메뉴 건너뛰기




Volumn 34, Issue 3, 2009, Pages 128-135

Autoregulatory feedback loops terminating the NF-κB response

Author keywords

[No Author keywords available]

Indexed keywords

IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; SUMO PROTEIN;

EID: 62849118323     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tibs.2008.12.003     Document Type: Review
Times cited : (133)

References (72)
  • 1
    • 34447293087 scopus 로고    scopus 로고
    • Oscillations and temporal signalling in cells
    • Tiana G., et al. Oscillations and temporal signalling in cells. Phys. Biol. 4 (2007) R1-R17
    • (2007) Phys. Biol. , vol.4
    • Tiana, G.1
  • 2
    • 47949099098 scopus 로고    scopus 로고
    • Origin and physiological roles of inflammation
    • Medzhitov R. Origin and physiological roles of inflammation. Nature 454 (2008) 428-435
    • (2008) Nature , vol.454 , pp. 428-435
    • Medzhitov, R.1
  • 3
    • 30044449982 scopus 로고    scopus 로고
    • Resolution of inflammation: the beginning programs the end
    • Serhan C.N., and Savill J. Resolution of inflammation: the beginning programs the end. Nat. Immunol. 6 (2005) 1191-1197
    • (2005) Nat. Immunol. , vol.6 , pp. 1191-1197
    • Serhan, C.N.1    Savill, J.2
  • 4
    • 33947303355 scopus 로고    scopus 로고
    • Resolution of inflammation: intracellular feedback loops in the endothelium
    • Winsauer G., and de Martin R. Resolution of inflammation: intracellular feedback loops in the endothelium. Thromb. Haemost. 97 (2007) 364-369
    • (2007) Thromb. Haemost. , vol.97 , pp. 364-369
    • Winsauer, G.1    de Martin, R.2
  • 5
    • 33646382406 scopus 로고    scopus 로고
    • Transient IκB kinase activity mediates temporal NF-κB dynamics in response to a wide range of tumor necrosis factor-α doses
    • Cheong R., et al. Transient IκB kinase activity mediates temporal NF-κB dynamics in response to a wide range of tumor necrosis factor-α doses. J. Biol. Chem. 281 (2006) 2945-2950
    • (2006) J. Biol. Chem. , vol.281 , pp. 2945-2950
    • Cheong, R.1
  • 6
    • 39949083374 scopus 로고    scopus 로고
    • Wires in the soup: quantitative models of cell signaling
    • Cheong R., and Levchenko A. Wires in the soup: quantitative models of cell signaling. Trends Cell Biol. 18 (2008) 112-118
    • (2008) Trends Cell Biol. , vol.18 , pp. 112-118
    • Cheong, R.1    Levchenko, A.2
  • 7
    • 45149090556 scopus 로고    scopus 로고
    • Nuclear ubiquitin ligases, NF-κB degradation, and the control of inflammation
    • Natoli G., and Chiocca S. Nuclear ubiquitin ligases, NF-κB degradation, and the control of inflammation. Sci. Signal. 1 (2008) pe1
    • (2008) Sci. Signal. , vol.1
    • Natoli, G.1    Chiocca, S.2
  • 8
    • 20644450101 scopus 로고    scopus 로고
    • Negative regulation of Toll-like receptor 4 signaling by the Toll-like receptor homolog RP105
    • Divanovic S., et al. Negative regulation of Toll-like receptor 4 signaling by the Toll-like receptor homolog RP105. Nat. Immunol. 6 (2005) 571-578
    • (2005) Nat. Immunol. , vol.6 , pp. 571-578
    • Divanovic, S.1
  • 9
    • 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 (1998) 2085-2088
    • (1998) Science , vol.282 , pp. 2085-2088
    • Poltorak, A.1
  • 10
    • 0031587953 scopus 로고    scopus 로고
    • Expression of ST2, an interleukin-1 receptor homologue, is induced by proinflammatory stimuli
    • Kumar S., et al. Expression of ST2, an interleukin-1 receptor homologue, is induced by proinflammatory stimuli. Biochem. Biophys. Res. Commun. 235 (1997) 474-478
    • (1997) Biochem. Biophys. Res. Commun. , vol.235 , pp. 474-478
    • Kumar, S.1
  • 11
    • 0037178785 scopus 로고    scopus 로고
