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Volumn 402, Issue 6760 SUPPL. 1, 1999, Pages

Signalling through the high-affinity IgE receptor FcεRI

Author keywords

[No Author keywords available]

Indexed keywords

FC RECEPTOR; GUANOSINE TRIPHOSPHATASE; IMMUNOGLOBULIN E; IMMUNOGLOBULIN E RECEPTOR;

EID: 0033604543     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/35037021     Document Type: Review
Times cited : (643)

References (66)
  • 1
    • 0032970154 scopus 로고    scopus 로고
    • The high-affinity IgE receptor (Fc epsilon RI): From physiology to pathology
    • Kinet, J. P. The high-affinity IgE receptor (Fc epsilon RI): from physiology to pathology. Annu. Rev. Immunol. 17, 931-972 (1999).
    • (1999) Annu. Rev. Immunol. , vol.17 , pp. 931-972
    • Kinet, J.P.1
  • 2
    • 0028014460 scopus 로고
    • Signal transduction by lymphocyte antigen receptors
    • Weiss, A. & Littman, D. R. Signal transduction by lymphocyte antigen receptors. Cell 76, 263-274 (1994).
    • (1994) Cell , vol.76 , pp. 263-274
    • Weiss, A.1    Littman, D.R.2
  • 3
    • 0029082078 scopus 로고
    • Antigen and Fc receptor signalling. The awesome power of the immunoreceptor tyrosine-based activation motif (ITAM)
    • Cambier, J. Antigen and Fc receptor signalling. The awesome power of the immunoreceptor tyrosine-based activation motif (ITAM). J. Immunol. 155, 3281-3285 (1995).
    • (1995) J. Immunol. , vol.155 , pp. 3281-3285
    • Cambier, J.1
  • 4
    • 0024980981 scopus 로고
    • Antigen receptor tail clue
    • Reth, M. Antigen receptor tail clue. Nature 338, 383-384 (1989).
    • (1989) Nature , vol.338 , pp. 383-384
    • Reth, M.1
  • 5
    • 0032560608 scopus 로고    scopus 로고
    • Thermodynamics of the interaction of human immunoglobulin E with its high-affinity receptor Fc epsilon RI
    • Keown, M. B., Henry, A. J., Ghirlando, R., Sutton, B. J. & Gould, H. J. Thermodynamics of the interaction of human immunoglobulin E with its high-affinity receptor Fc epsilon RI. Biochemistry 37, 8863-8869 (1998).
    • (1998) Biochemistry , vol.37 , pp. 8863-8869
    • Keown, M.B.1    Henry, A.J.2    Ghirlando, R.3    Sutton, B.J.4    Gould, H.J.5
  • 6
    • 0028143496 scopus 로고
    • The binding site on human immunoglobulin E for its high affinity receptor
    • Presta, L. et al. The binding site on human immunoglobulin E for its high affinity receptor. J. Biol. Chem. 269, 26368-26373 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 26368-26373
    • Presta, L.1
  • 7
    • 0031443213 scopus 로고    scopus 로고
    • Participation of the N-terrninal region of Cepsilon3 in the binding of human IgE to its high-affinity receptor FcepsilonRI
    • Henry, A. J. et al. Participation of the N-terrninal region of Cepsilon3 in the binding of human IgE to its high-affinity receptor FcepsilonRI. Biochemistry 36, 15568-15578 (1997).
