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Volumn 40, Issue 16, 2012, Pages 7676-7689

Heterochromatin protein 1 gamma and IκB kinase alpha interdependence during tumour necrosis factor gene transcription elongation in activated macrophages

Author keywords

[No Author keywords available]

Indexed keywords

DNA DIRECTED RNA POLYMERASE III; HETEROCHROMATIN PROTEIN 1; HETEROCHROMATIN PROTEIN 1 GAMMA; HISTONE H3; I KAPPA B KINASE ALPHA; SERINE; TUMOR NECROSIS FACTOR; UNCLASSIFIED DRUG;

EID: 84870486222     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gks509     Document Type: Article
Times cited : (32)

References (54)
  • 1
    • 38849199203 scopus 로고    scopus 로고
    • Shared principles in NF-kappaB signaling
    • Hayden, M.S. and Ghosh, S. (2008) Shared principles in NF-kappaB signaling. Cell, 132, 344-362.
    • (2008) Cell , vol.132 , pp. 344-362
    • Hayden, M.S.1    Ghosh, S.2
  • 2
    • 55549140173 scopus 로고    scopus 로고
    • Role of the histone H3 lysine 4 methyltransferase, SET7/9, in the regulation of NF-kappaB-dependent inflammatory genes. Relevance to diabetes and inflammation
    • Li, Y., Reddy, M.A., Miao, F., Shanmugam, N., Yee, J.K., Hawkins, D., Ren, B. and Natarajan, R. (2008) Role of the histone H3 lysine 4 methyltransferase, SET7/9, in the regulation of NF-kappaB-dependent inflammatory genes. Relevance to diabetes and inflammation. J. Biol. Chem., 283, 26771-26781.
    • (2008) J. Biol. Chem. , vol.283 , pp. 26771-26781
    • Li, Y.1    Reddy, M.A.2    Miao, F.3    Shanmugam, N.4    Yee, J.K.5    Hawkins, D.6    Ren, B.7    Natarajan, R.8
  • 3
    • 0032039076 scopus 로고    scopus 로고
    • Phosphorylation of NF-kappa B p65 by PKA stimulates transcriptional activity by promoting a novel bivalent interaction with the coactivator CBP/ p300
    • Zhong, H., Voll, R.E. and Ghosh, S. (1998) Phosphorylation of NF-kappa B p65 by PKA stimulates transcriptional activity by promoting a novel bivalent interaction with the coactivator CBP/ p300. Mol. Cell, 1, 661-671.
    • (1998) Mol. Cell , vol.1 , pp. 661-671
    • Zhong, H.1    Voll, R.E.2    Ghosh, S.3
  • 4
    • 0038790283 scopus 로고    scopus 로고
    • IKKalpha: A chromatin modifier
    • Swaminathan, S. (2003) IKKalpha: a chromatin modifier. Nat. Cell. Biol., 5, 503.
    • (2003) Nat. Cell. Biol. , vol.5 , pp. 503
    • Swaminathan, S.1
  • 5
    • 67649648237 scopus 로고    scopus 로고
    • Control of inducible gene expression by signal-dependent transcriptional elongation
    • Hargreaves, D.C., Horng, T. and Medzhitov, R. (2009) Control of inducible gene expression by signal-dependent transcriptional elongation. Cell, 138, 129-145.
    • (2009) Cell , vol.138 , pp. 129-145
    • Hargreaves, D.C.1    Horng, T.2    Medzhitov, R.3
  • 6
    • 0034741714 scopus 로고    scopus 로고
    • NF-kappaB binds P-TEFb to stimulate transcriptional elongation by RNA polymerase II
    • Barboric, M., Nissen, R.M., Kanazawa, S., Jabrane-Ferrat, N. and Peterlin, B.M. (2001) NF-kappaB binds P-TEFb to stimulate transcriptional elongation by RNA polymerase II. Mol. Cell, 8, 327-337.
