메뉴 건너뛰기




Volumn 10, Issue 4, 2009, Pages 333-339

Integration of cytokine and heterologous receptor signaling pathways

Author keywords

[No Author keywords available]

Indexed keywords

CELL RECEPTOR; CYTOKINE; CYTOKINE RECEPTOR; IMMUNOGLOBULIN; IMMUNOMODULATING AGENT; INTERLEUKIN 10; JANUS KINASE; STAT PROTEIN;

EID: 62849116942     PISSN: 15292908     EISSN: 15292916     Source Type: Journal    
DOI: 10.1038/ni.1713     Document Type: Review
Times cited : (81)

References (109)
  • 1
    • 33847351136 scopus 로고    scopus 로고
    • The JAK-STAT signaling pathway: Input and output integration
    • Murray, P.J. The JAK-STAT signaling pathway: Input and output integration. J. Immunol. 178, 2623-2629 (2007).
    • (2007) J. Immunol , vol.178 , pp. 2623-2629
    • Murray, P.J.1
  • 2
    • 0025719982 scopus 로고
    • Cytokines in context
    • Nathan, C. & Sporn, M. Cytokines in context. J. Cell Biol. 113 981-986 (1991).
    • (1991) J. Cell Biol , vol.113 , pp. 981-986
    • Nathan, C.1    Sporn, M.2
  • 3
    • 33750522675 scopus 로고    scopus 로고
    • Jaks and cytokine receptors - an intimate relationship
    • Haan, C., Kreis, S., Margue, C. & Behrmann, I. Jaks and cytokine receptors - an intimate relationship. Biochem. Pharmacol. 72 1538-1546 (2006).
    • (2006) Biochem. Pharmacol , vol.72 , pp. 1538-1546
    • Haan, C.1    Kreis, S.2    Margue, C.3    Behrmann, I.4
  • 5
    • 0028786276 scopus 로고
    • The Janus protein tyrosine kinase family and its role in cytokine signaling
    • Ihle, J.N. The Janus protein tyrosine kinase family and its role in cytokine signaling. Adv. Immunol. 60, 1-35 (1995).
    • (1995) Adv. Immunol , vol.60 , pp. 1-35
    • Ihle, J.N.1
  • 6
    • 0026735084 scopus 로고
    • JAK2, a third member of the JAK family of protein tyrosine kinases
    • Harpur, A.G., Andres, A.C., Ziemiecki, A., Aston, R.R. & Wilks, A.F. JAK2, a third member of the JAK family of protein tyrosine kinases. Oncogene 7, 1347-1353 (1992).
    • (1992) Oncogene , vol.7 , pp. 1347-1353
    • Harpur, A.G.1    Andres, A.C.2    Ziemiecki, A.3    Aston, R.R.4    Wilks, A.F.5
  • 7
    • 0026344661 scopus 로고
    • Cloning members of protein-tyrosine kinase family using polymerase chain reaction
    • Wilks, A.F. Cloning members of protein-tyrosine kinase family using polymerase chain reaction. Methods Enzymol. 200, 533-546 (1991).
    • (1991) Methods Enzymol , vol.200 , pp. 533-546
    • Wilks, A.F.1
  • 8
    • 0028117163 scopus 로고
    • Cytokine signal transduction
    • Kishimoto, T., Taga, T. & Akira, S. Cytokine signal transduction. Cell 76, 253-262 (1994).
    • (1994) Cell , vol.76 , pp. 253-262
    • Kishimoto, T.1    Taga, T.2    Akira, S.3
  • 9
    • 0035367819 scopus 로고    scopus 로고
    • Signaling by type I and II cytokine receptors: Ten years after
    • Gadina, M. et al. Signaling by type I and II cytokine receptors: ten years after. Curr. Opin. Immunol. 13, 363-373 (2001).
    • (2001) Curr. Opin. Immunol , vol.13 , pp. 363-373
    • Gadina, M.1
  • 10
    • 0031919849 scopus 로고    scopus 로고
    • Jaks and STATs: Biological implications
    • Leonard, W.J. & O'Shea, J.J. Jaks and STATs: Biological implications. Annu. Rev. Immunol. 16, 293-322 (1998).
    • (1998) Annu. Rev. Immunol , vol.16 , pp. 293-322
    • Leonard, W.J.1    O'Shea, J.J.2
  • 11
    • 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.), S121-S131 (2002).
    • (2002) Cell , vol.109 , Issue.SUPPL.
    • O'Shea, J.J.1    Gadina, M.2    Schreiber, R.D.3
  • 13
    • 0034046605 scopus 로고    scopus 로고
    • STAT family of transcription factors in cytokine-mediated biological responses
    • Takeda, K. & Akira, S. STAT family of transcription factors in cytokine-mediated biological responses. Cytokine Growth Factor Rev. 11, 199-207 (2000).
    • (2000) Cytokine Growth Factor Rev , vol.11 , pp. 199-207
    • Takeda, K.1    Akira, S.2
  • 14
    • 0035811006 scopus 로고    scopus 로고
    • Biologic consequences of Stat1-independent IFN signaling
    • Gil, M.P. et al. Biologic consequences of Stat1-independent IFN signaling. Proc. Natl. Acad. Sci. USA 98, 6680-6685 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 6680-6685
    • Gil, M.P.1
  • 15
    • 0036476551 scopus 로고    scopus 로고
    • Stat1-dependent and -independent pathways in IFN-γ-dependent signaling
    • Ramana, C.V., Gil, M.P., Schreiber, R.D. & Stark, G.R. Stat1-dependent and -independent pathways in IFN-γ-dependent signaling. Trends Immunol. 23, 96-101 (2002).
    • (2002) Trends Immunol , vol.23 , pp. 96-101
    • Ramana, C.V.1    Gil, M.P.2    Schreiber, R.D.3    Stark, G.R.4
  • 16
    • 4744364574 scopus 로고    scopus 로고
    • Alternative activation of STAT1 and STAT3 in response to interferon-γ
    • Qing, Y. & Stark, G.R. Alternative activation of STAT1 and STAT3 in response to interferon-γ. J. Biol. Chem. 279, 41679-41685 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 41679-41685
    • Qing, Y.1    Stark, G.R.2
  • 17
    • 0037062503 scopus 로고    scopus 로고
    • Mutational switch of an IL-6 response to an interferon-γ-like response
    • Costa-Pereira, A.P. et al. Mutational switch of an IL-6 response to an interferon-γ-like response. Proc. Natl. Acad. Sci. USA 99, 8043-8047 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 8043-8047
    • Costa-Pereira, A.P.1
  • 18
    • 36248957695 scopus 로고    scopus 로고
    • NKG2D signaling is coupled to the interleukin 15 receptor signaling pathway
    • Horng, T., Bezbradica, J.S. & Medzhitov, R. NKG2D signaling is coupled to the interleukin 15 receptor signaling pathway. Nat. Immunol. 8, 1345-1352 (2007).
