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Volumn 5, Issue 10, 2004, Pages 1061-1068

Interferon-α induction through Toll-like receptors involves a direct interaction of IRF7 with MyD88 and TRAF6

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA INTERFERON; INTERFERON REGULATORY FACTOR 3; INTERFERON REGULATORY FACTOR 7; MYELOID DIFFERENTIATION FACTOR 88; TOLL LIKE RECEPTOR; TOLL LIKE RECEPTOR 7; TOLL LIKE RECEPTOR 8; TOLL LIKE RECEPTOR 9; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 6; UBIQUITIN PROTEIN LIGASE; CELL SURFACE RECEPTOR; DIFFERENTIATION ANTIGEN; DNA BINDING PROTEIN; IMMUNOGLOBULIN RECEPTOR; IRF7 PROTEIN, HUMAN; IRF7 PROTEIN, MOUSE; MEMBRANE PROTEIN; MYD88 PROTEIN, HUMAN; MYD88 PROTEIN, MOUSE; PROTEIN; SIGNAL TRANSDUCING ADAPTOR PROTEIN; TLR7 PROTEIN, HUMAN; TLR8 PROTEIN, HUMAN; TLR9 PROTEIN, HUMAN; UBIQUITIN;

EID: 5444274514     PISSN: 15292908     EISSN: None     Source Type: Journal    
DOI: 10.1038/ni1118     Document Type: Article
Times cited : (873)

References (50)
  • 1
    • 0030666222 scopus 로고    scopus 로고
    • Innate immunity: The virtues of a nonclonal system of recognition
    • Medzhitov, R. & Janeway, C.J. Innate immunity: the virtues of a nonclonal system of recognition. Cell 91, 295-298 (1997).
    • (1997) Cell , vol.91 , pp. 295-298
    • Medzhitov, R.1    Janeway, C.J.2
  • 3
    • 0035909372 scopus 로고    scopus 로고
    • Recognition of double-stranded RNA and activation of NF-κB by Toll-like receptor 3
    • Alexopoulou, L., Holt, A.C., Medzhitov, R. & Flavell, R.A. Recognition of double-stranded RNA and activation of NF-κB by Toll-like receptor 3. Nature 413, 732-738 (2001).
    • (2001) Nature , vol.413 , pp. 732-738
    • Alexopoulou, L.1    Holt, A.C.2    Medzhitov, R.3    Flavell, R.A.4
  • 4
    • 1542317550 scopus 로고    scopus 로고
    • Innate antiviral responses by means of TLR7-mediated recognition of single-stranded RNA
    • Diebold, S.S. et al. Innate antiviral responses by means of TLR7-mediated recognition of single-stranded RNA. Science 303, 1529-1531 (2004).
    • (2004) Science , vol.303 , pp. 1529-1531
    • Diebold, S.S.1
  • 5
    • 0035953543 scopus 로고    scopus 로고
    • The innate immune response to bacterial flagellin is mediated by Toll-like receptor 5
    • Hayashi, F. et al. The innate immune response to bacterial flagellin is mediated by Toll-like receptor 5. Nature 410, 1099-1103 (2001).
    • (2001) Nature , vol.410 , pp. 1099-1103
    • Hayashi, F.1
  • 6
    • 1542317578 scopus 로고    scopus 로고
    • Species-specific recognition of single-stranded RNA via toll-like receptor 7 and 8
    • Heil, F. et al. Species-specific recognition of single-stranded RNA via toll-like receptor 7 and 8. Science 303, 1526-1529 (2004).
    • (2004) Science , vol.303 , pp. 1526-1529
    • Heil, F.1
  • 7
    • 0036008014 scopus 로고    scopus 로고
    • Small anti-viral compounds activate immune cells via the TLR7 MyD88-dependent signaling pathway
    • Hemmi, H. et al. Small anti-viral compounds activate immune cells via the TLR7 MyD88-dependent signaling pathway. Nat. Immunol. 3, 196-200 (2002).
    • (2002) Nat. Immunol. , vol.3 , pp. 196-200
    • Hemmi, H.1
  • 8
    • 0034619794 scopus 로고    scopus 로고
    • A Toll-like receptor recognizes bacterial DNA
    • Hemmi, H. et al. A Toll-like receptor recognizes bacterial DNA. Nature 408, 740-745 (2000).
