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Volumn 18, Issue 1, 1998, Pages 75-83

Interleukin 5 signals through Shc and Grb2 in human eosinophils

Author keywords

[No Author keywords available]

Indexed keywords

EPIDERMAL GROWTH FACTOR RECEPTOR; GRB2 PROTEIN, HUMAN; GROWTH FACTOR RECEPTOR BOUND PROTEIN 2; INTERLEUKIN 5; PHOSPHOTYROSINE; PROTEIN; SIGNAL TRANSDUCING ADAPTOR PROTEIN; SRC HOMOLOGY 2 DOMAIN CONTAINING, TRANSFORMING PROTEIN 1; SRC HOMOLOGY 2 DOMAIN-CONTAINING, TRANSFORMING PROTEIN 1; VESICULAR TRANSPORT ADAPTOR PROTEIN;

EID: 0031605365     PISSN: 10441549     EISSN: None     Source Type: Journal    
DOI: 10.1165/ajrcmb.18.1.2766     Document Type: Article
Times cited : (40)

References (65)
  • 1
    • 0025721109 scopus 로고    scopus 로고
    • Eosinophils, T-lymphocytes, mast cells, neutrophils, and macrophages in bronchial biopsy specimens from atopic subjects with asthma: Comparison with biopsy specimens from atopic subjects without asthma and normal control subjects and relationship to bronchial hyperresponsiveness
    • Bradley, B. L., M. Azzawi, M. Jacobson, B. Assoufi, J. V. Collins, A. M. A. Irani, L. B. Schwartz, S. R. Durham, P. K. Jeffery, and A. B. Kay. 1997. Eosinophils, T-lymphocytes, mast cells, neutrophils, and macrophages in bronchial biopsy specimens from atopic subjects with asthma: comparison with biopsy specimens from atopic subjects without asthma and normal control subjects and relationship to bronchial hyperresponsiveness. J. Allergy Clin, Immunol. 88:661-674.
    • (1997) J. Allergy Clin, Immunol. , vol.88 , pp. 661-674
    • Bradley, B.L.1    Azzawi, M.2    Jacobson, M.3    Assoufi, B.4    Collins, J.V.5    Irani, A.M.A.6    Schwartz, L.B.7    Durham, S.R.8    Jeffery, P.K.9    A B, K.10
  • 2
    • 0028094796 scopus 로고
    • Pulmonary function, activated t cells peripheral blood eosinophilia, and serum activity for eosinophil survival in vitro: A longitudinal study in bronchial asthma
    • Virehow, J. C., A. Oehling, L., Boer, T. T. Hansel, P. Werner, H. Matthys, K. Blaser, and C. Walker. 1994. Pulmonary function, activated T cells peripheral blood eosinophilia, and serum activity for eosinophil survival in vitro: a longitudinal study in bronchial asthma. J. Allergy Clin, Immunol 94: 240-244.
    • (1994) J. Allergy Clin, Immunol , vol.94 , pp. 240-244
    • Virehow, J.C.1    Oehling, A.2    Boer, L.3    Hansel, T.T.4    Werner, P.5    Matthys, H.6    Blaser, K.7    Walker, C.8
  • 3
    • 0023785820 scopus 로고
    • Human eosinophils derived major basic protein causes hyperreactivity of respiratory smooth muscle: Role of the epithelium
    • Flavahan, N. A., N. R. Silfman, G. J. Gleich, and P. M. Vanhoutte. 1988. Human eosinophils derived major basic protein causes hyperreactivity of respiratory smooth muscle: role of the epithelium. Am. Rev. Respir. Dis. 138:685-688.
    • (1988) Am. Rev. Respir. Dis. , vol.138 , pp. 685-688
    • Flavahan, N.A.1    Silfman, N.R.2    Gleich, G.J.3    Vanhoutte, P.M.4
  • 5
    • 0027490363 scopus 로고
    • Eosinophil survival activity identified as interleukin-5 is associated with eosinophil recruitment and degranulation and lung injury twenty-four hours after segmental antigen lung challenge
    • Ohnishi, T., S. Sur, D. S. Collins, J. E. Fish, G. J. Gleich, and S. P. Peters. 1993. Eosinophil survival activity identified as interleukin-5 is associated with eosinophil recruitment and degranulation and lung injury twenty-four hours after segmental antigen lung challenge. J. Allergy Clin. Immunol. 92:607-615.