    • (1997) Biochemistry , vol.36 , pp. 15568-15578
    • Henry, A.J.1
  • 8
    • 0027217555 scopus 로고
    • Phage and Escherichia coli expression of the human high affinity immunoglobulin E receptor alpha-subunit ectodomain. Domain localization of the IgE-binding site
    • Robertson, M. W. Phage and Escherichia coli expression of the human high affinity immunoglobulin E receptor alpha-subunit ectodomain. Domain localization of the IgE-binding site. J. Biol. Chem. 268, 12736-12743 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 12736-12743
    • Robertson, M.W.1
  • 9
    • 0028928202 scopus 로고
    • Glycosylation of human truncated Fc epsilon RI alpha chain is necessary for efficient folding in the endoplasmic reticulum
    • Letourneur, O., Sechi, S., Willette Brown, J., Robertson, M. W. & Kinet, J. P. Glycosylation of human truncated Fc epsilon RI alpha chain is necessary for efficient folding in the endoplasmic reticulum. J. Biol. Chem. 270, 8249-8256 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 8249-8256
    • Letourneur, O.1    Sechi, S.2    Willette Brown, J.3    Robertson, M.W.4    Kinet, J.P.5
  • 10
    • 0032419721 scopus 로고    scopus 로고
    • Crystal structure of the human high-affinity IgE receptor
    • Garman, S. C., Kinet, J. P. & Jardetzky, T. S. Crystal structure of the human high-affinity IgE receptor. Cell 95, 951-961 (1998).
    • (1998) Cell , vol.95 , pp. 951-961
    • Garman, S.C.1    Kinet, J.P.2    Jardetzky, T.S.3
  • 11
    • 0025791981 scopus 로고
    • Structure function relationships in mast cell high affinity receptor for IgE
    • Alber, G., Miller, L., Jelsema, C. L., Varin-Blank, N. & Metzger, H. Structure function relationships in mast cell high affinity receptor for IgE. J. Biol. Chem. 266, 22613-22620 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 22613-22620
    • Alber, G.1    Miller, L.2    Jelsema, C.L.3    Varin-Blank, N.4    Metzger, H.5
  • 12
    • 0030929805 scopus 로고    scopus 로고
    • Fc receptor biology
    • Daeron, M. Fc receptor biology. Annu. Rev. Immunol. 15, 203-234 (1997).
    • (1997) Annu. Rev. Immunol. , vol.15 , pp. 203-234
    • Daeron, M.1
  • 13
    • 0028895654 scopus 로고
    • Modular binding domains in signal transduction proteins
    • Cohen, G. B., Ren, R. & Baltimore, D. Modular binding domains in signal transduction proteins. Cell 80, 237-248 (1995).
    • (1995) Cell , vol.80 , pp. 237-248
    • Cohen, G.B.1    Ren, R.2    Baltimore, D.3
  • 14
    • 0029045870 scopus 로고
    • Reconstitution of interactions between tyrosine kinases and the high affinity IgE receptor which are controlled by receptor clustering
    • Scharenberg, A. M., Lin, S., Cuenod, B., Yamamura, H. & Kinet, J. P. Reconstitution of interactions between tyrosine kinases and the high affinity IgE receptor which are controlled by receptor clustering. EMBO J. 14, 3385-3394 (1995).
    • (1995) EMBO J. , vol.14 , pp. 3385-3394
    • Scharenberg, A.M.1    Lin, S.2    Cuenod, B.3    Yamamura, H.4    Kinet, J.P.5
  • 15
    • 0027998862 scopus 로고
    • Differential control of the tyrosine kinases Lyn and Syk by the two signaling chains of the high affinity immunoglobulin E receptor
    • Jouvin, M. H. et al. Differential control of the tyrosine kinases Lyn and Syk by the two signaling chains of the high affinity immunoglobulin E receptor. J. Biol Chem. 269, 5918-5925 (1994).
    • (1994) J. Biol Chem. , vol.269 , pp. 5918-5925
    • Jouvin, M.H.1
  • 16
    • 0031092657 scopus 로고    scopus 로고
    • 2+ mobilization, but not degranulation, in lyn-deficient bone marrow-derived mast cells
    • 2+ mobilization, but not degranulation, in lyn-deficient bone marrow-derived mast cells. J. Immunol. 158, 2350-2355 (1997).
    • (1997) J. Immunol. , vol.158 , pp. 2350-2355
    • Nishizumi, H.1    Yamamoto, T.2
  • 17
    • 0030472724 scopus 로고    scopus 로고
    • Critical role for the tyrosine kinase Syk in signalling through the high affinity IgE receptor of mast cells
    • Costello, P. S. et al. Critical role for the tyrosine kinase Syk in signalling through the high affinity IgE receptor of mast cells. Oncogene 13, 2595-2605 (1996).
