메뉴 건너뛰기




Volumn 52, Issue , 1998, Pages 67-108

Structural basis for cytokine hormone-receptor recognition and receptor activation

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA INTERFERON; BETA INTERFERON; BLOOD CLOTTING FACTOR 7A; CYTOKINE; CYTOKINE RECEPTOR; ERYTHROPOIETIN; GAMMA INTERFERON; HUMAN GROWTH HORMONE; INTERLEUKIN 10; PROLACTIN; TRANSCRIPTION FACTOR;

EID: 0031739144     PISSN: 00653233     EISSN: None     Source Type: Book Series    
DOI: 10.1016/s0065-3233(08)60433-7     Document Type: Review
Times cited : (55)

References (105)
  • 2
    • 0022998246 scopus 로고
    • Role of polycationic C-terminal portion in the structure and activity of recombinant human interferon-gamma
    • Arakawa, T., Hsu, Y. R., Parker, C. G., and Lai, P. H. (1986). Role of polycationic C-terminal portion in the structure and activity of recombinant human interferon-gamma. J. Biol. Chem. 261, 8534-8539.
    • (1986) J. Biol. Chem. , vol.261 , pp. 8534-8539
    • Arakawa, T.1    Hsu, Y.R.2    Parker, C.G.3    Lai, P.H.4
  • 4
    • 0028774180 scopus 로고
    • The interleukin-2 and interleukin-4 receptors studied by molecular modelling
    • Bamborough, P., Hedgecock, C. J. R., and Richards, W. G. (1994). The interleukin-2 and interleukin-4 receptors studied by molecular modelling. Structure 2, 839-851.
    • (1994) Structure , vol.2 , pp. 839-851
    • Bamborough, P.1    Hedgecock, C.J.R.2    Richards, W.G.3
  • 6
    • 0025765004 scopus 로고
    • A systematic mutational analysis of hormone-binding determinants in the human growth hormone receptor
    • Bass, S. H., Mulkerrin, M. G., and Wells, J. A. (1991). A systematic mutational analysis of hormone-binding determinants in the human growth hormone receptor. Proc. Natl. Acad. Sci. U.S.A. 88, 4498-4502.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 4498-4502
    • Bass, S.H.1    Mulkerrin, M.G.2    Wells, J.A.3
  • 7
    • 0025162844 scopus 로고
    • Structural design and molecular evolution of a cytokine receptor superfamily
    • Bazan, J. F. (1990). Structural design and molecular evolution of a cytokine receptor superfamily. Proc. Natl. Acad. Sci. U.S.A. 87, 6934-6938.
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 6934-6938
    • Bazan, J.F.1
  • 8
    • 0026763387 scopus 로고
    • Unraveling the structure of IL-2
    • Bazan, J. F., and McKay, D. B. (1992). Unraveling the structure of IL-2. Science 257, 410-413.
    • (1992) Science , vol.257 , pp. 410-413
    • Bazan, J.F.1    McKay, D.B.2
  • 9
    • 0025192084 scopus 로고
    • 2+, phospholipids and tissue-factor apoprotein to the activation of human blood-coagulation factor X by activated factor VII
    • 2+, phospholipids and tissue-factor apoprotein to the activation of human blood-coagulation factor X by activated factor VII. Biochem. J. 265, 327-336.
    • (1990) Biochem. J. , vol.265 , pp. 327-336
    • Bom, V.J.1    Bertina, R.M.2
  • 12
    • 0028916599 scopus 로고
    • A hot spot of binding energy in a hormone-receptor interface
    • Clackson, T., and Wells, J. A. (1995). A hot spot of binding energy in a hormone-receptor interface. Science 267, 383-386.
    • (1995) Science , vol.267 , pp. 383-386
    • Clackson, T.1    Wells, J.A.2
  • 13
    • 26844539025 scopus 로고    scopus 로고
    • Structural and functional analysis of the 1:1 growth hormone: Receptor complex reveals the molecular basis for receptor affinity
    • submitted for publication
    • Clackson, T., Ultsch, M. H., Wells, J. A., and de Vos, A. M. (1997). Structural and functional analysis of the 1:1 growth hormone: Receptor complex reveals the molecular basis for receptor affinity. J. Mol. Biol. (submitted for publication).
    • (1997) J. Mol. Biol.
    • Clackson, T.1    Ultsch, M.H.2    Wells, J.A.3    De Vos, A.M.4
  • 14
    • 0024403619 scopus 로고
    • High resolution epitope mapping of hGH-receptor interactions by alanine-scanning mutagenesis
    • Cunningham, B. C., and Wells, J. A. (1989). High resolution epitope mapping of hGH-receptor interactions by alanine-scanning mutagenesis. Science 244, 1081-1085.
    • (1989) Science , vol.244 , pp. 1081-1085
    • Cunningham, B.C.1    Wells, J.A.2
  • 15
    • 0026335990 scopus 로고
    • Rational design of receptor-specific variants of human growth hormone
    • Cunningham, B. C., and Wells, J. A. (1991). Rational design of receptor-specific variants of human growth hormone. Proc. Natl. Acad. Sci. U.S.A. 88, 3407-3411.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 3407-3411
    • Cunningham, B.C.1    Wells, J.A.2
  • 16
    • 0027132013 scopus 로고
    • Comparison of a structural and functional epitope
    • Cunningham, B. C., and Wells, J. A. (1993). Comparison of a structural and functional epitope. J. Mol. Biol. 234, 554-563.
