메뉴 건너뛰기




Volumn 71, Issue , 2005, Pages 321-344

Cytokine Recognition by Human Interleukin 5 Receptor

Author keywords

[No Author keywords available]

Indexed keywords

CYTOKINE; DISULFIDE; EPITOPE; IL5RA PROTEIN, HUMAN; INTERLEUKIN 5; INTERLEUKIN 5 RECEPTOR; INTERLEUKIN 5 RECEPTOR ALPHA; INTERLEUKIN RECEPTOR; PEPTIDE LIBRARY;

EID: 27744453929     PISSN: 00836729     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0083-6729(05)71011-6     Document Type: Review
Times cited : (8)

References (72)
  • 1
    • 0031671711 scopus 로고    scopus 로고
    • The mechanism of IL-5 signal transduction
    • Adachi T., and Alam R. The mechanism of IL-5 signal transduction. Am. J. Physiol. 275 (1998) C623-C633
    • (1998) Am. J. Physiol. , vol.275
    • Adachi, T.1    Alam, R.2
  • 2
    • 0033083258 scopus 로고    scopus 로고
    • The mapping of the Lyn kinase binding site of the common beta subunit of IL-3/granulocyte-macrophage colony-stimulating factor/IL-5 receptor
    • Adachi T., Pazdrak K., Stafford S., and Alam R. The mapping of the Lyn kinase binding site of the common beta subunit of IL-3/granulocyte-macrophage colony-stimulating factor/IL-5 receptor. J. Immunol. 162 (1999) 1496-1501
    • (1999) J. Immunol. , vol.162 , pp. 1496-1501
    • Adachi, T.1    Pazdrak, K.2    Stafford, S.3    Alam, R.4
  • 3
    • 0033565287 scopus 로고    scopus 로고
    • A novel Lyn-binding peptide inhibitor blocks eosinophil differentiation, survival, and airway eosinophilic inflammation
    • Adachi T., Stafford S., Sur S., and Alam R. A novel Lyn-binding peptide inhibitor blocks eosinophil differentiation, survival, and airway eosinophilic inflammation. J. Immunol. 163 (1999) 939-946
    • (1999) J. Immunol. , vol.163 , pp. 939-946
    • Adachi, T.1    Stafford, S.2    Sur, S.3    Alam, R.4
  • 4
    • 0029059051 scopus 로고
    • The interleukin-5/receptor interaction activates Lyn and Jak2 tyrosine kinases and propagates signals via the Ras-Raf-1-MAP kinase and the Jak-STAT pathways in eosinophils
    • Alam R., Pazdrak K., Stafford S., and Forsythe P. The interleukin-5/receptor interaction activates Lyn and Jak2 tyrosine kinases and propagates signals via the Ras-Raf-1-MAP kinase and the Jak-STAT pathways in eosinophils. Int. Arch. Allergy Immunol. 107 (1995) 226-227
    • (1995) Int. Arch. Allergy Immunol. , vol.107 , pp. 226-227
    • Alam, R.1    Pazdrak, K.2    Stafford, S.3    Forsythe, P.4
  • 5
    • 0014800819 scopus 로고
    • Mechanism of eosinophilia. II. Role of the lymphocyte
    • Basten A., and Beeson P.B. Mechanism of eosinophilia. II. Role of the lymphocyte. J. Exp. Med. 131 (1970) 1288-1305
    • (1970) J. Exp. Med. , vol.131 , pp. 1288-1305
    • Basten, A.1    Beeson, P.B.2
  • 6
    • 0028052289 scopus 로고
    • The role of the WSXWS equivalent motif in growth hormone receptor function
    • Baumgartner J.W., Wells C.A., Chen C.M., and Waters M.J. The role of the WSXWS equivalent motif in growth hormone receptor function. J. Biol. Chem. 269 (1994) 29094-29101
    • (1994) J. Biol. Chem. , vol.269 , pp. 29094-29101
    • Baumgartner, J.W.1    Wells, C.A.2    Chen, C.M.3    Waters, M.J.4
  • 7
    • 0025162844 scopus 로고
    • Structural design and molecular evolution of a cytokine receptor superfamily
    • Bazan J.F. Structural design and molecular evolution of a cytokine receptor superfamily. Proc. Natl. Acad. Sci. USA 87 (1990) 6934-6938
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 6934-6938
    • Bazan, J.F.1
  • 8
    • 0038609651 scopus 로고    scopus 로고
    • Hexameric structure and assembly of the interleukin-6/IL-6 alpha-receptor/gp130 complex