    • (1993) J. Allergy Clin. Immunol. , vol.92 , pp. 607-615
    • Ohnishi, T.1    Sur, S.2    Collins, D.S.3    Fish, J.E.4    Gleich, G.J.5    Peters, S.P.6
  • 7
    • 0030028768 scopus 로고    scopus 로고
    • Interleukin 5 deficiency abolishes eosinophilia, airway hyperreactivity, and lung damage in a mouse asthma model
    • Foster, P. S., S. P. Hogan, A. J. Ramsay, K. I. Matthaei, and I. G. Young, 1996. Interleukin 5 deficiency abolishes eosinophilia, airway hyperreactivity, and lung damage in a mouse asthma model. J. Exp. Med. 183:195-201.
    • (1996) J. Exp. Med. , vol.183 , pp. 195-201
    • Foster, P.S.1    Hogan, S.P.2    Ramsay, A.J.3    Matthaei, K.I.4    Young, I.G.5
  • 8
    • 0024591512 scopus 로고
    • Human interleukin-5 (IL-5) regulates the production of eosinophils in human bone marrow cultures: Comparison and interaction with IL-1, IL-3. IL-6. And GMCSF
    • Clutterbuck, E. J., E. M. Hirst, and C. J. Sanderson. 1989. Human interleukin-5 (IL-5) regulates the production of eosinophils in human bone marrow cultures: comparison and interaction with IL-1, IL-3. IL-6. and GMCSF. Blood 73:1504-1512.
    • (1989) Blood , vol.73 , pp. 1504-1512
    • Clutterbuck, E.J.1    Hirst, E.M.2    Sanderson, C.J.3
  • 9
    • 0024508145 scopus 로고
    • Humoral regulation of eosinophilopoiesis in vitro: Analysis of the targets of interleukin-3, granulocyte/ macrophage colony-stimulating factor (GM-CSF), and interleukin-5
    • Sonoda, Y., N. Arai, and M. Ogawa. 1989. Humoral regulation of eosinophilopoiesis in vitro: analysis of the targets of interleukin-3, granulocyte/ macrophage colony-stimulating factor (GM-CSF), and interleukin-5. Leukemia 3:14-18.
    • (1989) Leukemia , vol.3 , pp. 14-18
    • Sonoda, Y.1    Arai, N.2    Ogawa, M.3
  • 11
    • 0027613602 scopus 로고
    • Selective regulation of expression of surface adhesion molecules Mac-1, L-selectin, and VLA-4 on human eosinophils and neutrophils
    • Neeley, S. P., K. J. Hamann, S. R. White, S. I., Baranowski, R. A. Burch, and A. R. Leff. 1993. Selective regulation of expression of surface adhesion molecules Mac-1, L-selectin, and VLA-4 on human eosinophils and neutrophils. Am. J. Respir. Cell Mol. Biol. 8:633-639.
    • (1993) Am. J. Respir. Cell Mol. Biol. , vol.8 , pp. 633-639
    • Neeley, S.P.1    Hamann, K.J.2    White, S.R.3    Baranowski, S.I.4    Burch, R.A.5    Leff, A.R.6
  • 12
    • 0025169452 scopus 로고
    • IL-5 enhances the in vitro adhesion of human eosinophils, but not neutrophils, in a leukocyte integrin (CD11/18)-dependent manner
    • Walsh, G. M., A. Hartnell, A. J. Wardlaw, K. Kurihara, C. J. Sanderson, and A. B. Kay. 1990. IL-5 enhances the in vitro adhesion of human eosinophils, but not neutrophils, in a leukocyte integrin (CD11/18)-dependent manner. Immunology 71:258-265.
    • (1990) Immunology , vol.71 , pp. 258-265
    • Walsh, G.M.1    Hartnell, A.2    Wardlaw, A.J.3    Kurihara, K.4    Sanderson, C.J.5    Kay, A.B.6
  • 13
  • 14
    • 0027507513 scopus 로고
    • CD69 is expressed by human eosinophils activated in vivo in asthma and in vitro by cytokines
    • Hartnell, A., D. S. Robinson, A. B. Kay, and A. J. Wardlaw. 1993. CD69 is expressed by human eosinophils activated in vivo in asthma and in vitro by cytokines, Immunology 80:281-286.
