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Volumn 35, Issue 9, 2011, Pages 982-990

Transduction of binding affinity by B lymphocytes: A new dimension in immunological regulation

Author keywords

Affinity; Disulfide; Glycosylation; Immunoglobulin; Teleost

Indexed keywords

B LYMPHOCYTE RECEPTOR; DISULFIDE; IMMUNOGLOBULIN M;

EID: 79959567244     PISSN: 0145305X     EISSN: 0145305X     Source Type: Journal    
DOI: 10.1016/j.dci.2011.01.015     Document Type: Review
Times cited : (18)

References (80)
  • 1
    • 0020491430 scopus 로고
    • Heterogeneity of asparagine-linked oligosaccharides of five glycosylation sites on immunoglobulin M heavy chain from mineral oil plasmacytoma 104E
    • Anderson D.R., Grimes W.J. Heterogeneity of asparagine-linked oligosaccharides of five glycosylation sites on immunoglobulin M heavy chain from mineral oil plasmacytoma 104E. J. Biol. Chem. 1982, 257:14858-14864.
    • (1982) J. Biol. Chem. , vol.257 , pp. 14858-14864
    • Anderson, D.R.1    Grimes, W.J.2
  • 3
    • 33747116052 scopus 로고    scopus 로고
    • Mannan binding lectin and its interaction with immunoglobulins in health and disease
    • Arnold J.N., Dwek R.A., Rudd P.M., Sim R.B. Mannan binding lectin and its interaction with immunoglobulins in health and disease. Immunol. Lett. 2006, 106:103-110.
    • (2006) Immunol. Lett. , vol.106 , pp. 103-110
    • Arnold, J.N.1    Dwek, R.A.2    Rudd, P.M.3    Sim, R.B.4
  • 4
    • 0029823905 scopus 로고    scopus 로고
    • Humoral immune response of flounder to Edwardsiella tarda: the presence of various sizes of immunoglobulins in flounder
    • Bang J.-D., Kim J.-W., Lee S.-D., Park S.-I., Chun S.-G., Jeong C.-S., Park J.-W. Humoral immune response of flounder to Edwardsiella tarda: the presence of various sizes of immunoglobulins in flounder. Dis. Aqua Org. 1996, 26:197-203.
    • (1996) Dis. Aqua Org. , vol.26 , pp. 197-203
    • Bang, J.-D.1    Kim, J.-W.2    Lee, S.-D.3    Park, S.-I.4    Chun, S.-G.5    Jeong, C.-S.6    Park, J.-W.7
  • 5
    • 0042620298 scopus 로고    scopus 로고
    • Membrane proteins with immunoglobulin-like domains-a master superfamily of interaction molecules
    • Barclay A.N. Membrane proteins with immunoglobulin-like domains-a master superfamily of interaction molecules. Semin. Immunol. 2003, 15:215-223.
    • (2003) Semin. Immunol. , vol.15 , pp. 215-223
    • Barclay, A.N.1
  • 7
    • 0032100706 scopus 로고    scopus 로고
    • Affinity dependence of the B cell response to antigen: a threshold, a ceiling, and the importance of off-rate
    • Batista F.D., Neuberger M.S. Affinity dependence of the B cell response to antigen: a threshold, a ceiling, and the importance of off-rate. Immunity 1998, 8:751-759.
    • (1998) Immunity , vol.8 , pp. 751-759
    • Batista, F.D.1    Neuberger, M.S.2
  • 8
    • 0017088202 scopus 로고
    • Effect of glycosylation on the in vivo circulating half-life of ribonuclease
    • Baynes J.W., Wold F. Effect of glycosylation on the in vivo circulating half-life of ribonuclease. J. Biol. Chem. 1976, 251:6016-6024.
    • (1976) J. Biol. Chem. , vol.251 , pp. 6016-6024
    • Baynes, J.W.1    Wold, F.2
  • 10
    • 0034936968 scopus 로고    scopus 로고
    • Role of natural and immune IgM antibodies in immune responses
    • Boes M. Role of natural and immune IgM antibodies in immune responses. Mol. Immunol. 2000, 37:1141-1149.