    • IRAK-M is a negative regulator of Toll-like receptor signaling
    • Kobayashi K., et al. IRAK-M is a negative regulator of Toll-like receptor signaling. Cell 110 (2002) 191-202
    • (2002) Cell , vol.110 , pp. 191-202
    • Kobayashi, K.1
  • 12
    • 34250805968 scopus 로고    scopus 로고
    • IRAK-M is involved in the pathogenesis of early-onset persistent asthma
    • Balaci L., et al. IRAK-M is involved in the pathogenesis of early-onset persistent asthma. Am. J. Hum. Genet. 80 (2007) 1103-1114
    • (2007) Am. J. Hum. Genet. , vol.80 , pp. 1103-1114
    • Balaci, L.1
  • 13
    • 22544451204 scopus 로고    scopus 로고
    • A novel splice variant of interleukin-1 receptor (IL-1R)-associated kinase 1 plays a negative regulatory role in Toll/IL-1R-induced inflammatory signaling
    • Rao N., et al. A novel splice variant of interleukin-1 receptor (IL-1R)-associated kinase 1 plays a negative regulatory role in Toll/IL-1R-induced inflammatory signaling. Mol. Cell. Biol. 25 (2005) 6521-6532
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 6521-6532
    • Rao, N.1
  • 14
    • 0037454946 scopus 로고    scopus 로고
    • Inhibition of interleukin 1 receptor/Toll-like receptor signaling through the alternatively spliced, short form of MyD88 is due to its failure to recruit IRAK-4
    • Burns K., et al. Inhibition of interleukin 1 receptor/Toll-like receptor signaling through the alternatively spliced, short form of MyD88 is due to its failure to recruit IRAK-4. J. Exp. Med. 197 (2003) 263-268
    • (2003) J. Exp. Med. , vol.197 , pp. 263-268
    • Burns, K.1
  • 15
    • 0042236366 scopus 로고    scopus 로고
    • MyD88S, a splice variant of MyD88, differentially modulates NF-κB- and AP-1-dependent gene expression
    • Janssens S., et al. MyD88S, a splice variant of MyD88, differentially modulates NF-κB- and AP-1-dependent gene expression. FEBS Lett. 548 (2003) 103-107
    • (2003) FEBS Lett. , vol.548 , pp. 103-107
    • Janssens, S.1
  • 16
    • 1642423503 scopus 로고    scopus 로고
    • Zinc-finger protein A20, a regulator of inflammation and cell survival, has de-ubiquitinating activity
    • Evans P.C., et al. Zinc-finger protein A20, a regulator of inflammation and cell survival, has de-ubiquitinating activity. Biochem. J. 378 (2004) 727-734
    • (2004) Biochem. J. , vol.378 , pp. 727-734
    • Evans, P.C.1
  • 17
    • 38549146936 scopus 로고    scopus 로고
    • Molecular basis for the unique deubiquitinating activity of the NF-κB inhibitor A20
    • Lin S.C., et al. Molecular basis for the unique deubiquitinating activity of the NF-κB inhibitor A20. J. Mol. Biol. 376 (2008) 526-540
    • (2008) J. Mol. Biol. , vol.376 , pp. 526-540
    • Lin, S.C.1
  • 18
    • 3943054838 scopus 로고    scopus 로고
    • De-ubiquitination and ubiquitin ligase domains of A20 downregulate NF-κB signalling
    • Wertz I.E., et al. De-ubiquitination and ubiquitin ligase domains of A20 downregulate NF-κB signalling. Nature 430 (2004) 694-699
    • (2004) Nature , vol.430 , pp. 694-699
    • Wertz, I.E.1
  • 19
    • 39449083378 scopus 로고    scopus 로고
    • The E3 ligase Itch negatively regulates inflammatory signaling pathways by controlling the function of the ubiquitin-editing enzyme A20
    • Shembade N., et al. The E3 ligase Itch negatively regulates inflammatory signaling pathways by controlling the function of the ubiquitin-editing enzyme A20. Nat. Immunol. 9 (2008) 254-262
    • (2008) Nat. Immunol. , vol.9 , pp. 254-262
    • Shembade, N.1
  • 20
    • 39449129941 scopus 로고    scopus 로고
    • Inflammatory cardiac valvulitis in TAX1BP1-deficient mice through selective NF-κB activation
