메뉴 건너뛰기




Volumn 246, Issue 1, 2012, Pages 183-192

NF-κB and chromatin: Ten years on the path from basic mechanisms to candidate drugs

Author keywords

Monocytes macrophages; Signal transduction; Transcription factors

Indexed keywords

DNA; HISTONE H3; I KAPPA B KINASE ALPHA; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERLEUKIN 4; LIPOPOLYSACCHARIDE; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 14; MITOGEN ACTIVATED PROTEIN KINASE 3; MYELOID DIFFERENTIATION FACTOR 88; TOLL LIKE RECEPTOR 3; TOLL LIKE RECEPTOR 4; TRANSCRIPTION FACTOR REL; UNTRANSLATED RNA;

EID: 84858734708     PISSN: 01052896     EISSN: 1600065X     Source Type: Journal    
DOI: 10.1111/j.1600-065X.2012.01103.x     Document Type: Article
Times cited : (56)

References (91)
  • 1
    • 0023724778 scopus 로고
    • I kappa B: a specific inhibitor of the NF-kappa B transcription factor
    • Baeuerle PA, Baltimore D. I kappa B: a specific inhibitor of the NF-kappa B transcription factor. Science 1988;242:540-546.
    • (1988) Science , vol.242 , pp. 540-546
    • Baeuerle, P.A.1    Baltimore, D.2
  • 2
    • 0025304791 scopus 로고
    • Purified human I kappa B can rapidly dissociate the complex of the NF-kappa B transcription factor with its cognate DNA
    • Zabel U, Baeuerle PA. Purified human I kappa B can rapidly dissociate the complex of the NF-kappa B transcription factor with its cognate DNA. Cell 1990;61:255-265.
    • (1990) Cell , vol.61 , pp. 255-265
    • Zabel, U.1    Baeuerle, P.A.2
  • 3
    • 84858744393 scopus 로고    scopus 로고
    • It takes two to tango: IkBs, the multifunctional partners of NF-κB
    • Hinz M, Arslan SC, Scheidereit C. It takes two to tango: IkBs, the multifunctional partners of NF-κB. Immunol Rev 2012;246:59-76.
    • (2012) Immunol Rev , vol.246 , pp. 59-76
    • Hinz, M.1    Arslan, S.C.2    Scheidereit, C.3
  • 4
    • 0027176524 scopus 로고
    • Rapid proteolysis of I kappa B-alpha is necessary for activation of transcription factor NF-kappa B
    • Henkel T, Machleidt T, Alkalay I, Kronke M, Ben-Neriah Y, Baeuerle PA. Rapid proteolysis of I kappa B-alpha is necessary for activation of transcription factor NF-kappa B. Nature 1993;365:182-185.
    • (1993) Nature , vol.365 , pp. 182-185
    • Henkel, T.1    Machleidt, T.2    Alkalay, I.3    Kronke, M.4    Ben-Neriah, Y.5    Baeuerle, P.A.6
  • 5
    • 0028986075 scopus 로고
    • Control of I kappa B-alpha proteolysis by site-specific, signal-induced phosphorylation
    • Brown K, Gerstberger S, Carlson L, Franzoso G, Siebenlist U. Control of I kappa B-alpha proteolysis by site-specific, signal-induced phosphorylation. Science 1995;267:1485-1488.
    • (1995) Science , vol.267 , pp. 1485-1488
    • Brown, K.1    Gerstberger, S.2    Carlson, L.3    Franzoso, G.4    Siebenlist, U.5
  • 6
    • 84858739354 scopus 로고    scopus 로고
    • Regulation of NFkB by ubiquitination and degradation of the IkBs
    • Kanarek N, Ben-Neriah Y. Regulation of NFkB by ubiquitination and degradation of the IkBs. Immunol Rev 2012;246:77-94.
    • (2012) Immunol Rev , vol.246 , pp. 77-94
    • Kanarek, N.1    Ben-Neriah, Y.2
  • 7
    • 0027168447 scopus 로고
    • NF-kappa B controls expression of inhibitor I kappa B alpha: evidence for an inducible autoregulatory pathway
    • Sun SC, Ganchi PA, Ballard DW, Greene WC. NF-kappa B controls expression of inhibitor I kappa B alpha: evidence for an inducible autoregulatory pathway. Science 1993;259:1912-1915.
    • (1993) Science , vol.259 , pp. 1912-1915
    • Sun, S.C.1    Ganchi, P.A.2    Ballard, D.W.3    Greene, W.C.4
  • 8
    • 0028967819 scopus 로고
    • Inducible nuclear expression of newly synthesized I kappa B alpha negatively regulates DNA-binding and transcriptional activities of NF-kappa B
    • Arenzana-Seisdedos F, Thompson J, Rodriguez MS, Bachelerie F, Thomas D, Hay RT. Inducible nuclear expression of newly synthesized I kappa B alpha negatively regulates DNA-binding and transcriptional activities of NF-kappa B. Mol Cell Biol 1995;15:2689-2696.