    • (2000) Nature , vol.408 , pp. 740-745
    • Hemmi, H.1
  • 9
    • 0033120081 scopus 로고    scopus 로고
    • Cutting edge: Toll-like receptor 4 (TLR4)-deficient mice are hyporesponsive to lipopolysaccharide: Evidence for TLR4 as the Lps gene product
    • Hoshino, K. et al. Cutting edge: Toll-like receptor 4 (TLR4)-deficient mice are hyporesponsive to lipopolysaccharide: evidence for TLR4 as the Lps gene product. J. Immunol. 162, 3749-3752 (1999).
    • (1999) J. Immunol. , vol.162 , pp. 3749-3752
    • Hoshino, K.1
  • 10
    • 0032509295 scopus 로고    scopus 로고
    • Defective LPS signaling in C3H/HeJ and C57BL/10ScCr mice: Mutations in Tlr4 gene
    • Poltorak, A. et al. Defective LPS signaling in C3H/HeJ and C57BL/10ScCr mice: mutations in Tlr4 gene. Science 282, 2085-2088 (1998).
    • (1998) Science , vol.282 , pp. 2085-2088
    • Poltorak, A.1
  • 11
    • 0033213590 scopus 로고    scopus 로고
    • Differential roles of TLR2 and TLR4 in recognition of gram-negative and gram-positive bacterial cell wall components
    • Takeuchi, O. et al. Differential roles of TLR2 and TLR4 in recognition of gram-negative and gram-positive bacterial cell wall components. Immunity 11, 443-451 (1999).
    • (1999) Immunity , vol.11 , pp. 443-451
    • Takeuchi, O.1
  • 12
    • 0034922923 scopus 로고    scopus 로고
    • Discrimination of bacterial lipoproteins by Toll-like receptor 6
    • Takeuchi, O. et al. Discrimination of bacterial lipoproteins by Toll-like receptor 6. Int. Immunol. 13, 933-940 (2001).
    • (2001) Int. Immunol. , vol.13 , pp. 933-940
    • Takeuchi, O.1
  • 13
    • 0036644042 scopus 로고    scopus 로고
    • Cutting edge: Role of Toll-like receptor 1 in mediating immune response to microbial lipoproteins
    • Takeuchi, O. et al. Cutting edge: role of Toll-like receptor 1 in mediating immune response to microbial lipoproteins. J. Immunol. 169, 10-14 (2002).
    • (2002) J. Immunol. , vol.169 , pp. 10-14
    • Takeuchi, O.1
  • 14
    • 1542377424 scopus 로고    scopus 로고
    • A toll-like receptor that prevents infection by uropathogenic bacteria
    • Zhang, D. et al. A toll-like receptor that prevents infection by uropathogenic bacteria. Science 303, 1522-1526 (2004).
    • (2004) Science , vol.303 , pp. 1522-1526
    • Zhang, D.1
  • 15
    • 3142724031 scopus 로고    scopus 로고
    • Toll-like receptor signalling
    • Akira, S. & Takeda, K. Toll-like receptor signalling. Nat. Rev. Immunol. 4, 499-511 (2004).
    • (2004) Nat. Rev. Immunol. , vol.4 , pp. 499-511
    • Akira, S.1    Takeda, K.2
  • 16
    • 0032127279 scopus 로고    scopus 로고
    • Targeted disruption of the MyD88 gene results in loss of IL-1- and IL-18-mediated function
    • Adachi, O. et al. Targeted disruption of the MyD88 gene results in loss of IL-1- and IL-18-mediated function. Immunity 9, 143-150 (1998).
    • (1998) Immunity , vol.9 , pp. 143-150
    • Adachi, O.1
  • 17
    • 0035817925 scopus 로고    scopus 로고
    • Mal (MyD88-adapter-like) is required for Toll-like receptor-4 signal transduction
    • Fitzgerald, K.A. et al. Mal (MyD88-adapter-like) is required for Toll-like receptor-4 signal transduction. Nature 413, 78-83 (2001).
