메뉴 건너뛰기




Volumn 76, Issue 5, 1999, Pages 2421-2431

Quantifying aggregation of IgE-FcεRI by multivalent antigen

Author keywords

[No Author keywords available]

Indexed keywords

2,4 DINITROPHENOL; ANTIGEN; CELL SURFACE RECEPTOR; FC RECEPTOR; FLUORESCEIN ISOTHIOCYANATE; HAPTEN; IMMUNOGLOBULIN E; PHYCOERYTHRIN;

EID: 0033059349     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(99)77397-2     Document Type: Article
Times cited : (35)

References (70)
  • 1
    • 0019460298 scopus 로고
    • IgE-induced histamine release from rat basophilic leukemia cell lines: Isolation of releasing and nonreleasing clones
    • Barsumian, E. L., C. Isersky, M. G. Petrino, and R. P. Siraganian. 1981. IgE-induced histamine release from rat basophilic leukemia cell lines: isolation of releasing and nonreleasing clones. Eur. J. Immunol. 11: 317-323.
    • (1981) Eur. J. Immunol. , vol.11 , pp. 317-323
    • Barsumian, E.L.1    Isersky, C.2    Petrino, M.G.3    Siraganian, R.P.4
  • 3
    • 0023082152 scopus 로고
    • Molecular mechanisms of transmembrane signaling in B lymphocytes
    • Cambier, J. C., and J. T. Ransom. 1987. Molecular mechanisms of transmembrane signaling in B lymphocytes. Annu. Rev. Immunol. 5:175-199.
    • (1987) Annu. Rev. Immunol. , vol.5 , pp. 175-199
    • Cambier, J.C.1    Ransom, J.T.2
  • 5
    • 0019208928 scopus 로고
    • Theory of clustering of cell surface receptors by ligands of arbitrary valence: Dependence of dose response patterns on a coarse cluster characteristic
    • DeLisi, C. 1980. Theory of clustering of cell surface receptors by ligands of arbitrary valence: dependence of dose response patterns on a coarse cluster characteristic. Math. Biosci. 52:159-184.
    • (1980) Math. Biosci. , vol.52 , pp. 159-184
    • DeLisi, C.1
  • 6
    • 0018190838 scopus 로고
    • Theory of equilibrium binding of symmetric bivalent haptens to cell surface antibody: Application to histamine release from basophils
    • Dembo, M., and B. Goldstein. 1978. Theory of equilibrium binding of symmetric bivalent haptens to cell surface antibody: application to histamine release from basophils. J. Immunol. 121:345-353.
    • (1978) J. Immunol. , vol.121 , pp. 345-353
    • Dembo, M.1    Goldstein, B.2
  • 7
    • 0019141549 scopus 로고
    • A model of cell activation and desensitization by surface immunoglobulin: The case of histamine release from human basophils
    • Dembo, M., and B. Goldstein. 1980. A model of cell activation and desensitization by surface immunoglobulin: the case of histamine release from human basophils. Cell. 22:59-67.
    • (1980) Cell , vol.22 , pp. 59-67
    • Dembo, M.1    Goldstein, B.2
  • 8
    • 0018102209 scopus 로고
    • Histamine release due to bivalent penicilloyl haptens: Control by the basophit plasma membrane
    • Dembo, M., B. Goldstein, A. K. Sobotka, and L. M. Lichtenstein. 1978. Histamine release due to bivalent penicilloyl haptens: control by the basophit plasma membrane. J. Immunol. 121:354-358.
    • (1978) J. Immunol. , vol.121 , pp. 354-358
    • Dembo, M.1    Goldstein, B.2    Sobotka, A.K.3    Lichtenstein, L.M.4
  • 9
    • 0018743531 scopus 로고
    • Histamine release due to bivalent penicilloyl haptens: Relation of activation and desensitization of basophils to dynamic aspects of ligand binding to cell surface antibody
    • Dembo, M., B. Goldstein, A. K. Sobotka, and L. M. Lichtenstein. 1979. Histamine release due to bivalent penicilloyl haptens: relation of activation and desensitization of basophils to dynamic aspects of ligand binding to cell surface antibody. J. Immunol. 122:518-528.