    • (2000) Mol. Immunol. , vol.37 , pp. 1141-1149
    • Boes, M.1
  • 11
    • 23344453236 scopus 로고    scopus 로고
    • Mucosal B cells: phenotypic characteristics, transcriptional regulation, and homing properties
    • Brandtzaeg P., Johansen F.-E. Mucosal B cells: phenotypic characteristics, transcriptional regulation, and homing properties. Immunol. Rev. 2005, 206:32-63.
    • (2005) Immunol. Rev. , vol.206 , pp. 32-63
    • Brandtzaeg, P.1    Johansen, F.-E.2
  • 12
    • 1642305355 scopus 로고    scopus 로고
    • Use of staphylococcal protein A in the analysis of teleost immunoglobulin structural diversity
    • Bromage E.S., Ye J., Owens L., Kaattari I.M., Kaattari S.L. Use of staphylococcal protein A in the analysis of teleost immunoglobulin structural diversity. Dev. Comp. Immunol. 2004, 28:803-814.
    • (2004) Dev. Comp. Immunol. , vol.28 , pp. 803-814
    • Bromage, E.S.1    Ye, J.2    Owens, L.3    Kaattari, I.M.4    Kaattari, S.L.5
  • 14
    • 1642340732 scopus 로고    scopus 로고
    • Lowering the affinity between antigen and the B cell receptor can enhance antigen presentation
    • Brooks K., Knight A.M. Lowering the affinity between antigen and the B cell receptor can enhance antigen presentation. Eur. J. Immunol. 2004, 34:837-843.
    • (2004) Eur. J. Immunol. , vol.34 , pp. 837-843
    • Brooks, K.1    Knight, A.M.2
  • 15
    • 0026695644 scopus 로고
    • Affinity purification of antigen-specific serum immunoglobulin from the European eel (Anguilla anguilla)
    • Buchmann K., Osergaard L., Glamann J. Affinity purification of antigen-specific serum immunoglobulin from the European eel (Anguilla anguilla). Scand. J. Immunol. 1992, 36:89-97.
    • (1992) Scand. J. Immunol. , vol.36 , pp. 89-97
    • Buchmann, K.1    Osergaard, L.2    Glamann, J.3
  • 16
    • 0036027673 scopus 로고    scopus 로고
    • Raison Antibody-antigen kinetics following immunization of rainbow trout (Oncorhynchus mykiss) with a T-cell dependent antigen
    • Cain K.D., Jones D.R., Raison Antibody-antigen kinetics following immunization of rainbow trout (Oncorhynchus mykiss) with a T-cell dependent antigen. Dev. Comp. Immunol. 2002, 26:181-190.
    • (2002) Dev. Comp. Immunol. , vol.26 , pp. 181-190
    • Cain, K.D.1    Jones, D.R.2
  • 17
    • 0029986845 scopus 로고    scopus 로고
    • IgM polymerization inhibits the Golgi-mediated processing of the mu-chain carboxy-terminal glycans
    • Cals M.M., Guenzi S., Carelli S., Simmen T., Sparvoli A., Sitia R. IgM polymerization inhibits the Golgi-mediated processing of the mu-chain carboxy-terminal glycans. Mol. Immunol. 1996, 33:15-24.
    • (1996) Mol. Immunol. , vol.33 , pp. 15-24
    • Cals, M.M.1    Guenzi, S.2    Carelli, S.3    Simmen, T.4    Sparvoli, A.5    Sitia, R.6
  • 19
    • 0016829726 scopus 로고
    • Phylogeny of immunoglobulin structure and function VII Monomeric and tetrameric immunoglobulins of the margate, a marine teleost fish
    • Clem L.W., McLean W.E. Phylogeny of immunoglobulin structure and function VII Monomeric and tetrameric immunoglobulins of the margate, a marine teleost fish. Immunology 1975, 29:791-799.
    • (1975) Immunology , vol.29 , pp. 791-799
    • Clem, L.W.1    McLean, W.E.2
  • 20
    • 0034942293 scopus 로고    scopus 로고
    • The role of carbohydrate in the assembly and function of polymeric IgG
    • Coloma M.F., Clift A., Wims L., Morrison S.L. The role of carbohydrate in the assembly and function of polymeric IgG. Mol. Immunol. 2000, 37:1081-1090.
    • (2000) Mol. Immunol. , vol.37 , pp. 1081-1090
    • Coloma, M.F.1    Clift, A.2    Wims, L.3    Morrison, S.L.4
  • 21
    • 0021894435 scopus 로고
    • The classical complement pathway: activation and regulation of the first complement component
    • Cooper N.R. The classical complement pathway: activation and regulation of the first complement component. Adv. Immunol. 1985, 37:151-216.
