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Volumn 15, Issue 1, 2004, Pages 33-48

The Class II cytokine receptor (CRF2) family: Overview and patterns of receptor-ligand interactions

Author keywords

Cytokine receptors; Cytokines; Interferons

Indexed keywords

CYTOKINE; CYTOKINE RECEPTOR; INTERFERON; INTERFERON RECEPTOR; INTERLEUKIN 10; INTERLEUKIN 10 RECEPTOR; INTERLEUKIN 19; INTERLEUKIN 20; INTERLEUKIN 22; INTERLEUKIN 24; RECEPTOR SUBTYPE; THROMBOPLASTIN;

EID: 1642432084     PISSN: 13596101     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cytogfr.2003.10.001     Document Type: Review
Times cited : (172)

References (102)
  • 1
    • 0025102756 scopus 로고
    • Haematopoietic receptors and helical cytokines
    • Bazan J.F. Haematopoietic receptors and helical cytokines. Immunol. Today. 11:1990;350-354.
    • (1990) Immunol. Today , vol.11 , pp. 350-354
    • Bazan, J.F.1
  • 2
    • 0025755810 scopus 로고
    • Structural symmetry of the extracellular domain of the cytokine/growth hormone/prolactin receptor family and interferon receptors revealed by hydrophobic cluster analysis
    • Thoreau E., Petridou B., Kelly P.A., Mornon J.P. Structural symmetry of the extracellular domain of the cytokine/growth hormone/prolactin receptor family and interferon receptors revealed by hydrophobic cluster analysis. FEBS Lett. 282:1991;26-31.
    • (1991) FEBS Lett. , vol.282 , pp. 26-31
    • Thoreau, E.1    Petridou, B.2    Kelly, P.A.3    Mornon, J.P.4
  • 3
    • 0031771256 scopus 로고    scopus 로고
    • The evolution of the Type I interferons
    • [published erratum appears in J Interferon Cytokine Res 1999 April;19(4):427]
    • Roberts R.M., Liu L., Guo Q., Leaman D., Bixby J. The evolution of the Type I interferons. J. Interferon Cytokine Res. 18:1998;805-816. [published erratum appears in J Interferon Cytokine Res 1999 April;19(4):427].
    • (1998) J. Interferon Cytokine Res. , vol.18 , pp. 805-816
    • Roberts, R.M.1    Liu, L.2    Guo, Q.3    Leaman, D.4    Bixby, J.5
  • 4
    • 0035955680 scopus 로고    scopus 로고
    • Interferon-kappa, a novel Type I interferon expressed in human keratinocytes
    • LaFleur D.W., Nardelli B., Tsareva T., Mather D., Feng P., Semenuk M.et al. Interferon-kappa, a novel Type I interferon expressed in human keratinocytes. J. Biol. Chem. 276:2001;39765-39771.
    • (2001) J. Biol. Chem. , vol.276 , pp. 39765-39771
    • Lafleur, D.W.1    Nardelli, B.2    Tsareva, T.3    Mather, D.4    Feng, P.5    Semenuk, M.6
  • 6
    • 0034089107 scopus 로고    scopus 로고
    • An interferon-like cytokine that preferentially influences B-lymphocyte precursors
    • Oritani K., Medina K.L., Tomiyama Y., Ishikawa J., Okajima Y., Ogawa M. et al. An interferon-like cytokine that preferentially influences B-lymphocyte precursors. Nat. Med. 6:2000;659-666.
    • (2000) Nat. Med. , vol.6 , pp. 659-666
    • Oritani, K.1    Medina, K.L.2    Tomiyama, Y.3    Ishikawa, J.4    Okajima, Y.5    Ogawa, M.6
  • 7
    • 0035885138 scopus 로고    scopus 로고
    • A new IFN-like cytokine, limitin, modulates the immune response without influencing thymocyte development
    • Takahashi I., Kosaka H., Oritani K., Heath W.R., Ishikawa J., Okajima Y.et al. A new IFN-like cytokine, limitin, modulates the immune response without influencing thymocyte development. J. Immunol. 167:2001;3156-3163.
    • (2001) J. Immunol. , vol.167 , pp. 3156-3163
    • Takahashi, I.1    Kosaka, H.2    Oritani, K.3    Heath, W.R.4    Ishikawa, J.5    Okajima, Y.6
  • 8
    • 0035031325 scopus 로고    scopus 로고
    • Limitin: An interferon-like cytokine without myeloerythroid suppressive properties
    • Oritani K., Kincade P.W., Tomiyama Y. Limitin: an interferon-like cytokine without myeloerythroid suppressive properties. J. Mol. Med. 79:2001;168-174.
    • (2001) J. Mol. Med. , vol.79 , pp. 168-174
    • Oritani, K.1    Kincade, P.W.2    Tomiyama, Y.3
  • 9
    • 0037221405 scopus 로고    scopus 로고
    • T lymphocytes constitutively produce an interferonlike cytokine limitin characterized as a heat- and acid-stable and heparin-binding glycoprotein
    • Oritani K., Hirota S., Nakagawa T., Takahashi I., Kawamoto S., Yamada M.et al. T lymphocytes constitutively produce an interferonlike cytokine limitin characterized as a heat- and acid-stable and heparin-binding glycoprotein. Blood. 101:2003;178-185.
    • (2003) Blood , vol.101 , pp. 178-185
    • Oritani, K.1    Hirota, S.2    Nakagawa, T.3    Takahashi, I.4    Kawamoto, S.5    Yamada, M.6
  • 10
    • 0034954034 scopus 로고    scopus 로고
    • Interferons alpha and beta as immune regulators - A new look
    • Biron C.A. Interferons alpha and beta as immune regulators - a new look. Immunity. 14:2001;661-664.
    • (2001) Immunity , vol.14 , pp. 661-664
    • Biron, C.A.1
  • 11
    • 0030889207 scopus 로고    scopus 로고
    • The IFN gamma receptor: A paradigm for cytokine receptor signaling
    • Bach E.A., Aguet M., Schreiber R.D. The IFN gamma receptor: a paradigm for cytokine receptor signaling. Annu. Rev. Immunol. 15:1997;563-591.