    • (1979) J. Immunol. , vol.122 , pp. 518-528
    • Dembo, M.1    Goldstein, B.2    Sobotka, A.K.3    Lichtenstein, L.M.4
  • 10
    • 0042689324 scopus 로고
    • Molecular determinants of immunogenicity: The immunon model of immune response
    • Dintzis, H. M., R. Z. Dintzis, and B. Vogelstein. 1976. Molecular determinants of immunogenicity: the immunon model of immune response. Proc. Natl. Acad. Sci. USA 73:3671-3675.
    • (1976) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 3671-3675
    • Dintzis, H.M.1    Dintzis, R.Z.2    Vogelstein, B.3
  • 11
    • 0020546049 scopus 로고
    • Studies on the immunogenicity and tolerogenicity of T-independent antigens
    • Dintzis, R. Z., M. H. Middleton, and H. M. Dintzis. 1983. Studies on the immunogenicity and tolerogenicity of T-independent antigens. J. Immunol. 131:2196-2203.
    • (1983) J. Immunol. , vol.131 , pp. 2196-2203
    • Dintzis, R.Z.1    Middleton, M.H.2    Dintzis, H.M.3
  • 12
    • 0026601947 scopus 로고
    • Engagement of the high-affinity IgE receptor activates src protein-related tyrosine kinases
    • Eiseman, E., and J. B. Bolen. 1992. Engagement of the high-affinity IgE receptor activates src protein-related tyrosine kinases. Nature. 355: 78-80.
    • (1992) Nature , vol.355 , pp. 78-80
    • Eiseman, E.1    Bolen, J.B.2
  • 13
  • 14
    • 0023425883 scopus 로고
    • The effect of receptor density on the forward rate constant for binding of ligands to cell surface receptors
    • Erickson, J., B. Goldstein, D. Holowka, and B. Baird. 1987. The effect of receptor density on the forward rate constant for binding of ligands to cell surface receptors. Biophys. J. 52:657-662.
    • (1987) Biophys. J. , vol.52 , pp. 657-662
    • Erickson, J.1    Goldstein, B.2    Holowka, D.3    Baird, B.4
  • 15
    • 0022649992 scopus 로고
    • Crosslinking of IgE-receptor complexes at the cell surface: A fluorescence method for studying the binding of monovalent and bivalent haptens to IgE
    • Erickson, J., P. Kane, B. Goldstein, D. Holowka, and B. Baird. 1986. Crosslinking of IgE-receptor complexes at the cell surface: a fluorescence method for studying the binding of monovalent and bivalent haptens to IgE. Mol. Immunol. 23:769-781.
    • (1986) Mol. Immunol. , vol.23 , pp. 769-781
    • Erickson, J.1    Kane, P.2    Goldstein, B.3    Holowka, D.4    Baird, B.5
  • 16
    • 0002641201 scopus 로고
    • Analysis of ligand binding and cross-linking of receptors in solution and on cell surfaces. Immunoglobulin E as a model receptor
    • F. G. Dewey, editor. Plenum, New York
    • Erickson, J., R. Posner, B. Goldstein, D. Holowka, and B. Baird. 1991. Analysis of ligand binding and cross-linking of receptors in solution and on cell surfaces. Immunoglobulin E as a model receptor. In Biophysical and Biochemical Aspects of Fluorescence Spectroscopy. F. G. Dewey, editor. Plenum, New York. 169-195.
    • (1991) Biophysical and Biochemical Aspects of Fluorescence Spectroscopy , pp. 169-195
    • Erickson, J.1    Posner, R.2    Goldstein, B.3    Holowka, D.4    Baird, B.5
  • 17
    • 0018908824 scopus 로고
    • Larger oligomers of IgE are more effective than dimers in stimulating rat basophilic leukemia cells
    • Fewtrell, C., and H. Metzger. 1980. Larger oligomers of IgE are more effective than dimers in stimulating rat basophilic leukemia cells. J. Immunol. 125:701-710.
    • (1980) J. Immunol. , vol.125 , pp. 701-710
    • Fewtrell, C.1    Metzger, H.2
  • 18
    • 0027373718 scopus 로고
    • Refined crystal structure of phycoerythrin from Porphyridium cruentum at 0.23-nm resolution and localization of the γ subunit
    • Ficner, R., and R. Huber. 1993. Refined crystal structure of phycoerythrin from Porphyridium cruentum at 0.23-nm resolution and localization of the γ subunit. Eur. J. Biochem. 218:103-106.