    • (1993) Immunology , vol.80 , pp. 281-286
    • Hartnell, A.1    Robinson, D.S.2    Kay, A.B.3    Wardlaw, A.J.4
  • 15
    • 0028279480 scopus 로고
    • Modulation of the enhanced migration of eosinophils from the airways of sensitized guinea pigs: Role of IL-5
    • Coeffier, E., D. Joseph, and B. B. Vargaftig. 1994. Modulation of the enhanced migration of eosinophils from the airways of sensitized guinea pigs: role of IL-5. Ann. N. Y. Acad. Sci. 725:274-281.
    • (1994) Ann. N. Y. Acad. Sci. , vol.725 , pp. 274-281
    • Coeffier, E.1    Joseph, D.2    Vargaftig, B.B.3
  • 16
    • 0028040933 scopus 로고
    • Eosinophil transendothelial migration induced by cytokines: III. Effect of the chemokine RANTES
    • Ebisawa, M., T. Yamada, C. Bickel, D. Klunk, and R. P. Schleimer. 1994. Eosinophil transendothelial migration induced by cytokines: III. Effect of the chemokine RANTES. J. Immunol. 153:2153-2160.
    • (1994) J. Immunol. , vol.153 , pp. 2153-2160
    • Ebisawa, M.1    Yamada, T.2    Bickel, C.3    Klunk, D.4    Schleimer, R.P.5
  • 17
    • 0027264467 scopus 로고
    • The influence of IL-3. IL-5. And GM-CSF on normal human eosinophil and neutrophil C3b-induced degranulation
    • Carlson, M., C. Peterson, and P. Venge. 1993. The influence of IL-3. IL-5. and GM-CSF on normal human eosinophil and neutrophil C3b-induced degranulation. Allergy 48:437-442.
    • (1993) Allergy , vol.48 , pp. 437-442
    • Carlson, M.1    Peterson, C.2    Venge, P.3
  • 21
    • 0025838711 scopus 로고
    • IL-3 and IL-5 prime normal human eosinophils to produce leukotriene C4 in response to soluble agonists
    • Takafuji, S., S. C. Bischoff, A. L. De Week, and C. A. Dahinden. 1991. IL-3 and IL-5 prime normal human eosinophils to produce leukotriene C4 in response to soluble agonists. J. Immunol. 147:3855-3861.
    • (1991) J. Immunol. , vol.147 , pp. 3855-3861
    • Takafuji, S.1    Bischoff, S.C.2    De Week, A.L.3    Dahinden, C.A.4
  • 22
    • 0026580593 scopus 로고
    • Apoptosis in human eosinophils: Programmed cell death in the eosinophil leads to phagocytosis by macrophages and is modulated by IL-5
    • Stern, M., L. Meagher, J. Savill, and C. Haslett. 1992. Apoptosis in human eosinophils: programmed cell death in the eosinophil leads to phagocytosis by macrophages and is modulated by IL-5. J. Immunol. 148:3543-3549.
    • (1992) J. Immunol. , vol.148 , pp. 3543-3549
    • Stern, M.1    Meagher, L.2    Savill, J.3    Haslett, C.4
  • 25
    • 0026317315 scopus 로고
    • Interleukin-5, interleukin-3, and granulocyte-macrophage colony-stimulating factor cross-compete for binding to cell surface receptors on human eosinophils
    • Lopez, A. F., M. A. Vadas, J. M. Woodcock, S. E. Milton, A. Lewis, M. J. Elliott, D. Gillis, R. Ireland, E. Olwell, and L. S. Park. 1991. Interleukin-5, interleukin-3, and granulocyte-macrophage colony-stimulating factor cross-compete for binding to cell surface receptors on human eosinophils. J. Biol. Chem. 266:24741-24747.
