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Volumn 434, Issue 7037, 2005, Pages 1138-1143

IKKα limits macrophage NF-κB activation and contributes to the resolution of inflammation

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; CYTOLOGY; DISEASES; ENZYMES; GENES; MICROORGANISMS;

EID: 17844386319     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature03491     Document Type: Article
Times cited : (576)

References (30)
  • 1
    • 0036779617 scopus 로고    scopus 로고
    • Anti-inflammatory lipid mediators and insights into the resolution of inflammation
    • Lawrence, T., Willoughby, D. A. & Gilroy, D. W. Anti-inflammatory lipid mediators and insights into the resolution of inflammation. Nature Rev. Immunol. 2, 787-795 (2002).
    • (2002) Nature Rev. Immunol. , vol.2 , pp. 787-795
    • Lawrence, T.1    Willoughby, D.A.2    Gilroy, D.W.3
  • 2
    • 2342464085 scopus 로고    scopus 로고
    • The two NF-κB activation pathways and their role in innate and adaptive immunity
    • Bonizzi, G. & Karin, M. The two NF-κB activation pathways and their role in innate and adaptive immunity. Trends Immunol. 25, 280-288 (2004).
    • (2004) Trends Immunol. , vol.25 , pp. 280-288
    • Bonizzi, G.1    Karin, M.2
  • 3
    • 0034084163 scopus 로고    scopus 로고
    • Phosphorylation meets ubiquitination: The control of NF-κB activity
    • Karin, M. & Ben-Neriah, Y. Phosphorylation meets ubiquitination: the control of NF-κB activity. Annu. Rev. Immunol. 18, 621-663 (2000).
    • (2000) Annu. Rev. Immunol. , vol.18 , pp. 621-663
    • Karin, M.1    Ben-Neriah, Y.2
  • 4
    • 0037044575 scopus 로고    scopus 로고
    • The IκB-NF-κB signaling module: Temporal control and selective gene activation
    • Hoffmann, A., Levchenko, A., Scott, M. L. & Baltimore, D. The IκB-NF-κB signaling module: temporal control and selective gene activation. Science 298, 1241-1245 (2002).
    • (2002) Science , vol.298 , pp. 1241-1245
    • Hoffmann, A.1    Levchenko, A.2    Scott, M.L.3    Baltimore, D.4
  • 5
    • 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, 694-699 (2004).
    • (2004) Nature , vol.430 , pp. 694-699
    • Wertz, I.E.1
  • 6
    • 0036234459 scopus 로고    scopus 로고
    • Missing pieces in the NF-κB puzzle
    • Ghosh, S. & Karin, M. Missing pieces in the NF-κB puzzle. Cell 109 (suppl.), S81-S96 (2002).
    • (2002) Cell , vol.109 , Issue.SUPPL.
    • Ghosh, S.1    Karin, M.2
  • 7
    • 0033634663 scopus 로고    scopus 로고
    • Female mice heterozygous for IKKγ/NEMO deficiencies develop a dermatopathy similar to the human X-linked disorder incontinentia pigmenti
    • Makris, C. et al. Female mice heterozygous for IKKγ/NEMO deficiencies develop a dermatopathy similar to the human X-linked disorder incontinentia pigmenti. Mol. Cell 5, 969-979 (2000).
    • (2000) Mol Cell , vol.5 , pp. 969-979
    • Makris, C.1
  • 8
    • 18644380147 scopus 로고    scopus 로고
    • The lymphotoxin-beta receptor induces different patterns of gene expression via two NF-κB pathways
    • Dejardin, E. et al. The lymphotoxin-beta receptor induces different patterns of gene expression via two NF-κB pathways. Immunity 17, 525-535 (2002).
    • (2002) Immunity , vol.17 , pp. 525-535
    • Dejardin, E.1
  • 9
    • 17944378526 scopus 로고    scopus 로고
    • Activation by IKKα of a second, evolutionary conserved, NF-κB signaling pathway
    • Senftleben, U. et al. Activation by IKKα of a second, evolutionary conserved, NF-κB signaling pathway. Science 293, 1495-1499 (2001).
    • (2001) Science , vol.293 , pp. 1495-1499
    • Senftleben, U.1
  • 10
    • 0037497184 scopus 로고    scopus 로고
    • A nucleosomal function for IκB kinase-α in NF-κB-dependent gene expression
    • Anest, V. et al. A nucleosomal function for IκB kinase-α in NF-κB-dependent gene expression. Nature 423, 659-663 (2003).
