메뉴 건너뛰기




Volumn 120, Issue 2, 1999, Pages 85-99

Immunoglobulin structure and function as revealed by electron microscopy

Author keywords

Antibody; Electron microscopy; Immunoglobulin; Review; Structure

Indexed keywords

IMMUNOGLOBULIN;

EID: 0032850235     PISSN: 10182438     EISSN: None     Source Type: Journal    
DOI: 10.1159/000024226     Document Type: Review
Times cited : (60)

References (80)
  • 1
    • 0017152608 scopus 로고
    • Crystallographic structure studies of an IgG molecule and an Fc fragment
    • Huber R, Deisenhofer J, Colman PM, Matsushima M: Crystallographic structure studies of an IgG molecule and an Fc fragment. Nature 1976;264:415-420.
    • (1976) Nature , vol.264 , pp. 415-420
    • Huber, R.1    Deisenhofer, J.2    Colman, P.M.3    Matsushima, M.4
  • 2
    • 0001500510 scopus 로고
    • Three-dimensional structure of an intact human immunoglohulin
    • Silverton EW, Navia MA, Davies DR: Three-dimensional structure of an intact human immunoglohulin. Proc Natl Acad Sci USA 1977; 74:5140-5144.
    • (1977) Proc Natl Acad Sci USA , vol.74 , pp. 5140-5144
    • Silverton, E.W.1    Navia, M.A.2    Davies, D.R.3
  • 3
    • 0018372576 scopus 로고
    • Changes in quaternary structure of IgG upon reduction of the interheavy-chain disulfide bond
    • Seegan GW, Smith CA, Schumaker VN: Changes in quaternary structure of IgG upon reduction of the interheavy-chain disulfide bond. Proc Natl Acad Sci USA 1979;76:907-911.
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 907-911
    • Seegan, G.W.1    Smith, C.A.2    Schumaker, V.N.3
  • 4
    • 0024803886 scopus 로고
    • Immunoelectron microscopy of idiotype-anti-idiotype complexes
    • Roux KH: Immunoelectron microscopy of idiotype-anti-idiotype complexes. Methods Enzymol 1989;178:130-144.
    • (1989) Methods Enzymol , vol.178 , pp. 130-144
    • Roux, K.H.1
  • 5
    • 0030270610 scopus 로고    scopus 로고
    • Negative stain immunoelectron microscopic analysis of small macromolecules of immunologic significance
    • Roux KH: Negative stain immunoelectron microscopic analysis of small macromolecules of immunologic significance. Methods 1996;10: 247.
    • (1996) Methods , vol.10 , pp. 247
    • Roux, K.H.1
  • 6
    • 0022545058 scopus 로고
    • Cyclic tetramolecular complexes of monoclonal antibodies: A new type of cross-linking reagent
    • Lansdorp PM, Aalberse RC, Bos R, Schutter WG, Van Bruggen EFJ: Cyclic tetramolecular complexes of monoclonal antibodies: A new type of cross-linking reagent. Eur J Immunol 1986;16:679-683.
    • (1986) Eur J Immunol , vol.16 , pp. 679-683
    • Lansdorp, P.M.1    Aalberse, R.C.2    Bos, R.3    Schutter, W.G.4    Van Bruggen, E.F.J.5
  • 7
    • 0020691229 scopus 로고
    • Two-dimensional crystallization technique for imaging macromolecules, with application to antigen-antibody-complement complexes
    • Uzgiris EE, Kornberg RD: Two-dimensional crystallization technique for imaging macromolecules, with application to antigen-antibody-complement complexes. Nature 1983; 301:125-129.
    • (1983) Nature , vol.301 , pp. 125-129
    • Uzgiris, E.E.1    Kornberg, R.D.2
  • 8
    • 0022410211 scopus 로고
    • Antibody crystallization on phospholipid films: Dynamics and the effects of antibody conformation
    • Uzgiris EE: Antibody crystallization on phospholipid films: Dynamics and the effects of antibody conformation. J Cell Biochem 1985;29: 239-251.
