메뉴 건너뛰기




Volumn 33, Issue 9, 2012, Pages 449-458

Dissecting negative regulation of Toll-like receptor signaling

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; DAMAGE ASSOCIATED MOLECULAR PATTERN; I KAPPA B KINASE ALPHA; I KAPPA B KINASE BETA; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERFERON REGULATORY FACTOR 3; LIGAND; MITOGEN ACTIVATED PROTEIN KINASE; MYELOID DIFFERENTIATION FACTOR 88; NUCLEOTIDE BINDING OLIGOMERIZATION DOMAIN LIKE RECEPTOR; PATHOGEN ASSOCIATED MOLECULAR PATTERN; PATTERN RECOGNITION RECEPTOR; RETINOIC ACID INDUCIBLE PROTEIN I; SIGNAL PEPTIDE; TIR ASSOCIATED PROTEIN; TIR DOMAIN CONTAINING ADAPTOR PROTEIN-INDUCING BETA INTERFERON; TOLL LIKE RECEPTOR; TOLL LIKE RECEPTOR 1; TOLL LIKE RECEPTOR 10; TOLL LIKE RECEPTOR 11; TOLL LIKE RECEPTOR 2; TOLL LIKE RECEPTOR 3; TOLL LIKE RECEPTOR 4; TOLL LIKE RECEPTOR 5; TOLL LIKE RECEPTOR 6; TOLL LIKE RECEPTOR 7; TOLL LIKE RECEPTOR 8; TOLL LIKE RECEPTOR 9; TOLL LIKE RECEPTOR ADAPTOR MOLECULE 2; TRAF FAMILYMEMBER IMMUNOGLOBULIN ENHANCER BINDING PROTEIN ACTIVATOR BINDING KINASE 1; UNCLASSIFIED DRUG;

EID: 84865298775     PISSN: 14714906     EISSN: 14714981     Source Type: Journal    
DOI: 10.1016/j.it.2012.05.002     Document Type: Review
Times cited : (358)

References (97)
  • 2
    • 32944464648 scopus 로고    scopus 로고
    • Pathogen recognition and innate immunity
    • Akira S., et al. Pathogen recognition and innate immunity. Cell 2006, 124:783-801.
    • (2006) Cell , vol.124 , pp. 783-801
    • Akira, S.1
  • 3
    • 77951260924 scopus 로고    scopus 로고
    • The role of pattern-recognition receptors in innate immunity: update on Toll-like receptors
    • Kawai T., Akira S. The role of pattern-recognition receptors in innate immunity: update on Toll-like receptors. Nat. Immunol. 2010, 11:373-384.
    • (2010) Nat. Immunol. , vol.11 , pp. 373-384
    • Kawai, T.1    Akira, S.2
  • 4
    • 78649526394 scopus 로고    scopus 로고
    • Sterile inflammation: sensing and reacting to damage
    • Chen G.Y., Nunez G. Sterile inflammation: sensing and reacting to damage. Nat. Rev. Immunol. 2010, 10:826-837.
    • (2010) Nat. Rev. Immunol. , vol.10 , pp. 826-837
    • Chen, G.Y.1    Nunez, G.2
  • 5
    • 20644450804 scopus 로고    scopus 로고
    • Negative regulation of toll-like receptor-mediated immune responses
    • Liew F.Y., et al. Negative regulation of toll-like receptor-mediated immune responses. Nat. Rev. Immunol. 2005, 5:446-458.
    • (2005) Nat. Rev. Immunol. , vol.5 , pp. 446-458
    • Liew, F.Y.1
  • 6
    • 67349092199 scopus 로고    scopus 로고
    • TAG, a splice variant of the adaptor TRAM, negatively regulates the adaptor MyD88-independent TLR4 pathway
    • Palsson-McDermott E.M., et al. TAG, a splice variant of the adaptor TRAM, negatively regulates the adaptor MyD88-independent TLR4 pathway. Nat. Immunol. 2009, 10:579-586.
    • (2009) Nat. Immunol. , vol.10 , pp. 579-586
    • Palsson-McDermott, E.M.1
  • 7
    • 34247566510 scopus 로고    scopus 로고
    • The family of five: TIR-domain-containing adaptors in Toll-like receptor signalling
    • O'Neill L.A., Bowie A.G. The family of five: TIR-domain-containing adaptors in Toll-like receptor signalling. Nat. Rev. Immunol. 2007, 7:353-364.
    • (2007) Nat. Rev. Immunol. , vol.7 , pp. 353-364
    • O'Neill, L.A.1    Bowie, A.G.2
  • 8
    • 33748871187 scopus 로고    scopus 로고
    • The human adaptor SARM negatively regulates adaptor protein TRIF-dependent Toll-like receptor signaling
    • Carty M., et al. The human adaptor SARM negatively regulates adaptor protein TRIF-dependent Toll-like receptor signaling. Nat. Immunol. 2006, 7:1074-1081.
    • (2006) Nat. Immunol. , vol.7 , pp. 1074-1081
    • Carty, M.1
  • 9
    • 15044345461 scopus 로고    scopus 로고
    • Integral role of IRF-5 in the gene induction programme activated by Toll-like receptors
    • Takaoka A., et al. Integral role of IRF-5 in the gene induction programme activated by Toll-like receptors. Nature 2005, 434:243-249.
    • (2005) Nature , vol.434 , pp. 243-249
    • Takaoka, A.1
  • 10
    • 27644548945 scopus 로고    scopus 로고
    • Negative regulation of Toll-like-receptor signaling by IRF-4
    • Negishi H., et al. Negative regulation of Toll-like-receptor signaling by IRF-4. Proc. Natl. Acad. Sci. U.S.A. 2005, 102:15989-15994.