    • (1985) Adv. Immunol. , vol.37 , pp. 151-216
    • Cooper, N.R.1
  • 22
    • 70349284531 scopus 로고    scopus 로고
    • The human IgM pentamer is a mushroom-shaped molecule with a flexural bias
    • Czajkowsky D.M., Shao Z.F. The human IgM pentamer is a mushroom-shaped molecule with a flexural bias. Proc. Natl. Acad. Sci. U.S.A. 2009, 106:14960-14965.
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 14960-14965
    • Czajkowsky, D.M.1    Shao, Z.F.2
  • 25
    • 14944348431 scopus 로고    scopus 로고
    • The immunoglobulin heavy-chain locus in zebrafish: identification and expression of a previously unknown isotype, immunoglobulin Z
    • Danilova N., Bussmann J., Jekosch K., Steiner L.A. The immunoglobulin heavy-chain locus in zebrafish: identification and expression of a previously unknown isotype, immunoglobulin Z. Nat. Immunol. 2005, 6:295-302.
    • (2005) Nat. Immunol. , vol.6 , pp. 295-302
    • Danilova, N.1    Bussmann, J.2    Jekosch, K.3    Steiner, L.A.4
  • 26
    • 0019230174 scopus 로고
    • Carbohydrate-mediated clearance of antibody-antigen complexes from the circulation. The role of high mannose oligosaccharides in the hepatic uptake of IgM-antigen complexes
    • Day J.F., Thornburg R.W., Thorpe S.R., Baynes J.W. Carbohydrate-mediated clearance of antibody-antigen complexes from the circulation. The role of high mannose oligosaccharides in the hepatic uptake of IgM-antigen complexes. J. Biol. Chem. 1980, 255:2360-2365.
    • (1980) J. Biol. Chem. , vol.255 , pp. 2360-2365
    • Day, J.F.1    Thornburg, R.W.2    Thorpe, S.R.3    Baynes, J.W.4
  • 27
    • 0032445509 scopus 로고    scopus 로고
    • Ichthyophthirius multifiliis: a model of cutaneous infection and immunity in fishes
    • Dickerson H., Clark T. Ichthyophthirius multifiliis: a model of cutaneous infection and immunity in fishes. Immunol. Rev. 1998, 166:377-384.
    • (1998) Immunol. Rev. , vol.166 , pp. 377-384
    • Dickerson, H.1    Clark, T.2
  • 28
    • 78049313303 scopus 로고    scopus 로고
    • The importance of natural IgM: scavenger, protector and regulator
    • Ehrenstein M.R., Notley C.A. The importance of natural IgM: scavenger, protector and regulator. Immunol. Rev. 2010, 10:778-786.
    • (2010) Immunol. Rev. , vol.10 , pp. 778-786
    • Ehrenstein, M.R.1    Notley, C.A.2
  • 29
    • 0011084483 scopus 로고
    • Variations in affinities of antibodies during the immune response
    • Eisen H.N., Siskind G.W. Variations in affinities of antibodies during the immune response. Biochemistry 1964, 3:996-1108.
    • (1964) Biochemistry , vol.3 , pp. 996-1108
    • Eisen, H.N.1    Siskind, G.W.2
  • 30
    • 0032556639 scopus 로고    scopus 로고
    • Heuristic models of the intermonomeric disulfide bonding process
    • Evans D.A., Klemer J.K., Kaattari S.L. Heuristic models of the intermonomeric disulfide bonding process. J. Theor. Biol. 1998, 195:505-524.
    • (1998) J. Theor. Biol. , vol.195 , pp. 505-524
    • Evans, D.A.1    Klemer, J.K.2    Kaattari, S.L.3
  • 31
    • 85190493034 scopus 로고    scopus 로고
    • Lippincott Williams and Wilkins, Philadelphia, W.E. Paul (Ed.)
    • Flajnik M.F., Miller K., Du Pasquier L. Fundamental Immunology 2003, 59-70. Lippincott Williams and Wilkins, Philadelphia. 5th ed. W.E. Paul (Ed.).