    • (2007) Nat. Immunol , vol.8 , pp. 1345-1352
    • Horng, T.1    Bezbradica, J.S.2    Medzhitov, R.3
  • 19
    • 9244249240 scopus 로고    scopus 로고
    • Amplification of IFN-α-induced STAT1 activation and inflammatory function by Syk and ITAM-containing adaptors
    • Tassiulas, I. et al. Amplification of IFN-α-induced STAT1 activation and inflammatory function by Syk and ITAM-containing adaptors. Nat. Immunol. 5, 1181-1189 (2004).
    • (2004) Nat. Immunol , vol.5 , pp. 1181-1189
    • Tassiulas, I.1
  • 20
    • 33747346235 scopus 로고    scopus 로고
    • Signal integration between IFNγ and TLR signalling pathways in macrophages
    • Schroder, K., Sweet, M.J. & Hume, D.A. Signal integration between IFNγ and TLR signalling pathways in macrophages. Immunobiology 211 511-524 (2006).
    • (2006) Immunobiology , vol.211 , pp. 511-524
    • Schroder, K.1    Sweet, M.J.2    Hume, D.A.3
  • 21
    • 0036565888 scopus 로고    scopus 로고
    • Stimulation of toll-like receptor 4 expression in human mononuclear phagocytes by interferon-γ: A molecular basis for priming and synergism with bacterial lipopolysaccharide
    • Bosisio, D. et al. Stimulation of toll-like receptor 4 expression in human mononuclear phagocytes by interferon-γ: A molecular basis for priming and synergism with bacterial lipopolysaccharide. Blood 99, 3427-3431 (2002).
    • (2002) Blood , vol.99 , pp. 3427-3431
    • Bosisio, D.1
  • 22
    • 0020564534 scopus 로고
    • Recombinant immune interferon increases immunoglobulin G Fc receptors on cultured human mononuclear phagocytes
    • Guyre, P.M., Morganelli, P.M. & Miller, R. Recombinant immune interferon increases immunoglobulin G Fc receptors on cultured human mononuclear phagocytes. J. Clin. Invest. 72, 393-397 (1983).
    • (1983) J. Clin. Invest , vol.72 , pp. 393-397
    • Guyre, P.M.1    Morganelli, P.M.2    Miller, R.3
  • 23
    • 22544487815 scopus 로고    scopus 로고
    • FcγRIV : A novel FcR with distinct IgG subclass specificity
    • Nimmerjahn, F., Bruhns, P., Horiuchi, K. & Ravetch, J.V. FcγRIV : A novel FcR with distinct IgG subclass specificity. Immunity 23 41-51 (2005).
    • (2005) Immunity , vol.23 , pp. 41-51
    • Nimmerjahn, F.1    Bruhns, P.2    Horiuchi, K.3    Ravetch, J.V.4
  • 24
    • 0034655267 scopus 로고    scopus 로고
    • Expression of a functional highaffinity IgG receptor, FcγRI, on human mast cells: Up-regulation by IFN-γ
    • Okayama, Y., Kirshenbaum, A.S. & Metcalfe, D.D. Expression of a functional highaffinity IgG receptor, FcγRI, on human mast cells: up-regulation by IFN-γ. J. Immunol. 164, 4332-4339 (2000).
    • (2000) J. Immunol , vol.164 , pp. 4332-4339
    • Okayama, Y.1    Kirshenbaum, A.S.2    Metcalfe, D.D.3
  • 25
    • 0035168783 scopus 로고    scopus 로고
    • Differential modulation of stimulatory and inhibitory Fcγ receptors on human monocytes by Th1 and Th2 cytokines
    • Pricop, L. et al. Differential modulation of stimulatory and inhibitory Fcγ receptors on human monocytes by Th1 and Th2 cytokines. J. Immunol. 166, 531-537 (2001).
    • (2001) J. Immunol , vol.166 , pp. 531-537
    • Pricop, L.1
  • 26
    • 4444240035 scopus 로고    scopus 로고
    • Coordinated induction by IL15 of a TCR-independent NKG2D signaling pathway converts CTL into lymphokine-activated killer cells in celiac disease
    • Meresse, B. et al. Coordinated induction by IL15 of a TCR-independent NKG2D signaling pathway converts CTL into lymphokine-activated killer cells in celiac disease. Immunity 21, 357-366 (2004).
    • (2004) Immunity , vol.21 , pp. 357-366
    • Meresse, B.1
  • 27
    • 34247100277 scopus 로고    scopus 로고
    • Dendritic cells prime natural killer cells by trans-presenting interleukin 15
    • Lucas, M., Schachterle, W., Oberle, K., Aichele, P. & Diefenbach, A. Dendritic cells prime natural killer cells by trans-presenting interleukin 15. Immunity 26, 503-517 (2007).
    • (2007) Immunity , vol.26 , pp. 503-517
    • Lucas, M.1    Schachterle, W.2    Oberle, K.3    Aichele, P.4    Diefenbach, A.5
  • 28
    • 0031774896 scopus 로고    scopus 로고
    • Stat5b is essential for natural killer cell-mediated proliferation and cytolytic activity
    • Imada, K. et al. Stat5b is essential for natural killer cell-mediated proliferation and cytolytic activity. J. Exp. Med. 188, 2067-2074 (1998).
    • (1998) J. Exp. Med , vol.188 , pp. 2067-2074
    • Imada, K.1
  • 29
    • 0037108518 scopus 로고    scopus 로고
    • Enforced expression of Bcl-2 restores the number of NK cells, but does not rescue the impaired development of NKT cells or intraepithelial lymphocytes, in IL-2/IL-15 receptor β-chain-deficient mice
    • Minagawa, M. et al. Enforced expression of Bcl-2 restores the number of NK cells, but does not rescue the impaired development of NKT cells or intraepithelial lymphocytes, in IL-2/IL-15 receptor β-chain-deficient mice. J. Immunol. 169, 4153-4160 (2002).