    • Boulanger M.J., Chow D.C., Brevnova E.E., and Garcia K.C. Hexameric structure and assembly of the interleukin-6/IL-6 alpha-receptor/gp130 complex. Science 300 (2003) 2101-2104
    • (2003) Science , vol.300 , pp. 2101-2104
    • Boulanger, M.J.1    Chow, D.C.2    Brevnova, E.E.3    Garcia, K.C.4
  • 9
    • 17744386517 scopus 로고    scopus 로고
    • Structure of the complete extracellular domain of the common beta subunit of the human GM-CSF, IL-3, and IL-5 receptors reveals a novel dimer configuration
    • Carr P.D., Gustin S.E., Church A.P., Murphy J.M., Ford S.C., Mann D.A., Woltring D.M., Walker I., Ollis D.L., and Young I.G. Structure of the complete extracellular domain of the common beta subunit of the human GM-CSF, IL-3, and IL-5 receptors reveals a novel dimer configuration. Cell 104 (2001) 291-300
    • (2001) Cell , vol.104 , pp. 291-300
    • Carr, P.D.1    Gustin, S.E.2    Church, A.P.3    Murphy, J.M.4    Ford, S.C.5    Mann, D.A.6    Woltring, D.M.7    Walker, I.8    Ollis, D.L.9    Young, I.G.10
  • 12
    • 0024410891 scopus 로고
    • Antibody to interleukin-5 inhibits helminth-induced eosinophilia in mice
    • Coffman R.L., Seymour B.W., Hudak S., Jackson J., and Rennick D. Antibody to interleukin-5 inhibits helminth-induced eosinophilia in mice. Science 245 (1989) 308-310
    • (1989) Science , vol.245 , pp. 308-310
    • Coffman, R.L.1    Seymour, B.W.2    Hudak, S.3    Jackson, J.4    Rennick, D.5
  • 13
    • 0028999993 scopus 로고
    • Characterization of critical residues in the cytoplasmic domain of the human interleukin-5 receptor alpha chain required for growth signal transduction
    • Cornelis S., Fache I., Van der Heyden J., Guisez Y., Tavernier J., Devos R., Fiers W., and Plaetinck G. Characterization of critical residues in the cytoplasmic domain of the human interleukin-5 receptor alpha chain required for growth signal transduction. Eur. J. Immunol. 7 (1995) 1857-1864
    • (1995) Eur. J. Immunol. , vol.7 , pp. 1857-1864
    • Cornelis, S.1    Fache, I.2    Van der Heyden, J.3    Guisez, Y.4    Tavernier, J.5    Devos, R.6    Fiers, W.7    Plaetinck, G.8
  • 14
    • 0026598960 scopus 로고
    • Human growth hormone and extracellular domain of its receptor: Crystal structure of the complex
    • de Vos A.M., Ultsch M., and Kossiakoff A.A. Human growth hormone and extracellular domain of its receptor: Crystal structure of the complex. Science 255 (1992) 306-312
    • (1992) Science , vol.255 , pp. 306-312
    • de Vos, A.M.1    Ultsch, M.2    Kossiakoff, A.A.3
  • 16
    • 0030062246 scopus 로고    scopus 로고
    • Creation of a biologically active interleukin-5
    • Dickason R.R., and Huston D.P. Creation of a biologically active interleukin-5. Nature 379 (1996) 652-655
    • (1996) Nature , vol.379 , pp. 652-655
    • Dickason, R.R.1    Huston, D.P.2
  • 21
    • 0026764441 scopus 로고
    • Rational design of potent antagonists to the human growth hormone receptor
    • Fuh G., Cunningham B.C., Fukunaga R., Nagata S., Goeddel D.V., and Wells J.A. Rational design of potent antagonists to the human growth hormone receptor. Science 256 (1992) 1677-1680
    • (1992) Science , vol.256 , pp. 1677-1680
    • Fuh, G.1    Cunningham, B.C.2    Fukunaga, R.3    Nagata, S.4    Goeddel, D.V.5    Wells, J.A.6
  • 23
    • 0027401966 scopus 로고
    • A model for the interaction of the GM-CSF, IL-3 and IL-5 receptors with their ligands
    • Goodall G.J., Bagley C.J., Vadas M.A., and Lopez A.F. A model for the interaction of the GM-CSF, IL-3 and IL-5 receptors with their ligands. Growth Factors 8 (1993) 87-97