    • (1995) Mol Cell Biol , vol.15 , pp. 2689-2696
    • Arenzana-Seisdedos, F.1    Thompson, J.2    Rodriguez, M.S.3    Bachelerie, F.4    Thomas, D.5    Hay, R.T.6
  • 9
    • 0032217268 scopus 로고    scopus 로고
    • The crystal structure of the IkappaBalpha/NF-kappaB complex reveals mechanisms of NF-kappaB inactivation
    • Huxford T, Huang DB, Malek S, Ghosh G. The crystal structure of the IkappaBalpha/NF-kappaB complex reveals mechanisms of NF-kappaB inactivation. Cell 1998;95:759-770.
    • (1998) Cell , vol.95 , pp. 759-770
    • Huxford, T.1    Huang, D.B.2    Malek, S.3    Ghosh, G.4
  • 10
    • 0030610362 scopus 로고    scopus 로고
    • A cytokine-responsive IkappaB kinase that activates the transcription factor NF-kappaB
    • DiDonato JA, Hayakawa M, Rothwarf DM, Zandi E, Karin M. A cytokine-responsive IkappaB kinase that activates the transcription factor NF-kappaB. Nature 1997;388:548-554.
    • (1997) Nature , vol.388 , pp. 548-554
    • DiDonato, J.A.1    Hayakawa, M.2    Rothwarf, D.M.3    Zandi, E.4    Karin, M.5
  • 12
    • 0030611595 scopus 로고    scopus 로고
    • IkappaB kinase-beta: NF-kappaB activation and complex formation with IkappaB kinase-alpha and NIK
    • Woronicz JD, Gao X, Cao Z, Rothe M, Goeddel DV. IkappaB kinase-beta: NF-kappaB activation and complex formation with IkappaB kinase-alpha and NIK. Science 1997;278:866-869.
    • (1997) Science , vol.278 , pp. 866-869
    • Woronicz, J.D.1    Gao, X.2    Cao, Z.3    Rothe, M.4    Goeddel, D.V.5
  • 13
    • 0030613551 scopus 로고    scopus 로고
    • The IkappaB kinase complex (IKK) contains two kinase subunits, IKKalpha and IKKbeta, necessary for IkappaB phosphorylation and NF-kappaB activation
    • Zandi E, Rothwarf DM, Delhase M, Hayakawa M, Karin M. The IkappaB kinase complex (IKK) contains two kinase subunits, IKKalpha and IKKbeta, necessary for IkappaB phosphorylation and NF-kappaB activation. Cell 1997;91:243-252.
    • (1997) Cell , vol.91 , pp. 243-252
    • Zandi, E.1    Rothwarf, D.M.2    Delhase, M.3    Hayakawa, M.4    Karin, M.5
  • 15
    • 17944401842 scopus 로고    scopus 로고
    • Identification of the receptor component of the IkappaBalpha-ubiquitin ligase
    • Yaron A, et al. Identification of the receptor component of the IkappaBalpha-ubiquitin ligase. Nature 1998;396:590-594.
    • (1998) Nature , vol.396 , pp. 590-594
    • Yaron, A.1
  • 16
    • 38849199203 scopus 로고    scopus 로고
    • Shared principles in NF-kappaB signaling
    • Hayden MS, Ghosh S. Shared principles in NF-kappaB signaling. Cell 2008;132:344-362.
    • (2008) Cell , vol.132 , pp. 344-362
    • Hayden, M.S.1    Ghosh, S.2
  • 17
    • 84863338304 scopus 로고    scopus 로고
    • Ubiquitination in signaling to and activation of IKK
    • Chen ZJ. Ubiquitination in signaling to and activation of IKK. Immunol Rev 2012;246:95-106.
    • (2012) Immunol Rev , vol.246 , pp. 95-106
    • Chen, Z.J.1
  • 18
    • 0030831210 scopus 로고    scopus 로고
    • A human homologue of the Drosophila Toll protein signals activation of adaptive immunity
    • Medzhitov R, Preston-Hurlburt P, Janeway CA Jr. A human homologue of the Drosophila Toll protein signals activation of adaptive immunity. Nature 1997;388:394-397.
    • (1997) Nature , vol.388 , pp. 394-397
    • Medzhitov, R.1    Preston-Hurlburt, P.2    Janeway Jr., C.A.3
  • 19
    • 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 1998;282:2085-2088.
    • (1998) Science , vol.282 , pp. 2085-2088
    • Poltorak, A.1
  • 20
    • 18244379306 scopus 로고    scopus 로고
    • Interactions of NF-kappaB with chromatin: the art of being at the right place at the right time
    • Natoli G, Saccani S, Bosisio D, Marazzi I. Interactions of NF-kappaB with chromatin: the art of being at the right place at the right time. Nat Immunol 2005;6:439-445.