    • Iha H., et al. Inflammatory cardiac valvulitis in TAX1BP1-deficient mice through selective NF-κB activation. EMBO J. 27 (2008) 629-641
    • (2008) EMBO J. , vol.27 , pp. 629-641
    • Iha, H.1
  • 21
    • 33846984613 scopus 로고    scopus 로고
    • LIND/ABIN-3 is a novel lipopolysaccharide-inducible inhibitor of NF-κB activation
    • Wullaert A., et al. LIND/ABIN-3 is a novel lipopolysaccharide-inducible inhibitor of NF-κB activation. J. Biol. Chem. 282 (2007) 81-90
    • (2007) J. Biol. Chem. , vol.282 , pp. 81-90
    • Wullaert, A.1
  • 22
    • 44649166613 scopus 로고    scopus 로고
    • Ubiquitin binding mediates the NF-κB inhibitory potential of ABIN proteins
    • Wagner S., et al. Ubiquitin binding mediates the NF-κB inhibitory potential of ABIN proteins. Oncogene 27 (2008) 3739-3745
    • (2008) Oncogene , vol.27 , pp. 3739-3745
    • Wagner, S.1
  • 23
    • 43749122598 scopus 로고    scopus 로고
    • NF-κB suppression by the deubiquitinating enzyme Cezanne: a novel negative feedback loop in pro-inflammatory signaling
    • Enesa K., et al. NF-κB suppression by the deubiquitinating enzyme Cezanne: a novel negative feedback loop in pro-inflammatory signaling. J. Biol. Chem. 283 (2008) 7036-7045
    • (2008) J. Biol. Chem. , vol.283 , pp. 7036-7045
    • Enesa, K.1
  • 24
    • 42449146639 scopus 로고    scopus 로고
    • Tumor suppressor CYLD: negative regulation of NF-κB signaling and more
    • Courtois G. Tumor suppressor CYLD: negative regulation of NF-κB signaling and more. Cell. Mol. Life Sci. 65 (2008) 1123-1132
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 1123-1132
    • Courtois, G.1
  • 25
    • 33646531810 scopus 로고    scopus 로고
    • Cyld inhibits tumor cell proliferation by blocking Bcl-3-dependent NF-κB signaling
    • Massoumi R., et al. Cyld inhibits tumor cell proliferation by blocking Bcl-3-dependent NF-κB signaling. Cell 125 (2006) 665-677
    • (2006) Cell , vol.125 , pp. 665-677
    • Massoumi, R.1
  • 26
    • 18144368948 scopus 로고    scopus 로고
    • Regulation of the deubiquitinating enzyme CYLD by IκB kinase γ-dependent phosphorylation
    • Reiley W., et al. Regulation of the deubiquitinating enzyme CYLD by IκB kinase γ-dependent phosphorylation. Mol. Cell. Biol. 25 (2005) 3886-3895
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 3886-3895
    • Reiley, W.1
  • 27
    • 33750598021 scopus 로고    scopus 로고
    • Impaired regulation of NF-κB and increased susceptibility to colitis-associated tumorigenesis in CYLD-deficient mice
    • Zhang J., et al. Impaired regulation of NF-κB and increased susceptibility to colitis-associated tumorigenesis in CYLD-deficient mice. J. Clin. Invest. 116 (2006) 3042-3049
    • (2006) J. Clin. Invest. , vol.116 , pp. 3042-3049
    • Zhang, J.1
  • 28
    • 1942453854 scopus 로고    scopus 로고
    • Degradation of Bcl10 induced by T-cell activation negatively regulates NF-κB signaling
    • Scharschmidt E., et al. Degradation of Bcl10 induced by T-cell activation negatively regulates NF-κB signaling. Mol. Cell. Biol. 24 (2004) 3860-3873
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 3860-3873
    • Scharschmidt, E.1
  • 29
    • 33846528701 scopus 로고    scopus 로고
    • Negative feedback loop in T cell activation through IκB kinase-induced phosphorylation and degradation of Bcl10
    • Lobry C., et al. Negative feedback loop in T cell activation through IκB kinase-induced phosphorylation and degradation of Bcl10. Proc. Natl. Acad. Sci. U. S. A. 104 (2007) 908-913
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 908-913
    • Lobry, C.1
  • 30
    • 33745494351 scopus 로고    scopus 로고
    • Essential role for IκB kinase β in remodeling Carma1-Bcl10-Malt1 complexes upon T cell activation