    • (1993) J. Mol. Biol. , vol.234 , pp. 554-563
    • Cunningham, B.C.1    Wells, J.A.2
  • 17
    • 0026332810 scopus 로고
    • Dimerization of the extracellular domain of the human growth hormone receptor by a single hormone molecule
    • Cunningham, B. C., Ultsch, M., de Vos, A. M., Mulkerrin, M. G., Clauser, K. R., and Wells, J. A. (1991). Dimerization of the extracellular domain of the human growth hormone receptor by a single hormone molecule. Science 254, 821-825.
    • (1991) Science , vol.254 , pp. 821-825
    • Cunningham, B.C.1    Ultsch, M.2    De Vos, A.M.3    Mulkerrin, M.G.4    Clauser, K.R.5    Wells, J.A.6
  • 18
    • 0026337077 scopus 로고
    • The coagulation cascade: Initiation, maintenance, and regulation
    • Davie, E. W., Fujikawa, K., and Kisiel, W. (1991). The coagulation cascade: Initiation, maintenance, and regulation. Biochemistry 30, 10363-10370.
    • (1991) Biochemistry , vol.30 , pp. 10363-10370
    • Davie, E.W.1    Fujikawa, K.2    Kisiel, W.3
  • 20
    • 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. (1992). Human growth hormone and extracellular domain of its receptor: Crystal structure of the complex. Science 255, 306-312.
    • (1992) Science , vol.255 , pp. 306-312
    • De Vos, A.M.1    Ultsch, M.2    Kossiakoff, A.A.3
  • 21
    • 0026000892 scopus 로고
    • Interleukin 10 (IL-10) and viral IL-10 strongly reduce antigen-specific human T cell proliferation by diminishing the antigen-presenting capacity of monocytes via downregulation of class II major histocompatibility complex expression
    • de Waal Malefyt, R., Haanen, J., Spits, H., Roncarolo, M. G., te Velde, A., Figdor, C., Johnson, K., Kastelein, R., Yssel, H., and de Vries, J. E. (1991a). Interleukin 10 (IL-10) and viral IL-10 strongly reduce antigen-specific human T cell proliferation by diminishing the antigen-presenting capacity of monocytes via downregulation of class II major histocompatibility complex expression. J. Exp. Med. 174, 915-924.
    • (1991) J. Exp. Med. , vol.174 , pp. 915-924
    • De Waal Malefyt, R.1    Haanen, J.2    Spits, H.3    Roncarolo, M.G.4    Te Velde, A.5    Figdor, C.6    Johnson, K.7    Kastelein, R.8    Yssel, H.9    De Vries, J.E.10
  • 22
    • 0026094306 scopus 로고
    • Interleukin 10 (IL-10) inhibits cytokine synthesis by human monocytes: An autoregulatory role of IL-10 produced by monocytes
    • de Waal Malefyt, R., Abrams, J., Bennett, B., Figdor, C. G., and de Vries, J. E. (1991b). Interleukin 10 (IL-10) inhibits cytokine synthesis by human monocytes: An autoregulatory role of IL-10 produced by monocytes. J. Exp. Med. 174, 1209-1220.
    • (1991) J. Exp. Med. , vol.174 , pp. 1209-1220
    • De Waal Malefyt, R.1    Abrams, J.2    Bennett, B.3    Figdor, C.G.4    De Vries, J.E.5
  • 23
    • 0026320870 scopus 로고
    • Novel fold and putative receptor binding site of granulocyte-macrophage colony-stimulating factor
    • Diederichs, K., Boone, T., and Karplus, P. A. (1991). Novel fold and putative receptor binding site of granulocyte-macrophage colony-stimulating factor. Science 254, 1779-1782.
    • (1991) Science , vol.254 , pp. 1779-1782
    • Diederichs, K.1    Boone, T.2    Karplus, P.A.3
  • 25
    • 0025125156 scopus 로고
    • Mitogenic and binding properties of monoclonal antibodies to the prolactin receptor in Nb2 rat lymphoma cells. Selection enhancement by anti-mouse IgG
    • Elberg, G., Kelley, P. A., Djiane, J., Binder, L., and Gertler, A. (1990). Mitogenic and binding properties of monoclonal antibodies to the prolactin receptor in Nb2 rat lymphoma cells. Selection enhancement by anti-mouse IgG. J. Biol. Chem. 265, 14770-14776.
    • (1990) J. Biol. Chem. , vol.265 , pp. 14770-14776
    • Elberg, G.1    Kelley, P.A.2    Djiane, J.3    Binder, L.4    Gertler, A.5
  • 26
    • 0027411525 scopus 로고
    • The molecular cell biology of interferon-γ and its receptor
    • Farrar, M. A., and Schreiber, R. D. (1993). The molecular cell biology of interferon-γ and its receptor. Annu. Rev. Immun. 11, 571-611.