    • (1993) Eur. J. Biochem. , vol.218 , pp. 103-106
    • Ficner, R.1    Huber, R.2
  • 19
    • 0027093323 scopus 로고
    • Isolation, crystallization, crystal structure analysis and refinement of B-phycoerythrin from the red alga Porphyridium sordidum at 2.2 Å resolution
    • Ficner, R., K. Lobeck, G. Schmidt, and R. Huber. 1992. Isolation, crystallization, crystal structure analysis and refinement of B-phycoerythrin from the red alga Porphyridium sordidum at 2.2 Å resolution. J. Mol. Biol. 228:935-950.
    • (1992) J. Mol. Biol. , vol.228 , pp. 935-950
    • Ficner, R.1    Lobeck, K.2    Schmidt, G.3    Huber, R.4
  • 21
    • 0027444798 scopus 로고
    • New insights into protein-tyrosine kinase receptor signaling complexes
    • Fry, M. J., G. Panayotou, G. W. Booker, and M. D. Waterfield. 1993. New insights into protein-tyrosine kinase receptor signaling complexes. Protein Sci. 2:1785-1797.
    • (1993) Protein Sci. , vol.2 , pp. 1785-1797
    • Fry, M.J.1    Panayotou, G.2    Booker, G.W.3    Waterfield, M.D.4
  • 22
    • 0001975128 scopus 로고
    • Desensitization, histamine release and the aggregation of IgE on human basophils
    • A. S. Perelson, editor. Addison-Wesley, Reading, MA
    • Goldstein, B. 1988. Desensitization, histamine release and the aggregation of IgE on human basophils. In Theoretical Immunology, Part One. A. S. Perelson, editor. Addison-Wesley, Reading, MA. 3-40.
    • (1988) Theoretical Immunology , Issue.PART ONE , pp. 3-40
    • Goldstein, B.1
  • 23
    • 0000608345 scopus 로고
    • Aggregation of cell surface receptors
    • Goldstein, B., and C. Wofsy. 1994. Aggregation of cell surface receptors. Lect. Math. Life Sci. 24:109-135.
    • (1994) Lect. Math. Life Sci. , vol.24 , pp. 109-135
    • Goldstein, B.1    Wofsy, C.2
  • 24
    • 0024335096 scopus 로고
    • Dimerization of B-type platelet derived growth factor receptors occurs after ligand binding and is closely associated with receptor kinase activation
    • Heldin, C. H., A. Ernlund, C. Rorsman, and L. Ronnstrand. 1989. Dimerization of B-type platelet derived growth factor receptors occurs after ligand binding and is closely associated with receptor kinase activation. J. Biol. Chem. 264:8905-8912.
    • (1989) J. Biol. Chem. , vol.264 , pp. 8905-8912
    • Heldin, C.H.1    Ernlund, A.2    Rorsman, C.3    Ronnstrand, L.4
  • 25
    • 0029977729 scopus 로고    scopus 로고
    • Antigen-mediated IgE receptor aggregation and signaling: A window on cell surface structure and dynamics
    • Holowka, D., and B. Baird. 1996. Antigen-mediated IgE receptor aggregation and signaling: a window on cell surface structure and dynamics. Annu. Rev. Biophys. Biomol. Struct. 25:79-112.
    • (1996) Annu. Rev. Biophys. Biomol. Struct. , vol.25 , pp. 79-112
    • Holowka, D.1    Baird, B.2
  • 26
    • 0020025675 scopus 로고
    • Further characterization of the beta-component of the receptor for immunoglobulin E
    • Holowka, D., and H. Metzger. 1982. Further characterization of the beta-component of the receptor for immunoglobulin E. Mol. Immunol. 19: 219-227.
    • (1982) Mol. Immunol. , vol.19 , pp. 219-227
    • Holowka, D.1    Metzger, H.2
  • 27
    • 0022636156 scopus 로고
    • Cross-linking of IgE-receptor complexes at the cell surface: Synthesis and characterization of a long bivalent hapten that is capable of triggering mast cells and rat basophilic leukemia cells
    • Kane, P., J. Erickson, C. Fewtrell, B. Baird, and D. Holowka. 1986. Cross-linking of IgE-receptor complexes at the cell surface: synthesis and characterization of a long bivalent hapten that is capable of triggering mast cells and rat basophilic leukemia cells. Mol. Immunol. 23: 783-790.