    • (2001) Nature , vol.413 , pp. 78-83
    • Fitzgerald, K.A.1
  • 18
    • 0042679529 scopus 로고    scopus 로고
    • Identification of Lps2 as a key transducer of MyD88-independent TIR signalling
    • Hoebe, K. et al. Identification of Lps2 as a key transducer of MyD88-independent TIR signalling. Nature 424, 743-748 (2003).
    • (2003) Nature , vol.424 , pp. 743-748
    • Hoebe, K.1
  • 19
    • 0035555301 scopus 로고    scopus 로고
    • TIRAP: An adapter molecule in the Toll signaling pathway
    • Horng, T., Barton, G.M. & Medzhitov, R. TIRAP: an adapter molecule in the Toll signaling pathway. Nat. Immunol. 2, 835-841 (2001).
    • (2001) Nat. Immunol. , vol.2 , pp. 835-841
    • Horng, T.1    Barton, G.M.2    Medzhitov, R.3
  • 20
    • 0037153130 scopus 로고    scopus 로고
    • The adaptor molecule TIRAP provides signalling specificity for Toll-like receptors
    • Horng, T., Barton, G.M., Flavell, R.A. & Medzhitov, R. The adaptor molecule TIRAP provides signalling specificity for Toll-like receptors. Nature 420, 329-333 (2002).
    • (2002) Nature , vol.420 , pp. 329-333
    • Horng, T.1    Barton, G.M.2    Flavell, R.A.3    Medzhitov, R.4
  • 21
    • 0033166472 scopus 로고    scopus 로고
    • Unresponsiveness of MyD88-deficient mice to endotoxin
    • Kawai, T., Adachi, O., Ogawa, T., Takeda, K. & Akira, S. Unresponsiveness of MyD88-deficient mice to endotoxin. Immunity 11, 115-122 (1999).
    • (1999) Immunity , vol.11 , pp. 115-122
    • Kawai, T.1    Adachi, O.2    Ogawa, T.3    Takeda, K.4    Akira, S.5
  • 22
    • 0035889228 scopus 로고    scopus 로고
    • Lipopolysaccharide stimulates the MyD88-independent pathway and results in activation of IFN-regulatory factor 3 and the expression of a subset of lipopolysaccharide-inducible genes
    • Kawai, T. et al. Lipopolysaccharide stimulates the MyD88-independent pathway and results in activation of IFN-regulatory factor 3 and the expression of a subset of lipopolysaccharide-inducible genes. J. Immunol. 167, 5887-5894 (2001).
    • (2001) J. Immunol. , vol.167 , pp. 5887-5894
    • Kawai, T.1
  • 23
    • 0037320451 scopus 로고    scopus 로고
    • TICAM-1, an adaptor molecule that participates in Toll-like receptor 3-mediated interferon-β induction
    • Oshiumi, H., Matsumoto, M., Funami, K., Akazawa, T. & Seya, T. TICAM-1, an adaptor molecule that participates in Toll-like receptor 3-mediated interferon-β induction. Nat. Immunol. 4, 161-167 (2003).
    • (2003) Nat. Immunol. , vol.4 , pp. 161-167
    • Oshiumi, H.1    Matsumoto, M.2    Funami, K.3    Akazawa, T.4    Seya, T.5
  • 24
    • 0037153191 scopus 로고    scopus 로고
    • Essential role for TIRAP in activation of the signalling cascade shared by TLR2 and TLR4
    • Yamamoto, M. et al. Essential role for TIRAP in activation of the signalling cascade shared by TLR2 and TLR4. Nature 420, 324-329 (2002).
    • (2002) Nature , vol.420 , pp. 324-329
    • Yamamoto, M.1
  • 25
    • 0043176281 scopus 로고    scopus 로고
    • Role of adaptor TRIF in the MyD88-independent toll-like receptor signaling pathway
    • Yamamoto, M. et al. Role of adaptor TRIF in the MyD88-independent toll-like receptor signaling pathway. Science 301, 640-643 (2003).
    • (2003) Science , vol.301 , pp. 640-643
    • Yamamoto, M.1
  • 26
    • 0242624622 scopus 로고    scopus 로고
    • TRAM is specifically involved in the Toll-like receptor 4-mediated MyD88-independent signaling pathway
    • Yamamoto, M. et al. TRAM is specifically involved in the Toll-like receptor 4-mediated MyD88-independent signaling pathway. Nat. Immunol. 4, 1144-1150 (2003).