    • (1993) Annu. Rev. Immun. , vol.11 , pp. 571-611
    • Farrar, M.A.1    Schreiber, R.D.2
  • 27
    • 0024408824 scopus 로고
    • Two types of mouse T helper cell: IV. Th2 clones secrete a factor that inhibits cytokine production by Th1 clones
    • Florentino, D. F., Bond, M. W., and Mosmann, T. R. (1989). Two types of mouse T helper cell: IV. Th2 clones secrete a factor that inhibits cytokine production by Th1 clones. J. Exp. Med. 170, 2081-2095.
    • (1989) J. Exp. Med. , vol.170 , pp. 2081-2095
    • Florentino, D.F.1    Bond, M.W.2    Mosmann, T.R.3
  • 28
    • 0026759532 scopus 로고
    • Stoichiometry of interaction between interferon-γ and its receptor
    • Fountoulakis, M., Zulauf, M., Lustig, A., and Garotta, G. (1992). Stoichiometry of interaction between interferon-γ and its receptor. Eur. J. Biochem. 208, 781-787.
    • (1992) Eur. J. Biochem. , vol.208 , pp. 781-787
    • Fountoulakis, M.1    Zulauf, M.2    Lustig, A.3    Garotta, G.4
  • 29
    • 0025259656 scopus 로고
    • The human growth hormone receptor: Secretion from Escherichia coli and disulfide bonding pattern of the extracellular binding domain
    • Fuh, G., Mulkerrin, M. M., Bass, S., McFarland, N., Brochier, M., Bourell, J. H., Light, D. R., and Wells, J. A. (1990). The human growth hormone receptor: Secretion from Escherichia coli and disulfide bonding pattern of the extracellular binding domain. J. Biol. Chem. 265, 3111-3115.
    • (1990) J. Biol. Chem. , vol.265 , pp. 3111-3115
    • Fuh, G.1    Mulkerrin, M.M.2    Bass, S.3    McFarland, N.4    Brochier, M.5    Bourell, J.H.6    Light, D.R.7    Wells, J.A.8
  • 30
    • 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. (1992). Rational design of potent antagonists to the human growth hormone receptor. Science 256, 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
  • 31
    • 0028019121 scopus 로고
    • Identification of the factor VIIa binding site on tissue factor by homologous loop swap and alanine scanning mutagenesis
    • Gibbs, C. S., McCurdy, S. N., Leung, L. L. K., and Paborsky, L. R. (1994). Identification of the factor VIIa binding site on tissue factor by homologous loop swap and alanine scanning mutagenesis. Biochemistry 33, 14003-14010.
    • (1994) Biochemistry , vol.33 , pp. 14003-14010
    • Gibbs, C.S.1    McCurdy, S.N.2    Leung, L.L.K.3    Paborsky, L.R.4
  • 32
    • 0027249338 scopus 로고
    • Interferon-gamma induces receptor dimerization in solution and on cells
    • Greenlund, A. C., Schreiber, R. D., Goeddel, D. V., and Pennica, D. (1993). Interferon-gamma induces receptor dimerization in solution and on cells. J. Biol. Chem. 268, 18103-18110.
    • (1993) J. Biol. Chem. , vol.268 , pp. 18103-18110
    • Greenlund, A.C.1    Schreiber, R.D.2    Goeddel, D.V.3    Pennica, D.4
  • 33
    • 0028175454 scopus 로고
    • Ligand-induced IFN gamma receptor tyrosine phosphorylation couples the receptor to its signal transduction system (p91)
    • Greenlund, A. C., Farrar, M. A., Viviano, B. L., and Schreiber, R. D. (1994). Ligand-induced IFN gamma receptor tyrosine phosphorylation couples the receptor to its signal transduction system (p91). EMBO J. 13, 1591-1600.
    • (1994) EMBO J. , vol.13 , pp. 1591-1600
    • Greenlund, A.C.1    Farrar, M.A.2    Viviano, B.L.3    Schreiber, R.D.4
  • 34
    • 0028847977 scopus 로고
    • A model of the complex between interleukin-4 and its receptors
    • Gustchina, A., Zdanov, A., Schalk-Hihi, C., and Wlodawer, A. (1995). A model of the complex between interleukin-4 and its receptors. Proteins 21, 140-148.
