메뉴 건너뛰기




Volumn 102, Issue 5, 2011, Pages 1081-1087

Histone deacetylase inhibitors block nuclear factor-κB-dependent transcription by interfering with RNA polymerase II recruitment

Author keywords

[No Author keywords available]

Indexed keywords

CYCLOOXYGENASE 2; DEXAMETHASONE; DNA; HISTONE DEACETYLASE; HISTONE DEACETYLASE INHIBITOR; I KAPPA B ALPHA; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERLEUKIN 1BETA; INTERLEUKIN 6; INTERLEUKIN 8; KY 2 PEPTIDE; PLASMID VECTOR; RNA POLYMERASE II; TETRAPEPTIDE; TRICHOSTATIN A; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG;

EID: 79954842538     PISSN: 13479032     EISSN: 13497006     Source Type: Journal    
DOI: 10.1111/j.1349-7006.2011.01904.x     Document Type: Article
Times cited : (32)

References (52)
  • 1
    • 65249123485 scopus 로고    scopus 로고
    • Histone acetylation: truth of consequences?
    • Choi JK, Howe LJ. Histone acetylation: truth of consequences? Biochem Cell Biol 2009; 87(1): 139-50.
    • (2009) Biochem Cell Biol , vol.87 , Issue.1 , pp. 139-150
    • Choi, J.K.1    Howe, L.J.2
  • 2
    • 30344477367 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer
    • Minucci S, Pelicci PG. Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer. Nat Rev Cancer 2006; 6(1): 38-51.
    • (2006) Nat Rev Cancer , vol.6 , Issue.1 , pp. 38-51
    • Minucci, S.1    Pelicci, P.G.2
  • 3
    • 0034730127 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor selectively induces p21WAF1 expression and gene-associated histone acetylation
    • Richon VM, Sandhoff TW, Rifkind RA, Marks PA. Histone deacetylase inhibitor selectively induces p21WAF1 expression and gene-associated histone acetylation. Proc Natl Acad Sci U S A 2000; 97(18): 10014-9.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , Issue.18 , pp. 10014-10019
    • Richon, V.M.1    Sandhoff, T.W.2    Rifkind, R.A.3    Marks, P.A.4
  • 4
    • 73449117582 scopus 로고    scopus 로고
    • Immunomodulatory effects of deacetylase inhibitors: therapeutic targeting of FOXP3+ regulatory T cells
    • Wang L, de Zoeten EF, Greene MI, Hancock WW. Immunomodulatory effects of deacetylase inhibitors: therapeutic targeting of FOXP3+ regulatory T cells. Nat Rev Drug Discov 2009; 8(12): 969-81.
    • (2009) Nat Rev Drug Discov , vol.8 , Issue.12 , pp. 969-981
    • Wang, L.1    de Zoeten, E.F.2    Greene, M.I.3    Hancock, W.W.4
  • 5
    • 1842531133 scopus 로고    scopus 로고
    • Butyrate suppresses Cox-2 activation in colon cancer cells through HDAC inhibition
    • Tong X, Yin L, Giardina C. Butyrate suppresses Cox-2 activation in colon cancer cells through HDAC inhibition. Biochem Biophys Res Commun 2004; 317(2): 463-71.
    • (2004) Biochem Biophys Res Commun , vol.317 , Issue.2 , pp. 463-471
    • Tong, X.1    Yin, L.2    Giardina, C.3
  • 6
    • 0024996768 scopus 로고
    • Potent and specific inhibition of mammalian histone deacetylase both in vivo and in vitro by trichostatin A
    • Yoshida M, Kijima M, Akita M, Beppu T. Potent and specific inhibition of mammalian histone deacetylase both in vivo and in vitro by trichostatin A. J Biol Chem 1990; 265(28): 17174-9.
    • (1990) J Biol Chem , vol.265 , Issue.28 , pp. 17174-17179
    • Yoshida, M.1    Kijima, M.2    Akita, M.3    Beppu, T.4
  • 7
    • 0036735385 scopus 로고    scopus 로고
    • FK228 (depsipeptide) as a natural prodrug that inhibits class I histone deacetylases
    • Furumai R, Matsuyama A, Kobashi N et al. FK228 (depsipeptide) as a natural prodrug that inhibits class I histone deacetylases. Cancer Res 2002; 62(17): 4916-21.
    • (2002) Cancer Res , vol.62 , Issue.17 , pp. 4916-4921
    • Furumai, R.1    Matsuyama, A.2    Kobashi, N.3
  • 8