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 15989-15994
    • Negishi, H.1
  • 11
    • 42949098526 scopus 로고    scopus 로고
    • TIPE2, a negative regulator of innate and adaptive immunity that maintains immune homeostasis
    • Sun H., et al. TIPE2, a negative regulator of innate and adaptive immunity that maintains immune homeostasis. Cell 2008, 133:415-426.
    • (2008) Cell , vol.133 , pp. 415-426
    • Sun, H.1
  • 12
    • 18544383460 scopus 로고    scopus 로고
    • Pleiotropic defects in lymphocyte activation caused by caspase-8 mutations lead to human immunodeficiency
    • Chun H.J., et al. Pleiotropic defects in lymphocyte activation caused by caspase-8 mutations lead to human immunodeficiency. Nature 2002, 419:395-399.
    • (2002) Nature , vol.419 , pp. 395-399
    • Chun, H.J.1
  • 13
    • 34147165459 scopus 로고    scopus 로고
    • Essential role for caspase-8 in Toll-like receptors and NFkappaB signaling
    • Lemmers B., et al. Essential role for caspase-8 in Toll-like receptors and NFkappaB signaling. J. Biol. Chem. 2007, 282:7416-7423.
    • (2007) J. Biol. Chem. , vol.282 , pp. 7416-7423
    • Lemmers, B.1
  • 14
    • 79953046719 scopus 로고    scopus 로고
    • The inflammasome NLRs in immunity, inflammation, and associated diseases
    • Davis B.K., et al. The inflammasome NLRs in immunity, inflammation, and associated diseases. Annu. Rev. Immunol. 2011, 29:707-735.
    • (2011) Annu. Rev. Immunol. , vol.29 , pp. 707-735
    • Davis, B.K.1
  • 15
    • 79959329537 scopus 로고    scopus 로고
    • NLRX1 negatively regulates TLR-induced NF-kappaB signaling by targeting TRAF6 and IKK
    • Xia X., et al. NLRX1 negatively regulates TLR-induced NF-kappaB signaling by targeting TRAF6 and IKK. Immunity 2011, 34:843-853.
    • (2011) Immunity , vol.34 , pp. 843-853
    • Xia, X.1
  • 16
    • 79960205819 scopus 로고    scopus 로고
    • NLRX1/NOD5 deficiency does not affect MAVS signalling
    • Rebsamen M., et al. NLRX1/NOD5 deficiency does not affect MAVS signalling. Cell Death Differ. 2011, 18:1387.
    • (2011) Cell Death Differ. , vol.18 , pp. 1387
    • Rebsamen, M.1
  • 17
    • 77951902675 scopus 로고    scopus 로고
    • NLRC5 negatively regulates the NF-kappaB and type I interferon signaling pathways
    • Cui J., et al. NLRC5 negatively regulates the NF-kappaB and type I interferon signaling pathways. Cell 2010, 141:483-496.
    • (2010) Cell , vol.141 , pp. 483-496
    • Cui, J.1
  • 18
    • 78751495854 scopus 로고    scopus 로고
    • NLRC5 deficiency does not influence cytokine induction by virus and bacteria infections
    • Kumar H., et al. NLRC5 deficiency does not influence cytokine induction by virus and bacteria infections. J. Immunol. 2010, 186:994-1000.
    • (2010) J. Immunol. , vol.186 , pp. 994-1000
    • Kumar, H.1
  • 19
    • 69049086481 scopus 로고    scopus 로고
    • TANK is a negative regulator of Toll-like receptor signaling and is critical for the prevention of autoimmune nephritis
    • Kawagoe T., et al. TANK is a negative regulator of Toll-like receptor signaling and is critical for the prevention of autoimmune nephritis. Nat. Immunol. 2009, 10:965-972.
    • (2009) Nat. Immunol. , vol.10 , pp. 965-972
    • Kawagoe, T.1
  • 20
    • 80052020185 scopus 로고    scopus 로고
    • The orphan nuclear receptor SHP acts as a negative regulator in inflammatory signaling triggered by Toll-like receptors
    • Yuk J.M., et al. The orphan nuclear receptor SHP acts as a negative regulator in inflammatory signaling triggered by Toll-like receptors. Nat. Immunol. 2011, 12:742-751.
    • (2011) Nat. Immunol. , vol.12 , pp. 742-751
    • Yuk, J.M.1
  • 21
    • 50049086910 scopus 로고    scopus 로고
    • The kinases MSK1 and MSK2 act as negative regulators of Toll-like receptor signaling
    • Ananieva O., et al. The kinases MSK1 and MSK2 act as negative regulators of Toll-like receptor signaling. Nat. Immunol. 2008, 9:1028-1036.
    • (2008) Nat. Immunol. , vol.9 , pp. 1028-1036
    • Ananieva, O.1
  • 22
    • 84856301921 scopus 로고    scopus 로고
    • TAK1 negatively regulates NF-kappaB and p38 MAP kinase activation in Gr-1(+)CD11b(+) neutrophils
    • Ajibade A.A., et al. TAK1 negatively regulates NF-kappaB and p38 MAP kinase activation in Gr-1(+)CD11b(+) neutrophils. Immunity 2012, 36:43-54.
    • (2012) Immunity , vol.36 , pp. 43-54
    • Ajibade, A.A.1
  • 23
    • 42449121356 scopus 로고    scopus 로고
    • Phosphatase SHP-1 promotes TLR- and RIG-I-activated production of type I interferon by inhibiting the kinase IRAK1
    • An H., et al. Phosphatase SHP-1 promotes TLR- and RIG-I-activated production of type I interferon by inhibiting the kinase IRAK1. Nat. Immunol. 2008, 9:542-550.