    • (2003) Fundamental Immunology , pp. 59-70
    • Flajnik, M.F.1    Miller, K.2    Du Pasquier, L.3
  • 33
    • 0021281941 scopus 로고
    • Novel mannosidase inhibitor blocking conversion of high mannose to complex oligosaccharides
    • Fuhrmann U., Bause E., Legler G., Ploegh H. Novel mannosidase inhibitor blocking conversion of high mannose to complex oligosaccharides. Nature 1984, 307:755-758.
    • (1984) Nature , vol.307 , pp. 755-758
    • Fuhrmann, U.1    Bause, E.2    Legler, G.3    Ploegh, H.4
  • 34
    • 0033045652 scopus 로고    scopus 로고
    • Influence of the μ-chain C-terminal sequence on polymerization of immunoglobulin M
    • Getahun A., Lundqvist M., Middleton D., Warr G., Pilstrom L. Influence of the μ-chain C-terminal sequence on polymerization of immunoglobulin M. Immunology 1999, 97:408-413.
    • (1999) Immunology , vol.97 , pp. 408-413
    • Getahun, A.1    Lundqvist, M.2    Middleton, D.3    Warr, G.4    Pilstrom, L.5
  • 35
    • 0024548991 scopus 로고
    • Cloning and sequence analysis of channel catfish heavy chain cDNA indicate phylogenetic diversity within the IgM immunoglobulin family
    • Ghaffari S.H., Lobb C.J. Cloning and sequence analysis of channel catfish heavy chain cDNA indicate phylogenetic diversity within the IgM immunoglobulin family. J. Immunol. 1989, 142:1356-1365.
    • (1989) J. Immunol. , vol.142 , pp. 1356-1365
    • Ghaffari, S.H.1    Lobb, C.J.2
  • 37
    • 18744371880 scopus 로고    scopus 로고
    • Discovery of a unique Ig heavy-chain isotype (IgT) in rainbow trout: implications for a distinctive B cell developmental pathway in teleost fish
    • Hansen J.D., Landis E.D., Phillips R.B. Discovery of a unique Ig heavy-chain isotype (IgT) in rainbow trout: implications for a distinctive B cell developmental pathway in teleost fish. Proc. Natl. Acad. Sci. U.S.A. 2005, 102:6919-6924.
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 6919-6924
    • Hansen, J.D.1    Landis, E.D.2    Phillips, R.B.3
  • 38
    • 0027164238 scopus 로고
    • Immunoglobulin in the eggs of the channel catfish (Ictalurus punctatus)
    • Hayman J.R., Lobb C.J. Immunoglobulin in the eggs of the channel catfish (Ictalurus punctatus). Dev. Comp. Immunol. 1993, 17:241-248.
    • (1993) Dev. Comp. Immunol. , vol.17 , pp. 241-248
    • Hayman, J.R.1    Lobb, C.J.2
  • 39
    • 0037397499 scopus 로고    scopus 로고
    • Disulfide bonds as switches for protein function
    • Hogg P.J. Disulfide bonds as switches for protein function. Trends Biochem. Sci. 2003, 28:210-214.
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 210-214
    • Hogg, P.J.1
  • 40
    • 38249015651 scopus 로고
    • Fish B lymphocytes: defining their form and function
    • Kaattari S.L. Fish B lymphocytes: defining their form and function. Ann. Rev. Fish Dis. 1992, 1:161-180.
    • (1992) Ann. Rev. Fish Dis. , vol.1 , pp. 161-180
    • Kaattari, S.L.1
  • 41
    • 0032416105 scopus 로고    scopus 로고
    • Varied redox forms of teleost IgM: an alternative to isotypic diversity?
    • Kaattari S., Evans D., Klemer J. Varied redox forms of teleost IgM: an alternative to isotypic diversity?. Immunol. Rev. 1998, 166:133-142.
    • (1998) Immunol. Rev. , vol.166 , pp. 133-142
    • Kaattari, S.1    Evans, D.2    Klemer, J.3
  • 42
  • 43
    • 0036027536 scopus 로고    scopus 로고
    • Affinity maturation in trout: clonal dominance of high affinity antibodies late in the immune response
    • Kaattari S.L., Zhang H.L., Khor I.W., Kaattari I.M., Shapiro D.A. Affinity maturation in trout: clonal dominance of high affinity antibodies late in the immune response. Dev. Comp. Immunol. 2002, 26:191-200.
