytotoxicity and correlation with ABO haemolytic disease of the newborn. Br J Haematol (1988) 70(4):465-9. doi:10.1111/j.1365-2141.1988.tb02518.x
    • (1988) Br J Haematol , vol.70 , Issue.4 , pp. 465-469
    • Brouwers, H.A.1    Overbeeke, M.A.2    Ouwehand, W.H.3    Keuning, K.4    van Ertbruggen, I.5    van Leeuwen, E.F.6
  • 26
    • 0030733895 scopus 로고    scopus 로고
    • Immunoglobulin G subclasses of anti-human platelet antigen 1a in maternal sera: relation to the severity of neonatal alloimmune thrombocytopenia
    • Mawas F, Wiener E, Williamson LM, Rodeck CH. Immunoglobulin G subclasses of anti-human platelet antigen 1a in maternal sera: relation to the severity of neonatal alloimmune thrombocytopenia. Eur J Haematol (1997) 59(5):287-92. doi:10.1111/j.1600-0609.1997.tb01688.x
    • (1997) Eur J Haematol , vol.59 , Issue.5 , pp. 287-292
    • Mawas, F.1    Wiener, E.2    Williamson, L.M.3    Rodeck, C.H.4
  • 27
    • 0025114636 scopus 로고
    • Anti-Rh (D) IgG subclasses and severity of Rh hemolytic disease of the newborn
    • Pollock JM, Bowman JM. Anti-Rh (D) IgG subclasses and severity of Rh hemolytic disease of the newborn. Vox Sang (1990) 59(3):176-9. doi:10.1111/j.1423-0410.1990.tb00854.x
    • (1990) Vox Sang , vol.59 , Issue.3 , pp. 176-179
    • Pollock, J.M.1    Bowman, J.M.2
  • 28
    • 33749439541 scopus 로고    scopus 로고
    • Isolated IgG3 deficiency in children: to treat or not to treat? Case presentation and review of the literature
    • Meyts I, Bossuyt X, Proesmans M, Boeck KD. Isolated IgG3 deficiency in children: to treat or not to treat? Case presentation and review of the literature. Pediatr Allergy Immunol (2006) 17(7):544-50. doi:10.1111/j.1399-3038.2006.00454.x
    • (2006) Pediatr Allergy Immunol , vol.17 , Issue.7 , pp. 544-550
    • Meyts, I.1    Bossuyt, X.2    Proesmans, M.3    Boeck, K.D.4
  • 29
    • 0020700160 scopus 로고
    • Serologic aspects of IgG4 antibodies I. Prolonged immunization results in an IgG4-restricted response
    • Aalberse RC, van der Gaag R, van Leeuwen J. Serologic aspects of IgG4 antibodies. I. Prolonged immunization results in an IgG4-restricted response. J Immunol (1983) 130:722-6.
    • (1983) J Immunol , vol.130 , pp. 722-726
    • Aalberse, R.C.1    van der Gaag, R.2    van Leeuwen, J.3
  • 31
    • 10744232817 scopus 로고    scopus 로고
    • Grass pollen immunotherapy induces mucosal and peripheral IL-10 responses and blocking IgG activity
    • Nouri-Aria KT, Wachholz PA, Francis JN, Jacobson MR, Walker SM, Wilcock LK, et al. Grass pollen immunotherapy induces mucosal and peripheral IL-10 responses and blocking IgG activity. J Immunol (2004) 172(5):3252-9. doi:10.4049/jimmunol.172.5.3252
    • (2004) J Immunol , vol.172 , Issue.5 , pp. 3252-3259
    • Nouri-Aria, K.T.1    Wachholz, P.A.2    Francis, J.N.3    Jacobson, M.R.4    Walker, S.M.5    Wilcock, L.K.6
  • 32
    • 79955477145 scopus 로고    scopus 로고
    • Immunological mechanisms of allergen-specific immunotherapy
    • Jutel M, Akdis CA. Immunological mechanisms of allergen-specific immunotherapy. Allergy (2011) 66(6):725-32. doi:10.1111/j.1398-9995.2011.02589.x
    • (2011) Allergy , vol.66 , Issue.6 , pp. 725-732
    • Jutel, M.1    Akdis, C.A.2
  • 33
    • 47649116958 scopus 로고    scopus 로고
    • IgG subclasses of anti-FVIII antibodies during immune tolerance induction in patients with hemophilia A
    • van Helden PM, van den Berg HM, Gouw SC, Kaijen PH, Zuurveld MG, Mauser-Bunschoten EP, et al. IgG subclasses of anti-FVIII antibodies during immune tolerance induction in patients with hemophilia A. Br J Haematol (2008) 142(4):644-52. doi:10.1111/j.1365-2141.2008.07232.x
    • (2008) Br J Haematol , vol.142 , Issue.4 , pp. 644-652
    • van Helden, P.M.1    van den Berg, H.M.2    Gouw, S.C.3    Kaijen, P.H.4    Zuurveld, M.G.5    Mauser-Bunschoten, E.P.6
  • 34
    • 0000998359 scopus 로고
    • Gamma G4-globulin antibody causing inhibition of clotting factor VIII
    • Andersen BR, Terry WD. Gamma G4-globulin antibody causing inhibition of clotting factor VIII. Nature (1968) 217(5124):174-5. doi:10.1038/217174a0
    • (1968) Nature , vol.217 , Issue.5124 , pp. 174-175
    • Andersen, B.R.1    Terry, W.D.2
  • 35
    • 0020742152 scopus 로고
    • Analysis of IgG heavy chain subclasses of alloantibodies to factor IX by crossed immunoelectrophoresis of factor IX using the intermediate gel technique
    • Iizuka A, Nagao T. Analysis of IgG heavy chain subclasses of alloantibodies to factor IX by crossed immunoelectrophoresis of factor IX using the intermediate gel technique. Br J Haematol (1983) 53(4):687-8. doi:10.1111/j.1365-2141.1983.tb07323.x
    • (1983) Br J Haematol , vol.53 , Issue.4 , pp. 687-688
    • Iizuka, A.1    Nagao, T.2
  • 38
    • 77957296662 scopus 로고    scopus 로고
    • Induction of immunoglobulin G4 in human filariasis: an indicator of immunoregulation
    • Adjobimey T, Hoerauf A. Induction of immunoglobulin G4 in human filariasis: an indicator of immunoregulation. Ann Trop Med Parasitol (2010) 104(6):455-64. doi:10.1179/136485910X12786389891407
    • (2010) Ann Trop Med Parasitol , vol.104 , Issue.6 , pp. 455-464
    • Adjobimey, T.1    Hoerauf, A.2
  • 39
    • 0027173545 scopus 로고
    • Differential expression of IgE and IgG4 specific antibody responses in asymptomatic and chronic human filariasis
    • Kurniawan A, Yazdanbakhsh M, van Ree R, Aalberse R, Selkirk ME, Partono F, et al. Differential expression of IgE and IgG4 specific antibody responses in asymptomatic and chronic human filariasis. J Immunol (1993) 150(9):3941-50.
    • (1993) J Immunol , vol.150 , Issue.9 , pp. 3941-3950
    • Kurniawan, A.1    Yazdanbakhsh, M.2    van Ree, R.3    Aalberse, R.4    Selkirk, M.E.5    Partono, F.6
  • 40
    • 78650471809 scopus 로고    scopus 로고
    • Serologic issues in IgG4-related systemic disease and autoimmune pancreatitis
    • Sah RP, Chari ST. Serologic issues in IgG4-related systemic disease and autoimmune pancreatitis. Curr Opin Rheumatol (2011) 23(1):108-13. doi:10.1097/BOR.0b013e3283413469
    • (2011) Curr Opin Rheumatol , vol.23 , Issue.1 , pp. 108-113
    • Sah, R.P.1    Chari, S.T.2
  • 41
    • 84865350392 scopus 로고    scopus 로고
    • Value of serum IgG4 in the diagnosis of IgG4-related disease and in differentiation from rheumatic diseases and other diseases
    • Yamamoto M, Tabeya T, Naishiro Y, Yajima H, Ishigami K, Shimizu Y, et al. Value of serum IgG4 in the diagnosis of IgG4-related disease and in differentiation from rheumatic diseases and other diseases. Mod Rheumatol (2012) 22(3):419-25. doi:10.1007/s10165-011-0532-6
    • (2012) Mod Rheumatol , vol.22 , Issue.3 , pp. 419-425
    • Yamamoto, M.1    Tabeya, T.2    Naishiro, Y.3    Yajima, H.4    Ishigami, K.5    Shimizu, Y.6
  • 43
    • 0020628974 scopus 로고
    • Structural correlates of immunoglobulin diversity
    • Potter M. Structural correlates of immunoglobulin diversity. Surv Immunol Res (1983) 2(1):27-42.
    • (1983) Surv Immunol Res , vol.2 , Issue.1 , pp. 27-42
    • Potter, M.1
  • 44
    • 0027212854 scopus 로고
    • Length distribution of CDRH3 in antibodies
    • Wu TT, Johnson G, Kabat EA. Length distribution of CDRH3 in antibodies. Proteins (1993) 16(1):1-7. doi:10.1002/prot.340160102
    • (1993) Proteins , vol.16 , Issue.1 , pp. 1-7
    • Wu, T.T.1    Johnson, G.2    Kabat, E.A.3
  • 45
    • 0018102566 scopus 로고
    • Variable region genes for the immunoglobulin framework are assembled from small segments of DNA - a hypothesis
    • Kabat EA, Wu TT, Bilofsky H. Variable region genes for the immunoglobulin framework are assembled from small segments of DNA - a hypothesis. Proc Natl Acad Sci U S A (1978) 75(5):2429-33. doi:10.1073/pnas.75.5.2429
    • (1978) Proc Natl Acad Sci U S A , vol.75 , Issue.5 , pp. 2429-2433
    • Kabat, E.A.1    Wu, T.T.2    Bilofsky, H.3
  • 46
    • 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, Grau S, Jager C, Sondermann P, Brunker P, Waldhauer I, et al. Unique carbohydrate-carbohydrate interactions are required for high affinity binding between Fc{gamma}RIII and antibodies lacking core fucose. Proc Natl Acad Sci U S A (2011) 108(31):12669-74. doi:10.1073/pnas.1108455108
    • (2011) Proc Natl Acad Sci U S A , vol.108 , Issue.31 , pp. 12669-12674
    • Ferrara, C.1    Grau, S.2    Jager, C.3    Sondermann, P.4    Brunker, P.5    Waldhauer, I.6
  • 47
    • 0035844212 scopus 로고    scopus 로고
    • The structure of a human type III Fcgamma receptor in complex with Fc
    • Radaev S, Motyka S, Fridman WH, Sautes-Fridman C, Sun PD. The structure of a human type III Fcgamma receptor in complex with Fc. J Biol Chem (2001) 276(19):16469-77. doi:10.1074/jbc.M100350200
    • (2001) J Biol Chem , vol.276 , Issue.19 , pp. 16469-16477
    • Radaev, S.1    Motyka, S.2    Fridman, W.H.3    Sautes-Fridman, C.4    Sun, P.D.5
  • 48
    • 0343185953 scopus 로고    scopus 로고
    • Structural basis of the interaction between IgG and Fcgamma receptors
    • Kato K, Sautes-Fridman C, Yamada W, Kobayashi K, Uchiyama S, Kim H, et al. Structural basis of the interaction between IgG and Fcgamma receptors. J Mol Biol (2000) 295(2):213-24. doi:10.1006/jmbi.1999.3351
    • (2000) J Mol Biol , vol.295 , Issue.2 , pp. 213-224
    • Kato, K.1    Sautes-Fridman, C.2    Yamada, W.3    Kobayashi, K.4    Uchiyama, S.5    Kim, H.6
  • 49
    • 0036010538 scopus 로고    scopus 로고
    • Recognition of immunoglobulins by Fcgamma receptors
    • Radaev S, Sun P. Recognition of immunoglobulins by Fcgamma receptors. Mol Immunol (2002) 38(14):1073-83. doi:10.1016/S0161-5890(02)00036-6
    • (2002) Mol Immunol , vol.38 , Issue.14 , pp. 1073-1083
    • Radaev, S.1    Sun, P.2
  • 51
    • 0034663798 scopus 로고    scopus 로고
    • Crystal structure and immunoglobulin G binding properties of the human major histocompatibility complex-related Fc receptor (,)
    • West AP Jr, Bjorkman PJ. Crystal structure and immunoglobulin G binding properties of the human major histocompatibility complex-related Fc receptor (,). Biochemistry (2000) 39(32):9698-708. doi:10.1021/bi000749m
    • (2000) Biochemistry , vol.39 , Issue.32 , pp. 9698-9708
    • West A.P, Jr.1    Bjorkman, P.J.2
  • 52
    • 0028089908 scopus 로고
    • Crystal structure of the complex of rat neonatal Fc receptor with Fc
    • Burmeister WP, Huber AH, Bjorkman PJ. Crystal structure of the complex of rat neonatal Fc receptor with Fc. Nature (1994) 372(6504):379-83. doi:10.1038/372379a0
    • (1994) Nature , vol.372 , Issue.6504 , pp. 379-383
    • Burmeister, W.P.1    Huber, A.H.2    Bjorkman, P.J.3
  • 53
    • 43149100344 scopus 로고    scopus 로고
    • TRIM21 is an IgG receptor that is structurally, thermodynamically, and kinetically conserved
    • Keeble AH, Khan Z, Forster A, James LC. TRIM21 is an IgG receptor that is structurally, thermodynamically, and kinetically conserved. Proc Natl Acad Sci U S A (2008) 105(16):6045-50. doi:10.1073/pnas.0800159105
    • (2008) Proc Natl Acad Sci U S A , vol.105 , Issue.16 , pp. 6045-6050
    • Keeble, A.H.1    Khan, Z.2    Forster, A.3    James, L.C.4
  • 54
    • 84893121418 scopus 로고    scopus 로고
    • A prominent lack of IgG1-Fc fucosylation of platelet alloantibodies in pregnancy
    • Kapur R, Kustiawan I, Vestrheim A, Koeleman C, Visser R, Einarsdottir HK, et al. A prominent lack of IgG1-Fc fucosylation of platelet alloantibodies in pregnancy. Blood (2014) 123(4):471-80. doi:10.1182/blood-2013-09-527978
    • (2014) Blood , vol.123 , Issue.4 , pp. 471-480
    • Kapur, R.1    Kustiawan, I.2    Vestrheim, A.3    Koeleman, C.4    Visser, R.5    Einarsdottir, H.K.6
  • 55
    • 61849098877 scopus 로고    scopus 로고
    • Regulated glycosylation patterns of IgG during alloimmune responses against human platelet antigens
    • Wuhrer M, Porcelijn L, Kapur R, Koeleman CA, Deelder A, de Haas M, et al. Regulated glycosylation patterns of IgG during alloimmune responses against human platelet antigens. J Proteome Res (2009) 8(2):450-6. doi:10.1021/pr800651j
    • (2009) J Proteome Res , vol.8 , Issue.2 , pp. 450-456
    • Wuhrer, M.1    Porcelijn, L.2    Kapur, R.3    Koeleman, C.A.4    Deelder, A.5    de Haas, M.6
  • 56
    • 0025909201 scopus 로고
    • Antibody variable region glycosylation: position effects on antigen binding and carbohydrate structure
    • Wright A, Tao MH, Kabat EA, Morrison SL. Antibody variable region glycosylation: position effects on antigen binding and carbohydrate structure. EMBO J (1991) 10(10):2717-23.