    • (1996) Oncogene , vol.13 , pp. 2595-2605
    • Costello, P.S.1
  • 18
    • 0030018183 scopus 로고    scopus 로고
    • Transfection of Syk protein tyrosine kinase reconstitutes high affinity IgE receptor-mediated degranulation in a Syk-negative variant of rat basophilic leukemia RBL-2H3 cells
    • Zhang, J., Berenstein, E. H., Evans, R. L. & Siraganian, R. P. Transfection of Syk protein tyrosine kinase reconstitutes high affinity IgE receptor-mediated degranulation in a Syk-negative variant of rat basophilic leukemia RBL-2H3 cells. J. Exp. Med. 184, 71-79 (1996).
    • (1996) J. Exp. Med. , vol.184 , pp. 71-79
    • Zhang, J.1    Berenstein, E.H.2    Evans, R.L.3    Siraganian, R.P.4
  • 19
    • 0030849446 scopus 로고    scopus 로고
    • The unique domain as the site on Lyn kinase for its constitutive association with the high affinity receptor for IgE
    • Vonakis, B. M., Chen, H., Haleem-Smith, H. & Metzger, H. The unique domain as the site on Lyn kinase for its constitutive association with the high affinity receptor for IgE. J. Biol. Chem. 272, 24072-24080 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 24072-24080
    • Vonakis, B.M.1    Chen, H.2    Haleem-Smith, H.3    Metzger, H.4
  • 20
    • 0028035310 scopus 로고
    • Transphosphorylation as the mechanism by which the high-affinity receptor for IgE is phosphorylated upon aggregation
    • Pribluda, V. S., Pribluda, C. & Metzger, H. Transphosphorylation as the mechanism by which the high-affinity receptor for IgE is phosphorylated upon aggregation. Proc. Natl Acad. Sci. USA 91, 11246-11250 (1994).
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 11246-11250
    • Pribluda, V.S.1    Pribluda, C.2    Metzger, H.3
  • 21
    • 0031042637 scopus 로고    scopus 로고
    • syk kinase activation by a src kinase-initiated activation loop phosphorylation chain reaction
    • El-Hillal, O., Kurosaki, T., Yamamura, H., Kinet, J. P. & Scharenberg, A. M. syk kinase activation by a src kinase-initiated activation loop phosphorylation chain reaction. Proc. Natl Acad. Sci. USA 94, 1919-1924 (1997).
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 1919-1924
    • El-Hillal, O.1    Kurosaki, T.2    Yamamura, H.3    Kinet, J.P.4    Scharenberg, A.M.5
  • 22
    • 0030881799 scopus 로고    scopus 로고
    • Roles of C-terminal Src kinase in the initiation and the termination of the high affinity IgE receptor-mediated signaling
    • Honda, Z. et al. Roles of C-terminal Src kinase in the initiation and the termination of the high affinity IgE receptor-mediated signaling. J. Biol. Chem. 272, 25753-25760 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 25753-25760
    • Honda, Z.1
  • 23
    • 0031017838 scopus 로고    scopus 로고
    • Activation of the Src-family tyrosine kinase Hck by SH3 domain displacement
    • Moarefi, I. et al. Activation of the Src-family tyrosine kinase Hck by SH3 domain displacement. Nature 385, 650-653 (1997).
    • (1997) Nature , vol.385 , pp. 650-653
    • Moarefi, I.1
  • 24
    • 0032986606 scopus 로고    scopus 로고
    • The regulation of antigen-receptor signaling by protein tyrosine phosphatases: A hole in the story
    • Thomas, M. L. The regulation of antigen-receptor signaling by protein tyrosine phosphatases: a hole in the story. Curr. Opin. Immunol. 11, 270-276 (1999).