    • (2008) Nat. Immunol. , vol.9 , pp. 542-550
    • An, H.1
  • 24
    • 65549154373 scopus 로고    scopus 로고
    • Leishmania-induced IRAK-1 inactivation is mediated by SHP-1 interacting with an evolutionarily conserved KTIM motif
    • Abu-Dayyeh I., et al. Leishmania-induced IRAK-1 inactivation is mediated by SHP-1 interacting with an evolutionarily conserved KTIM motif. PLoS Negl. Trop. Dis. 2008, 2:e305.
    • (2008) PLoS Negl. Trop. Dis. , vol.2
    • Abu-Dayyeh, I.1
  • 25
    • 33845438110 scopus 로고    scopus 로고
    • SHP-2 phosphatase negatively regulates the TRIF adaptor protein-dependent type I interferon and proinflammatory cytokine production
    • An H., et al. SHP-2 phosphatase negatively regulates the TRIF adaptor protein-dependent type I interferon and proinflammatory cytokine production. Immunity 2006, 25:919-928.
    • (2006) Immunity , vol.25 , pp. 919-928
    • An, H.1
  • 26
    • 39549107115 scopus 로고    scopus 로고
    • Homeostatic MyD88-dependent signals cause lethal inflammation in the absence of A20
    • Turer E.E., et al. Homeostatic MyD88-dependent signals cause lethal inflammation in the absence of A20. J. Exp. Med. 2008, 205:451-464.
    • (2008) J. Exp. Med. , vol.205 , pp. 451-464
    • Turer, E.E.1
  • 27
    • 81355150892 scopus 로고    scopus 로고
    • Direct, noncatalytic mechanism of IKK inhibition by A20
    • Skaug B., et al. Direct, noncatalytic mechanism of IKK inhibition by A20. Mol. Cell 2011, 44:559-571.
    • (2011) Mol. Cell , vol.44 , pp. 559-571
    • Skaug, B.1
  • 28
    • 28844460239 scopus 로고    scopus 로고
    • The tumor suppressor cylindromatosis (CYLD) acts as a negative regulator for toll-like receptor 2 signaling via negative cross-talk with TRAF6 AND TRAF7
    • Yoshida H., et al. The tumor suppressor cylindromatosis (CYLD) acts as a negative regulator for toll-like receptor 2 signaling via negative cross-talk with TRAF6 AND TRAF7. J. Biol. Chem. 2005, 280:41111-41121.
    • (2005) J. Biol. Chem. , vol.280 , pp. 41111-41121
    • Yoshida, H.1
  • 29
    • 84859507872 scopus 로고    scopus 로고
    • Ubiquitin-specific protease 4 mitigates Toll-like/interleukin-1 receptor signaling and regulates innate immune activation
    • Zhou F., et al. Ubiquitin-specific protease 4 mitigates Toll-like/interleukin-1 receptor signaling and regulates innate immune activation. J. Biol. Chem. 2012, 287:11002-11010.
    • (2012) J. Biol. Chem. , vol.287 , pp. 11002-11010
    • Zhou, F.1
  • 30
    • 36448943427 scopus 로고    scopus 로고
    • DUBA: a deubiquitinase that regulates type I interferon production
    • Kayagaki N., et al. DUBA: a deubiquitinase that regulates type I interferon production. Science 2007, 318:1628-1632.
    • (2007) Science , vol.318 , pp. 1628-1632
    • Kayagaki, N.1
  • 31
    • 84655176306 scopus 로고    scopus 로고
    • The role of ubiquitylation in immune defence and pathogen evasion
    • Jiang X., Chen Z.J. The role of ubiquitylation in immune defence and pathogen evasion. Nat. Rev. Immunol. 2011, 12:35-48.
    • (2011) Nat. Rev. Immunol. , vol.12 , pp. 35-48
    • Jiang, X.1    Chen, Z.J.2
  • 32
    • 34249660614 scopus 로고    scopus 로고
    • SOCS proteins, cytokine signalling and immune regulation
    • Yoshimura A., et al. SOCS proteins, cytokine signalling and immune regulation. Nat. Rev. Immunol. 2007, 7:454-465.
    • (2007) Nat. Rev. Immunol. , vol.7 , pp. 454-465
    • Yoshimura, A.1
  • 33
    • 62849123774 scopus 로고    scopus 로고
    • Cross-regulation of signaling by ITAM-associated receptors
    • Ivashkiv L.B. Cross-regulation of signaling by ITAM-associated receptors. Nat. Immunol. 2009, 10:340-347.
    • (2009) Nat. Immunol. , vol.10 , pp. 340-347
    • Ivashkiv, L.B.1
  • 34
    • 77951892594 scopus 로고    scopus 로고
    • Indirect inhibition of Toll-like receptor and type I interferon responses by ITAM-coupled receptors and integrins
    • Wang L., et al. Indirect inhibition of Toll-like receptor and type I interferon responses by ITAM-coupled receptors and integrins. Immunity 2010, 32:518-530.
    • (2010) Immunity , vol.32 , pp. 518-530
    • Wang, L.1
  • 35
    • 77954946392 scopus 로고    scopus 로고
    • Integrin CD11b negatively regulates TLR-triggered inflammatory responses by activating Syk and promoting degradation of MyD88 and TRIF via Cbl-b
    • Han C., et al. Integrin CD11b negatively regulates TLR-triggered inflammatory responses by activating Syk and promoting degradation of MyD88 and TRIF via Cbl-b. Nat. Immunol. 2010, 11:734-742.
    • (2010) Nat. Immunol. , vol.11 , pp. 734-742
    • Han, C.1
  • 36
    • 33646908228 scopus 로고    scopus 로고
    • Phosphoinositide-mediated adaptor recruitment controls Toll-like receptor signaling
    • Kagan J.C., Medzhitov R. Phosphoinositide-mediated adaptor recruitment controls Toll-like receptor signaling. Cell 2006, 125:943-955.