    • (1991) EMBO J , vol.10 , Issue.10 , pp. 2717-2723
    • Wright, A.1    Tao, M.H.2    Kabat, E.A.3    Morrison, S.L.4
  • 57
    • 84877152391 scopus 로고    scopus 로고
    • Natural variation in Fc glycosylation of HIV-specific antibodies impacts antiviral activity
    • Ackerman ME, Crispin M, Yu X, Baruah K, Boesch AW, Harvey DJ, et al. Natural variation in Fc glycosylation of HIV-specific antibodies impacts antiviral activity. J Clin Invest (2013) 123(5):2183-92. doi:10.1172/JCI65708DS1
    • (2013) J Clin Invest , vol.123 , Issue.5 , pp. 2183-2192
    • Ackerman, M.E.1    Crispin, M.2    Yu, X.3    Baruah, K.4    Boesch, A.W.5    Harvey, D.J.6
  • 58
    • 79959555556 scopus 로고    scopus 로고
    • Enrichment of sialylated IgG by lectin fractionation does not enhance the efficacy of immunoglobulin G in a murine model of immune thrombocytopenia
    • Guhr T, Bloem J, Derksen NI, Wuhrer M, Koenderman AH, Aalberse RC, et al. Enrichment of sialylated IgG by lectin fractionation does not enhance the efficacy of immunoglobulin G in a murine model of immune thrombocytopenia. PLoS One (2011) 6(6):e21246. doi:10.1371/journal.pone.0021246
    • (2011) PLoS One , vol.6 , Issue.6
    • Guhr, T.1    Bloem, J.2    Derksen, N.I.3    Wuhrer, M.4    Koenderman, A.H.5    Aalberse, R.C.6
  • 59
    • 69949107840 scopus 로고    scopus 로고
    • A close look at human IgG sialylation and subclass distribution after lectin fractionation
    • Stadlmann J, Weber A, Pabst M, Anderle H, Kunert R, Ehrlich HJ, et al. A close look at human IgG sialylation and subclass distribution after lectin fractionation. Proteomics (2009) 9(17):4143-53. doi:10.1002/pmic.200800931
    • (2009) Proteomics , vol.9 , Issue.17 , pp. 4143-4153
    • Stadlmann, J.1    Weber, A.2    Pabst, M.3    Anderle, H.4    Kunert, R.5    Ehrlich, H.J.6
  • 60
    • 34247116573 scopus 로고    scopus 로고
    • Human follicular lymphoma cells contain oligomannose glycans in the antigen-binding site of the B-cell receptor
    • Radcliffe CM, Arnold JN, Suter DM, Wormald MR, Harvey DJ, Royle L, et al. Human follicular lymphoma cells contain oligomannose glycans in the antigen-binding site of the B-cell receptor. J Biol Chem (2007) 282(10):7405-15. doi:10.1074/jbc.M602690200
    • (2007) J Biol Chem , vol.282 , Issue.10 , pp. 7405-7415
    • Radcliffe, C.M.1    Arnold, J.N.2    Suter, D.M.3    Wormald, M.R.4    Harvey, D.J.5    Royle, L.6
  • 61
    • 0023530681 scopus 로고
    • Human IgG subclass measurements in the clinical laboratory
    • Hamilton RG. Human IgG subclass measurements in the clinical laboratory. Clin Chem (1987) 33(10):1707-25.
    • (1987) Clin Chem , vol.33 , Issue.10 , pp. 1707-1725
    • Hamilton, R.G.1
  • 62
    • 0031253752 scopus 로고    scopus 로고
    • Flexibility of human IgG subclasses
    • Roux KH, Strelets L, Michaelsen TE. Flexibility of human IgG subclasses. J Immunol (1997) 159(7):3372-82.
    • (1997) J Immunol , vol.159 , Issue.7 , pp. 3372-3382
    • Roux, K.H.1    Strelets, L.2    Michaelsen, T.E.3
  • 63
    • 0027324328 scopus 로고
    • Human IgG3 is decreased and IgG1, IgG2 and IgG4 are unchanged in molecular size by mild reduction and reoxidation without any major change in effector functions
    • Michaelsen TE, Naess LM, Aase A. Human IgG3 is decreased and IgG1, IgG2 and IgG4 are unchanged in molecular size by mild reduction and reoxidation without any major change in effector functions. Mol Immunol (1993) 30(1):35-45. doi:10.1016/0161-5890(93)90424-A
    • (1993) Mol Immunol , vol.30 , Issue.1 , pp. 35-45
    • Michaelsen, T.E.1    Naess, L.M.2    Aase, A.3
  • 64
    • 0015095191 scopus 로고
    • The unique molecular weight of the heavy chain from human IgG3
    • Saluk PH, Clem LW. The unique molecular weight of the heavy chain from human IgG3. J Immunol (1971) 107(1):298-301.
    • (1971) J Immunol , vol.107 , Issue.1 , pp. 298-301
    • Saluk, P.H.1    Clem, L.W.2
  • 65
    • 0035965869 scopus 로고    scopus 로고
    • Crystallohydrodynamics for solving the hydration problem for multi-domain proteins: open physiological conformations for human IgG.
    • Carrasco B, Garcia de la Torre J, Davis KG, Jones S, Athwal D, Walters C, et al. Crystallohydrodynamics for solving the hydration problem for multi-domain proteins: open physiological conformations for human IgG. Biophys Chem (2001) 93(2-3):181-96. doi:10.1016/S0301-4622(01)00220-4
    • (2001) Biophys Chem , vol.93 , Issue.2-3 , pp. 181-196
    • Carrasco, B.1    Garcia de la Torre, J.2    Davis, K.G.3    Jones, S.4    Athwal, D.5    Walters, C.6
  • 66
    • 47049097120 scopus 로고    scopus 로고
    • Human IgG2 antibodies display disulfide-mediated structural isoforms
    • Wypych J, Li M, Guo A, Zhang Z, Martinez T, Allen MJ, et al. Human IgG2 antibodies display disulfide-mediated structural isoforms. J Biol Chem (2008) 283(23):16194-205. doi:10.1074/jbc.M709987200
    • (2008) J Biol Chem , vol.283 , Issue.23 , pp. 16194-16205
    • Wypych, J.1    Li, M.2    Guo, A.3    Zhang, Z.4    Martinez, T.5    Allen, M.J.6
  • 67
    • 76149108167 scopus 로고    scopus 로고
    • Determination of Fab-hinge disulfide connectivity in structural isoforms of a recombinant human immunoglobulin G2 antibody
    • Zhang B, Harder AG, Connelly HM, Maheu LL, Cockrill SL. Determination of Fab-hinge disulfide connectivity in structural isoforms of a recombinant human immunoglobulin G2 antibody. Anal Chem (2010) 82(3):1090-9. doi:10.1021/ac902466z
    • (2010) Anal Chem , vol.82 , Issue.3 , pp. 1090-1099
    • Zhang, B.1    Harder, A.G.2    Connelly, H.M.3    Maheu, L.L.4    Cockrill, S.L.5
  • 68
    • 47049114087 scopus 로고    scopus 로고
    • Structural and functional characterization of disulfide isoforms of the human IgG2 subclass
    • Dillon TM, Ricci MS, Vezina C, Flynn GC, Liu YD, Rehder DS, et al. Structural and functional characterization of disulfide isoforms of the human IgG2 subclass. J Biol Chem (2008) 283(23):16206-15. doi:10.1074/jbc.M709988200
    • (2008) J Biol Chem , vol.283 , Issue.23 , pp. 16206-16215
    • Dillon, T.M.1    Ricci, M.S.2    Vezina, C.3    Flynn, G.C.4    Liu, Y.D.5    Rehder, D.S.6
  • 69
    • 77950281386 scopus 로고    scopus 로고
    • Mutations within a human IgG2 antibody form distinct and homogeneous disulfide isomers but do not affect Fc gamma receptor or C1q binding
    • Lightle S, Aykent S, Lacher N, Mitaksov V, Wells K, Zobel J, et al. Mutations within a human IgG2 antibody form distinct and homogeneous disulfide isomers but do not affect Fc gamma receptor or C1q binding. Protein Sci (2010) 19(4):753-62. doi:10.1002/pro.352
    • (2010) Protein Sci , vol.19 , Issue.4 , pp. 753-762
    • Lightle, S.1    Aykent, S.2    Lacher, N.3    Mitaksov, V.4    Wells, K.5    Zobel, J.6
  • 70
    • 0037443466 scopus 로고    scopus 로고
    • Human IgG2 can form covalent dimers
    • Yoo EM, Wims LA, Chan LA, Morrison SL. Human IgG2 can form covalent dimers. J Immunol (2003) 170(6):3134-8. doi:10.4049/jimmunol.170.6.3134
    • (2003) J Immunol , vol.170 , Issue.6 , pp. 3134-3138
    • Yoo, E.M.1    Wims, L.A.2    Chan, L.A.3    Morrison, S.L.4
  • 71
    • 0030934272 scopus 로고    scopus 로고
    • The CXXC motif: a rheostat in the active site
    • Chivers PT, Prehoda KE, Raines RT. The CXXC motif: a rheostat in the active site. Biochemistry (1997) 36(14):4061-6. doi:10.1021/bi9628580
    • (1997) Biochemistry , vol.36 , Issue.14 , pp. 4061-4066
    • Chivers, P.T.1    Prehoda, K.E.2    Raines, R.T.3
  • 72
    • 0031058617 scopus 로고    scopus 로고
    • Intrachain disulfide bond in the core hinge region of human IgG4
    • Bloom JW, Madanat MS, Marriott D, Wong T, Chan SY. Intrachain disulfide bond in the core hinge region of human IgG4. Protein Sci (1997) 6(2):407-15. doi:10.1002/pro.5560060217
    • (1997) Protein Sci , vol.6 , Issue.2 , pp. 407-415
    • Bloom, J.W.1    Madanat, M.S.2    Marriott, D.3    Wong, T.4    Chan, S.Y.5
  • 73
    • 0027216004 scopus 로고
    • A single amino acid substitution abolishes the heterogeneity of chimeric mouse/human (IgG4) antibody
    • Angal S, King DJ, Bodmer MW, Turner A, Lawson AD, Roberts G, et al. A single amino acid substitution abolishes the heterogeneity of chimeric mouse/human (IgG4) antibody. Mol Immunol (1993) 30(1):105-8. doi:10.1016/0161-5890(93)90432-B
    • (1993) Mol Immunol , vol.30 , Issue.1 , pp. 105-108
    • Angal, S.1    King, D.J.2    Bodmer, M.W.3    Turner, A.4    Lawson, A.D.5    Roberts, G.6
  • 74
  • 75
    • 0022995766 scopus 로고
    • Serologic aspects of IgG4 antibodies II. IgG4 antibodies form small, nonprecipitating immune complexes due to functional monovalency
    • Van der Zee JS, Van Swieten P, Aalberse RC. Serologic aspects of IgG4 antibodies. II. IgG4 antibodies form small, nonprecipitating immune complexes due to functional monovalency. J Immunol (1986) 137(11):3566-71.
