메뉴 건너뛰기




Volumn 105, Issue 3, 1997, Pages 161-186

Interferons α/β and their receptors: Place in the hierarchy of cytokines

Author keywords

Cytokines; Interferons ; Receptors

Indexed keywords

ALPHA INTERFERON; BETA INTERFERON; CYTOKINE; INTERFERON; INTERFERON RECEPTOR; VACCINE;

EID: 0030948056     PISSN: 09034641     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1699-0463.1997.tb00556.x     Document Type: Review
Times cited : (13)

References (220)
  • 2
    • 0023685684 scopus 로고
    • Molecular cloning and expression of the human interferon-γ receptor
    • Agut, M., Dembic, Z. & Merlin, G.: Molecular cloning and expression of the human interferon-γ receptor. Cell 55: 273-280, 1988.
    • (1988) Cell , vol.55 , pp. 273-280
    • Agut, M.1    Dembic, Z.2    Merlin, G.3
  • 3
    • 0028216387 scopus 로고
    • Chemokine receptors and molecular mimicry
    • Ahuja, S. K., Gao, J.-L. & Murphy, P. M.: Chemokine receptors and molecular mimicry. Immunol. Today. 15: 281-287, 1994.
    • (1994) Immunol. Today , vol.15 , pp. 281-287
    • Ahuja, S.K.1    Gao, J.-L.2    Murphy, P.M.3
  • 5
    • 0026771315 scopus 로고
    • Multiple amino acid substitutions suggest a structural basis for the separation of biological activity and receptor binding in a mutant IL-1β protein
    • Auron, P. E., Quigley, G. J., Rosenwasser, L. J. & Gehrke, L.: Multiple amino acid substitutions suggest a structural basis for the separation of biological activity and receptor binding in a mutant IL-1β protein. Biochemistry 31: 6632-6638, 1992.
    • (1992) Biochemistry , vol.31 , pp. 6632-6638
    • Auron, P.E.1    Quigley, G.J.2    Rosenwasser, L.J.3    Gehrke, L.4
  • 6
    • 43949153331 scopus 로고
    • CC chemokines in allergic inflammation
    • Baggiolini, M. & Dahinden, C. A.: CC chemokines in allergic inflammation. Immunol. Today 75: 127-133, 1994.
    • (1994) Immunol. Today , vol.75 , pp. 127-133
    • Baggiolini, M.1    Dahinden, C.A.2
  • 8
    • 0027931295 scopus 로고
    • Predictive modelling of the 3-D structure of interleukin 13
    • Bamborough, P., Duncan, D. & Richards, W. G.: Predictive modelling of the 3-D structure of interleukin 13. Protein Eng. 7: 1077-1082, 1994.
    • (1994) Protein Eng. , vol.7 , pp. 1077-1082
    • Bamborough, P.1    Duncan, D.2    Richards, W.G.3
  • 10
    • 0028774180 scopus 로고
    • The IL-2 and IL-4 receptors studied by molecular modelling
    • Bamborough, P., Hedgecock, C. J. R. & Richards, W. G.: The IL-2 and IL-4 receptors studied by molecular modelling. Structure 2: 839-851, 1994.
    • (1994) Structure , vol.2 , pp. 839-851
    • Bamborough, P.1    Hedgecock, C.J.R.2    Richards, W.G.3
  • 11
    • 0027211704 scopus 로고
    • Crystal structure of the soluble human 55 kd TNF receptor-human TNFβ complex: Implications for TNF receptor activation
    • Banner, D. W., D'Arcy, A., Janes, W., Gentz, R., Schoenfeld, H.-J., Broger, C, Loetscher, H. & Lesslaner, W.: Crystal structure of the soluble human 55 kd TNF receptor-human TNFβ complex: implications for TNF receptor activation. Cell 73: 431-445, 1993.
    • (1993) Cell , vol.73 , pp. 431-445
    • Banner, D.W.1    D'Arcy, A.2    Janes, W.3    Gentz, R.4    Schoenfeld, H.-J.5    Broger, C.6    Loetscher, H.7    Lesslaner, W.8
  • 12
    • 0024400767 scopus 로고
    • Antibodies against a peptide representative of a conserved region of human IFN-α
    • Barasoain, I., Portoles, A., Aramburu, J. F. & Rojo, J. M.: Antibodies against a peptide representative of a conserved region of human IFN-α. J. Immunol. 143: 507-512, 1989.
    • (1989) J. Immunol. , vol.143 , pp. 507-512
    • Barasoain, I.1    Portoles, A.2    Aramburu, J.F.3    Rojo, J.M.4
  • 13
    • 0029009058 scopus 로고
    • Postmodern complexes
    • Bazan, J. F.: Postmodern complexes. Nature 376: 217-218, 1995.
    • (1995) Nature , vol.376 , pp. 217-218
    • Bazan, J.F.1
  • 14
    • 0024469936 scopus 로고
    • A novel family of growth factor receptors: A common binding domain in the growth hormone, prolactin, erythropoietin and IL-6 receptors, and the p75 IL-2 receptor β-chain
    • Bazan, J. F.: A novel family of growth factor receptors: a common binding domain in the growth hormone, prolactin, erythropoietin and IL-6 receptors, and the p75 IL-2 receptor β-chain. Biochem. Biophys. Res. Commun. 164: 788-795, 1989.
    • (1989) Biochem. Biophys. Res. Commun. , vol.164 , pp. 788-795
    • Bazan, J.F.1
  • 15
    • 0025857387 scopus 로고
    • Genetic and structural homology of stem cell factor and macrophage colonystimulating factor
    • Bazan, J. F.: Genetic and structural homology of stem cell factor and macrophage colonystimulating factor. Cell 65: 9-10, 1991.
    • (1991) Cell , vol.65 , pp. 9-10
    • Bazan, J.F.1
  • 16
    • 0025102756 scopus 로고
    • Haemopoietic receptors and helical cytokines
    • Bazan, J. F.: Haemopoietic receptors and helical cytokines. Immunol. Today 11: 350-354, 1990.
    • (1990) Immunol. Today , vol.11 , pp. 350-354
    • Bazan, J.F.1
  • 17
    • 0025356737 scopus 로고
    • Shared architecture of hormone binding domains in type I and II interferon receptors
    • Bazan, J. F.: Shared architecture of hormone binding domains in type I and II interferon receptors. Cell 61: 753-754, 1990.
    • (1990) Cell , vol.61 , pp. 753-754
    • Bazan, J.F.1
  • 18
    • 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: 6934-6938, 1990.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 6934-6938
    • Bazan, J.F.1
  • 19
    • 0026763387 scopus 로고
    • Unraveling the structure of IL-2
    • Bazan, J. F.: Unraveling the structure of IL-2. Science 257: 410-412, 1992.
    • (1992) Science , vol.257 , pp. 410-412
    • Bazan, J.F.1
  • 20
    • 0027238097 scopus 로고
    • A monoclonal antibody to recombinant human IFN-α receptor inhibits biological activity of several species of human IFN-α, IFN-β and IFN-ω
    • Benoit, P., Maguire, D., Plavec, I., Kocher, H., Tovey, M. & Meyer, F.: A monoclonal antibody to recombinant human IFN-α receptor inhibits biological activity of several species of human IFN-α, IFN-β and IFN-ω. J. Immunol. 150: 707-716, 1993.
    • (1993) J. Immunol. , vol.150 , pp. 707-716
    • Benoit, P.1    Maguire, D.2    Plavec, I.3    Kocher, H.4    Tovey, M.5    Meyer, F.6
  • 21
    • 0028646202 scopus 로고
    • Cytokines and natural regulators of cytokines
    • Bentdzen, K.: Cytokines and natural regulators of cytokines. Immunol. Lett. 43: 111-123, 1994.
    • (1994) Immunol. Lett. , vol.43 , pp. 111-123
    • Bentdzen, K.1
  • 22
    • 0029021306 scopus 로고
    • Serum gangliosides as endogenous immunomodulators
    • Bergelson, L. D.: Serum gangliosides as endogenous immunomodulators. Immunol. Today 16: 483-486, 1995.
    • (1995) Immunol. Today , vol.16 , pp. 483-486
    • Bergelson, L.D.1
  • 23
    • 0016355854 scopus 로고
    • Inhibition of interferon action by gangliosides
    • Besankon, F. & Ankel, H. : Inhibition of interferon action by gangliosides. Nature 252: 478-480, 1974.
    • (1974) Nature , vol.252 , pp. 478-480
    • Besankon, F.1    Ankel, H.2
  • 24
    • 0016135909 scopus 로고
    • Inhibition of interferon action by plant lectins
    • Besankon, F. & Ankel, H.: Inhibition of interferon action by plant lectins. Nature 250: 782-785, 1974.
    • (1974) Nature , vol.250 , pp. 782-785
    • Besankon, F.1    Ankel, H.2
  • 25
    • 0017310685 scopus 로고
    • Specificity and reversibility of interferon ganglioside interaction
    • Besankon, F., Ankel, H. & Basu, S.: Specificity and reversibility of interferon ganglioside interaction. Nature 259: 576-578, 1976.
    • (1976) Nature , vol.259 , pp. 576-578
    • Besankon, F.1    Ankel, H.2    Basu, S.3
  • 26
    • 0027297047 scopus 로고
    • Erythropoietin structure-function relationships. Mutant proteins that test a model of tertiary structure
    • Boissel, J.-P., Lee, W.-R., Presnell, S. R., Cohen, F. E. & Bunn, H. F.: Erythropoietin structure-function relationships. Mutant proteins that test a model of tertiary structure. J. Biol. Chem. 268: 15983-15993, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 15983-15993
    • Boissel, J.-P.1    Lee, W.-R.2    Presnell, S.R.3    Cohen, F.E.4    Bunn, H.F.5
  • 30
    • 0027236656 scopus 로고
    • The role of asparagine-32 in forming the receptor-binding epitope of human epidermal growth factor
    • Campion, S.- R., Biamonti, C., Montelione, G. T. & Niyogi, S. K.: The role of asparagine-32 in forming the receptor-binding epitope of human epidermal growth factor. Protein Eng. 6: 651 - 659, 1993.