    • (1993) Growth Factors , vol.8 , pp. 87-97
    • Goodall, G.J.1    Bagley, C.J.2    Vadas, M.A.3    Lopez, A.F.4
  • 25
    • 0025982014 scopus 로고
    • In vivo administration of antibody to murine IL-5 receptor inhibits eosinophilia of IL-5 transgenic mice
    • Hitoshi Y., Yamaguchi N., Korenaga M., Mita S., Tominaga A., and Takatsu K. In vivo administration of antibody to murine IL-5 receptor inhibits eosinophilia of IL-5 transgenic mice. Int. Immunol. 3 (1991) 135-139
    • (1991) Int. Immunol. , vol.3 , pp. 135-139
    • Hitoshi, Y.1    Yamaguchi, N.2    Korenaga, M.3    Mita, S.4    Tominaga, A.5    Takatsu, K.6
  • 26
    • 1542304706 scopus 로고    scopus 로고
    • Kinetic interaction analysis of human interleukin 5 receptor alpha mutants reveals a unique binding topology and charge distribution for cytokine recognition
    • Ishino T., Pasut G., Scibek J., and Chaiken I. Kinetic interaction analysis of human interleukin 5 receptor alpha mutants reveals a unique binding topology and charge distribution for cytokine recognition. J. Biol. Chem. 279 (2004) 9547-9556
    • (2004) J. Biol. Chem. , vol.279 , pp. 9547-9556
    • Ishino, T.1    Pasut, G.2    Scibek, J.3    Chaiken, I.4
  • 27
    • 0031931409 scopus 로고    scopus 로고
    • Definition of the role of tyrosine residues of the common beta subunit regulating multiple signaling pathways of granulocyte-macrophage colony-stimulating factor receptor
    • Itoh T., Liu R., Yokota T., Arai K.I., and Watanabe S. Definition of the role of tyrosine residues of the common beta subunit regulating multiple signaling pathways of granulocyte-macrophage colony-stimulating factor receptor. Mol. Cell. Biol. 18 (1998) 742-752
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 742-752
    • Itoh, T.1    Liu, R.2    Yokota, T.3    Arai, K.I.4    Watanabe, S.5
  • 29
    • 0034944334 scopus 로고    scopus 로고
    • Hematopoietic growth factor mimetics
    • Kaushansky K. Hematopoietic growth factor mimetics. Ann. NY Acad. Sci. 938 (2001) 131-138
    • (2001) Ann. NY Acad. Sci. , vol.938 , pp. 131-138
    • Kaushansky, K.1
  • 30
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • 51-55.
    • Koradi R., Billeter M., and Wuthrich K. MOLMOL: A program for display and analysis of macromolecular structures. J. Mol. Graph 14 (1996) 29-32, 51-55.
    • (1996) J. Mol. Graph , vol.14 , pp. 29-32
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 31
    • 0036006154 scopus 로고    scopus 로고
    • Coiled coil miniprotein randomization on phage leads to charge pattern mimicry of the receptor recognition determinant of interleukin 5
    • Li C., Plugariu C.G., Bajgier J., White J.R., Liefer K.M., Wu S.J., and Chaiken I. Coiled coil miniprotein randomization on phage leads to charge pattern mimicry of the receptor recognition determinant of interleukin 5. J. Mol. Recog. 15 (2002) 33-43
    • (2002) J. Mol. Recog. , vol.15 , pp. 33-43
    • Li, C.1    Plugariu, C.G.2    Bajgier, J.3    White, J.R.4    Liefer, K.M.5    Wu, S.J.6    Chaiken, I.7
  • 32
    • 0029969736 scopus 로고    scopus 로고
    • Mutants of single chain interleukin 5 show asymmetric recruitment of receptor alpha and betac subunits
    • Li J., Cook R., and Chaiken I. Mutants of single chain interleukin 5 show asymmetric recruitment of receptor alpha and betac subunits. J. Biol. Chem. 271 (1996) 31729-31734
    • (1996) J. Biol. Chem. , vol.271 , pp. 31729-31734
    • Li, J.1    Cook, R.2    Chaiken, I.3
  • 33
    • 0030068041 scopus 로고    scopus 로고
    • Single chain human interleukin 5 and its asymmetric mutagenesis for mapping receptor binding sites