    • (2002) J. Immunol , vol.169 , pp. 4153-4160
    • Minagawa, M.1
  • 30
    • 41949097030 scopus 로고    scopus 로고
    • The biology of interleukin-2
    • Malek, T.R. The biology of interleukin-2. Annu. Rev. Immunol. 26, 453-479 (2008).
    • (2008) Annu. Rev. Immunol , vol.26 , pp. 453-479
    • Malek, T.R.1
  • 31
    • 54549103162 scopus 로고    scopus 로고
    • Priming for T helper type 2 differentiation by interleukin 2-mediated induction of interleukin 4 receptor α-chain expression
    • Liao, W. et al. Priming for T helper type 2 differentiation by interleukin 2-mediated induction of interleukin 4 receptor α-chain expression. Nat. Immunol. 9, 1288-1296 (2008).
    • (2008) Nat. Immunol , vol.9 , pp. 1288-1296
    • Liao, W.1
  • 33
    • 8044250881 scopus 로고    scopus 로고
    • Regulation of the interleukin (IL)-12R β2 subunit expression in developing T helper 1 (Th1) and Th2 cells
    • Szabo, S.J., Dighe, A.S., Gubler, U. & Murphy, K.M. Regulation of the interleukin (IL)-12R β2 subunit expression in developing T helper 1 (Th1) and Th2 cells. J. Exp. Med. 185, 817-824 (1997).
    • (1997) J. Exp. Med , vol.185 , pp. 817-824
    • Szabo, S.J.1    Dighe, A.S.2    Gubler, U.3    Murphy, K.M.4
  • 34
    • 32244442562 scopus 로고    scopus 로고
    • TGFß in the context of an inflammatory cytokine milieu supports de novo differentiation of IL-17-producing T cells
    • Veldhoen, M., Hocking, R.J., Atkins, C.J., Locksley, R.M. & Stockinger, B. TGFß in the context of an inflammatory cytokine milieu supports de novo differentiation of IL-17-producing T cells. Immunity 24 179-189 (2006).
    • (2006) Immunity , vol.24 , pp. 179-189
    • Veldhoen, M.1    Hocking, R.J.2    Atkins, C.J.3    Locksley, R.M.4    Stockinger, B.5
  • 35
    • 33748588423 scopus 로고    scopus 로고
    • + T helper cells
    • + T helper cells. Cell 126, 1121-1133 (2006).
    • (2006) Cell , vol.126 , pp. 1121-1133
    • Ivanov, I.I.1
  • 36
    • 41549134361 scopus 로고    scopus 로고
    • Th17 cell differentiation: The long and winding road
    • McGeachy, M.J. & Cua, D.J. Th17 cell differentiation: The long and winding road. Immunity 28, 445-453 (2008).
    • (2008) Immunity , vol.28 , pp. 445-453
    • McGeachy, M.J.1    Cua, D.J.2
  • 37
    • 0029001660 scopus 로고
    • Components of a Stat recognition code: Evidence for two layers of molecular selectivity
    • Schindler, U., Wu, P., Rothe, M., Brasseur, M. & McKnight, S.L. Components of a Stat recognition code: Evidence for two layers of molecular selectivity. Immunity 2, 689-697 (1995).
    • (1995) Immunity , vol.2 , pp. 689-697
    • Schindler, U.1    Wu, P.2    Rothe, M.3    Brasseur, M.4    McKnight, S.L.5
  • 38
    • 0028913109 scopus 로고
    • A STAT protein domain that determines DNA sequence recognition suggests a novel DNA-binding domain
    • Horvath, C.M., Wen, Z. & Darnell, J.E. Jr. A STAT protein domain that determines DNA sequence recognition suggests a novel DNA-binding domain. Genes Dev. 9, 984-994 (1995).
    • (1995) Genes Dev , vol.9 , pp. 984-994
    • Horvath, C.M.1    Wen, Z.2    Darnell Jr., J.E.3
  • 39
    • 0842266786 scopus 로고    scopus 로고
    • Interferon-γ: An overview of signals, mechanisms and functions
    • Schroder, K., Hertzog, P.J., Ravasi, T. & Hume, D.A. Interferon-γ: An overview of signals, mechanisms and functions. J. Leukoc. Biol. 75, 163-189 (2004).
    • (2004) J. Leukoc. Biol , vol.75 , pp. 163-189
    • Schroder, K.1    Hertzog, P.J.2    Ravasi, T.3    Hume, D.A.4
  • 40
    • 0032845125 scopus 로고    scopus 로고
    • Interacting regions in Stat3 and c-Jun that participate in cooperative transcriptional activation
    • Zhang, X., Wrzeszczynska, M.H., Horvath, C.M. & Darnell, J.E. Jr. Interacting regions in Stat3 and c-Jun that participate in cooperative transcriptional activation. Mol. Cell. Biol. 19, 7138-7146 (1999).
    • (1999) Mol. Cell. Biol , vol.19 , pp. 7138-7146
    • Zhang, X.1    Wrzeszczynska, M.H.2    Horvath, C.M.3    Darnell Jr., J.E.4
  • 41
    • 44649178270 scopus 로고    scopus 로고
    • Janus-kinase-3-dependent signals induce chromatin remodeling at the Ifng locus during T helper 1 cell differentiation
    • Shi, M., Lin, T.H., Appell, K.C. & Berg, L.J. Janus-kinase-3-dependent signals induce chromatin remodeling at the Ifng locus during T helper 1 cell differentiation. Immunity 28, 763-773 (2008).
    • (2008) Immunity , vol.28 , pp. 763-773
    • Shi, M.1    Lin, T.H.2    Appell, K.C.3    Berg, L.J.4
  • 42
    • 0344064893 scopus 로고    scopus 로고
    • Stat5 activation plays a critical role in Th2 differentiation
    • Zhu, J., Cote-Sierra, J., Guo, L. & Paul, W.E. Stat5 activation plays a critical role in Th2 differentiation. Immunity 19, 739-748 (2003).
    • (2003) Immunity , vol.19 , pp. 739-748
    • Zhu, J.1    Cote-Sierra, J.2    Guo, L.3    Paul, W.E.4
  • 43
    • 36749029364 scopus 로고    scopus 로고
    • Demethylation of a specific hypersensitive site in the Th2 locus control region
    • Kim, S.T., Fields, P.E. & Flavell, R.A. Demethylation of a specific hypersensitive site in the Th2 locus control region. Proc. Natl. Acad. Sci. USA 104, 17052-17057 (2007).