    • (1999) Curr. Opin. Immunol. , vol.11 , pp. 270-276
    • Thomas, M.L.1
  • 25
    • 0032983905 scopus 로고    scopus 로고
    • Membrane organization in immunoglobulin E receptor signaling
    • Sheets, E. D., Holowka, D. & Baird, B. Membrane organization in immunoglobulin E receptor signaling. Curr. Opin. Chem. Biol. 3, 95-99 (1999).
    • (1999) Curr. Opin. Chem. Biol. , vol.3 , pp. 95-99
    • Sheets, E.D.1    Holowka, D.2    Baird, B.3
  • 26
    • 0032498231 scopus 로고    scopus 로고
    • LAT: The ZAP-70 tyrosine kinase substrate that links T cell receptor to cellular activation
    • Zhang, W., Sloan-Lancaster, J., Kitchen, J., Trible, R. P. & Samelson, L. E. LAT: the ZAP-70 tyrosine kinase substrate that links T cell receptor to cellular activation. Cell 92, 83-92 (1998).
    • (1998) Cell , vol.92 , pp. 83-92
    • Zhang, W.1    Sloan-Lancaster, J.2    Kitchen, J.3    Trible, R.P.4    Samelson, L.E.5
  • 27
    • 0032212728 scopus 로고    scopus 로고
    • LAT is required for TCR-mediated activation of PLCgammal and the Ras pathway
    • Finco, T. S., Kadlecek, T., Zhang, W., Samelson, L. E. & Weiss, A. LAT is required for TCR-mediated activation of PLCgammal and the Ras pathway. Immunity 9, 617-626 (1998).
    • (1998) Immunity , vol.9 , pp. 617-626
    • Finco, T.S.1    Kadlecek, T.2    Zhang, W.3    Samelson, L.E.4    Weiss, A.5
  • 28
    • 0032921873 scopus 로고    scopus 로고
    • Linker for activation of T cells (LAT), a novel immunohistochemical marker for T cells, NK cells, mast cells, and megakaryocytes: Evaluation in normal and pathological conditions
    • Facchetti, F. et al. Linker for activation of T cells (LAT), a novel immunohistochemical marker for T cells, NK cells, mast cells, and megakaryocytes: evaluation in normal and pathological conditions. Am. J. Pathol. 154, 1037-1046 (1999).
    • (1999) Am. J. Pathol. , vol.154 , pp. 1037-1046
    • Facchetti, F.1
  • 29
    • 10544219605 scopus 로고    scopus 로고
    • Distinct specificity in the recognition of phosphoinositides by the pleckstrin homology domains of dynamin and Bruton's tyrosine kinase
    • Salim, K. et al. Distinct specificity in the recognition of phosphoinositides by the pleckstrin homology domains of dynamin and Bruton's tyrosine kinase. EMBO J. 15, 6241-6250 (1996).
    • (1996) EMBO J. , vol.15 , pp. 6241-6250
    • Salim, K.1
  • 30
    • 0030820924 scopus 로고    scopus 로고
    • A comparative analysis of the phosphoinositide binding specificity of pleckstrin homology domains
    • Rameh, L. E. et al. A comparative analysis of the phosphoinositide binding specificity of pleckstrin homology domains. J. Biol. Chem. 272, 22059-22066 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 22059-22066
    • Rameh, L.E.1
  • 31
    • 0030038840 scopus 로고    scopus 로고
    • Activation of BTK by a phosphorylation mechanism initiated by SRC family kinases
    • Rawlings, D. J. et al. Activation of BTK by a phosphorylation mechanism initiated by SRC family kinases. Science 271, 822-825 (1996).
    • (1996) Science , vol.271 , pp. 822-825
    • Rawlings, D.J.1
  • 32
    • 0032503687 scopus 로고    scopus 로고
    • PtdIns-3,4,5-P3: A regulatory nexus between tyrosine kinases and sustained calcium signals
    • Scharenberg, A. M. & Kinet, J. P. PtdIns-3,4,5-P3: a regulatory nexus between tyrosine kinases and sustained calcium signals. Cell 94, 5-8 (1998).