    • (2005) Nat Immunol , vol.6 , pp. 439-445
    • Natoli, G.1    Saccani, S.2    Bosisio, D.3    Marazzi, I.4
  • 21
    • 77957253048 scopus 로고    scopus 로고
    • Control of NF-kappaB-dependent transcriptional responses by chromatin organization
    • Natoli G. Control of NF-kappaB-dependent transcriptional responses by chromatin organization. Cold Spring Harb Perspect Biol 2009;1:a000224.
    • (2009) Cold Spring Harb Perspect Biol , vol.1
    • Natoli, G.1
  • 23
    • 0033451474 scopus 로고    scopus 로고
    • Rapid and selective remodeling of a positioned nucleosome during the induction of IL-12 p40 transcription
    • Weinmann AS, Plevy SE, Smale ST. Rapid and selective remodeling of a positioned nucleosome during the induction of IL-12 p40 transcription. Immunity 1999;11:665-675.
    • (1999) Immunity , vol.11 , pp. 665-675
    • Weinmann, A.S.1    Plevy, S.E.2    Smale, S.T.3
  • 24
    • 0033064319 scopus 로고    scopus 로고
    • Mapping DNA interaction sites of chromosomal proteins using immunoprecipitation and polymerase chain reaction
    • Hecht A, Grunstein M. Mapping DNA interaction sites of chromosomal proteins using immunoprecipitation and polymerase chain reaction. Methods Enzymol 1999;304:399-414.
    • (1999) Methods Enzymol , vol.304 , pp. 399-414
    • Hecht, A.1    Grunstein, M.2
  • 25
    • 0035908126 scopus 로고    scopus 로고
    • Two waves of nuclear factor kappaB recruitment to target promoters
    • Saccani S, Pantano S, Natoli G. Two waves of nuclear factor kappaB recruitment to target promoters. J Exp Med 2001;193:1351-1359.
    • (2001) J Exp Med , vol.193 , pp. 1351-1359
    • Saccani, S.1    Pantano, S.2    Natoli, G.3
  • 26
    • 32044439558 scopus 로고    scopus 로고
    • Selective and antagonistic functions of SWI/SNF and Mi-2beta nucleosome remodeling complexes during an inflammatory response
    • Ramirez-Carrozzi VR, 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
  • 27
    • 79952539053 scopus 로고    scopus 로고
    • ATP-dependent chromatin remodeling: genetics, genomics and mechanisms
    • Hargreaves DC, Crabtree GR. ATP-dependent chromatin remodeling: genetics, genomics and mechanisms. Cell Res 2011;21:396-420.
    • (2011) Cell Res , vol.21 , pp. 396-420
    • Hargreaves, D.C.1    Crabtree, G.R.2
  • 28
    • 0035997356 scopus 로고    scopus 로고
    • ATP-dependent nucleosome remodeling
    • Becker PB, Horz W. ATP-dependent nucleosome remodeling. Annu Rev Biochem 2002;71:247-273.
    • (2002) Annu Rev Biochem , vol.71 , pp. 247-273
    • Becker, P.B.1    Horz, W.2
  • 29
    • 18644376284 scopus 로고    scopus 로고
    • IRF3 mediates a TLR3/TLR4-specific antiviral gene program
    • Doyle S, et al. IRF3 mediates a TLR3/TLR4-specific antiviral gene program. Immunity 2002;17:251-263.
    • (2002) Immunity , vol.17 , pp. 251-263
    • Doyle, S.1
  • 30
  • 31
    • 45549090987 scopus 로고    scopus 로고
    • Class-specific regulation of pro-inflammatory genes by MyD88 pathways and IkappaBzeta
    • Kayama H, et al. Class-specific regulation of pro-inflammatory genes by MyD88 pathways and IkappaBzeta. J Biol Chem 2008;283:12468-12477.
    • (2008) J Biol Chem , vol.283 , pp. 12468-12477
    • Kayama, H.1
  • 32
    • 0032556894 scopus 로고    scopus 로고
    • Crystal structure of p50/p65 heterodimer of transcription factor NF-kappaB bound to DNA
    • Chen FE, Huang DB, Chen YQ, Ghosh G. Crystal structure of p50/p65 heterodimer of transcription factor NF-kappaB bound to DNA. Nature 1998;391:410-413.
    • (1998) Nature , vol.391 , pp. 410-413
    • Chen, F.E.1    Huang, D.B.2    Chen, Y.Q.3    Ghosh, G.4
  • 33
    • 5644289433 scopus 로고    scopus 로고
    • The histone octamer is invisible when NF-kappaB binds to the nucleosome
    • Angelov D, et al. The histone octamer is invisible when NF-kappaB binds to the nucleosome. J Biol Chem 2004;279:42374-42382.