    • (1991) J. Biol. Chem. , vol.266 , pp. 24741-24747
    • Lopez, A.F.1    Vadas, M.A.2    Woodcock, J.M.3    Milton, S.E.4    Lewis, A.5    Elliott, M.J.6    Gillis, D.7    Ireland, R.8    Olwell, E.9    Park, L.S.10
  • 26
    • 0025821280 scopus 로고
    • Characterization of a receptor for interleukin-5 on human eosinophils and the myeloid leukemia line HL-60
    • Ingley, E., and I. G. Young. 1991. Characterization of a receptor for interleukin-5 on human eosinophils and the myeloid leukemia line HL-60. Blood 78:339-344.
    • (1991) Blood , vol.78 , pp. 339-344
    • Ingley, E.1    Young, I.G.2
  • 28
    • 0028956998 scopus 로고
    • The intracellular signal transduction mechanism of interleukin 5 in eosinophils: The involvement of lyn tyrosine kinase and the Ras-Raf-1-MEK-microtubule-associated protein kinase pathway
    • Pazdrak, K., D. Schreiber, P. Forsythe, L. Justement, and R. Alam. 1995. The intracellular signal transduction mechanism of interleukin 5 in eosinophils: the involvement of lyn tyrosine kinase and the Ras-Raf-1-MEK-microtubule-associated protein kinase pathway. J. Exp. Med. 181:1827-1834.
    • (1995) J. Exp. Med. , vol.181 , pp. 1827-1834
    • Pazdrak, K.1    Schreiber, D.2    Forsythe, P.3    Justement, L.4    Alam, R.5
  • 29
    • 0029058148 scopus 로고
    • The activation of the Jak-STAT 1 signaling pathway by IL-5 in eosinophils
    • Pazdrak, K., S. Stafford, and R. Alam. 1995. The activation of the Jak-STAT 1 signaling pathway by IL-5 in eosinophils. J. Immunol. 155:397-402.
    • (1995) J. Immunol. , vol.155 , pp. 397-402
    • Pazdrak, K.1    Stafford, S.2    Alam, R.3
  • 30
    • 0030030916 scopus 로고    scopus 로고
    • IL-5 activates a 45-kilo-dalton mitogen-activated protein kinase and Jak-2 tyrosine kinase in human eosinophils
    • Bates, M. E., P. J. Bertics, and W. W. Busse. 1996. IL-5 activates a 45-kilo-dalton mitogen-activated protein kinase and Jak-2 tyrosine kinase in human eosinophils. J. Immunol. 156:711-718.
    • (1996) J. Immunol. , vol.156 , pp. 711-718
    • Bates, M.E.1    Bertics, P.J.2    Busse, W.W.3
  • 31
    • 0028234529 scopus 로고
    • Jak-STAT pathways and transcriptional activation in response to IFNs and other extracellular signaling proteins
    • Darnell, J. E., Jr., I. M. Kerr, and G. R. Stark. 1994. Jak-STAT pathways and transcriptional activation in response to IFNs and other extracellular signaling proteins (Review). Science 264:1415-1421.
    • (1994) Science , vol.264 , pp. 1415-1421
    • Darnell J.E., Jr.1    Kerr, I.M.2    Stark, G.R.3
  • 34
    • 0028944585 scopus 로고
    • Growth hormone-promoted tyrosyl phosphorylation of SHC proteins and SHC association with Grb2
    • VanderKuur, J., G. Allevato, N. Billestrup, G. Norstedt, and C. Carter-Su. 1995. Growth hormone-promoted tyrosyl phosphorylation of SHC proteins and SHC association with Grb2. J. Biol. Chem. 270:7587-7593.