    • (1995) Proteins , vol.21 , pp. 140-148
    • Gustchina, A.1    Zdanov, A.2    Schalk-Hihi, C.3    Wlodawer, A.4
  • 36
    • 0027258762 scopus 로고
    • The structure of granulocyte-colony-stimulating factor and its relationship to other growth factors
    • Hill, C. P., Osslund, T. D., and Eisenberg, D. (1993). The structure of granulocyte-colony-stimulating factor and its relationship to other growth factors. Proc. Natl. Acad. Sci. U.S.A. 90, 5167-5171.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 5167-5171
    • Hill, C.P.1    Osslund, T.D.2    Eisenberg, D.3
  • 37
    • 0028963213 scopus 로고
    • Increased cell-surface expression and enhanced folding in the endoplasmic reticulum of a mutant erythropoietin receptor
    • Hilton, D. J., Watowich, S. S., Murray, P. J., and Lodish, H. F. (1995). Increased cell-surface expression and enhanced folding in the endoplasmic reticulum of a mutant erythropoietin receptor. Proc. Natl. Acad. Sci. U.S.A. 92, 190-194.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 190-194
    • Hilton, D.J.1    Watowich, S.S.2    Murray, P.J.3    Lodish, H.F.4
  • 38
    • 0029928504 scopus 로고    scopus 로고
    • Saturation mutagenesis of the WSXWS motif of the erythropoietin receptor
    • Hilton, D. J., Watowich, S. S., Katz, L., and Lodish, H. F. (1996). Saturation mutagenesis of the WSXWS motif of the erythropoietin receptor. J. Biol. Chem. 271, 4699-4708.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4699-4708
    • Hilton, D.J.1    Watowich, S.S.2    Katz, L.3    Lodish, H.F.4
  • 39
    • 0021760405 scopus 로고
    • Differential expression of human interferon genes
    • Hiscott, J., Cantell, K., and Weissmann, C. (1984). Differential expression of human interferon genes. Nucleic Acids Res. 12, 3727-3746.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 3727-3746
    • Hiscott, J.1    Cantell, K.2    Weissmann, C.3
  • 40
    • 0028351169 scopus 로고
    • Crystal structure of tandem type III fibronectin domains from Drosophila neuroglian at 2.0 Å
    • Huber, A. H., Wang, Y.-M., Bieber, A. J., and Bjorkman, P. J. (1994). Crystal structure of tandem type III fibronectin domains from Drosophila neuroglian at 2.0 Å. Neuron 12, 717-731.
    • (1994) Neuron , vol.12 , pp. 717-731
    • Huber, A.H.1    Wang, Y.-M.2    Bieber, A.J.3    Bjorkman, P.J.4
  • 41
    • 0028175969 scopus 로고
    • Interferon-gamma induces tyrosine phosphorylation of interferon-gamma receptor and regulated association of protein tyrosine kinases, Jak1 and Jak2, with its receptor
    • Igarashi, K., Garotta, G., Ozmen, L., Ziemiecki, A., Wilks, A. F., Harpur, A. G., Larner, A. C., and Finbloom, D. S. (1994). Interferon-gamma induces tyrosine phosphorylation of interferon-gamma receptor and regulated association of protein tyrosine kinases, Jak1 and Jak2, with its receptor. J. Biol. Chem. 269, 14333-14336.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14333-14336
    • Igarashi, K.1    Garotta, G.2    Ozmen, L.3    Ziemiecki, A.4    Wilks, A.F.5    Harpur, A.G.6    Larner, A.C.7    Finbloom, D.S.8
  • 42
    • 0029671421 scopus 로고    scopus 로고
    • Identification of an interferon-gamma receptor alpha chain sequence required for JAK-1 binding
    • Kaplan, D. H., Greenlund, A. C., Tanner, J. W., Shaw, A. S., and Schreiber, R. D. (1996). Identification of an interferon-gamma receptor alpha chain sequence required for JAK-1 binding. J. Biol. Chem. 271, 9-12.
    • (1996) J. Biol. Chem. , vol.271 , pp. 9-12
    • Kaplan, D.H.1    Greenlund, A.C.2    Tanner, J.W.3    Shaw, A.S.4    Schreiber, R.D.5
  • 43
    • 0029093452 scopus 로고
    • Analysis of the factor VIIa binding site on human tissue factor: Effects of tissue factor mutations on the kinetics and thermodynamics of binding
    • Kelley, R. F., Costas, K. E., O'Connell, M. P., and Lazarus, R. A. (1995). Analysis of the factor VIIa binding site on human tissue factor: Effects of tissue factor mutations on the kinetics and thermodynamics of binding. Biochemistry 34, 10383-10392.
    • (1995) Biochemistry , vol.34 , pp. 10383-10392
    • Kelley, R.F.1    Costas, K.E.2    O'Connell, M.P.3    Lazarus, R.A.4
  • 44
    • 0027943660 scopus 로고
    • Comparison of the intermediate complexes of human growth hormone bound to the human growth hormone and prolactin receptors
    • Kossiakoff, A. A., Somers, W., Ultsch, M., Andow, K., Muller, Y. A., and de Vos, A. M. (1994). Comparison of the intermediate complexes of human growth hormone bound to the human growth hormone and prolactin receptors. Protein Sci. 3, 1697-1705.
    • (1994) Protein Sci. , vol.3 , pp. 1697-1705
    • Kossiakoff, A.A.1    Somers, W.2    Ultsch, M.3    Andow, K.4    Muller, Y.A.5    De Vos, A.M.6
  • 45
    • 0026655855 scopus 로고
    • The evaluation of complex-dependent alterations in human factor VIIa
    • Lawson, J. H., Butenas, S., and Mann, K. G. (1992). The evaluation of complex-dependent alterations in human factor VIIa. J. Biol. Chem. 267, 4834-4843.