    • (1986) J Immunol , vol.137 , Issue.11 , pp. 3566-3571
    • Van der Zee, J.S.1    Van Swieten, P.2    Aalberse, R.C.3
  • 76
    • 34548694517 scopus 로고    scopus 로고
    • Anti-inflammatory activity of human IgG4 antibodies by dynamic Fab arm exchange
    • van der Neut KM, Schuurman J, Losen M, Bleeker WK, Martinez-Martinez P, Vermeulen E, et al. Anti-inflammatory activity of human IgG4 antibodies by dynamic Fab arm exchange. Science (2007) 317(5844):1554-7. doi:10.1126/science.1144603
    • (2007) Science , vol.317 , Issue.5844 , pp. 1554-1557
    • van der Neut, K.M.1    Schuurman, J.2    Losen, M.3    Bleeker, W.K.4    Martinez-Martinez, P.5    Vermeulen, E.6
  • 77
    • 84896889967 scopus 로고    scopus 로고
    • Dynamics of inter-heavy chain interactions in human immunoglobulin G (IgG) subclasses studied by kinetic Fab arm exchange
    • Rispens T, Davies AM, Ooijevaar-de Heer P, Absalah S, Bende O, Sutton BJ, et al. Dynamics of inter-heavy chain interactions in human immunoglobulin G (IgG) subclasses studied by kinetic Fab arm exchange. J Biol Chem (2014) 289(9):6098-109. doi:10.1074/jbc.M113.541813
    • (2014) J Biol Chem , vol.289 , Issue.9 , pp. 6098-6109
    • Rispens, T.1    Davies, A.M.2    Ooijevaar-de Heer, P.3    Absalah, S.4    Bende, O.5    Sutton, B.J.6
  • 78
    • 80052512948 scopus 로고    scopus 로고
    • Species-specific determinants in the IgG CH3 domain enable Fab-arm exchange by affecting the noncovalent CH3-CH3 interaction strength
    • Labrijn AF, Rispens T, Meesters J, Rose RJ, den Bleker TH, Loverix S, et al. Species-specific determinants in the IgG CH3 domain enable Fab-arm exchange by affecting the noncovalent CH3-CH3 interaction strength. J Immunol (2011) 187(6):3238-46. doi:10.4049/jimmunol.1003336
    • (2011) J Immunol , vol.187 , Issue.6 , pp. 3238-3246
    • Labrijn, A.F.1    Rispens, T.2    Meesters, J.3    Rose, R.J.4    den Bleker, T.H.5    Loverix, S.6
  • 80
    • 84866696938 scopus 로고    scopus 로고
    • Human Gm, Km, and Am allotypes and their molecular characterization: a remarkable demonstration of polymorphism
    • Lefranc MP, Lefranc G. Human Gm, Km, and Am allotypes and their molecular characterization: a remarkable demonstration of polymorphism. Methods Mol Biol (2012) 882:635-80. doi:10.1007/978-1-61779-842-9_34
    • (2012) Methods Mol Biol , vol.882 , pp. 635-680
    • Lefranc, M.P.1    Lefranc, G.2
  • 81
    • 0024439023 scopus 로고
    • Polymorphisms of human immunoglobulins: Gm, Am, Em and Km allotypes
    • de Lange GG. Polymorphisms of human immunoglobulins: Gm, Am, Em and Km allotypes. Exp Clin Immunogenet (1989) 6(1):7-17.
    • (1989) Exp Clin Immunogenet , vol.6 , Issue.1 , pp. 7-17
    • de Lange, G.G.1
  • 82
    • 70349769842 scopus 로고    scopus 로고
    • Human immunoglobulin allotypes: possible implications for immunogenicity
    • Jefferis R, Lefranc MP. Human immunoglobulin allotypes: possible implications for immunogenicity. MAbs (2009) 1(4):332-8. doi:10.4161/mabs.1.4.9122
    • (2009) MAbs , vol.1 , Issue.4 , pp. 332-338
    • Jefferis, R.1    Lefranc, M.P.2
  • 83
    • 0034750593 scopus 로고    scopus 로고
    • DNA sequence variability of IGHG3 alleles associated to the main G3m haplotypes in human populations
    • Dard P, Lefranc MP, Osipova L, Sanchez-Mazas A. DNA sequence variability of IGHG3 alleles associated to the main G3m haplotypes in human populations. Eur J Hum Genet (2001) 9(10):765-72. doi:10.1038/sj.ejhg.5200700
    • (2001) Eur J Hum Genet , vol.9 , Issue.10 , pp. 765-772
    • Dard, P.1    Lefranc, M.P.2    Osipova, L.3    Sanchez-Mazas, A.4
  • 84
    • 0031714381 scopus 로고    scopus 로고
    • Molecular characterization of immunoglobulin G4 gene isoallotypes
    • Brusco A, Saviozzi S, Cinque F, DeMarchi M, Boccazzi C, De LG, et al. Molecular characterization of immunoglobulin G4 gene isoallotypes. Eur J Immunogenet (1998) 25(5):349-55. doi:10.1111/j.1744-313X.1998.tb01152.x
    • (1998) Eur J Immunogenet , vol.25 , Issue.5 , pp. 349-355
    • Brusco, A.1    Saviozzi, S.2    Cinque, F.3    DeMarchi, M.4    Boccazzi, C.5    De, L.G.6
  • 85
    • 0028991057 scopus 로고
    • Molecular characterization of Gm (n+) and G2m (n-) allotypes
    • Brusco A, de Lange GG, Boccazzi C, Carbonara AO. Molecular characterization of Gm (n+) and G2m (n-) allotypes. Immunogenetics (1995) 42(5):414-7. doi:10.1007/BF00179404
    • (1995) Immunogenetics , vol.42 , Issue.5 , pp. 414-417
    • Brusco, A.1    de Lange, G.G.2    Boccazzi, C.3    Carbonara, A.O.4
  • 86
    • 0003580769 scopus 로고
    • Monoclonal Antibodies Against Human Immunoglobulin Allotypes. Ph.D. thesis.
    • University of London.London
    • de Lange G. Monoclonal Antibodies Against Human Immunoglobulin Allotypes. Ph.D. thesis, University of London, London (1988).
    • (1988)
    • de Lange, G.1
  • 87
    • 0000890791 scopus 로고
    • Antibody to hereditary human gamma-globulin (Gm) factor resulting from maternal-fetal incompatibility
    • Fudenberg HH, Fudenberg BR. Antibody to hereditary human gamma-globulin (Gm) factor resulting from maternal-fetal incompatibility. Science (1964) 145(3628):170-1. doi:10.1126/science.145.3628.170
    • (1964) Science , vol.145 , Issue.3628 , pp. 170-171
    • Fudenberg, H.H.1    Fudenberg, B.R.2
  • 88
    • 0022333438 scopus 로고
    • Immunoglobulin allotypes in a Chinese population: comparison of haplotype frequencies with other Asian groups.
    • de Lange G, Zhong FM, Henke J, Feng ZC, Bernhardt R, van Leeuwen F, et al. Immunoglobulin allotypes in a Chinese population: comparison of haplotype frequencies with other Asian groups. J Immunogenet (1985) 12(4-5):191-5. doi:10.1111/j.1744-313X.1985.tb00846.x
    • (1985) J Immunogenet , vol.12 , Issue.4-5 , pp. 191-195
    • de Lange, G.1    Zhong, F.M.2    Henke, J.3    Feng, Z.C.4    Bernhardt, R.5    van Leeuwen, F.6
  • 89
    • 82455171807 scopus 로고    scopus 로고
    • Rapid LC-MS screening for IgG Fc modifications and allelic variants in blood.
    • Goetze AM, Zhang Z, Liu L, Jacobsen FW, Flynn GC. Rapid LC-MS screening for IgG Fc modifications and allelic variants in blood. Mol Immunol (2011) 49(1-2):338-52. doi:10.1016/j.molimm.2011.09.002
    • (2011) Mol Immunol , vol.49 , Issue.1-2 , pp. 338-352
    • Goetze, A.M.1    Zhang, Z.2    Liu, L.3    Jacobsen, F.W.4    Flynn, G.C.5
  • 90
    • 0018306574 scopus 로고
    • An amino acid substitution in the gamma 1 chain of human immunoglobulin G associated with the Gm (2) allotype
    • Cook CE, Steinberg AG. An amino acid substitution in the gamma 1 chain of human immunoglobulin G associated with the Gm (2) allotype. Mol Immunol (1979) 16(8):555-8. doi:10.1016/0161-5890(79)90117-2
    • (1979) Mol Immunol , vol.16 , Issue.8 , pp. 555-558
    • Cook, C.E.1    Steinberg, A.G.2
  • 92
    • 0038193485 scopus 로고    scopus 로고
    • Three new alleles of IGHG2 and their prevalence in Danish Caucasians, Mozambican Blacks and Japanese
    • Hougs L, Garred P, Kawasaki T, Kawasaki N, Svejgaard A, Barington T. Three new alleles of IGHG2 and their prevalence in Danish Caucasians, Mozambican Blacks and Japanese. Tissue Antigens (2003) 61(3):231-9. doi:10.1034/j.1399-0039.2003.00048.x
    • (2003) Tissue Antigens , vol.61 , Issue.3 , pp. 231-239
    • Hougs, L.1    Garred, P.2    Kawasaki, T.3    Kawasaki, N.4    Svejgaard, A.5    Barington, T.6
  • 93
    • 78650444450 scopus 로고    scopus 로고
    • Surprising negative association between IgG1 allotype disparity and anti-adalimumab formation: a cohort study 1
    • Bartelds GM, de Groot E, Nurmohamed MT, Hart MH, van Eede PH, Wijbrandts CA, et al. Surprising negative association between IgG1 allotype disparity and anti-adalimumab formation: a cohort study 1. Arthritis Res Ther (2010) 12(6):R221. doi:10.1186/ar3208
    • (2010) Arthritis Res Ther , vol.12 , Issue.6
    • Bartelds, G.M.1    de Groot, E.2    Nurmohamed, M.T.3    Hart, M.H.4    van Eede, P.H.5    Wijbrandts, C.A.6
  • 94
    • 67149139366 scopus 로고    scopus 로고
    • IgG1 heavy chain-coding gene polymorphism (G1m allotypes) and development of antibodies-to-infliximab 8
    • Magdelaine-Beuzelin C, Vermeire S, Goodall M, Baert F, Noman M, Assche GV, et al. IgG1 heavy chain-coding gene polymorphism (G1m allotypes) and development of antibodies-to-infliximab 8. Pharmacogenet Genomics (2009) 19(5):383-7. doi:10.1097/FPC.0b013e32832a06bf
    • (2009) Pharmacogenet Genomics , vol.19 , Issue.5 , pp. 383-387
    • Magdelaine-Beuzelin, C.1    Vermeire, S.2    Goodall, M.3    Baert, F.4    Noman, M.5    Assche, G.V.6
  • 95
    • 0015257040 scopus 로고
    • Correlations between the concentrations of the four sub-classes of IgG and Gm allotypes in normal human sera
    • Morell A, Skvaril F, Steinberg AG, Van Loghem E, Terry WD. Correlations between the concentrations of the four sub-classes of IgG and Gm allotypes in normal human sera. J Immunol (1972) 108(1):195-206.
    • (1972) J Immunol , vol.108 , Issue.1 , pp. 195-206
    • Morell, A.1    Skvaril, F.2    Steinberg, A.G.3    Van Loghem, E.4    Terry, W.D.5
  • 96
    • 0018876711 scopus 로고
    • Secondary structure of mRNAefficiency of translation initiation.
    • Iserentant D, Fiers W. Secondary structure of mRNA and efficiency of translation initiation. Gene (1980) 9(1-2):1-12. doi:10.1016/0378-1119(80)90163-8
    • (1980) Gene , vol.9 , Issue.1-2 , pp. 1-12
    • Iserentant, D.1    Fiers, W.2
  • 97
    • 84899821225 scopus 로고    scopus 로고
    • Deciphering the rules by which dynamics of mRNA secondary structure affect translation efficiency in Saccharomyces cerevisiae
    • Mao Y, Liu H, Liu Y, Tao S. Deciphering the rules by which dynamics of mRNA secondary structure affect translation efficiency in Saccharomyces cerevisiae. Nucleic Acids Res (2014) 42(8):4813-22. doi:10.1093/nar/gku159
    • (2014) Nucleic Acids Res , vol.42 , Issue.8 , pp. 4813-4822
    • Mao, Y.1    Liu, H.2    Liu, Y.3    Tao, S.4
  • 98
    • 0033838336 scopus 로고    scopus 로고
    • An allotype-associated polymorphism in the gamma3 promoter determines the germ-line gamma3 transcriptional rate but does not influence switching and subsequent IgG3 production
    • <2388::AID-IMMU2388>3.0.CO;2-C
    • Pan Q, Petit-Frere C, Hammarstrom L. An allotype-associated polymorphism in the gamma3 promoter determines the germ-line gamma3 transcriptional rate but does not influence switching and subsequent IgG3 production. Eur J Immunol (2000) 30(8):2388-93. doi:10.1002/1521-4141(2000)30:8<2388::AID-IMMU2388>3.0.CO;2-C
    • (2000) Eur J Immunol , vol.30 , Issue.8 , pp. 2388-2393
    • Pan, Q.1    Petit-Frere, C.2    Hammarstrom, L.3
  • 99
    • 84896055730 scopus 로고    scopus 로고
    • Complement is activated by IgG hexamers assembled at the cell surface
    • Diebolder C, Beurskens FJ, de Jong RN, Koning RI, Strumane K, Lindorfer M, et al. Complement is activated by IgG hexamers assembled at the cell surface. Science (2014) 343(6176):1260-3. doi:10.1126/science.1248943
    • (2014) Science , vol.343 , Issue.6176 , pp. 1260-1263
    • Diebolder, C.1    Beurskens, F.J.2    de Jong, R.N.3    Koning, R.I.4    Strumane, K.5    Lindorfer, M.6
  • 101
    • 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, Stanworth D, et al. Association of rheumatoid arthritis and primary osteoarthritis with changes in the glycosylation pattern of total serum IgG. Nature (1985) 316(6027):452-7. doi:10.1038/316452a0
    • (1985) Nature , vol.316 , Issue.6027 , pp. 452-457
    • Parekh, R.B.1    Dwek, R.A.2    Sutton, B.J.3    Fernandes, D.L.4    Leung, A.5    Stanworth, D.6
  • 102
    • 84910647104 scopus 로고    scopus 로고
    • IgG Fab glycosylation analysis using a new mass spectrometric high-throughput profiling method reveals pregnancy-associated changes.