    • (2003) Nature , vol.423 , pp. 659-663
    • Anest, V.1
  • 11
    • 0038511129 scopus 로고    scopus 로고
    • Histone H3 phosphorylation by IKK-α is critical for cytokine-induced gene expression
    • Yamamoto, Y., Verma, U. N., Prajapati, S., Kwak, Y. T. & Gaynor, R. B. Histone H3 phosphorylation by IKK-α is critical for cytokine-induced gene expression. Nature 423, 655-659 (2003).
    • (2003) Nature , vol.423 , pp. 655-659
    • Yamamoto, Y.1    Verma, U.N.2    Prajapati, S.3    Kwak, Y.T.4    Gaynor, R.B.5
  • 12
    • 5144229510 scopus 로고    scopus 로고
    • Sword and shield: Linked group B streptococcal β-hemolysin/cytolysin and carotenoid pigment function to subvert host phagocyte defense
    • Liu, G. Y. et al. Sword and shield: Linked group B streptococcal β-hemolysin/cytolysin and carotenoid pigment function to subvert host phagocyte defense. Proc. Natl. Acad. Sci. USA 101, 14491-14496 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 14491-14496
    • Liu, G.Y.1
  • 13
    • 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
  • 14
    • 0033592748 scopus 로고    scopus 로고
    • The Toll-like receptor 2 is recruited to macrophage phagosomes and discriminates between pathogens
    • Underbill, D. M. et al. The Toll-like receptor 2 is recruited to macrophage phagosomes and discriminates between pathogens. Nature 401, 811-815 (1999).
    • (1999) Nature , vol.401 , pp. 811-815
    • Underbill, D.M.1
  • 15
    • 9144275033 scopus 로고    scopus 로고
    • Activation of IKKα target genes depends on recognition of specific kappaB binding sites by RelB:p52 dimers
    • Bonizzi, G. et al. Activation of IKKα target genes depends on recognition of specific kappaB binding sites by RelB:p52 dimers. EMBO J. 23, 4202-4210 (2004).
    • (2004) EMBO J. , vol.23 , pp. 4202-4210
    • Bonizzi, G.1
  • 16
    • 0037184995 scopus 로고    scopus 로고
    • Pattern recognition receptors: Doubling up for the innate immune response
    • Gordon, S. Pattern recognition receptors: doubling up for the innate immune response. Cell 111, 927-930 (2002).
    • (2002) Cell , vol.111 , pp. 927-930
    • Gordon, S.1
  • 17
    • 0037144590 scopus 로고    scopus 로고
    • Macrophage apoptosis by anthrax lethal factor through p38 MAP kinase inhibition
    • Park, J. M., Greten, F. R., Li, Z. W. & Karin, M. Macrophage apoptosis by anthrax lethal factor through p38 MAP kinase inhibition. Science 297, 2048-2051 (2002).
    • (2002) Science , vol.297 , pp. 2048-2051
    • Park, J.M.1    Greten, F.R.2    Li, Z.W.3    Karin, M.4
  • 18
    • 3342994912 scopus 로고    scopus 로고
    • Inhibition of nitric oxide synthase exacerbates group B streptococcus sepsis and arthritis in mice
    • Puliti, M., von Hunolstein, C., Bistoni, F., Orefici, G. & Tissi, L. Inhibition of nitric oxide synthase exacerbates group B streptococcus sepsis and arthritis in mice. Infect. Immun. 72, 4891-4894 (2004).
    • (2004) Infect. Immun. , vol.72 , pp. 4891-4894
    • Puliti, M.1    Von Hunolstein, C.2    Bistoni, F.3    Orefici, G.4    Tissi, L.5
  • 19
    • 0141703513 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha-induced IKK phosphorylation of NF-κB p65 on serine 536 is mediated through the TRAF2, TRAF5, and TAK1 signaling pathway
    • Sakurai, H. et al. Tumor necrosis factor-alpha-induced IKK phosphorylation of NF-κB p65 on serine 536 is mediated through the TRAF2, TRAF5, and TAK1 signaling pathway. J. Biol Chem. 278, 36916-36923 (2003).
    • (2003) J. Biol Chem. , vol.278 , pp. 36916-36923
    • Sakurai, H.1
  • 20
    • 0034637610 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha activation of NF-κB requires the phosphorylation of Ser-471 in the transactivation domain of c-Rel
    • Martin, A. G. & Fresno, M. Tumor necrosis factor-alpha activation of NF-κB requires the phosphorylation of Ser-471 in the transactivation domain of c-Rel. J. Biol. Chem. 275, 24383-24391 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 24383-24391
    • Martin, A.G.1    Fresno, M.2
  • 21
    • 0034720191 scopus 로고    scopus 로고
    • cRel-TD kinase: A serine/threonine kinase binding in vivo and in vitro c-Rel and phosphorylating its transactivation domain
    • Fognani, C., Rondi, R., Romano, A. & Blasi, F. cRel-TD kinase: a serine/threonine kinase binding in vivo and in vitro c-Rel and phosphorylating its transactivation domain. Oncogene 19, 2224-2232 (2000).