    • (1997) Annu. Rev. Immunol. , vol.15 , pp. 563-591
    • Bach, E.A.1    Aguet, M.2    Schreiber, R.D.3
  • 12
    • 0030994132 scopus 로고    scopus 로고
    • The interferon receptors
    • Pestka S. The interferon receptors. Semin. Oncol. 24:1997;S9-18-S9-40.
    • (1997) Semin. Oncol. , vol.24
    • Pestka, S.1
  • 13
    • 0036005884 scopus 로고    scopus 로고
    • The roles of IFN gamma in protection against tumor development and cancer immunoediting
    • Ikeda H., Old L.J., Schreiber R.D. The roles of IFN gamma in protection against tumor development and cancer immunoediting. Cytokine Growth Factor Rev. 13:2002;95-109.
    • (2002) Cytokine Growth Factor Rev. , vol.13 , pp. 95-109
    • Ikeda, H.1    Old, L.J.2    Schreiber, R.D.3
  • 15
    • 0036091086 scopus 로고    scopus 로고
    • Viral and cellular interleukin-10 (IL-10)-related cytokines: From structures to functions
    • Dumoutier L., Renauld J.C. Viral and cellular interleukin-10 (IL-10)-related cytokines: from structures to functions. Eur. Cytokine Netw. 13:2002;5-15.
    • (2002) Eur. Cytokine Netw. , vol.13 , pp. 5-15
    • Dumoutier, L.1    Renauld, J.C.2
  • 17
    • 0035992506 scopus 로고    scopus 로고
    • The family of IL-10-related cytokines and their receptors: Related, but to what extent?
    • Kotenko S.V. The family of IL-10-related cytokines and their receptors: related, but to what extent? Cytokine Growth Factor Rev. 13:2002;223-240.
    • (2002) Cytokine Growth Factor Rev. , vol.13 , pp. 223-240
    • Kotenko, S.V.1
  • 19
    • 0037243222 scopus 로고    scopus 로고
    • IFN-lambdas mediate antiviral protection through a distinct Class II cytokine receptor complex
    • Kotenko S.V., Gallagher G., Baurin V.V., Lewis-Antes A., Shen M., Shah N.K.et al. IFN-lambdas mediate antiviral protection through a distinct Class II cytokine receptor complex. Nat. Immunol. 4:2003;69-77.
    • (2003) Nat. Immunol. , vol.4 , pp. 69-77
    • Kotenko, S.V.1    Gallagher, G.2    Baurin, V.V.3    Lewis-Antes, A.4    Shen, M.5    Shah, N.K.6
  • 20
    • 0029926396 scopus 로고    scopus 로고
    • The crystal structure of the complex of blood coagulation factor VIIa with soluble tissue factor
    • Banner D.W., D'Arcy A., Chene C., Winkler F.K., Guha A., Konigsberg W.H.et al. The crystal structure of the complex of blood coagulation factor VIIa with soluble tissue factor. Nature. 380:1996;41-46.
    • (1996) Nature , vol.380 , pp. 41-46
    • Banner, D.W.1    D'Arcy, A.2    Chene, C.3    Winkler, F.K.4    Guha, A.5    Konigsberg, W.H.6
  • 21
    • 0031739144 scopus 로고    scopus 로고
    • Structural basis for cytokine hormone-receptor recognition and receptor activation
    • Kossiakoff A.A., De Vos A.M. Structural basis for cytokine hormone-receptor recognition and receptor activation. Adv. Protein Chem. 52:1998;67-108.
    • (1998) Adv. Protein Chem. , vol.52 , pp. 67-108
    • Kossiakoff, A.A.1    De Vos, A.M.2
  • 22
    • 0036793231 scopus 로고    scopus 로고
    • Crystal structures of alpha-helical cytokine-receptor complexes: We've only scratched the surface
    • Walter M.R. Crystal structures of alpha-helical cytokine-receptor complexes: we've only scratched the surface. Biotechniques. 33:2002;S46-S57.
    • (2002) Biotechniques , vol.33
    • Walter, M.R.1
  • 23
    • 0032692405 scopus 로고    scopus 로고
    • The Type I interferon receptor: Structure, function, and evolution of a family business
    • Mogensen K.E., Lewerenz M., Reboul J., Lutfalla G., Uze G. The Type I interferon receptor: structure, function, and evolution of a family business. J. Interferon Cytokine Res. 19:1999;1069-1098.
    • (1999) J. Interferon Cytokine Res. , vol.19 , pp. 1069-1098
    • Mogensen, K.E.1    Lewerenz, M.2    Reboul, J.3    Lutfalla, G.4    Uze, G.5
  • 24
    • 0025162844 scopus 로고
    • Structural design and molecular evolution of a cytokine receptor
    • Bazan J.F. Structural design and molecular evolution of a cytokine receptor. Proc. Natl. Acad. Sci. U.S.A. 87:1990;6934-6938.
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 6934-6938
    • Bazan, J.F.1
  • 26
    • 0030799157 scopus 로고    scopus 로고
    • Identification and functional characterization of a second chain of the interleukin-10 receptor complex
    • Kotenko S.V., Krause C.D., Izotova L.S., Pollack B.P., Wu W., Pestka S. Identification and functional characterization of a second chain of the interleukin-10 receptor complex. EMBO J. 16:1997;5894-5903.
    • (1997) EMBO J. , vol.16 , pp. 5894-5903
    • Kotenko, S.V.1    Krause, C.D.2    Izotova, L.S.3    Pollack, B.P.4    Wu, W.5    Pestka, S.6
  • 27
    • 0031046189 scopus 로고    scopus 로고
    • Chimeric erythropoietin-interferon gamma receptors reveal differences in functional architecture of intracellular domains for signal transduction
    • Muthukumaran G., Kotenko S., Donnelly R., Ihle J.N., Pestka S. Chimeric erythropoietin-interferon gamma receptors reveal differences in functional architecture of intracellular domains for signal transduction. J. Biol. Chem. 272:1997;4993-4999.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4993-4999
    • Muthukumaran, G.1    Kotenko, S.2    Donnelly, R.3    Ihle, J.N.4    Pestka, S.5
  • 29
    • 0037133529 scopus 로고    scopus 로고
    • The human interferon receptor: NMR-based modeling, mapping of the IFN-alpha 2 binding site, and observed ligand-induced tightening
    • Chill J.H., Nivasch R., Levy R., Albeck S., Schreiber G., Anglister J. The human interferon receptor: NMR-based modeling, mapping of the IFN-alpha 2 binding site, and observed ligand-induced tightening. Biochemistry. 41:2002;3575-3585.