    • (1985) J Cell Biochem , vol.29 , pp. 239-251
    • Uzgiris, E.E.1
  • 9
    • 0023653893 scopus 로고
    • Self-organization of IgE immunoglobulins on phospholipid films
    • Uzgiris EE: Self-organization of IgE immunoglobulins on phospholipid films. Biochem J 1987;242:293-296.
    • (1987) Biochem J , vol.242 , pp. 293-296
    • Uzgiris, E.E.1
  • 10
    • 0016688080 scopus 로고
    • Molecular structure determination by electron microscopy of unstained crystalline specimens
    • Unwin PN, Henderson R: Molecular structure determination by electron microscopy of unstained crystalline specimens. J Mol Biol 1975;94:425-440.
    • (1975) J Mol Biol , vol.94 , pp. 425-440
    • Unwin, P.N.1    Henderson, R.2
  • 11
    • 0023113466 scopus 로고
    • Forms of a self associating autoantihody complex between a monoclonal human IgG1 and human serum albumin
    • Jentoft JE, Bolinger L, Ainslie GR, Tandler B: Forms of a self associating autoantihody complex between a monoclonal human IgG1 and human serum albumin. Mol Immunol 1987;24: 163-169.
    • (1987) Mol Immunol , vol.24 , pp. 163-169
    • Jentoft, J.E.1    Bolinger, L.2    Ainslie, G.R.3    Tandler, B.4
  • 12
    • 0021783435 scopus 로고
    • Comparative electron microscopic studies of single biomolecules negatively stained and freeze-dried metal-shadowed
    • Tesche B, Schmiady H: Comparative electron microscopic studies of single biomolecules negatively stained and freeze-dried metal-shadowed. Ultramicroscopy 1985;16:423-435.
    • (1985) Ultramicroscopy , vol.16 , pp. 423-435
    • Tesche, B.1    Schmiady, H.2
  • 14
    • 0025799419 scopus 로고
    • Visualization of natural autoantibody polyreactivity by rotary metal-shadowing electron microscopy
    • Baccala R, Builbert B, Labrousse H, Avrameas S, Gounon P: Visualization of natural autoantibody polyreactivity by rotary metal-shadowing electron microscopy. Res Immunol 1991; 142:299-312.
    • (1991) Res Immunol , vol.142 , pp. 299-312
    • Baccala, R.1    Builbert, B.2    Labrousse, H.3    Avrameas, S.4    Gounon, P.5
  • 17
    • 0027121512 scopus 로고
    • Identification of a Fab interaction footprint site on an icosahedral virus by cryoelectron microscopy and X-ray crystallography
    • Wang G, Porta C, Chen Z, Baker TS, Johnson JE: Identification of a Fab interaction footprint site on an icosahedral virus by cryoelectron microscopy and X-ray crystallography. Nature 1992;355:275-278.
    • (1992) Nature , vol.355 , pp. 275-278
    • Wang, G.1    Porta, C.2    Chen, Z.3    Baker, T.S.4    Johnson, J.E.5
  • 19
    • 8244249460 scopus 로고    scopus 로고
    • Structure of the complex of an Fab fragment of a neutralizing antibody with foot-and-mouth disease virus: Positioning of a highly mobile antigenic loop
    • Hewat EA, Verdaguer N, Fita I, Blakemore W, Brookes S, King A, Newman J, Domingo E, Mateu MG, Stuart DI: Structure of the complex of an Fab fragment of a neutralizing antibody with foot-and-mouth disease virus: Positioning of a highly mobile antigenic loop. EMBO J 1997;16:1492-1500.
    • (1997) EMBO J , vol.16 , pp. 1492-1500
    • Hewat, E.A.1    Verdaguer, N.2    Fita, I.3    Blakemore, W.4    Brookes, S.5    King, A.6    Newman, J.7    Domingo, E.8    Mateu, M.G.9    Stuart, D.I.10
  • 20
    • 0031967887 scopus 로고    scopus 로고
    • Structure of a neutralizing antibody bound monovalently to human rhinovirus 2
    • Hewat EA, Marlovits TC, Blaas D: Structure of a neutralizing antibody bound monovalently to human rhinovirus 2. J Virol 1998;72: 4396-4402.