    • (1992) J. Biol. Chem. , vol.267 , pp. 4834-4843
    • Lawson, J.H.1    Butenas, S.2    Mann, K.G.3
  • 46
    • 0026490256 scopus 로고
    • Structure of a fibronectin type III domain from tenascin phased by MAD analysis of the selenomethionyl protein
    • Leahy, D. J., Hendrickson, W. A., Aukhil, I., and Erickson, H. P. (1992). Structure of a fibronectin type III domain from tenascin phased by MAD analysis of the selenomethionyl protein. Science 258, 987-991.
    • (1992) Science , vol.258 , pp. 987-991
    • Leahy, D.J.1    Hendrickson, W.A.2    Aukhil, I.3    Erickson, H.P.4
  • 47
    • 0023620960 scopus 로고
    • Reduced receptor binding by a human interferon-γ fragment lacking 11 carboxy-terminal amino acids
    • Leinikki, P. O., Calderon, J., Luquette, M. H., and Schreiber, R. D. (1987). Reduced receptor binding by a human interferon-γ fragment lacking 11 carboxy-terminal amino acids. J. Immunol. 139, 3360-3366.
    • (1987) J. Immunol. , vol.139 , pp. 3360-3366
    • Leinikki, P.O.1    Calderon, J.2    Luquette, M.H.3    Schreiber, R.D.4
  • 49
    • 0027141509 scopus 로고
    • Crystal structure of canine and bovine granulocyte-colony stimulating factor (G-CSF)
    • Lovejoy, B., Cascio, D., and Eisenberg, D. (1993). Crystal structure of canine and bovine granulocyte-colony stimulating factor (G-CSF). J. Mol. Biol. 234, 640-653.
    • (1993) J. Mol. Biol. , vol.234 , pp. 640-653
    • Lovejoy, B.1    Cascio, D.2    Eisenberg, D.3
  • 51
    • 0022615379 scopus 로고
    • An interferon analogue, [Ala 30, 32, 33] HuIFN-α2, acting as a HuIFN-α2 antagonist on bovine cells
    • Marcucci, F., and deMaeyer, E. (1986). An interferon analogue, [Ala 30, 32, 33] HuIFN-α2, acting as a HuIFN-α2 antagonist on bovine cells. Biochem. Biophys. Res. Commun. 134, 1412-1418.
    • (1986) Biochem. Biophys. Res. Commun. , vol.134 , pp. 1412-1418
    • Marcucci, F.1    DeMaeyer, E.2
  • 52
    • 0029068150 scopus 로고
    • Interferon gamma signals via a high-affinity multisubunit receptor complex that contains two types of polypeptide chain
    • Marsters, S. A., Pennica, D., Bach, E., Schreiber, R. D., and Ashkenazi, A. (1995). Interferon gamma signals via a high-affinity multisubunit receptor complex that contains two types of polypeptide chain. Proc. Natl. Acad. Sci. U.S.A. 92, 5401-5405.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 5401-5405
    • Marsters, S.A.1    Pennica, D.2    Bach, E.3    Schreiber, R.D.4    Ashkenazi, A.5
  • 53
  • 54
    • 0027227660 scopus 로고
    • Structural, functional and evolutionary implications of the three-dimensional crystal structure of murine interferon-beta
    • Mitsui, Y., Senda, T., Shimazu, T., Matsuda, S., and Utsumi, J. (1993). Structural, functional and evolutionary implications of the three-dimensional crystal structure of murine interferon-beta. Pharmacol. Ther. 58, 93-132.
    • (1993) Pharmacol. Ther. , vol.58 , pp. 93-132
    • Mitsui, Y.1    Senda, T.2    Shimazu, T.3    Matsuda, S.4    Utsumi, J.5
  • 57
    • 0023643043 scopus 로고
    • Molecular cloning of the cDNA for tissue factor, the cellular receptor for the initiation of the coagulation protease cascade
    • Morrissey, J. H., Fakhrai, H., and Edgington, T. S. (1987). Molecular cloning of the cDNA for tissue factor, the cellular receptor for the initiation of the coagulation protease cascade. Cell (Cambridge, Mass.) 50, 129-135.
    • (1987) Cell (Cambridge, Mass.) , vol.50 , pp. 129-135
    • Morrissey, J.H.1    Fakhrai, H.2    Edgington, T.S.3
  • 59
    • 0028094639 scopus 로고
    • Structure of the extracellular domain of human tissue factor: Location of the factor VIIa binding site
    • Muller, Y. A., Ultsch, M. H., Kelly, R. F., and de Vos, A. M. (1994). Structure of the extracellular domain of human tissue factor: Location of the factor VIIa binding site. Biochemistry 33, 10864-10870.
    • (1994) Biochemistry , vol.33 , pp. 10864-10870
    • Muller, Y.A.1    Ultsch, M.H.2    Kelly, R.F.3    De Vos, A.M.4
  • 60
    • 0029864435 scopus 로고    scopus 로고
    • The crystal structure of the extracellular domain of human tissue factor refined to 1.7 Å resolution
    • Muller, Y. A., Ultsch, M. H., and de Vos, A. M. (1996). The crystal structure of the extracellular domain of human tissue factor refined to 1.7 Å resolution. J. Mol. Biol. 256, 144-159.