    • (2002) Biochemistry , vol.41 , pp. 3575-3585
    • Chill, J.H.1    Nivasch, R.2    Levy, R.3    Albeck, S.4    Schreiber, G.5    Anglister, J.6
  • 30
    • 0032927276 scopus 로고    scopus 로고
    • Comparative genomic analysis of the interferon/interleukin-10 receptor gene cluster
    • Reboul J., Gardiner K., Monneron D., Uze G., Lutfalla G. Comparative genomic analysis of the interferon/interleukin-10 receptor gene cluster. Genome Res. 9:1999;242-250.
    • (1999) Genome Res. , vol.9 , pp. 242-250
    • Reboul, J.1    Gardiner, K.2    Monneron, D.3    Uze, G.4    Lutfalla, G.5
  • 31
    • 0027355586 scopus 로고
    • GART, SON, IFNAR, and CRF2-4 genes cluster on human chromosome 21 and mouse chromosome 16
    • Cheng S., Lutfalla G., Uze G., Chumakov I.M., Gardiner K. GART, SON, IFNAR, and CRF2-4 genes cluster on human chromosome 21 and mouse chromosome 16. Mammalian Genome. 4:1993;338-342.
    • (1993) Mammalian Genome , vol.4 , pp. 338-342
    • Cheng, S.1    Lutfalla, G.2    Uze, G.3    Chumakov, I.M.4    Gardiner, K.5
  • 32
    • 9144250427 scopus 로고    scopus 로고
    • Comparative genomic analysis reveals independent expansion of a lineage-specific gene family in vertebrates: The Class II cytokine receptors and their ligands in mammals and fish
    • Lutfalla G., Crollius H.R., Stange-Thomann N., Jaillon O., Mogensen K., Monneron D. Comparative genomic analysis reveals independent expansion of a lineage-specific gene family in vertebrates: the Class II cytokine receptors and their ligands in mammals and fish. BMC Genomics. 4:2003;29.
    • (2003) BMC Genomics , vol.4 , pp. 29
    • Lutfalla, G.1    Crollius, H.R.2    Stange-Thomann, N.3    Jaillon, O.4    Mogensen, K.5    Monneron, D.6
  • 34
    • 0026618659 scopus 로고
    • Soluble interferon-alpha receptor molecules are present in body fluids
    • Novick D., Cohen B., Rubinstein M. Soluble interferon-alpha receptor molecules are present in body fluids. FEBS Lett. 314:1992;445-448.
    • (1992) FEBS Lett. , vol.314 , pp. 445-448
    • Novick, D.1    Cohen, B.2    Rubinstein, M.3
  • 35
    • 0028820423 scopus 로고
    • Mutant U5A 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.et al. Mutant U5A 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. 14:1995;5100-5108.
    • (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
  • 36
    • 0029044993 scopus 로고
    • Soluble and membrane-anchored forms of the human IFN-alpha/beta receptor
    • Novick D., Cohen B., Tal N., Rubinstein M. Soluble and membrane-anchored forms of the human IFN-alpha/beta receptor. J. Leukoc. Biol. 57:1995;712-718.
    • (1995) J. Leukoc. Biol. , vol.57 , pp. 712-718
    • Novick, D.1    Cohen, B.2    Tal, N.3    Rubinstein, M.4
  • 37
    • 0030765360 scopus 로고    scopus 로고
    • Cloning and characterization of soluble and transmembrane isoforms of a novel component of the murine Type I interferon receptor, IFNAR 2
    • Owczarek C.M., Hwang S.Y., Holland K.A., Gulluyan L.M., Tavaria M., Weaver B.et al. Cloning and characterization of soluble and transmembrane isoforms of a novel component of the murine Type I interferon receptor, IFNAR 2. J. Biol. Chem. 272:1997;23865-23870.
    • (1997) J. Biol. Chem. , vol.272 , pp. 23865-23870
    • Owczarek, C.M.1    Hwang, S.Y.2    Holland, K.A.3    Gulluyan, L.M.4    Tavaria, M.5    Weaver, B.6
  • 38
    • 0035863894 scopus 로고    scopus 로고
    • The soluble murine Type I interferon receptor Ifnar-2 is present in serum, is independently regulated, and has both agonistic and antagonistic properties
    • Hardy M.P., Owczarek C.M., Trajanovska S., Liu X., Kola I., Hertzog P.J. The soluble murine Type I interferon receptor Ifnar-2 is present in serum, is independently regulated, and has both agonistic and antagonistic properties. Blood. 97:2001;473-482.
    • (2001) Blood , vol.97 , pp. 473-482
    • Hardy, M.P.1    Owczarek, C.M.2    Trajanovska, S.3    Liu, X.4    Kola, I.5    Hertzog, P.J.6
  • 39
    • 0035933041 scopus 로고    scopus 로고
    • Antiviral activities of the soluble extracellular domains of Type I interferon receptors
    • Han C.S., Chen Y., Ezashi T., Roberts R.M. Antiviral activities of the soluble extracellular domains of Type I interferon receptors. Proc. Natl. Acad. Sci. U.S.A. 98:2001;6138-6143.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 6138-6143
    • Han, C.S.1    Chen, Y.2    Ezashi, T.3    Roberts, R.M.4
  • 40
    • 0029993080 scopus 로고    scopus 로고
    • Differential responsiveness of a splice variant of the human Type I interferon receptor to interferons
    • Cook J.R., Cleary C.M., Mariano T.M., Izotova L., Pestka S. Differential responsiveness of a splice variant of the human Type I interferon receptor to interferons. J. Biol. Chem. 271:1996;13448-13453.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13448-13453
    • Cook, J.R.1    Cleary, C.M.2    Mariano, T.M.3    Izotova, L.4    Pestka, S.5
  • 41
    • 0037335747 scopus 로고    scopus 로고
    • Cloning of a new Type II cytokine receptor activating signal transducer and activator of transcription (STAT)1, STAT2 and STAT3
    • Dumoutier L., Lejeune D., Hor S., Fickenscher H., Renauld J.C. Cloning of a new Type II cytokine receptor activating signal transducer and activator of transcription (STAT)1, STAT2 and STAT3. Biochem. J. 370:2003;391-396.