    • (1998) J Virol , vol.72 , pp. 4396-4402
    • Hewat, E.A.1    Marlovits, T.C.2    Blaas, D.3
  • 23
    • 0025650041 scopus 로고
    • Imaging single-stranded DNA, antigen-antibody reaction and polymerized langmuir-blodgett films with an atomic force microscope
    • Weisenhorn AL, Gaub HE, Hansma HG, Sinsheimer RL, Kelderman GL, Kansma PK: Imaging single-stranded DNA, antigen-antibody reaction and polymerized langmuir-blodgett films with an atomic force microscope. Scanning Microscopy 1990;4:511-516.
    • (1990) Scanning Microscopy , vol.4 , pp. 511-516
    • Weisenhorn, A.L.1    Gaub, H.E.2    Hansma, H.G.3    Sinsheimer, R.L.4    Kelderman, G.L.5    Kansma, P.K.6
  • 24
    • 0028808187 scopus 로고
    • Imaging of single antigens, antibodies, and specific immunocomplex formation by scanning force microscopy
    • Quist AP, Bergman AA, Reimann CT, Oscarsson SO, Sundqvist BUR: Imaging of single antigens, antibodies, and specific immunocomplex formation by scanning force microscopy. Scan Microsc 1995;9:395-400.
    • (1995) Scan Microsc , vol.9 , pp. 395-400
    • Quist, A.P.1    Bergman, A.A.2    Reimann, C.T.3    Oscarsson, S.O.4    Sundqvist, B.U.R.5
  • 25
    • 0029845352 scopus 로고    scopus 로고
    • Imaging biological structures with the cryo atomic force microscope
    • Zhang Y, Sheng S, Shao Z: Imaging biological structures with the cryo atomic force microscope. Biophys J 1996;71:2168-2176.
    • (1996) Biophys J , vol.71 , pp. 2168-2176
    • Zhang, Y.1    Sheng, S.2    Shao, Z.3
  • 26
    • 0001479421 scopus 로고
    • Molecular mechanism of formation of an antigen-antibody complex
    • Feinstein A, Rowe AJ: Molecular mechanism of formation of an antigen-antibody complex. Nature 1965;205:147-149.
    • (1965) Nature , vol.205 , pp. 147-149
    • Feinstein, A.1    Rowe, A.J.2
  • 27
    • 0014202658 scopus 로고
    • Electron microscopy of an antibody-hapten complex
    • Valentine RC, Green NM: Electron microscopy of an antibody-hapten complex. J Mol Biol 1967;27:615-617.
    • (1967) J Mol Biol , vol.27 , pp. 615-617
    • Valentine, R.C.1    Green, N.M.2
  • 28
    • 0022908968 scopus 로고    scopus 로고
    • Computer models of the human immunoglobulins. Shape and segmental flexibility
    • Pumphrey R: Computer models of the human immunoglobulins. Shape and segmental flexibility. Immunol Today 1986:174-178
    • Immunol Today , vol.1986 , pp. 174-178
    • Pumphrey, R.1
  • 29
    • 0027973873 scopus 로고
    • Human/mouse chimeric monoclonal antibodies with human IgG1, IgG2, IgG3 and IgG4 constant domains: Electron microscopic and hydrodynamic characterization
    • Phillips ML, Tao M-H, Morrison SL, Schumaker VN: Human/mouse chimeric monoclonal antibodies with human IgG1, IgG2, IgG3 and IgG4 constant domains: Electron microscopic and hydrodynamic characterization. Molec Immunol 1994;31:1201-1210.
    • (1994) Molec Immunol , vol.31 , pp. 1201-1210
    • Phillips, M.L.1    Tao, M.-H.2    Morrison, S.L.3    Schumaker, V.N.4
  • 31
    • 0014259754 scopus 로고
    • The ultrastructure of normal and pathological IgM
    • Chesebro B, Bloth B, Svehag SE: The ultrastructure of normal and pathological IgM. J Exp Med 1968;127:399-410.