    • 13544265432 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: new drugs for the treatment of inflammatory diseases?
    • Blanchard F, Chipoy C. Histone deacetylase inhibitors: new drugs for the treatment of inflammatory diseases? Drug Discov Today 2005; 10(3): 197-204.
    • (2005) Drug Discov Today , vol.10 , Issue.3 , pp. 197-204
    • Blanchard, F.1    Chipoy, C.2
  • 9
    • 34047218122 scopus 로고    scopus 로고
    • HDAC inhibitors as anti-inflammatory agents
    • Adcock IM. HDAC inhibitors as anti-inflammatory agents. Br J Pharmacol 2007; 150(7): 829-31.
    • (2007) Br J Pharmacol , vol.150 , Issue.7 , pp. 829-831
    • Adcock, I.M.1
  • 10
    • 0346873023 scopus 로고    scopus 로고
    • A therapeutic strategy uses histone deacetylase inhibitors to modulate the expression of genes involved in the pathogenesis of rheumatoid arthritis
    • Chung YL, Lee MY, Wang AJ, Yao LF. A therapeutic strategy uses histone deacetylase inhibitors to modulate the expression of genes involved in the pathogenesis of rheumatoid arthritis. Mol Ther 2003; 8(5): 707-17.
    • (2003) Mol Ther , vol.8 , Issue.5 , pp. 707-717
    • Chung, Y.L.1    Lee, M.Y.2    Wang, A.J.3    Yao, L.F.4
  • 11
    • 60549085246 scopus 로고    scopus 로고
    • Targeting histone deacetylase activity in rheumatoid arthritis and asthma as prototypes of inflammatory disease: should we keep our HATs on?
    • Grabiec AM, Tak PP, Reedquist KA. Targeting histone deacetylase activity in rheumatoid arthritis and asthma as prototypes of inflammatory disease: should we keep our HATs on? Arthritis Res Ther 2008; 10(5): 226.
    • (2008) Arthritis Res Ther , vol.10 , Issue.5 , pp. 226
    • Grabiec, A.M.1    Tak, P.P.2    Reedquist, K.A.3
  • 12
    • 5644239630 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor suppression of autoantibody-mediated arthritis in mice via regulation of p16INK4a and p21(WAF1/Cip1) expression
    • Nishida K, Komiyama T, Miyazawa S et al. Histone deacetylase inhibitor suppression of autoantibody-mediated arthritis in mice via regulation of p16INK4a and p21(WAF1/Cip1) expression. Arthritis Rheum 2004; 50(10): 3365-76.
    • (2004) Arthritis Rheum , vol.50 , Issue.10 , pp. 3365-3376
    • Nishida, K.1    Komiyama, T.2    Miyazawa, S.3
  • 13
    • 46149125241 scopus 로고    scopus 로고
    • A pervasive role of histone acetyltransferases and deacetylases in an NF-kappaB-signaling code
    • Calao M, Burny A, Quivy V, Dekoninck A, Van Lint C. A pervasive role of histone acetyltransferases and deacetylases in an NF-kappaB-signaling code. Trends Biochem Sci 2008; 33(7): 339-49.
    • (2008) Trends Biochem Sci , vol.33 , Issue.7 , pp. 339-349
    • Calao, M.1    Burny, A.2    Quivy, V.3    Dekoninck, A.4    Van Lint, C.5
  • 15
    • 0035979737 scopus 로고    scopus 로고
    • Duration of nuclear NF-kappaB action regulated by reversible acetylation
    • Chen L, Fischle W, Verdin E, Greene WC. Duration of nuclear NF-kappaB action regulated by reversible acetylation. Science 2001; 293(5535): 1653-7.
    • (2001) Science , vol.293 , Issue.5535 , pp. 1653-1657
    • Chen, L.1    Fischle, W.2    Verdin, E.3    Greene, W.C.4
  • 16
    • 0141594607 scopus 로고    scopus 로고
    • Regulation of distinct biological activities of the NF-kappaB transcription factor complex by acetylation
    • Chen LF, Greene WC. Regulation of distinct biological activities of the NF-kappaB transcription factor complex by acetylation. J Mol Med 2003; 81(9): 549-57.
    • (2003) J Mol Med , vol.81 , Issue.9 , pp. 549-557
    • Chen, L.F.1    Greene, W.C.2
  • 17
    • 2342522110 scopus 로고    scopus 로고
    • Shaping the nuclear action of NF-kappaB
    • Chen LF, Greene WC. Shaping the nuclear action of NF-kappaB. Nat Rev Mol Cell Biol 2004; 5(5): 392-401.