    • (2004) J Biol Chem , vol.279 , pp. 42374-42382
    • Angelov, D.1
  • 34
    • 33747500567 scopus 로고    scopus 로고
    • A genomic code for nucleosome positioning
    • Segal E, et al. A genomic code for nucleosome positioning. Nature 2006;442:772-778.
    • (2006) Nature , vol.442 , pp. 772-778
    • Segal, E.1
  • 35
    • 62649085538 scopus 로고    scopus 로고
    • The DNA-encoded nucleosome organization of a eukaryotic genome
    • Kaplan N, et al. The DNA-encoded nucleosome organization of a eukaryotic genome. Nature 2009;458:362-366.
    • (2009) Nature , vol.458 , pp. 362-366
    • Kaplan, N.1
  • 36
    • 60349089645 scopus 로고    scopus 로고
    • Nucleosome positioning and gene regulation: advances through genomics
    • Jiang C, Pugh BF. Nucleosome positioning and gene regulation: advances through genomics. Nat Rev Genet 2009;10:161-172.
    • (2009) Nat Rev Genet , vol.10 , pp. 161-172
    • Jiang, C.1    Pugh, B.F.2
  • 38
    • 67649669255 scopus 로고    scopus 로고
    • A unifying model for the selective regulation of inducible transcription by CpG islands and nucleosome remodeling
    • Ramirez-Carrozzi VR, et al. A unifying model for the selective regulation of inducible transcription by CpG islands and nucleosome remodeling. Cell 2009;138:114-128.
    • (2009) Cell , vol.138 , pp. 114-128
    • Ramirez-Carrozzi, V.R.1
  • 39
    • 67649648237 scopus 로고    scopus 로고
    • Control of inducible gene expression by signal-dependent transcriptional elongation
    • Hargreaves DC, Horng T, Medzhitov R. Control of inducible gene expression by signal-dependent transcriptional elongation. Cell 2009;138:129-145.
    • (2009) Cell , vol.138 , pp. 129-145
    • Hargreaves, D.C.1    Horng, T.2    Medzhitov, R.3
  • 40
    • 79956330964 scopus 로고    scopus 로고
    • CpG islands and the regulation of transcription
    • Deaton AM, Bird A. CpG islands and the regulation of transcription. Genes Dev 2011;25:1010-1022.
    • (2011) Genes Dev , vol.25 , pp. 1010-1022
    • Deaton, A.M.1    Bird, A.2
  • 41
    • 77952908743 scopus 로고    scopus 로고
    • A large fraction of extragenic RNA pol II transcription sites overlap enhancers
    • De Santa F, et al. A large fraction of extragenic RNA pol II transcription sites overlap enhancers. PLoS Biol 2010;8:e1000384.
    • (2010) PLoS Biol , vol.8
    • De Santa, F.1
  • 42
    • 77951116072 scopus 로고    scopus 로고
    • CpG islands influence chromatin structure via the CpG-binding protein Cfp1
    • Thomson JP, et al. CpG islands influence chromatin structure via the CpG-binding protein Cfp1. Nature 2010;464:1082-1086.
    • (2010) Nature , vol.464 , pp. 1082-1086
    • Thomson, J.P.1
  • 43
    • 29244438472 scopus 로고    scopus 로고
    • CpG-binding protein (CXXC finger protein 1) is a component of the mammalian Set1 histone H3-Lys4 methyltransferase complex, the analogue of the yeast Set1/COMPASS complex
    • Lee JH, Skalnik DG. CpG-binding protein (CXXC finger protein 1) is a component of the mammalian Set1 histone H3-Lys4 methyltransferase complex, the analogue of the yeast Set1/COMPASS complex. J Biol Chem 2005;280:41725-41731.
    • (2005) J Biol Chem , vol.280 , pp. 41725-41731
    • Lee, J.H.1    Skalnik, D.G.2
  • 44
    • 77949971595 scopus 로고    scopus 로고
    • Selective transcription in response to an inflammatory stimulus
    • Smale ST. Selective transcription in response to an inflammatory stimulus. Cell 2010;140:833-844.
    • (2010) Cell , vol.140 , pp. 833-844
    • Smale, S.T.1
  • 45
    • 66149122282 scopus 로고    scopus 로고
    • Two modes of transcriptional activation at native promoters by NF-kappaB p65
    • van Essen D, Engist B, Natoli G, Saccani S. Two modes of transcriptional activation at native promoters by NF-kappaB p65. PLoS Biol 2009;7:e73.
    • (2009) PLoS Biol , vol.7
    • van Essen, D.1    Engist, B.2    Natoli, G.3    Saccani, S.4
  • 46
    • 77949977555 scopus 로고    scopus 로고
    • Identification and characterization of enhancers controlling the inflammatory gene expression program in macrophages
    • Ghisletti S, et al. Identification and characterization of enhancers controlling the inflammatory gene expression program in macrophages. Immunity 2010;32:317-328.