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 17052-17057
    • Kim, S.T.1    Fields, P.E.2    Flavell, R.A.3
  • 44
    • 0037436119 scopus 로고    scopus 로고
    • + T cellmediated suppression by dendritic cells
    • + T cellmediated suppression by dendritic cells. Science 299, 1033-1036 (2003).
    • (2003) Science , vol.299 , pp. 1033-1036
    • Pasare, C.1    Medzhitov, R.2
  • 45
    • 33646595287 scopus 로고    scopus 로고
    • IFN-γ suppresses IL-10 production and synergizes with TLR2 by regulating GSK3 and CREB/AP-1 proteins
    • Hu, X. et al. IFN-γ suppresses IL-10 production and synergizes with TLR2 by regulating GSK3 and CREB/AP-1 proteins. Immunity 24, 563-574 (2006).
    • (2006) Immunity , vol.24 , pp. 563-574
    • Hu, X.1
  • 46
    • 2542478996 scopus 로고    scopus 로고
    • The role of suppressors of cytokine signaling (SOCS) proteins in regulation of the immune response
    • Alexander, W.S. & Hilton, D.J. The role of suppressors of cytokine signaling (SOCS) proteins in regulation of the immune response. Annu. Rev. Immunol. 22, 503-529 (2004).
    • (2004) Annu. Rev. Immunol , vol.22 , pp. 503-529
    • Alexander, W.S.1    Hilton, D.J.2
  • 47
    • 34249660614 scopus 로고    scopus 로고
    • SOCS proteins, cytokine signalling and immune regulation
    • Yoshimura, A., Naka, T. & Kubo, M. SOCS proteins, cytokine signalling and immune regulation. Nat. Rev. Immunol. 7, 454-465 (2007).
    • (2007) Nat. Rev. Immunol , vol.7 , pp. 454-465
    • Yoshimura, A.1    Naka, T.2    Kubo, M.3
  • 48
    • 18744371050 scopus 로고    scopus 로고
    • SOCS-1 participates in negative regulation of LPS responses
    • Nakagawa, R. et al. SOCS-1 participates in negative regulation of LPS responses. Immunity 17, 677-687 (2002).
    • (2002) Immunity , vol.17 , pp. 677-687
    • Nakagawa, R.1
  • 49
    • 31344467156 scopus 로고    scopus 로고
    • Suppressor of cytokine signaling 1 negatively regulates Toll-like receptor signaling by mediating Mal degradation
    • Mansell, A. et al. Suppressor of cytokine signaling 1 negatively regulates Toll-like receptor signaling by mediating Mal degradation. Nat. Immunol. 7, 148-155 (2006).
    • (2006) Nat. Immunol , vol.7 , pp. 148-155
    • Mansell, A.1
  • 50
    • 0347955360 scopus 로고    scopus 로고
    • Regulation of NF-κB signaling by Pin1-dependent prolyl isomerization and ubiquitin-mediated proteolysis of p65/RelA
    • Ryo, A. et al. Regulation of NF-κB signaling by Pin1-dependent prolyl isomerization and ubiquitin-mediated proteolysis of p65/RelA. Mol. Cell 12, 1413-1426 (2003).
    • (2003) Mol. Cell , vol.12 , pp. 1413-1426
    • Ryo, A.1
  • 51
    • 36849033963 scopus 로고    scopus 로고
    • TAM receptors are pleiotropic inhibitors of the innate immune response
    • Rothlin, C.V., Ghosh, S., Zuniga, E.I., Oldstone, M.B. & Lemke, G. TAM receptors are pleiotropic inhibitors of the innate immune response. Cell 131, 1124-1136 (2007).
    • (2007) Cell , vol.131 , pp. 1124-1136
    • Rothlin, C.V.1    Ghosh, S.2    Zuniga, E.I.3    Oldstone, M.B.4    Lemke, G.5
  • 53
    • 0028219966 scopus 로고
    • An IL-4 receptor region containing an insulin receptor motif is important for IL-4-mediated IRS-1 phosphorylation and cell growth
    • Keegan, A.D. et al. An IL-4 receptor region containing an insulin receptor motif is important for IL-4-mediated IRS-1 phosphorylation and cell growth. Cell 76, 811-820 (1994).
    • (1994) Cell , vol.76 , pp. 811-820
    • Keegan, A.D.1
  • 54
    • 0029148591 scopus 로고
    • Role of IRS-2 in insulin and cytokine signalling
    • Sun, X.J. et al. Role of IRS-2 in insulin and cytokine signalling. Nature 377, 173-177 (1995).
    • (1995) Nature , vol.377 , pp. 173-177
    • Sun, X.J.1
  • 55
    • 0033921265 scopus 로고    scopus 로고
    • Aronica, M.A., Goenka, S. & Boothby, M. IL-4-dependent induction of BCL-2 and BCL-X(L)IN activated T lymphocytes through a STAT6- and pi 3-kinase-independent pathway. Cytokine 12, 578-587 (2000).
    • Aronica, M.A., Goenka, S. & Boothby, M. IL-4-dependent induction of BCL-2 and BCL-X(L)IN activated T lymphocytes through a STAT6- and pi 3-kinase-independent pathway. Cytokine 12, 578-587 (2000).
  • 56
    • 0034282897 scopus 로고    scopus 로고
    • The docking molecule gab2 is induced by lymphocyte activation and is involved in signaling by interleukin-2 and interleukin-15 but not other common γ chain-using cytokines
    • Gadina, M. et al. The docking molecule gab2 is induced by lymphocyte activation and is involved in signaling by interleukin-2 and interleukin-15 but not other common γ chain-using cytokines. J. Biol. Chem. 275, 26959-26966 (2000).
    • (2000) J. Biol. Chem , vol.275 , pp. 26959-26966
    • Gadina, M.1
  • 57
    • 0032523416 scopus 로고    scopus 로고
    • Involvement of SHP-2 in multiple aspects of IL-2 signaling: Evidence for a positive regulatory role
    • Gadina, M., Stancato, L.M., Bacon, C.M., Larner, A.C. & O'Shea, J.J. Involvement of SHP-2 in multiple aspects of IL-2 signaling: Evidence for a positive regulatory role. J. Immunol. 160, 4657-4661 (1998).