    • (2004) Nat Rev Mol Cell Biol , vol.5 , Issue.5 , pp. 392-401
    • Chen, L.F.1    Greene, W.C.2
  • 18
    • 0037011056 scopus 로고    scopus 로고
    • Acetylation of RelA at discrete sites regulates distinct nuclear functions of NF-kappaB
    • Chen LF, Mu Y, Greene WC. Acetylation of RelA at discrete sites regulates distinct nuclear functions of NF-kappaB. EMBO J 2002; 21(23): 6539-48.
    • (2002) EMBO J , vol.21 , Issue.23 , pp. 6539-6548
    • Chen, L.F.1    Mu, Y.2    Greene, W.C.3
  • 19
    • 3242719545 scopus 로고    scopus 로고
    • Modulation of NF-kappaB-dependent transcription and cell survival by the SIRT1 deacetylase
    • Yeung F, Hoberg JE, Ramsey CS et al. Modulation of NF-kappaB-dependent transcription and cell survival by the SIRT1 deacetylase. EMBO J 2004; 23(12): 2369-80.
    • (2004) EMBO J , vol.23 , Issue.12 , pp. 2369-2380
    • Yeung, F.1    Hoberg, J.E.2    Ramsey, C.S.3
  • 20
    • 4143083971 scopus 로고    scopus 로고
    • Regulation at multiple levels of NF-kappaB-mediated transactivation by protein acetylation
    • Quivy V, Van Lint C. Regulation at multiple levels of NF-kappaB-mediated transactivation by protein acetylation. Biochem Pharmacol 2004; 68(6): 1221-9.
    • (2004) Biochem Pharmacol , vol.68 , Issue.6 , pp. 1221-1229
    • Quivy, V.1    Van Lint, C.2
  • 21
    • 33845997798 scopus 로고    scopus 로고
    • Suberoylanilide hydroxamic acid induces Akt-mediated phosphorylation of p300, which promotes acetylation and transcriptional activation of RelA/p65
    • Liu Y, Denlinger CE, Rundall BK, Smith PW, Jones DR. Suberoylanilide hydroxamic acid induces Akt-mediated phosphorylation of p300, which promotes acetylation and transcriptional activation of RelA/p65. J Biol Chem 2006; 281(42): 31359-68.
    • (2006) J Biol Chem , vol.281 , Issue.42 , pp. 31359-31368
    • Liu, Y.1    Denlinger, C.E.2    Rundall, B.K.3    Smith, P.W.4    Jones, D.R.5
  • 22
    • 6344247464 scopus 로고    scopus 로고
    • Chlamydocin-hydroxamic acid analogues as histone deacetylase inhibitors
    • Nishino N, Jose B, Shinta R, Kato T, Komatsu Y, Yoshida M. Chlamydocin-hydroxamic acid analogues as histone deacetylase inhibitors. Bioorg Med Chem 2004; 12(22): 5777-84.
    • (2004) Bioorg Med Chem , vol.12 , Issue.22 , pp. 5777-5784
    • Nishino, N.1    Jose, B.2    Shinta, R.3    Kato, T.4    Komatsu, Y.5    Yoshida, M.6
  • 23
    • 33749173298 scopus 로고    scopus 로고
    • Neddylation of a breast cancer-associated protein recruits a class III histone deacetylase that represses NFkappaB-dependent transcription
    • Gao F, Cheng J, Shi T, Yeh ET. Neddylation of a breast cancer-associated protein recruits a class III histone deacetylase that represses NFkappaB-dependent transcription. Nat Cell Biol 2006; 8(10): 1171-7.
    • (2006) Nat Cell Biol , vol.8 , Issue.10 , pp. 1171-1177
    • Gao, F.1    Cheng, J.2    Shi, T.3    Yeh, E.T.4
  • 24
    • 0038819943 scopus 로고    scopus 로고
    • Ineffectiveness of histone deacetylase inhibitors to induce apoptosis involves the transcriptional activation of NF-kappa B through the Akt pathway
    • Mayo MW, Denlinger CE, Broad RM et al. Ineffectiveness of histone deacetylase inhibitors to induce apoptosis involves the transcriptional activation of NF-kappa B through the Akt pathway. J Biol Chem 2003; 278(21): 18980-9.
    • (2003) J Biol Chem , vol.278 , Issue.21 , pp. 18980-18989
    • Mayo, M.W.1    Denlinger, C.E.2    Broad, R.M.3
  • 25
    • 0035361402 scopus 로고    scopus 로고
    • Cyclic hydroxamic-acid-containing peptide 31, a potent synthetic histone deacetylase inhibitor with antitumor activity