    • (2003) Biochem. J. , vol.370 , pp. 391-396
    • Dumoutier, L.1    Lejeune, D.2    Hor, S.3    Fickenscher, H.4    Renauld, J.C.5
  • 43
    • 0035877120 scopus 로고    scopus 로고
    • Identification, cloning, and characterization of a novel soluble receptor that binds IL-22 and neutralizes its activity
    • Kotenko S.V., Izotova L.S., Mirochnitchenko O.V., Esterova E., Dickensheets H., Donnelly R.P.et al. Identification, cloning, and characterization of a novel soluble receptor that binds IL-22 and neutralizes its activity. J. Immunol. 166:2001;7096-7103.
    • (2001) J. Immunol. , vol.166 , pp. 7096-7103
    • Kotenko, S.V.1    Izotova, L.S.2    Mirochnitchenko, O.V.3    Esterova, E.4    Dickensheets, H.5    Donnelly, R.P.6
  • 44
    • 0035877222 scopus 로고    scopus 로고
    • Cloning and characterization of IL-22 binding protein, a natural antagonist of IL-10-related T cell-derived inducible factor/IL-22
    • Dumoutier L., Lejeune D., Colau D., Renauld J.C. Cloning and characterization of IL-22 binding protein, a natural antagonist of IL-10-related T cell-derived inducible factor/IL-22. J. Immunol. 166:2001;7090-7095.
    • (2001) J. Immunol. , vol.166 , pp. 7090-7095
    • Dumoutier, L.1    Lejeune, D.2    Colau, D.3    Renauld, J.C.4
  • 45
    • 0034658583 scopus 로고    scopus 로고
    • Jak-Stat signal transduction pathway through the eyes of cytokine Class II receptor complexes
    • Kotenko S.V., Pestka S. Jak-Stat signal transduction pathway through the eyes of cytokine Class II receptor complexes. Oncogene. 19:2000;2557-2565.
    • (2000) Oncogene , vol.19 , pp. 2557-2565
    • Kotenko, S.V.1    Pestka, S.2
  • 46
    • 0028234529 scopus 로고
    • Jak-STAT pathways and transcriptional activation in response to IFNs and other extracellular signaling proteins
    • Darnell J.E. Jr., Kerr I.M., Stark G.R. Jak-STAT pathways and transcriptional activation in response to IFNs and other extracellular signaling proteins. Science. 264:1994;1415-1421.
    • (1994) Science , vol.264 , pp. 1415-1421
    • Darnell Jr., J.E.1    Kerr, I.M.2    Stark, G.R.3
  • 47
    • 0036256836 scopus 로고    scopus 로고
    • Series introduction. JAK-STAT signaling in human disease
    • Schindler C.W. Series introduction. JAK-STAT signaling in human disease. J. Clin. Invest. 109:2002;1133-1137.
    • (2002) J. Clin. Invest. , vol.109 , pp. 1133-1137
    • Schindler, C.W.1
  • 48
    • 0036233585 scopus 로고    scopus 로고
    • Cytokine signaling in 2002: New surprises in the Jak/Stat pathway
    • O'Shea J.J., Gadina M., Schreiber R.D. Cytokine signaling in 2002: new surprises in the Jak/Stat pathway. Cell. 109(Suppl.):2002;S121-S131.
    • (2002) Cell , vol.109 , Issue.SUPPL.
    • O'Shea, J.J.1    Gadina, M.2    Schreiber, R.D.3
  • 49
    • 0036690536 scopus 로고    scopus 로고
    • Review: IFN-alpha/beta receptor interactions to biologic outcomes: Understanding the circuitry
    • Brierley M.M., Fish E.N. Review: IFN-alpha/beta receptor interactions to biologic outcomes: understanding the circuitry. J Interferon Cytokine Res. 22:2002;835-845.
    • (2002) J Interferon Cytokine Res. , vol.22 , pp. 835-845
    • Brierley, M.M.1    Fish, E.N.2
  • 50
    • 0036771729 scopus 로고    scopus 로고
    • Signal transduction by Type I interferons
    • David M. Signal transduction by Type I interferons. Biotechniques. 33:2002;S58-S65.
    • (2002) Biotechniques , vol.33
    • David, M.1
  • 51
    • 0012263559 scopus 로고    scopus 로고
    • Seeing the light: Preassembly and ligand-induced changes of the interferon gamma receptor complex in cells
    • Krause C.D., Mei E., Xie J., Jia Y., Bopp M.A., Hochstrasser R.M.et al. Seeing the light: preassembly and ligand-induced changes of the interferon gamma receptor complex in cells. Mol. Cell Proteomics. 1:2002;805-815.
    • (2002) Mol. Cell Proteomics , vol.1 , pp. 805-815
    • Krause, C.D.1    Mei, E.2    Xie, J.3    Jia, Y.4    Bopp, M.A.5    Hochstrasser, R.M.6
  • 52
    • 0034733672 scopus 로고    scopus 로고
    • Cross-talk between interferon-gamma and interferon-alpha/beta signaling components in caveolar membrane domains
    • Takaoka A., Mitani Y., Suemori H., Sato M., Yokochi T., Noguchi S.et al. Cross-talk between interferon-gamma and interferon-alpha/beta signaling components in caveolar membrane domains. Science. 288:2000;2357-2360.
    • (2000) Science , vol.288 , pp. 2357-2360
    • Takaoka, A.1    Mitani, Y.2    Suemori, H.3    Sato, M.4    Yokochi, T.5    Noguchi, S.6
  • 53
    • 0035820185 scopus 로고    scopus 로고
    • Caveolae and clathrin-coated vesicles: Two possible internalization pathways for IFN-gamma and IFN-gamma receptor
    • Sadir R., Lambert A., Lortat-Jacob H., Morel G. Caveolae and clathrin-coated vesicles: two possible internalization pathways for IFN-gamma and IFN-gamma receptor. Cytokine. 14:2001;19-26.