    • Wegener E., et al. Essential role for IκB kinase β in remodeling Carma1-Bcl10-Malt1 complexes upon T cell activation. Mol. Cell 23 (2006) 13-23
    • (2006) Mol. Cell , vol.23 , pp. 13-23
    • Wegener, E.1
  • 31
    • 40949163764 scopus 로고    scopus 로고
    • TRIM30 α negatively regulates TLR-mediated NF-κB activation by targeting TAB2 and TAB3 for degradation
    • Shi M., et al. TRIM30 α negatively regulates TLR-mediated NF-κB activation by targeting TAB2 and TAB3 for degradation. Nat. Immunol. 9 (2008) 369-377
    • (2008) Nat. Immunol. , vol.9 , pp. 369-377
    • Shi, M.1
  • 32
    • 34249066486 scopus 로고    scopus 로고
    • PDLIM2-mediated termination of transcription factor NF-κB activation by intranuclear sequestration and degradation of the p65 subunit
    • Tanaka T., et al. PDLIM2-mediated termination of transcription factor NF-κB activation by intranuclear sequestration and degradation of the p65 subunit. Nat. Immunol. 8 (2007) 584-591
    • (2007) Nat. Immunol. , vol.8 , pp. 584-591
    • Tanaka, T.1
  • 33
    • 33846475712 scopus 로고    scopus 로고
    • COMMD1 promotes the ubiquitination of NF-κB subunits through a cullin-containing ubiquitin ligase
    • Maine G.N., et al. COMMD1 promotes the ubiquitination of NF-κB subunits through a cullin-containing ubiquitin ligase. EMBO J. 26 (2007) 436-447
    • (2007) EMBO J. , vol.26 , pp. 436-447
    • Maine, G.N.1
  • 34
    • 41949114612 scopus 로고    scopus 로고
    • IEX-1 directly interferes with RelA/p65 dependent transactivation and regulation of apoptosis
    • Arlt A., et al. IEX-1 directly interferes with RelA/p65 dependent transactivation and regulation of apoptosis. Biochim. Biophys. Acta 1783 (2008) 941-952
    • (2008) Biochim. Biophys. Acta , vol.1783 , pp. 941-952
    • Arlt, A.1
  • 35
    • 0037462477 scopus 로고    scopus 로고
    • Twist regulates cytokine gene expression through a negative feedback loop that represses NF-κB activity
    • Sosic D., et al. Twist regulates cytokine gene expression through a negative feedback loop that represses NF-κB activity. Cell 112 (2003) 169-180
    • (2003) Cell , vol.112 , pp. 169-180
    • Sosic, D.1
  • 36
    • 33744949739 scopus 로고    scopus 로고
    • A novel member of the IκB family, human IκB-ζ, inhibits transactivation of p65 and its DNA binding
    • Totzke G., et al. A novel member of the IκB family, human IκB-ζ, inhibits transactivation of p65 and its DNA binding. J. Biol. Chem. 281 (2006) 12645-12654
    • (2006) J. Biol. Chem. , vol.281 , pp. 12645-12654
    • Totzke, G.1
  • 37
    • 34249039031 scopus 로고    scopus 로고
    • Proinflammatory stimuli induce IKKα-mediated phosphorylation of PIAS1 to restrict inflammation and immunity
    • Liu B., et al. Proinflammatory stimuli induce IKKα-mediated phosphorylation of PIAS1 to restrict inflammation and immunity. Cell 129 (2007) 903-914
    • (2007) Cell , vol.129 , pp. 903-914
    • Liu, B.1
  • 38
    • 17844386319 scopus 로고    scopus 로고
    • IKKα limits macrophage NF-κB activation and contributes to the resolution of inflammation
    • Lawrence T., et al. IKKα limits macrophage NF-κB activation and contributes to the resolution of inflammation. Nature 434 (2005) 1138-1143
    • (2005) Nature , vol.434 , pp. 1138-1143
    • Lawrence, T.1
  • 39
    • 0027245086 scopus 로고
    • Cytokine-inducible expression in endothelial cells of an IκB α-like gene is regulated by NF κB
    • de Martin R., et al. Cytokine-inducible expression in endothelial cells of an IκB α-like gene is regulated by NF κB. EMBO J. 12 (1993) 2773-2779
    • (1993) EMBO J. , vol.12 , pp. 2773-2779
    • de Martin, R.1
  • 40