    • (1993) Protein Eng. , vol.6 , pp. 651-659
    • Campion, S.R.1    Biamonti, C.2    Montelione, G.T.3    Niyogi, S.K.4
  • 32
    • 0024555819 scopus 로고
    • The three-dimensional structure of bovine platelet factor 4 at 3.0Å resolution
    • Charles, R. S., Walz, D. A. & Edwards, B. F. P.: The three-dimensional structure of bovine platelet factor 4 at 3.0Å resolution. J. Biol. Chem. 264: 2092-2099, 1989.
    • (1989) J. Biol. Chem. , vol.264 , pp. 2092-2099
    • Charles, R.S.1    Walz, D.A.2    Edwards, B.F.P.3
  • 33
    • 0026489233 scopus 로고
    • Anatomy and evolution of proteins displaying the viral capsid jellyroll topology
    • Chelvanayagam. G., Heringa, J. & Argos, P.: Anatomy and evolution of proteins displaying the viral capsid jellyroll topology. J. Mol. Biol. 228: 220-242, 1992.
    • (1992) J. Mol. Biol. , vol.228 , pp. 220-242
    • Chelvanayagam, G.1    Heringa, J.2    Argos, P.3
  • 34
    • 0028843419 scopus 로고
    • Three-dimensional structures of a and β chemokines
    • Clore, G. M. & Gronenborn, A. M.: Three-dimensional structures of a and β chemokines. FASEB J. 9: 57-62, 1995.
    • (1995) FASEB J. , vol.9 , pp. 57-62
    • Clore, G.M.1    Gronenborn, A.M.2
  • 35
    • 0024853551 scopus 로고
    • Determination of the secondary structure of interleukin-8 by nuclear magnetic resonance spectroscopy
    • Clore, G. M., Appella, E., Yamada, M., Matsushima, K. & Gronenborn, A. M.: Determination of the secondary structure of interleukin-8 by nuclear magnetic resonance spectroscopy. J. Biol. Chem. 264: 18907-18911, 1989.
    • (1989) J. Biol. Chem. , vol.264 , pp. 18907-18911
    • Clore, G.M.1    Appella, E.2    Yamada, M.3    Matsushima, K.4    Gronenborn, A.M.5
  • 37
    • 0025772135 scopus 로고
    • High-resolution threedimensional structure of interleukin 1β in solution by three- and four-dimensional nuclear magnetic resonance spectroscopy
    • Clore, G. M., Wingfield, P. O., Wingfield, P. T. & Gronenborn, A. M.: High-resolution threedimensional structure of interleukin 1β in solution by three- and four-dimensional nuclear magnetic resonance spectroscopy. Biochemistry 30: 2315-2323, 1991.
    • (1991) Biochemistry , vol.30 , pp. 2315-2323
    • Clore, G.M.1    Wingfield, P.O.2    Wingfield, P.T.3    Gronenborn, A.M.4
  • 38
    • 0028053158 scopus 로고
    • Mapping the binding surface of interleukin-8 complexed with an N-terminal fragment of the type 1 human interleukin-8 receptor
    • Clubb, R. T., Omichinski, J. G., Clore, G. M. & Gronenborn, A. M.: Mapping the binding surface of interleukin-8 complexed with an N-terminal fragment of the type 1 human interleukin-8 receptor. FEBS Lett. 338: 93-97, 1994.
    • (1994) FEBS Lett. , vol.338 , pp. 93-97
    • Clubb, R.T.1    Omichinski, J.G.2    Clore, G.M.3    Gronenborn, A.M.4
  • 39
    • 0029052176 scopus 로고
    • Ligand-indueed association of the type I interferon receptor components
    • Cohen, B., Novick, D., Barak, S. & Rubinstein, M.: Ligand-indueed association of the type I interferon receptor components. Mol. Cell. Biol. 15: 4208-4214, 1995.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4208-4214
    • Cohen, B.1    Novick, D.2    Barak, S.3    Rubinstein, M.4
  • 40
    • 0026462899 scopus 로고
    • Structural analysis of the human IFN-γ receptor: A small segment of the intracellular domain is specifically required for class I MHC antigen induction and antiviral activity
    • Cook, J. R., Jung, V., Schwartz, B., Wang, P. & Pestka, S.: Structural analysis of the human IFN-γ receptor: A small segment of the intracellular domain is specifically required for class I MHC antigen induction and antiviral activity. Proc. Natl. Acad. Sci. USA 89: 11317-11321, 1992.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 11317-11321
    • Cook, J.R.1    Jung, V.2    Schwartz, B.3    Wang, P.4    Pestka, S.5
  • 41
    • 0025822851 scopus 로고
    • Solution structure of human insulin-like growth factor 1 : A nuclear magnetic resonance and restrained molecular dynamics study
    • Cooke, R. M., Harvey, T. S. & Campbell, I. D.: Solution structure of human insulin-like growth factor 1 : A nuclear magnetic resonance and restrained molecular dynamics study. Biochemistry 30: 5484-5491, 1991.
    • (1991) Biochemistry , vol.30 , pp. 5484-5491
    • Cooke, R.M.1    Harvey, T.S.2    Campbell, I.D.3
  • 44
    • 0025615418 scopus 로고
    • Zinc mediation of the binding of human growth hormone to the human prolactin receptor
    • Cunningham, B. C., Bass, S., Fuh, G. & Wells, J. A.: Zinc mediation of the binding of human growth hormone to the human prolactin receptor. Science 250: 1709-1712, 1990.
    • (1990) Science , vol.250 , pp. 1709-1712
    • Cunningham, B.C.1    Bass, S.2    Fuh, G.3    Wells, J.A.4
  • 45
    • 0028924966 scopus 로고
    • Structure-function relationships in human interleukin-11. Identification of regions involved in activity by chemical modification and sitedirected mutagenesis
    • Czupryn, M. J., Mccoy, J. M. & Scoble, H. A.: Structure-function relationships in human interleukin-11. Identification of regions involved in activity by chemical modification and sitedirected mutagenesis. J. Biol. Chem. 270: 978-985, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 978-985
    • Czupryn, M.J.1    Mccoy, J.M.2    Scoble, H.A.3
  • 46
    • 0028215220 scopus 로고
    • Cloning, genomic organization, and chromosomal localization of the Scya5 gene encoding the murine chemokine RANTES
    • Danoff, T. M., Lalley, P. A., Chang, Y. S., Heeger, P. S. & Neilson, E. G.: Cloning, genomic organization, and chromosomal localization of the Scya5 gene encoding the murine chemokine RANTES. J. Immunol. 152: 1182-1189, 1994.
    • (1994) J. Immunol. , vol.152 , pp. 1182-1189
    • Danoff, T.M.1    Lalley, P.A.2    Chang, Y.S.3    Heeger, P.S.4    Neilson, E.G.5
  • 47
    • 0027429069 scopus 로고
    • Crystal structure of TGF-β2 refined at 1.8Å resolution
    • Daopin, S., Li, M. & Davies, D. R.: Crystal structure of TGF-β2 refined at 1.8Å resolution. Proteins 17: 176-192, 1993.
    • (1993) Proteins , vol.17 , pp. 176-192
    • Daopin, S.1    Li, M.2    Davies, D.R.3
  • 48
    • 0027122245 scopus 로고
    • Crystal structure of transforming growth factor- β2: An unusual fold for the superfamily
    • Daopin, S., Piez, K. A., Ogawa, Y. & Davies, D. R. : Crystal structure of transforming growth factor- β2: An unusual fold for the superfamily. Science 257: 369-373, 1992.
    • (1992) Science , vol.257 , pp. 369-373
    • Daopin, S.1    Piez, K.A.2    Ogawa, Y.3    Davies, D.R.4
  • 49
    • 0028887623 scopus 로고
    • Cytokines and their receptor complexes
    • Davies, D. & Wlodawer, A.: Cytokines and their receptor complexes. FASEB J. 9: 50-56, 1995.
    • (1995) FASEB J. , vol.9 , pp. 50-56
    • Davies, D.1    Wlodawer, A.2
  • 50
    • 0027073357 scopus 로고
    • Engineering disulfide bond greatly increases specific activity of recombinant murine interferon-β
    • Day, C., Schwartz, B., Li. B.-L. & Pestka, S.: Engineering disulfide bond greatly increases specific activity of recombinant murine interferon-β. J. Interferon Res. 12: 139-143, 1992.
    • (1992) J. Interferon Res. , vol.12 , pp. 139-143
    • Day, C.1    Schwartz, B.2    Li, B.-L.3    Pestka, S.4
  • 51
    • 0028291136 scopus 로고
    • Receptor binding properties of four-helix bundle growth factors deduced from electrostatic analysis
    • Demchuk, E., Mueller, T., Oschkinat, H., Sebald, W. & Wade, R. C. : Receptor binding properties of four-helix bundle growth factors deduced from electrostatic analysis. Protein Sci. 3: 920-935, 1994.
    • (1994) Protein Sci. , vol.3 , pp. 920-935
    • Demchuk, E.1    Mueller, T.2    Oschkinat, H.3    Sebald, W.4    Wade, R.C.5
  • 54
    • 0028168753 scopus 로고
    • Modelling of interhelical contacts in interferons-β, -γ, and dimeric interleukin-5
    • Denesyuk, A. I., Zav'yalov, V. P. & Korpela, T.: Modelling of interhelical contacts in interferons-β, -γ, and dimeric interleukin-5. Biochem. Biophys. Res. Commun. 207: 1401-1405, 1994.
    • (1994) Biochem. Biophys. Res. Commun. , vol.207 , pp. 1401-1405
    • Denesyuk, A.I.1    Zav'yalov, V.P.2    Korpela, T.3
  • 56
    • 0026320870 scopus 로고
    • Novel fold and putative receptor binding site of granulocyte-macrophage colony-stimulating factor
    • Diederichs, K., Boone, T. & Karplus, P. A.: Novel fold and putative receptor binding site of granulocyte-macrophage colony-stimulating factor. Science 254: 1779-1782, 1991.