    • (2001) Cytokine , vol.14 , pp. 19-26
    • Sadir, R.1    Lambert, A.2    Lortat-Jacob, H.3    Morel, G.4
  • 54
    • 0037103134 scopus 로고    scopus 로고
    • Lipid microdomains are required sites for the selective endocytosis and nuclear translocation of IFN-gamma, its receptor chain IFN-gamma receptor-1, and the phosphorylation and nuclear translocation of STAT1alpha
    • Subramaniam P.S., Johnson H.M. Lipid microdomains are required sites for the selective endocytosis and nuclear translocation of IFN-gamma, its receptor chain IFN-gamma receptor-1, and the phosphorylation and nuclear translocation of STAT1alpha. J. Immunol. 169:2002;1959-1969.
    • (2002) J. Immunol. , vol.169 , pp. 1959-1969
    • Subramaniam, P.S.1    Johnson, H.M.2
  • 55
    • 0029067876 scopus 로고
    • Crystal structure of a complex between interferon-gamma and its soluble high-affinity receptor [see comments]
    • Walter M.R., Windsor W.T., Nagabhushan T.L., Lundell D.J., Lunn C.A., Zauodny P.J.et al. Crystal structure of a complex between interferon-gamma and its soluble high-affinity receptor [see comments]. Nature. 376:1995;230-235.
    • (1995) Nature , vol.376 , pp. 230-235
    • Walter, M.R.1    Windsor, W.T.2    Nagabhushan, T.L.3    Lundell, D.J.4    Lunn, C.A.5    Zauodny, P.J.6
  • 56
    • 0034665458 scopus 로고    scopus 로고
    • Observation of an unexpected third receptor molecule in the crystal structure of human interferon-gamma receptor complex
    • Thiel D.J., le Du M.H., Walter R.L., D'Arcy A., Chene C., Fountoulakis M., Garotta G.et al. Observation of an unexpected third receptor molecule in the crystal structure of human interferon-gamma receptor complex. Struct. Fold Des. 8:2000;927-936.
    • (2000) Struct. Fold Des. , vol.8 , pp. 927-936
    • Thiel, D.J.1    Le Du, M.H.2    Walter, R.L.3    D'Arcy, A.4    Chene, C.5    Fountoulakis, M.6    Garotta, G.7
  • 57
    • 0034897552 scopus 로고    scopus 로고
    • Crystal structure of the IL-10/IL-10R1 complex reveals a shared receptor binding site
    • Josephson K., Logsdon N.J., Walter M.R. Crystal structure of the IL-10/IL-10R1 complex reveals a shared receptor binding site. Immunity. 15:2001;35-46.
    • (2001) Immunity , vol.15 , pp. 35-46
    • Josephson, K.1    Logsdon, N.J.2    Walter, M.R.3
  • 59
    • 0028114236 scopus 로고
    • Crystal structure of the extracellular region of human tissue factor
    • [published erratum appears in Nature 1994 October 20;371(6499):720]
    • Harlos K., Martin D.M., O'Brien D.P., Jones E.Y., Stuart D.I., Polikarpov I.et al. Crystal structure of the extracellular region of human tissue factor. Nature. 370:1994;662-666. [published erratum appears in Nature 1994 October 20;371(6499):720].
    • (1994) Nature , vol.370 , pp. 662-666
    • Harlos, K.1    Martin, D.M.2    O'Brien, D.P.3    Jones, E.Y.4    Stuart, D.I.5    Polikarpov, I.6
  • 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., De Vos A.M. The crystal structure of the extracellular domain of human tissue factor refined to 1.7 Å resolution. J. Mol. Biol. 256:1996;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
    • 0037632418 scopus 로고    scopus 로고
    • The human Type I interferon receptor: NMR structure reveals the molecular basis of ligand binding
    • Chill J.H., Quadt S.R., Levy R., Schreiber G., Anglister J. The human Type I interferon receptor: NMR structure reveals the molecular basis of ligand binding. Structure. 11:2003;791-802.
    • (2003) Structure , vol.11 , pp. 791-802
    • Chill, J.H.1    Quadt, S.R.2    Levy, R.3    Schreiber, G.4    Anglister, J.5
  • 62
    • 0033585030 scopus 로고    scopus 로고
    • Mutational and structural analysis of the binding interface between Type I interferons and their receptor Ifnar2
    • Piehler J., Schreiber G. Mutational and structural analysis of the binding interface between Type I interferons and their receptor Ifnar2. J. Mol. Biol. 294:1999;223-237.
    • (1999) J. Mol. Biol. , vol.294 , pp. 223-237
    • Piehler, J.1    Schreiber, G.2
  • 63
    • 0035907274 scopus 로고    scopus 로고
    • Identification of critical residues in bovine IFNAR-1 responsible for interferon binding
    • Cutrone E.C., Langer J.A. Identification of critical residues in bovine IFNAR-1 responsible for interferon binding. J. Biol. Chem. 276:2001;17140-17148.
    • (2001) J. Biol. Chem. , vol.276 , pp. 17140-17148
    • Cutrone, E.C.1    Langer, J.A.2
  • 64
    • 0035091323 scopus 로고    scopus 로고
    • The structure and activity of a monomeric interferon-gamma:alpha-chain receptor signaling complex
    • Randal M., Kossiakoff A.A. The structure and activity of a monomeric interferon-gamma:alpha-chain receptor signaling complex. Structure. 9:2001;155-163.
    • (2001) Structure , vol.9 , pp. 155-163
    • Randal, M.1    Kossiakoff, A.A.2
  • 65
    • 0032530322 scopus 로고    scopus 로고
    • Mapping human interferon-alpha (IFN-α2) binding determinants of the Type I interferon receptor subunit IFNAR-1 with human/bovine IFNAR-1 chimeras
    • Goldman L.A., Cutrone E.C., Dang A., Hao X.M., Lim J.K., Langer J.A. Mapping human interferon-alpha (IFN-α2) binding determinants of the Type I interferon receptor subunit IFNAR-1 with human/bovine IFNAR-1 chimeras. Biochemistry. 37:1998;13003-13010.