    • (1986) Mol. Immunol. , vol.23 , pp. 783-790
    • Kane, P.1    Erickson, J.2    Fewtrell, C.3    Baird, B.4    Holowka, D.5
  • 28
    • 0021264238 scopus 로고
    • The fab fragment of a directly activating monoclonal antibody that precipitates a disulfide-linked heterodimer from a helper T cell clone blocks activation by either allogeneic Ia or antigen and self-Ia
    • Kaye, J., and C. A. Janeway, Jr. 1984. The Fab fragment of a directly activating monoclonal antibody that precipitates a disulfide-linked heterodimer from a helper T cell clone blocks activation by either allogeneic Ia or antigen and self-Ia. J. Exp. Med. 159:1397-1412.
    • (1984) J. Exp. Med. , vol.159 , pp. 1397-1412
    • Kaye, J.1    Janeway C.A., Jr.2
  • 29
    • 0020602877 scopus 로고
    • Both a monoclonal antibody and antisera specific for determinants unique to individual cloned helper T cell lines can substitute for antigen and antigen-presenting cells in the activation of T cells
    • Kaye, J., S. Porcelli, J. Tite, B. Jones, and C. A. Janeway, Jr. 1983. Both a monoclonal antibody and antisera specific for determinants unique to individual cloned helper T cell lines can substitute for antigen and antigen-presenting cells in the activation of T cells. J. Exp. Med. 158: 836-856.
    • (1983) J. Exp. Med. , vol.158 , pp. 836-856
    • Kaye, J.1    Porcelli, S.2    Tite, J.3    Jones, B.4    Janeway C.A., Jr.5
  • 30
    • 0026540751 scopus 로고
    • Multichain immune recognition receptors: Similarities in structure and signaling pathways
    • Keegan, A. D., and W. E. Paul. 1992. Multichain immune recognition receptors: similarities in structure and signaling pathways. Immunol. Today. 13:63-68.
    • (1992) Immunol. Today , vol.13 , pp. 63-68
    • Keegan, A.D.1    Paul, W.E.2
  • 31
    • 0016285205 scopus 로고
    • The interaction of IgE with rat basophilic leukemia cells. II. Quantitative aspects of the binding reaction
    • Kulczycki, A., Jr., and H. Metzger. 1974. The interaction of IgE with rat basophilic leukemia cells. II. Quantitative aspects of the binding reaction. J. Exp. Med. 140:1676-1695.
    • (1974) J. Exp. Med. , vol.140 , pp. 1676-1695
    • Kulczycki A., Jr.1    Metzger, H.2
  • 34
    • 0003104975 scopus 로고    scopus 로고
    • A TCR binds to antagonist ligands with lower affinities and faster dissociation rates than to agonists
    • Lyons, D. S., S. A. Lieberman, J. Hampl, J. J. Boniface, Y. Chien, L. J. Berg, and M. M. Davis. 1996. A TCR binds to antagonist ligands with lower affinities and faster dissociation rates than to agonists. Immunity. 5:53-61.
    • (1996) Immunity , vol.5 , pp. 53-61
    • Lyons, D.S.1    Lieberman, S.A.2    Hampl, J.3    Boniface, J.J.4    Chien, Y.5    Berg, L.J.6    Davis, M.M.7
  • 35
    • 0020537586 scopus 로고
    • Studies of antigen binding on human basophils. I. Antigen binding and functional consequences
    • MacGlashan, Jr., D., and L. M. Lichtenstein. 1983. Studies of antigen binding on human basophils. I. Antigen binding and functional consequences. J. Immunol. 130:2330-2336.
    • (1983) J. Immunol. , vol.130 , pp. 2330-2336
    • MacGlashan D., Jr.1    Lichtenstein, L.M.2
  • 36
    • 0022225695 scopus 로고
    • Test of a theory relating to the cross-linking of IgE antibody on the surface of human basophils
    • MacGlashan, Jr., D. W., M. Dembo, and B. Goldstein. 1985. Test of a theory relating to the cross-linking of IgE antibody on the surface of human basophils. J. Immunol. 135:4129-4134.