    • (2001) Mol. Cell , vol.8 , pp. 327-337
    • Barboric, M.1    Nissen, R.M.2    Kanazawa, S.3    Jabrane-Ferrat, N.4    Peterlin, B.M.5
  • 7
    • 70149112313 scopus 로고    scopus 로고
    • Histone crosstalk between H3S10ph and H4K16ac generates a histone code that mediates transcription elongation
    • Zippo, A., Serafini, R., Rocchigiani, M., Pennacchini, S., Krepelova, A. and Oliviero, S. (2009) Histone crosstalk between H3S10ph and H4K16ac generates a histone code that mediates transcription elongation. Cell, 138, 1122-1136.
    • (2009) Cell , vol.138 , pp. 1122-1136
    • Zippo, A.1    Serafini, R.2    Rocchigiani, M.3    Pennacchini, S.4    Krepelova, A.5    Oliviero, S.6
  • 8
    • 0038511129 scopus 로고    scopus 로고
    • Histone H3 phosphorylation by IKK-alpha is critical for cytokine-induced gene expression
    • Yamamoto, Y., Verma, U.N., Prajapati, S., Kwak, Y.T. and Gaynor, R.B. (2003) Histone H3 phosphorylation by IKK-alpha is critical for cytokine-induced gene expression. Nature, 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
  • 9
    • 0037497184 scopus 로고    scopus 로고
    • A nucleosomal function for IkappaB kinase-alpha in NF-kappaB-dependent gene expression
    • Anest, V., Hanson, J.L., Cogswell, P.C., Steinbrecher, K.A., Strahl, B.D. and Baldwin, A.S. (2003) A nucleosomal function for IkappaB kinase-alpha in NF-kappaB-dependent gene expression. Nature, 423, 659-663.
    • (2003) Nature , vol.423 , pp. 659-663
    • Anest, V.1    Hanson, J.L.2    Cogswell, P.C.3    Steinbrecher, K.A.4    Strahl, B.D.5    Baldwin, A.S.6
  • 10
    • 0037154967 scopus 로고    scopus 로고
    • Integrating mRNA processing with transcription
    • Proudfoot, N.J., Furger, A. and Dye, M.J. (2002) Integrating mRNA processing with transcription. Cell, 108, 501-512.
    • (2002) Cell , vol.108 , pp. 501-512
    • Proudfoot, N.J.1    Furger, A.2    Dye, M.J.3
  • 11
    • 44149124228 scopus 로고    scopus 로고
    • Cracking the RNA polymerase II CTD code
    • Egloff, S. and Murphy, S. (2008) Cracking the RNA polymerase II CTD code. Trends. Genet., 24, 280-288.
    • (2008) Trends. Genet. , vol.24 , pp. 280-288
    • Egloff, S.1    Murphy, S.2
  • 12
    • 0038740693 scopus 로고    scopus 로고
    • Tails of intrigue: Phosphorylation of RNA polymerase II mediates histone methylation
    • Hampsey, M. and Reinberg, D. (2003) Tails of intrigue: phosphorylation of RNA polymerase II mediates histone methylation. Cell, 113, 429-432.
    • (2003) Cell , vol.113 , pp. 429-432
    • Hampsey, M.1    Reinberg, D.2
  • 13
    • 34249299791 scopus 로고    scopus 로고
    • The complex language of chromatin regulation during transcription
    • Berger, S.L. (2007) The complex language of chromatin regulation during transcription. Nature, 447, 407-412.