    • (1991) Science , vol.254 , pp. 1779-1782
    • Diederichs, K.1    Boone, T.2    Karplus, P.A.3
  • 58
    • 0029148972 scopus 로고
    • Cloning and expression of a long form of the beta subunit of the interferon alpha beta receptor that is required for signaling
    • Domanski, P., Witte, M., Kellum, M., Rubinstein, M., Hacket, R., Pitha, P. & Colamonici, O. R.: Cloning and expression of a long form of the beta subunit of the interferon alpha beta receptor that is required for signaling. J. Biol. Chem. 270: 21606-21611, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21606-21611
    • Domanski, P.1    Witte, M.2    Kellum, M.3    Rubinstein, M.4    Hacket, R.5    Pitha, P.6    Colamonici, O.R.7
  • 59
    • 0026182918 scopus 로고
    • Fluorescence polarization, circular dichroism and microcalorimetry study of structural features of human recombinant leukocyte interferon A
    • Dudich, I. V., Dudich, E. I., Kulevatsky, D. P. & Zav'yalov, V. P.: Fluorescence polarization, circular dichroism and microcalorimetry study of structural features of human recombinant leukocyte interferon A. Mol. Biol. Mosc. 25: 1061-1070, 1991.
    • (1991) Mol. Biol. Mosc. , vol.25 , pp. 1061-1070
    • Dudich, I.V.1    Dudich, E.I.2    Kulevatsky, D.P.3    Zav'yalov, V.P.4
  • 60
    • 0026833324 scopus 로고
    • Scanning difference microcalorimetry and circular dichroism study of recombinant γ-interferon structure
    • Dudich, I. V., Zav'yalov, V. P., Bumelis, A. V. & Paulauskas, D. V.: Scanning difference microcalorimetry and circular dichroism study of recombinant γ-interferon structure. Mol. Biol. Mosc. 26: 441-451, 1992.
    • (1992) Mol. Biol. Mosc. , vol.26 , pp. 441-451
    • Dudich, I.V.1    Zav'yalov, V.P.2    Bumelis, A.V.3    Paulauskas, D.V.4
  • 62
    • 0024357657 scopus 로고
    • The structure of tumor necrosis factor-α at 2.6Å resolution
    • Eck, M. J. & Sprang, S. R.: The structure of tumor necrosis factor-α at 2.6Å resolution. J. Biol. Chem. 264: 17595-17605, 1989.
    • (1989) J. Biol. Chem. , vol.264 , pp. 17595-17605
    • Eck, M.J.1    Sprang, S.R.2
  • 63
    • 0026787018 scopus 로고
    • The structure of human lymhotoxin (tumor necrosis factor-β) at 1.9Å resolution
    • Eck, M. J., Ultsch, M., Rinderknecht, E., De Vos, A. M. & Sprang, S. R.: The structure of human lymhotoxin (tumor necrosis factor-β) at 1.9Å resolution. J. Biol. Chem. 267: 2119-2122, 1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 2119-2122
    • Eck, M.J.1    Ultsch, M.2    Rinderknecht, E.3    De Vos, A.M.4    Sprang, S.R.5
  • 64
    • 0025333391 scopus 로고
    • Biological activities of synthetic peptides of the sequence of human interferon-alpha
    • Eichman, E., Maiorov, V. A., Kozhich, A. T., Noll, F. & Zav'yalov, V. P.: Biological activities of synthetic peptides of the sequence of human interferon-alpha. Immunol. Lett. 24: 233-236, 1990.
    • (1990) Immunol. Lett. , vol.24 , pp. 233-236
    • Eichman, E.1    Maiorov, V.A.2    Kozhich, A.T.3    Noll, F.4    Zav'yalov, V.P.5
  • 65
    • 0025812626 scopus 로고
    • X-ray structure of human relaxin at 1.5Å. Comparison to insulin and implications for receptor binding determinants
    • Eigenbrot, C., Randal, M., Quan, C., Burnier, J. I., O'Connell, L., Rinderknecht, E. & Kossiakoff, A. A.: X-ray structure of human relaxin at 1.5Å. Comparison to insulin and implications for receptor binding determinants. J. Mol. Biol. 227: 15-21, 1991.
    • (1991) J. Mol. Biol. , vol.227 , pp. 15-21
    • Eigenbrot, C.1    Randal, M.2    Quan, C.3    Burnier, J.I.4    O'Connell, L.5    Rinderknecht, E.6    Kossiakoff, A.A.7
  • 66
    • 0028988974 scopus 로고
    • 15N NMR resonance assignments, secondary structure, and backbone topology of a variant of human interleukin-3
    • 15N NMR resonance assignments, secondary structure, and backbone topology of a variant of human interleukin-3. Biochemistry 34: 6540-6551, 1995.
    • (1995) Biochemistry , vol.34 , pp. 6540-6551
    • Feng, Y.1    Klein, B.K.2    Vu, L.3    Avkent, S.4    Mcwherter, C.H.A.5
  • 68
    • 0024502589 scopus 로고
    • The role of three domains in the biological activity of human interferon-alpha
    • Fish, E. N., Banerjee, K. & Stebbing, N.: The role of three domains in the biological activity of human interferon-alpha. J. Interferon Res. 9: 97-114, 1989.
    • (1989) J. Interferon Res. , vol.9 , pp. 97-114
    • Fish, E.N.1    Banerjee, K.2    Stebbing, N.3
  • 69
    • 0026908951 scopus 로고
    • Definition of receptor binding domains in interferon alpha
    • Fish, E. N.: Definition of receptor binding domains in interferon alpha. J. Interferon Res. 12: 257-266, 1992.
    • (1992) J. Interferon Res. , vol.12 , pp. 257-266
    • Fish, E.N.1
  • 70
    • 0027332995 scopus 로고
    • Cloning of a TGFβ type I receptor that forms a heteromeric complex with the TGFβ type II receptor
    • Franzen, P., Dijke, P., Ichijo, H., Yamashita, H., Schultz, P., Helden, C.-H. & Miyazono, K.: Cloning of a TGFβ type I receptor that forms a heteromeric complex with the TGFβ type II receptor. Cell 75: 681-692, 1993.
    • (1993) Cell , vol.75 , pp. 681-692
    • Franzen, P.1    Dijke, P.2    Ichijo, H.3    Yamashita, H.4    Schultz, P.5    Helden, C.-H.6    Miyazono, K.7
  • 72
    • 0027536507 scopus 로고
    • Mechanism-based design of prolactin receptor antagonists
    • Fuh, G., Colosi, P., Wood, W. I. & Wells, J. A.: Mechanism-based design of prolactin receptor antagonists. J. Biol. Chem. 268: 5376-5381, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 5376-5381
    • Fuh, G.1    Colosi, P.2    Wood, W.I.3    Wells, J.A.4
  • 73
    • 0025861158 scopus 로고
    • Functional domains of the granulocyte colony-stimulating factor receptor
    • Fukunaga, R., Ishizaka-Ikeda, E., Pan, C.-X., Seto, Y. & Nagata, S.: Functional domains of the granulocyte colony-stimulating factor receptor. EMBO J. 10: 2855-2865, 1991.
    • (1991) EMBO J. , vol.10 , pp. 2855-2865
    • Fukunaga, R.1    Ishizaka-Ikeda, E.2    Pan, C.-X.3    Seto, Y.4    Nagata, S.5
  • 74
    • 0025270168 scopus 로고
    • Expression cloning of a receptor for murine granulocyte colony-stimulating factor
    • Fnkunaga, R., Ishizaka-Ikeda, E., Seto, Y. & Nagata, S.: Expression cloning of a receptor for murine granulocyte colony-stimulating factor. Cell 61: 341-350, 1990.
    • (1990) Cell , vol.61 , pp. 341-350
    • Fnkunaga, R.1    Ishizaka-Ikeda, E.2    Seto, Y.3    Nagata, S.4
  • 75
    • 0024846310 scopus 로고
    • Expression cloning of a receptor for human granulocyte-macrophage colonystimulating factor
    • Gearing, D. P., King, J. A., Gough, N. M. & Nicola, N. A.: Expression cloning of a receptor for human granulocyte-macrophage colonystimulating factor. EMBO J. 8: 3667-3676, 1989.
    • (1989) EMBO J. , vol.8 , pp. 3667-3676
    • Gearing, D.P.1    King, J.A.2    Gough, N.M.3    Nicola, N.A.4
  • 77
    • 0027939351 scopus 로고
    • Evidence for glycosphingolipid modification of the type I interferon receptor
    • Ghislain, J., Lingwood, C. A. & Fish, E. N.: Evidence for glycosphingolipid modification of the type I interferon receptor. J. Immunol. 153: 3655-3663, 1994.
    • (1994) J. Immunol. , vol.153 , pp. 3655-3663
    • Ghislain, J.1    Lingwood, C.A.2    Fish, E.N.3
  • 80
    • 0026077101 scopus 로고
    • Aspartic acid 50 and tyrosine 108 are essential for receptor binding and cytotoxic activity of tumour necrosis factor beta (lymphotoxin)
    • Goh, C. R., Loh, C. S. & Porter, A. G.: Aspartic acid 50 and tyrosine 108 are essential for receptor binding and cytotoxic activity of tumour necrosis factor beta (lymphotoxin). Protein Eng. 4: 785-791, 1991.
    • (1991) Protein Eng. , vol.4 , pp. 785-791
    • Goh, C.R.1    Loh, C.S.2    Porter, A.G.3
  • 84
    • 0019971912 scopus 로고
    • Structure of human immune interferon gene
    • Gray, P. W. & Goeddel, D. V.: Structure of human immune interferon gene. Nature 298: 859-863, 1982.
    • (1982) Nature , vol.298 , pp. 859-863
    • Gray, P.W.1    Goeddel, D.V.2
  • 85
    • 0026031627 scopus 로고
    • Modelling the three-dimensional structure of the monocyte chemo-attractant and activating protein MCAF/MCP-1 on the basis of the solution structure of interleukin-8
    • Gronenborn, A. M. & Clore, G. M.: Modelling the three-dimensional structure of the monocyte chemo-attractant and activating protein MCAF/MCP-1 on the basis of the solution structure of interleukin-8. Protein Eng. 4: 263-269, 1991.
    • (1991) Protein Eng. , vol.4 , pp. 263-269
    • Gronenborn, A.M.1    Clore, G.M.2
  • 86
    • 0028847977 scopus 로고
    • A model of the complex between interleukin-4 and its receptors
    • Gustehina, A., Zdanov, A., Schalk-Hihi, C. & Wlodawer, A.: A model of the complex between interleukin-4 and its receptors. Proteins 21: 140-148, 1995.