    • (1998) J. Immunol , vol.160 , pp. 4657-4661
    • Gadina, M.1    Stancato, L.M.2    Bacon, C.M.3    Larner, A.C.4    O'Shea, J.J.5
  • 59
    • 11144357191 scopus 로고    scopus 로고
    • + regulatory T cells
    • + regulatory T cells. J. Immunol. 172, 5287-5296 (2004).
    • (2004) J. Immunol , vol.172 , pp. 5287-5296
    • Bensinger, S.J.1
  • 60
    • 0029115522 scopus 로고
    • Tyrosine phosphorylation and activation of STAT5, STAT3, and Janus kinases by interleukins 2 and 15
    • Johnston, J.A. et al. Tyrosine phosphorylation and activation of STAT5, STAT3, and Janus kinases by interleukins 2 and 15. Proc. Natl. Acad. Sci. USA 92, 8705-8709 (1995).
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8705-8709
    • Johnston, J.A.1
  • 61
    • 33745812074 scopus 로고    scopus 로고
    • Budagian, V., Bulanova, E., Paus, R. & Bulfone-Paus, S. IL-15/IL-15 receptor biology: A guided tour through an expanding universe. Cytokine Growth Factor Rev. 17, 259-280 (2006).
    • Budagian, V., Bulanova, E., Paus, R. & Bulfone-Paus, S. IL-15/IL-15 receptor biology: A guided tour through an expanding universe. Cytokine Growth Factor Rev. 17, 259-280 (2006).
  • 62
    • 0035576258 scopus 로고    scopus 로고
    • The IL-15Rα chain signals through association with Syk in human B cells
    • Bulanova, E. et al. The IL-15Rα chain signals through association with Syk in human B cells. J. Immunol. 167, 6292-6302 (2001).
    • (2001) J. Immunol , vol.167 , pp. 6292-6302
    • Bulanova, E.1
  • 63
    • 0032535695 scopus 로고    scopus 로고
    • Interleukin-15 (IL-15) induces NF-κB activation and IL-8 production in human neutrophils
    • McDonald, P.P., Russo, M.P., Ferrini, S. & Cassatella, M.A. Interleukin-15 (IL-15) induces NF-κB activation and IL-8 production in human neutrophils. Blood 92, 4828-4835 (1998).
    • (1998) Blood , vol.92 , pp. 4828-4835
    • McDonald, P.P.1    Russo, M.P.2    Ferrini, S.3    Cassatella, M.A.4
  • 64
    • 3042826228 scopus 로고    scopus 로고
    • Interleukin-15 enhances human neutrophil phagocytosis by a Syk-dependent mechanism: Importance of the IL-15Rα chain
    • Ratthe, C. & Girard, D. Interleukin-15 enhances human neutrophil phagocytosis by a Syk-dependent mechanism: Importance of the IL-15Rα chain. J. Leukoc. Biol. 76, 162-168 (2004).
    • (2004) J. Leukoc. Biol , vol.76 , pp. 162-168
    • Ratthe, C.1    Girard, D.2
  • 65
    • 0033826512 scopus 로고    scopus 로고
    • New role for Shc in activation of the phosphatidylinositol 3-kinase/Akt pathway
    • Gu, H. et al. New role for Shc in activation of the phosphatidylinositol 3-kinase/Akt pathway. Mol. Cell. Biol. 20 7109-7120 (2000).
    • (2000) Mol. Cell. Biol , vol.20 , pp. 7109-7120
    • Gu, H.1
  • 66
    • 0038561082 scopus 로고    scopus 로고
    • Mast cells express novel functional IL-15 receptor α isoforms
    • Bulanova, E. et al. Mast cells express novel functional IL-15 receptor α isoforms. J. Immunol. 170, 5045-5055 (2003).
    • (2003) J. Immunol , vol.170 , pp. 5045-5055
    • Bulanova, E.1
  • 67
    • 29244436892 scopus 로고    scopus 로고
    • A promiscuous liaison between IL-15 receptor and Axl receptor tyrosine kinase in cell death control
    • Budagian, V. et al. A promiscuous liaison between IL-15 receptor and Axl receptor tyrosine kinase in cell death control. EMBO J. 24, 4260-4270 (2005).
    • (2005) EMBO J , vol.24 , pp. 4260-4270
    • Budagian, V.1
  • 68
    • 0034109091 scopus 로고    scopus 로고
    • The CD2-subset of the Ig superfamily of cell surface molecules: Receptor-ligand pairs expressed by NK cells and other immune cells
    • Tangye, S.G., Phillips, J.H. & Lanier, L.L. The CD2-subset of the Ig superfamily of cell surface molecules: Receptor-ligand pairs expressed by NK cells and other immune cells. Semin. Immunol. 12, 149-157 (2000).
    • (2000) Semin. Immunol , vol.12 , pp. 149-157
    • Tangye, S.G.1    Phillips, J.H.2    Lanier, L.L.3
  • 69
    • 4944266186 scopus 로고    scopus 로고
    • A role for the immunological synapse in lineage commitment of CD4 lymphocytes
    • Maldonado, R.A., Irvine, D.J., Schreiber, R. & Glimcher, L.H. A role for the immunological synapse in lineage commitment of CD4 lymphocytes. Nature 431, 527-532 (2004).
    • (2004) Nature , vol.431 , pp. 527-532
    • Maldonado, R.A.1    Irvine, D.J.2    Schreiber, R.3    Glimcher, L.H.4
  • 70
    • 33947730608 scopus 로고    scopus 로고
    • Asymmetric T lymphocyte division in the initiation of adaptive immune responses
    • Chang, J.T. et al. Asymmetric T lymphocyte division in the initiation of adaptive immune responses. Science 315, 1687-1691 (2007).
    • (2007) Science , vol.315 , pp. 1687-1691
    • Chang, J.T.1
  • 71
    • 43249092876 scopus 로고    scopus 로고
    • Colocalization of the IL-12 receptor and FcγRIa to natural killer cell lipid rafts leads to activation of ERK and enhanced production of interferon-γ
    • Kondadasula, S.V. et al. Colocalization of the IL-12 receptor and FcγRIa to natural killer cell lipid rafts leads to activation of ERK and enhanced production of interferon-γ. Blood 111, 4173-4183 (2008).