    • (2010) Immunity , vol.32 , pp. 317-328
    • Ghisletti, S.1
  • 47
    • 77952567987 scopus 로고    scopus 로고
    • Simple combinations of lineage-determining transcription factors prime cis-regulatory elements required for macrophage and B cell identities
    • Heinz S, et al. Simple combinations of lineage-determining transcription factors prime cis-regulatory elements required for macrophage and B cell identities. Mol Cell 2010;38:576-589.
    • (2010) Mol Cell , vol.38 , pp. 576-589
    • Heinz, S.1
  • 48
    • 0028136726 scopus 로고
    • Requirement of transcription factor PU.1 in the development of multiple hematopoietic lineages
    • Scott EW, Simon MC, Anastasi J, Singh H. Requirement of transcription factor PU.1 in the development of multiple hematopoietic lineages. Science 1994;265:1573-1577.
    • (1994) Science , vol.265 , pp. 1573-1577
    • Scott, E.W.1    Simon, M.C.2    Anastasi, J.3    Singh, H.4
  • 49
    • 0030069058 scopus 로고    scopus 로고
    • Terminal myeloid gene expression and differentiation requires the transcription factor PU.1
    • Simon MC, Olson M, Scott E, Hack A, Su G, Singh H. Terminal myeloid gene expression and differentiation requires the transcription factor PU.1. Curr Top Microbiol Immunol 1996;211:113-119.
    • (1996) Curr Top Microbiol Immunol , vol.211 , pp. 113-119
    • Simon, M.C.1    Olson, M.2    Scott, E.3    Hack, A.4    Su, G.5    Singh, H.6
  • 50
    • 0032146794 scopus 로고    scopus 로고
    • PU.1 induces myeloid lineage commitment in multipotent hematopoietic progenitors
    • Nerlov C, Graf T. PU.1 induces myeloid lineage commitment in multipotent hematopoietic progenitors. Genes Dev 1998;12:2403-2412.
    • (1998) Genes Dev , vol.12 , pp. 2403-2412
    • Nerlov, C.1    Graf, T.2
  • 51
    • 78650210727 scopus 로고    scopus 로고
    • Bcl-6 and NF-κB cistromes mediate opposing regulation of the innate immune response
    • Barish GD, et al. Bcl-6 and NF-κB cistromes mediate opposing regulation of the innate immune response. Genes Dev 2010;24:2760-2765.
    • (2010) Genes Dev , vol.24 , pp. 2760-2765
    • Barish, G.D.1
  • 52
    • 77954928774 scopus 로고    scopus 로고
    • Maintaining cell identity through global control of genomic organization
    • Natoli G. Maintaining cell identity through global control of genomic organization. Immunity 2010;33:12-24.
    • (2010) Immunity , vol.33 , pp. 12-24
    • Natoli, G.1
  • 53
    • 77950339177 scopus 로고    scopus 로고
    • Conservation and regulatory associations of a wide affinity range of mouse transcription factor binding sites
    • Jaeger SA, Chan ET, Berger MF, Stottmann R, Hughes TR, Bulyk ML. Conservation and regulatory associations of a wide affinity range of mouse transcription factor binding sites. Genomics 2010;95:185-195.
    • (2010) Genomics , vol.95 , pp. 185-195
    • Jaeger, S.A.1    Chan, E.T.2    Berger, M.F.3    Stottmann, R.4    Hughes, T.R.5    Bulyk, M.L.6
  • 54
    • 77954954652 scopus 로고    scopus 로고
    • Genome-wide analysis of ETS-family DNA-binding in vitro and in vivo
    • Wei GH, et al. Genome-wide analysis of ETS-family DNA-binding in vitro and in vivo. EMBO J 2010;29:2147-2160.
    • (2010) EMBO J , vol.29 , pp. 2147-2160
    • Wei, G.H.1
  • 55
    • 33847076849 scopus 로고    scopus 로고
    • Chromatin modifications and their function
    • Kouzarides T. Chromatin modifications and their function. Cell 2007;128:693-705.
    • (2007) Cell , vol.128 , pp. 693-705
    • Kouzarides, T.1
  • 56
    • 0027465862 scopus 로고
    • A positive role for histone acetylation in transcription factor access to nucleosomal DNA
    • Lee DY, Hayes JJ, Pruss D, Wolffe AP. A positive role for histone acetylation in transcription factor access to nucleosomal DNA. Cell 1993;72:73-84.
    • (1993) Cell , vol.72 , pp. 73-84
    • Lee, D.Y.1    Hayes, J.J.2    Pruss, D.3    Wolffe, A.P.4
  • 57
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl BD, Allis CD. The language of covalent histone modifications. Nature 2000;403:41-45.