    • Bondt A, Rombouts Y, Selman MH, Hensbergen PJ, Reiding KR, Hazes JM, et al. IgG Fab glycosylation analysis using a new mass spectrometric high-throughput profiling method reveals pregnancy-associated changes. Mol Cell Proteomics (2014). doi:10.1074/mcp.M114.039537
    • (2014) Mol Cell Proteomics
    • Bondt, A.1    Rombouts, Y.2    Selman, M.H.3    Hensbergen, P.J.4    Reiding, K.R.5    Hazes J.M., .6
  • 103
    • 84907597618 scopus 로고    scopus 로고
    • Low anti-RhD IgG-Fc-fucosylation in pregnancy: a new variable predicting severity in haemolytic disease of the fetus and newborn
    • Kapur R, Della Valle L, Sonneveld M, Hipgrave Ederveen A, Visser R, Ligthart P, et al. Low anti-RhD IgG-Fc-fucosylation in pregnancy: a new variable predicting severity in haemolytic disease of the fetus and newborn. Br J Haematol (2014) 166(6):936-45. doi:10.1111/bjh.12965
    • (2014) Br J Haematol , vol.166 , Issue.6 , pp. 936-945
    • Kapur, R.1    Della Valle, L.2    Sonneveld, M.3    Hipgrave Ederveen, A.4    Visser, R.5    Ligthart, P.6
  • 104
    • 84891958414 scopus 로고    scopus 로고
    • Glycosylation of immunoglobulin g: role of genetic and epigenetic influences
    • Menni C, Keser T, Mangino M, Bell JT, Erte I, Akmacic I, et al. Glycosylation of immunoglobulin g: role of genetic and epigenetic influences. PLoS One (2013) 8(12):e82558. doi:10.1371/journal.pone.0082558
    • (2013) PLoS One , vol.8 , Issue.12
    • Menni, C.1    Keser, T.2    Mangino, M.3    Bell, J.T.4    Erte, I.5    Akmacic, I.6
  • 105
    • 84862826701 scopus 로고    scopus 로고
    • Human IgG Fc-glycosylation profiling reveals associations with age, sex, female sex hormones and thyroid cancer
    • Chen G, Wang Y, Qiu L, Qin X, Liu H, Wang X, et al. Human IgG Fc-glycosylation profiling reveals associations with age, sex, female sex hormones and thyroid cancer. J Proteomics (2012) 75(10):2824-34. doi:10.1016/j.jprot.2012.02.001
    • (2012) J Proteomics , vol.75 , Issue.10 , pp. 2824-2834
    • Chen, G.1    Wang, Y.2    Qiu, L.3    Qin, X.4    Liu, H.5    Wang, X.6
  • 107
    • 79954416352 scopus 로고    scopus 로고
    • Progesterone induces a switch in oligosaccharyltransferase isoform expression: consequences on IgG N-glycosylation
    • Prados MB, La Blunda J, Szekeres-Bartho J, Caramelo J, Miranda S. Progesterone induces a switch in oligosaccharyltransferase isoform expression: consequences on IgG N-glycosylation. Immunol Lett (2011) 137(1-2):28-37. doi:10.1016/j.imlet.2011.01.017
    • (2011) Immunol Lett , vol.137 , Issue.1-2 , pp. 28-37
    • Prados, M.B.1    La Blunda, J.2    Szekeres-Bartho, J.3    Caramelo, J.4    Miranda, S.5
  • 108
    • 84867806174 scopus 로고    scopus 로고
    • Chemical and structural analysis of an antibody folding intermediate trapped during glycan biosynthesis
    • Bowden TA, Baruah K, Coles CH, Harvey DJ, Yu X, Song BD, et al. Chemical and structural analysis of an antibody folding intermediate trapped during glycan biosynthesis. J Am Chem Soc (2012) 134(42):17554-63. doi:10.1021/ja306068g
    • (2012) J Am Chem Soc , vol.134 , Issue.42 , pp. 17554-17563
    • Bowden, T.A.1    Baruah, K.2    Coles, C.H.3    Harvey, D.J.4    Yu, X.5    Song, B.D.6
  • 109
    • 0035824579 scopus 로고    scopus 로고
    • Role of oligosaccharide residues of IgG1-Fc in Fc gamma RIIb binding
    • Mimura Y, Sondermann P, Ghirlando R, Lund J, Young SP, Goodall M, et al. Role of oligosaccharide residues of IgG1-Fc in Fc gamma RIIb binding. J Biol Chem (2001) 276(49):45539-47. doi:10.1074/jbc.M107478200
    • (2001) J Biol Chem , vol.276 , Issue.49 , pp. 45539-45547
    • Mimura, Y.1    Sondermann, P.2    Ghirlando, R.3    Lund, J.4    Young, S.P.5    Goodall, M.6
  • 110
    • 0034691322 scopus 로고    scopus 로고
    • The 3.2-A crystal structure of the human IgG1 Fc fragment-Fc gammaRIII complex
    • Sondermann P, Huber R, Oosthuizen V, Jacob U. The 3.2-A crystal structure of the human IgG1 Fc fragment-Fc gammaRIII complex. Nature (2000) 406(6793):267-73. doi:10.1038/35018508
    • (2000) Nature , vol.406 , Issue.6793 , pp. 267-273
    • Sondermann, P.1    Huber, R.2    Oosthuizen, V.3    Jacob, U.4
  • 111
    • 80054944116 scopus 로고    scopus 로고
    • Structural basis for improved efficacy of therapeutic antibodies on defucosylation of their Fc glycans
    • Mizushima T, Yagi H, Takemoto E, Shibata-Koyama M, Isoda Y, Iida S, et al. Structural basis for improved efficacy of therapeutic antibodies on defucosylation of their Fc glycans. Genes Cells (2011) 16(11):1071-80. doi:10.1111/j.1365-2443.2011.01552.x
    • (2011) Genes Cells , vol.16 , Issue.11 , pp. 1071-1080
    • Mizushima, T.1    Yagi, H.2    Takemoto, E.3    Shibata-Koyama, M.4    Isoda, Y.5    Iida, S.6
  • 112
    • 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 RL, Lai J, Keck R, O'Connell LY, Hong K, Meng YG, et al. Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human Fcgamma RIII and antibody-dependent cellular toxicity. J Biol Chem (2002) 277(30):26733-40. doi:10.1074/jbc.M202069200
    • (2002) J Biol Chem , vol.277 , Issue.30 , pp. 26733-26740
    • Shields, R.L.1    Lai, J.2    Keck, R.3    O'Connell, L.Y.4    Hong, K.5    Meng, Y.G.6
  • 113
    • 71749094615 scopus 로고    scopus 로고
    • Production of therapeutic antibodies with controlled fucosylation
    • Yamane-Ohnuki N, Satoh M. Production of therapeutic antibodies with controlled fucosylation. MAbs (2009) 1(3):230-6. doi:10.4161/mabs.1.3.8328
    • (2009) MAbs , vol.1 , Issue.3 , pp. 230-236
    • Yamane-Ohnuki, N.1    Satoh, M.2
  • 114
    • 67649394336 scopus 로고    scopus 로고
    • Recombinant antibody therapeutics: the impact of glycosylation on mechanisms of action
    • Jefferis R. Recombinant antibody therapeutics: the impact of glycosylation on mechanisms of action. Trends Pharmacol Sci (2009) 30(7):356-62. doi:10.1016/j.tips.2009.04.007
    • (2009) Trends Pharmacol Sci , vol.30 , Issue.7 , pp. 356-362
    • Jefferis, R.1
  • 115
    • 59749104215 scopus 로고    scopus 로고
    • Nonfucosylated rituximab potentiates human neutrophil phagocytosis through its high binding for FcgammaRIIIb and MHC class II expression on the phagocytotic neutrophils
    • Shibata-Koyama M, Iida S, Misaka H, Mori K, Yano K, Shitara K, et al. Nonfucosylated rituximab potentiates human neutrophil phagocytosis through its high binding for FcgammaRIIIb and MHC class II expression on the phagocytotic neutrophils. Exp Hematol (2009) 37(3):309-21. doi:10.1016/j.exphem.2008.11.006
    • (2009) Exp Hematol , vol.37 , Issue.3 , pp. 309-321
    • Shibata-Koyama, M.1    Iida, S.2    Misaka, H.3    Mori, K.4    Yano, K.5    Shitara, K.6
  • 116
    • 55249121695 scopus 로고    scopus 로고
    • Antibody fucosylation differentially impacts cytotoxicity mediated by NK and PMN effector cells
    • Peipp M, Lammerts van Bueren JJ, Schneider-Merck T, Bleeker WK, Dechant M, Beyer T, et al. Antibody fucosylation differentially impacts cytotoxicity mediated by NK and PMN effector cells. Blood (2008) 112(6):2390-9. doi:10.1182/blood-2008-03-144600
    • (2008) Blood , vol.112 , Issue.6 , pp. 2390-2399
    • Peipp, M.1    Lammerts van Bueren, J.J.2    Schneider-Merck, T.3    Bleeker, W.K.4    Dechant, M.5    Beyer, T.6
  • 118
    • 84857357868 scopus 로고    scopus 로고
    • Immunoglobulin G Fc N-glycan profiling in patients with gastric cancer by LC-ESI-MS: relation to tumor progression and survival
    • Kodar K, Stadlmann J, Klaamas K, Sergeyev B, Kurtenkov O. Immunoglobulin G Fc N-glycan profiling in patients with gastric cancer by LC-ESI-MS: relation to tumor progression and survival. Glycoconj J (2012) 29(1):57-66. doi:10.1007/s10719-011-9364-z
    • (2012) Glycoconj J , vol.29 , Issue.1 , pp. 57-66
    • Kodar, K.1    Stadlmann, J.2    Klaamas, K.3    Sergeyev, B.4    Kurtenkov, O.5
  • 119
    • 83055166012 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis and Fcgamma receptor binding of homogeneous glycoforms of antibody Fc domain Presence of a bisecting sugar moiety enhances the affinity of Fc to FcgammaIIIa receptor
    • Zou G, Ochiai H, Huang W, Yang Q, Li C, Wang LX. Chemoenzymatic synthesis and Fcgamma receptor binding of homogeneous glycoforms of antibody Fc domain. Presence of a bisecting sugar moiety enhances the affinity of Fc to FcgammaIIIa receptor. J Am Chem Soc (2011) 133(46):18975-91. doi:10.1021/ja208390n
    • (2011) J Am Chem Soc , vol.133 , Issue.46 , pp. 18975-18991
    • Zou, G.1    Ochiai, H.2    Huang, W.3    Yang, Q.4    Li, C.5    Wang, L.X.6
  • 120
    • 84873404470 scopus 로고    scopus 로고
    • High-throughput IgG Fc N-glycosylation profiling by mass spectrometry of glycopeptides
    • Bakovic MP, Selman MH, Hoffmann M, Rudan I, Campbell H, Deelder AM, et al. High-throughput IgG Fc N-glycosylation profiling by mass spectrometry of glycopeptides. J Proteome Res (2013) 12(2):821-31. doi:10.1021/pr300887z
    • (2013) J Proteome Res , vol.12 , Issue.2 , pp. 821-831
    • Bakovic, M.P.1    Selman, M.H.2    Hoffmann, M.3    Rudan, I.4    Campbell, H.5    Deelder, A.M.6
  • 121
    • 33646070900 scopus 로고    scopus 로고
    • Modulation of therapeutic antibody effector functions by glycosylation engineering: influence of Golgi enzyme localization domain and co-expression of heterologous beta1, 4-N-acetylglucosaminyltransferase III and Golgi alpha-mannosidase II
    • Ferrara C, Brunker P, Suter T, Moser S, Puntener U, Umana P. Modulation of therapeutic antibody effector functions by glycosylation engineering: influence of Golgi enzyme localization domain and co-expression of heterologous beta1, 4-N-acetylglucosaminyltransferase III and Golgi alpha-mannosidase II. Biotechnol Bioeng (2006) 93(5):851-61. doi:10.1002/bit.20777
    • (2006) Biotechnol Bioeng , vol.93 , Issue.5 , pp. 851-861
    • Ferrara, C.1    Brunker, P.2    Suter, T.3    Moser, S.4    Puntener, U.5    Umana, P.6
  • 122
    • 84902550854 scopus 로고    scopus 로고
    • IgG-effector functions: "the good, the bad and the ugly"
    • Kapur R, Einarsdottir HK, Vidarsson G. IgG-effector functions: "the good, the bad and the ugly". Immunol Lett (2014) 160(2):139-44. doi:10.1016/j.imlet.2014.01.015
    • (2014) Immunol Lett , vol.160 , Issue.2 , pp. 139-144
    • Kapur, R.1    Einarsdottir, H.K.2    Vidarsson, G.3
  • 123
    • 84885204309 scopus 로고    scopus 로고
    • Association between galactosylation of immunoglobulin G and improvement of rheumatoid arthritis during pregnancy is independent of sialylation
    • Bondt A, Selman MH, Deelder AM, Hazes JM, Willemsen SP, Wuhrer M, et al. Association between galactosylation of immunoglobulin G and improvement of rheumatoid arthritis during pregnancy is independent of sialylation. J Proteome Res (2013) 12(10):4522-31. doi:10.1021/pr400589m
    • (2013) J Proteome Res , vol.12 , Issue.10 , pp. 4522-4531
    • Bondt, A.1    Selman, M.H.2    Deelder, A.M.3    Hazes, J.M.4    Willemsen, S.P.5    Wuhrer, M.6
  • 124
    • 84906217310 scopus 로고    scopus 로고
    • Structural characterization of anti-inflammatory immunoglobulin g fc proteins
    • Ahmed AA, Giddens J, Pincetic A, Lomino JV, Ravetch JV, Wang LX, et al. Structural characterization of anti-inflammatory immunoglobulin g fc proteins. J Mol Biol (2014) 426(18):3166-79. doi:10.1016/j.jmb.2014.07.006
    • (2014) J Mol Biol , vol.426 , Issue.18 , pp. 3166-3179
    • Ahmed, A.A.1    Giddens, J.2    Pincetic, A.3    Lomino, J.V.4    Ravetch, J.V.5    Wang, L.X.6