    • (1968) J Exp Med , vol.127 , pp. 399-410
    • Chesebro, B.1    Bloth, B.2    Svehag, S.E.3
  • 32
    • 0014775121 scopus 로고
    • Electron microscopic studies of mouse immunoglobulin M: Structure and reconstitution following reduction
    • Parkhouse RME, Askonas BA, Dourmashkin RR: Electron microscopic studies of mouse immunoglobulin M: Structure and reconstitution following reduction. Immunology 1970; 18:575-584.
    • (1970) Immunology , vol.18 , pp. 575-584
    • Parkhouse, R.M.E.1    Askonas, B.A.2    Dourmashkin, R.R.3
  • 33
    • 0015247268 scopus 로고
    • The three-dimensional conformation of gamma M and gamma A globulin molecules
    • Feinstein A, Munn EA, Richardson NE: The three-dimensional conformation of gamma M and gamma A globulin molecules. Ann NY Acad Sci 1971;190:104-121.
    • (1971) Ann NY Acad Sci , vol.190 , pp. 104-121
    • Feinstein, A.1    Munn, E.A.2    Richardson, N.E.3
  • 34
    • 0019773255 scopus 로고
    • Electron microscopy of the natural IgM-like hemagglutinin of the ratfish (Callorhynchus callorhynchus)
    • Garrido J, Ioannes A: Electron microscopy of the natural IgM-like hemagglutinin of the ratfish (Callorhynchus callorhynchus). Dev Comp Immunol 1981;5:691-696.
    • (1981) Dev Comp Immunol , vol.5 , pp. 691-696
    • Garrido, J.1    Ioannes, A.2
  • 36
    • 0017137272 scopus 로고
    • Xenopus laevis 19S immunoglobulin: Ultrastructure and J chain isolation
    • Hadji-Azimi I, Michea-Hamzehpour M: Xenopus laevis 19S immunoglobulin: Ultrastructure and J chain isolation. Immunology 1976;30: 587-591.
    • (1976) Immunology , vol.30 , pp. 587-591
    • Hadji-Azimi, I.1    Michea-Hamzehpour, M.2
  • 38
    • 0014966642 scopus 로고
    • The ultrastructure of carp (Cyprinus carpio) immunoglobulin: A tetrameric macroglobulin
    • Shelton E, Smith M: The ultrastructure of carp (Cyprinus carpio) immunoglobulin: A tetrameric macroglobulin. J Mol Biol 1970;54: 615-617.
    • (1970) J Mol Biol , vol.54 , pp. 615-617
    • Shelton, E.1    Smith, M.2
  • 39
    • 0017856190 scopus 로고
    • Small-angle X-ray studies of a human immunoglobulin M
    • Wilhelm P, Pilz I, Palm W, Bauer K: Small-angle X-ray studies of a human immunoglobulin M. Eur J Biochem 1978;84:457-463.
    • (1978) Eur J Biochem , vol.84 , pp. 457-463
    • Wilhelm, P.1    Pilz, I.2    Palm, W.3    Bauer, K.4
  • 40
    • 0022358372 scopus 로고
    • Immunoglobulin M possesses two binding sites for complement subcomponent C1q, and soluble 1:1 and 2:1 complexes are formed in solution at reduced ionic strength
    • Poon PH, Phillips ML, Schumaker VN: Immunoglobulin M possesses two binding sites for complement subcomponent C1q, and soluble 1:1 and 2:1 complexes are formed in solution at reduced ionic strength. J Biol Chem 1985;260:9357-9365.
    • (1985) J Biol Chem , vol.260 , pp. 9357-9365
    • Poon, P.H.1    Phillips, M.L.2    Schumaker, V.N.3
  • 41
    • 0024436948 scopus 로고
    • Intermolecular disulfide bonding in IgM: Effects of replacing cystein residues in the mu heavy chain
    • Davis AC, Roux KH, Pursey J, Shulman MJ: Intermolecular disulfide bonding in IgM: Effects of replacing cystein residues in the mu heavy chain. EMBO J 1989;8:2519-2526.