    • (2007) Nature , vol.447 , pp. 407-412
    • Berger, S.L.1
  • 14
    • 16244384503 scopus 로고    scopus 로고
    • A novel domain in Set2 mediates RNA polymerase II interaction and couples histone H3 K36 methylation with transcript elongation
    • Kizer, K.O., Phatnani, H.P., Shibata, Y., Hall, H., Greenleaf, A.L. and Strahl, B.D. (2005) A novel domain in Set2 mediates RNA polymerase II interaction and couples histone H3 K36 methylation with transcript elongation. Mol. Cell. Biol., 25, 3305-3316.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 3305-3316
    • Kizer, K.O.1    Phatnani, H.P.2    Shibata, Y.3    Hall, H.4    Greenleaf, A.L.5    Strahl, B.D.6
  • 15
    • 23044431656 scopus 로고    scopus 로고
    • Histone H3 lysine 9 methylation and HP1gamma are associated with transcription elongation through mammalian chromatin
    • Vakoc, C.R., Mandat, S.A., Olenchock, B.A. and Blobel, G.A. (2005) Histone H3 lysine 9 methylation and HP1gamma are associated with transcription elongation through mammalian chromatin. Mol. Cell, 19, 381-391.
    • (2005) Mol. Cell , vol.19 , pp. 381-391
    • Vakoc, C.R.1    Mandat, S.A.2    Olenchock, B.A.3    Blobel, G.A.4
  • 16
    • 77957662160 scopus 로고    scopus 로고
    • Heterochromatin protein 1 (HP1) connects the FACT histone chaperone complex to the phosphorylated CTD of RNA polymerase II
    • Kwon, S.H., Florens, L., Swanson, S.K., Washburn, M.P., Abmayr, S.M. and Workman, J.L. (2010) Heterochromatin protein 1 (HP1) connects the FACT histone chaperone complex to the phosphorylated CTD of RNA polymerase II. Genes. Dev., 24, 2133-2145.
    • (2010) Genes. Dev. , vol.24 , pp. 2133-2145
    • Kwon, S.H.1    Florens, L.2    Swanson, S.K.3    Washburn, M.P.4    Abmayr, S.M.5    Workman, J.L.6
  • 17
    • 0035282573 scopus 로고    scopus 로고
    • Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins
    • Lachner, M., O'Carroll, D., Rea, S., Mechtler, K. and Jenuwein, T. (2001) Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins. Nature, 410, 116-120.
    • (2001) Nature , vol.410 , pp. 116-120
    • Lachner, M.1    O'carroll, D.2    Rea, S.3    Mechtler, K.4    Jenuwein, T.5
  • 18
    • 0038412822 scopus 로고    scopus 로고
    • The DNA methyltransferases associate with HP1 and the SUV39H1 histone methyltransferase
    • Fuks, F., Hurd, P.J., Deplus, R. and Kouzarides, T. (2003) The DNA methyltransferases associate with HP1 and the SUV39H1 histone methyltransferase. Nucleic Acids Res., 31, 2305-2312.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 2305-2312
    • Fuks, F.1    Hurd, P.J.2    Deplus, R.3    Kouzarides, T.4
  • 19
    • 0034353169 scopus 로고    scopus 로고
    • HP1gamma associates with euchromatin and heterochromatin in mammalian nuclei and chromosomes
    • Minc, E., Courvalin, J.C. and Buendia, B. (2000) HP1gamma associates with euchromatin and heterochromatin in mammalian nuclei and chromosomes. Cytogenet. Cell Genet., 90, 279-284.
    • (2000) Cytogenet. Cell Genet. , vol.90 , pp. 279-284
    • Minc, E.1    Courvalin, J.C.2    Buendia, B.3
  • 20
    • 33645725188 scopus 로고    scopus 로고
    • Evidence for the existence of an HP1-mediated subcode within the histone code
    • Lomberk, G., Bensi, D., Fernandez-Zapico, M.E. and Urrutia, R. (2006) Evidence for the existence of an HP1-mediated subcode within the histone code. Nat. Cell Biol., 8, 407-415.
    • (2006) Nat. Cell Biol. , vol.8 , pp. 407-415
    • Lomberk, G.1    Bensi, D.2    Fernandez-Zapico, M.E.3    Urrutia, R.4
  • 21
    • 0033959911 scopus 로고    scopus 로고
    • Identification of heterochromatin protein 1 (HP1) as a phosphorylation target by Pim-1 kinase and the effect of phosphorylation on the transcriptional repression function of HP1(1)
    • Koike, N., Maita, H., Taira, T., Ariga, H. and Iguchi-Ariga, S.M. (2000) Identification of heterochromatin protein 1 (HP1) as a phosphorylation target by Pim-1 kinase and the effect of phosphorylation on the transcriptional repression function of HP1(1). FEBS Lett., 467, 17-21.