    • (2003) Nat. Immunol. , vol.4 , pp. 1144-1150
    • Yamamoto, M.1
  • 27
    • 2342477917 scopus 로고    scopus 로고
    • The novel functions of ubiquitination in signaling
    • Sun, L. & Chen, Z.J. The novel functions of ubiquitination in signaling. Curr. Opin. Cell Biol. 16, 119-126 (2004).
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 119-126
    • Sun, L.1    Chen, Z.J.2
  • 28
    • 0034461577 scopus 로고    scopus 로고
    • Phosphorylation-induced dimerization of interferon regulatory factor 7 unmasks DNA binding and a bipartite transactivation domain
    • Marie, I., Smith, E., Prakash, A. & Levy, D.E. Phosphorylation- induced dimerization of interferon regulatory factor 7 unmasks DNA binding and a bipartite transactivation domain. Mol. Cell. Biol. 20, 8803-8814 (2000).
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 8803-8814
    • Marie, I.1    Smith, E.2    Prakash, A.3    Levy, D.E.4
  • 29
    • 0032481352 scopus 로고    scopus 로고
    • Direct triggering of the type I interferon system by virus infection: Activation of a transcription factor complex containing IRF-3 and CBP/p300
    • Yoneyama, M. et al. Direct triggering of the type I interferon system by virus infection: activation of a transcription factor complex containing IRF-3 and CBP/p300. EMBO J. 17, 1087-1095 (1998).
    • (1998) EMBO J. , vol.17 , pp. 1087-1095
    • Yoneyama, M.1
  • 30
    • 0038393016 scopus 로고    scopus 로고
    • IKKε and TBK1 are essential components of the IRF3 signaling pathway
    • Fitzgerald, K.A. et al. IKKε and TBK1 are essential components of the IRF3 signaling pathway. Nat. Immunol. 4, 491-496 (2003).
    • (2003) Nat. Immunol. , vol.4 , pp. 491-496
    • Fitzgerald, K.A.1
  • 31
    • 0038363463 scopus 로고    scopus 로고
    • Triggering the interferon antiviral response through an IKK-related pathway
    • Sharma, S. et al. Triggering the interferon antiviral response through an IKK-related pathway. Science 300, 1148-1151 (2003).
    • (2003) Science , vol.300 , pp. 1148-1151
    • Sharma, S.1
  • 32
    • 4344566281 scopus 로고    scopus 로고
    • The roles of two IκB Kinase-related kinases in lipopolysaccharide and double stranded RNA signaling and viral infection
    • Hemmi, H. et al. The roles of two IκB Kinase-related kinases in lipopolysaccharide and double stranded RNA signaling and viral infection. J. Exp. Med. 199, 1641-1650 (2004).
    • (2004) J. Exp. Med. , vol.199 , pp. 1641-1650
    • Hemmi, H.1
  • 33
    • 0345827590 scopus 로고    scopus 로고
    • IFN-regulatory factor 3-dependent gene expression is defective in Tbk1-deficient mouse embryonic fibroblasts
    • McWhirter, S.M. et al. IFN-regulatory factor 3-dependent gene expression is defective in Tbk1-deficient mouse embryonic fibroblasts. Proc. Natl. Acad. Sci. USA 101, 233-238 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 233-238
    • McWhirter, S.M.1
  • 34
    • 3042647375 scopus 로고    scopus 로고
    • Differential requirement for TANK-binding kinase-1 in type I interferon responses to Toll-like receptor activation and viral infection
    • Perry, A.K., Chow, E.K., Goodnougn, J.B., Yeh, W.C. & Cheng, G. Differential requirement for TANK-binding kinase-1 in type I interferon responses to Toll-like receptor activation and viral infection. J. Exp. Med. 199, 1651-1658 (2004).