    • (2008) Blood , vol.111 , pp. 4173-4183
    • Kondadasula, S.V.1
  • 72
    • 0034733672 scopus 로고    scopus 로고
    • Cross talk between interferon-γ and -α/ß signaling components in caveolar membrane domains
    • Takaoka, A. et al. Cross talk between interferon-γ and -α/ß signaling components in caveolar membrane domains. Science 288 2357-2360 (2000).
    • (2000) Science , vol.288 , pp. 2357-2360
    • Takaoka, A.1
  • 73
    • 0034884781 scopus 로고    scopus 로고
    • Cross talk of the interferon-α/ß signalling complex with gp130 for effective interleukin-6 signalling
    • Mitani, Y. et al. Cross talk of the interferon-α/ß signalling complex with gp130 for effective interleukin-6 signalling. Genes Cells 6, 631-640 (2001).
    • (2001) Genes Cells , vol.6 , pp. 631-640
    • Mitani, Y.1
  • 74
    • 0036734498 scopus 로고    scopus 로고
    • Sensitization of IFN-γ Jak-STAT signaling during macrophage activation
    • Hu, X. et al. Sensitization of IFN-γ Jak-STAT signaling during macrophage activation. Nat. Immunol. 3, 859-866 (2002).
    • (2002) Nat. Immunol , vol.3 , pp. 859-866
    • Hu, X.1
  • 75
    • 0032854459 scopus 로고    scopus 로고
    • Upregulation of type I interferon receptor by IFN-gamma
    • Mizukoshi, E. et al. Upregulation of type I interferon receptor by IFN-gamma. J. Interferon Cytokine Res. 19, 1019-1023 (1999).
    • (1999) J. Interferon Cytokine Res , vol.19 , pp. 1019-1023
    • Mizukoshi, E.1
  • 76
    • 38449093322 scopus 로고    scopus 로고
    • Tuning' of type I interferon-induced Jak-STAT1 signaling by calciumdependent kinases in macrophages
    • Wang, L. et al. 'Tuning' of type I interferon-induced Jak-STAT1 signaling by calciumdependent kinases in macrophages. Nat. Immunol. 9, 186-193 (2008).
    • (2008) Nat. Immunol , vol.9 , pp. 186-193
    • Wang, L.1
  • 77
    • 0032127465 scopus 로고    scopus 로고
    • Stat1 combines signals derived from IFN-γ and LPS receptors during macrophage activation
    • Kovarik, P., Stoiber, D., Novy, M. & Decker, T. Stat1 combines signals derived from IFN-γ and LPS receptors during macrophage activation. EMBO J. 17, 3660-3668 (1998).
    • (1998) EMBO J , vol.17 , pp. 3660-3668
    • Kovarik, P.1    Stoiber, D.2    Novy, M.3    Decker, T.4
  • 78
    • 0035862950 scopus 로고    scopus 로고
    • Specificity of signaling by STAT1 depends on SH2 and C-terminal domains that regulate Ser727 phosphorylation, differentially affecting specific target gene expression
    • Kovarik, P. et al. Specificity of signaling by STAT1 depends on SH2 and C-terminal domains that regulate Ser727 phosphorylation, differentially affecting specific target gene expression. EMBO J. 20, 91-100 (2001).
    • (2001) EMBO J , vol.20 , pp. 91-100
    • Kovarik, P.1
  • 79
    • 0034284088 scopus 로고    scopus 로고
    • Importance of the MKK6/p38 pathway for interleukin-12-induced STAT4 serine phosphorylation and transcriptional activity
    • Visconti, R. et al. Importance of the MKK6/p38 pathway for interleukin-12-induced STAT4 serine phosphorylation and transcriptional activity. Blood 96, 1844-1852 (2000).
    • (2000) Blood , vol.96 , pp. 1844-1852
    • Visconti, R.1
  • 80
    • 0037197260 scopus 로고    scopus 로고
    • Requirement of Ca2+ and CaMKII for Stat1 Ser-727 phosphorylation in response to IFN-γ
    • Nair, J.S. et al. Requirement of Ca2+ and CaMKII for Stat1 Ser-727 phosphorylation in response to IFN-γ. Proc. Natl. Acad. Sci. USA 99, 5971-5976 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 5971-5976
    • Nair, J.S.1
  • 81
    • 0034658024 scopus 로고    scopus 로고
    • Serine phosphorylation of STATs
    • Decker, T. & Kovarik, P. Serine phosphorylation of STATs. Oncogene 19, 2628-2637 (2000).
    • (2000) Oncogene , vol.19 , pp. 2628-2637
    • Decker, T.1    Kovarik, P.2
  • 82
    • 0033598839 scopus 로고    scopus 로고
    • Stress-induced phosphorylation of STAT1 at Ser727 requires p38 mitogen-activated protein kinase whereas IFN-γ uses a different signaling pathway
    • Kovarik, P. et al. Stress-induced phosphorylation of STAT1 at Ser727 requires p38 mitogen-activated protein kinase whereas IFN-γ uses a different signaling pathway. Proc. Natl. Acad. Sci. USA 96 13956-13961 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 13956-13961
    • Kovarik, P.1
  • 83
    • 33947678731 scopus 로고    scopus 로고
    • Immune complexes suppress IFN-γ signaling by activation of the FcγRI pathway
    • Boekhoudt, G.H., Frazier-Jessen, M.R. & Feldman, G.M. Immune complexes suppress IFN-γ signaling by activation of the FcγRI pathway. J. Leukoc. Biol. 81, 1086-1092 (2007).
    • (2007) J. Leukoc. Biol , vol.81 , pp. 1086-1092
    • Boekhoudt, G.H.1    Frazier-Jessen, M.R.2    Feldman, G.M.3
  • 84
    • 0028833563 scopus 로고
    • IgG immune complexes inhibit IFNgamma- induced transcription of the Fc gamma RI gene in human monocytes by preventing the tyrosine phosphorylation of the p91 (Stat1) transcription factor
    • Feldman, G.M., Chuang, E.J. & Finbloom, D.S. IgG immune complexes inhibit IFNgamma- induced transcription of the Fc gamma RI gene in human monocytes by preventing the tyrosine phosphorylation of the p91 (Stat1) transcription factor. J. Immunol. 154, 318-325 (1995).