    • (1998) Cell , vol.94 , pp. 5-8
    • Scharenberg, A.M.1    Kinet, J.P.2
  • 34
    • 0028897659 scopus 로고
    • Regulation of the adapter molecule Grb2 by the FceRI in the mast cell line RBL2H3
    • Turner, H., Reif, K., Rivera, J. & Cantrell, D. A. Regulation of the adapter molecule Grb2 by the FceRI in the mast cell line RBL2H3. J. Biol. Chem. 270, 9500-9506 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 9500-9506
    • Turner, H.1    Reif, K.2    Rivera, J.3    Cantrell, D.A.4
  • 35
    • 0031002348 scopus 로고    scopus 로고
    • The role of the PH domain in the signal dependent membrane targeting of Sos
    • Chen, R., Corbalan-Garcia, S. & Bar-Sagi, D. The role of the PH domain in the signal dependent membrane targeting of Sos. EMBO J. 16, 1351-1359 (1997).
    • (1997) EMBO J. , vol.16 , pp. 1351-1359
    • Chen, R.1    Corbalan-Garcia, S.2    Bar-Sagi, D.3
  • 36
    • 0032559211 scopus 로고    scopus 로고
    • Coupling of Ras and Rac guanosine triphosphatases through the Ras exchanger Sos
    • Nimnual, A. S., Yatsula, B. A. & Bar-Sagi, D. Coupling of Ras and Rac guanosine triphosphatases through the Ras exchanger Sos. Science 279, 560-563 (1998).
    • (1998) Science , vol.279 , pp. 560-563
    • Nimnual, A.S.1    Yatsula, B.A.2    Bar-Sagi, D.3
  • 38
    • 0029658306 scopus 로고    scopus 로고
    • p95vav associates with tyrosine-phosphorylated SLP-76 in antigen-stimulated T cells
    • Tuosto, L., Michel, F. & Acuto, O. p95vav associates with tyrosine-phosphorylated SLP-76 in antigen-stimulated T cells. J. Exp. Med. 184, 1161-1166 (1996).
    • (1996) J. Exp. Med. , vol.184 , pp. 1161-1166
    • Tuosto, L.1    Michel, F.2    Acuto, O.3
  • 39
    • 0031033292 scopus 로고    scopus 로고
    • Phosphotyrosine-dependent activation of Rac-1 GDP/GTP exchange by the vav proto-oncogene product
    • Crespo, P., Schuebel, K. E., Ostrom, A. A., Gutkind, J. S. & Bustelo, X. R. Phosphotyrosine-dependent activation of Rac-1 GDP/GTP exchange by the vav proto-oncogene product. Nature 385, 169-172 (1997).
    • (1997) Nature , vol.385 , pp. 169-172
    • Crespo, P.1    Schuebel, K.E.2    Ostrom, A.A.3    Gutkind, J.S.4    Bustelo, X.R.5
  • 40
    • 0343181431 scopus 로고    scopus 로고
    • The hematopoietic-specific adaptor protein gads functions in T-cell signaling via interactions with the SLP-76 and LAT adaptors
    • Liu, S. K., Fang, N., Koretzky, G. A. & McGlade, C. J. The hematopoietic-specific adaptor protein gads functions in T-cell signaling via interactions with the SLP-76 and LAT adaptors. Curr. Biol. 9, 67-75 (1999).
    • (1999) Curr. Biol. , vol.9 , pp. 67-75
    • Liu, S.K.1    Fang, N.2    Koretzky, G.A.3    McGlade, C.J.4
  • 41
    • 0031026474 scopus 로고    scopus 로고
    • Distinct Ras effector pathways are involved in FcεRI regulation of the transcriptional activity of Elk-1 and NFAT in mast cells
    • Turner, H. & Cantrell, D. A. Distinct Ras effector pathways are involved in FcεRI regulation of the transcriptional activity of Elk-1 and NFAT in mast cells. J. Exp. Med. 185, 43-57 (1997).