    • (1985) J. Immunol. , vol.135 , pp. 4129-4134
    • MacGlashan D.W., Jr.1    Dembo, M.2    Goldstein, B.3
  • 37
    • 0020694341 scopus 로고
    • Qualitative differences between dimeric and trimeric stimulation of human basophils
    • MacGlashan, Jr., D. W., R. P. Schleimer, and L. M. Lichtenstein. 1983. Qualitative differences between dimeric and trimeric stimulation of human basophils. J. Immunol. 130:4-6.
    • (1983) J. Immunol. , vol.130 , pp. 4-6
    • MacGlashan D.W., Jr.1    Schleimer, R.P.2    Lichtenstein, L.M.3
  • 39
    • 0028902752 scopus 로고
    • Zeta phosphorylation without ZAP-70 activation induced by TCR antagonists or partial agonists
    • Madrenas, J., R. L. Wange, J. L. Wang, N. Isakov, L. E. Samelson, and R. N. Germain. 1995. Zeta phosphorylation without ZAP-70 activation induced by TCR antagonists or partial agonists. Science. 267:515-518.
    • (1995) Science , vol.267 , pp. 515-518
    • Madrenas, J.1    Wange, R.L.2    Wang, J.L.3    Isakov, N.4    Samelson, L.E.5    Germain, R.N.6
  • 40
    • 0021364151 scopus 로고
    • Small oligomers of immunoglobulin E (IgE) cause large-scale clustering of IgE receptors on the surface of rat basophilic leukemia cells
    • Menon, A. K., D. Holowka, and B. Baird. 1984. Small oligomers of immunoglobulin E (IgE) cause large-scale clustering of IgE receptors on the surface of rat basophilic leukemia cells. J. Cell. Biol. 98:577-583.
    • (1984) J. Cell. Biol. , vol.98 , pp. 577-583
    • Menon, A.K.1    Holowka, D.2    Baird, B.3
  • 41
    • 0026675654 scopus 로고
    • Transmembrane signaling: The joy of aggregation
    • Metzger, H. 1992. Transmembrane signaling: the joy of aggregation. J. Immunol. 149:1477-1487.
    • (1992) J. Immunol. , vol.149 , pp. 1477-1487
    • Metzger, H.1
  • 42
    • 0031848098 scopus 로고    scopus 로고
    • Extending the range of rate constants available from BIACORE: Interpreting mass transport-influenced binding data
    • Myszka D. G., X. He, M. Dembo, T. A. Morton, and B. Goldstein. 1998. Extending the range of rate constants available from BIACORE: interpreting mass transport-influenced binding data. Biophys. J. 75:583-594.
    • (1998) Biophys. J. , vol.75 , pp. 583-594
    • Myszka, D.G.1    He, X.2    Dembo, M.3    Morton, T.A.4    Goldstein, B.5
  • 43
    • 0032563231 scopus 로고    scopus 로고
    • Fidelity of T cell activation through multistep T cell receptor ζ phosphorylation
    • Neumeister Kersh, E., A. S. Shaw, and P. M. Allen. 1998. Fidelity of T cell activation through multistep T cell receptor ζ phosphorylation. Science. 281:572-575.
    • (1998) Science , vol.281 , pp. 572-575
    • Neumeister Kersh, E.1    Shaw, A.S.2    Allen, P.M.3
  • 44
    • 0028289241 scopus 로고
    • Anatomy of the antibody molecule
    • Padlan, E. A. 1994. Anatomy of the antibody molecule. Mol. Immunol. 31:169-217.
    • (1994) Mol. Immunol. , vol.31 , pp. 169-217
    • Padlan, E.A.1
  • 45
    • 0026639821 scopus 로고
    • Triggering signaling cascades by receptor tyrosine kinases
    • Pazin, M. J., and L. T. Williams. 1992. Triggering signaling cascades by receptor tyrosine kinases. Trends Biochem. Sci. 17:374-378.
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 374-378
    • Pazin, M.J.1    Williams, L.T.2
  • 46
    • 0018939138 scopus 로고
    • Receptor clustering on a cell surface. II. Theory of receptor cross-linking by ligands bearing two chemically distinct functional groups
    • Perelson, A. S. 1980. Receptor clustering on a cell surface. II. Theory of receptor cross-linking by ligands bearing two chemically distinct functional groups. Math. Biosci. 49:87-110.