    • (1995) Proteins , vol.21 , pp. 140-148
    • Gustehina, A.1    Zdanov, A.2    Schalk-Hihi, C.3    Wlodawer, A.4
  • 87
    • 0028117299 scopus 로고
    • Cytokine therapeutics: Lesions from interferon α
    • Gutterman, J. U.: Cytokine therapeutics: lesions from interferon α. Proc. Natl. Acad. Sci. USA 91: 1198-1205, 1994.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 1198-1205
    • Gutterman, J.U.1
  • 88
    • 0028104676 scopus 로고
    • The three-dimensional structure of rat cytokine CINC/Gro in solution by homonuclear 3D NMR
    • Hanzawa, H., Haruygama, H., Watanabe, K. & Tsurufuju, S.: The three-dimensional structure of rat cytokine CINC/Gro in solution by homonuclear 3D NMR. FEBS Lett. 354: 207-212, 1994.
    • (1994) FEBS Lett. , vol.354 , pp. 207-212
    • Hanzawa, H.1    Haruygama, H.2    Watanabe, K.3    Tsurufuju, S.4
  • 89
    • 0024403321 scopus 로고
    • Interleukin-2 receptor β-chain gene: Generation of three receptor forms by cloned human alpha and beta chain cDNA's
    • Hatakeyama, M., Tsudo, M., Minamoto, S., Kono, T., Doi, T., Miyata, T., Miyasaka, M. & Taniguchi, T.: Interleukin-2 receptor β-chain gene: generation of three receptor forms by cloned human alpha and beta chain cDNA's. Science 244: 551-556, 1989.
    • (1989) Science , vol.244 , pp. 551-556
    • Hatakeyama, M.1    Tsudo, M.2    Minamoto, S.3    Kono, T.4    Doi, T.5    Miyata, T.6    Miyasaka, M.7    Taniguchi, T.8
  • 91
    • 0028567868 scopus 로고
    • De novo design of β-sheet proteins
    • Hecht, M. H.: De novo design of β-sheet proteins. Proc. Natl. Acad. Sci. USA 91: 8729-8730, 1994.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 8729-8730
    • Hecht, M.H.1
  • 92
    • 0027293058 scopus 로고
    • Partial functional mapping of the human interleukin-8 type A receptor. Identification of a major ligand binding domain
    • Herbert, C. A., Chuntharapai, A., Smith, M., Colby, T., Kim, J. & Horuk, R.: Partial functional mapping of the human interleukin-8 type A receptor. Identification of a major ligand binding domain. J. Biol. Chem. 268: 18549-18553, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 18549-18553
    • Herbert, C.A.1    Chuntharapai, A.2    Smith, M.3    Colby, T.4    Kim, J.5    Horuk, R.6
  • 93
    • 0027258762 scopus 로고
    • The structure of granoloeyte-colony-stimulating factor and its relationship to other growth factors
    • Hill, C. P., Osslund, T. D. & Eisenberg, D.: The structure of granoloeyte-colony-stimulating factor and its relationship to other growth factors. Proc. Natl. Acad. Sci. USA 90: 5167-5171, 1993.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5167-5171
    • Hill, C.P.1    Osslund, T.D.2    Eisenberg, D.3
  • 96
    • 0026662288 scopus 로고
    • Human epidermal growth factor. High resolution solution structure and comparison with epidermal growth factor α
    • Hommel, U., Harvey, T. S., Driscoll, P. C. & Campbell, I. D.: Human epidermal growth factor. High resolution solution structure and comparison with epidermal growth factor α. J. Mol. Biol. 227: 271-282, 1992.
    • (1992) J. Mol. Biol. , vol.227 , pp. 271-282
    • Hommel, U.1    Harvey, T.S.2    Driscoll, P.C.3    Campbell, I.D.4
  • 97
    • 43949155066 scopus 로고
    • The interleukin-8-receptor family: From chemokines to malaria
    • Horuk, R.: The interleukin-8-receptor family: from chemokines to malaria. Immunol. Today 15: 169-174, 1994.
    • (1994) Immunol. Today , vol.15 , pp. 169-174
    • Horuk, R.1
  • 98
    • 0025996911 scopus 로고
    • Receptor binding redefined by a structural switch in a mutant human insulin
    • Hua, Q. X., Shoelson, S. E., Kochoyan, M. & Weiss, M. A.: Receptor binding redefined by a structural switch in a mutant human insulin. Nature 354: 238-241, 1991.
    • (1991) Nature , vol.354 , pp. 238-241
    • Hua, Q.X.1    Shoelson, S.E.2    Kochoyan, M.3    Weiss, M.A.4
  • 99
    • 0029064557 scopus 로고
    • Neutrophic factors: From structure-function studies to designing effective therapeutics
    • Ibanez, C. F.: Neutrophic factors: from structure-function studies to designing effective therapeutics. Trends Biotechnol. 13: 217-227, 1995.
    • (1995) Trends Biotechnol. , vol.13 , pp. 217-227
    • Ibanez, C.F.1
  • 100
    • 0028921573 scopus 로고
    • Jaks and Stats in signaling by the cytokine receptor superfamily
    • Ihle, J. N. & Kerr, I. M.: Jaks and Stats in signaling by the cytokine receptor superfamily. Trends Genet. 11: 69-74, 1995.
    • (1995) Trends Genet. , vol.11 , pp. 69-74
    • Ihle, J.N.1    Kerr, I.M.2
  • 103
    • 0024539057 scopus 로고
    • Structure of tumor necrosis factor
    • Jones, E. Y., Stuart, D. I. & Walker, N. P. C.: Structure of tumor necrosis factor. Nature 338: 225-228, 1989.
    • (1989) Nature , vol.338 , pp. 225-228
    • Jones, E.Y.1    Stuart, D.I.2    Walker, N.P.C.3
  • 106
    • 0026464730 scopus 로고
    • Three-dimensional nuclear magnetic resonance structures of mouse epidermal growth factor in acidic and physiological pH solutions
    • Kohda, D. & Inagaki, F.: Three-dimensional nuclear magnetic resonance structures of mouse epidermal growth factor in acidic and physiological pH solutions. Biochemistry 31: 11928-11939, 1992.
    • (1992) Biochemistry , vol.31 , pp. 11928-11939
    • Kohda, D.1    Inagaki, F.2
  • 108
    • 0027731604 scopus 로고
    • Sharing of the interleukin-2 (IL-2) receptor γ chain between receptors for IL-2 and IL-4
    • Kondo, M., Takeshita, T., Ishii, N., Nakamura, M., Watanabe, S., Arai, K.-I. & Sugamura, K.: Sharing of the interleukin-2 (IL-2) receptor γ chain between receptors for IL-2 and IL-4. Science 262: 1874-1877, 1993.
    • (1993) Science , vol.262 , pp. 1874-1877
    • Kondo, M.1    Takeshita, T.2    Ishii, N.3    Nakamura, M.4    Watanabe, S.5    Arai, K.-I.6    Sugamura, K.7
  • 110
    • 0026058721 scopus 로고
    • Mapping of two immunodominant structures on human interferon alpha 2c and their role in binding to cells
    • Kontsek, P., Borecky, L., Kontsekova, E., Macicova, I., Kolcunova, A., Novak, M. & Krchnak, V.: Mapping of two immunodominant structures on human interferon alpha 2c and their role in binding to cells. Mol. Immunol. 28: 1289-1297, 1991.
    • (1991) Mol. Immunol. , vol.28 , pp. 1289-1297
    • Kontsek, P.1    Borecky, L.2    Kontsekova, E.3    Macicova, I.4    Kolcunova, A.5    Novak, M.6    Krchnak, V.7
  • 111
    • 0027463273 scopus 로고
    • Peptide-mapping of three neutralizing epitopes into predicted biologically active sites of human interferon-α2
    • Kontsek, P., Borecky, L., Zav'yalov, V. P. & Maiorov, V. A.: Peptide-mapping of three neutralizing epitopes into predicted biologically active sites of human interferon-α2. Immunol. Lett. 35: 281-284, 1993.
    • (1993) Immunol. Lett. , vol.35 , pp. 281-284
    • Kontsek, P.1    Borecky, L.2    Zav'yalov, V.P.3    Maiorov, V.A.4
  • 112
    • 0027451432 scopus 로고
    • Two distinct functional sites of human interleukin 4 are identified by variants impaired in either receptor binding or receptor activation
    • Kruse, N., Shen, B.-J., Arnold, S., Tony, H.-P., Müller, T. & Sebald, W.: Two distinct functional sites of human interleukin 4 are identified by variants impaired in either receptor binding or receptor activation. EMBO J. 12: 5121-5129, 1993.
    • (1993) EMBO J. , vol.12 , pp. 5121-5129
    • Kruse, N.1    Shen, B.-J.2    Arnold, S.3    Tony, H.-P.4    Müller, T.5    Sebald, W.6
  • 114
    • 0026490256 scopus 로고
    • Structure of a fibronectin type III domain from tenascin phased by MAD analysis of the selenomethionyl protein
    • Leahy, D. H., Hendrickson, W. A., Aukhil, I. & Erickson, H. P.: Structure of a fibronectin type III domain from tenascin phased by MAD analysis of the selenomethionyl protein. Science 258: 987-991, 1992.
    • (1992) Science , vol.258 , pp. 987-991
    • Leahy, D.H.1    Hendrickson, W.A.2    Aukhil, I.3    Erickson, H.P.4
  • 115
    • 0027500807 scopus 로고
    • Structure-function analysis of the C-terminal segment of human interleukin-6
    • Li, X., Rock, F., Chong, P., Cockle, S., Keating, A., Zilterner, H. & Klein, M.: Structure-function analysis of the C-terminal segment of human interleukin-6. J. Biol. Chem. 268: 22377-22384, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22377-22384
    • Li, X.1    Rock, F.2    Chong, P.3    Cockle, S.4    Keating, A.5    Zilterner, H.6    Klein, M.7
  • 116
    • 0028350053 scopus 로고
    • Expression cloning and characterization of a human IL-1O receptor
    • Liu, Y., Wei, S. H.-Y., Ho, A. S.-Y., Malefyt, R. W. & Moore, K. W.: Expression cloning and characterization of a human IL-1O receptor. J. Immunol. 152: 1821-1829, 1994.