    • (1996) J. Mol. Biol. , vol.256 , pp. 144-159
    • Muller, Y.A.1    Ultsch, M.H.2    De Vos, A.M.3
  • 61
    • 0022351911 scopus 로고
    • Tissue factor accelerates the activation of coagulation factor VII: The role of a bifunctional coagulation cofactor
    • Nemerson, Y., and Repke, D. (1985). Tissue factor accelerates the activation of coagulation factor VII: The role of a bifunctional coagulation cofactor. Thromb. Res. 40, 351-358.
    • (1985) Thromb. Res. , vol.40 , pp. 351-358
    • Nemerson, Y.1    Repke, D.2
  • 62
    • 0026727235 scopus 로고
    • Three-dimensional structure of dimeric human recombinant macrophage colony-stimulating factor
    • Pandit, J., Bohm, A., Jancarik, J., Halenbeck, R., Koths, K., and Kim, S.-H. (1992). Three-dimensional structure of dimeric human recombinant macrophage colony-stimulating factor. Science 258, 1358-1362.
    • (1992) Science , vol.258 , pp. 1358-1362
    • Pandit, J.1    Bohm, A.2    Jancarik, J.3    Halenbeck, R.4    Koths, K.5    Kim, S.-H.6
  • 64
    • 0026764439 scopus 로고
    • Three-dimensional solution structure of human interleukin-4 by multidimensional heteronuclear magnetic resonance spectroscopy
    • Powers, R., Garrett, D. S., March, C. J., Frieden, E. A., Gronenborn, A. M., and Clore, G. M. (1992). Three-dimensional solution structure of human interleukin-4 by multidimensional heteronuclear magnetic resonance spectroscopy. Science 256, 1673-1677.
    • (1992) Science , vol.256 , pp. 1673-1677
    • Powers, R.1    Garrett, D.S.2    March, C.J.3    Frieden, E.A.4    Gronenborn, A.M.5    Clore, G.M.6
  • 67
    • 0032570710 scopus 로고    scopus 로고
    • Activation of chimeric and full length growth hormone receptors by growth hormone receptor monoclonal antibodies: Evidence that a specific conformational change is required for full length receptor binding?
    • submitted for publication
    • Rowlinson, S. W., Behncken, S. N., Rowland, J. E., Clarkson, R. W., Strasburger, C. J., Wu, Z., Baumbach, W., and Waters, M. J. (1998). Activation of chimeric and full length growth hormone receptors by growth hormone receptor monoclonal antibodies: Evidence that a specific conformational change is required for full length receptor binding? J. Biol. Chem. (submitted for publication).
    • (1998) J. Biol. Chem.
    • Rowlinson, S.W.1    Behncken, S.N.2    Rowland, J.E.3    Clarkson, R.W.4    Strasburger, C.J.5    Wu, Z.6    Baumbach, W.7    Waters, M.J.8
  • 69
    • 0028299054 scopus 로고
    • Mutational mapping of functional residues in tissue factor VII: Identification of factor VII recognition determinants in both structural modules of the predicted cytokine receptor homology domain
    • Ruf, W., Schullek, J. R., Stone, M. J., and Edgington, T. S. (1994). Mutational mapping of functional residues in tissue factor VII: Identification of factor VII recognition determinants in both structural modules of the predicted cytokine receptor homology domain. Biochemistry 33, 1565-1572.
    • (1994) Biochemistry , vol.33 , pp. 1565-1572
    • Ruf, W.1    Schullek, J.R.2    Stone, M.J.3    Edgington, T.S.4
  • 71
    • 0029149376 scopus 로고
    • The Jak kinases differentially associate with the alpha and beta (accessory factor) chains of the interferon gamma receptor to form a functional receptor unit capable of activating STAT transcription factors
    • Sakatsume, M., Igarashi, K., Winestock, K. D., Garotta, G., Larner, A. C., and Finbloom, D. S. (1995). The Jak kinases differentially associate with the alpha and beta (accessory factor) chains of the interferon gamma receptor to form a functional receptor unit capable of activating STAT transcription factors. J. Biol. Chem. 270, 17528-17534.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17528-17534
    • Sakatsume, M.1    Igarashi, K.2    Winestock, K.D.3    Garotta, G.4    Larner, A.C.5    Finbloom, D.S.6
  • 72
    • 0004822706 scopus 로고
    • Structure of recombinant bovine interferon-γ at 3.0 Å resolution
    • Samudzi, C. T., and Rubin, J. R. (1993). Structure of recombinant bovine interferon-γ at 3.0 Å resolution. Acta Crystallogr. Sect. D 49, 513-521.
    • (1993) Acta Crystallogr. Sect. D , vol.49 , pp. 513-521
    • Samudzi, C.T.1    Rubin, J.R.2
  • 73
    • 0025786186 scopus 로고
    • Crystal structure of recombinant rabbit interferon-γ at 2.7 Å resolution
    • Samudzi, C. T., Burton, L. E., and Rubin, J. R. (1991). Crystal structure of recombinant rabbit interferon-γ at 2.7 Å resolution. J. Biol. Chem. 266, 21791-21797.