    • Li J., Cook R., Dede K., and Chaiken I. Single chain human interleukin 5 and its asymmetric mutagenesis for mapping receptor binding sites. J. Biol. Chem. 271 (1996) 1817-1820
    • (1996) J. Biol. Chem. , vol.271 , pp. 1817-1820
    • Li, J.1    Cook, R.2    Dede, K.3    Chaiken, I.4
  • 34
    • 0030989164 scopus 로고    scopus 로고
    • Monomeric isomers of human interleukin 5 show that 1:1 receptor recruitment is sufficient for function
    • Li J., Cook R., Doyle M.L., Hensley P., McNulty D.E., and Chaiken I. Monomeric isomers of human interleukin 5 show that 1:1 receptor recruitment is sufficient for function. Proc. Natl. Acad. Sci. USA 94 (1997) 6694-6699
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 6694-6699
    • Li, J.1    Cook, R.2    Doyle, M.L.3    Hensley, P.4    McNulty, D.E.5    Chaiken, I.6
  • 35
    • 0033548259 scopus 로고    scopus 로고
    • Crystallographic evidence for preformed dimers of erythropoietin receptor before ligand activation
    • Livnah O., Stura E.A., Middleton S.A., Johnson D.L., Jolliffe L.K., and Wilson I.A. Crystallographic evidence for preformed dimers of erythropoietin receptor before ligand activation. Science 283 (1999) 987-990
    • (1999) Science , vol.283 , pp. 987-990
    • Livnah, O.1    Stura, E.A.2    Middleton, S.A.3    Johnson, D.L.4    Jolliffe, L.K.5    Wilson, I.A.6
  • 36
    • 0026454547 scopus 로고
    • GM-CSF, IL-3 and IL-5: Cross-competition on human haemopoietic cells
    • Lopez A.F., Elliott M.J., Woodcock J., and Vadas M.A. GM-CSF, IL-3 and IL-5: Cross-competition on human haemopoietic cells. Immunol. Today 13 (1992) 495-500
    • (1992) Immunol. Today , vol.13 , pp. 495-500
    • Lopez, A.F.1    Elliott, M.J.2    Woodcock, J.3    Vadas, M.A.4
  • 38
    • 0141956433 scopus 로고    scopus 로고
    • Biology of common beta receptor-signaling cytokines: IL-3, IL-5, and GM-CSF
    • Martinez-Moczygemba M., and Huston D.P. Biology of common beta receptor-signaling cytokines: IL-3, IL-5, and GM-CSF. J. Allergy Clin. Immunol. 112 (2003) 653-665
    • (2003) J. Allergy Clin. Immunol. , vol.112 , pp. 653-665
    • Martinez-Moczygemba, M.1    Huston, D.P.2
  • 39
  • 40
    • 0025856291 scopus 로고
    • Structure-function analysis of interleukin-5 utilizing mouse/human chimeric molecules
    • McKenzie A.N., Barry S.C., Strath M., and Sanderson C.J. Structure-function analysis of interleukin-5 utilizing mouse/human chimeric molecules. EMBO J. 10 (1991) 1193-1199
    • (1991) EMBO J. , vol.10 , pp. 1193-1199
    • McKenzie, A.N.1    Barry, S.C.2    Strath, M.3    Sanderson, C.J.4
  • 42
    • 0027155448 scopus 로고
    • A novel dimer configuration revealed by the crystal structure at 2.4 A resolution of human interleukin-5
    • Milburn M.V., Hassell A.M., Lambert M.H., Jordan S.R., Proudfoot A.E., Graber P., and Wells T.N. A novel dimer configuration revealed by the crystal structure at 2.4 A resolution of human interleukin-5. Nature 363 (1993) 172-176
    • (1993) Nature , vol.363 , pp. 172-176
    • Milburn, M.V.1    Hassell, A.M.2    Lambert, M.H.3    Jordan, S.R.4    Proudfoot, A.E.5    Graber, P.6    Wells, T.N.7
  • 43
    • 0028793124 scopus 로고
    • Mutagenesis in the C-terminal region of human interleukin 5 reveals a central patch for receptor alpha chain recognition
    • Morton T., Li J., Cook R., and Chaiken I. Mutagenesis in the C-terminal region of human interleukin 5 reveals a central patch for receptor alpha chain recognition. Proc. Natl. Acad. Sci. USA 92 (1995) 10879-10883