    • (2006) Cell , vol.125 , pp. 943-955
    • Kagan, J.C.1    Medzhitov, R.2
  • 37
    • 34249066486 scopus 로고    scopus 로고
    • PDLIM2-mediated termination of transcription factor NF-kappaB activation by intranuclear sequestration and degradation of the p65 subunit
    • Tanaka T., et al. PDLIM2-mediated termination of transcription factor NF-kappaB activation by intranuclear sequestration and degradation of the p65 subunit. Nat. Immunol. 2007, 8:584-591.
    • (2007) Nat. Immunol. , vol.8 , pp. 584-591
    • Tanaka, T.1
  • 38
    • 40949163764 scopus 로고    scopus 로고
    • TRIM30 alpha negatively regulates TLR-mediated NF-kappa B activation by targeting TAB2 and TAB3 for degradation
    • Shi M., et al. TRIM30 alpha negatively regulates TLR-mediated NF-kappa B activation by targeting TAB2 and TAB3 for degradation. Nat. Immunol. 2008, 9:369-377.
    • (2008) Nat. Immunol. , vol.9 , pp. 369-377
    • Shi, M.1
  • 39
    • 84863229333 scopus 로고    scopus 로고
    • E3 ubiquitin ligase tripartite motif 38 negatively regulates TLR-mediated immune responses by proteasomal degradation of TNF receptor-associated factor 6 in macrophages
    • Zhao W., et al. E3 ubiquitin ligase tripartite motif 38 negatively regulates TLR-mediated immune responses by proteasomal degradation of TNF receptor-associated factor 6 in macrophages. J. Immunol. 2012, 188:2567-2574.
    • (2012) J. Immunol. , vol.188 , pp. 2567-2574
    • Zhao, W.1
  • 40
    • 33744499683 scopus 로고    scopus 로고
    • Negative regulation of interferon-regulatory factor 3-dependent innate antiviral response by the prolyl isomerase Pin1
    • Saitoh T., et al. Negative regulation of interferon-regulatory factor 3-dependent innate antiviral response by the prolyl isomerase Pin1. Nat. Immunol. 2006, 7:598-605.
    • (2006) Nat. Immunol. , vol.7 , pp. 598-605
    • Saitoh, T.1
  • 41
    • 80052026067 scopus 로고    scopus 로고
    • Essential role for the prolyl isomerase Pin1 in Toll-like receptor signaling and type I interferon-mediated immunity
    • Tun-Kyi A., et al. Essential role for the prolyl isomerase Pin1 in Toll-like receptor signaling and type I interferon-mediated immunity. Nat. Immunol. 2011, 12:733-741.
    • (2011) Nat. Immunol. , vol.12 , pp. 733-741
    • Tun-Kyi, A.1
  • 42
    • 78650130030 scopus 로고    scopus 로고
    • The ubiquitin E3 ligase RAUL negatively regulates type i interferon through ubiquitination of the transcription factors IRF7 and IRF3
    • Yu Y., Hayward G.S. The ubiquitin E3 ligase RAUL negatively regulates type i interferon through ubiquitination of the transcription factors IRF7 and IRF3. Immunity 2010, 33:863-877.
    • (2010) Immunity , vol.33 , pp. 863-877
    • Yu, Y.1    Hayward, G.S.2
  • 43
    • 78751672975 scopus 로고    scopus 로고
    • Autophagy in immunity and inflammation
    • Levine B., et al. Autophagy in immunity and inflammation. Nature 2011, 469:323-335.
    • (2011) Nature , vol.469 , pp. 323-335
    • Levine, B.1
  • 44
    • 56249090667 scopus 로고    scopus 로고
    • Loss of the autophagy protein Atg16L1 enhances endotoxin-induced IL-1beta production
    • Saitoh T., et al. Loss of the autophagy protein Atg16L1 enhances endotoxin-induced IL-1beta production. Nature 2008, 456:264-268.
    • (2008) Nature , vol.456 , pp. 264-268
    • Saitoh, T.1
  • 45
    • 56249135538 scopus 로고    scopus 로고
    • A key role for autophagy and the autophagy gene Atg16l1 in mouse and human intestinal Paneth cells
    • Cadwell K., et al. A key role for autophagy and the autophagy gene Atg16l1 in mouse and human intestinal Paneth cells. Nature 2008, 456:259-263.
    • (2008) Nature , vol.456 , pp. 259-263
    • Cadwell, K.1
  • 46
    • 32044439558 scopus 로고    scopus 로고
    • Selective and antagonistic functions of SWI/SNF and Mi-2beta nucleosome remodeling complexes during an inflammatory response
    • Ramirez-Carrozzi V.R., et al. Selective and antagonistic functions of SWI/SNF and Mi-2beta nucleosome remodeling complexes during an inflammatory response. Genes Dev. 2006, 20:282-296.
    • (2006) Genes Dev. , vol.20 , pp. 282-296
    • Ramirez-Carrozzi, V.R.1
  • 47
    • 35748973890 scopus 로고    scopus 로고
    • Negative regulation of TLR-signaling pathways by activating transcription factor-3
    • Whitmore M.M., et al. Negative regulation of TLR-signaling pathways by activating transcription factor-3. J. Immunol. 2007, 179:3622-3630.
    • (2007) J. Immunol. , vol.179 , pp. 3622-3630
    • Whitmore, M.M.1
  • 48
    • 30444456370 scopus 로고    scopus 로고
    • IkappaBNS inhibits induction of a subset of Toll-like receptor-dependent genes and limits inflammation
    • Kuwata H., et al. IkappaBNS inhibits induction of a subset of Toll-like receptor-dependent genes and limits inflammation. Immunity 2006, 24:41-51.