    • (2004) J. Exp. Med. , vol.199 , pp. 1651-1658
    • Perry, A.K.1    Chow, E.K.2    Goodnougn, J.B.3    Yeh, W.C.4    Cheng, G.5
  • 35
    • 0034602156 scopus 로고    scopus 로고
    • Multiple regulatory domains control IRF-7 activity in response to virus infection
    • Lin, R., Mamane, Y. & Hiscott, J. Multiple regulatory domains control IRF-7 activity in response to virus infection. J. Biol. Chem. 275, 34320-34327 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 34320-34327
    • Lin, R.1    Mamane, Y.2    Hiscott, J.3
  • 36
    • 0033680737 scopus 로고    scopus 로고
    • Distinct and essential roles of transcription factors IRF-3 and IRF-7 in response to viruses for IFN-α/β gene induction
    • Sato, M. et al. Distinct and essential roles of transcription factors IRF-3 and IRF-7 in response to viruses for IFN-α/β gene induction. Immunity 13, 539-548 (2000).
    • (2000) Immunity , vol.13 , pp. 539-548
    • Sato, M.1
  • 37
    • 0037443644 scopus 로고    scopus 로고
    • The roles of Toll-like receptor 9, MyD88, and DNA-dependent protein kinase catalytic subunit in the effects of two distinct CpG DNAs on dendritic cell subsets
    • Hemmi, H., Kaisho, T., Takeda, K. & Akira, S. The roles of Toll-like receptor 9, MyD88, and DNA-dependent protein kinase catalytic subunit in the effects of two distinct CpG DNAs on dendritic cell subsets. J. Immunol. 170, 3059-3064 (2003).
    • (2003) J. Immunol. , vol.170 , pp. 3059-3064
    • Hemmi, H.1    Kaisho, T.2    Takeda, K.3    Akira, S.4
  • 38
    • 9144234252 scopus 로고    scopus 로고
    • Comparative analysis of IRF and IFN-α expression in human plasmacytoid and monocyte-derived dendritic cells
    • Izaguirre, A. et al. Comparative analysis of IRF and IFN-α expression in human plasmacytoid and monocyte-derived dendritic cells. J. Leukoc. Biol. 74, 1125-1138 (2003).
    • (2003) J. Leukoc. Biol. , vol.74 , pp. 1125-1138
    • Izaguirre, A.1
  • 39
    • 0037407691 scopus 로고    scopus 로고
    • Activation with CpG-A and CpG-B oligonucleotides reveals two distinct regulatory pathways of type I IFN synthesis in human plasmacytoid dendritic cells
    • Kerkmann, M. et al. Activation with CpG-A and CpG-B oligonucleotides reveals two distinct regulatory pathways of type I IFN synthesis in human plasmacytoid dendritic cells. J. Immunol. 170, 4465-4474 (2003).
    • (2003) J. Immunol. , vol.170 , pp. 4465-4474
    • Kerkmann, M.1
  • 40
    • 0034053445 scopus 로고    scopus 로고
    • Reconstitution of virus-mediated expression of interferon alpha genes in human fibroblast cells by ectopic interferon regulatory factor-7
    • Yeow, W.S. et al. Reconstitution of virus-mediated expression of interferon alpha genes in human fibroblast cells by ectopic interferon regulatory factor-7. J. Biol. Chem. 275, 6313-6320 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 6313-6320
    • Yeow, W.S.1
  • 41
    • 0035865054 scopus 로고    scopus 로고
    • Human peripheral blood cells differentially recognize and respond to two distinct CPG motifs
    • Verthelyi, D., Ishii, K.J., Gursel, M., Takeshita, F. & Klinman, D.M. Human peripheral blood cells differentially recognize and respond to two distinct CPG motifs. J. Immunol. 166, 2372-2377 (2001).
    • (2001) J. Immunol. , vol.166 , pp. 2372-2377
    • Verthelyi, D.1    Ishii, K.J.2    Gursel, M.3    Takeshita, F.4    Klinman, D.M.5
  • 42
    • 0034644474 scopus 로고    scopus 로고
    • Activation of the IκB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain
    • Deng, L. et al. Activation of the IκB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain. Cell 103, 351-361 (2000).