  • 125
    • 33746888249 scopus 로고    scopus 로고
    • Anti-inflammatory activity of immunoglobulin G resulting frosialylation
    • Kaneko Y, Nimmerjahn F, Ravetch JV. Anti-inflammatory activity of immunoglobulin G resulting frosialylation. Science (2006) 313(5787):670-3. doi:10.1126/science.1129594
    • (2006) Science , vol.313 , Issue.5787 , pp. 670-673
    • Kaneko, Y.1    Nimmerjahn, F.2    Ravetch, J.V.3
  • 126
    • 42349085035 scopus 로고    scopus 로고
    • Recapitulation of IVIG anti-inflammatory activity with a recombinant IgG Fc
    • Anthony RM, Nimmerjahn F, Ashline DJ, Reinhold VN, Paulson JC, Ravetch JV. Recapitulation of IVIG anti-inflammatory activity with a recombinant IgG Fc. Science (2008) 320(5874):373-6. doi:10.1126/science.1154315
    • (2008) Science , vol.320 , Issue.5874 , pp. 373-376
    • Anthony, R.M.1    Nimmerjahn, F.2    Ashline, D.J.3    Reinhold, V.N.4    Paulson, J.C.5    Ravetch, J.V.6
  • 127
    • 79151475628 scopus 로고    scopus 로고
    • The complement system
    • Sarma JV, Ward PA. The complement system. Cell Tissue Res (2011) 343(1):227-35. doi:10.1007/s00441-010-1034-0
    • (2011) Cell Tissue Res , vol.343 , Issue.1 , pp. 227-235
    • Sarma, J.V.1    Ward, P.A.2
  • 128
    • 0023765625 scopus 로고
    • Human monoclonal IgG isotypes differ in complement activating function at the level of C4 as well as C1q
    • Bindon CI, Hale G, Bruggemann M, Waldmann H. Human monoclonal IgG isotypes differ in complement activating function at the level of C4 as well as C1q. J Exp Med (1988) 168(1):127-42. doi:10.1084/jem.168.1.127
    • (1988) J Exp Med , vol.168 , Issue.1 , pp. 127-142
    • Bindon, C.I.1    Hale, G.2    Bruggemann, M.3    Waldmann, H.4
  • 129
    • 0017102773 scopus 로고
    • Ultracentifuge studies of the binding of IgG of different subclasses to the Clq subunit of the first component of complement
    • Schumaker VN, Calcott MA, Spiegelberg HL, Muller-Eberhard HJ. Ultracentifuge studies of the binding of IgG of different subclasses to the Clq subunit of the first component of complement. Biochemistry (1976) 15(23):5175-81. doi:10.1021/bi00668a035
    • (1976) Biochemistry , vol.15 , Issue.23 , pp. 5175-5181
    • Schumaker, V.N.1    Calcott, M.A.2    Spiegelberg, H.L.3    Muller-Eberhard, H.J.4
  • 130
    • 0027213573 scopus 로고
    • Structural features of human immunoglobulin G that determine isotype-specific differences in complement activation
    • Tao MH, Smith RI, Morrison SL. Structural features of human immunoglobulin G that determine isotype-specific differences in complement activation. J Exp Med (1993) 178(2):661-7. doi:10.1084/jem.178.2.661
    • (1993) J Exp Med , vol.178 , Issue.2 , pp. 661-667
    • Tao, M.H.1    Smith, R.I.2    Morrison, S.L.3
  • 131
    • 0034655265 scopus 로고    scopus 로고
    • Mapping of the C1q binding site on rituxan, a chimeric antibody with a human IgG1 Fc
    • Idusogie EE, Presta LG, Gazzano-Santoro H, Totpal K, Wong PY, Ultsch M, et al. Mapping of the C1q binding site on rituxan, a chimeric antibody with a human IgG1 Fc. J Immunol (2000) 164(8):4178-84. doi:10.4049/jimmunol.164.8.4178
    • (2000) J Immunol , vol.164 , Issue.8 , pp. 4178-4184
    • Idusogie, E.E.1    Presta, L.G.2    Gazzano-Santoro, H.3    Totpal, K.4    Wong, P.Y.5    Ultsch, M.6
  • 132
    • 0028970836 scopus 로고
    • The N-terminal end of the CH2 domain of chimeric human IgG1 anti-HLA-DR is necessary for C1q, Fc gamma RI and Fc gamma RIII binding
    • Morgan A, Jones ND, Nesbitt AM, Chaplin L, Bodmer MW, Emtage JS. The N-terminal end of the CH2 domain of chimeric human IgG1 anti-HLA-DR is necessary for C1q, Fc gamma RI and Fc gamma RIII binding. Immunology (1995) 86(2):319-24.
    • (1995) Immunology , vol.86 , Issue.2 , pp. 319-324
    • Morgan, A.1    Jones, N.D.2    Nesbitt, A.M.3    Chaplin, L.4    Bodmer, M.W.5    Emtage, J.S.6
  • 133
    • 0027933426 scopus 로고
    • Human IgG isotype-specific amino acid residues affecting complement-mediated cell lysis and phagocytosis
    • Brekke OH, Michaelsen TE, Aase A, Sandin RH, Sandlie I. Human IgG isotype-specific amino acid residues affecting complement-mediated cell lysis and phagocytosis. Eur J Immunol (1994) 24(10):2542-7. doi:10.1002/eji.1830241042
    • (1994) Eur J Immunol , vol.24 , Issue.10 , pp. 2542-2547
    • Brekke, O.H.1    Michaelsen, T.E.2    Aase, A.3    Sandin, R.H.4    Sandlie, I.5
  • 134
    • 33745823893 scopus 로고    scopus 로고
    • Modulation of the effector functions of a human IgG1 through engineering of its hinge region
    • Dall'Acqua WF, Cook KE, Damschroder MM, Woods RM, Wu H. Modulation of the effector functions of a human IgG1 through engineering of its hinge region. J Immunol (2006) 177(2):1129-38. doi:10.4049/jimmunol.177.2.1129
    • (2006) J Immunol , vol.177 , Issue.2 , pp. 1129-1138
    • Dall'Acqua, W.F.1    Cook, K.E.2    Damschroder, M.M.3    Woods, R.M.4    Wu, H.5
  • 135
    • 3543069883 scopus 로고
    • Segmental flexibility and complement fixation of genetically engineered chimeric human, rabbit and mouse antibodies
    • Dangl JL, Wensel TG, Morrison SL, Stryer L, Herzenberg LA, Oi VT. Segmental flexibility and complement fixation of genetically engineered chimeric human, rabbit and mouse antibodies. EMBO J (1988) 7(7):1989-94.
    • (1988) EMBO J , vol.7 , Issue.7 , pp. 1989-1994
    • Dangl, J.L.1    Wensel, T.G.2    Morrison, S.L.3    Stryer, L.4    Herzenberg, L.A.5    Oi, V.T.6
  • 136
    • 36849050718 scopus 로고    scopus 로고
    • Solution conformation of wild-type and mutant IgG3 and IgG4 immunoglobulins using crystallohydrodynamics: possible implications for complement activation
    • Lu Y, Harding SE, Michaelsen TE, Longman E, Davis KG, Ortega A, et al. Solution conformation of wild-type and mutant IgG3 and IgG4 immunoglobulins using crystallohydrodynamics: possible implications for complement activation. Biophys J (2007) 93(11):3733-44. doi:10.1529/biophysj.107.108993
    • (2007) Biophys J , vol.93 , Issue.11 , pp. 3733-3744
    • Lu, Y.1    Harding, S.E.2    Michaelsen, T.E.3    Longman, E.4    Davis, K.G.5    Ortega, A.6
  • 137
    • 0025176807 scopus 로고
    • Influence of the hinge region on complement activation, C1q binding, and segmental flexibility in chimeric human immunoglobulins
    • Tan LK, Shopes RJ, Oi VT, Morrison SL. Influence of the hinge region on complement activation, C1q binding, and segmental flexibility in chimeric human immunoglobulins. Proc Natl Acad Sci U S A (1990) 87(1):162-6. doi:10.1073/pnas.87.1.162
    • (1990) Proc Natl Acad Sci U S A , vol.87 , Issue.1 , pp. 162-166
    • Tan, L.K.1    Shopes, R.J.2    Oi, V.T.3    Morrison, S.L.4
  • 138
    • 45549090117 scopus 로고    scopus 로고
    • Engineered antibodies of IgG1/IgG3 mixed isotype with enhanced cytotoxic activities
    • Natsume A, In M, Takamura H, Nakagawa T, Shimizu Y, Kitajima K, et al. Engineered antibodies of IgG1/IgG3 mixed isotype with enhanced cytotoxic activities. Cancer Res (2008) 68(10):3863-72. doi:10.1158/0008-5472.CAN-07-6297
    • (2008) Cancer Res , vol.68 , Issue.10 , pp. 3863-3872
    • Natsume, A.1    In, M.2    Takamura, H.3    Nakagawa, T.4    Shimizu, Y.5    Kitajima, K.6
  • 139
    • 0036161996 scopus 로고    scopus 로고
    • IgG4 breaking the rules
    • Aalberse RC, Schuurman J. IgG4 breaking the rules. Immunology (2002) 105(1):9-19. doi:10.1046/j.0019-2805.2001.01341.x
    • (2002) Immunology , vol.105 , Issue.1 , pp. 9-19
    • Aalberse, R.C.1    Schuurman, J.2
  • 140
    • 78649734726 scopus 로고    scopus 로고
    • Masking of the Fc region in human IgG4 by constrained X-ray scattering modelling: implications for antibody function and therapy 1
    • Abe Y, Gor J, Bracewell DG, Perkins SJ, Dalby PA. Masking of the Fc region in human IgG4 by constrained X-ray scattering modelling: implications for antibody function and therapy 1. Biochem J (2010) 432(1):101-11. doi:10.1042/BJ20100641
    • (2010) Biochem J , vol.432 , Issue.1 , pp. 101-111
    • Abe, Y.1    Gor, J.2    Bracewell, D.G.3    Perkins, S.J.4    Dalby, P.A.5
  • 142
    • 0038619043 scopus 로고    scopus 로고
    • Central role of complement in passive protection by human IgG1 and IgG2 anti-pneumococcal antibodies in mice
    • Saeland E, Vidarsson G, Leusen JH, Van Garderen E, Nahm MH, Vile-Weekhout H, et al. Central role of complement in passive protection by human IgG1 and IgG2 anti-pneumococcal antibodies in mice. J Immunol (2003) 170(12):6158-64. doi:10.4049/jimmunol.170.12.6158
    • (2003) J Immunol , vol.170 , Issue.12 , pp. 6158-6164
    • Saeland, E.1    Vidarsson, G.2    Leusen, J.H.3    Van Garderen, E.4    Nahm, M.H.5    Vile-Weekhout, H.6
  • 143
    • 0027930273 scopus 로고
    • Opsonization and antibodies to capsular and cell wall polysaccharides of Streptococcus pneumoniae
    • Vidarsson G, Jonsdottir I, Jonsson S, Valdimarsson H. Opsonization and antibodies to capsular and cell wall polysaccharides of Streptococcus pneumoniae. J Infect Dis (1994) 170:592-9. doi:10.1093/infdis/170.3.592
    • (1994) J Infect Dis , vol.170 , pp. 592-599
    • Vidarsson, G.1    Jonsdottir, I.2    Jonsson, S.3    Valdimarsson, H.4
  • 144
    • 80053065703 scopus 로고    scopus 로고
    • Structural basis for Fc gammaRIIa recognition of human IgG and formation of inflammatory signaling complexes
    • Ramsland PA, Farrugia W, Bradford TM, Sardjono CT, Esparon S, Trist HM, et al. Structural basis for Fc gammaRIIa recognition of human IgG and formation of inflammatory signaling complexes. J Immunol (2011) 187(6):3208-17. doi:10.4049/jimmunol.1101467
    • (2011) J Immunol , vol.187 , Issue.6 , pp. 3208-3217
    • Ramsland, P.A.1    Farrugia, W.2    Bradford, T.M.3    Sardjono, C.T.4    Esparon, S.5    Trist, H.M.6
  • 145
    • 84893657950 scopus 로고    scopus 로고
    • The function of Fc receptors in dendritic cells and macrophages
    • Guilliams M, Bruhns P, Saeys Y, Hammad H, Lambrecht BN. The function of Fc receptors in dendritic cells and macrophages. Nat Rev Immunol (2014) 14(2):94-108. doi:10.1038/nri3582
    • (2014) Nat Rev Immunol , vol.14 , Issue.2 , pp. 94-108
    • Guilliams, M.1    Bruhns, P.2    Saeys, Y.3    Hammad, H.4    Lambrecht, B.N.5
  • 146
    • 0026650462 scopus 로고
    • Three genes for the human high affinity Fc receptor for IgG (Fc gamma RI) encode four distinct transcription products
    • Ernst LK, van de Winkel JG, Chiu IM, Anderson CL. Three genes for the human high affinity Fc receptor for IgG (Fc gamma RI) encode four distinct transcription products. J Biol Chem (1992) 267(22):15692-700.
    • (1992) J Biol Chem , vol.267 , Issue.22 , pp. 15692-15700
    • Ernst, L.K.1    van de Winkel, J.G.2    Chiu, I.M.3    Anderson, C.L.4
  • 147
    • 0031646641 scopus 로고    scopus 로고
    • Molecular characterization of six variant Fcgamma receptor class I (CD64) transcripts.
    • Ernst LK, Duchemin AM, Miller KL, Anderson CL. Molecular characterization of six variant Fcgamma receptor class I (CD64) transcripts. Mol Immunol (1998) 35(14-15):943-54. doi:10.1016/S0161-5890(98)00079-0
    • (1998) Mol Immunol , vol.35 , Issue.14-15 , pp. 943-954
    • Ernst, L.K.1    Duchemin, A.M.2    Miller, K.L.3    Anderson, C.L.4
  • 148
    • 0031674586 scopus 로고    scopus 로고
    • The second and third extracellular domains of FcgammaRI (CD64) confer the unique high affinity binding of IgG2a.