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10879-10883
    • Morton, T.1    Li, J.2    Cook, R.3    Chaiken, I.4
  • 44
    • 0028963550 scopus 로고
    • Interleukin-3, granulocyte-macrophage colony stimulating factor and interleukin-5 transduce signals through two STAT5 homologs
    • Mui A.L., Wakao H., O' Farrell A.M., Harada N., and Miyajima A. Interleukin-3, granulocyte-macrophage colony stimulating factor and interleukin-5 transduce signals through two STAT5 homologs. EMBO J. 14 (1995) 1166-1175
    • (1995) EMBO J. , vol.14 , pp. 1166-1175
    • Mui, A.L.1    Wakao, H.2    O' Farrell, A.M.3    Harada, N.4    Miyajima, A.5
  • 46
    • 0030697889 scopus 로고    scopus 로고
    • The activation of the JAK2/STAT5 pathway is commonly involved in signaling through the human IL-5 receptor
    • Ogata N., Kikuchi Y., Kouro T., Tomonaga M., and Takatsu K. The activation of the JAK2/STAT5 pathway is commonly involved in signaling through the human IL-5 receptor. Int. Arch. Allergy Immunol. 114 (1997) 24-27
    • (1997) Int. Arch. Allergy Immunol. , vol.114 , pp. 24-27
    • Ogata, N.1    Kikuchi, Y.2    Kouro, T.3    Tomonaga, M.4    Takatsu, K.5
  • 47
    • 0032055856 scopus 로고    scopus 로고
    • JAK2 and JAK1 constitutively associate with an interleukin-5 (IL-5) receptor alpha and beta-c subunit, respectively, and are activated upon IL-5 stimulation
    • Ogata N., Kouro T., Yamada A., Koike M., Hanai N., Ishikawa T., and Takatsu K. JAK2 and JAK1 constitutively associate with an interleukin-5 (IL-5) receptor alpha and beta-c subunit, respectively, and are activated upon IL-5 stimulation. Blood 91 (1998) 2264-2271
    • (1998) Blood , vol.91 , pp. 2264-2271
    • Ogata, N.1    Kouro, T.2    Yamada, A.3    Koike, M.4    Hanai, N.5    Ishikawa, T.6    Takatsu, K.7
  • 48
    • 0036300518 scopus 로고    scopus 로고
    • Solution structure of a phage-derived peptide antagonist in complex with vascular endothelial growth factor
    • Pan B., Li B., Russell S.J., Tom J.Y., Cochran A.G., and Fairbrother W.J. Solution structure of a phage-derived peptide antagonist in complex with vascular endothelial growth factor. J. Mol. Biol. 316 (2002) 769-787
    • (2002) J. Mol. Biol. , vol.316 , pp. 769-787
    • Pan, B.1    Li, B.2    Russell, S.J.3    Tom, J.Y.4    Cochran, A.G.5    Fairbrother, W.J.6
  • 49
    • 0030742318 scopus 로고    scopus 로고
    • Src homology 2 protein tyrosine phosphatase (SHPTP2)/Src homology 2 phosphatase 2 (SHP2) tyrosine phosphatase is a positive regulator of the interleukin 5 receptor signal transduction pathways leading to the prolongation of eosinophil survival
    • Pazdrak K., Adachi T., and Alam R. Src homology 2 protein tyrosine phosphatase (SHPTP2)/Src homology 2 phosphatase 2 (SHP2) tyrosine phosphatase is a positive regulator of the interleukin 5 receptor signal transduction pathways leading to the prolongation of eosinophil survival. J. Exp. Med. 186 (1997) 561-568
    • (1997) J. Exp. Med. , vol.186 , pp. 561-568
    • Pazdrak, K.1    Adachi, T.2    Alam, R.3
  • 50
    • 0028881246 scopus 로고
    • Mechanism of inhibition of eosinophil activation by transforming growth factor-beta. Inhibition of Lyn, MAP, Jak2 kinases and STAT1 nuclear factor
    • Pazdrak K., Justement L., and Alam R. Mechanism of inhibition of eosinophil activation by transforming growth factor-beta. Inhibition of Lyn, MAP, Jak2 kinases and STAT1 nuclear factor. J. Immunol. 155 (1995) 4454-4458
    • (1995) J. Immunol. , vol.155 , pp. 4454-4458
    • Pazdrak, K.1    Justement, L.2    Alam, R.3
  • 51
    • 0032479926 scopus 로고    scopus 로고