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 58
    • 35848961668 scopus 로고    scopus 로고
    • How chromatin-binding modules interpret histone modifications: lessons from professional pocket pickers
    • Taverna SD, Li H, Ruthenburg AJ, Allis CD, Patel DJ. How chromatin-binding modules interpret histone modifications: lessons from professional pocket pickers. Nat Struct Mol Biol 2007;14:1025-1040.
    • (2007) Nat Struct Mol Biol , vol.14 , pp. 1025-1040
    • Taverna, S.D.1    Li, H.2    Ruthenburg, A.J.3    Allis, C.D.4    Patel, D.J.5
  • 59
    • 34249026300 scopus 로고    scopus 로고
    • High-resolution profiling of histone methylations in the human genome
    • Barski A, et al. High-resolution profiling of histone methylations in the human genome. Cell 2007;129:823-837.
    • (2007) Cell , vol.129 , pp. 823-837
    • Barski, A.1
  • 60
    • 34547624303 scopus 로고    scopus 로고
    • Genome-wide maps of chromatin state in pluripotent and lineage-committed cells
    • Mikkelsen TS, et al. Genome-wide maps of chromatin state in pluripotent and lineage-committed cells. Nature 2007;448:553-560.
    • (2007) Nature , vol.448 , pp. 553-560
    • Mikkelsen, T.S.1
  • 62
    • 0036712454 scopus 로고    scopus 로고
    • Dynamic changes in histone H3 Lys 9 methylation occurring at tightly regulated inducible inflammatory genes
    • Saccani S, Natoli G. Dynamic changes in histone H3 Lys 9 methylation occurring at tightly regulated inducible inflammatory genes. Genes Dev 2002;16:2219-2224.
    • (2002) Genes Dev , vol.16 , pp. 2219-2224
    • Saccani, S.1    Natoli, G.2
  • 63
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • Jenuwein T, Allis CD. Translating the histone code. Science 2001;293:1074-1080.
    • (2001) Science , vol.293 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 64
    • 0015296118 scopus 로고
    • The distribution and turnover of labeled methyl groups in histone fractions of cultured mammalian cells
    • Byvoet P, Shepherd GR, Hardin JM, Noland BJ. The distribution and turnover of labeled methyl groups in histone fractions of cultured mammalian cells. Arch Biochem Biophys 1972;148:558-567.
    • (1972) Arch Biochem Biophys , vol.148 , pp. 558-567
    • Byvoet, P.1    Shepherd, G.R.2    Hardin, J.M.3    Noland, B.J.4
  • 65
    • 11144332565 scopus 로고    scopus 로고
    • Histone demethylation mediated by the nuclear amine oxidase homolog LSD1
    • Shi Y, et al. Histone demethylation mediated by the nuclear amine oxidase homolog LSD1. Cell 2004;119:941-953.
    • (2004) Cell , vol.119 , pp. 941-953
    • Shi, Y.1
  • 66
    • 43249102851 scopus 로고    scopus 로고
    • Erasing the methyl mark: histone demethylases at the center of cellular differentiation and disease
    • Cloos PA, Christensen J, Agger K, Helin K. Erasing the methyl mark: histone demethylases at the center of cellular differentiation and disease. Genes Dev 2008;22:1115-1140.
    • (2008) Genes Dev , vol.22 , pp. 1115-1140
    • Cloos, P.A.1    Christensen, J.2    Agger, K.3    Helin, K.4
  • 67
    • 77956541159 scopus 로고    scopus 로고
    • A feed-forward circuit controlling inducible NF-kappaB target gene activation by promoter histone demethylation
    • van Essen D, Zhu Y, Saccani S. A feed-forward circuit controlling inducible NF-kappaB target gene activation by promoter histone demethylation. Mol Cell 2010;39:750-760.
    • (2010) Mol Cell , vol.39 , pp. 750-760
    • van Essen, D.1    Zhu, Y.2    Saccani, S.3
  • 69
    • 34548644772 scopus 로고    scopus 로고
    • The histone H3 lysine-27 demethylase Jmjd3 links inflammation to inhibition of polycomb-mediated gene silencing
    • De Santa F, Totaro MG, Prosperini E, Notarbartolo S, Testa G, Natoli G. The histone H3 lysine-27 demethylase Jmjd3 links inflammation to inhibition of polycomb-mediated gene silencing. Cell 2007;130:1083-1094.
    • (2007) Cell , vol.130 , pp. 1083-1094
    • De Santa, F.1    Totaro, M.G.2    Prosperini, E.3    Notarbartolo, S.4    Testa, G.5    Natoli, G.6
  • 70
    • 70350754328 scopus 로고    scopus 로고
    • Jmjd3 contributes to the control of gene expression in LPS-activated macrophages
    • De Santa F, et al. Jmjd3 contributes to the control of gene expression in LPS-activated macrophages. EMBO J 2009;28:3341-3352.