    • (2002) Dev. Comp. Immunol. , vol.26 , pp. 191-200
    • Kaattari, S.L.1    Zhang, H.L.2    Khor, I.W.3    Kaattari, I.M.4    Shapiro, D.A.5
  • 44
    • 0020061123 scopus 로고
    • Studies on subunit components of immunoglobulin M from a bony fish, the chum salmon (Oncorhynchus keta)
    • Kobayashi K., Hara A., Takano K., Hirai H. Studies on subunit components of immunoglobulin M from a bony fish, the chum salmon (Oncorhynchus keta). Mol. Immunol. 1982, 19:95-103.
    • (1982) Mol. Immunol. , vol.19 , pp. 95-103
    • Kobayashi, K.1    Hara, A.2    Takano, K.3    Hirai, H.4
  • 45
    • 0019971005 scopus 로고
    • Germinal centre B cells: antigen specificity and changes in heavy chain class expression
    • Krall G., Weissman I.L., Butcher E.C. Germinal centre B cells: antigen specificity and changes in heavy chain class expression. Nature 1982, 298:377-379.
    • (1982) Nature , vol.298 , pp. 377-379
    • Krall, G.1    Weissman, I.L.2    Butcher, E.C.3
  • 47
    • 77952314719 scopus 로고    scopus 로고
    • Antigen affinity discrimination is an intrinsic function of the B cell receptor
    • Liu W., Meckel T., Tolar P., Shon H.W., Pierce S.K. Antigen affinity discrimination is an intrinsic function of the B cell receptor. J. Exp. Med. 2010, 1095-1111.
    • (2010) J. Exp. Med. , pp. 1095-1111
    • Liu, W.1    Meckel, T.2    Tolar, P.3    Shon, H.W.4    Pierce, S.K.5
  • 48
    • 0022003132 scopus 로고
    • Covalent structure and affinity of channel catfish anti-dinitrophenyl antibodies
    • Lobb C.J. Covalent structure and affinity of channel catfish anti-dinitrophenyl antibodies. Mol. Immunol. 1985, 22:993-999.
    • (1985) Mol. Immunol. , vol.22 , pp. 993-999
    • Lobb, C.J.1
  • 49
    • 0023549815 scopus 로고
    • Secretory immunity induced in catfish Ictalurus punctatus, following bath immunization
    • Lobb C.J. Secretory immunity induced in catfish Ictalurus punctatus, following bath immunization. Dev. Comp. Immunol. 1987, 11:727-738.
    • (1987) Dev. Comp. Immunol. , vol.11 , pp. 727-738
    • Lobb, C.J.1
  • 50
    • 0019403518 scopus 로고
    • Phylogeny of immunoglobulin structure and function-X. Humoral immunoglobulins of the sheepshead, Archosargus probatocephalus
    • Lobb C.J., Clem L.W. Phylogeny of immunoglobulin structure and function-X. Humoral immunoglobulins of the sheepshead, Archosargus probatocephalus. Dev. Comp. Immunol. 1981, 5:271-282.
    • (1981) Dev. Comp. Immunol. , vol.5 , pp. 271-282
    • Lobb, C.J.1    Clem, L.W.2
  • 51
    • 0019832286 scopus 로고
    • Phylogeny of immunoglobulin structure and function. XI. Secretory immunoglobulins in the cutaneous mucus of the sheepshead, Archosargus probatocephalus
    • Lobb C.J., Clem L.W. Phylogeny of immunoglobulin structure and function. XI. Secretory immunoglobulins in the cutaneous mucus of the sheepshead, Archosargus probatocephalus. Dev. Comp. Immunol. 1981, 5:587-596.
    • (1981) Dev. Comp. Immunol. , vol.5 , pp. 587-596
    • Lobb, C.J.1    Clem, L.W.2
  • 52
    • 0020550876 scopus 로고
    • Distinctive subpopulations of catfish serum antibody and immunoglobulin
    • Lobb C.J., Clem L.W. Distinctive subpopulations of catfish serum antibody and immunoglobulin. Mol. Immunol. 1983, 8:811-818.
    • (1983) Mol. Immunol. , vol.8 , pp. 811-818
    • Lobb, C.J.1    Clem, L.W.2
  • 53
    • 0001883936 scopus 로고    scopus 로고
    • Comparison of immunoglobulin (IgM) from four fish species
    • Magnadottir B. Comparison of immunoglobulin (IgM) from four fish species. Icelandic Agric. Sci. 1998, 12:47-59.