    • (1995) J. Biol. Chem. , vol.270 , pp. 7587-7593
    • VanderKuur, J.1    Allevato, G.2    Billestrup, N.3    Norstedt, G.4    Carter-Su, C.5
  • 35
    • 0028901649 scopus 로고
    • Tyrosine phosphorylation of She is mediated through Lyn and Syk in B cell receptor signaling
    • Nagai, K., M. Takata, H. Yamamura, and T. Kurosaki. 1995. Tyrosine phosphorylation of She is mediated through Lyn and Syk in B cell receptor signaling. J. Biol. Chem. 270:6824-6829.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6824-6829
    • Nagai, K.1    Takata, M.2    Yamamura, H.3    Kurosaki, T.4
  • 36
    • 0029148780 scopus 로고
    • G protein-coupled chemoattractant receptors regulate Lyn tyrosine kinase: She adapter protein signaling complexes
    • Ptasznik, A., A. Traynor-Kaplan, and G. M. Bokoch. 1995. G protein-coupled chemoattractant receptors regulate Lyn tyrosine kinase: She adapter protein signaling complexes. J. Biol. Chem. 270:19969-19973.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19969-19973
    • Ptasznik, A.1    Traynor-Kaplan, A.2    Bokoch, G.M.3
  • 37
    • 0028876287 scopus 로고
    • Src homologous and collagen (She) protein binds to F-actin and translocates to the cytoskeleton upon nerve growth factor stimulation in PC12 cells
    • Thomas, D., S. D. Patterson, and R. A. Bradshaw. 1995. Src homologous and collagen (She) protein binds to F-actin and translocates to the cytoskeleton upon nerve growth factor stimulation in PC12 cells. J. Biol. Chem. 270:28924-28931.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28924-28931
    • Thomas, D.1    Patterson, S.D.2    Bradshaw, R.A.3
  • 38
    • 0029124755 scopus 로고
    • Binding of She to the NPXY motif is mediated by its N-terminal domain
    • Prigent, S. A., T. S. Pillay, K. S. Ravichandran, and W. J. Gullick. 1995. Binding of She to the NPXY motif is mediated by its N-terminal domain. J. Biol. Chem. 270:22097-22100.
    • (1995) J. Biol. Chem. , vol.270 , pp. 22097-22100
    • Prigent, S.A.1    Pillay, T.S.2    Ravichandran, K.S.3    Gullick, W.J.4
  • 40
    • 0027153103 scopus 로고
    • Epidermal growth factor regulates p21ras through the formation of a complex of receptor, Grb2 adapter protein, and Sos nucleotide exchange factor
    • Buday, L., and J. Downward. 1993. Epidermal growth factor regulates p21ras through the formation of a complex of receptor, Grb2 adapter protein, and Sos nucleotide exchange factor. Cell 73:611-620.
    • (1993) Cell , vol.73 , pp. 611-620
    • Buday, L.1    Downward, J.2
  • 41
    • 0027294981 scopus 로고
    • The SH2 and SH3 domains of mammalian Grb2 couple the EGF receptor to the ras activator msos1
    • Rozakis-Adcock, M., R. Fernley, J. Wade, T. Pawson, and D. Bowtell, 1993. The SH2 and SH3 domains of mammalian Grb2 couple the EGF receptor to the Ras activator mSos1 (see comments), Nature (London) 363:83-85.
    • (1993) Nature (London) , vol.363 , pp. 83-85
    • Rozakis-Adcock, M.1    Fernley, R.2    Wade, J.3    Pawson, T.4    Bowtell, D.5
  • 43
    • 0026523559 scopus 로고
    • Ras mediates nerve growth factor receptor modulation of three signal-transducing protein kinases: MAP kinase. Raf-1. and RSK
    • Wood, K. W., C. Sarnecki, T. M. Roberts, and J. Blenis. 1992. Ras mediates nerve growth factor receptor modulation of three signal-transducing protein kinases: MAP kinase. Raf-1. and RSK. Cell 68:1041-1050.
    • (1992) Cell , vol.68 , pp. 1041-1050
    • Wood, K.W.1    Sarnecki, C.2    Roberts, T.M.3    Blenis, J.4
  • 44
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 277:680-685.
    • (1970) Nature (London) , vol.277 , pp. 680-685
    • Laemmli, U.K.1
  • 45
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., T. Staehelin, and J. Gordon. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76:4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 46
    • 0028123081 scopus 로고
    • Multiple hemopoietins, with the exception of interleukin-4, induce modification of She and mSOS-1. But not their translocation
    • Welham, M. J., V. Duronio, K. B. Leslie, D. Bowtell, and J. W. Schrader. 1994. Multiple hemopoietins, with the exception of interleukin-4, induce modification of She and mSOS-1. but not their translocation. J. Biol. Chem, 269:21165-21176.