    • Hulett MD, Hogarth PM. The second and third extracellular domains of FcgammaRI (CD64) confer the unique high affinity binding of IgG2a. Mol Immunol (1998) 35(14-15):989-96. doi:10.1016/S0161-5890(98)00069-8
    • (1998) Mol Immunol , vol.35 , Issue.14-15 , pp. 989-996
    • Hulett, M.D.1    Hogarth, P.M.2
  • 149
    • 0025762394 scopus 로고
    • The binding affinity of human IgG for its high affinity Fc receptor is determined by multiple amino acids in the CH2 domain and is modulated by the hinge region
    • Canfield SM, Morrison SL. The binding affinity of human IgG for its high affinity Fc receptor is determined by multiple amino acids in the CH2 domain and is modulated by the hinge region. J Exp Med (1991) 173(6):1483-91. doi:10.1084/jem.173.6.1483
    • (1991) J Exp Med , vol.173 , Issue.6 , pp. 1483-1491
    • Canfield, S.M.1    Morrison, S.L.2
  • 150
    • 0025943212 scopus 로고
    • Identification of the Fc gamma receptor class I binding site in human IgG through the use of recombinant IgG1/IgG2 hybrid and point-mutated antibodies
    • Chappel MS, Isenman DE, Everett M, Xu YY, Dorrington KJ, Klein MH. Identification of the Fc gamma receptor class I binding site in human IgG through the use of recombinant IgG1/IgG2 hybrid and point-mutated antibodies. Proc Natl Acad Sci U S A (1991) 88(20):9036-40. doi:10.1073/pnas.88.20.9036
    • (1991) Proc Natl Acad Sci U S A , vol.88 , Issue.20 , pp. 9036-9040
    • Chappel, M.S.1    Isenman, D.E.2    Everett, M.3    Xu, Y.Y.4    Dorrington, K.J.5    Klein, M.H.6
  • 151
    • 0035794194 scopus 로고    scopus 로고
    • High resolution mapping of the binding site on human IgG1 for Fc gamma RI, Fc gamma RII, Fc gamma RIII, and FcRn and design of IgG1 variants with improved binding to the Fc gamma R
    • Shields RL, Namenuk AK, Hong K, Meng YG, Rae J, Briggs J, et al. High resolution mapping of the binding site on human IgG1 for Fc gamma RI, Fc gamma RII, Fc gamma RIII, and FcRn and design of IgG1 variants with improved binding to the Fc gamma R. J Biol Chem (2001) 276(9):6591-604. doi:10.1074/jbc.M009483200
    • (2001) J Biol Chem , vol.276 , Issue.9 , pp. 6591-6604
    • Shields, R.L.1    Namenuk, A.K.2    Hong, K.3    Meng, Y.G.4    Rae, J.5    Briggs, J.6
  • 152
    • 0026050344 scopus 로고
    • Human Fc gamma RI and Fc gamma RII interact with distinct but overlapping sites on human IgG
    • Lund J, Winter G, Jones PT, Pound JD, Tanaka T, Walker MR, et al. Human Fc gamma RI and Fc gamma RII interact with distinct but overlapping sites on human IgG. J Immunol (1991) 147(8):2657-62.
    • (1991) J Immunol , vol.147 , Issue.8 , pp. 2657-2662
    • Lund, J.1    Winter, G.2    Jones, P.T.3    Pound, J.D.4    Tanaka, T.5    Walker, M.R.6
  • 153
    • 0032810008 scopus 로고    scopus 로고
    • Recombinant human IgG molecules lacking Fcgamma receptor I binding and monocyte triggering activities
    • <2613::AID-IMMU2613>3.0.CO;2-J
    • Armour KL, Clark MR, Hadley AG, Williamson LM. Recombinant human IgG molecules lacking Fcgamma receptor I binding and monocyte triggering activities. Eur J Immunol (1999) 29(8):2613-24. doi:10.1002/(SICI)1521-4141(199908)29:08<2613::AID-IMMU2613>3.0.CO;2-J
    • (1999) Eur J Immunol , vol.29 , Issue.8 , pp. 2613-2624
    • Armour, K.L.1    Clark, M.R.2    Hadley, A.G.3    Williamson, L.M.4
  • 154
    • 0031688616 scopus 로고    scopus 로고
    • The influence of the hinge region length in binding of human IgG to human Fcgamma receptors
    • Redpath S, Michaelsen TE, Sandlie I, Clark MR. The influence of the hinge region length in binding of human IgG to human Fcgamma receptors. Hum Immunol (1998) 59(11):720-7. doi:10.1016/S0198-8859(98)00075-5
    • (1998) Hum Immunol , vol.59 , Issue.11 , pp. 720-727
    • Redpath, S.1    Michaelsen, T.E.2    Sandlie, I.3    Clark, M.R.4
  • 155
    • 0026492077 scopus 로고
    • On the interaction of IgG subclasses with the low affinity Fc gamma RIIa (CD32) on human monocytes, neutrophils, and platelets Analysis of a functional polymorphism to human IgG2
    • Parren PW, Warmerdam PA, Boeije LC, Arts J, Westerdaal NA, Vlug A, et al. On the interaction of IgG subclasses with the low affinity Fc gamma RIIa (CD32) on human monocytes, neutrophils, and platelets. Analysis of a functional polymorphism to human IgG2. J Clin Invest (1992) 90(4):1537-46. doi:10.1172/JCI116022
    • (1992) J Clin Invest , vol.90 , Issue.4 , pp. 1537-1546
    • Parren, P.W.1    Warmerdam, P.A.2    Boeije, L.C.3    Arts, J.4    Westerdaal, N.A.5    Vlug, A.6
  • 156
    • 0142226958 scopus 로고    scopus 로고
    • Differential binding to human FcgammaRIIa and FcgammaRIIb receptors by human IgG wildtype and mutant antibodies
    • Armour KL, van de Winkel JG, Williamson LM, Clark MR. Differential binding to human FcgammaRIIa and FcgammaRIIb receptors by human IgG wildtype and mutant antibodies. Mol Immunol (2003) 40(9):585-93. doi:10.1016/j.molimm.2003.08.004
    • (2003) Mol Immunol , vol.40 , Issue.9 , pp. 585-593
    • Armour, K.L.1    van de Winkel, J.G.2    Williamson, L.M.3    Clark, M.R.4
  • 157
    • 0034657794 scopus 로고    scopus 로고
    • The IgG Fc contains distinct Fc receptor (FcR) binding sites: the leukocyte receptors Fc gamma RI and Fc gamma RIIa bind to a region in the Fc distinct from that recognized by neonatal FcR and protein A
    • Wines BD, Powell MS, Parren PW, Barnes N, Hogarth PM. The IgG Fc contains distinct Fc receptor (FcR) binding sites: the leukocyte receptors Fc gamma RI and Fc gamma RIIa bind to a region in the Fc distinct from that recognized by neonatal FcR and protein A. J Immunol (2000) 164(10):5313-8. doi:10.4049/jimmunol.164.10.5313
    • (2000) J Immunol , vol.164 , Issue.10 , pp. 5313-5318
    • Wines, B.D.1    Powell, M.S.2    Parren, P.W.3    Barnes, N.4    Hogarth, P.M.5
  • 159
    • 38949142316 scopus 로고    scopus 로고
    • Copy number variation of the activating FCGR2C gene predisposes to idiopathic thrombocytopenic purpura
    • Breunis WB, van Mirre E, Bruin M, Geissler J, de BM, Peters M, et al. Copy number variation of the activating FCGR2C gene predisposes to idiopathic thrombocytopenic purpura. Blood (2008) 111(3):1029-38. doi:10.1182/blood-2007-03-079913
    • (2008) Blood , vol.111 , Issue.3 , pp. 1029-1038
    • Breunis, W.B.1    van Mirre, E.2    Bruin, M.3    Geissler, J.4    de, B.M.5    Peters, M.6
  • 160
    • 32344449790 scopus 로고    scopus 로고
    • Optimization of humanized IgGs in glycoengineered Pichia pastoris
    • Li H, Sethuraman N, Stadheim TA, Zha D, Prinz B, Ballew N, et al. Optimization of humanized IgGs in glycoengineered Pichia pastoris. Nat Biotechnol (2006) 24(2):210-5. doi:10.1038/nbt1178
    • (2006) Nat Biotechnol , vol.24 , Issue.2 , pp. 210-215
    • Li, H.1    Sethuraman, N.2    Stadheim, T.A.3    Zha, D.4    Prinz, B.5    Ballew, N.6
  • 161
    • 32044447251 scopus 로고    scopus 로고
    • Selection of a human anti-RhD monoclonal antibody for therapeutic use: impact of IgG glycosylation on activating and inhibitory Fc gamma R functions.
    • Siberil S, de Romeuf C, Bihoreau N, Fernandez N, Meterreau JL, Regenman A, et al. Selection of a human anti-RhD monoclonal antibody for therapeutic use: impact of IgG glycosylation on activating and inhibitory Fc gamma R functions. Clin Immunol (2006) 118(2-3):170-9. doi:10.1016/j.clim.2005.10.008
    • (2006) Clin Immunol , vol.118 , Issue.2-3 , pp. 170-179
    • Siberil, S.1    de Romeuf, C.2    Bihoreau, N.3    Fernandez, N.4    Meterreau, J.L.5    Regenman, A.6
  • 162
    • 0025058350 scopus 로고
    • Biallelic neutrophil Na-antigen system is associated with a polymorphism on the phospho-inositol-linked Fc gamma receptor III (CD16)
    • Huizinga TW, Kleijer M, Tetteroo PA, Roos D, von dem Borne AE. Biallelic neutrophil Na-antigen system is associated with a polymorphism on the phospho-inositol-linked Fc gamma receptor III (CD16). Blood (1990) 75(1):213-7.
    • (1990) Blood , vol.75 , Issue.1 , pp. 213-217
    • Huizinga, T.W.1    Kleijer, M.2    Tetteroo, P.A.3    Roos, D.4    von dem Borne, A.E.5
  • 163
    • 0024521291 scopus 로고
    • Binding characteristics of dimeric IgG subclass complexes to human neutrophils
    • Huizinga TW, Kerst M, Nuyens JH, Vlug A, von dem Borne AE, Roos D, et al. Binding characteristics of dimeric IgG subclass complexes to human neutrophils. J Immunol (1989) 142(7):2359-64.