    • (1995) J. Immunol , vol.154 , pp. 318-325
    • Feldman, G.M.1    Chuang, E.J.2    Finbloom, D.S.3
  • 85
    • 22544474648 scopus 로고    scopus 로고
    • Inhibition of IFN-α signaling by a PKC- and protein tyrosine phosphatase SHP-2-dependent pathway
    • Du, Z. et al. Inhibition of IFN-α signaling by a PKC- and protein tyrosine phosphatase SHP-2-dependent pathway. Proc. Natl. Acad. Sci. USA 102, 10267-10272 (2005).
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 10267-10272
    • Du, Z.1
  • 86
    • 0033233214 scopus 로고    scopus 로고
    • LPS and TNFα induce SOCS3 mRNA and inhibit IL-6-induced activation of STAT3 in macrophages
    • Bode, J.G. et al. LPS and TNFα induce SOCS3 mRNA and inhibit IL-6-induced activation of STAT3 in macrophages. FEBS Lett. 463 365-370 (1999).
    • (1999) FEBS Lett , vol.463 , pp. 365-370
    • Bode, J.G.1
  • 87
    • 0037530607 scopus 로고    scopus 로고
    • TNF-α induces tyrosine phosphorylation and recruitment of the Src homology protein-tyrosine phosphatase 2 to the gp130 signal-transducing subunit of the IL-6 receptor complex
    • Bode, J.G. et al. TNF-α induces tyrosine phosphorylation and recruitment of the Src homology protein-tyrosine phosphatase 2 to the gp130 signal-transducing subunit of the IL-6 receptor complex. J. Immunol. 171, 257-266 (2003).
    • (2003) J. Immunol , vol.171 , pp. 257-266
    • Bode, J.G.1
  • 88
    • 38849162742 scopus 로고    scopus 로고
    • Mechanism of crosstalk inhibition of IL-6 signaling in response to LPS and TNFα
    • Kiu, H. et al. Mechanism of crosstalk inhibition of IL-6 signaling in response to LPS and TNFα. Growth Factors 25, 319-328 (2007).
    • (2007) Growth Factors , vol.25 , pp. 319-328
    • Kiu, H.1
  • 89
    • 0034675851 scopus 로고    scopus 로고
    • Transient inhibition of interleukin 4 signaling by T cell receptor ligation
    • Zhu, J. et al. Transient inhibition of interleukin 4 signaling by T cell receptor ligation. J. Exp. Med. 192, 1125-1134 (2000).
    • (2000) J. Exp. Med , vol.192 , pp. 1125-1134
    • Zhu, J.1
  • 90
    • 52949087160 scopus 로고    scopus 로고
    • A signal-switch hypothesis for cross-regulation of cytokine and TLR signalling pathways
    • Ivashkiv, L.B. A signal-switch hypothesis for cross-regulation of cytokine and TLR signalling pathways. Nat. Rev. Immunol. 8, 816-822 (2008).
    • (2008) Nat. Rev. Immunol , vol.8 , pp. 816-822
    • Ivashkiv, L.B.1
  • 91
    • 36049007739 scopus 로고    scopus 로고
    • NK cell survival mediated through the regulatory synapse with human DCs requires IL-15Rα
    • Brilot, F., Strowig, T., Roberts, S.M., Arrey, F. & Munz, C. NK cell survival mediated through the regulatory synapse with human DCs requires IL-15Rα. J. Clin. Invest. 117, 3316-3329 (2007).
    • (2007) J. Clin. Invest , vol.117 , pp. 3316-3329
    • Brilot, F.1    Strowig, T.2    Roberts, S.M.3    Arrey, F.4    Munz, C.5
  • 92
    • 3342924000 scopus 로고    scopus 로고
    • V amosi, G. et al. IL-2 and IL-15 receptor α-subunits are coexpressed in a supramolecular receptor cluster in lipid rafts of T cells. Proc. Natl. Acad. Sci. USA 101, 11082-11087 (2004).
    • V amosi, G. et al. IL-2 and IL-15 receptor α-subunits are coexpressed in a supramolecular receptor cluster in lipid rafts of T cells. Proc. Natl. Acad. Sci. USA 101, 11082-11087 (2004).
  • 93
    • 0037184955 scopus 로고    scopus 로고
    • The organizing principle in the formation of the T cell receptor-CD3 complex
    • Call, M.E., Pyrdol, J., Wiedmann, M. & Wucherpfennig, K.W. The organizing principle in the formation of the T cell receptor-CD3 complex. Cell 111, 967-979 (2002).
    • (2002) Cell , vol.111 , pp. 967-979
    • Call, M.E.1    Pyrdol, J.2    Wiedmann, M.3    Wucherpfennig, K.W.4
  • 94
    • 33646718143 scopus 로고    scopus 로고
    • The assembly of diverse immune receptors is focused on a polar membrane-embedded interaction site
    • Feng, J., Call, M.E. & Wucherpfennig, K.W. The assembly of diverse immune receptors is focused on a polar membrane-embedded interaction site. PLoS Biol. 4, e142 (2006).
    • (2006) PLoS Biol , vol.4
    • Feng, J.1    Call, M.E.2    Wucherpfennig, K.W.3
  • 95
    • 34548319444 scopus 로고    scopus 로고
    • Role of the extracellular and transmembrane domain of Ig-α/ß in assembly of the B cell antigen receptor (BCR)
    • Dylke, J., Lopes, J., Dang-Lawson, M., Machtaler, S. & Matsuuchi, L. Role of the extracellular and transmembrane domain of Ig-α/ß in assembly of the B cell antigen receptor (BCR). Immunol. Lett. 112, 47-57 (2007).
    • (2007) Immunol. Lett , vol.112 , pp. 47-57
    • Dylke, J.1    Lopes, J.2    Dang-Lawson, M.3    Machtaler, S.4    Matsuuchi, L.5
  • 96
    • 0028210391 scopus 로고
    • A mutation of the mu transmembrane that disrupts endoplasmic reticulum retention. Effects on association with accessory proteins and signal transduction
    • Stevens, T.L., Blum, J.H., Foy, S.P., Matsuuchi, L. & DeFranco, A.L. A mutation of the mu transmembrane that disrupts endoplasmic reticulum retention. Effects on association with accessory proteins and signal transduction. J. Immunol. 152, 4397-4406 (1994).
    • (1994) J. Immunol , vol.152 , pp. 4397-4406
    • Stevens, T.L.1    Blum, J.H.2    Foy, S.P.3    Matsuuchi, L.4    DeFranco, A.L.5
  • 97
    • 46049088691 scopus 로고    scopus 로고
    • Protein-protein interactions in the membrane: Sequence, structural, and biological motifs
    • Moore, D.T., Berger, B.W. & DeGrado, W.F. Protein-protein interactions in the membrane: Sequence, structural, and biological motifs. Structure 16, 991-1001 (2008).