    • (1998) Icelandic Agric. Sci. , vol.12 , pp. 47-59
    • Magnadottir, B.1
  • 55
    • 0019412814 scopus 로고
    • Influence of IgG and IgM receptor triggering on human natural killer cell cytotoxicity measured on the level of the single effector cell
    • Merrill J.E., Ullberg M., Jondal M. Influence of IgG and IgM receptor triggering on human natural killer cell cytotoxicity measured on the level of the single effector cell. Eur. J. Immunol. 1981, 11:536-541.
    • (1981) Eur. J. Immunol. , vol.11 , pp. 536-541
    • Merrill, J.E.1    Ullberg, M.2    Jondal, M.3
  • 56
    • 0028952933 scopus 로고
    • Characterization of the glycosylation of a human IgM produced by a human-mouse hybridoma
    • Monica T.J., Williams S.B., Goochee C.F., Maliorella B.L. Characterization of the glycosylation of a human IgM produced by a human-mouse hybridoma. Glycobiology 1995, 5:175-185.
    • (1995) Glycobiology , vol.5 , pp. 175-185
    • Monica, T.J.1    Williams, S.B.2    Goochee, C.F.3    Maliorella, B.L.4
  • 57
    • 0035860349 scopus 로고    scopus 로고
    • Affinity purification and partial characterisation of systemic immunoglobulin of the snapper (Pagrus auratus)
    • Morrison R.N., Nowak B.F. Affinity purification and partial characterisation of systemic immunoglobulin of the snapper (Pagrus auratus). Aquaculture 2001, 201:1-17.
    • (2001) Aquaculture , vol.201 , pp. 1-17
    • Morrison, R.N.1    Nowak, B.F.2
  • 58
    • 0025365308 scopus 로고
    • Internal movements in immunoglobulin molecules
    • Nezlin R. Internal movements in immunoglobulin molecules. Adv. Immunol. 1990, 48:1-41.
    • (1990) Adv. Immunol. , vol.48 , pp. 1-41
    • Nezlin, R.1
  • 60
    • 0030267033 scopus 로고    scopus 로고
    • Modulation of protein structure and function by asparagine-linked glycosylation
    • O'Connor S.E., Imperiali B. Modulation of protein structure and function by asparagine-linked glycosylation. Chem. Biol. 1996, 3:803-812.
    • (1996) Chem. Biol. , vol.3 , pp. 803-812
    • O'Connor, S.E.1    Imperiali, B.2
  • 61
    • 0020025008 scopus 로고
    • Role of IgM in human monocyte-mediated target cell destruction in vitro
    • Ohlander C., Perlmann P. Role of IgM in human monocyte-mediated target cell destruction in vitro. Scand. J. Immunol. 1982, 15:363-370.
    • (1982) Scand. J. Immunol. , vol.15 , pp. 363-370
    • Ohlander, C.1    Perlmann, P.2
  • 62
    • 33645856486 scopus 로고    scopus 로고
    • Antigen recognition strength regulates the choice between extrafollicular plasma cell and germinal center B cell differentiation
    • Paus D., Phan T.G., Chan T.D., Gardam S., Basten A., Brink R. Antigen recognition strength regulates the choice between extrafollicular plasma cell and germinal center B cell differentiation. J. Exp. Med. 2006, 203:1081-1091.
    • (2006) J. Exp. Med. , vol.203 , pp. 1081-1091
    • Paus, D.1    Phan, T.G.2    Chan, T.D.3    Gardam, S.4    Basten, A.5    Brink, R.6
  • 64
    • 0018956701 scopus 로고
    • The biological half-lives of four rat immunoglobulin isotypes
    • Peppard J.V., Orlans E. The biological half-lives of four rat immunoglobulin isotypes. Immunology 1980, 40:683-686.
    • (1980) Immunology , vol.40 , pp. 683-686
    • Peppard, J.V.1    Orlans, E.2
  • 65
    • 78049287668 scopus 로고    scopus 로고
    • The tipping points in the initiation of B cell signaling: how small changes make big differences
    • Pierce S.K., Liu W. The tipping points in the initiation of B cell signaling: how small changes make big differences. Nat. Rev. Immunol. 2010, 10:767-778.