    • (2006) Immunity , vol.24 , pp. 41-51
    • Kuwata, H.1
  • 49
    • 34547815755 scopus 로고    scopus 로고
    • Negative regulation of toll-like receptor signaling by NF-kappaB p50 ubiquitination blockade
    • Carmody R.J., et al. Negative regulation of toll-like receptor signaling by NF-kappaB p50 ubiquitination blockade. Science 2007, 317:675-678.
    • (2007) Science , vol.317 , pp. 675-678
    • Carmody, R.J.1
  • 50
    • 63049083734 scopus 로고    scopus 로고
    • A Nurr1/CoREST pathway in microglia and astrocytes protects dopaminergic neurons from inflammation-induced death
    • Saijo K., et al. A Nurr1/CoREST pathway in microglia and astrocytes protects dopaminergic neurons from inflammation-induced death. Cell 2009, 137:47-59.
    • (2009) Cell , vol.137 , pp. 47-59
    • Saijo, K.1
  • 51
    • 68949172534 scopus 로고    scopus 로고
    • The aryl hydrocarbon receptor in immunity
    • Esser C., et al. The aryl hydrocarbon receptor in immunity. Trends Immunol. 2009, 30:447-454.
    • (2009) Trends Immunol. , vol.30 , pp. 447-454
    • Esser, C.1
  • 52
    • 69549126213 scopus 로고    scopus 로고
    • Aryl hydrocarbon receptor in combination with Stat1 regulates LPS-induced inflammatory responses
    • Kimura A., et al. Aryl hydrocarbon receptor in combination with Stat1 regulates LPS-induced inflammatory responses. J. Exp. Med. 2009, 206:2027-2035.
    • (2009) J. Exp. Med. , vol.206 , pp. 2027-2035
    • Kimura, A.1
  • 53
    • 8544255551 scopus 로고    scopus 로고
    • The tandem CCCH zinc finger protein tristetraprolin and its relevance to cytokine mRNA turnover and arthritis
    • Carrick D.M., et al. The tandem CCCH zinc finger protein tristetraprolin and its relevance to cytokine mRNA turnover and arthritis. Arthritis Res. Ther. 2004, 6:248-264.
    • (2004) Arthritis Res. Ther. , vol.6 , pp. 248-264
    • Carrick, D.M.1
  • 54
    • 67349167059 scopus 로고    scopus 로고
    • Zc3h12a is an RNase essential for controlling immune responses by regulating mRNA decay
    • Matsushita K., et al. Zc3h12a is an RNase essential for controlling immune responses by regulating mRNA decay. Nature 2009, 458:1185-1190.
    • (2009) Nature , vol.458 , pp. 1185-1190
    • Matsushita, K.1
  • 55
    • 78650371990 scopus 로고    scopus 로고
    • MCP-induced protein 1 deubiquitinates TRAF proteins and negatively regulates JNK and NF-kappaB signaling
    • Liang J., et al. MCP-induced protein 1 deubiquitinates TRAF proteins and negatively regulates JNK and NF-kappaB signaling. J. Exp. Med. 2010, 207:2959-2973.
    • (2010) J. Exp. Med. , vol.207 , pp. 2959-2973
    • Liang, J.1
  • 56
    • 81255154489 scopus 로고    scopus 로고
    • The IkappaB kinase complex regulates the stability of cytokine-encoding mRNA induced by TLR-IL-1R by controlling degradation of regnase-1
    • Iwasaki H., et al. The IkappaB kinase complex regulates the stability of cytokine-encoding mRNA induced by TLR-IL-1R by controlling degradation of regnase-1. Nat. Immunol. 2011, 12:1167-1175.
    • (2011) Nat. Immunol. , vol.12 , pp. 1167-1175
    • Iwasaki, H.1
  • 57
    • 79952186298 scopus 로고    scopus 로고
    • MicroRNAs: the fine-tuners of Toll-like receptor signalling
    • O'Neill L.A., et al. MicroRNAs: the fine-tuners of Toll-like receptor signalling. Nat. Rev. Immunol. 2011, 11:163-175.
    • (2011) Nat. Rev. Immunol. , vol.11 , pp. 163-175
    • O'Neill, L.A.1
  • 58
    • 33846845071 scopus 로고    scopus 로고
    • MicroRNA-155 is induced during the macrophage inflammatory response
    • O'Connell R.M., et al. MicroRNA-155 is induced during the macrophage inflammatory response. Proc. Natl. Acad. Sci. U.S.A. 2007, 104:1604-1609.
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 1604-1609
    • O'Connell, R.M.1
  • 59
    • 78651517001 scopus 로고    scopus 로고
    • MicroRNA-155 silencing enhances inflammatory response and lipid uptake in oxidized low-density lipoprotein-stimulated human THP-1 macrophages
    • Huang R.S., et al. MicroRNA-155 silencing enhances inflammatory response and lipid uptake in oxidized low-density lipoprotein-stimulated human THP-1 macrophages. J. Investig. Med. 2010, 58:961-967.
    • (2010) J. Investig. Med. , vol.58 , pp. 961-967
    • Huang, R.S.1
  • 60
    • 77951294330 scopus 로고    scopus 로고
    • Identification of MyD88 as a novel target of miR-155, involved in negative regulation of Helicobacter pylori-induced inflammation
    • Tang B., et al. Identification of MyD88 as a novel target of miR-155, involved in negative regulation of Helicobacter pylori-induced inflammation. FEBS Lett. 2010, 584:1481-1486.