    • (1994) J. Immunol. , vol.152 , pp. 1821-1829
    • Liu, Y.1    Wei, S.H.-Y.2    Ho, A.S.-Y.3    Malefyt, R.W.4    Moore, K.W.5
  • 120
    • 0025886263 scopus 로고
    • Structure-activity relationship study of human interleukin 3: Role of the C-terminal region for biological activity
    • Lokker, N. A., Zenke, G., Strittmatter, U., Fagg, B. & Movva, N. R.: Structure-activity relationship study of human interleukin 3: role of the C-terminal region for biological activity. EMBO J. 10: 2125-2131, 1991.
    • (1991) EMBO J. , vol.10 , pp. 2125-2131
    • Lokker, N.A.1    Zenke, G.2    Strittmatter, U.3    Fagg, B.4    Movva, N.R.5
  • 121
    • 0027141509 scopus 로고
    • Crystal structure of canine and bovine granulocyte-colony stimulating factor (G-CSF)
    • Lovejoy, B., Cascio, D. & Eisenberg, D.: Crystal structure of canine and bovine granulocyte-colony stimulating factor (G-CSF). J. Mol. Biol. 234: 640-653, 1993.
    • (1993) J. Mol. Biol. , vol.234 , pp. 640-653
    • Lovejoy, B.1    Cascio, D.2    Eisenberg, D.3
  • 122
    • 0028820423 scopus 로고
    • Mutant USA cells are complemented by an interferon-alpha beta receptor subunit generated by alternative processing of a new member of a cytokine receptor gene cluster
    • Lutfalla, G., Holland, S. J., Cinato, E., Monneron, D., Reboul, J., Rogers, N. C., Smith, J. M., Stark, G. R., Gardiner, K., Mogensen, K. E. et al.: Mutant USA cells are complemented by an interferon-alpha beta receptor subunit generated by alternative processing of a new member of a cytokine receptor gene cluster. EMBO J. 14: 5100-5108, 1995.
    • (1995) EMBO J. , vol.14 , pp. 5100-5108
    • Lutfalla, G.1    Holland, S.J.2    Cinato, E.3    Monneron, D.4    Reboul, J.5    Rogers, N.C.6    Smith, J.M.7    Stark, G.R.8    Gardiner, K.9    Mogensen, K.E.10
  • 123
    • 0024817465 scopus 로고
    • Prothymosin α is an evolutionary conserved protein covalently linked to a small RNA
    • Makarova, T., Grebenshikov, N., Egorov, C., Vartapetian, A. & Bogdanov, A.: Prothymosin α is an evolutionary conserved protein covalently linked to a small RNA. FEBS Lett. 257: 247-250, 1989.
    • (1989) FEBS Lett. , vol.257 , pp. 247-250
    • Makarova, T.1    Grebenshikov, N.2    Egorov, C.3    Vartapetian, A.4    Bogdanov, A.5
  • 124
    • 0028965079 scopus 로고
    • The crystal structure of recombinant human neutrophil-activating peptide-2 (MGL) at 1.9Å
    • Malkowski, M. G., Wu, J. Y., Lazar, J. B., Johnson, P. H. & Edwards, B. F. P.: The crystal structure of recombinant human neutrophil-activating peptide-2 (MGL) at 1.9Å. J. Biol. Chem. 270: 7077-7087, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 7077-7087
    • Malkowski, M.G.1    Wu, J.Y.2    Lazar, J.B.3    Johnson, P.H.4    Edwards, B.F.P.5
  • 125
    • 0025728020 scopus 로고
    • A new superfamily of cell surface proteins related to the nerve growth factor receptor
    • Mallett, S. & Barclay, A. N.: A new superfamily of cell surface proteins related to the nerve growth factor receptor. Immunol. Today 12: 220-223, 1991.
    • (1991) Immunol. Today , vol.12 , pp. 220-223
    • Mallett, S.1    Barclay, A.N.2
  • 126
    • 0022615379 scopus 로고
    • An interferon analogue, [Ala 30, 32, 33] HuIFN-α2, acting as a HuIFN-a2 antagonist on bovine cells
    • Marcucci, F. & de Mayer, E.: An interferon analogue, [Ala 30, 32, 33] HuIFN-α2, acting as a HuIFN-a2 antagonist on bovine cells. Biochem. Biopohys. Res. Commun. 134: 1412-1418, 1986.
    • (1986) Biochem. Biopohys. Res. Commun. , vol.134 , pp. 1412-1418
    • Marcucci, F.1    De Mayer, E.2
  • 127
    • 0027251256 scopus 로고
    • A structural superfamily of growth factors containing a cysteine knot motif
    • Mcdonald, N. Q. & Hendrickson, W. A.: A structural superfamily of growth factors containing a cysteine knot motif. Cell 73: 421-424, 1993.
    • (1993) Cell , vol.73 , pp. 421-424
    • Mcdonald, N.Q.1    Hendrickson, W.A.2
  • 128
    • 0029046795 scopus 로고
    • Crystal structure of dimeric human ciliary neurotrophic factor determined by MAD phasing
    • Mcdonald, N. Q., Panayotatos, N. & Hendrickson, W. A.: Crystal structure of dimeric human ciliary neurotrophic factor determined by MAD phasing. EMBO J. 14: 2689-2699, 1995.
    • (1995) EMBO J. , vol.14 , pp. 2689-2699
    • Mcdonald, N.Q.1    Panayotatos, N.2    Hendrickson, W.A.3
  • 129
    • 0021021637 scopus 로고
    • Cholera toxin genes: Nucleotide sequence, deletion analysis and vaccine development
    • Mekalanos, J. J., Swartz, D. J., Pearson, G. D. N., Harford, N., Groyne, F. & de Wilde, M.: Cholera toxin genes: nucleotide sequence, deletion analysis and vaccine development. Nature 306: 551-557, 1983.
    • (1983) Nature , vol.306 , pp. 551-557
    • Mekalanos, J.J.1    Swartz, D.J.2    Pearson, G.D.N.3    Harford, N.4    Groyne, F.5    De Wilde, M.6
  • 130
    • 0026570847 scopus 로고
    • Determination of ligand-binding specificity by alternative splicing: Two distinct growth factor receptors encoded by a single gene
    • Miki, T., Bottaro, D. P., Fleming, T. P., Smith, C. L, Burges, W. H., Chan, A. M.-L. & Aaronson, S. A.: Determination of ligand-binding specificity by alternative splicing: two distinct growth factor receptors encoded by a single gene. Proc. Natl. Acad. Sci. USA 89: 246-250, 1992.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 246-250
    • Miki, T.1    Bottaro, D.P.2    Fleming, T.P.3    Smith, C.L.4    Burges, W.H.5    Chan, A.M.-L.6    Aaronson, S.A.7
  • 131
    • 0027155448 scopus 로고
    • A novel dimer configuration revealed by the crystal structure at 2.4Å resolution of human interleukin-5
    • Milburn, M. V., Hassell, A. M., Lambert, M. H., Jordan, S. R., Proudfoot, A. E. I., Graber, P. & Wells, T. N. C.: A novel dimer configuration revealed by the crystal structure at 2.4Å resolution of human interleukin-5. Nature 363: 172-176, 1993.
    • (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.I.5    Graber, P.6    Wells, T.N.C.7
  • 133
    • 0027227660 scopus 로고
    • Structural, functional and evolutionary implications of the three-dimensional crystal structure of murine interferon-β
    • Mitsui, Y., Senda, T., Shimazu, T., Matsuda, S. & Utsumi, J.: Structural, functional and evolutionary implications of the three-dimensional crystal structure of murine interferon-β. Pharmacol. Ther. 58: 93-132, 1993.
    • (1993) Pharmacol. Ther. , vol.58 , pp. 93-132
    • Mitsui, Y.1    Senda, T.2    Shimazu, T.3    Matsuda, S.4    Utsumi, J.5
  • 134
    • 0021966053 scopus 로고
    • Evolution of interferon genes
    • Gresser, I. (Ed.): Academic Press, London
    • Miyata, T., Hayashida, H., Kiruno, R., Toh, H. & Kawade, Y.: Evolution of interferon genes. In: Gresser, I. (Ed.): Interferon 6. Academic Press, London, 1985, pp. 1-30.
    • (1985) Interferon , vol.6 , pp. 1-30
    • Miyata, T.1    Hayashida, H.2    Kiruno, R.3    Toh, H.4    Kawade, Y.5
  • 135
    • 0026795824 scopus 로고
    • Secondary structure of human interleukin 2 from 3D heteronuclear NMR experiments
    • Mott, H. R., Driscoll, P. C., Boyd, J., Cooke, R. M., Weir, M. P. & Campbell, I. D.: Secondary structure of human interleukin 2 from 3D heteronuclear NMR experiments. Biochemistry 31: 7741-7744, 1992.
    • (1992) Biochemistry , vol.31 , pp. 7741-7744
    • Mott, H.R.1    Driscoll, P.C.2    Boyd, J.3    Cooke, R.M.4    Weir, M.P.5    Campbell, I.D.6
  • 136
    • 0027308075 scopus 로고
    • Solution structure of human type-α transforming growth factor determined by heteronuclear NMR spectroscopy and refined by energy minimization with restraints
    • Moy, F. J., Li, Y.-C., Rauenbuehler, P., Winkler, M. E., Scheraga, H. A. & Montelione, G. T.: Solution structure of human type-α transforming growth factor determined by heteronuclear NMR spectroscopy and refined by energy minimization with restraints. Biochemistry 32: 7334-7353, 1993.
    • (1993) Biochemistry , vol.32 , pp. 7334-7353
    • Moy, F.J.1    Li, Y.-C.2    Rauenbuehler, P.3    Winkler, M.E.4    Scheraga, H.A.5    Montelione, G.T.6
  • 138
    • 0028330220 scopus 로고
    • Principles determining the structure of α-sheet barrels in proteins. II. The observed structures
    • Murzin, A. G., Lesk, A. M. & Chothia, C.: Principles determining the structure of α-sheet barrels in proteins. II. The observed structures. J. Mol. Biol. 236: 1382-1400, 1994.