    • (2000) FEBS Lett. , vol.467 , pp. 17-21
    • Koike, N.1    Maita, H.2    Taira, T.3    Ariga, H.4    Iguchi-Ariga, S.M.5
  • 22
    • 53149130940 scopus 로고    scopus 로고
    • The LPS-induced transcriptional upregulation of the chicken lysozyme locus involves CTCF eviction and noncoding RNA transcription
    • Lefevre, P., Witham, J., Lacroix, C.E., Cockerill, P.N. and Bonifer, C. (2008) The LPS-induced transcriptional upregulation of the chicken lysozyme locus involves CTCF eviction and noncoding RNA transcription. Mol. Cell, 32, 129-139.
    • (2008) Mol. Cell , vol.32 , pp. 129-139
    • Lefevre, P.1    Witham, J.2    Lacroix, C.E.3    Cockerill, P.N.4    Bonifer, C.5
  • 24
    • 0036645169 scopus 로고    scopus 로고
    • Transcription factor complex formation and chromatin fine structure alterations at the murine c-fms (CSF-1 receptor) locus during maturation of myeloid precursor cells
    • Tagoh, H., Himes, R., Clarke, D., Leenen, P.J., Riggs, A.D., Hume, D. and Bonifer, C. (2002) Transcription factor complex formation and chromatin fine structure alterations at the murine c-fms (CSF-1 receptor) locus during maturation of myeloid precursor cells. Genes Dev., 16, 1721-1737.
    • (2002) Genes Dev. , vol.16 , pp. 1721-1737
    • Tagoh, H.1    Himes, R.2    Clarke, D.3    Leenen, P.J.4    Riggs, A.D.5    Hume, D.6    Bonifer, C.7
  • 25
    • 70349728484 scopus 로고    scopus 로고
    • A recurrent network involving the transcription factors PU.1 and Gfi1 orchestrates innate and adaptive immune cell fates
    • Spooner, C.J., Cheng, J.X., Pujadas, E., Laslo, P. and Singh, H. (2009) A recurrent network involving the transcription factors PU.1 and Gfi1 orchestrates innate and adaptive immune cell fates. Immunity, 31, 576-586.
    • (2009) Immunity , vol.31 , pp. 576-586
    • Spooner, C.J.1    Cheng, J.X.2    Pujadas, E.3    Laslo, P.4    Singh, H.5
  • 26
    • 23044483908 scopus 로고    scopus 로고
    • Differentiation-dependent alterations in histone methylation and chromatin architecture at the inducible chicken lysozyme gene
    • Lefevre, P., Lacroix, C., Tagoh, H., Hoogenkamp, M., Melnik, S., Ingram, R. and Bonifer, C. (2005) Differentiation-dependent alterations in histone methylation and chromatin architecture at the inducible chicken lysozyme gene. J. Biol. Chem., 280, 27552-27560.
    • (2005) J. Biol. Chem. , vol.280 , pp. 27552-27560
    • Lefevre, P.1    Lacroix, C.2    Tagoh, H.3    Hoogenkamp, M.4    Melnik, S.5    Ingram, R.6    Bonifer, C.7
  • 27
    • 33746523602 scopus 로고    scopus 로고
    • Analyzing histone modification using crosslinked chromatin treated with micrococcal nuclease
    • Lefevre, P. and Bonifer, C. (2006) Analyzing histone modification using crosslinked chromatin treated with micrococcal nuclease. Methods Mol. Biol., 325, 315-325.