    • Lyn, Jak2, and Raf-1 kinases are critical for the antiapoptotic effect of interleukin 5, whereas only Raf-1 kinase is essential for eosinophil activation and degranulation
    • Pazdrak K., Olszewska-Pazdrak B., Stafford S., Garofalo R.P., and Alam R. Lyn, Jak2, and Raf-1 kinases are critical for the antiapoptotic effect of interleukin 5, whereas only Raf-1 kinase is essential for eosinophil activation and degranulation. J. Exp. Med. 188 (1998) 421-429
    • (1998) J. Exp. Med. , vol.188 , pp. 421-429
    • Pazdrak, K.1    Olszewska-Pazdrak, B.2    Stafford, S.3    Garofalo, R.P.4    Alam, R.5
  • 55
    • 0034536831 scopus 로고    scopus 로고
    • Interleukin-5: A drug target for allergic diseases
    • Sanderson C.J., and Urwin D. Interleukin-5: A drug target for allergic diseases. Curr. Opin. Invest. Drugs 1 (2000) 435-441
    • (2000) Curr. Opin. Invest. Drugs , vol.1 , pp. 435-441
    • Sanderson, C.J.1    Urwin, D.2
  • 56
    • 0037102095 scopus 로고    scopus 로고
    • Biosensor analysis of dynamics of interleukin 5 receptor subunit beta(c) interaction with IL-5:IL-5R(alpha) complexes
    • Scibek J.J., Evergren E., Zahn S., Canziani G.A., Van Ryk D., and Chaiken I.M. Biosensor analysis of dynamics of interleukin 5 receptor subunit beta(c) interaction with IL-5:IL-5R(alpha) complexes. Anal. Biochem. 307 (2002) 258-265
    • (2002) Anal. Biochem. , vol.307 , pp. 258-265
    • Scibek, J.J.1    Evergren, E.2    Zahn, S.3    Canziani, G.A.4    Van Ryk, D.5    Chaiken, I.M.6
  • 58
    • 0036300793 scopus 로고    scopus 로고
    • Amino acid determinants of beta-hairpin conformation in erythropoeitin receptor agonist peptides derived from a phage display library
    • Skelton N.J., Russell S., de Sauvage F., and Cochran A.G. Amino acid determinants of beta-hairpin conformation in erythropoeitin receptor agonist peptides derived from a phage display library. J. Mol. Biol. 316 (2002) 1111-1125
    • (2002) J. Mol. Biol. , vol.316 , pp. 1111-1125
    • Skelton, N.J.1    Russell, S.2    de Sauvage, F.3    Cochran, A.G.4
  • 59
    • 0037083422 scopus 로고    scopus 로고
    • Lyn tyrosine kinase is important for IL-5-stimulated eosinophil differentiation
    • Stafford S., Lowell C., Sur S., and Alam R. Lyn tyrosine kinase is important for IL-5-stimulated eosinophil differentiation. J. Immunol. 168 (2002) 1978-1983
    • (2002) J. Immunol. , vol.168 , pp. 1978-1983
    • Stafford, S.1    Lowell, C.2    Sur, S.3    Alam, R.4
  • 60
    • 0029894667 scopus 로고    scopus 로고
    • Human interleukin-3 (IL-3) induces disulfide-linked IL-3 receptor alpha- and beta-chain heterodimerization, which is required for receptor activation but not high-affinity binding
    • Stomski F.C., Sun Q., Bagley C.J., Woodcock J., Goodall G., Andrews R.K., Berndt M.C., and Lopez A.F. Human interleukin-3 (IL-3) induces disulfide-linked IL-3 receptor alpha- and beta-chain heterodimerization, which is required for receptor activation but not high-affinity binding. Mol. Cell. Biol. 16 (1996) 3035-3046
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 3035-3046
    • Stomski, F.C.1    Sun, Q.2    Bagley, C.J.3    Woodcock, J.4    Goodall, G.5    Andrews, R.K.6    Berndt, M.C.7    Lopez, A.F.8
  • 61
    • 0031974879 scopus 로고    scopus 로고
    • Identification of a Cys motif in the common beta chain of the interleukin 3, granulocyte-macrophage colony-stimulating factor, and interleukin 5 receptors essential for disulfide-linked receptor heterodimerization and activation of all three receptors