    • (1991) J. Biol. Chem. , vol.266 , pp. 21791-21797
    • Samudzi, C.T.1    Burton, L.E.2    Rubin, J.R.3
  • 76
    • 0029069145 scopus 로고
    • Transcriptional responses to polypeptide ligands: The JAK-STAT pathway
    • Schindler, C., and Darnell, J. E. (1995). Transcriptional responses to polypeptide ligands: The JAK-STAT pathway. Annu. Rev. Biochem. 64, 621-651.
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 621-651
    • Schindler, C.1    Darnell, J.E.2
  • 77
    • 0027934795 scopus 로고
    • Key ligand interface residues in tissue factor contribute independently to factor VIIa binding
    • Schullek, J. R., Ruf, W., and Edgington, T. S. (1994). Key ligand interface residues in tissue factor contribute independently to factor VIIa binding. J. Biol. Chem. 269, 19399-19403.
    • (1994) J. Biol. Chem. , vol.269 , pp. 19399-19403
    • Schullek, J.R.1    Ruf, W.2    Edgington, T.S.3
  • 78
    • 0023898834 scopus 로고
    • Evidence for a polypeptide segment at the carboxyl terminus of recombinant human γ interferon involved in expression of biological activity
    • Seelig, G. F., Wijdenes, J., Nagabhushan, T. L., and Trotta, P. P. (1988). Evidence for a polypeptide segment at the carboxyl terminus of recombinant human γ interferon involved in expression of biological activity. Biochemistry 27, 1981-1987.
    • (1988) Biochemistry , vol.27 , pp. 1981-1987
    • Seelig, G.F.1    Wijdenes, J.2    Nagabhushan, T.L.3    Trotta, P.P.4
  • 80
    • 0028791828 scopus 로고
    • Refined crystal structure of recombinant murine interferon-β at 2.15 Å resolution
    • Senda, T., Saitoh, S. I., and Mitsui, Y. (1995). Refined crystal structure of recombinant murine interferon-β at 2.15 Å resolution. J. Mol. Biol. 253, 187-207.
    • (1995) J. Mol. Biol. , vol.253 , pp. 187-207
    • Senda, T.1    Saitoh, S.I.2    Mitsui, Y.3
  • 83
    • 0028032203 scopus 로고
    • The x-ray structure of a growth hormone-prolactin receptor complex
    • Somers, W., Ultsch, M., de Vos, A. M., and Kossiakoff, A. A. (1994). The x-ray structure of a growth hormone-prolactin receptor complex. Nature (London) 372, 478-481.
    • (1994) Nature (London) , vol.372 , pp. 478-481
    • Somers, W.1    Ultsch, M.2    De Vos, A.M.3    Kossiakoff, A.A.4
  • 84
    • 0031041014 scopus 로고    scopus 로고
    • 1.9 Å crystal structure of interleukin 6: Implications for a novel mode of receptor dimerization and signaling
    • Somers, W., Stahl, M., and Seehra, J. S. (1997). 1.9 Å crystal structure of interleukin 6: Implications for a novel mode of receptor dimerization and signaling. EMBO J. 16, 989-997.
    • (1997) EMBO J. , vol.16 , pp. 989-997
    • Somers, W.1    Stahl, M.2    Seehra, J.S.3
  • 86
    • 0027145507 scopus 로고
    • Cytokine structural taxonomy and mechanisms of receptor engagement
    • Sprang, S. R., and Bazan, J. F. (1993). Cytokine structural taxonomy and mechanisms of receptor engagement. Curr. Opin. Struct. Biol. 3, 815-827.
    • (1993) Curr. Opin. Struct. Biol. , vol.3 , pp. 815-827
    • Sprang, S.R.1    Bazan, J.F.2
  • 87
    • 0025341018 scopus 로고
    • Identification of a novel thymocyte growth-promoting factor derived from B cell lymphomas
    • Suda, T., O'Garra, A., MacNeil, I., Fischer, M., Bond, M. W., and Zlotnik, A. (1990). Identification of a novel thymocyte growth-promoting factor derived from B cell lymphomas. Cell. Immunol. 129, 228-240.
    • (1990) Cell. Immunol. , vol.129 , pp. 228-240
    • Suda, T.1    O'Garra, A.2    MacNeil, I.3    Fischer, M.4    Bond, M.W.5    Zlotnik, A.6
  • 88
    • 0029770041 scopus 로고    scopus 로고
    • Crystal structure of an antagonist mutant of human growth hormone, G120R, in complex with its receptor at 2.9 Å resolution
    • Sundstrom, M., Lundqvist, T., Rodin, J., Giebel, L. B., Milligan, D., and Norstedt, G. (1996). Crystal structure of an antagonist mutant of human growth hormone, G120R, in complex with its receptor at 2.9 Å resolution. J. Biol. Chem. 271, 32197-32203.