    • (2006) Methods Mol. Biol. , vol.325 , pp. 315-325
    • Lefevre, P.1    Bonifer, C.2
  • 28
    • 0038316508 scopus 로고    scopus 로고
    • Developmentally regulated recruitment of transcription factors and chromatin modification activities to chicken lysozyme cis-regulatory elements in vivo
    • Lefevre, P., Melnik, S., Wilson, N., Riggs, A.D. and Bonifer, C. (2003) Developmentally regulated recruitment of transcription factors and chromatin modification activities to chicken lysozyme cis-regulatory elements in vivo. Mol. Cell. Biol., 23, 4386-4400.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 4386-4400
    • Lefevre, P.1    Melnik, S.2    Wilson, N.3    Riggs, A.D.4    Bonifer, C.5
  • 29
    • 0041806599 scopus 로고    scopus 로고
    • The double bromodomain protein Brd4 binds to acetylated chromatin during interphase and mitosis
    • Dey, A., Chitsaz, F., Abbasi, A., Misteli, T. and Ozato, K. (2003) The double bromodomain protein Brd4 binds to acetylated chromatin during interphase and mitosis. Proc. Natl Acad. Sci. USA, 100, 8758-8763.
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 8758-8763
    • Dey, A.1    Chitsaz, F.2    Abbasi, A.3    Misteli, T.4    Ozato, K.5
  • 30
    • 46149108345 scopus 로고    scopus 로고
    • Rapid, transcription-independent loss of nucleosomes over a large chromatin domain at Hsp70 loci
    • Petesch, S.J. and Lis, J.T. (2008) Rapid, transcription-independent loss of nucleosomes over a large chromatin domain at Hsp70 loci. Cell, 134, 74-84.
    • (2008) Cell , vol.134 , pp. 74-84
    • Petesch, S.J.1    Lis, J.T.2
  • 31
    • 36749019654 scopus 로고    scopus 로고
    • Activation-dependent intrachromosomal interactions formed by the TNF gene promoter and two distal enhancers
    • Tsytsykova, A.V., Rajsbaum, R., Falvo, J.V., Ligeiro, F., Neely, S.R. and Goldfeld, A.E. (2007) Activation-dependent intrachromosomal interactions formed by the TNF gene promoter and two distal enhancers. Proc. Natl Acad. Sci. USA, 104, 16850-16855.
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 16850-16855
    • Tsytsykova, A.V.1    Rajsbaum, R.2    Falvo, J.V.3    Ligeiro, F.4    Neely, S.R.5    Goldfeld, A.E.6
  • 32
    • 77957726025 scopus 로고    scopus 로고
    • IL-10 inhibits transcription elongation of the human TNF gene in primary macrophages
    • Smallie, T., Ricchetti, G., Horwood, N.J., Feldmann, M., Clark, A.R. and Williams, L.M. (2010) IL-10 inhibits transcription elongation of the human TNF gene in primary macrophages. J. Exp. Med., 207, 2081-2088.
    • (2010) J. Exp. Med. , vol.207 , pp. 2081-2088
    • Smallie, T.1    Ricchetti, G.2    Horwood, N.J.3    Feldmann, M.4    Clark, A.R.5    Williams, L.M.6
  • 34
    • 0036299092 scopus 로고    scopus 로고
    • The histone variant H3.3 marks active chromatin by replication- independent nucleosome assembly
    • Ahmad, K. and Henikoff, S. (2002) The histone variant H3.3 marks active chromatin by replication-independent nucleosome assembly. Mol. Cell, 9, 1191-1200.
    • (2002) Mol. Cell , vol.9 , pp. 1191-1200
    • Ahmad, K.1    Henikoff, S.2
  • 37
    • 6344241039 scopus 로고    scopus 로고
    • SMRT derepression by the IkappaB kinase alpha: A prerequisite to NF-kappaB transcription and survival
    • Hoberg, J.E., Yeung, F. and Mayo, M.W. (2004) SMRT derepression by the IkappaB kinase alpha: a prerequisite to NF-kappaB transcription and survival. Mol. Cell, 16, 245-255.