    • (1980) Math. Biosci. , vol.49 , pp. 87-110
    • Perelson, A.S.1
  • 47
    • 0019454791 scopus 로고
    • Receptor clustering on a cell surface. III. Theory of receptor cross-linking by multivalent ligands: Description by ligand states
    • Perelson, A. S. 1981. Receptor clustering on a cell surface. III. Theory of receptor cross-linking by multivalent ligands: description by ligand states. Math. Biosci. 53:1-39.
    • (1981) Math. Biosci. , vol.53 , pp. 1-39
    • Perelson, A.S.1
  • 48
    • 0001505146 scopus 로고
    • Some mathematical models of receptor clustering by multivalent ligands
    • A. S. Perelson, C. DeLisi, and F. W. Wiegel, editors. Marcel Dekker, New York
    • Perelson, A. S. 1984. Some mathematical models of receptor clustering by multivalent ligands. In Cell Surface Dynamics: Concepts and Models. A. S. Perelson, C. DeLisi, and F. W. Wiegel, editors. Marcel Dekker, New York. 223-276.
    • (1984) Cell Surface Dynamics: Concepts and Models , pp. 223-276
    • Perelson, A.S.1
  • 49
    • 0019216482 scopus 로고
    • Receptor clustering on a cell surface. I. Theory of receptor cross-linking by ligands bearing two chemically identical functional groups
    • Perelson, A. S., and C. DeLisi. 1980. Receptor clustering on a cell surface. I. Theory of receptor cross-linking by ligands bearing two chemically identical functional groups. Math. Biosci. 48:71-110.
    • (1980) Math. Biosci. , vol.48 , pp. 71-110
    • Perelson, A.S.1    DeLisi, C.2
  • 51
    • 0032225579 scopus 로고    scopus 로고
    • Measurement of receptor crosslinking at the cell surface via multiparameter flow cytometry
    • Posner, R. G., J. Bold, Y. Bernstein, J. Rasor, J. Braslow, W. S. Hlavacek, and A. S. Perelson. 1998. Measurement of receptor crosslinking at the cell surface via multiparameter flow cytometry. SPIE. 3256:132-143.
    • (1998) SPIE , vol.3256 , pp. 132-143
    • Posner, R.G.1    Bold, J.2    Bernstein, Y.3    Rasor, J.4    Braslow, J.5    Hlavacek, W.S.6    Perelson, A.S.7
  • 52
    • 0028096718 scopus 로고
    • Binding of bivalent ligand to cell surface IgE: Can one detect ring formation?
    • Posner, R. G., and M. Dembo. 1994. Binding of bivalent ligand to cell surface IgE: can one detect ring formation? Mol. Immunol. 31: 1439-1445.
    • (1994) Mol. Immunol. , vol.31 , pp. 1439-1445
    • Posner, R.G.1    Dembo, M.2
  • 53
    • 0025847106 scopus 로고
    • Dissociation kinetics of bivalent ligand immunoglobulin E aggregates in solution
    • Posner, R. G., J. W. Erickson, D. Holowka, B. Baird, and B. Goldstein. 1991. Dissociation kinetics of bivalent ligand immunoglobulin E aggregates in solution. Biochemistry. 30:2348-2356.
    • (1991) Biochemistry , vol.30 , pp. 2348-2356
    • Posner, R.G.1    Erickson, J.W.2    Holowka, D.3    Baird, B.4    Goldstein, B.5
  • 54
    • 0029128987 scopus 로고
    • Simultaneous cross-linking by two nontriggering bivalent ligands causes synergistic signaling of IgE Fc∈RI complexes
    • Posner, R. G., K. Subramanian, B. Goldstein, J. Thomas, T. Feder, D. Holowka, and B. Baird. 1995a. Simultaneous cross-linking by two nontriggering bivalent ligands causes synergistic signaling of IgE Fc∈RI complexes. J. Immunol. 155:3601-3609.