    • (1994) J. Mol. Biol. , vol.236 , pp. 1382-1400
    • Murzin, A.G.1    Lesk, A.M.2    Chothia, C.3
  • 140
    • 70449242194 scopus 로고
    • Inhibition de 1'infection vaccinale par un facteur liquide dans le tissu infecté par le virus homologue
    • Nagano, Y. & Kojima, Y.: Inhibition de 1'infection vaccinale par un facteur liquide dans le tissu infecté par le virus homologue. C. R. Soc. Biol. 152: 1627-1629, 1958.
    • (1958) C. R. Soc. Biol. , vol.152 , pp. 1627-1629
    • Nagano, Y.1    Kojima, Y.2
  • 141
    • 84960987965 scopus 로고
    • Pouvoir immunisant du virus vaccinal inactivé par des rayons ultraviolets
    • Nagano, Y. & Kojima, Y.: Pouvoir immunisant du virus vaccinal inactivé par des rayons ultraviolets. C. R. Soc. Biol. 148: 1700-1702, 1954.
    • (1954) C. R. Soc. Biol. , vol.148 , pp. 1700-1702
    • Nagano, Y.1    Kojima, Y.2
  • 142
    • 0027751556 scopus 로고
    • Interleukin-2 receptor γ chain: A functional component of the interleukin-7 receptor
    • Noguchi, M., Nakamura, Y., Russell, S. M., Ziegler, S. F., Tsang, M., Cao, X. & Leonard, W. J.: Interleukin-2 receptor γ chain: a functional component of the interleukin-7 receptor. Science 262: 1877-1880, 1993.
    • (1993) Science , vol.262 , pp. 1877-1880
    • Noguchi, M.1    Nakamura, Y.2    Russell, S.M.3    Ziegler, S.F.4    Tsang, M.5    Cao, X.6    Leonard, W.J.7
  • 143
    • 0028299340 scopus 로고
    • The human interferon-α/β receptor: Characterization and molecular cloning
    • Novick, D., Cohen, B. & Rubinstein, M.: The human interferon-α/β receptor: characterization and molecular cloning. Cell 77: 391-400, 1994.
    • (1994) Cell , vol.77 , pp. 391-400
    • Novick, D.1    Cohen, B.2    Rubinstein, M.3
  • 144
    • 0028917463 scopus 로고
    • Receptor for interleukin 13. Interaction with interleukin 4 by a mechanism that does not involve the common γ chain shared by recpetors for interleukins 2, 4, 7, 9, and 15
    • Obiri, N. I., Debinski, W., Leonard, W. J. & Pari, R. K.: Receptor for interleukin 13. Interaction with interleukin 4 by a mechanism that does not involve the common γ chain shared by recpetors for interleukins 2, 4, 7, 9, and 15. J. Biol. Chem. 270: 8797-8804, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 8797-8804
    • Obiri, N.I.1    Debinski, W.2    Leonard, W.J.3    Pari, R.K.4
  • 145
    • 0026744790 scopus 로고
    • Crystal structure of human platelet-derived growth factor BB
    • Oefner, C., D'Arcy, A., Winkler, F. K., Eggimann, B. & Hosang, M.: Crystal structure of human platelet-derived growth factor BB. EMBO J. 11: 3921-3926, 1992.
    • (1992) EMBO J. , vol.11 , pp. 3921-3926
    • Oefner, C.1    D'Arcy, A.2    Winkler, F.K.3    Eggimann, B.4    Hosang, M.5
  • 146
    • 0027134979 scopus 로고
    • Model structures and action of interleukin 1 and its antagonist
    • Oldfield, T. J., Murray-Rust, P. & Hubbard, R. E.: Model structures and action of interleukin 1 and its antagonist. Protein Eng. 6: 865-871, 1993.
    • (1993) Protein Eng. , vol.6 , pp. 865-871
    • Oldfield, T.J.1    Murray-Rust, P.2    Hubbard, R.E.3
  • 147
    • 0027954759 scopus 로고
    • Structure activity studies of human tumour necrosis factors
    • Ostade, X. F., Tavernier, J. & Fiers, W.: Structure activity studies of human tumour necrosis factors. Protein Eng. 7: 5-22, 1994.
    • (1994) Protein Eng. , vol.7 , pp. 5-22
    • Ostade, X.F.1    Tavernier, J.2    Fiers, W.3
  • 148
    • 0026058148 scopus 로고
    • Localization of the active site of human tumour necrosis factor (hTNF) by mutational analysis
    • Ostade, X. V., Tavernier, J., Prange, T. & Fiers, W.: Localization of the active site of human tumour necrosis factor (hTNF) by mutational analysis. EMBO J. 10: 827-836, 1991.
    • (1991) EMBO J. , vol.10 , pp. 827-836
    • Ostade, X.V.1    Tavernier, J.2    Prange, T.3    Fiers, W.4
  • 149
    • 0027293729 scopus 로고
    • Inter-species chimeras of leukaemia inhibitory factor define a major human receptor-binding determinant
    • Owczarek, C. M., Layton, M. J., Metcalf, D., Lock, P., Willson, T. A., Gough, N. M. & Nicola, N. A.: Inter-species chimeras of leukaemia inhibitory factor define a major human receptor-binding determinant. EMBO J. 12: 3487-3495, 1993.
    • (1993) EMBO J. , vol.12 , pp. 3487-3495
    • Owczarek, C.M.1    Layton, M.J.2    Metcalf, D.3    Lock, P.4    Willson, T.A.5    Gough, N.M.6    Nicola, N.A.7
  • 151
    • 0026727235 scopus 로고
    • Three-dimensional structure of dimeric human recombinant macrophage colony-stimulating factor
    • Pandit, J., Bohm, A., Jancarik, J., Halenbeck, R., Koths, K. & Kim, S.-H.: Three-dimensional structure of dimeric human recombinant macrophage colony-stimulating factor. Science 258: 1358-1362, 1992.
    • (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
  • 152
    • 0026764439 scopus 로고
    • Three-dimensional solution structure of human interleukin-4 by multidimensional heteronuclear magnetic resonance spectroscopy
    • Powers, R., Garret, D. S., March, C. J., Frieden, E. A., Gronenborn, A. M. & Clore, G. M.: Three-dimensional solution structure of human interleukin-4 by multidimensional heteronuclear magnetic resonance spectroscopy. Science 256: 1673-1677, 1992.
    • (1992) Science , vol.256 , pp. 1673-1677
    • Powers, R.1    Garret, D.S.2    March, C.J.3    Frieden, E.A.4    Gronenborn, A.M.5    Clore, G.M.6
  • 153
    • 0027236528 scopus 로고
    • The high-resolution, three-dimensional solution structure of human interleukin-4 determined by multidimensional heteronuclear magnetic resonance spectroscopy
    • Powers, R., Garret, D. S., March, C. J., Frieden, E. A., Gronenborn, A. M. & Clore, G. M.: The high-resolution, three-dimensional solution structure of human interleukin-4 determined by multidimensional heteronuclear magnetic resonance spectroscopy. Biochemistry 32: 6744-6762, 1993.
    • (1993) Biochemistry , vol.32 , pp. 6744-6762
    • Powers, R.1    Garret, D.S.2    March, C.J.3    Frieden, E.A.4    Gronenborn, A.M.5    Clore, G.M.6
  • 154
    • 0023957427 scopus 로고
    • Crystal structure of the cytokine interleukin-1β
    • Priestle, J. P., Schär, H.-P. & Crütter, M. G.: Crystal structure of the cytokine interleukin-1β. EMBO J. 7: 339-343, 1988.
    • (1988) EMBO J. , vol.7 , pp. 339-343
    • Priestle, J.P.1    Schär, H.-P.2    Crütter, M.G.3
  • 155
    • 0024804106 scopus 로고
    • Crystallographic refinement of interleukin-1β at 2.0Å resolution
    • Priestle, J. P., Schär, H.-P. & Grütter, M. G.: Crystallographic refinement of interleukin-1β at 2.0Å resolution. Proc. Natl. Acad. Sci. USA 86: 9667-9671, 1989.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 9667-9671
    • Priestle, J.P.1    Schär, H.-P.2    Grütter, M.G.3
  • 158
    • 0026051784 scopus 로고
    • Oncostatin M is a member of a cytokine family that includes leukemia-inhibitory factor, granulocyte colony-stimulating factor, and interleukin 6
    • Rose, T. M. & Bruce, A. G.: Oncostatin M is a member of a cytokine family that includes leukemia-inhibitory factor, granulocyte colony-stimulating factor, and interleukin 6. Proc. Natl. Acad. Sci. USA 88: 8641-8645, 1991.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 8641-8645
    • Rose, T.M.1    Bruce, A.G.2
  • 161
    • 0025786186 scopus 로고
    • Crystal structure of recombinant rabbit interferon-γ at 2.7Å resolution
    • Samudzi, C. T., Burton, L. E. & Rubin, I. R.: Crystal structure of recombinant rabbit interferon-γ at 2.7Å resolution. J. Biol. Chem. 15. 21791-21797, 1991.
    • (1991) J. Biol. Chem. , vol.15 , pp. 21791-21797
    • Samudzi, C.T.1    Burton, L.E.2    Rubin, I.R.3
  • 162
    • 0028348567 scopus 로고
    • Multimeric cytokine receptors: Common versus specific functions
    • Sato, N. & Miyajima, A.: Multimeric cytokine receptors: common versus specific functions. Curr. Opin. Cell Biol. 6: 174-179, 1994.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 174-179
    • Sato, N.1    Miyajima, A.2
  • 163
    • 0028202123 scopus 로고
    • Generation of interleukin-6 receptor antagonists by molecularmodeling guided mutagenesis of residues important for gp130 activation
    • Savino, R., Lahm, A., Salvati, A. L., Ciapponi, L., Sporeno, E., Altamura, S., Paonessa, G., Toniatti, C. & Ciliberto, G.: Generation of interleukin-6 receptor antagonists by molecularmodeling guided mutagenesis of residues important for gp130 activation. EMBO J. 13: 1357-1367, 1994.
    • (1994) EMBO J. , vol.13 , pp. 1357-1367
    • Savino, R.1    Lahm, A.2    Salvati, A.L.3    Ciapponi, L.4    Sporeno, E.5    Altamura, S.6    Paonessa, G.7    Toniatti, C.8    Ciliberto, G.9
  • 165
    • 0026633842 scopus 로고
    • An unusual feature revealed by the crystal structure at 2.2Å resolution of human transforming growth factor-β2
    • Schlunegger, M. P. & Grütter, M. G.: An unusual feature revealed by the crystal structure at 2.2Å resolution of human transforming growth factor-β2. Nature 358: 430-434, 1992.