    • (2010) FEBS Lett. , vol.584 , pp. 1481-1486
    • Tang, B.1
  • 61
    • 62449173209 scopus 로고    scopus 로고
    • MicroRNA-155 modulates the interleukin-1 signaling pathway in activated human monocyte-derived dendritic cells
    • Ceppi M., et al. MicroRNA-155 modulates the interleukin-1 signaling pathway in activated human monocyte-derived dendritic cells. Proc. Natl. Acad. Sci. U.S.A. 2009, 106:2735-2740.
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 2735-2740
    • Ceppi, M.1
  • 62
    • 38049030287 scopus 로고    scopus 로고
    • Modulation of miR-155 and miR-125b levels following lipopolysaccharide/TNF-alpha stimulation and their possible roles in regulating the response to endotoxin shock
    • Tili E., et al. Modulation of miR-155 and miR-125b levels following lipopolysaccharide/TNF-alpha stimulation and their possible roles in regulating the response to endotoxin shock. J. Immunol. 2007, 179:5082-5089.
    • (2007) J. Immunol. , vol.179 , pp. 5082-5089
    • Tili, E.1
  • 63
    • 37249092180 scopus 로고    scopus 로고
    • A viral microRNA functions as an orthologue of cellular miR-155
    • Gottwein E., et al. A viral microRNA functions as an orthologue of cellular miR-155. Nature 2007, 450:1096-1099.
    • (2007) Nature , vol.450 , pp. 1096-1099
    • Gottwein, E.1
  • 64
    • 34247594818 scopus 로고    scopus 로고
    • Regulation of the germinal center response by microRNA-155
    • Thai T.H., et al. Regulation of the germinal center response by microRNA-155. Science 2007, 316:604-608.
    • (2007) Science , vol.316 , pp. 604-608
    • Thai, T.H.1
  • 65
    • 34247584465 scopus 로고    scopus 로고
    • Requirement of bic/microRNA-155 for normal immune function
    • Rodriguez A., et al. Requirement of bic/microRNA-155 for normal immune function. Science 2007, 316:608-611.
    • (2007) Science , vol.316 , pp. 608-611
    • Rodriguez, A.1
  • 66
    • 66349137358 scopus 로고    scopus 로고
    • Inositol phosphatase SHIP1 is a primary target of miR-155
    • O'Connell R.M., et al. Inositol phosphatase SHIP1 is a primary target of miR-155. Proc. Natl. Acad. Sci. U.S.A. 2009, 106:7113-7118.
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 7113-7118
    • O'Connell, R.M.1
  • 67
    • 33747608638 scopus 로고    scopus 로고
    • NF-kappaB-dependent induction of microRNA miR-146, an inhibitor targeted to signaling proteins of innate immune responses
    • Taganov K.D., et al. NF-kappaB-dependent induction of microRNA miR-146, an inhibitor targeted to signaling proteins of innate immune responses. Proc. Natl. Acad. Sci. U.S.A. 2006, 103:12481-12486.
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 12481-12486
    • Taganov, K.D.1
  • 68
    • 79959362128 scopus 로고    scopus 로고
    • NF-kappaB dysregulation in microRNA-146a-deficient mice drives the development of myeloid malignancies
    • Zhao J.L., et al. NF-kappaB dysregulation in microRNA-146a-deficient mice drives the development of myeloid malignancies. Proc. Natl. Acad. Sci. U.S.A. 2011, 108:9184-9189.
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 9184-9189
    • Zhao, J.L.1
  • 69
    • 77958105934 scopus 로고    scopus 로고
    • MiR-146a mediates protective innate immune tolerance in the neonate intestine
    • Chassin C., et al. miR-146a mediates protective innate immune tolerance in the neonate intestine. Cell Host Microbe 2010, 8:358-368.
    • (2010) Cell Host Microbe , vol.8 , pp. 358-368
    • Chassin, C.1
  • 70
    • 75649113377 scopus 로고    scopus 로고
    • Negative regulation of TLR4 via targeting of the proinflammatory tumor suppressor PDCD4 by the microRNA miR-21
    • Sheedy F.J., et al. Negative regulation of TLR4 via targeting of the proinflammatory tumor suppressor PDCD4 by the microRNA miR-21. Nat. Immunol. 2010, 11:141-147.
    • (2010) Nat. Immunol. , vol.11 , pp. 141-147
    • Sheedy, F.J.1
  • 71
    • 56749133272 scopus 로고    scopus 로고
    • Viral evasion and subversion of pattern-recognition receptor signalling
    • Bowie A.G., Unterholzner L. Viral evasion and subversion of pattern-recognition receptor signalling. Nat. Rev. Immunol. 2008, 8:911-922.
    • (2008) Nat. Rev. Immunol. , vol.8 , pp. 911-922
    • Bowie, A.G.1    Unterholzner, L.2
  • 72
    • 29144462494 scopus 로고    scopus 로고
    • Hepatitis C virus protease NS3/4A cleaves mitochondrial antiviral signaling protein off the mitochondria to evade innate immunity
    • Li X.D., et al. Hepatitis C virus protease NS3/4A cleaves mitochondrial antiviral signaling protein off the mitochondria to evade innate immunity. Proc. Natl. Acad. Sci. U.S.A. 2005, 102:17717-17722.
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 17717-17722
    • Li, X.D.1
  • 73
    • 17144366260 scopus 로고    scopus 로고
    • Vaccinia virus protein A46R targets multiple Toll-like-interleukin-1 receptor adaptors and contributes to virulence
    • Stack J., et al. Vaccinia virus protein A46R targets multiple Toll-like-interleukin-1 receptor adaptors and contributes to virulence. J. Exp. Med. 2005, 201:1007-1018.
    • (2005) J. Exp. Med. , vol.201 , pp. 1007-1018
    • Stack, J.1
  • 74
    • 0037415598 scopus 로고    scopus 로고
    • The poxvirus protein A52R targets Toll-like receptor signaling complexes to suppress host defense
    • Harte M.T., et al. The poxvirus protein A52R targets Toll-like receptor signaling complexes to suppress host defense. J. Exp. Med. 2003, 197:343-351.