    • (1997) J. Exp. Med. , vol.185 , pp. 43-57
    • Turner, H.1    Cantrell, D.A.2
  • 42
    • 0032479870 scopus 로고    scopus 로고
    • Rac-1 regulates nuclear factor of activated T cells (NFAT) C1 nuclear translocation in response to FcεRI stimulation of mast cells
    • Turner, H., Gomez, M., Mckenzie, E., Kirchem, A., Lennard, A. & Cantrell, D. Rac-1 regulates nuclear factor of activated T cells (NFAT) C1 nuclear translocation in response to FcεRI stimulation of mast cells. J. Exp. Med. 188, 527-537 (1998).
    • (1998) J. Exp. Med. , vol.188 , pp. 527-537
    • Turner, H.1    Gomez, M.2    Mckenzie, E.3    Kirchem, A.4    Lennard, A.5    Cantrell, D.6
  • 43
    • 0031571873 scopus 로고    scopus 로고
    • Involvement of the ras-like GTPase rab3d in RBL-2H3 mast cell exocytosis following stimulation via high affinity IgE receptors (Fc epsilonRI)
    • Roa, M., Paumet, F., Le Mao, J., David, B. & Blank, U. Involvement of the ras-like GTPase rab3d in RBL-2H3 mast cell exocytosis following stimulation via high affinity IgE receptors (Fc epsilonRI). J. Immunol. 159, 2815-2823 (1997).
    • (1997) J. Immunol. , vol.159 , pp. 2815-2823
    • Roa, M.1    Paumet, F.2    Le Mao, J.3    David, B.4    Blank, U.5
  • 44
    • 0032559362 scopus 로고    scopus 로고
    • Rho GTPases and the actin cytoskeleton
    • Hall, A. Rho GTPases and the actin cytoskeleton. Science 279, 509-514 (1998).
    • (1998) Science , vol.279 , pp. 509-514
    • Hall, A.1
  • 45
    • 0028982914 scopus 로고
    • Fcε RI mediated induction of nuclear factor of activated T cells
    • Hutchinson, L. & McCloskey, M. Fcε RI mediated induction of nuclear factor of activated T cells. J. Biol. Chem. 270, 16333-16338 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 16333-16338
    • Hutchinson, L.1    McCloskey, M.2
  • 46
    • 0030973579 scopus 로고    scopus 로고
    • Transcription factors of the NFAT family
    • Rao, A., Luo, C. & Hogan, P. Transcription factors of the NFAT family. Annu. Rev. Immunol. 15, 707-748 (1997).
    • (1997) Annu. Rev. Immunol. , vol.15 , pp. 707-748
    • Rao, A.1    Luo, C.2    Hogan, P.3
  • 47
    • 0032968164 scopus 로고    scopus 로고
    • Capacitative calcium entry channels
    • Putney, J. W. Jr & McKay, R. R. Capacitative calcium entry channels. BioEssays 21, 38-46 (1999).
    • (1999) BioEssays , vol.21 , pp. 38-46
    • Putney Jr., J.W.1    McKay, R.R.2
  • 48
    • 0030810066 scopus 로고    scopus 로고
    • Store depletion and calcium influx
    • Parekh, A. B. & Penner, R. Store depletion and calcium influx. Physiol. Rev. 77, 901-930 (1997).
    • (1997) Physiol. Rev. , vol.77 , pp. 901-930
    • Parekh, A.B.1    Penner, R.2
  • 49
    • 0026594980 scopus 로고
    • Depletion of intracellular calcium stores activates a calcium current in mast cells
    • Hoth, M. & Penner, R. Depletion of intracellular calcium stores activates a calcium current in mast cells. Nature 355, 353-356 (1992).
    • (1992) Nature , vol.355 , pp. 353-356
    • Hoth, M.1    Penner, R.2
  • 50
    • 0025951923 scopus 로고
    • Phosphorylation and dephosphorylation of the high affinity receptor for IgE immediately after receptor engagement and disengagement
    • Paolini, R., Jouvin, M. H. & Kinet, J. P. Phosphorylation and dephosphorylation of the high affinity receptor for IgE immediately after receptor engagement and disengagement. Nature 353, 855-858 (1991).