    • (1998) Biochemistry , vol.37 , pp. 13003-13010
    • Goldman, L.A.1    Cutrone, E.C.2    Dang, A.3    Hao, X.M.4    Lim, J.K.5    Langer, J.A.6
  • 66
    • 0034116821 scopus 로고    scopus 로고
    • Structure-function study of the extracellular domain of the human Type I interferon receptor (IFNAR)-1 subunit
    • Kumaran J., Colamonici O.R., Fish E.N. Structure-function study of the extracellular domain of the human Type I interferon receptor (IFNAR)-1 subunit. J. Interferon Cytokine Res. 20:2000;479-485.
    • (2000) J. Interferon Cytokine Res. , vol.20 , pp. 479-485
    • Kumaran, J.1    Colamonici, O.R.2    Fish, E.N.3
  • 67
    • 0032498113 scopus 로고    scopus 로고
    • Bovine Type I interferon receptor protein BoIFNAR-1 has high-affinity and broad specificity for human Type I interferons
    • Langer J.A., Yang J., Carmillo P., Ling L.E. Bovine Type I interferon receptor protein BoIFNAR-1 has high-affinity and broad specificity for human Type I interferons. FEBS Lett. 421:1998;131-135.
    • (1998) FEBS Lett. , vol.421 , pp. 131-135
    • Langer, J.A.1    Yang, J.2    Carmillo, P.3    Ling, L.E.4
  • 68
    • 0032566486 scopus 로고    scopus 로고
    • Shared receptor components but distinct complexes for alpha and beta interferons
    • Lewerenz M., Mogensen K.E., Uze G. Shared receptor components but distinct complexes for alpha and beta interferons. J. Mol. Biol. 282:1998;585-599.
    • (1998) J. Mol. Biol. , vol.282 , pp. 585-599
    • Lewerenz, M.1    Mogensen, K.E.2    Uze, G.3
  • 69
    • 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. 58:1993;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
  • 70
    • 0031766727 scopus 로고    scopus 로고
    • The structure of human interferon-beta: Implications for activity
    • Karpusas M., Whitty A., Runkel L., Hochman P. The structure of human interferon-beta: implications for activity. Cell Mol. Life Sci. 54:1998;1203-1216.
    • (1998) Cell Mol. Life Sci. , vol.54 , pp. 1203-1216
    • Karpusas, M.1    Whitty, A.2    Runkel, L.3    Hochman, P.4
  • 72
    • 0034646293 scopus 로고    scopus 로고
    • Systematic mutational mapping of sites on human interferon-beta-1a that are important for receptor binding and functional activity
    • Runkel L., DeDios C., Karpusas M., Betzenhauser M., Muldowney C., Zafari M.et al. Systematic mutational mapping of sites on human interferon-beta-1a that are important for receptor binding and functional activity. Biochemistry. 39:2000;2538-2551.
    • (2000) Biochemistry , vol.39 , pp. 2538-2551
    • Runkel, L.1    Dedios, C.2    Karpusas, M.3    Betzenhauser, M.4    Muldowney, C.5    Zafari, M.6
  • 73
    • 0034704093 scopus 로고    scopus 로고
    • New structural and functional aspects of the Type I interferon-receptor interaction revealed by comprehensive mutational analysis of the binding interface
    • Piehler J., Roisman L.C., Schreiber G. New structural and functional aspects of the Type I interferon-receptor interaction revealed by comprehensive mutational analysis of the binding interface. J. Biol. Chem. 275:2000;40425-40433.
    • (2000) J. Biol. Chem. , vol.275 , pp. 40425-40433
    • Piehler, J.1    Roisman, L.C.2    Schreiber, G.3
  • 74
    • 0035818558 scopus 로고    scopus 로고
    • Structure of the interferon-receptor complex determined by distance constraints from double-mutant cycles and flexible docking
    • Roisman L.C., Piehler J., Trosset J.Y., Scheraga H.A., Schreiber G. Structure of the interferon-receptor complex determined by distance constraints from double-mutant cycles and flexible docking. Proc. Natl. Acad. Sci. U.S.A. 98:2001;13231-13236.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 13231-13236
    • Roisman, L.C.1    Piehler, J.2    Trosset, J.Y.3    Scheraga, H.A.4    Schreiber, G.5
  • 75
    • 0030998098 scopus 로고    scopus 로고
    • Crystal structure of the type-I interleukin-1 receptor complexed with interleukin-1beta
    • Vigers G.P., Anderson L.J., Caffes P., Brandhuber B.J. Crystal structure of the type-I interleukin-1 receptor complexed with interleukin-1beta. Nature. 386:1997;190-194.
    • (1997) Nature , vol.386 , pp. 190-194
    • Vigers, G.P.1    Anderson, L.J.2    Caffes, P.3    Brandhuber, B.J.4
  • 76
    • 0031000052 scopus 로고    scopus 로고
    • A new cytokine-receptor binding mode revealed by the crystal structure of the IL-1 receptor with an antagonist
    • Schreuder H., Tardif C., Trump-Kallmeyer S., Soffientini A., Sarubbi E., Akeson A.et al. A new cytokine-receptor binding mode revealed by the crystal structure of the IL-1 receptor with an antagonist. Nature. 386:1997;194-200.
    • (1997) Nature , vol.386 , pp. 194-200
    • Schreuder, H.1    Tardif, C.2    Trump-Kallmeyer, S.3    Soffientini, A.4    Sarubbi, E.5    Akeson, A.6
  • 77
    • 0034711314 scopus 로고    scopus 로고
    • X-ray crystal structure of a small antagonist peptide bound to interleukin-1 receptor type 1
    • Vigers G.P., Dripps D.J., Edwards C.K. III, Brandhuber B.J. X-ray crystal structure of a small antagonist peptide bound to interleukin-1 receptor type 1. J. Biol. Chem. 275:2000;36927-36933.
    • (2000) J. Biol. Chem. , vol.275 , pp. 36927-36933
    • Vigers, G.P.1    Dripps, D.J.2    Edwards III, C.K.3    Brandhuber, B.J.4
  • 78
    • 0031042220 scopus 로고    scopus 로고
    • Contributions of cloned Type I interferon receptor subunits to differential ligand binding
    • Cutrone E.C., Langer J.A. Contributions of cloned Type I interferon receptor subunits to differential ligand binding. FEBS Lett. 404:1997;197-202.