    • (1989) EMBO J , vol.8 , pp. 2519-2526
    • Davis, A.C.1    Roux, K.H.2    Pursey, J.3    Shulman, M.J.4
  • 43
    • 0026009904 scopus 로고
    • Solution structure of human and mouse immunoglobulin M by synchroton x-ray scattering and molecular graphics modelling: A possible mechanism for complement activation
    • Perkins SJ, Nealis AS, Sutton BJ, Feinstein A: Solution structure of human and mouse immunoglobulin M by synchroton x-ray scattering and molecular graphics modelling: A possible mechanism for complement activation. J Mol Biol 1991;221:1345-1366.
    • (1991) J Mol Biol , vol.221 , pp. 1345-1366
    • Perkins, S.J.1    Nealis, A.S.2    Sutton, B.J.3    Feinstein, A.4
  • 44
    • 0023403373 scopus 로고
    • Polymeric immunoglobulin M is secreted by transfectants of non-lymphoid cells in the absence of immunoglobulin J chain
    • Cattaneo A, Neuberger MS: Polymeric immunoglobulin M is secreted by transfectants of non-lymphoid cells in the absence of immunoglobulin J chain. EMBO J 1987;6:2753-2758.
    • (1987) EMBO J , vol.6 , pp. 2753-2758
    • Cattaneo, A.1    Neuberger, M.S.2
  • 46
    • 0015242948 scopus 로고
    • Electron microscopy of human and mouse myeloma serum IgA
    • Dourmashkin RB, Virella G, Parkhouse RM: Electron microscopy of human and mouse myeloma serum IgA. J Mol Biol 1971;56:207-208.
    • (1971) J Mol Biol , vol.56 , pp. 207-208
    • Dourmashkin, R.B.1    Virella, G.2    Parkhouse, R.M.3
  • 47
    • 0032578554 scopus 로고    scopus 로고
    • Structural analysis of the nurse shark (new) antigen receptor (NAR): Molecular convergence of NAR and unusual mammalian immunoglobulins
    • Roux KH, Greenberg AS, Greene L, Strelets L, Avila D, McKinney EC, Flajnik MF: Structural analysis of the nurse shark (new) antigen receptor (NAR): Molecular convergence of NAR and unusual mammalian immunoglobulins. Proc Natl Acad Sci USA 1998;95:11804-11809.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 11804-11809
    • Roux, K.H.1    Greenberg, A.S.2    Greene, L.3    Strelets, L.4    Avila, D.5    McKinney, E.C.6    Flajnik, M.F.7
  • 48
    • 0025365308 scopus 로고
    • Internal movement in immunoglobulin molecules
    • Nezlin R: Internal movement in immunoglobulin molecules. Adv Immunol 1990;48:1-40.
    • (1990) Adv Immunol , vol.48 , pp. 1-40
    • Nezlin, R.1
  • 49
    • 0021112606 scopus 로고
    • Electron microscopic evidence for the axial rotation and inter-domain flexibility of the Fab regions of immunoglobulin G
    • Wrigley NG, Brown EB, Shehel JJ: Electron microscopic evidence for the axial rotation and inter-domain flexibility of the Fab regions of immunoglobulin G. J Mol Biol 1983;169:771-774.
    • (1983) J Mol Biol , vol.169 , pp. 771-774
    • Wrigley, N.G.1    Brown, E.B.2    Shehel, J.J.3
  • 50
    • 0022366272 scopus 로고
    • Approach to the direct intramolecular localization of antigenic determinants in Androctonus australis hemocyanin with monoclonal antibodies by molecular immunoelectron microscopy
    • Lamy I, Lamy J, Billiald P, Sizaret P-Y, Cave G, Frank J, Motta G: Approach to the direct intramolecular localization of antigenic determinants in Androctonus australis hemocyanin with monoclonal antibodies by molecular immunoelectron microscopy. Biochemistry 1985;24:5532:5542.