    • (1991) Nature , vol.353 , pp. 855-858
    • Paolini, R.1    Jouvin, M.H.2    Kinet, J.P.3
  • 51
    • 0031279370 scopus 로고    scopus 로고
    • Syk-independent tyrosine phosphorylation and association of the protein tyrosine phosphatases SHP-1 and SHP-2 with the high affinity IgE receptor
    • Kimura, T. et al. Syk-independent tyrosine phosphorylation and association of the protein tyrosine phosphatases SHP-1 and SHP-2 with the high affinity IgE receptor. J. Immunol. 159, 4426-4434 (1997).
    • (1997) J. Immunol. , vol.159 , pp. 4426-4434
    • Kimura, T.1
  • 52
    • 0030946792 scopus 로고    scopus 로고
    • The negative signaling molecule SH2 domain-containing inositol- Polyphosphate 5-phosphatase (SHIP) binds to the tyrosine-phosphorylated beta subunit of the high affinity IgE receptor
    • Kimura, T., Sakamoto, H., Appella, E. & Siraganian, R. P. The negative signaling molecule SH2 domain-containing inositol- polyphosphate 5-phosphatase (SHIP) binds to the tyrosine-phosphorylated beta subunit of the high affinity IgE receptor. J. Biol. Chem. 272, 13991-13996 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 13991-13996
    • Kimura, T.1    Sakamoto, H.2    Appella, E.3    Siraganian, R.P.4
  • 53
    • 0031964602 scopus 로고    scopus 로고
    • Tandem SH2 domains confer high specificity in tyrosine kinase signaling
    • Ottinger, E. A., Botfield, M. C. & Shoelson, S. E. Tandem SH2 domains confer high specificity in tyrosine kinase signaling. J. Biol. Chem. 273, 729-735 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 729-735
    • Ottinger, E.A.1    Botfield, M.C.2    Shoelson, S.E.3
  • 54
    • 0030604541 scopus 로고    scopus 로고
    • The Fc(epsilon)RIbeta subunit functions as an amplifier of Fc(epsilon)RIgamma-mediated cell activation signals
    • Lin, S., Cicala, C., Scharenberg, A. M. & Kinet, J. P. The Fc(epsilon)RIbeta subunit functions as an amplifier of Fc(epsilon)RIgamma-mediated cell activation signals. Cell 85, 985-995 (1996).
    • (1996) Cell , vol.85 , pp. 985-995
    • Lin, S.1    Cicala, C.2    Scharenberg, A.M.3    Kinet, J.P.4
  • 55
    • 0032034277 scopus 로고    scopus 로고
    • Allergy-associated FcRbeta is a molecular amplifier of IgE- and IgG-mediated in vivo responses
    • Dombrowicz, D. et al. Allergy-associated FcRbeta is a molecular amplifier of IgE- and IgG-mediated in vivo responses. Immunity 8, 517-529 (1998).
    • (1998) Immunity , vol.8 , pp. 517-529
    • Dombrowicz, D.1
  • 56
    • 0027459054 scopus 로고
    • Localisation of atopy and beta subunit of high-affinity IgE receptor (Fc epsilon RI) on chromosome 11q
    • Sandford, A. J. et al. Localisation of atopy and beta subunit of high-affinity IgE receptor (Fc epsilon RI) on chromosome 11q. Lancet 341, 332-334 (1993).
    • (1993) Lancet , vol.341 , pp. 332-334
    • Sandford, A.J.1
  • 57
    • 0032801811 scopus 로고    scopus 로고
    • Chromosome 11q13 and atopic asthma
    • Adra, C. et al. Chromosome 11q13 and atopic asthma. Clin. Genet. 55, 431-437 (1999).
    • (1999) Clin. Genet. , vol.55 , pp. 431-437
    • Adra, C.1
  • 58
    • 0028358985 scopus 로고
    • Association between atopy and variants of the β subunit of the high-affinity immunoglobulin E receptor
    • Shirakawa, T. et al. Association between atopy and variants of the β subunit of the high-affinity immunoglobulin E receptor. Nature Genet. 7, 125-129 (1994).