    • (1997) FEBS Lett. , vol.404 , pp. 197-202
    • Cutrone, E.C.1    Langer, J.A.2
  • 79
    • 0038609651 scopus 로고    scopus 로고
    • Hexameric structure and assembly of the interleukin-6/IL-6 alpha-receptor/gp130 complex
    • Boulanger M.J., Chow D.C., Brevnova E.E., Garcia K.C. Hexameric structure and assembly of the interleukin-6/IL-6 alpha-receptor/gp130 complex. Science. 300:2003;2101-2104.
    • (2003) Science , vol.300 , pp. 2101-2104
    • Boulanger, M.J.1    Chow, D.C.2    Brevnova, E.E.3    Garcia, K.C.4
  • 80
    • 0027318516 scopus 로고
    • Structure and function of human growth hormone: Implications for the hematopoietins
    • Wells J.A., De Vos A.M. Structure and function of human growth hormone: implications for the hematopoietins. Annu. Rev. Biophys. Biomol. Struct. 22:1993;329-351.
    • (1993) Annu. Rev. Biophys. Biomol. Struct. , vol.22 , pp. 329-351
    • Wells, J.A.1    De Vos, A.M.2
  • 81
    • 0025317502 scopus 로고
    • Definition of general topological equivalence in protein structures. A procedure involving comparison of properties and relationships through simulated annealing and dynamic programming
    • Sali A, Blundell TL. Definition of general topological equivalence in protein structures. A procedure involving comparison of properties and relationships through simulated annealing and dynamic programming. J Mol Biol 1990;212(20):403-28.
    • (1990) J Mol Biol , vol.212 , Issue.20 , pp. 403-428
    • Sali, A.1    Blundell, T.L.2
  • 83
    • 0030050701 scopus 로고    scopus 로고
    • Binding in the growth hormone receptor complex
    • Wells J.A. Binding in the growth hormone receptor complex. Proc. Natl. Acad. Sci. U.S.A. 93:1996;1-6.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 1-6
    • Wells, J.A.1
  • 84
    • 0036399552 scopus 로고    scopus 로고
    • Interferon-alpha/beta-receptor interactions: A complex story unfolding
    • Deonarain R., Chan D.C., Platanias L.C., Fish E.N. Interferon-alpha/beta- receptor interactions: a complex story unfolding. Curr. Pharm. Des. 8:2002;2131-2137.
    • (2002) Curr. Pharm. Des. , vol.8 , pp. 2131-2137
    • Deonarain, R.1    Chan, D.C.2    Platanias, L.C.3    Fish, E.N.4
  • 85
    • 0034851253 scopus 로고    scopus 로고
    • The TF:VIIa complex: Clinical significance, structure-function relationships and its role in signaling and metastasis
    • Konigsberg W., Kirchhofer D., Riederer M.A., Nemerson Y. The TF:VIIa complex: clinical significance, structure-function relationships and its role in signaling and metastasis. Thromb. Haemost. 86:2001;757-771.
    • (2001) Thromb. Haemost. , vol.86 , pp. 757-771
    • Konigsberg, W.1    Kirchhofer, D.2    Riederer, M.A.3    Nemerson, Y.4
  • 86
    • 0023685684 scopus 로고
    • Molecular cloning and expression of the human interferon-gamma receptor
    • Aguet M., Dembic Z., Merlin G. Molecular cloning and expression of the human interferon-gamma receptor. Cell. 55:1988;273-280.
    • (1988) Cell , vol.55 , pp. 273-280
    • Aguet, M.1    Dembic, Z.2    Merlin, G.3
  • 87
    • 0028268368 scopus 로고
    • Identification and sequence of an accessory factor required for activation of the human interferon gamma receptor
    • Soh J., Donnelly R.J., Kotenko S., Mariano T.M., Cook J.R., Wang N.et al. Identification and sequence of an accessory factor required for activation of the human interferon gamma receptor. Cell. 76:1994;793-802.
    • (1994) Cell , vol.76 , pp. 793-802
    • Soh, J.1    Donnelly, R.J.2    Kotenko, S.3    Mariano, T.M.4    Cook, J.R.5    Wang, N.6
  • 88
    • 0028219965 scopus 로고
    • A novel member of the interferon receptor family complements functionality of the murine interferon gamma receptor in human cells
    • Hemmi S., Bohni R., Stark G., Di Marco F., Aguet M. A novel member of the interferon receptor family complements functionality of the murine interferon gamma receptor in human cells. Cell. 76:1994;803-810.
    • (1994) Cell , vol.76 , pp. 803-810
    • Hemmi, S.1    Bohni, R.2    Stark, G.3    Di Marco, F.4    Aguet, M.5
  • 89
    • 0025015138 scopus 로고
    • Genetic transfer of a functional human interferon-α receptor into a mouse cells: Cloning and expression of its cDNA
    • Uzé G., Lutfalla G., Gresser I. Genetic transfer of a functional human interferon-α receptor into a mouse cells: cloning and expression of its cDNA. Cell. 60:1990;225-234.
    • (1990) Cell , vol.60 , pp. 225-234
    • Uzé, G.1    Lutfalla, G.2    Gresser, I.3
  • 90
    • 0028299340 scopus 로고
    • The human interferon alpha/beta receptor: Characterization and molecular cloning
    • Novick D., Cohen B., Rubinstein M. The human interferon alpha/beta receptor: characterization and molecular cloning. Cell. 77:1994;391-400.
    • (1994) Cell , vol.77 , pp. 391-400
    • Novick, D.1    Cohen, B.2    Rubinstein, M.3
  • 91
    • 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., Hackett R., Pitha P.et al. 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. 270:1995;21606-21611.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21606-21611
    • Domanski, P.1    Witte, M.2    Kellum, M.3    Rubinstein, M.4    Hackett, R.5    Pitha, P.6
  • 92
    • 0029052176 scopus 로고
    • Ligand-induced association of the Type I interferon receptor components
    • Cohen B., Novick D., Barak S., Rubinstein M. Ligand-induced association of the Type I interferon receptor components. Mol. Cell Biol. 15:1995;4208-4214.