    • (1996) J. Biol. Chem. , vol.271 , pp. 32197-32203
    • Sundstrom, M.1    Lundqvist, T.2    Rodin, J.3    Giebel, L.B.4    Milligan, D.5    Norstedt, G.6
  • 89
    • 0028217202 scopus 로고
    • The crystal structure of affinity-matured human growth hormone at 2 Å resolution
    • Ultsch, M., Somers, W., Kossiakoff, A. A., and de Vos, A. M. (1994). The crystal structure of affinity-matured human growth hormone at 2 Å resolution. J. Mol. Biol. 236, 286-299.
    • (1994) J. Mol. Biol. , vol.236 , pp. 286-299
    • Ultsch, M.1    Somers, W.2    Kossiakoff, A.A.3    De Vos, A.M.4
  • 90
    • 0028944489 scopus 로고
    • α and β interferons and their receptor and their friends and relations
    • Uze, G., Lutfalla, G., and Mogensen, K. E. (1995). α and β interferons and their receptor and their friends and relations. J. Interferon Cytokine Res. 15, 3-26.
    • (1995) J. Interferon Cytokine Res. , vol.15 , pp. 3-26
    • Uze, G.1    Lutfalla, G.2    Mogensen, K.E.3
  • 92
    • 0029148581 scopus 로고
    • Crystal structure of interleukin 10 reveals an interferon-γ like fold
    • Walter, M. R., and Nagabhushan, T. L. (1995). Crystal structure of interleukin 10 reveals an interferon-γ like fold. Biochemistry 34, 12118-12125.
    • (1995) Biochemistry , vol.34 , pp. 12118-12125
    • Walter, M.R.1    Nagabhushan, T.L.2
  • 93
    • 0026520373 scopus 로고
    • Three-dimensional structure of recombinant human granulocyte-macrophage colony-stimulating factor
    • Walter, M. R., Cook, W. J., Ealick, S. E., Nagabhushan, T. L., Trotta, P. P., and Bugg, C. E. (1992a). Three-dimensional structure of recombinant human granulocyte-macrophage colony-stimulating factor. J. Mol. Biol. 224, 1075-1085.
    • (1992) J. Mol. Biol. , vol.224 , pp. 1075-1085
    • Walter, M.R.1    Cook, W.J.2    Ealick, S.E.3    Nagabhushan, T.L.4    Trotta, P.P.5    Bugg, C.E.6
  • 98
    • 0026350498 scopus 로고
    • Systematic mutational analyses of protein-protein interfaces
    • (J. J. Langone, ed.), Academic Press San Diego, CA
    • Wells, J. A. (1991). Systematic mutational analyses of protein-protein interfaces. In "Methods in Enzymology" (J. J. Langone, ed.), Vol. 202, pp. 390-411. Academic Press San Diego, CA.
    • (1991) Methods in Enzymology , vol.202 , pp. 390-411
    • Wells, J.A.1
  • 99
    • 0029982521 scopus 로고    scopus 로고
    • Hematopoietic receptor complexes
    • Wells, J. A., and de Vos, A. M. (1996). Hematopoietic receptor complexes. Annu. Rev. Biochem. 65, 609-634.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 609-634
    • Wells, J.A.1    De Vos, A.M.2
  • 100
    • 33845772515 scopus 로고
    • Interferon-like virus inhibitor induced in human leukocytes by phytohemagglutinin
    • Wheelock, E. F. (1965). Interferon-like virus inhibitor induced in human leukocytes by phytohemagglutinin. Science 149, 310-311.
    • (1965) Science , vol.149 , pp. 310-311
    • Wheelock, E.F.1
  • 101
    • 0001495165 scopus 로고
    • Localization of tissue factor in the normal vessel wall and in the atherosclerotic plaque
    • Wilcox, J. N., Smith, K. M., Schwartz, S. M., and Gordon, D. (1989). Localization of tissue factor in the normal vessel wall and in the atherosclerotic plaque. Proc. Natl. Acad. Sci. U.S.A. 86, 2839-2843.
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , pp. 2839-2843
    • Wilcox, J.N.1    Smith, K.M.2    Schwartz, S.M.3    Gordon, D.4
  • 102
    • 0026661731 scopus 로고
    • Crystal structure of human recombinant interleukin-4 at 2.25 Å resolution
    • Wlodawer, A. Pavlovsky, A., and Gustchina, A. (1992). Crystal structure of human recombinant interleukin-4 at 2.25 Å resolution. FEBS Lett. 309, 59-64.
    • (1992) FEBS Lett. , vol.309 , pp. 59-64
    • Wlodawer, A.1    Pavlovsky, A.2    Gustchina, A.3
  • 104
    • 0029644946 scopus 로고
    • Crystal structure of interleukin-10 reveals the functional dimer with an unexpected topological similarity to interferon-γ
    • Zdanov, A., Schalk-Hihi, C., Gustchina, A., Tsang, M., Weatherbee, J., and Wlodawer, A. (1995). Crystal structure of interleukin-10 reveals the functional dimer with an unexpected topological similarity to interferon-γ. Structure 3, 591-601.
    • (1995) Structure , vol.3 , pp. 591-601
    • Zdanov, A.1    Schalk-Hihi, C.2    Gustchina, A.3    Tsang, M.4    Weatherbee, J.5    Wlodawer, A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.