    • (1995) J. Immunol. , vol.155 , pp. 3601-3609
    • Posner, R.G.1    Subramanian, K.2    Goldstein, B.3    Thomas, J.4    Feder, T.5    Holowka, D.6    Baird, B.7
  • 55
    • 0028931731 scopus 로고
    • The kinetics of bivalent ligand-bivalent receptor aggregation: Ring formation and the breakdown of the equivalent site approximation
    • Posner, R. G., C. Wofsy, and B. Goldstein. 1995b. The kinetics of bivalent ligand-bivalent receptor aggregation: ring formation and the breakdown of the equivalent site approximation. Math. Biosci. 126:171-190.
    • (1995) Math. Biosci. , vol.126 , pp. 171-190
    • Posner, R.G.1    Wofsy, C.2    Goldstein, B.3
  • 57
    • 0020659319 scopus 로고
    • Biological role of epidermal growth factor receptor clustering: Investigation with monoclonal anti-receptor antibodies
    • Schreiber, A. B., T. A. Libermann, I. Lax, Y. Yarden, and J. Schlessinger. 1982. Biological role of epidermal growth factor receptor clustering: investigation with monoclonal anti-receptor antibodies. J. Biol. Chem. 258:846-853.
    • (1982) J. Biol. Chem. , vol.258 , pp. 846-853
    • Schreiber, A.B.1    Libermann, T.A.2    Lax, I.3    Yarden, Y.4    Schlessinger, J.5
  • 58
    • 0023657709 scopus 로고
    • Oligomerization and ring closure of immunoglobulin E class antibodies by divalent haptens
    • Schweitzer-Stenner, R., A. Licht, I. Luscher, and I. Pecht. 1987. Oligomerization and ring closure of immunoglobulin E class antibodies by divalent haptens. Biochemistry. 26:3602-3612.
    • (1987) Biochemistry , vol.26 , pp. 3602-3612
    • Schweitzer-Stenner, R.1    Licht, A.2    Luscher, I.3    Pecht, I.4
  • 59
    • 0023341187 scopus 로고
    • DNP-phycobiliproteins, fluorescent antigens to study dynamic properties of antigen-IgE-receptor complexes on RBL-2H3 rat mast-cells
    • Seagrave, J. C., G. G. Deanin, J. C. Martin, B. H. Davis, and J. M. Oliver. 1987. DNP-phycobiliproteins, fluorescent antigens to study dynamic properties of antigen-IgE-receptor complexes on RBL-2H3 rat mast-cells. Cytometry. 8:287-295.
    • (1987) Cytometry , vol.8 , pp. 287-295
    • Seagrave, J.C.1    Deanin, G.G.2    Martin, J.C.3    Davis, B.H.4    Oliver, J.M.5
  • 60
    • 0025302772 scopus 로고
    • Antigen-dependent transition of IgE to a detergent-insoluble form is associated with reduced IgE receptor-dependent secretion from RBL-2H3 mast cells
    • Seagrave, J. C., and J. M. Oliver. 1990. Antigen-dependent transition of IgE to a detergent-insoluble form is associated with reduced IgE receptor-dependent secretion from RBL-2H3 mast cells. J. Cell. Physiol. 144:128-136.
    • (1990) J. Cell. Physiol. , vol.144 , pp. 128-136
    • Seagrave, J.C.1    Oliver, J.M.2
  • 61
    • 0000457253 scopus 로고
    • Dimeric immunoglobulin E serves as a unit signal for mast cell degranulation
    • Segal, D. M., J. D. Taurog, and H. Metzger. 1977. Dimeric immunoglobulin E serves as a unit signal for mast cell degranulation. Proc. Natl. Acad. Sci. USA. 74:2993-2997.
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 2993-2997
    • Segal, D.M.1    Taurog, J.D.2    Metzger, H.3
  • 62
    • 0016428184 scopus 로고
    • Specific in vitro histamine release from basophils by bivalent haptens: Evidence for activation by simple bridging of membrane bound antibody
    • Siraganian, R. P., W. A. Hook, and B. B. Levine. 1975. Specific in vitro histamine release from basophils by bivalent haptens: evidence for activation by simple bridging of membrane bound antibody. Immunochemistry. 12:149-157.