    • (1995) Mol. Cell Biol. , vol.15 , pp. 4208-4214
    • Cohen, B.1    Novick, D.2    Barak, S.3    Rubinstein, M.4
  • 94
    • 0028350053 scopus 로고
    • Expression cloning and characterization of a human IL-10 receptor
    • Liu Y., Wei S.H., Ho A.S., de Waal Malefyt R., Moore K.W. Expression cloning and characterization of a human IL-10 receptor. J. Immunol. 152:1994;1821-1829.
    • (1994) J. Immunol. , vol.152 , pp. 1821-1829
    • Liu, Y.1    Wei, S.H.2    Ho, A.S.3    De Waal Malefyt, R.4    Moore, K.W.5
  • 95
    • 0032536530 scopus 로고    scopus 로고
    • The orphan receptor CRF2-4 is an essential subunit of the interleukin 10 receptor
    • Spencer S.D., Di Marco F., Hooley J., Pitts-Meek S., Bauer M., Ryan A.M.et al. The orphan receptor CRF2-4 is an essential subunit of the interleukin 10 receptor. J. Exp. Med. 187:1998;571-578.
    • (1998) J. Exp. Med. , vol.187 , pp. 571-578
    • Spencer, S.D.1    Di Marco, F.2    Hooley, J.3    Pitts-Meek, S.4    Bauer, M.5    Ryan, A.M.6
  • 96
    • 0034613201 scopus 로고    scopus 로고
    • Interleukin (IL)-22, a novel human cytokine that signals through the interferon receptor-related proteins CRF2-4 and IL-22R
    • Xie M.H., Aggarwal S., Ho W.H., Foster J., Zhang Z., Stinson J.et al. Interleukin (IL)-22, a novel human cytokine that signals through the interferon receptor-related proteins CRF2-4 and IL-22R. J. Biol. Chem. 275:2000;31335- 31339.
    • (2000) J. Biol. Chem. , vol.275 , pp. 31335-31339
    • Xie, M.H.1    Aggarwal, S.2    Ho, W.H.3    Foster, J.4    Zhang, Z.5    Stinson, J.6
  • 97
    • 0035951795 scopus 로고    scopus 로고
    • Identification of the functional interleukin-22 (IL-22) receptor complex: The IL-10R2 chain (IL-10Rbeta) is a common chain of both the IL-10 and IL-22 (IL-10-related T cell-derived inducible factor, IL-TIF) receptor complexes
    • Kotenko S.V., Izotova L.S., Mirochnitchenko O.V., Esterova E., Dickensheets H., Donnelly R.P.et al. Identification of the functional interleukin-22 (IL-22) receptor complex: the IL-10R2 chain (IL-10Rbeta) is a common chain of both the IL-10 and IL-22 (IL-10-related T cell-derived inducible factor, IL-TIF) receptor complexes. J. Biol. Chem. 276:2001;2725-2732.
    • (2001) J. Biol. Chem. , vol.276 , pp. 2725-2732
    • Kotenko, S.V.1    Izotova, L.S.2    Mirochnitchenko, O.V.3    Esterova, E.4    Dickensheets, H.5    Donnelly, R.P.6
  • 98
    • 17744373448 scopus 로고    scopus 로고
    • Interleukin 20: Discovery, receptor identification, and role in epidermal function
    • Blumberg H., Conklin D., Xu W.F., Grossmann A., Brender T., Carollo S.et al. Interleukin 20: discovery, receptor identification, and role in epidermal function. Cell. 104:2001;9-19.
    • (2001) Cell , vol.104 , pp. 9-19
    • Blumberg, H.1    Conklin, D.2    Xu, W.F.3    Grossmann, A.4    Brender, T.5    Carollo, S.6
  • 99
    • 0035478639 scopus 로고    scopus 로고
    • Cutting edge: STAT activation by IL-19, IL-20 and mda-7 through IL-20 receptor complexes of two types
    • Dumoutier L., Leemans C., Lejeune D., Kotenko S.V., Renauld J.C.et al. Cutting edge: STAT activation by IL-19, IL-20 and mda-7 through IL-20 receptor complexes of two types. J. Immunol. 167:2001;3545-3549.
    • (2001) J. Immunol. , vol.167 , pp. 3545-3549
    • Dumoutier, L.1    Leemans, C.2    Lejeune, D.3    Kotenko, S.V.4    Renauld, J.C.5
  • 100
    • 0036510539 scopus 로고    scopus 로고
    • Interleukin 24 (MDA-7/MOB-5) signals through two heterodimeric receptors, IL-22R1/IL-20R2 and IL-20R1/IL-20R2
    • Wang M., Tan Z., Zhang R., Kotenko S.V., Liang P. Interleukin 24 (MDA-7/MOB-5) signals through two heterodimeric receptors, IL-22R1/IL-20R2 and IL-20R1/IL-20R2. J. Biol. Chem. 277:2002;7341-7347.
    • (2002) J. Biol. Chem. , vol.277 , pp. 7341-7347
    • Wang, M.1    Tan, Z.2    Zhang, R.3    Kotenko, S.V.4    Liang, P.5
  • 101
    • 0037033092 scopus 로고    scopus 로고
    • Interleukins 19, 20, and 24 signal through two distinct receptor complexes. Differences in receptor-ligand interactions mediate unique biological functions
    • Parrish-Novak J., Xu W., Brender T., Yao L., Jones C., West J.et al. Interleukins 19, 20, and 24 signal through two distinct receptor complexes. Differences in receptor-ligand interactions mediate unique biological functions. J. Biol. Chem. 277:2002;47517-47523.
    • (2002) J. Biol. Chem. , vol.277 , pp. 47517-47523
    • Parrish-Novak, J.1    Xu, W.2    Brender, T.3    Yao, L.4    Jones, C.5    West, J.6
  • 102
    • 85030906299 scopus 로고    scopus 로고
    • US Patent 6,544,505 (2003)
    • D.C. Conklin et al., US Patent 6,544,505 (2003).
    • Conklin Et Al., D.C.1


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