    • 0027168447 scopus 로고
    • NF-κB controls expression of inhibitor IκBα: evidence for an inducible autoregulatory pathway
    • Sun S.C., et al. NF-κB controls expression of inhibitor IκBα: evidence for an inducible autoregulatory pathway. Science 259 (1993) 1912-1915
    • (1993) Science , vol.259 , pp. 1912-1915
    • Sun, S.C.1
  • 41
    • 0027462682 scopus 로고
    • Mutual regulation of the transcriptional activator NF-κB and its inhibitor
    • Brown K., et al. Mutual regulation of the transcriptional activator NF-κB and its inhibitor. IκB-α. Proc. Natl. Acad. Sci. U. S. A. 90 (1993) 2532-2536
    • (1993) IκB-α. Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 2532-2536
    • Brown, K.1
  • 42
    • 0027168948 scopus 로고
    • The p65 subunit of NF-κB regulates IκB by two distinct mechanisms
    • Scott M.L., et al. The p65 subunit of NF-κB regulates IκB by two distinct mechanisms. Genes Dev. 7 (1993) 1266-1276
    • (1993) Genes Dev. , vol.7 , pp. 1266-1276
    • Scott, M.L.1
  • 43
    • 0036911146 scopus 로고    scopus 로고
    • Regulation of IκBβ expression in testis
    • Budde L.M., et al. Regulation of IκBβ expression in testis. Mol. Biol. Cell 13 (2002) 4179-4194
    • (2002) Mol. Biol. Cell , vol.13 , pp. 4179-4194
    • Budde, L.M.1
  • 44
    • 33747388013 scopus 로고    scopus 로고
    • IκBε provides negative feedback to control NF-κB oscillations, signaling dynamics, and inflammatory gene expression
    • Kearns J.D., et al. IκBε provides negative feedback to control NF-κB oscillations, signaling dynamics, and inflammatory gene expression. J. Cell Biol. 173 (2006) 659-664
    • (2006) J. Cell Biol. , vol.173 , pp. 659-664
    • Kearns, J.D.1
  • 45
    • 0025304791 scopus 로고
    • Purified human IκB can rapidly dissociate the complex of the NF-κB transcription factor with its cognate DNA
    • Zabel U., and Baeuerle P.A. Purified human IκB can rapidly dissociate the complex of the NF-κB transcription factor with its cognate DNA. Cell 61 (1990) 255-265
    • (1990) Cell , vol.61 , pp. 255-265
    • Zabel, U.1    Baeuerle, P.A.2
  • 46
    • 0029664657 scopus 로고    scopus 로고
    • IκBα deficiency results in a sustained NF-κB response and severe widespread dermatitis in mice
    • Klement J.F., et al. IκBα deficiency results in a sustained NF-κB response and severe widespread dermatitis in mice. Mol. Cell. Biol. 16 (1996) 2341-2349
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 2341-2349
    • Klement, J.F.1
  • 47
    • 0032555927 scopus 로고    scopus 로고
    • Functional redundancy of the nuclear factor κB inhibitors IκBα and IκBβ
    • Cheng J.D., et al. Functional redundancy of the nuclear factor κB inhibitors IκBα and IκBβ. J. Exp. Med. 188 (1998) 1055-1062
    • (1998) J. Exp. Med. , vol.188 , pp. 1055-1062
    • Cheng, J.D.1
  • 48
    • 48749085156 scopus 로고    scopus 로고
    • Encoding NF-κB temporal control in response to TNF: distinct roles for the negative regulators IκBα and A20
    • Werner S.L., et al. Encoding NF-κB temporal control in response to TNF: distinct roles for the negative regulators IκBα and A20. Genes Dev. 22 (2008) 2093-2101
    • (2008) Genes Dev. , vol.22 , pp. 2093-2101
    • Werner, S.L.1
  • 49
    • 24344480077 scopus 로고    scopus 로고
    • Interleukin-6 plays a crucial role in the hepatic expression of SOCS3 during acute inflammatory processes in vivo
    • Yang X.P., et al. Interleukin-6 plays a crucial role in the hepatic expression of SOCS3 during acute inflammatory processes in vivo. J. Hepatol. 43 (2005) 704-710
    • (2005) J. Hepatol. , vol.43 , pp. 704-710
    • Yang, X.P.1
  • 50
    • 33745194935 scopus 로고    scopus 로고