    • (2010) Nat. Rev. Immunol. , vol.10 , pp. 767-778
    • Pierce, S.K.1    Liu, W.2
  • 66
    • 0030140654 scopus 로고    scopus 로고
    • Immunoglobulin in fish-genes, expression and structure
    • Pilstrom L., Bengten E. Immunoglobulin in fish-genes, expression and structure. Fish Shellfish Immunol. 1996, 6:243-262.
    • (1996) Fish Shellfish Immunol. , vol.6 , pp. 243-262
    • Pilstrom, L.1    Bengten, E.2
  • 67
    • 0025225502 scopus 로고
    • Induction of RNA-stabilized DNA conformers by transcription of an immunoglobulin switch region
    • Reaban M.E., Griffin J.A. Induction of RNA-stabilized DNA conformers by transcription of an immunoglobulin switch region. Nature 1990, 348:342-344.
    • (1990) Nature , vol.348 , pp. 342-344
    • Reaban, M.E.1    Griffin, J.A.2
  • 68
    • 0025213243 scopus 로고
    • The binding of IgE to murine Fc epsilon RII is calcium-dependent but not inhibited by carbohydrate
    • Richards M.L., Katz D.H. The binding of IgE to murine Fc epsilon RII is calcium-dependent but not inhibited by carbohydrate. J. Immunol. 1990, 144:2638-2646.
    • (1990) J. Immunol. , vol.144 , pp. 2638-2646
    • Richards, M.L.1    Katz, D.H.2
  • 70
    • 0036591316 scopus 로고    scopus 로고
    • Nonimmune IgM, but not I(g)G binds to the surface of Plasmodium falciparum-infected erythrocytes and correlates with rosetting and severe malaria
    • Rowe J.A., Shafi J., Kai O.K., Marsh K., Raza A. Nonimmune IgM, but not I(g)G binds to the surface of Plasmodium falciparum-infected erythrocytes and correlates with rosetting and severe malaria. Am. J. Trop. Med. Hyg. 2002, 66:692-699.
    • (2002) Am. J. Trop. Med. Hyg. , vol.66 , pp. 692-699
    • Rowe, J.A.1    Shafi, J.2    Kai, O.K.3    Marsh, K.4    Raza, A.5
  • 71
    • 0014706575 scopus 로고
    • In vitro induction of a primary response to the dinitrophenyl determinant
    • Segal S., Globerson A., Feldman M., Haimovich J., Sela M. In vitro induction of a primary response to the dinitrophenyl determinant. J. Exp. Med. 1970, 131:93-99.
    • (1970) J. Exp. Med. , vol.131 , pp. 93-99
    • Segal, S.1    Globerson, A.2    Feldman, M.3    Haimovich, J.4    Sela, M.5
  • 73
    • 0023856770 scopus 로고
    • The half-lives of serum immunoglobulins in adult mice
    • Vieira P., Rajewsky K. The half-lives of serum immunoglobulins in adult mice. Eur. J. Immunol. 1988, 18:313-316.
    • (1988) Eur. J. Immunol. , vol.18 , pp. 313-316
    • Vieira, P.1    Rajewsky, K.2
  • 74
    • 0021004720 scopus 로고
    • Immunoglobulin of the toadfish Spheroides glaber
    • Warr G.W. Immunoglobulin of the toadfish Spheroides glaber. Comp. Biochem. Physiol. 1983, 76B:507-514.
    • (1983) Comp. Biochem. Physiol. , vol.76 B , pp. 507-514
    • Warr, G.W.1
  • 75
    • 0029017509 scopus 로고
    • Assembly of IgM: role of disulfide bonding and noncovalent interactions
    • Wiersma E.J., Shulman M.J. Assembly of IgM: role of disulfide bonding and noncovalent interactions. J. Immunol. 1995, 154:5265-5272.
    • (1995) J. Immunol. , vol.154 , pp. 5265-5272
    • Wiersma, E.J.1    Shulman, M.J.2
  • 79
    • 76249121805 scopus 로고    scopus 로고
    • The strength of B cell interaction with antigen determines the degree of IgM polymerization
    • Ye J., Bromage E.S., Kaattari S.L. The strength of B cell interaction with antigen determines the degree of IgM polymerization. J. Immunol. 2010, 184:844-850.
    • (2010) J. Immunol. , vol.184 , pp. 844-850
    • Ye, J.1    Bromage, E.S.2    Kaattari, S.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.