    • (1975) Immunochemistry , vol.12 , pp. 149-157
    • Siraganian, R.P.1    Hook, W.A.2    Levine, B.B.3
  • 63
    • 0027967385 scopus 로고
    • Partial T cell signaling: Altered phospho-zeta and lack of zap70 recruitment in APL-induced T cell anergy
    • Sloan-Lancaster, J., A. S. Shaw, J. B. Rothbard, and P. M. Allen. 1994. Partial T cell signaling: altered phospho-zeta and lack of zap70 recruitment in APL-induced T cell anergy. Cell. 79:913-922.
    • (1994) Cell , vol.79 , pp. 913-922
    • Sloan-Lancaster, J.1    Shaw, A.S.2    Rothbard, J.B.3    Allen, P.M.4
  • 64
    • 0020052004 scopus 로고
    • Binding properties of IgE receptors on normal mouse mast cells
    • Sterk, A. R., and T. Ishizaka. 1982. Binding properties of IgE receptors on normal mouse mast cells. J. Immunol. 128:838-843.
    • (1982) J. Immunol. , vol.128 , pp. 838-843
    • Sterk, A.R.1    Ishizaka, T.2
  • 65
    • 0030586127 scopus 로고    scopus 로고
    • Equilibrium binding of multivalent ligands to cells: Effects of cell and receptor density
    • Sulzer, B., and A. S. Perelson. 1996. Equilibrium binding of multivalent ligands to cells: effects of cell and receptor density. Math. Biosci. 135:147-185.
    • (1996) Math. Biosci. , vol.135 , pp. 147-185
    • Sulzer, B.1    Perelson, A.S.2
  • 66
    • 0032562995 scopus 로고    scopus 로고
    • An unusual mechanism for ligand antagonism
    • Torigoe, C., J. K. Inman, and H. Metzger. 1998. An unusual mechanism for ligand antagonism. Science. 281:568-572.
    • (1998) Science , vol.281 , pp. 568-572
    • Torigoe, C.1    Inman, J.K.2    Metzger, H.3
  • 67
    • 0023154356 scopus 로고
    • The effect of co-operativity on the equilibrium binding of symmetric bivalent ligands to antibodies: Theoretical results with application to histamine release from basophils
    • Wofsy, C., and B. Goldstein. 1987. The effect of co-operativity on the equilibrium binding of symmetric bivalent ligands to antibodies: theoretical results with application to histamine release from basophils. Mol. Immunol. 24:151-161.
    • (1987) Mol. Immunol. , vol.24 , pp. 151-161
    • Wofsy, C.1    Goldstein, B.2
  • 68
    • 0031573523 scopus 로고    scopus 로고
    • Exploiting the difference between intrinsic and extrinsic kinases: Implications for regulation of signaling by immunoreceptors
    • Wofsy, C., C. Torigoe, U. M. Kent, H. Metzger, and B. Goldstein. 1997. Exploiting the difference between intrinsic and extrinsic kinases: implications for regulation of signaling by immunoreceptors. J. Immunol. 159:5984-5992.
    • (1997) J. Immunol. , vol.159 , pp. 5984-5992
    • Wofsy, C.1    Torigoe, C.2    Kent, U.M.3    Metzger, H.4    Goldstein, B.5
  • 69
    • 0029001897 scopus 로고
    • Flow cytometric analysis of T-independent antigen binding to dinitrophenyl-specific cells
    • Woodard, S. L., M. Aldo-Benson, D. A. Roess, and B. G. Barisas. 1995. Flow cytometric analysis of T-independent antigen binding to dinitrophenyl-specific cells. J. Immunol. 155:163-171.
    • (1995) J. Immunol. , vol.155 , pp. 163-171
    • Woodard, S.L.1    Aldo-Benson, M.2    Roess, D.A.3    Barisas, B.G.4
  • 70
    • 0032055568 scopus 로고    scopus 로고
    • Kinetics of multivalent antigen DNP-BSA binding to IgE-Fc∈RI in relationship to the stimulated tyrosine phosphorylation of Fc∈RI
    • Xu, K., B. Goldstein, D. Holowka, and B. Baird. 1998. Kinetics of multivalent antigen DNP-BSA binding to IgE-Fc∈RI in relationship to the stimulated tyrosine phosphorylation of Fc∈RI. J. Immunol. 160: 3225-3235.
    • (1998) J. Immunol. , vol.160 , pp. 3225-3235
    • Xu, K.1    Goldstein, B.2    Holowka, D.3    Baird, B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.