    • (1985) Biochemistry , vol.24 , pp. 5532
    • Lamy, I.1    Lamy, J.2    Billiald, P.3    Sizaret, P.-Y.4    Cave, G.5    Frank, J.6    Motta, G.7
  • 51
    • 0024573950 scopus 로고
    • Concerning the axial rotational flexibility of the Fab regions of immunoglobulin G
    • Wade RH, Taveau JC, Lamy JN: Concerning the axial rotational flexibility of the Fab regions of immunoglobulin G. J Mol Biol 1989; 206:349-356.
    • (1989) J Mol Biol , vol.206 , pp. 349-356
    • Wade, R.H.1    Taveau, J.C.2    Lamy, J.N.3
  • 52
    • 0020422254 scopus 로고
    • Immunoelectron microscopic localization of idiotypes and allotypes on immunoglobulin molecules
    • Roux KH, Metzger DW: Immunoelectron microscopic localization of idiotypes and allotypes on immunoglobulin molecules. J Immunol 1982;129:2548-2553.
    • (1982) J Immunol , vol.129 , pp. 2548-2553
    • Roux, K.H.1    Metzger, D.W.2
  • 53
    • 0021254591 scopus 로고
    • Direct demonstration of multiple VH allotypes on rabbit Ig molecules: Allotype characteristics and Fab arm rotational flexibility revealed by immunoelectron microscopy
    • Roux KH: Direct demonstration of multiple VH allotypes on rabbit Ig molecules: Allotype characteristics and Fab arm rotational flexibility revealed by immunoelectron microscopy. Eur J Immunol 1984;14:459-464.
    • (1984) Eur J Immunol , vol.14 , pp. 459-464
    • Roux, K.H.1
  • 55
    • 0023870785 scopus 로고
    • Structure determination of a monoclonal Fab fragment specific for histidine-containing protein of the phosphoenolypyruvate: Sugar phosphotransferase system of Escherichia coli
    • Prasad L, Vandonselaar M, Lee JS, Delbaere L: Structure determination of a monoclonal Fab fragment specific for histidine-containing protein of the phosphoenolypyruvate: Sugar phosphotransferase system of Escherichia coli. J Biol Chem 1988;15:2571-2574.
    • (1988) J Biol Chem , vol.15 , pp. 2571-2574
    • Prasad, L.1    Vandonselaar, M.2    Lee, J.S.3    Delbaere, L.4
  • 56
    • 0021217827 scopus 로고
    • Induced latent allotypes within rabbit anti-crossreactive idiotype reagents: Direct immunoelectron microscopic evidence
    • Roux KH, Metzger DW, Kazdin DS, Horng WJ: Induced latent allotypes within rabbit anti-crossreactive idiotype reagents: Direct immunoelectron microscopic evidence. Eur J Immunol 1984;14:910-915.
    • (1984) Eur J Immunol , vol.14 , pp. 910-915
    • Roux, K.H.1    Metzger, D.W.2    Kazdin, D.S.3    Horng, W.J.4
  • 57
    • 0022370518 scopus 로고
    • A reevaluation of rabbit anti-allotype antibody for the presence of cross-reactive idiotypes. I. A species-specific idiotope on rabbit anti-a1 antibody is recognized by guinea pig anti-IdX antibody
    • Roux KH, McCormack WT, Dhanarajan P: A reevaluation of rabbit anti-allotype antibody for the presence of cross-reactive idiotypes. I. A species-specific idiotope on rabbit anti-a1 antibody is recognized by guinea pig anti-IdX antibody. J Immunol 1985;135:1961-1966.
    • (1985) J Immunol , vol.135 , pp. 1961-1966
    • Roux, K.H.1    McCormack, W.T.2    Dhanarajan, P.3
  • 58
    • 0023214922 scopus 로고
    • Mouse monoclonal antibody bearing a VH framework region determinant similar to a rabbit Vha1 allotype
    • McClain BR, Roux KH: Mouse monoclonal antibody bearing a VH framework region determinant similar to a rabbit Vha1 allotype. Immunology 1987;61:397-402.