    • (1994) J. Biol. Chem , vol.269 , pp. 21165-21176
    • Welham, M.J.1    Duronio, V.2    Leslie, K.B.3    Bowtell, D.4    Schrader, J.W.5
  • 47
    • 0028046579 scopus 로고
    • Platelet-derived growth factor stimulates phosphorylation of growth factor receptor-binding protein-2 in vascular smooth muscle cells
    • Benjamin, C. W., D. A. Linseman, and D. A. Jones. 1994. Platelet-derived growth factor stimulates phosphorylation of growth factor receptor-binding protein-2 in vascular smooth muscle cells. J. Biol. Chem. 269:31346-31349.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31346-31349
    • Benjamin, C.W.1    Linseman, D.A.2    Jones, D.A.3
  • 48
    • 13344278677 scopus 로고    scopus 로고
    • Interaction between the phosphotyrosine binding domain of She and the insulin receptor is required for She phosphorylation by insulin in vivo
    • Isakoff, S. J., Y. P. Yu, Y. C. Su, P. Blaikie, V. Yajnik, E. Rose, K. M. Weidner, M. Sachs, B. Margolis, and E. Y. Skolnik. 1996. Interaction between the phosphotyrosine binding domain of She and the insulin receptor is required for She phosphorylation by insulin in vivo. J. Biol. Chem. 271: 3959-3962.
    • (1996) J. Biol. Chem. , vol.271 , pp. 3959-3962
    • Isakoff, S.J.1    Yu, Y.P.2    Su, Y.C.3    Blaikie, P.4    Yajnik, V.5    Rose, E.6    Weidner, K.M.7    Sachs, M.8    Margolis, B.9    Skolnik, E.Y.10
  • 50
    • 0027144454 scopus 로고
    • Evidence for the potentiation of epidermal growth factor receptor tyrosine kinase activity by association with the detergent-insoluble cellular cytoskeleton: Analysis of intact and carboxy-terminally truncated receptors
    • Gronowski, A. M., and P. J. Bertics. 1993. Evidence for the potentiation of epidermal growth factor receptor tyrosine kinase activity by association with the detergent-insoluble cellular cytoskeleton: analysis of intact and carboxy-terminally truncated receptors. Endocrinology 133:2838-2846.
    • (1993) Endocrinology , vol.133 , pp. 2838-2846
    • Gronowski, A.M.1    Bertics, P.J.2
  • 51
    • 0029130717 scopus 로고
    • She isoform-specific tyrosine phosphorylation by the insulin and epidermal growth factor receptors
    • Okada, S., K. Yamauchi, and J. E. Pessin. 1995. She isoform-specific tyrosine phosphorylation by the insulin and epidermal growth factor receptors. J. Biol. Chem. 270:20737-20741.
    • (1995) J. Biol. Chem. , vol.270 , pp. 20737-20741
    • Okada, S.1    Yamauchi, K.2    Pessin, J.E.3
  • 52
    • 0029045242 scopus 로고
    • Erythropoietin-induced recruitment of She via a receptor phosphotyrosine-independent. Jak2-associated pathway
    • He, T. C., N. Jiang, H. Zhuang, and D. M. Wojchowski. 1995. Erythropoietin-induced recruitment of She via a receptor phosphotyrosine-independent. Jak2-associated pathway. J. Biol. Chem. 270:11055-11061.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11055-11061
    • He, T.C.1    Jiang, N.2    Zhuang, H.3    Wojchowski, D.M.4
  • 53
    • 0028938419 scopus 로고
    • V-Abl-mediated apoptotic suppression is associated with shc phosphorylation without concomitant mitogen-activated protein kinase activation
    • Owen-Lynch, P. J., A. K. Wong, and A. D. Whetton. 1995. v-Abl-mediated apoptotic suppression is associated with SHC phosphorylation without concomitant mitogen-activated protein kinase activation. J. Biol. Chem. 270:5956-5962.
    • (1995) J. Biol. Chem. , vol.270 , pp. 5956-5962
    • Owen-Lynch, P.J.1    Wong, A.K.2    Whetton, A.D.3
  • 54
    • 0029127179 scopus 로고
    • Signal transduction by a CD16/ CD7/Jak2 fusion protein
    • Sakai, I., L. Nabell, and A. S. Kraft. 1995. Signal transduction by a CD16/ CD7/Jak2 fusion protein. J. Biol. Chem. 270:18420-18427.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18420-18427
    • Sakai, I.1    Nabell, L.2    Kraft, A.S.3
  • 55
    • 0026483357 scopus 로고
    • Function of Ras as a molecular switch in signal transduction
    • Satoh, T., M. Nakafuku, and Y. Kaziro. 1992. Function of Ras as a molecular switch in signal transduction (Review). J. Biol. Chem. 267:24149-24152.