    • (1992) Nature , vol.358 , pp. 430-434
    • Schlunegger, M.P.1    Grütter, M.G.2
  • 166
    • 0027253228 scopus 로고
    • Refined crystal structure of human transforming growth factor β2 at 1.95Å resolution
    • Schlunegger, M. P. & Grüitter, M. G.: Refined crystal structure of human transforming growth factor β2 at 1.95Å resolution. J. Mol. Biol. 231: 445-458, 1993.
    • (1993) J. Mol. Biol. , vol.231 , pp. 445-458
    • Schlunegger, M.P.1    Grüitter, M.G.2
  • 171
    • 0028999259 scopus 로고
    • Proton NMR assignments and solution conformation of RANTES, a chemokine of the C-C type
    • Skelton, N. J., Aspiras, F., Ogez, J. & Schall, T. J.: Proton NMR assignments and solution conformation of RANTES, a chemokine of the C-C type. Biochemistry 34: 5329-5342. 1995.
    • (1995) Biochemistry , vol.34 , pp. 5329-5342
    • Skelton, N.J.1    Aspiras, F.2    Ogez, J.3    Schall, T.J.4
  • 173
    • 0028353492 scopus 로고
    • The TNF receptor superfamily of cellular and viral proteins: Activation, costimulation, and death
    • Smith, C. A., Farrah, T. & Goodwin, R. G.: The TNF receptor superfamily of cellular and viral proteins: activation, costimulation, and death. Cell 76: 959-962, 1994.
    • (1994) Cell , vol.76 , pp. 959-962
    • Smith, C.A.1    Farrah, T.2    Goodwin, R.G.3
  • 176
    • 0027145507 scopus 로고
    • Cytokine structural taxonomy and mechanisms of receptor engagement
    • Sprang, S. R. & Bazan, J. F.: Cytokine structural taxonomy and mechanisms of receptor engagement. Curr. Opin. Struct. Biol. 3: 815-827, 1993.
    • (1993) Curr. Opin. Struct. Biol. , vol.3 , pp. 815-827
    • Sprang, S.R.1    Bazan, J.F.2
  • 177
    • 0026691065 scopus 로고
    • Secondary structure and topology of interleukin-1 receptor antagonist protein determined by heteronuclear threedimensional NMR spectroscopy
    • Stockman, B. J., Scahill, T. A., Roy, M., Ulrich, E. L., Strakalaitis, N. A., Brunner, D. P., Yem, A. W. & Deibel, M. R.: Secondary structure and topology of interleukin-1 receptor antagonist protein determined by heteronuclear threedimensional NMR spectroscopy. Biochemistry 31: 5237-5245, 1992.
    • (1992) Biochemistry , vol.31 , pp. 5237-5245
    • Stockman, B.J.1    Scahill, T.A.2    Roy, M.3    Ulrich, E.L.4    Strakalaitis, N.A.5    Brunner, D.P.6    Yem, A.W.7    Deibel, M.R.8
  • 178
    • 0028232724 scopus 로고
    • Limb alterations in brachypodism mice due to mutations in a new member of the TGF β-superfamily
    • Storm, E. E., Huynh, T. V., Copeland, N. G., Jenkins, N. A., Kingsley, D. M. & Lee, S.-J.: Limb alterations in brachypodism mice due to mutations in a new member of the TGF β-superfamily. Nature 368: 639-643, 1994.
    • (1994) Nature , vol.368 , pp. 639-643
    • Storm, E.E.1    Huynh, T.V.2    Copeland, N.G.3    Jenkins, N.A.4    Kingsley, D.M.5    Lee, S.-J.6
  • 179
    • 0026661146 scopus 로고
    • A model of the platelet factor 4 complex with heparin
    • Stuckey, J. A., Charles, R. St. & Edwards, B. F. P.: A model of the platelet factor 4 complex with heparin. Proteins 14: 277-287, 1992.
    • (1992) Proteins , vol.14 , pp. 277-287
    • Stuckey, J.A.1    Charles, R.St.2    Edwards, B.F.P.3
  • 180
    • 0028176586 scopus 로고
    • A mouse TGF-β type I receptor that requires type II receptor for ligand binding
    • Susuki, A., Shioda, N., Maeda, T., Tada, M. & Ueno, N.: A mouse TGF-β type I receptor that requires type II receptor for ligand binding. Biochem. Biophys. Res. Commun. 198: 1063-1069, 1994.
    • (1994) Biochem. Biophys. Res. Commun. , vol.198 , pp. 1063-1069
    • Susuki, A.1    Shioda, N.2    Maeda, T.3    Tada, M.4    Ueno, N.5
  • 181
    • 0027458109 scopus 로고
    • A study of structural determinants in the interleukin-I fold
    • Swindells, M. B. & Thornton, J. M.: A study of structural determinants in the interleukin-I fold. Protein Eng. 6: 711-715, 1993.
    • (1993) Protein Eng. , vol.6 , pp. 711-715
    • Swindells, M.B.1    Thornton, J.M.2
  • 182
    • 0026492546 scopus 로고
    • Structural similarity between TGF-β2 and nerve growth factor
    • Swindells, M. B., Daopin, S., Cohen, G. H. & Davies, D.: Structural similarity between TGF-β2 and nerve growth factor. Science 258: 1160-1162, 1992.
    • (1992) Science , vol.258 , pp. 1160-1162
    • Swindells, M.B.1    Daopin, S.2    Cohen, G.H.3    Davies, D.4
  • 183
    • 0026376817 scopus 로고
    • Role of a two-chain 1L-6 receptor system in immune and hematopoietic cell regulation
    • Taga, T. & Kishimoto, T.: Role of a two-chain 1L-6 receptor system in immune and hematopoietic cell regulation. Crit. Rev. Immunol. 11: 265-280, 1992.
    • (1992) Crit. Rev. Immunol. , vol.11 , pp. 265-280
    • Taga, T.1    Kishimoto, T.2
  • 184
    • 0025818263 scopus 로고
    • Identification of the second subunit of the murine interleukin-5 receptor: Interleukin-3 receptor-like protein, AIC2B is a component of the high affinity interleukin-5 receptor
    • Takaki, S., Mita, S., Kitamura, T., Yonehara, S., Yamaguchi, N., Tominaga, A., Miyajima, A. & Takatsu, K.: Identification of the second subunit of the murine interleukin-5 receptor: interleukin-3 receptor-like protein, AIC2B is a component of the high affinity interleukin-5 receptor. EMBO J. 10: 2833-2838, 1991.
    • (1991) EMBO J. , vol.10 , pp. 2833-2838
    • Takaki, S.1    Mita, S.2    Kitamura, T.3    Yonehara, S.4    Yamaguchi, N.5    Tominaga, A.6    Miyajima, A.7    Takatsu, K.8
  • 187
    • 0018955427 scopus 로고
    • The nucleotide sequence of human fibroblast interferon cDNA
    • Taniguchi, T., Ohno, S., Fujii-Kuriyama, Y. & Muramatsu, M.: The nucleotide sequence of human fibroblast interferon cDNA. Gene 10: 11-15, 1980.
    • (1980) Gene , vol.10 , pp. 11-15
    • Taniguchi, T.1    Ohno, S.2    Fujii-Kuriyama, Y.3    Muramatsu, M.4
  • 188
    • 0028218987 scopus 로고
    • Energetic characterization of the basic fibroblast growth factor-heparin interaction: Identification of the heparin binding domain
    • Thompson, L. D., Pantoliano, M. W. & Springer, B. A.: Energetic characterization of the basic fibroblast growth factor-heparin interaction: identification of the heparin binding domain. Biochemistry 33: 3831-3840, 1994.
    • (1994) Biochemistry , vol.33 , pp. 3831-3840
    • Thompson, L.D.1    Pantoliano, M.W.2    Springer, B.A.3
  • 190
    • 2442745249 scopus 로고
    • Localization of epitopes for binding of the monoclonal antibodies LI-1 and LI-8 leukocyte interferons
    • Kirchner, H. & Schellekens, H. (Eds.): Elsevier, Amsterdam
    • Trown, P. W., Heimer, E. P., Felix, A. M. & Bohoslawec, O.: Localization of epitopes for binding of the monoclonal antibodies LI-1 and LI-8 leukocyte interferons. In: Kirchner, H. & Schellekens, H. (Eds.): The Biology of the Interferon System. Elsevier, Amsterdam 1984, pp. 69-76.
    • (1984) The Biology of the Interferon System , pp. 69-76
    • Trown, P.W.1    Heimer, E.P.2    Felix, A.M.3    Bohoslawec, O.4
  • 191
    • 0029146996 scopus 로고
    • Interleukin-3-associated expression of gangliosides in mouse myelogenous leukemia NFS60 cells introduced with interleukin-3 gene: Expression of ganglioside GD1a and key involvement of CMP-NeuAc: lactosylceramide α2→3-sialyltransferase in GD1a expression
    • Tsunoda, A., Nakamura, M., Kirito, K., Hara, K. & Saito, M.: Interleukin-3-associated expression of gangliosides in mouse myelogenous leukemia NFS60 cells introduced with interleukin-3 gene: expression of ganglioside GD1a and key involvement of CMP-NeuAc: lactosylceramide α2→3-sialyltransferase in GD1a expression. Biochemistry 34: 9356-9367, 1995.
    • (1995) Biochemistry , vol.34 , pp. 9356-9367
    • Tsunoda, A.1    Nakamura, M.2    Kirito, K.3    Hara, K.4    Saito, M.5
  • 192
    • 0028217202 scopus 로고
    • The crystal structure of affinitymatured human growth hormone at 2Å resolution
    • Ultsch, M. H., Somers, W., Kossiakoff, A. A. & de Vos, A. M.: The crystal structure of affinitymatured human growth hormone at 2Å resolution. J. Mol. Biol. 236: 286-299, 1994.