    • (1987) Immunology , vol.61 , pp. 397-402
    • McClain, B.R.1    Roux, K.H.2
  • 60
    • 0023369233 scopus 로고
    • Construction of an extended three-dimensional idiotope map by electron microscopic analysis of idiotope-anti-idiotope complexes
    • Roux KH, Monafo WJ, Davie JM, Greenspan NS: Construction of an extended three-dimensional idiotope map by electron microscopic analysis of idiotope-anti-idiotope complexes. Proc Natl Acad Sci USA 1987;84:4984-4988.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 4984-4988
    • Roux, K.H.1    Monafo, W.J.2    Davie, J.M.3    Greenspan, N.S.4
  • 61
    • 0021987892 scopus 로고
    • Serologic and topographic characterization of idiotopes on murine monoclonal anti-streptococcal group A carbohydrate antibodies
    • Greenspan NS, Davie JM: Serologic and topographic characterization of idiotopes on murine monoclonal anti-streptococcal group A carbohydrate antibodies. J Immunol 1985;134: 1065-1072.
    • (1985) J Immunol , vol.134 , pp. 1065-1072
    • Greenspan, N.S.1    Davie, J.M.2
  • 63
    • 0028228107 scopus 로고
    • Monitoring the formation of soluble immune complexes composed of idiotype and anti-idiotype antibodies by electron microscopy
    • Roux KH, Greenspan NS: Monitoring the formation of soluble immune complexes composed of idiotype and anti-idiotype antibodies by electron microscopy. Mol Immunol 1994; 31:599-606.
    • (1994) Mol Immunol , vol.31 , pp. 599-606
    • Roux, K.H.1    Greenspan, N.S.2
  • 64
    • 0025176995 scopus 로고
    • Electron microscopic study of ring-shaped, bivalent hapten, bivalent antidansyl monoclonal antibody complexes with identical variable domains but IgG1, IgG2 and IgG2b constant domains
    • Phillips ML, Oi VT, Schumaker VN: Electron microscopic study of ring-shaped, bivalent hapten, bivalent antidansyl monoclonal antibody complexes with identical variable domains but IgG1, IgG2 and IgG2b constant domains. Mol Immunol 1990;27:181-190.
    • (1990) Mol Immunol , vol.27 , pp. 181-190
    • Phillips, M.L.1    Oi, V.T.2    Schumaker, V.N.3
  • 65
    • 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;7:1989-1994.
    • (1988) EMBO J , vol.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
  • 67
    • 0032532015 scopus 로고    scopus 로고
    • Comparisons of the ability of human IgG3 hinge mutants, IgM, IgE, and IgA2, to form small immune complexes: A role for flexibility and geometry
    • Roux KH, Strelets L, Brekke OH, Sandlie I, Michaelsen TE: Comparisons of the ability of human IgG3 hinge mutants, IgM, IgE, and IgA2, to form small immune complexes: A role for flexibility and geometry. J Immunol 1998;161:4083-4090.
    • (1998) J Immunol , vol.161 , pp. 4083-4090
    • Roux, K.H.1    Strelets, L.2    Brekke, O.H.3    Sandlie, I.4    Michaelsen, T.E.5
  • 71
    • 0032478777 scopus 로고    scopus 로고
    • Orientation of antigen binding sites in dimeric and trimeric single chain Fv antibody fragments
    • Lawrence LJ, Kortt AA, Iliades P, Tulloch PA, Hudson PJ: Orientation of antigen binding sites in dimeric and trimeric single chain Fv antibody fragments. FEBS Lett 1998;425: 479-484.
    • (1998) FEBS Lett , vol.425 , pp. 479-484
    • Lawrence, L.J.1    Kortt, A.A.2    Iliades, P.3    Tulloch, P.A.4    Hudson, P.J.5
  • 73
    • 0025101122 scopus 로고
    • A view of the human idiotypic repertoire: Electron microscopic and immunologic analyses of spontaneous idiotype-anti-idiotype dimers in pooled human IgG
    • Roux KH, Tankersley DL: A view of the human idiotypic repertoire: electron microscopic and immunologic analyses of spontaneous idiotype-anti-idiotype dimers in pooled human IgG. J Immunol 1990;144:1387-1395.