    • (2000) Cell , vol.103 , pp. 351-361
    • Deng, L.1
  • 43
    • 0036796384 scopus 로고    scopus 로고
    • Differential involvement of IFN-β in Toll-like receptor-stimulated dendritic cell activation
    • Hoshino, K., Kaisho, T., Iwabe, T., Takeuchi, O. & Akira, S. Differential involvement of IFN-β in Toll-like receptor-stimulated dendritic cell activation. Int. Immunol. 14, 1225-1231 (2002).
    • (2002) Int. Immunol. , vol.14 , pp. 1225-1231
    • Hoshino, K.1    Kaisho, T.2    Iwabe, T.3    Takeuchi, O.4    Akira, S.5
  • 44
    • 0141923690 scopus 로고    scopus 로고
    • Toll/IL-1 receptor domain-containing adaptor inducing IFN-β (TRIF) associates with TNF receptor-associated factor 6 and TANK-binding kinase 1, and activates two distinct transcription factors, NF-κB and IFN-regulatory factor-3, in the Toll-like receptor signaling
    • Sato, S. et al. Toll/IL-1 receptor domain-containing adaptor inducing IFN-β (TRIF) associates with TNF receptor-associated factor 6 and TANK-binding kinase 1, and activates two distinct transcription factors, NF-κB and IFN-regulatory factor-3, in the Toll-like receptor signaling. J. Immunol. 171, 4304-4310 (2003).
    • (2003) J. Immunol. , vol.171 , pp. 4304-4310
    • Sato, S.1
  • 45
    • 0037114185 scopus 로고    scopus 로고
    • Cutting edge: A novel Toll/IL-1 receptor domain-containing adapter that preferentially activates the IFN-β promoter in the Toll-like receptor signaling
    • Yamamoto, M. et al. Cutting edge: a novel Toll/IL-1 receptor domain-containing adapter that preferentially activates the IFN-β promoter in the Toll-like receptor signaling. J. Immunol. 169, 6668-6672 (2002).
    • (2002) J. Immunol. , vol.169 , pp. 6668-6672
    • Yamamoto, M.1
  • 46
    • 0035963331 scopus 로고    scopus 로고
    • Spatio-temporal images of growth-factor-induced activation of Ras and Rap1
    • Mochizuki, N. et al. Spatio-temporal images of growth-factor-induced activation of Ras and Rap1. Nature 411, 1065-1068 (2001).
    • (2001) Nature , vol.411 , pp. 1065-1068
    • Mochizuki, N.1
  • 47
    • 0036724188 scopus 로고    scopus 로고
    • Activation of rac and cdc42 video imaged by fluorescent resonance energy transfer-based single-molecule probes in the membrane of living cells
    • Itoh, R.E. et al. Activation of rac and cdc42 video imaged by fluorescent resonance energy transfer-based single-molecule probes in the membrane of living cells. Mol. Cell. Biol. 22, 6582-6591 (2002).
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 6582-6591
    • Itoh, R.E.1
  • 48
    • 0031201023 scopus 로고    scopus 로고
    • -/- mice: Role for IFN-γ in activating apoptosis of hepatocytes
    • -/- mice: role for IFN-γ in activating apoptosis of hepatocytes. J. Immunol. 159, 1418-1428 (1997).
    • (1997) J. Immunol. , vol.159 , pp. 1418-1428
    • Tagawa, Y.1    Sekikawa, K.2    Iwakura, Y.3
  • 49
    • 0034597554 scopus 로고    scopus 로고
    • Interaction of EGF receptor and grb2 in living cells visualized by fluorescence resonance energy transfer (FRET) microscopy
    • Sorkin, A., McClure, M., Huang, F. & Carter, R. Interaction of EGF receptor and grb2 in living cells visualized by fluorescence resonance energy transfer (FRET) microscopy. Curr. Biol. 10, 1395-1398 (2000).
    • (2000) Curr. Biol. , vol.10 , pp. 1395-1398
    • Sorkin, A.1    McClure, M.2    Huang, F.3    Carter, R.4
  • 50
    • 0345826149 scopus 로고    scopus 로고
    • Bcl10 activates the NF-κB pathway through ubiquitination of NEMO
    • Zhou, H. et al. Bcl10 activates the NF-κB pathway through ubiquitination of NEMO. Nature 427, 167-171 (2004).
    • (2004) Nature , vol.427 , pp. 167-171
    • Zhou, H.1


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