    • (2004) Mol. Cell , vol.16 , pp. 245-255
    • Hoberg, J.E.1    Yeung, F.2    Mayo, M.W.3
  • 38
    • 17844386319 scopus 로고    scopus 로고
    • IKKalpha limits macrophage NF-kappaB activation and contributes to the resolution of inflammation
    • Lawrence, T., Bebien, M., Liu, G.Y., Nizet, V. and Karin, M. (2005) IKKalpha limits macrophage NF-kappaB activation and contributes to the resolution of inflammation. Nature, 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
  • 40
    • 33745855826 scopus 로고    scopus 로고
    • NIK is involved in nucleosomal regulation by enhancing histone H3 phosphorylation by IKKalpha
    • Park, G.Y., Wang, X., Hu, N., Pedchenko, T.V., Blackwell, T.S. and Christman, J.W. (2006) NIK is involved in nucleosomal regulation by enhancing histone H3 phosphorylation by IKKalpha. J. Biol. Chem., 281, 18684-18690.
    • (2006) J. Biol. Chem. , vol.281 , pp. 18684-18690
    • Park, G.Y.1    Wang, X.2    Hu, N.3    Pedchenko, T.V.4    Blackwell, T.S.5    Christman, J.W.6
  • 41
    • 0036143654 scopus 로고    scopus 로고
    • P38-Dependent marking of inflammatory genes for increased NF-kappa B recruitment
    • Saccani, S., Pantano, S. and Natoli, G. (2002) p38-Dependent marking of inflammatory genes for increased NF-kappa B recruitment. Nat. Immunol., 3, 69-75.
    • (2002) Nat. Immunol. , vol.3 , pp. 69-75
    • Saccani, S.1    Pantano, S.2    Natoli, G.3
  • 42
    • 3142615882 scopus 로고    scopus 로고
    • Recognition of RNA polymerase II carboxy-terminal domain by 30-RNA-processing factors
    • Meinhart, A. and Cramer, P. (2004) Recognition of RNA polymerase II carboxy-terminal domain by 30-RNA-processing factors. Nature, 430, 223-226.
    • (2004) Nature , vol.430 , pp. 223-226
    • Meinhart, A.1    Cramer, P.2
  • 43
    • 22344443368 scopus 로고    scopus 로고
    • CTD-dependent dismantling of the RNA polymerase II elongation complex by the pre-mRNA 30-end processing factor, Pcf11
    • Zhang, Z., Fu, J. and Gilmour, D.S. (2005) CTD-dependent dismantling of the RNA polymerase II elongation complex by the pre-mRNA 30-end processing factor, Pcf11. Genes Dev., 19, 1572-1580.
    • (2005) Genes Dev. , vol.19 , pp. 1572-1580
    • Zhang, Z.1    Fu, J.2    Gilmour, D.S.3
  • 44
    • 40249085830 scopus 로고    scopus 로고
    • Regulation of an inducible promoter by an HP1beta-HP1gamma switch
    • Mateescu, B., Bourachot, B., Rachez, C., Ogryzko, V. and Muchardt, C. (2008) Regulation of an inducible promoter by an HP1beta-HP1gamma switch. EMBO Rep., 9, 267-272.
    • (2008) EMBO Rep. , vol.9 , pp. 267-272
    • Mateescu, B.1    Bourachot, B.2    Rachez, C.3    Ogryzko, V.4    Muchardt, C.5
  • 45
    • 0037512273 scopus 로고    scopus 로고
    • The Set2 histone methyltransferase functions through the phosphorylated carboxyl-terminal domain of RNA polymerase II
    • Li, B., Howe, L., Anderson, S., Yates, J.R. 3rd and Workman, J.L. (2003) The Set2 histone methyltransferase functions through the phosphorylated carboxyl-terminal domain of RNA polymerase II. J. Biol. Chem., 278, 8897-8903.