    • Suppressor of cytokine Signaling-3 inhibits interleukin-1 signaling by targeting the TRAF-6/TAK1 complex
    • Frobose H., et al. Suppressor of cytokine Signaling-3 inhibits interleukin-1 signaling by targeting the TRAF-6/TAK1 complex. Mol. Endocrinol. 20 (2006) 1587-1596
    • (2006) Mol. Endocrinol. , vol.20 , pp. 1587-1596
    • Frobose, H.1
  • 51
    • 36849033963 scopus 로고    scopus 로고
    • TAM receptors are pleiotropic inhibitors of the innate immune response
    • Rothlin C.V., et al. TAM receptors are pleiotropic inhibitors of the innate immune response. Cell 131 (2007) 1124-1136
    • (2007) Cell , vol.131 , pp. 1124-1136
    • Rothlin, C.V.1
  • 52
    • 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 (2006) 148-155
    • (2006) Nat. Immunol. , vol.7 , pp. 148-155
    • Mansell, A.1
  • 53
    • 0033537719 scopus 로고    scopus 로고
    • Positive and negative regulation of IκB kinase activity through IKKβ subunit phosphorylation
    • Delhase M., et al. Positive and negative regulation of IκB kinase activity through IKKβ subunit phosphorylation. Science 284 (1999) 309-313
    • (1999) Science , vol.284 , pp. 309-313
    • Delhase, M.1
  • 54
    • 42449137850 scopus 로고    scopus 로고
    • Deactivation of the kinase IKK by CUEDC2 through recruitment of the phosphatase PP1
    • Li H.Y., et al. Deactivation of the kinase IKK by CUEDC2 through recruitment of the phosphatase PP1. Nat. Immunol. 9 (2008) 533-541
    • (2008) Nat. Immunol. , vol.9 , pp. 533-541
    • Li, H.Y.1
  • 55
    • 33747608638 scopus 로고    scopus 로고
    • NF-κB-dependent induction of microRNA miR-146, an inhibitor targeted to signaling proteins of innate immune responses
    • Taganov K.D., et al. NF-κB-dependent induction of microRNA miR-146, an inhibitor targeted to signaling proteins of innate immune responses. Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 12481-12486
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 12481-12486
    • Taganov, K.D.1
  • 56
    • 57749094930 scopus 로고    scopus 로고
    • G9a and HP1 couple histone and DNA methylation to TNFα transcription silencing during endotoxin tolerance
    • El Gazzar M., et al. G9a and HP1 couple histone and DNA methylation to TNFα transcription silencing during endotoxin tolerance. J. Biol. Chem. 283 (2008) 32198-32208
    • (2008) J. Biol. Chem. , vol.283 , pp. 32198-32208
    • El Gazzar, M.1
  • 57
    • 34250823515 scopus 로고    scopus 로고
    • Gene-specific control of inflammation by TLR-induced chromatin modifications
    • Foster S.L., et al. Gene-specific control of inflammation by TLR-induced chromatin modifications. Nature 447 (2007) 972-978
    • (2007) Nature , vol.447 , pp. 972-978
    • Foster, S.L.1
  • 58
    • 18344393786 scopus 로고    scopus 로고
    • Peptide-induced negative selection of thymocytes activates transcription of an NF-κB inhibitor
    • Fiorini E., et al. Peptide-induced negative selection of thymocytes activates transcription of an NF-κB inhibitor. Mol. Cell 9 (2002) 637-648
    • (2002) Mol. Cell , vol.9 , pp. 637-648
    • Fiorini, E.1
  • 59
    • 0042733592 scopus 로고    scopus 로고
    • SIGIRR, a negative regulator of Toll-like receptor-interleukin 1 receptor signaling
    • Wald D., et al. SIGIRR, a negative regulator of Toll-like receptor-interleukin 1 receptor signaling. Nat. Immunol. 4 (2003) 920-927
    • (2003) Nat. Immunol. , vol.4 , pp. 920-927
    • Wald, D.1
  • 60
    • 0037697247 scopus 로고    scopus 로고
    • SINK is a p65-interacting negative regulator of NF-κB-dependent transcription
    • Wu M., et al. SINK is a p65-interacting negative regulator of NF-κB-dependent transcription. J. Biol. Chem. 278 (2003) 27072-27079