    • (1992) J. Biol. Chem. , vol.267 , pp. 24149-24152
    • Satoh, T.1    Nakafuku, M.2    Kaziro, Y.3
  • 56
  • 57
    • 0028968362 scopus 로고
    • Overexpression of She proteins potentiates the proliferative response to the granulocyte-macrophage colony-stimulating factor and recruitment of Grb2/SoS and Grb2/p140 complexes to the beta receptor subunit
    • Lanfrancone, L., G. Pelicci, M. F. Brizzi, M. G. Arouica, C. Casciari, S. Giuli, L. Pegoraro, T. Pawson, and P. G. Pelicci. 1995. Overexpression of She proteins potentiates the proliferative response to the granulocyte-macrophage colony-stimulating factor and recruitment of Grb2/SoS and Grb2/p140 complexes to the beta receptor subunit. Oncogene 10:907-917.
    • (1995) Oncogene , vol.10 , pp. 907-917
    • Lanfrancone, L.1    Pelicci, G.2    Brizzi, M.F.3    Arouica, M.G.4    Casciari, C.5    Giuli, S.6    Pegoraro, L.7    Pawson, T.8    Pelicci, P.G.9
  • 58
    • 0027485538 scopus 로고
    • Multiple cytokines induce the tyrosine phosphorylation of She and its association with Grb2 in hemopoietic cells
    • Cutler, R. L., L. Liu, J. E. Damen, and G. Krystal. 1993. Multiple cytokines induce the tyrosine phosphorylation of She and its association with Grb2 in hemopoietic cells. J. Biol. Chem. 268:21463-21465.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21463-21465
    • Cutler, R.L.1    Liu, L.2    Damen, J.E.3    Krystal, G.4
  • 59
    • 0028041512 scopus 로고
    • Multiple cytokines stimulate the binding of a common 145-kilodalton protein to She at the Grb2 recognition site of She
    • Liu, L., J. E. Damen, R. L. Cutler, and G. Krystal. 1994. Multiple cytokines stimulate the binding of a common 145-kilodalton protein to She at the Grb2 recognition site of She. Mol. Cell. Biol. 14:6926-6935.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 6926-6935
    • Liu, L.1    Damen, J.E.2    Cutler, R.L.3    Krystal, G.4
  • 62
    • 0027296646 scopus 로고
    • Molecular cloning, expression, and characterization of the human mitogen-activated protein kinase p44erk1
    • Charest, D. L., G. Mordret, K. W. Harder, F. Jirik, and S. L. Pelech, 1993. Molecular cloning, expression, and characterization of the human mitogen-activated protein kinase p44erk1. Mol. Cell. Biol. 13:4679-4690.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 4679-4690
    • Charest, D.L.1    Mordret, G.2    Harder, K.W.3    Jirik, F.4    Pelech, S.L.5
  • 64
    • 0028932435 scopus 로고
    • Association of phosphatidylinositol 3-kinase with She in chronic myelogenous leukemia cells
    • Harrison-Findik, D., M. Susa, and L. Varticovski. 1995. Association of phosphatidylinositol 3-kinase with She in chronic myelogenous leukemia cells. Oncogene 10:1385-1391.
    • (1995) Oncogene , vol.10 , pp. 1385-1391
    • Harrison-Findik, D.1    Susa, M.2    Varticovski, L.3
  • 65
    • 0029902217 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of She is not required for proliferation or viability signaling by granulocyte-macrophage colony-stimulating factor in hematopoietic cell lines
    • Durstin, M., R. C. Inhorn, and J. D. Griffin. 1996. Tyrosine phosphorylation of She is not required for proliferation or viability signaling by granulocyte-macrophage colony-stimulating factor in hematopoietic cell lines. J. Immunol. 157:534-540.
    • (1996) J. Immunol. , vol.157 , pp. 534-540
    • Durstin, M.1    Inhorn, R.C.2    Griffin, J.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.