    • (2003) J. Exp. Med. , vol.197 , pp. 343-351
    • Harte, M.T.1
  • 75
    • 65449183853 scopus 로고    scopus 로고
    • Viral avoidance and exploitation of the ubiquitin system
    • Randow F., Lehner P.J. Viral avoidance and exploitation of the ubiquitin system. Nat. Cell Biol. 2009, 11:527-534.
    • (2009) Nat. Cell Biol. , vol.11 , pp. 527-534
    • Randow, F.1    Lehner, P.J.2
  • 76
    • 77955109451 scopus 로고    scopus 로고
    • A bacterial E3 ubiquitin ligase IpaH9.8 targets NEMO/IKKgamma to dampen the host NF-kappaB-mediated inflammatory response
    • Ashida H., et al. A bacterial E3 ubiquitin ligase IpaH9.8 targets NEMO/IKKgamma to dampen the host NF-kappaB-mediated inflammatory response. Nat. Cell Biol. 2010, 12:66-73.
    • (2010) Nat. Cell Biol. , vol.12 , pp. 66-73
    • Ashida, H.1
  • 77
    • 33744797119 scopus 로고    scopus 로고
    • Viral modulators of cullin RING ubiquitin ligases: culling the host defense
    • Barry M., Fruh K. Viral modulators of cullin RING ubiquitin ligases: culling the host defense. Sci. STKE 2006, 2006:pe21.
    • (2006) Sci. STKE , vol.2006
    • Barry, M.1    Fruh, K.2
  • 78
    • 40649114040 scopus 로고    scopus 로고
    • HIV-1 accessory proteins VPR and Vif modulate antiviral response by targeting IRF-3 for degradation
    • Okumura A., et al. HIV-1 accessory proteins VPR and Vif modulate antiviral response by targeting IRF-3 for degradation. Virology 2008, 373:85-97.
    • (2008) Virology , vol.373 , pp. 85-97
    • Okumura, A.1
  • 79
    • 79952123931 scopus 로고    scopus 로고
    • Microbial manipulation of receptor crosstalk in innate immunity
    • Hajishengallis G., Lambris J.D. Microbial manipulation of receptor crosstalk in innate immunity. Nat. Rev. Immunol. 2011, 11:187-200.
    • (2011) Nat. Rev. Immunol. , vol.11 , pp. 187-200
    • Hajishengallis, G.1    Lambris, J.D.2
  • 80
    • 0037237593 scopus 로고    scopus 로고
    • Mycobacteria target DC-SIGN to suppress dendritic cell function
    • Geijtenbeek T.B. Mycobacteria target DC-SIGN to suppress dendritic cell function. J. Exp. Med. 2003, 197:7-17.
    • (2003) J. Exp. Med. , vol.197 , pp. 7-17
    • Geijtenbeek, T.B.1
  • 81
    • 34248544993 scopus 로고    scopus 로고
    • C-type lectin DC-SIGN modulates Toll-like receptor signaling via Raf-1 kinase-dependent acetylation of transcription factor NF-kappaB
    • Gringhuis S.I., et al. C-type lectin DC-SIGN modulates Toll-like receptor signaling via Raf-1 kinase-dependent acetylation of transcription factor NF-kappaB. Immunity 2007, 26:605-616.
    • (2007) Immunity , vol.26 , pp. 605-616
    • Gringhuis, S.I.1
  • 82
    • 70349201241 scopus 로고    scopus 로고
    • Carbohydrate-specific signaling through the DC-SIGN signalosome tailors immunity to Mycobacterium tuberculosis, HIV-1 and Helicobacter pylori
    • Gringhuis S.I., et al. Carbohydrate-specific signaling through the DC-SIGN signalosome tailors immunity to Mycobacterium tuberculosis, HIV-1 and Helicobacter pylori. Nat. Immunol. 2009, 10:1081-1088.
    • (2009) Nat. Immunol. , vol.10 , pp. 1081-1088
    • Gringhuis, S.I.1
  • 83
    • 33745679123 scopus 로고    scopus 로고
    • Targeting signal transduction as a strategy to treat inflammatory diseases
    • O'Neill L.A. Targeting signal transduction as a strategy to treat inflammatory diseases. Nat. Rev. Drug Discov. 2006, 5:549-563.
    • (2006) Nat. Rev. Drug Discov. , vol.5 , pp. 549-563
    • O'Neill, L.A.1
  • 84
    • 34249677845 scopus 로고    scopus 로고
    • Therapeutic targeting of innate immunity with Toll-like receptor agonists and antagonists
    • Kanzler H., et al. Therapeutic targeting of innate immunity with Toll-like receptor agonists and antagonists. Nat. Med. 2007, 13:552-559.
    • (2007) Nat. Med. , vol.13 , pp. 552-559
    • Kanzler, H.1
  • 85
    • 0037372661 scopus 로고    scopus 로고
    • Inhibition of endotoxin response by e5564, a novel Toll-like receptor 4-directed endotoxin antagonist
    • Mullarkey M., et al. Inhibition of endotoxin response by e5564, a novel Toll-like receptor 4-directed endotoxin antagonist. J. Pharmacol. Exp. Ther. 2003, 304:1093-1102.
    • (2003) J. Pharmacol. Exp. Ther. , vol.304 , pp. 1093-1102
    • Mullarkey, M.1
  • 86
    • 67349182481 scopus 로고    scopus 로고
    • The structural basis of lipopolysaccharide recognition by the TLR4-MD-2 complex
    • Park B.S., et al. The structural basis of lipopolysaccharide recognition by the TLR4-MD-2 complex. Nature 2009, 458:1191-1195.