    • (2003) J. Biol. Chem. , vol.278 , pp. 8897-8903
    • Li, B.1    Howe, L.2    Anderson, S.3    Yates III, J.R.4    Workman, J.L.5
  • 46
    • 27744577727 scopus 로고    scopus 로고
    • Histone H3 methylation by Set2 directs deacetylation of coding regions by Rpd3S to suppress spurious intragenic transcription
    • Carrozza, M.J., Li, B., Florens, L., Suganuma, T., Swanson, S.K., Lee, K.K., Shia, W.J., Anderson, S., Yates, J., Washburn, M.P. et al. (2005) Histone H3 methylation by Set2 directs deacetylation of coding regions by Rpd3S to suppress spurious intragenic transcription. Cell, 123, 581-592.
    • (2005) Cell , vol.123 , pp. 581-592
    • Carrozza, M.J.1    Li, B.2    Florens, L.3    Suganuma, T.4    Swanson, S.K.5    Lee, K.K.6    Shia, W.J.7    Anderson, S.8    Yates, J.9    Washburn, M.P.10
  • 47
    • 69949132191 scopus 로고    scopus 로고
    • Chromatin organization marks exon-intron structure
    • Schwartz, S., Meshorer, E. and Ast, G. (2009) Chromatin organization marks exon-intron structure. Nat. Struct. Mol. Biol., 16, 990-995.
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 990-995
    • Schwartz, S.1    Meshorer, E.2    Ast, G.3
  • 50
    • 79952364016 scopus 로고    scopus 로고
    • Histone H3 lysine 9 trimethylation and HP1gamma favor inclusion of alternative exons
    • Saint-Andre, V., Batsche, E., Rachez, C. and Muchardt, C. (2011) Histone H3 lysine 9 trimethylation and HP1gamma favor inclusion of alternative exons. Nat. Struct. Mol. Biol., 18, 337-344.
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 337-344
    • Saint-Andre, V.1    Batsche, E.2    Rachez, C.3    Muchardt, C.4
  • 51
    • 34147156583 scopus 로고    scopus 로고
    • A site to remember: H3K36 methylation a mark for histone deacetylation
    • Lee, J.S. and Shilatifard, A. (2007) A site to remember: H3K36 methylation a mark for histone deacetylation. Mutat. Res., 618, 130-134.
    • (2007) Mutat. Res. , vol.618 , pp. 130-134
    • Lee, J.S.1    Shilatifard, A.2
  • 52
    • 33748163064 scopus 로고    scopus 로고
    • Proline isomerization of histone H3 regulates lysine methylation and gene expression
    • Nelson, C.J., Santos-Rosa, H. and Kouzarides, T. (2006) Proline isomerization of histone H3 regulates lysine methylation and gene expression. Cell, 126, 905-916.
    • (2006) Cell , vol.126 , pp. 905-916
    • Nelson, C.J.1    Santos-Rosa, H.2    Kouzarides, T.3
  • 53
    • 80455178828 scopus 로고    scopus 로고
    • Histone variant H3.3 stimulates HSP70 transcription through cooperation with HP1{gamma}
    • Kim, H., Heo, K., Choi, J., Kim, K. and An, W. (2011) Histone variant H3.3 stimulates HSP70 transcription through cooperation with HP1{gamma}. Nucleic Acids Res., 39, 8329-8341.
    • (2011) Nucleic Acids Res. , vol.39 , pp. 8329-8341
    • Kim, H.1    Heo, K.2    Choi, J.3    Kim, K.4    An, W.5
  • 54
    • 0033518118 scopus 로고    scopus 로고
    • Transcriptional elongation of c-myb is regulated by NF-kappaB (p50/RelB)
    • Suhasini, M. and Pilz, R.B. (1999) Transcriptional elongation of c-myb is regulated by NF-kappaB (p50/RelB). Oncogene, 18, 7360-7369.
    • (1999) Oncogene , vol.18 , pp. 7360-7369
    • Suhasini, M.1    Pilz, R.B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.