    • (1990) J Immunol , vol.144 , pp. 1387-1395
    • Roux, K.H.1    Tankersley, D.L.2
  • 74
    • 0023727485 scopus 로고
    • Anti-IgM-mediating B cell signaling: Molecular analysis of ligand binding requisites for human B cell activation and tolerance
    • Rudich SM, Roux KH, Winchester RJ, Mongini PKA: Anti-IgM-mediating B cell signaling: molecular analysis of ligand binding requisites for human B cell activation and tolerance. J Exp Med 1988;268:247-266.
    • (1988) J Exp Med , vol.268 , pp. 247-266
    • Rudich, S.M.1    Roux, K.H.2    Winchester, R.J.3    Mongini, P.K.A.4
  • 75
    • 0028855669 scopus 로고
    • Electron microscopy of antibody complexes of influenza virus haemagglutinin in the fusion pH conformation
    • Wharton SA, Calder LJ, Ruigrok RWH, Skehel JJ, Steinbauer DA, Wiley DC: Electron microscopy of antibody complexes of influenza virus haemagglutinin in the fusion pH conformation. EMBO J 1995;14:240-246.
    • (1995) EMBO J , vol.14 , pp. 240-246
    • Wharton, S.A.1    Calder, L.J.2    Ruigrok, R.W.H.3    Skehel, J.J.4    Steinbauer, D.A.5    Wiley, D.C.6
  • 76
    • 0020693696 scopus 로고
    • Fc-mediated immune precipitation. III. Visualization by electron microscopy
    • Moller NPH, Christiansen G: Fc-mediated immune precipitation. III. Visualization by electron microscopy. Immunology 1983;48:469.
    • (1983) Immunology , vol.48 , pp. 469
    • Moller, N.P.H.1    Christiansen, G.2
  • 77
    • 0014768883 scopus 로고
    • The fixation of complement and the activated first component (C1) of complement by complexes formed between antibody and divalent hapten
    • Hyslop NE, Dourmashkin RR, Green NM, Porter RR: The fixation of complement and the activated first component (C1) of complement by complexes formed between antibody and divalent hapten. J Exp Med 1970;131:783-802.
    • (1970) J Exp Med , vol.131 , pp. 783-802
    • Hyslop, N.E.1    Dourmashkin, R.R.2    Green, N.M.3    Porter, R.R.4
  • 78
    • 0022905472 scopus 로고
    • Is IgM-like dislocation a common feature of antibody function?
    • Burton DR: Is IgM-like dislocation a common feature of antibody function? Immunol Today 1986;7:165-167.
    • (1986) Immunol Today , vol.7 , pp. 165-167
    • Burton, D.R.1
  • 79
    • 0028828789 scopus 로고
    • Bent domain structure of recombinant human IgE-Fc in solution by X-ray and neutron scattering in conjunction with an automated curve fitting procedure
    • Beavil AJ, Young RJ, Sutton BJ, Perkins SJ: Bent domain structure of recombinant human IgE-Fc in solution by X-ray and neutron scattering in conjunction with an automated curve fitting procedure. Biochemistry 1995;34: 14449-14461.
    • (1995) Biochemistry , vol.34 , pp. 14449-14461
    • Beavil, A.J.1    Young, R.J.2    Sutton, B.J.3    Perkins, S.J.4
  • 80
    • 0027306163 scopus 로고
    • Structure of a human rhinovirus-bivalently bound antibody complex: Implications for viral neutralization and antibody flexibility
    • Smith T, Olson N, Cheng R, Chase E, Baker T: Structure of a human rhinovirus-bivalently bound antibody complex: Implications for viral neutralization and antibody flexibility. Proc Natl Acad Sci USA 1993;90:7015-7018.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 7015-7018
    • Smith, T.1    Olson, N.2    Cheng, R.3    Chase, E.4    Baker, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.