    • (2000) Oncogene , vol.19 , pp. 2224-2232
    • Fognani, C.1    Rondi, R.2    Romano, A.3    Blasi, F.4
  • 22
    • 0034724166 scopus 로고    scopus 로고
    • Functional overlap of sequences that activate transcription and signal ubiquitin-mediated proteolysis
    • Salghetti, S. E., Muratani, M., Wijnen, H., Futcher, B. & Tansey, W. P. Functional overlap of sequences that activate transcription and signal ubiquitin-mediated proteolysis. Proc. Natl Acad. Sci. USA 97, 3118-3123 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 3118-3123
    • Salghetti, S.E.1    Muratani, M.2    Wijnen, H.3    Futcher, B.4    Tansey, W.P.5
  • 23
    • 1342264315 scopus 로고    scopus 로고
    • A corepressor/coactivator exchange complex required for transcriptional activation by nuclear receptors and other regulated transcription factors
    • Perissi, V., Aggarwal, A., Glass, C. K., Rose, D. W. & Rosenfeld, M. G. A corepressor/coactivator exchange complex required for transcriptional activation by nuclear receptors and other regulated transcription factors. Cell 116, 511-526 (2004).
    • (2004) Cell , vol.116 , pp. 511-526
    • Perissi, V.1    Aggarwal, A.2    Glass, C.K.3    Rose, D.W.4    Rosenfeld, M.G.5
  • 24
    • 3142771914 scopus 로고    scopus 로고
    • Degradation of promoter-bound p65/RelA is essential for the prompt termination of the nuclear factor κB response
    • Saccani, S., Marazzi, I., Beg, A. A. & Natoli, G. Degradation of promoter-bound p65/RelA is essential for the prompt termination of the nuclear factor κB response. J. Exp. Med. 200, 107-113 (2004).
    • (2004) J. Exp. Med. , vol.200 , pp. 107-113
    • Saccani, S.1    Marazzi, I.2    Beg, A.A.3    Natoli, G.4
  • 25
    • 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
  • 26
    • 0032567342 scopus 로고    scopus 로고
    • Degradation of proto-oncoprotein c-Rel by the ubiquitin-proteasome pathway
    • Chen, E. et al. Degradation of proto-oncoprotein c-Rel by the ubiquitin-proteasome pathway. J. Biol. Chem. 273, 35201-35207 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 35201-35207
    • Chen, E.1
  • 27
    • 0028817585 scopus 로고
    • Multiorgan inflammation and hematopoietic abnormalities in mice with a targeted disruption of RelB, a member of the NF-κB/Rel family
    • Weih, F. et al. Multiorgan inflammation and hematopoietic abnormalities in mice with a targeted disruption of RelB, a member of the NF-κB/Rel family. Cell 80, 331-340(1995).
    • (1995) Cell , vol.80 , pp. 331-340
    • Weih, F.1
  • 28
    • 0038771214 scopus 로고    scopus 로고
    • Modulation of NF-κB activity by exchange of dimers
    • Saccani, S., Pantano, S. & Natoli, G. Modulation of NF-κB activity by exchange of dimers. Mol. Cell 11, 1563-1574 (2003).
    • (2003) Mol. Cell , vol.11 , pp. 1563-1574
    • Saccani, S.1    Pantano, S.2    Natoli, G.3
  • 29
    • 0027168447 scopus 로고
    • NF-κB controls expression of inhibitor Iκbα: Evidence for an inducible autoregulatory pathway
    • Sun, S. C., Ganchi, P. A., Ballard, D. W. & Greene, W. C. NF-κB controls expression of inhibitor Iκbα: evidence for an inducible autoregulatory pathway. Science 259, 1912-1915 (1993).
    • (1993) Science , vol.259 , pp. 1912-1915
    • Sun, S.C.1    Ganchi, P.A.2    Ballard, D.W.3    Greene, W.C.4
  • 30
    • 3042523535 scopus 로고    scopus 로고
    • Activation of transcription factor NF-κB requires ELKS, an IκB kinase regulatory subunit
    • Ducut Sigala, J. L. et al. Activation of transcription factor NF-κB requires ELKS, an IκB kinase regulatory subunit. Science 304, 1963-1967 (2004).
    • (2004) Science , vol.304 , pp. 1963-1967
    • Ducut Sigala, J.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.