    • (1989) J Immunol , vol.142 , Issue.7 , pp. 2359-2364
    • Huizinga, T.W.1    Kerst, M.2    Nuyens, J.H.3    Vlug, A.4    von dem Borne, A.E.5    Roos, D.6
  • 164
    • 0000146003 scopus 로고
    • A theoretical model of gamma-globulin catabolism
    • Brambell FW, Hemmings WA, Morris IG. A theoretical model of gamma-globulin catabolism. Nature (1964) 203:1352-4. doi:10.1038/2031352a0
    • (1964) Nature , vol.203 , pp. 1352-1354
    • Brambell, F.W.1    Hemmings, W.A.2    Morris, I.G.3
  • 165
    • 0014022299 scopus 로고
    • The transmission of immunity from mother to young and the catabolism of immunoglobulins
    • Brambell FW. The transmission of immunity from mother to young and the catabolism of immunoglobulins. Lancet (1966) 2(7473):1087-93. doi:10.1016/S0140-6736(66)92190-8
    • (1966) Lancet , vol.2 , Issue.7473 , pp. 1087-1093
    • Brambell, F.W.1
  • 166
    • 0029927482 scopus 로고    scopus 로고
    • Abnormally short serum half-lives of IgG in beta 2-microglobulin-deficient mice
    • Ghetie V, Hubbard JG, Kim JK, Tsen MF, Lee Y, Ward ES. Abnormally short serum half-lives of IgG in beta 2-microglobulin-deficient mice. Eur J Immunol (1996) 26(3):690-6. doi:10.1002/eji.1830260327
    • (1996) Eur J Immunol , vol.26 , Issue.3 , pp. 690-696
    • Ghetie, V.1    Hubbard, J.G.2    Kim, J.K.3    Tsen, M.F.4    Lee, Y.5    Ward, E.S.6
  • 167
    • 0029856774 scopus 로고    scopus 로고
    • Increased clearance of IgG in mice that lack beta 2-microglobulin: possible protective role of FcRn
    • Israel EJ, Wilsker DF, Hayes KC, Schoenfeld D, Simister NE. Increased clearance of IgG in mice that lack beta 2-microglobulin: possible protective role of FcRn. Immunology (1996) 89(4):573-8. doi:10.1046/j.1365-2567.1996.d01-775.x
    • (1996) Immunology , vol.89 , Issue.4 , pp. 573-578
    • Israel, E.J.1    Wilsker, D.F.2    Hayes, K.C.3    Schoenfeld, D.4    Simister, N.E.5
  • 168
    • 0029891262 scopus 로고    scopus 로고
    • The protection receptor for IgG catabolism is the beta2-microglobulin-containing neonatal intestinal transport receptor
    • Junghans RP, Anderson CL. The protection receptor for IgG catabolism is the beta2-microglobulin-containing neonatal intestinal transport receptor. Proc Natl Acad Sci U S A (1996) 93(11):5512-6. doi:10.1073/pnas.93.11.5512
    • (1996) Proc Natl Acad Sci U S A , vol.93 , Issue.11 , pp. 5512-5516
    • Junghans, R.P.1    Anderson, C.L.2
  • 169
    • 0037379288 scopus 로고    scopus 로고
    • The MHC class I-like IgG receptor controls perinatal IgG transport, IgG homeostasis, and fate of IgG-Fc-coupled drugs
    • Roopenian DC, Christianson GJ, Sproule TJ, Brown AC, Akilesh S, Jung N, et al. The MHC class I-like IgG receptor controls perinatal IgG transport, IgG homeostasis, and fate of IgG-Fc-coupled drugs. J Immunol (2003) 170(7):3528-33. doi:10.4049/jimmunol.170.7.3528
    • (2003) J Immunol , vol.170 , Issue.7 , pp. 3528-3533
    • Roopenian, D.C.1    Christianson, G.J.2    Sproule, T.J.3    Brown, A.C.4    Akilesh, S.5    Jung, N.6
  • 170
    • 0037415556 scopus 로고    scopus 로고
    • The major histocompatibility complex-related Fc receptor for IgG (FcRn) binds albumin and prolongs its lifespan
    • Chaudhury C, Mehnaz S, Robinson JM, Hayton WL, Pearl DK, Roopenian DC, et al. The major histocompatibility complex-related Fc receptor for IgG (FcRn) binds albumin and prolongs its lifespan. J Biol Chem (2003) 197(3):315-22. doi:10.1084/jem.20021829
    • (2003) J Biol Chem , vol.197 , Issue.3 , pp. 315-322
    • Chaudhury, C.1    Mehnaz, S.2    Robinson, J.M.3    Hayton, W.L.4    Pearl, D.K.5    Roopenian, D.C.6
  • 171
    • 0026569633 scopus 로고
    • Expression and crystallization of a soluble and functional form of an Fc receptor related to class I histocompatibility molecules
    • Gastinel LN, Simister NE, Bjorkman PJ. Expression and crystallization of a soluble and functional form of an Fc receptor related to class I histocompatibility molecules. Proc Natl Acad Sci U S A (1992) 89(2):638-42. doi:10.1073/pnas.89.2.638
    • (1992) Proc Natl Acad Sci U S A , vol.89 , Issue.2 , pp. 638-642
    • Gastinel, L.N.1    Simister, N.E.2    Bjorkman, P.J.3
  • 172
    • 84896051838 scopus 로고    scopus 로고
    • H435-containing immunoglobulin G3 allotypes are transported efficiently across the human placenta: implications for alloantibody-mediated diseases of the newborn
    • Einarsdottir H, Ji Y, Visser R, Mo C, Luo G, Scherjon S, et al. H435-containing immunoglobulin G3 allotypes are transported efficiently across the human placenta: implications for alloantibody-mediated diseases of the newborn. Transfusion (2014) 54(3):665-71. doi:10.1111/trf.12334
    • (2014) Transfusion , vol.54 , Issue.3 , pp. 665-671
    • Einarsdottir, H.1    Ji, Y.2    Visser, R.3    Mo, C.4    Luo, G.5    Scherjon, S.6
  • 173
    • 33745508741 scopus 로고    scopus 로고
    • Perspective - FcRn transports albumin: relevance to immunology and medicine
    • Anderson CL, Chaudhury C, Kim J, Bronson CL, Wani MA, Mohanty S. Perspective - FcRn transports albumin: relevance to immunology and medicine. Trends Immunol (2006) 27(7):343-8. doi:10.1016/j.it.2006.05.004
    • (2006) Trends Immunol , vol.27 , Issue.7 , pp. 343-348
    • Anderson, C.L.1    Chaudhury, C.2    Kim, J.3    Bronson, C.L.4    Wani, M.A.5    Mohanty, S.6
  • 174
    • 0031685365 scopus 로고    scopus 로고
    • Functional expression of the MHC class I-related receptor, FcRn, in endothelial cells of mice
    • Borvak J, Richardson J, Medesan C, Antohe F, Radu C, Simionescu M, et al. Functional expression of the MHC class I-related receptor, FcRn, in endothelial cells of mice. Int Immunol (1998) 10(9):1289-98. doi:10.1093/intimm/10.9.1289
    • (1998) Int Immunol , vol.10 , Issue.9 , pp. 1289-1298
    • Borvak, J.1    Richardson, J.2    Medesan, C.3    Antohe, F.4    Radu, C.5    Simionescu, M.6
  • 175
    • 39549088649 scopus 로고    scopus 로고
    • Neonatal FcR expression in bone marrow-derived cells functions to protect serum IgG from catabolism
    • Akilesh S, Christianson GJ, Roopenian DC, Shaw AS. Neonatal FcR expression in bone marrow-derived cells functions to protect serum IgG from catabolism. J Immunol (2007) 179(7):4580-8. doi:10.4049/jimmunol.179.7.4580
    • (2007) J Immunol , vol.179 , Issue.7 , pp. 4580-4588
    • Akilesh, S.1    Christianson, G.J.2    Roopenian, D.C.3    Shaw, A.S.4
  • 176
    • 80052579373 scopus 로고    scopus 로고
    • Recent advances using FcRn overexpression in transgenic animals to overcome impediments of standard antibody technologies to improve the generation of specific antibodies
    • Kacskovics I, Cervenak J, Erdei A, Goldsby RA, Butler JE. Recent advances using FcRn overexpression in transgenic animals to overcome impediments of standard antibody technologies to improve the generation of specific antibodies. MAbs (2011) 3(5):431-9. doi:10.4161/mabs.3.5.17023
    • (2011) MAbs , vol.3 , Issue.5 , pp. 431-439
    • Kacskovics, I.1    Cervenak, J.2    Erdei, A.3    Goldsby, R.A.4    Butler, J.E.5
  • 177
    • 2942516894 scopus 로고    scopus 로고
    • Human neonatal Fc receptor mediates transport of IgG into luminal secretions for delivery of antigens to mucosal dendritic cells
    • Yoshida M, Claypool SM, Wagner JS, Mizoguchi E, Mizoguchi A, Roopenian DC, et al. Human neonatal Fc receptor mediates transport of IgG into luminal secretions for delivery of antigens to mucosal dendritic cells. Immunity (2004) 20(6):769-83. doi:10.1016/j.immuni.2004.05.007
    • (2004) Immunity , vol.20 , Issue.6 , pp. 769-783
    • Yoshida, M.1    Claypool, S.M.2    Wagner, J.S.3    Mizoguchi, E.4    Mizoguchi, A.5    Roopenian, D.C.6
  • 178
    • 0028980061 scopus 로고
    • Requirement for a beta 2-microglobulin-associated Fc receptor for acquisition of maternal IgG by fetal and neonatal mice
    • Israel EJ, Patel VK, Taylor SF, Marshak-Rothstein A, Simister NE. Requirement for a beta 2-microglobulin-associated Fc receptor for acquisition of maternal IgG by fetal and neonatal mice. J Immunol (1995) 154(12):6246-51.
    • (1995) J Immunol , vol.154 , Issue.12 , pp. 6246-6251
    • Israel, E.J.1    Patel, V.K.2    Taylor, S.F.3    Marshak-Rothstein, A.4    Simister, N.E.5
  • 179
    • 0030880901 scopus 로고    scopus 로고
    • Expression of the neonatal Fc receptor, FcRn, on human intestinal epithelial cells
    • Israel EJ, Taylor S, Wu Z, Mizoguchi E, Blumberg RS, Bhan A, et al. Expression of the neonatal Fc receptor, FcRn, on human intestinal epithelial cells. Immunology (1997) 92(1):69-74. doi:10.1046/j.1365-2567.1997.00326.x
    • (1997) Immunology , vol.92 , Issue.1 , pp. 69-74
    • Israel, E.J.1    Taylor, S.2    Wu, Z.3    Mizoguchi, E.4    Blumberg, R.S.5    Bhan, A.6
  • 180
    • 84863524257 scopus 로고    scopus 로고
    • Electron tomography of late stages of FcRn-mediated antibody transcytosis in neonatal rat small intestine
    • Ladinsky MS, Huey-Tubman KE, Bjorkman PJ. Electron tomography of late stages of FcRn-mediated antibody transcytosis in neonatal rat small intestine. Mol Biol Cell (2012) 23(13):2537-45. doi:10.1091/mbc.E12-02-0093
    • (2012) Mol Biol Cell , vol.23 , Issue.13 , pp. 2537-2545
    • Ladinsky, M.S.1    Huey-Tubman, K.E.2    Bjorkman, P.J.3
  • 181
    • 0037025895 scopus 로고    scopus 로고
    • Receptor-mediated immunoglobulin G transport across mucosal barriers in adult life: functional expression of FcRn in the mammalian lung
    • Spiekermann GM, Finn PW, Ward ES, Dumont J, Dickinson BL, Blumberg RS, et al. Receptor-mediated immunoglobulin G transport across mucosal barriers in adult life: functional expression of FcRn in the mammalian lung. J Exp Med (2002) 196(3):303-10. doi:10.1084/jem.20020400
    • (2002) J Exp Med , vol.196 , Issue.3 , pp. 303-310
    • Spiekermann, G.M.1    Finn, P.W.2    Ward, E.S.3    Dumont, J.4    Dickinson, B.L.5    Blumberg, R.S.6
  • 182
    • 1642546286 scopus 로고    scopus 로고
    • Bidirectional transepithelial IgG transport by a strongly polarized basolateral membrane Fcgamma-receptor
    • Claypool SM, Dickinson BL, Wagner JS, Johansen FE, Venu N, Borawski JA, et al. Bidirectional transepithelial IgG transport by a strongly polarized basolateral membrane Fcgamma-receptor. Mol Biol Cell (2004) 15(4):1746-59. doi:10.1091/mbc.E03-11-0832
    • (2004) Mol Biol Cell , vol.15 , Issue.4 , pp. 1746-1759
    • Claypool, S.M.1    Dickinson, B.L.2    Wagner, J.S.3    Johansen, F.E.4    Venu, N.5    Borawski, J.A.6
  • 183
    • 0032741975 scopus 로고    scopus 로고
    • Bidirectional FcRn-dependent IgG transport in a polarized human intestinal epithelial cell line
    • Dickinson BL, Badizadegan K, Wu Z, Ahouse JC, Zhu X, Simister NE, et al. Bidirectional FcRn-dependent IgG transport in a polarized human intestinal epithelial cell line. J Clin Invest (1999) 104(7):903-11. doi:10.1172/JCI6968
    • (1999) J Clin Invest , vol.104 , Issue.7 , pp. 903-911
    • Dickinson, B.L.1    Badizadegan, K.2    Wu, Z.3    Ahouse, J.C.4    Zhu, X.5    Simister, N.E.6
  • 184
    • 0037317875 scopus 로고    scopus 로고
    • Distribution of the IgG Fc receptor, FcRn, in the human fetal intestine
    • Shah U, Dickinson BL, Blumberg RS, Simister NE, Lencer WI, Walker WA. Distribution of the IgG Fc receptor, FcRn, in the human fetal intestine. Pediatr Res (2003) 53(2):295-301. doi:10.1203/01.PDR.0000047663.81816.E3
    • (2003) Pediatr Res , vol.53 , Issue.2 , pp. 295-301
    • Shah, U.1    Dickinson, B.L.2    Blumberg, R.S.3    Simister, N.E.4    Lencer, W.I.5    Walker, W.A.6
  • 185
    • 80054729360 scopus 로고    scopus 로고
    • In vitro and in vivo methods for assessing FcRn-mediated reverse transcytosis across the blood-brain barrier
    • Caram-Salas N, Boileau E, Farrington GK, Garber E, Brunette E, Abulrob A, et al. In vitro and in vivo methods for assessing FcRn-mediated reverse transcytosis across the blood-brain barrier. Methods Mol Biol (2011) 763:383-401. doi:10.1007/978-1-61779-191-8_26
    • (2011) Methods Mol Biol , vol.763 , pp. 383-401
    • Caram-Salas, N.1    Boileau, E.2    Farrington, G.K.3    Garber, E.4    Brunette, E.5    Abulrob, A.6
  • 186
    • 0033960282 scopus 로고    scopus 로고
    • IgG surfaces as an important component in mucosal protection
    • Robert-Guroff M. IgG surfaces as an important component in mucosal protection. Nat Med (2000) 6(2):129-30. doi:10.1038/72206
    • (2000) Nat Med , vol.6 , Issue.2 , pp. 129-130
    • Robert-Guroff, M.1
  • 187
    • 33746684369 scopus 로고    scopus 로고
    • Neonatal Fc receptor for IgG regulates mucosal immune responses to luminal bacteria