    • (1994) Nature Genet. , vol.7 , pp. 125-129
    • Shirakawa, T.1
  • 59
    • 0028979725 scopus 로고
    • Fc epsilon RI-beta polymorphism and risk of atopy in a general population sample
    • Hill, M. R. et al. Fc epsilon RI-beta polymorphism and risk of atopy in a general population sample. Br. Med. J. 311, 776-779 (1995).
    • (1995) Br. Med. J. , vol.311 , pp. 776-779
    • Hill, M.R.1
  • 60
    • 0031020466 scopus 로고    scopus 로고
    • IgE enhances mouse mast cell Fc(epsilon)RI expression in vitro and in vivo: Evidence for a novel amplification mechanism in IgE-dependent reactions
    • Yamaguchi, M. et al. IgE enhances mouse mast cell Fc(epsilon)RI expression in vitro and in vivo: evidence for a novel amplification mechanism in IgE-dependent reactions. J. Exp. Med. 185, 663-672 (1997).
    • (1997) J. Exp. Med. , vol.185 , pp. 663-672
    • Yamaguchi, M.1
  • 61
    • 0026750278 scopus 로고
    • Identification of the low affinity receptor for immunoglobulin E on mouse mast cells and macrophages as Fc gamma RII and Fc gamma RIII
    • Takizawa, F., Adamczewski, M. & Kinet, J. P. Identification of the low affinity receptor for immunoglobulin E on mouse mast cells and macrophages as Fc gamma RII and Fc gamma RIII. J. Exp. Med. 176, 469-475 (1992).
    • (1992) J. Exp. Med. , vol.176 , pp. 469-475
    • Takizawa, F.1    Adamczewski, M.2    Kinet, J.P.3
  • 62
    • 0025915405 scopus 로고
    • Characterization of truncated alpha chain products from human, rat, and mouse high affinity receptor for immunoglobulin E
    • Blank, U., Ra, C. S. & Kinet, J. P. Characterization of truncated alpha chain products from human, rat, and mouse high affinity receptor for immunoglobulin E. J. Biol. Chem. 266, 2639-2646 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 2639-2646
    • Blank, U.1    Ra, C.S.2    Kinet, J.P.3
  • 63
    • 0028118817 scopus 로고
    • Expression of functional high affinity immunoglobulin E receptors (Fc epsilon RI) on monocytes of atopic individuals
    • Maurer, D. et al. Expression of functional high affinity immunoglobulin E receptors (Fc epsilon RI) on monocytes of atopic individuals. J. Exp. Med. 179, 745-750 (1994).
    • (1994) J. Exp. Med. , vol.179 , pp. 745-750
    • Maurer, D.1
  • 64
    • 0029066660 scopus 로고
    • The high affinity IgE receptor (Fc epsilon RI) mediates IgE-dependent allergen presentation
    • Maurer, D. et al. The high affinity IgE receptor (Fc epsilon RI) mediates IgE-dependent allergen presentation. J. Immunol. 154, 6285-6290 (1995).
    • (1995) J. Immunol. , vol.154 , pp. 6285-6290
    • Maurer, D.1
  • 65
    • 0028071646 scopus 로고
    • Active anaphylaxis in IgE-deficient mice
    • Oettgen, H. C. et al. Active anaphylaxis in IgE-deficient mice. Nature 370, 367-370 (1994).
    • (1994) Nature , vol.370 , pp. 367-370
    • Oettgen, H.C.1
  • 66
    • 0033577901 scopus 로고    scopus 로고
    • Modulation of immunoglobulin (Ig)E-mediated systemic anaphylaxis by low-affinity Fc receptors for IgG
    • Ujike, A. et al. Modulation of immunoglobulin (Ig)E-mediated systemic anaphylaxis by low-affinity Fc receptors for IgG. J. Exp. Med. 189, 1573-1579 (1999).
    • (1999) J. Exp. Med. , vol.189 , pp. 1573-1579
    • Ujike, A.1


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