    • (1994) J. Mol. Biol. , vol.236 , pp. 286-299
    • Ultsch, M.H.1    Somers, W.2    Kossiakoff, A.A.3    De Vos, A.M.4
  • 193
    • 0028944489 scopus 로고
    • α and ß interferons and their receptor and their friends and relations
    • Uze, G., Lutfalla, G. & Mogensen, K. E.: α and ß interferons and their receptor and their friends and relations. J. Interferon Cytokine Res. 15: 3-26, 1995.
    • (1995) J. Interferon Cytokine Res. , vol.15 , pp. 3-26
    • Uze, G.1    Lutfalla, G.2    Mogensen, K.E.3
  • 196
    • 0026598960 scopus 로고
    • Human growth hormone and extracellular domain of its receptor: Crystal structure of the complex
    • Vos, A. M., Ultsch, M. & Kossiakoff, A. A.: Human growth hormone and extracellular domain of its receptor: crystal structure of the complex. Science 255: 306-312, 1992.
    • (1992) Science , vol.255 , pp. 306-312
    • Vos, A.M.1    Ultsch, M.2    Kossiakoff, A.A.3
  • 197
    • 0027441948 scopus 로고
    • Cloning of cDNA for the a subunit of mouse insulin-like growth factor I receptor and the role of the receptor in metanephric development
    • Wada, J., Liu, Z. Z., Alvares, K., Kumar, A., Wallner, E., Makino, H. & Kanwar, Y. S.: Cloning of cDNA for the a subunit of mouse insulin-like growth factor I receptor and the role of the receptor in metanephric development. Proc. Natl. Acad. Sci. USA 90: 10360-10364, 1993.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10360-10364
    • Wada, J.1    Liu, Z.Z.2    Alvares, K.3    Kumar, A.4    Wallner, E.5    Makino, H.6    Kanwar, Y.S.7
  • 203
    • 0027264747 scopus 로고
    • Hematopoietic cytokines: Similarities and differences in the structures, with implications for receptor binding
    • Wlodawer, A., Pavlovsky, A. & Gustchina, A.: Hematopoietic cytokines: similarities and differences in the structures, with implications for receptor binding. Protein Sci. 2: 1373-1382, 1993.
    • (1993) Protein Sci. , vol.2 , pp. 1373-1382
    • Wlodawer, A.1    Pavlovsky, A.2    Gustchina, A.3
  • 204
    • 0028218186 scopus 로고
    • The drosophila saxophone gene: A serine-threonine kinase receptor of the TGF-β superfamily
    • Xie, T., Finelli, A. L. & Padgett, R. W.: The drosophila saxophone gene: a serine-threonine kinase receptor of the TGF-β superfamily. Science 263: 1756-1759, 1994.
    • (1994) Science , vol.263 , pp. 1756-1759
    • Xie, T.1    Finelli, A.L.2    Padgett, R.W.3
  • 206
    • 0029670220 scopus 로고    scopus 로고
    • Phosphorylated interferon-α receptor 1 subunit (IFNaR1) acts as a docking site for the latent form of the 113 kDa STAT2 protein
    • Yan, H., Krishnan, K., Greenlund, A. C., Gupta, S., Lim, J. T. E., Schreiber, R. D., Schindler, C. W. & Krolewski, J. J.: Phosphorylated interferon-α receptor 1 subunit (IFNaR1) acts as a docking site for the latent form of the 113 kDa STAT2 protein. EMBO J. 15: 1064-1074, 1996.
    • (1996) EMBO J. , vol.15 , pp. 1064-1074
    • Yan, H.1    Krishnan, K.2    Greenlund, A.C.3    Gupta, S.4    Lim, J.T.E.5    Schreiber, R.D.6    Schindler, C.W.7    Krolewski, J.J.8
  • 208
    • 0021396644 scopus 로고
    • Evolutionary, conformational and functional relationships of α-, β- and γ-interferons
    • Moscow
    • Zav'yalov, V. P. & Denesyuk, A. I.: Evolutionary, conformational and functional relationships of α-, β- and γ-interferons. Doklady Akademii Nauk SSSR (Moscow) 275: 242-246. 1984.
    • (1984) Doklady Akademii Nauk SSSR , vol.275 , pp. 242-246
    • Zav'yalov, V.P.1    Denesyuk, A.I.2
  • 209
    • 0020059419 scopus 로고
    • Possible conformation of interferons: A prediction based on amino acid composition and sequence
    • Zav'yalov, V. P. & Denesyuk, A. I.: Possible conformation of interferons: a prediction based on amino acid composition and sequence. Immunol. Lett. 4: 7-14, 1982.
    • (1982) Immunol. Lett. , vol.4 , pp. 7-14
    • Zav'yalov, V.P.1    Denesyuk, A.I.2
  • 210
    • 0024451036 scopus 로고
    • Theoretical analysis of conformation and active sites of interferons
    • Zav'yalov, V. P., Denesyuk, A. I. & Zav'yalova, G. A.: Theoretical analysis of conformation and active sites of interferons. Immunol. Lett. 22: 173-182, 1989.
    • (1989) Immunol. Lett. , vol.22 , pp. 173-182
    • Zav'yalov, V.P.1    Denesyuk, A.I.2    Zav'yalova, G.A.3
  • 211
    • 0021830114 scopus 로고
    • sis of simian sarcoma virus are similar to those of interferons
    • sis of simian sarcoma virus are similar to those of interferons. Immunol. Lett. 10. 71-79, 1985.
    • (1985) Immunol. Lett. , vol.10 , pp. 71-79
    • Zav'yalov, V.P.1    Denesyuk, A.I.2
  • 212
    • 0025054296 scopus 로고
    • Theoretical conformational analysis of a family of α-helical immunocytokines
    • Zav'yalov, V. P., Denesyuk, A. I. & Zav'yalova, G. A.: Theoretical conformational analysis of a family of α-helical immunocytokines. Biochim. Biophys. Acta 1041: 178-185, 1990.
    • (1990) Biochim. Biophys. Acta , vol.1041 , pp. 178-185
    • Zav'yalov, V.P.1    Denesyuk, A.I.2    Zav'yalova, G.A.3
  • 213
    • 0026097187 scopus 로고
    • The octapeptide corresponding to the region of the highest homology between α-interferon and thymosin-α1 effectively competes with both cytokines for common high-affinity receptors on murine thymocytes
    • Zav'yalov, V. P., Navolotskaya, E. V., Abramov, V. M., Galaktionov, V. G., Isaev, I. S., Kaurov, O. A., Kozhich, A. T., Maiorov, V. A., Prusakov, A. N., Vasilenko, R. N. & Volodina, E. Y.: The octapeptide corresponding to the region of the highest homology between α-interferon and thymosin-α1 effectively competes with both cytokines for common high-affinity receptors on murine thymocytes. FEBS Lett. 278: 187-189, 1991.
    • (1991) FEBS Lett. , vol.278 , pp. 187-189
    • Zav'yalov, V.P.1    Navolotskaya, E.V.2    Abramov, V.M.3    Galaktionov, V.G.4    Isaev, I.S.5    Kaurov, O.A.6    Kozhich, A.T.7    Maiorov, V.A.8    Prusakov, A.N.9    Vasilenko, R.N.10    Volodina, E.Y.11
  • 214
    • 0029010829 scopus 로고
    • The sequence 130-137 of human interferon-α2 is involved in the competition of interferon, prothymosin α and cholera toxin B subunit for common receptors on human fibroblasts
    • Zav'yalov, V. P., Navolotskaya, E. K, Vasilenko, R. N., Abramov, V. M., Volodina, E. Y., Roslovtseva, O. A., Prusakov, A. N. & Kaurov, O. A.: The sequence 130-137 of human interferon-α2 is involved in the competition of interferon, prothymosin α and cholera toxin B subunit for common receptors on human fibroblasts. Mol. Immunol. 32: 425-431, 1995.
    • (1995) Mol. Immunol. , vol.32 , pp. 425-431
    • Zav'yalov, V.P.1    Navolotskaya, E.K.2    Vasilenko, R.N.3    Abramov, V.M.4    Volodina, E.Y.5    Roslovtseva, O.A.6    Prusakov, A.N.7    Kaurov, O.A.8
  • 215
    • 0026323941 scopus 로고
    • Three-dimensional structure of human basic fibroblast growth factor, a structural homolog of interleukin-1β
    • Zhang, J., Cousens, L. S., Barr, P. J. & Sprang, S. R.: Three-dimensional structure of human basic fibroblast growth factor, a structural homolog of interleukin-1β. Proc. Natl. Acad. Sci. USA 88: 3446-3450, 1991.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3446-3450
    • Zhang, J.1    Cousens, L.S.2    Barr, P.J.3    Sprang, S.R.4
  • 218
    • 0028176655 scopus 로고
    • Interleukin-13. an interleukin-4 cytokine that acts on monocytes and B cells but not on T cells
    • Zurawski, G. & de Vries, J. E.: Interleukin-13. an interleukin-4 cytokine that acts on monocytes and B cells but not on T cells. Immunol. Today 15: 19-26, 1994.
    • (1994) Immunol. Today , vol.15 , pp. 19-26
    • Zurawski, G.1    De Vries, J.E.2
  • 219
    • 0027373282 scopus 로고
    • Definition and spatial location of mouse interleukin-2 residues that interact with its heterotrimeric receptor
    • Zurawski, S. M., Vega, F., Double, E. L., Huyghe, B., Flaherty, K., Mckay, D. B. & Zurawski, G.: Definition and spatial location of mouse interleukin-2 residues that interact with its heterotrimeric receptor. EMBO J. 12: 5113-5119, 1993.
    • (1993) EMBO J. , vol.12 , pp. 5113-5119
    • Zurawski, S.M.1    Vega, F.2    Double, E.L.3    Huyghe, B.4    Flaherty, K.5    Mckay, D.B.6    Zurawski, G.7
  • 220
    • 0027274890 scopus 로고
    • Receptors for interleukin 13 and interleukin-4 are complex and share a novel component that functions in signal transduction
    • Zurawski, S. M., Vega, F. Jr., Huyghe, B. & Zurawski, G.: Receptors for interleukin 13 and interleukin-4 are complex and share a novel component that functions in signal transduction. EMBO J. 12: 2663-2670, 1993.
    • (1993) EMBO J. , vol.12 , pp. 2663-2670
    • Zurawski, S.M.1    Vega Jr., F.2    Huyghe, B.3    Zurawski, G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.