    • (2009) Nature , vol.458 , pp. 1191-1195
    • Park, B.S.1
  • 87
    • 0033532629 scopus 로고    scopus 로고
    • MD-2, a molecule that confers lipopolysaccharide responsiveness on Toll-like receptor 4
    • Shimazu R., et al. MD-2, a molecule that confers lipopolysaccharide responsiveness on Toll-like receptor 4. J. Exp. Med. 1999, 189:1777-1782.
    • (1999) J. Exp. Med. , vol.189 , pp. 1777-1782
    • Shimazu, R.1
  • 88
    • 34447529270 scopus 로고    scopus 로고
    • Ibudilast (AV-411). A new class therapeutic candidate for neuropathic pain and opioid withdrawal syndromes
    • Ledeboer A., et al. Ibudilast (AV-411). A new class therapeutic candidate for neuropathic pain and opioid withdrawal syndromes. Expert Opin. Investig. Drugs 2007, 16:935-950.
    • (2007) Expert Opin. Investig. Drugs , vol.16 , pp. 935-950
    • Ledeboer, A.1
  • 89
    • 26844467349 scopus 로고    scopus 로고
    • Nucleic acids of mammalian origin can act as endogenous ligands for Toll-like receptors and may promote systemic lupus erythematosus
    • Barrat F.J., et al. Nucleic acids of mammalian origin can act as endogenous ligands for Toll-like receptors and may promote systemic lupus erythematosus. J. Exp. Med. 2005, 202:1131-1139.
    • (2005) J. Exp. Med. , vol.202 , pp. 1131-1139
    • Barrat, F.J.1
  • 90
    • 4644330955 scopus 로고    scopus 로고
    • Toll-like receptor 9 binds single-stranded CpG-DNA in a sequence- and pH-dependent manner
    • Rutz M., et al. Toll-like receptor 9 binds single-stranded CpG-DNA in a sequence- and pH-dependent manner. Eur. J. Immunol. 2004, 34:2541-2550.
    • (2004) Eur. J. Immunol. , vol.34 , pp. 2541-2550
    • Rutz, M.1
  • 91
    • 79955046267 scopus 로고    scopus 로고
    • Mechanism of endosomal TLR inhibition by antimalarial drugs and imidazoquinolines
    • Kuznik A., et al. Mechanism of endosomal TLR inhibition by antimalarial drugs and imidazoquinolines. J. Immunol. 2011, 186:4794-4804.
    • (2011) J. Immunol. , vol.186 , pp. 4794-4804
    • Kuznik, A.1
  • 92
    • 0031936182 scopus 로고    scopus 로고
    • Antagonism of immunostimulatory CpG-oligodeoxynucleotides by quinacrine, chloroquine, and structurally related compounds
    • Macfarlane D.E., Manzel L. Antagonism of immunostimulatory CpG-oligodeoxynucleotides by quinacrine, chloroquine, and structurally related compounds. J. Immunol. 1998, 160:1122-1131.
    • (1998) J. Immunol. , vol.160 , pp. 1122-1131
    • Macfarlane, D.E.1    Manzel, L.2
  • 93
    • 79952753327 scopus 로고    scopus 로고
    • Therapeutical targeting of nucleic acid-sensing Toll-like receptors prevents experimental cerebral malaria
    • Franklin B.S., et al. Therapeutical targeting of nucleic acid-sensing Toll-like receptors prevents experimental cerebral malaria. Proc. Natl. Acad. Sci. U.S.A. 2011, 108:3689-3694.
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 3689-3694
    • Franklin, B.S.1
  • 94
    • 37549066665 scopus 로고    scopus 로고
    • Treatment of lupus-prone mice with a dual inhibitor of TLR7 and TLR9 leads to reduction of autoantibody production and amelioration of disease symptoms
    • Barrat F.J., et al. Treatment of lupus-prone mice with a dual inhibitor of TLR7 and TLR9 leads to reduction of autoantibody production and amelioration of disease symptoms. Eur. J. Immunol. 2007, 37:3582-3586.
    • (2007) Eur. J. Immunol. , vol.37 , pp. 3582-3586
    • Barrat, F.J.1
  • 95
    • 33644523710 scopus 로고    scopus 로고
    • MyD88-dependent and -independent signaling by IL-1 in neurons probed by bifunctional Toll/IL-1 receptor domain/BB-loop mimetics
    • Davis C.N., et al. MyD88-dependent and -independent signaling by IL-1 in neurons probed by bifunctional Toll/IL-1 receptor domain/BB-loop mimetics. Proc. Natl. Acad. Sci. U.S.A. 2006, 103:2953-2958.
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 2953-2958
    • Davis, C.N.1
  • 96
    • 34548415806 scopus 로고    scopus 로고
    • Pivotal advance: inhibition of MyD88 dimerization and recruitment of IRAK1 and IRAK4 by a novel peptidomimetic compound
    • Loiarro M., et al. Pivotal advance: inhibition of MyD88 dimerization and recruitment of IRAK1 and IRAK4 by a novel peptidomimetic compound. J. Leukoc. Biol. 2007, 82:801-810.
    • (2007) J. Leukoc. Biol. , vol.82 , pp. 801-810
    • Loiarro, M.1
  • 97
    • 68149139538 scopus 로고    scopus 로고
    • The ubiquitin-editing enzyme A20 (TNFAIP3) is a central regulator of immunopathology
    • Vereecke L., et al. The ubiquitin-editing enzyme A20 (TNFAIP3) is a central regulator of immunopathology. Trends Immunol. 2009, 30:383-391.
    • (2009) Trends Immunol. , vol.30 , pp. 383-391
    • Vereecke, L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.