    • (2008) Structure , vol.16 , pp. 991-1001
    • Moore, D.T.1    Berger, B.W.2    DeGrado, W.F.3
  • 98
    • 0036793242 scopus 로고    scopus 로고
    • Sweet 'n' sour: The impact of differential glycosylation on T cell responses
    • Daniels, M.A., Hogquist, K.A. & Jameson, S.C. Sweet 'n' sour: The impact of differential glycosylation on T cell responses. Nat. Immunol. 3, 903-910 (2002).
    • (2002) Nat. Immunol , vol.3 , pp. 903-910
    • Daniels, M.A.1    Hogquist, K.A.2    Jameson, S.C.3
  • 99
    • 0032742944 scopus 로고    scopus 로고
    • Roles for glycosylation of cell surface receptors involved in cellular immune recognition
    • Rudd, P.M. et al. Roles for glycosylation of cell surface receptors involved in cellular immune recognition. J. Mol. Biol. 293, 351-366 (1999).
    • (1999) J. Mol. Biol , vol.293 , pp. 351-366
    • Rudd, P.M.1
  • 100
    • 62849091082 scopus 로고    scopus 로고
    • Structures common to different glycans
    • 2nd edn, eds. Varki, A.C. et al. ch. 13 Cold Spring Harbor Laboratory Press, Woodbury, New York, USA
    • Stanley, P. & Cummings, R.D. Structures common to different glycans. in Essentials of Glycobiology 2nd edn. (eds. Varki, A.C. et al. ch. 13 (Cold Spring Harbor Laboratory Press, Woodbury, New York, USA, 2009).
    • (2009) Essentials of Glycobiology
    • Stanley, P.1    Cummings, R.D.2
  • 101
    • 0035496911 scopus 로고    scopus 로고
    • + T lymphocytes induce polarized exocytosis of secretory lysosomes by dendritic cells with release of interleukin-1β and cathepsin D
    • + T lymphocytes induce polarized exocytosis of secretory lysosomes by dendritic cells with release of interleukin-1β and cathepsin D. Blood 98, 2152-2159 (2001).
    • (2001) Blood , vol.98 , pp. 2152-2159
    • Gardella, S.1
  • 102
    • 85117738461 scopus 로고    scopus 로고
    • Semino, C., Angelini, G., Poggi, A. & Rubartelli, A. NK/iDC interaction results in IL-18 secretion by DCs at the synaptic cleft followed by NK cell activation and release of the DC maturation factor HMGB1. Blood 106, 609-616 (2005).
    • Semino, C., Angelini, G., Poggi, A. & Rubartelli, A. NK/iDC interaction results in IL-18 secretion by DCs at the synaptic cleft followed by NK cell activation and release of the DC maturation factor HMGB1. Blood 106, 609-616 (2005).
  • 103
    • 8644281284 scopus 로고    scopus 로고
    • NK cell activation by dendritic cells (DCs) requires the formation of a synapse leading to IL-12 polarization in DCs
    • Borg, C. et al. NK cell activation by dendritic cells (DCs) requires the formation of a synapse leading to IL-12 polarization in DCs. Blood 104, 3267-3275 (2004).
    • (2004) Blood , vol.104 , pp. 3267-3275
    • Borg, C.1
  • 104
    • 33344458030 scopus 로고    scopus 로고
    • T cells use two directionally distinct pathways for cytokine secretion
    • Huse, M., Lillemeier, B.F., Kuhns, M.S., Chen, D.S. & Davis, M.M. T cells use two directionally distinct pathways for cytokine secretion. Nat. Immunol. 7, 247-255 (2006).
    • (2006) Nat. Immunol , vol.7 , pp. 247-255
    • Huse, M.1    Lillemeier, B.F.2    Kuhns, M.S.3    Chen, D.S.4    Davis, M.M.5
  • 105
    • 0025978984 scopus 로고
    • Polarized expression of cytokines in cell conjugates of helper T cells and splenic B cells
    • Kupfer, A., Mosmann, T.R. & Kupfer, H. Polarized expression of cytokines in cell conjugates of helper T cells and splenic B cells. Proc. Natl. Acad. Sci. USA 88, 775-779 (1991).
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 775-779
    • Kupfer, A.1    Mosmann, T.R.2    Kupfer, H.3
  • 106
    • 28544452195 scopus 로고    scopus 로고
    • A role for the phagosome in cytokine secretion
    • Murray, R.Z., Kay, J.G., Sangermani, D.G. & Stow, J.L. A role for the phagosome in cytokine secretion. Science 310, 1492-1495 (2005).
    • (2005) Science , vol.310 , pp. 1492-1495
    • Murray, R.Z.1    Kay, J.G.2    Sangermani, D.G.3    Stow, J.L.4
  • 107
    • 44049096285 scopus 로고    scopus 로고
    • Scalable signaling mediated by T cell antigen receptor-CD3 ITAMs ensures effective negative selection and prevents autoimmunity
    • Holst, J. et al. Scalable signaling mediated by T cell antigen receptor-CD3 ITAMs ensures effective negative selection and prevents autoimmunity. Nat. Immunol. 9, 658-666 (2008).
    • (2008) Nat. Immunol , vol.9 , pp. 658-666
    • Holst, J.1
  • 108
    • 2442642691 scopus 로고    scopus 로고
    • RIP1 is an essential mediator of Toll-like receptor 3-induced NF-κB activation
    • Meylan, E. et al. RIP1 is an essential mediator of Toll-like receptor 3-induced NF-κB activation. Nat. Immunol. 5, 503-507 (2004).
    • (2004) Nat. Immunol , vol.5 , pp. 503-507
    • Meylan, E.1
  • 109
    • 33749345768 scopus 로고    scopus 로고
    • Dysregulation of interleukin-10-dependent gene expression in rheumatoid arthritis synovial macrophages
    • Antoniv, T.T. & Ivashkiv, L.B. Dysregulation of interleukin-10-dependent gene expression in rheumatoid arthritis synovial macrophages. Arthritis Rheum. 54, 2711-2721 (2006)
    • (2006) Arthritis Rheum , vol.54 , pp. 2711-2721
    • Antoniv, T.T.1    Ivashkiv, L.B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.