    • (2009) EMBO J , vol.28 , pp. 3341-3352
    • De Santa, F.1
  • 71
    • 77956954197 scopus 로고    scopus 로고
    • The Jmjd3-Irf4 axis regulates M2 macrophage polarization and host responses against helminth infection
    • Satoh T, et al. The Jmjd3-Irf4 axis regulates M2 macrophage polarization and host responses against helminth infection. Nat Immunol 2010;11:936-944.
    • (2010) Nat Immunol , vol.11 , pp. 936-944
    • Satoh, T.1
  • 72
    • 70350435962 scopus 로고    scopus 로고
    • Epigenetic regulation of the alternatively activated macrophage phenotype
    • Ishii M, et al. Epigenetic regulation of the alternatively activated macrophage phenotype. Blood 2009;114:3244-3254.
    • (2009) Blood , vol.114 , pp. 3244-3254
    • Ishii, M.1
  • 73
    • 19944431570 scopus 로고    scopus 로고
    • Arginine methyltransferase CARM1 is a promoter-specific regulator of NF-kappaB-dependent gene expression
    • Covic M, et al. Arginine methyltransferase CARM1 is a promoter-specific regulator of NF-kappaB-dependent gene expression. EMBO J 2005;24:85-96.
    • (2005) EMBO J , vol.24 , pp. 85-96
    • Covic, M.1
  • 74
    • 70350719193 scopus 로고    scopus 로고
    • CARM1 but not its enzymatic activity is required for transcriptional coactivation of NF-kappaB-dependent gene expression
    • Jayne S, Rothgiesser KM, Hottiger MO. CARM1 but not its enzymatic activity is required for transcriptional coactivation of NF-kappaB-dependent gene expression. J Mol Biol 2009;394:485-495.
    • (2009) J Mol Biol , vol.394 , pp. 485-495
    • Jayne, S.1    Rothgiesser, K.M.2    Hottiger, M.O.3
  • 75
    • 0025872683 scopus 로고
    • Rapid histone H3 phosphorylation in response to growth factors, phorbol esters, okadaic acid, and protein synthesis inhibitors
    • Mahadevan LC, Willis AC, Barratt MJ. Rapid histone H3 phosphorylation in response to growth factors, phorbol esters, okadaic acid, and protein synthesis inhibitors. Cell 1991;65:775-783.
    • (1991) Cell , vol.65 , pp. 775-783
    • Mahadevan, L.C.1    Willis, A.C.2    Barratt, M.J.3
  • 76
    • 0033200205 scopus 로고    scopus 로고
    • The nucleosomal response associated with immediate-early gene induction is mediated via alternative MAP kinase cascades: MSK1 as a potential histone H3/HMG-14 kinase
    • Thomson S, Clayton AL, Hazzalin CA, Rose S, Barratt MJ, Mahadevan LC. The nucleosomal response associated with immediate-early gene induction is mediated via alternative MAP kinase cascades: MSK1 as a potential histone H3/HMG-14 kinase. EMBO J 1999;18:4779-4793.
    • (1999) EMBO J , vol.18 , pp. 4779-4793
    • Thomson, S.1    Clayton, A.L.2    Hazzalin, C.A.3    Rose, S.4    Barratt, M.J.5    Mahadevan, L.C.6
  • 77
    • 0034679625 scopus 로고    scopus 로고
    • Phosphoacetylation of histone H3 on c-fos- and c-jun-associated nucleosomes upon gene activation
    • Clayton AL, Rose S, Barratt MJ, Mahadevan LC. Phosphoacetylation of histone H3 on c-fos- and c-jun-associated nucleosomes upon gene activation. EMBO J 2000;19:3714-3726.
    • (2000) EMBO J , vol.19 , pp. 3714-3726
    • Clayton, A.L.1    Rose, S.2    Barratt, M.J.3    Mahadevan, L.C.4
  • 78
    • 0036143654 scopus 로고    scopus 로고
    • p38-Dependent marking of inflammatory genes for increased NF-kappa B recruitment
    • Saccani S, Pantano S, Natoli G. p38-Dependent marking of inflammatory genes for increased NF-kappa B recruitment. Nat Immunol 2002;3:69-75.
    • (2002) Nat Immunol , vol.3 , pp. 69-75
    • Saccani, S.1    Pantano, S.2    Natoli, G.3
  • 79
    • 24944554790 scopus 로고    scopus 로고
    • Signaling pathways and genes that inhibit pathogen-induced macrophage apoptosis - CREB and NF-kappaB as key regulators
    • Park JM, et al. Signaling pathways and genes that inhibit pathogen-induced macrophage apoptosis - CREB and NF-kappaB as key regulators. Immunity 2005;23:319-329.