    • Yoshida M, Kobayashi K, Kuo TT, Bry L, Glickman JN, Claypool SM, et al. Neonatal Fc receptor for IgG regulates mucosal immune responses to luminal bacteria. J Clin Invest (2006) 116(8):2142. doi:10.1172/JCI27821.2142
    • (2006) J Clin Invest , vol.116 , Issue.8 , pp. 2142
    • Yoshida, M.1    Kobayashi, K.2    Kuo, T.T.3    Bry, L.4    Glickman, J.N.5    Claypool, S.M.6
  • 188
    • 84883659521 scopus 로고    scopus 로고
    • Antibodies and their receptors: different potential roles in mucosal defense
    • Horton RE, Vidarsson G. Antibodies and their receptors: different potential roles in mucosal defense. Front Immunol (2013) 4:200. doi:10.3389/fimmu.2013.00200
    • (2013) Front Immunol , vol.4 , pp. 200
    • Horton, R.E.1    Vidarsson, G.2
  • 189
    • 0035284906 scopus 로고    scopus 로고
    • MHC class I-related neonatal Fc receptor for IgG is functionally expressed in monocytes, intestinal macrophages, and dendritic cells
    • Zhu X, Meng G, Dickinson BL, Li X, Mizoguchi E, Miao L, et al. MHC class I-related neonatal Fc receptor for IgG is functionally expressed in monocytes, intestinal macrophages, and dendritic cells. J Immunol (2001) 166(5):3266-76. doi:10.4049/jimmunol.166.5.3266
    • (2001) J Immunol , vol.166 , Issue.5 , pp. 3266-3276
    • Zhu, X.1    Meng, G.2    Dickinson, B.L.3    Li, X.4    Mizoguchi, E.5    Miao, L.6
  • 190
    • 79251577108 scopus 로고    scopus 로고
    • Neonatal FcR overexpression boosts humoral immune response in transgenic mice
    • Cervenak J, Bender B, Schneider Z, Magna M, Carstea BV, Liliom K, et al. Neonatal FcR overexpression boosts humoral immune response in transgenic mice. J Immunol (2011) 186(2):959-68. doi:10.4049/jimmunol.1000353
    • (2011) J Immunol , vol.186 , Issue.2 , pp. 959-968
    • Cervenak, J.1    Bender, B.2    Schneider, Z.3    Magna, M.4    Carstea, B.V.5    Liliom, K.6
  • 191
  • 192
    • 79959946173 scopus 로고    scopus 로고
    • Neonatal Fc receptor for IgG (FcRn) regulates cross-presentation of IgG immune complexes by CD8-CD11b+ dendritic cells
    • Baker K, Qiao SW, Kuo TT, Aveson VG, Platzer B, Andersen JT, et al. Neonatal Fc receptor for IgG (FcRn) regulates cross-presentation of IgG immune complexes by CD8-CD11b+ dendritic cells. Proc Natl Acad Sci U S A (2011) 108(24):9927-32. doi:10.1073/pnas.1019037108
    • (2011) Proc Natl Acad Sci U S A , vol.108 , Issue.24 , pp. 9927-9932
    • Baker, K.1    Qiao, S.W.2    Kuo, T.T.3    Aveson, V.G.4    Platzer, B.5    Andersen, J.T.6
  • 193
    • 71849083999 scopus 로고    scopus 로고
    • Targeting the neonatal Fc receptor for antigen delivery using engineered Fc fragments
    • Mi W, Wanjie S, Lo ST, Gan Z, Pickl-Herk B, Ober RJ, et al. Targeting the neonatal Fc receptor for antigen delivery using engineered Fc fragments. J Immunol (2008) 181(11):7550. doi:10.4049/jimmunol.181.11.7550
    • (2008) J Immunol , vol.181 , Issue.11 , pp. 7550
    • Mi, W.1    Wanjie, S.2    Lo, S.T.3    Gan, Z.4    Pickl-Herk, B.5    Ober, R.J.6
  • 195
    • 13344259328 scopus 로고    scopus 로고
    • Antigen targeting to myeloid-specific human Fc gamma RI/CD64 triggers enhanced antibody responses in transgenic mice
    • Heijnen I, van Vugt MJ, Fanger N, Graziano RF, de Wit TP, Hofhuis FM, et al. Antigen targeting to myeloid-specific human Fc gamma RI/CD64 triggers enhanced antibody responses in transgenic mice. J Clin Invest (1996) 97(2):331-8. doi:10.1172/JCI118420
    • (1996) J Clin Invest , vol.97 , Issue.2 , pp. 331-338
    • Heijnen, I.1    van Vugt, M.J.2    Fanger, N.3    Graziano, R.F.4    de Wit, T.P.5    Hofhuis, F.M.6
  • 197
    • 34547455672 scopus 로고    scopus 로고
    • Fc receptor-like 5 inhibits B cell activation via SHP-1 tyrosine phosphatase recruitment
    • Haga CL, Ehrhardt GR, Boohaker RJ, Davis RS, Cooper MD. Fc receptor-like 5 inhibits B cell activation via SHP-1 tyrosine phosphatase recruitment. Proc Natl Acad Sci U S A (2007) 104(23):9770-5. doi:10.1073/pnas.0703354104
    • (2007) Proc Natl Acad Sci U S A , vol.104 , Issue.23 , pp. 9770-9775
    • Haga, C.L.1    Ehrhardt, G.R.2    Boohaker, R.J.3    Davis, R.S.4    Cooper, M.D.5
  • 198
    • 33748987876 scopus 로고    scopus 로고
    • Expression pattern of the human FcRH/IRTA receptors in normal tissue and in B-chronic lymphocytic leukemia
    • Polson AG, Zheng B, Elkins K, Chang W, Du C, Dowd P, et al. Expression pattern of the human FcRH/IRTA receptors in normal tissue and in B-chronic lymphocytic leukemia. Int Immunol (2006) 18(9):1363-73. doi:10.1093/intimm/dxl069
    • (2006) Int Immunol , vol.18 , Issue.9 , pp. 1363-1373
    • Polson, A.G.1    Zheng, B.2    Elkins, K.3    Chang, W.4    Du, C.5    Dowd, P.6
  • 199
    • 25144475070 scopus 로고    scopus 로고
    • Expression of the immunoregulatory molecule FcRH4 defines a distinctive tissue-based population of memory B cells
    • Ehrhardt GR, Hsu JT, Gartland L, Leu CM, Zhang S, Davis RS, et al. Expression of the immunoregulatory molecule FcRH4 defines a distinctive tissue-based population of memory B cells. J Exp Med (2005) 202(6):783-91. doi:10.1084/jem.20050879
    • (2005) J Exp Med , vol.202 , Issue.6 , pp. 783-791
    • Ehrhardt, G.R.1    Hsu, J.T.2    Gartland, L.3    Leu, C.M.4    Zhang, S.5    Davis, R.S.6
  • 200
    • 0027409214 scopus 로고
    • The mapping of the human 52-kD Ro/SSA autoantigen gene to human chromosome 11, and its polymorphisms
    • Frank MB, Itoh K, Fujisaku A, Pontarotti P, Mattei MG, Neas BR. The mapping of the human 52-kD Ro/SSA autoantigen gene to human chromosome 11, and its polymorphisms. Am J Hum Genet (1993) 52(1):183-91.
    • (1993) Am J Hum Genet , vol.52 , Issue.1 , pp. 183-191
    • Frank, M.B.1    Itoh, K.2    Fujisaku, A.3    Pontarotti, P.4    Mattei, M.G.5    Neas, B.R.6
  • 201
    • 0034523776 scopus 로고    scopus 로고
    • Autoantigen Ro52 directly interacts with human IgG heavy chain in vivo in mammalian cells
    • Yang YS, Yang MC, Wang B, Weissler JC. Autoantigen Ro52 directly interacts with human IgG heavy chain in vivo in mammalian cells. Mol Immunol (2000) 37(10):591-602. doi:10.1016/S0161-5890(00)00068-7
    • (2000) Mol Immunol , vol.37 , Issue.10 , pp. 591-602
    • Yang, Y.S.1    Yang, M.C.2    Wang, B.3    Weissler, J.C.4
  • 202
    • 33846220331 scopus 로고    scopus 로고
    • TRIM21 is a trimeric protein that binds IgG Fc via the B30.2 domain
    • Rhodes D, Trowsdale J. TRIM21 is a trimeric protein that binds IgG Fc via the B30.2 domain. Mol Immunol (2007) 44(9):2406-14. doi:10.1016/j.molimm.2006.10.013
    • (2007) Mol Immunol , vol.44 , Issue.9 , pp. 2406-2414
    • Rhodes, D.1    Trowsdale, J.2
  • 204
    • 84880361392 scopus 로고    scopus 로고
    • Simultaneous neutralization and innate immune detection of a replicating virus by TRIM21
    • Watkinson RE, Tam JC, Vaysburd MJ, James LC. Simultaneous neutralization and innate immune detection of a replicating virus by TRIM21. J Virol (2013) 87(13):7309-13. doi:10.1128/JVI.00647-13
    • (2013) J Virol , vol.87 , Issue.13 , pp. 7309-7313
    • Watkinson, R.E.1    Tam, J.C.2    Vaysburd, M.J.3    James, L.C.4
  • 206
    • 78650542340 scopus 로고    scopus 로고
    • Antibodies mediate intracellular immunity through tripartite motif-containing 21 (TRIM21)
    • Mallery DL, McEwan W, Bidgood SR, Towers GJ, Johnson CM, James LC. Antibodies mediate intracellular immunity through tripartite motif-containing 21 (TRIM21). Proc Natl Acad Sci U S A (2010) 107(46):19985-90. doi:10.1073/pnas.1014074107
    • (2010) Proc Natl Acad Sci U S A , vol.107 , Issue.46 , pp. 19985-19990
    • Mallery, D.L.1    McEwan, W.2    Bidgood, S.R.3    Towers, G.J.4    Johnson, C.M.5    James, L.C.6
  • 207
    • 80054687424 scopus 로고    scopus 로고
    • Intracellular antibody-mediated immunity and the role of TRIM21
    • McEwan W, Mallery DL, Rhodes D, Trowsdale J, James LC. Intracellular antibody-mediated immunity and the role of TRIM21. Bioessays (2011) 33(11):803-9. doi:10.1002/bies.201100093
    • (2011) Bioessays , vol.33 , Issue.11 , pp. 803-809
    • McEwan, W.1    Mallery, D.L.2    Rhodes, D.3    Trowsdale, J.4    James, L.C.5
  • 208
    • 84875458616 scopus 로고    scopus 로고
    • Intracellular antibody-bound pathogens stimulate immune signaling via the Fc receptor TRIM21
    • McEwan W, Tam JC, Watkinson RE, Bidgood SR, Mallery DL, James LC. Intracellular antibody-bound pathogens stimulate immune signaling via the Fc receptor TRIM21. Nat Immunol (2013) 14(4):327-36. doi:10.1038/ni.2548
    • (2013) Nat Immunol , vol.14 , Issue.4 , pp. 327-336
    • McEwan, W.1    Tam, J.C.2    Watkinson, R.E.3    Bidgood, S.R.4    Mallery, D.L.5    James, L.C.6
  • 209
    • 79960046406 scopus 로고    scopus 로고
    • Intravenous gammaglobulin suppresses inflammation through a novel T (H)2 pathway
    • Anthony RM, Kobayashi T, Wermeling F, Ravetch JV. Intravenous gammaglobulin suppresses inflammation through a novel T (H)2 pathway. Nature (2011) 475(7354):110-3. doi:10.1038/nature10134
    • (2011) Nature , vol.475 , Issue.7354 , pp. 110-113
    • Anthony, R.M.1    Kobayashi, T.2    Wermeling, F.3    Ravetch, J.V.4
  • 210
    • 58149378347 scopus 로고    scopus 로고
    • Identification of a receptor required for the anti-inflammatory activity of IVIG
    • Anthony RM, Wermeling F, Karlsson MC, Ravetch JV. Identification of a receptor required for the anti-inflammatory activity of IVIG. Proc Natl Acad Sci U S A (2008) 105(50):19571-8. doi:10.1073/pnas.0810163105
    • (2008) Proc Natl Acad Sci U S A , vol.105 , Issue.50 , pp. 19571-19578
    • Anthony, R.M.1    Wermeling, F.2    Karlsson, M.C.3    Ravetch, J.V.4
  • 211
    • 84896692591 scopus 로고    scopus 로고
    • Dendritic cell immunoreceptor: a novel receptor for intravenous immunoglobulin mediates induction of regulatory T cells
    • Massoud AH, Yona M, Xue D, Chouiali F, Alturaihi H, Ablona A, et al. Dendritic cell immunoreceptor: a novel receptor for intravenous immunoglobulin mediates induction of regulatory T cells. J Allergy Clin Immunol (2014) 133(3):853-63. doi:10.1016/j.jaci.2013.09.029
    • (2014) J Allergy Clin Immunol , vol.133 , Issue.3 , pp. 853-863
    • Massoud, A.H.1    Yona, M.2    Xue, D.3    Chouiali, F.4    Alturaihi, H.5    Ablona, A.6
  • 212
    • 84875749746 scopus 로고    scopus 로고
    • Dissecting the molecular mechanism of IVIg therapy: the interaction between serum IgG and DC-SIGN is independent of antibody glycoform or Fc domain
    • Yu X, Vasiljevic S, Mitchell D, Crispin M, Scanlan CN. Dissecting the molecular mechanism of IVIg therapy: the interaction between serum IgG and DC-SIGN is independent of antibody glycoform or Fc domain. J Mol Biol (2013) 425(8):1253-8. doi:10.1016/j.jmb.2013.02.006
    • (2013) J Mol Biol , vol.425 , Issue.8 , pp. 1253-1258
    • Yu, X.1    Vasiljevic, S.2    Mitchell, D.3    Crispin, M.4    Scanlan, C.N.5
  • 213
    • 33845483093 scopus 로고    scopus 로고
    • Immunologic and functional evidence for anti-Siglec-9 autoantibodies in intravenous immunoglobulin preparations
    • von Gunten S, Schaub A, Vogel M, Stadler BM, Miescher S, Simon HU. Immunologic and functional evidence for anti-Siglec-9 autoantibodies in intravenous immunoglobulin preparations. Blood (2006) 108(13):4255-9. doi:10.1182/blood-2006-05-021568
    • (2006) Blood , vol.108 , Issue.13 , pp. 4255-4259
    • von Gunten, S.1    Schaub, A.2    Vogel, M.3    Stadler, B.M.4    Miescher, S.5    Simon, H.U.6
  • 214
  • 215
    • 77956566546 scopus 로고    scopus 로고
    • IVIg modulates BCR signaling through CD22 and promotes apoptosis in mature human B lymphocytes
    • Seite JF, Cornec D, Renaudineau Y, Youinou P, Mageed RA, Hillion S. IVIg modulates BCR signaling through CD22 and promotes apoptosis in mature human B lymphocytes. Blood (2010) 116(10):1698-704. doi:10.1182/blood-2009-12-261461
    • (2010) Blood , vol.116 , Issue.10 , pp. 1698-1704
    • Seite, J.F.1    Cornec, D.2    Renaudineau, Y.3    Youinou, P.4    Mageed, R.A.5    Hillion, S.6
  • 216
    • 79959955221 scopus 로고    scopus 로고
    • Dimeric IVIG contains natural anti-Siglec-9 autoantibodies and their anti-idiotypes
    • Schaub A, von Gunten S, Vogel M, Wymann S, Ruegsegger M, Stadler BM, et al. Dimeric IVIG contains natural anti-Siglec-9 autoantibodies and their anti-idiotypes. Allergy (2011) 66(8):1030-7. doi:10.1111/j.1398-9995.2011.02579.x
    • (2011) Allergy , vol.66 , Issue.8 , pp. 1030-1037
    • Schaub, A.1    von Gunten, S.2    Vogel, M.3    Wymann, S.4    Ruegsegger, M.5    Stadler, B.M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.