    • Stomski F.C., Woodcock J.M., Zacharakis B., Bagley C.J., Sun Q., and Lopez A.F. Identification of a Cys motif in the common beta chain of the interleukin 3, granulocyte-macrophage colony-stimulating factor, and interleukin 5 receptors essential for disulfide-linked receptor heterodimerization and activation of all three receptors. J. Biol. Chem. 273 (1998) 1192-1199
    • (1998) J. Biol. Chem. , vol.273 , pp. 1192-1199
    • Stomski, F.C.1    Woodcock, J.M.2    Zacharakis, B.3    Bagley, C.J.4    Sun, Q.5    Lopez, A.F.6
  • 62
    • 0028113506 scopus 로고
    • A critical cytoplasmic domain of the interleukin-5 (IL-5) receptor alpha chain and its function in IL-5-mediated growth signal transduction
    • Takaki S., Kanazawa H., Shiiba M., and Takatsu K. A critical cytoplasmic domain of the interleukin-5 (IL-5) receptor alpha chain and its function in IL-5-mediated growth signal transduction. Mol. Cell. Biol. 14 (1994) 7404-7413
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 7404-7413
    • Takaki, S.1    Kanazawa, H.2    Shiiba, M.3    Takatsu, K.4
  • 63
    • 0028964465 scopus 로고
    • Cytokine signaling through nonreceptor protein tyrosine kinases
    • Taniguchi T. Cytokine signaling through nonreceptor protein tyrosine kinases. Science 268 (1995) 251-255
    • (1995) Science , vol.268 , pp. 251-255
    • Taniguchi, T.1
  • 64
    • 0025770219 scopus 로고
    • A human high affinity interleukin-5 receptor (IL-5R) is composed of an IL-5-specific alpha chain and a beta chain shared with the receptor for GM-CSF
    • Tavernier J., Devos R., Cornelis S., Tuypens T., Van der Heyden J., Fiers W., and Plaetinck G. A human high affinity interleukin-5 receptor (IL-5R) is composed of an IL-5-specific alpha chain and a beta chain shared with the receptor for GM-CSF. Cell 66 (1991) 1175-1184
    • (1991) Cell , vol.66 , pp. 1175-1184
    • Tavernier, J.1    Devos, R.2    Cornelis, S.3    Tuypens, T.4    Van der Heyden, J.5    Fiers, W.6    Plaetinck, G.7
  • 68
    • 0036793231 scopus 로고    scopus 로고
    • Crystal structures of alpha-helical cytokine-receptor complexes: We've only scratched the surface
    • Walter M.R. Crystal structures of alpha-helical cytokine-receptor complexes: We've only scratched the surface. Biotechniques 33 Suppl. (2002) 46-57
    • (2002) Biotechniques , vol.33 , Issue.SUPPL , pp. 46-57
    • Walter, M.R.1
  • 71
    • 0033575276 scopus 로고    scopus 로고
    • Randomization of the receptor alpha chain recruitment epitope reveals a functional interleukin-5 with charge depletion in the CD loop
    • Wu S.J., Li J., Tsui P., Cook R., Zhang W., Hu Y., Canziani G., and Chaiken I. Randomization of the receptor alpha chain recruitment epitope reveals a functional interleukin-5 with charge depletion in the CD loop. J. Biol. Chem. 274 (1999) 20479-20488
    • (1999) J. Biol. Chem. , vol.274 , pp. 20479-20488
    • Wu, S.J.1    Li, J.2    Tsui, P.3    Cook, R.4    Zhang, W.5    Hu, Y.6    Canziani, G.7    Chaiken, I.8
  • 72
    • 0034107113 scopus 로고    scopus 로고
    • Effect of IL-5, glucocorticoid, and Fas ligation on Bcl-2 homologue expression and caspase activation in circulating human eosinophils
    • Zangrilli J., Robertson N., Shetty A., Wu J., Hastie A., Fish J.E., Litwack G., and Peters S.P. Effect of IL-5, glucocorticoid, and Fas ligation on Bcl-2 homologue expression and caspase activation in circulating human eosinophils. Clin. Exp. Immunol. 120 (2000) 12-21
    • (2000) Clin. Exp. Immunol. , vol.120 , pp. 12-21
    • Zangrilli, J.1    Robertson, N.2    Shetty, A.3    Wu, J.4    Hastie, A.5    Fish, J.E.6    Litwack, G.7    Peters, S.P.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.