    • (2005) Immunity , vol.23 , pp. 319-329
    • Park, J.M.1
  • 81
    • 0038511129 scopus 로고    scopus 로고
    • Histone H3 phosphorylation by IKK-alpha is critical for cytokine-induced gene expression
    • Yamamoto Y, Verma UN, Prajapati S, Kwak YT, Gaynor RB. Histone H3 phosphorylation by IKK-alpha is critical for cytokine-induced gene expression. Nature 2003;423:655-659.
    • (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
  • 82
    • 15944379896 scopus 로고    scopus 로고
    • Formation of an IKKalpha-dependent transcription complex is required for estrogen receptor-mediated gene activation
    • Park KJ, Krishnan V, O'Malley BW, Yamamoto Y, Gaynor RB. Formation of an IKKalpha-dependent transcription complex is required for estrogen receptor-mediated gene activation. Mol Cell 2005;18:71-82.
    • (2005) Mol Cell , vol.18 , pp. 71-82
    • Park, K.J.1    Krishnan, V.2    O'Malley, B.W.3    Yamamoto, Y.4    Gaynor, R.B.5
  • 83
    • 34247274248 scopus 로고    scopus 로고
    • Nuclear cytokine-activated IKKalpha controls prostate cancer metastasis by repressing Maspin
    • Luo JL, et al. Nuclear cytokine-activated IKKalpha controls prostate cancer metastasis by repressing Maspin. Nature 2007;446:690-694.
    • (2007) Nature , vol.446 , pp. 690-694
    • Luo, J.L.1
  • 84
    • 40649097065 scopus 로고    scopus 로고
    • IKKalpha is a critical coregulator of a Smad4-independent TGFbeta-Smad2/3 signaling pathway that controls keratinocyte differentiation
    • Descargues P, et al. IKKalpha is a critical coregulator of a Smad4-independent TGFbeta-Smad2/3 signaling pathway that controls keratinocyte differentiation. Proc Natl Acad Sci U S A 2008;105:2487-2492.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 2487-2492
    • Descargues, P.1
  • 85
    • 55949089769 scopus 로고    scopus 로고
    • The tumor suppressor activity of IKKalpha in stratified epithelia is exerted in part via the TGF-beta antiproliferative pathway
    • Marinari B, et al. The tumor suppressor activity of IKKalpha in stratified epithelia is exerted in part via the TGF-beta antiproliferative pathway. Proc Natl Acad Sci U S A 2008;105:17091-17096.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 17091-17096
    • Marinari, B.1
  • 86
    • 24644433852 scopus 로고    scopus 로고
    • Enhanced NF-kappaB activation and cellular function in macrophages lacking IkappaB kinase 1 (IKK1)
    • Li Q, et al. Enhanced NF-kappaB activation and cellular function in macrophages lacking IkappaB kinase 1 (IKK1). Proc Natl Acad Sci U S A 2005;102:12425-12430.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 12425-12430
    • Li, Q.1
  • 87
    • 17844386319 scopus 로고    scopus 로고
    • IKKalpha limits macrophage NF-kappaB activation and contributes to the resolution of inflammation
    • Lawrence T, Bebien M, Liu GY, Nizet V, Karin M. IKKalpha limits macrophage NF-kappaB activation and contributes to the resolution of inflammation. Nature 2005;434:1138-1143.
    • (2005) Nature , vol.434 , pp. 1138-1143
    • Lawrence, T.1    Bebien, M.2    Liu, G.Y.3    Nizet, V.4    Karin, M.5
  • 88
    • 78651479749 scopus 로고    scopus 로고
    • The genomic landscapes of inflammation
    • Natoli G, Ghisletti S, Barozzi I. The genomic landscapes of inflammation. Genes Dev 2011;25:101-106.
    • (2011) Genes Dev , vol.25 , pp. 101-106
    • Natoli, G.1    Ghisletti, S.2    Barozzi, I.3
  • 89
    • 80051988785 scopus 로고    scopus 로고
    • Hierarchies of NF-kappaB target-gene regulation
    • Smale ST. Hierarchies of NF-kappaB target-gene regulation. Nat Immunol 2011;12:689-694.
    • (2011) Nat Immunol , vol.12 , pp. 689-694
    • Smale, S.T.1
  • 90
    • 24144465889 scopus 로고    scopus 로고
    • Molecular determinants of crosstalk between nuclear receptors and toll-like receptors
    • Ogawa S, et al. Molecular determinants of crosstalk between nuclear receptors and toll-like receptors. Cell 2005;122:707-721.
    • (2005) Cell , vol.122 , pp. 707-721
    • Ogawa, S.1
  • 91
    • 78650806593 scopus 로고    scopus 로고
    • Suppression of inflammation by a synthetic histone mimic
    • Nicodeme E, et al. Suppression of inflammation by a synthetic histone mimic. Nature 2010;468:1119-1123.
    • (2010) Nature , vol.468 , pp. 1119-1123
    • Nicodeme, E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.