    • (2003) J. Biol. Chem. , vol.278 , pp. 27072-27079
    • Wu, M.1
  • 61
    • 36049033394 scopus 로고    scopus 로고
    • Signaling to NF-κB by Toll-like receptors
    • Kawai T., and Akira S. Signaling to NF-κB by Toll-like receptors. Trends Mol. Med. 13 (2007) 460-469
    • (2007) Trends Mol. Med. , vol.13 , pp. 460-469
    • Kawai, T.1    Akira, S.2
  • 62
    • 34848820013 scopus 로고    scopus 로고
    • Diversity and regulation in the NF-κB system
    • Wietek C., and O'Neill L.A. Diversity and regulation in the NF-κB system. Trends Biochem. Sci. 32 (2007) 311-319
    • (2007) Trends Biochem. Sci. , vol.32 , pp. 311-319
    • Wietek, C.1    O'Neill, L.A.2
  • 63
    • 5644235488 scopus 로고    scopus 로고
    • NF-κB: a multifaceted transcription factor regulated at several levels
    • Schmitz M.L., et al. NF-κB: a multifaceted transcription factor regulated at several levels. ChemBioChem 5 (2004) 1348-1358
    • (2004) ChemBioChem , vol.5 , pp. 1348-1358
    • Schmitz, M.L.1
  • 64
    • 33845768987 scopus 로고    scopus 로고
    • Integrating cell-signalling pathways with NF-κB and IKK function
    • Perkins N.D. Integrating cell-signalling pathways with NF-κB and IKK function. Nat. Rev. Mol. Cell Biol. 8 (2007) 49-62
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 49-62
    • Perkins, N.D.1
  • 65
    • 33746028777 scopus 로고    scopus 로고
    • Intracellular pattern recognition receptors in the host response
    • Meylan E., et al. Intracellular pattern recognition receptors in the host response. Nature 442 (2006) 39-44
    • (2006) Nature , vol.442 , pp. 39-44
    • Meylan, E.1
  • 66
    • 24944586285 scopus 로고    scopus 로고
    • Achieving stability of lipopolysaccharide-induced NF-κB activation
    • Covert M.W., et al. Achieving stability of lipopolysaccharide-induced NF-κB activation. Science 309 (2005) 1854-1857
    • (2005) Science , vol.309 , pp. 1854-1857
    • Covert, M.W.1
  • 67
    • 38849199203 scopus 로고    scopus 로고
    • Shared principles in NF-κB signaling
    • Hayden M.S., and Ghosh S. Shared principles in NF-κB signaling. Cell 132 (2008) 344-362
    • (2008) Cell , vol.132 , pp. 344-362
    • Hayden, M.S.1    Ghosh, S.2
  • 68
    • 39049183044 scopus 로고    scopus 로고
    • Regulation and function of IKK and IKK-related kinases
    • Hacker H., and Karin M. Regulation and function of IKK and IKK-related kinases. Sci. STKE 2006 (2006) re13
    • (2006) Sci. STKE , vol.2006
    • Hacker, H.1    Karin, M.2
  • 69
    • 28544435897 scopus 로고    scopus 로고
    • Immunity by ubiquitylation: a reversible process of modification
    • Liu Y.C., et al. Immunity by ubiquitylation: a reversible process of modification. Nat. Rev. Immunol. 5 (2005) 941-952
    • (2005) Nat. Rev. Immunol. , vol.5 , pp. 941-952
    • Liu, Y.C.1
  • 70
    • 33749369277 scopus 로고    scopus 로고
    • Ubiquitin: tool and target for intracellular NF-κB inhibitors
    • Wullaert A., et al. Ubiquitin: tool and target for intracellular NF-κB inhibitors. Trends Immunol. 27 (2006) 533-540
    • (2006) Trends Immunol. , vol.27 , pp. 533-540
    • Wullaert, A.1
  • 71
    • 46249124976 scopus 로고    scopus 로고
    • Deubiquitylation and regulation of the immune response
    • Sun S.C. Deubiquitylation and regulation of the immune response. Nat. Rev. Immunol. 8 (2008) 501-511
    • (2008) Nat. Rev. Immunol. , vol.8 , pp. 501-511
    • Sun, S.C.1
  • 72
    • 42049108221 scopus 로고    scopus 로고
    • Cell biology: SUMO
    • Meulmeester E., and Melchior F. Cell biology: SUMO. Nature 452 (2008) 709-711
    • (2008) Nature , vol.452 , pp. 709-711
    • Meulmeester, E.1    Melchior, F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.