    • Komatsu Y, Tomizaki KY, Tsukamoto M et al. Cyclic hydroxamic-acid-containing peptide 31, a potent synthetic histone deacetylase inhibitor with antitumor activity. Cancer Res 2001; 61(11): 4459-66.
    • (2001) Cancer Res , vol.61 , Issue.11 , pp. 4459-4466
    • Komatsu, Y.1    Tomizaki, K.Y.2    Tsukamoto, M.3
  • 26
    • 0031575947 scopus 로고    scopus 로고
    • Protein synthesis inhibitors cycloheximide and anisomycin induce interleukin-6 gene expression and activate transcription factor NF-kappaB
    • Faggioli L, Costanzo C, Merola M, Furia A, Palmieri M. Protein synthesis inhibitors cycloheximide and anisomycin induce interleukin-6 gene expression and activate transcription factor NF-kappaB. Biochem Biophys Res Commun 1997; 233(2): 507-13.
    • (1997) Biochem Biophys Res Commun , vol.233 , Issue.2 , pp. 507-513
    • Faggioli, L.1    Costanzo, C.2    Merola, M.3    Furia, A.4    Palmieri, M.5
  • 27
    • 0038740693 scopus 로고    scopus 로고
    • Tails of intrigue: phosphorylation of RNA polymerase II mediates histone methylation
    • Hampsey M, Reinberg D. Tails of intrigue: phosphorylation of RNA polymerase II mediates histone methylation. Cell 2003; 113(4): 429-32.
    • (2003) Cell , vol.113 , Issue.4 , pp. 429-432
    • Hampsey, M.1    Reinberg, D.2
  • 28
    • 33746380872 scopus 로고    scopus 로고
    • Involvement of HDAC1 and the PI3K/PKC signaling pathways in NF-kappaB activation by the HDAC inhibitor apicidin
    • Kim YK, Seo DW, Kang DW, Lee HY, Han JW, Kim SN. Involvement of HDAC1 and the PI3K/PKC signaling pathways in NF-kappaB activation by the HDAC inhibitor apicidin. Biochem Biophys Res Commun 2006; 347(4): 1088-93.
    • (2006) Biochem Biophys Res Commun , vol.347 , Issue.4 , pp. 1088-1093
    • Kim, Y.K.1    Seo, D.W.2    Kang, D.W.3    Lee, H.Y.4    Han, J.W.5    Kim, S.N.6
  • 29
    • 0033527448 scopus 로고    scopus 로고
    • The nuclear factor-kappaB engages CBP/p300 and histone acetyltransferase activity for transcriptional activation of the interleukin-6 gene promoter
    • Vanden Berghe W, De Bosscher K, Boone E, Plaisance S, Haegeman G. The nuclear factor-kappaB engages CBP/p300 and histone acetyltransferase activity for transcriptional activation of the interleukin-6 gene promoter. J Biol Chem 1999; 274(45): 32091-8.
    • (1999) J Biol Chem , vol.274 , Issue.45 , pp. 32091-32098
    • Vanden Berghe, W.1    De Bosscher, K.2    Boone, E.3    Plaisance, S.4    Haegeman, G.5
  • 30
    • 0036203419 scopus 로고    scopus 로고
    • The phosphorylation status of nuclear NF-kappa B determines its association with CBP/p300 or HDAC-1
    • Zhong H, May MJ, Jimi E, Ghosh S. The phosphorylation status of nuclear NF-kappa B determines its association with CBP/p300 or HDAC-1. Mol Cell 2002; 9(3): 625-36.
    • (2002) Mol Cell , vol.9 , Issue.3 , pp. 625-636
    • Zhong, H.1    May, M.J.2    Jimi, E.3    Ghosh, S.4
  • 31
    • 0042971647 scopus 로고    scopus 로고
    • Potentiation of tumor necrosis factor-induced NF-kappa B activation by deacetylase inhibitors is associated with a delayed cytoplasmic reappearance of I kappa B alpha
    • Adam E, Quivy V, Bex F et al. Potentiation of tumor necrosis factor-induced NF-kappa B activation by deacetylase inhibitors is associated with a delayed cytoplasmic reappearance of I kappa B alpha. Mol Cell Biol 2003; 23(17): 6200-9.
    • (2003) Mol Cell Biol , vol.23 , Issue.17 , pp. 6200-6209
    • Adam, E.1    Quivy, V.2    Bex, F.3
  • 32
    • 0037462725 scopus 로고    scopus 로고
    • Post-activation turn-off of NF-kappa B-dependent transcription is regulated by acetylation of p65
    • Kiernan R, Bres V, Ng RW et al. Post-activation turn-off of NF-kappa B-dependent transcription is regulated by acetylation of p65. J Biol Chem 2003; 278(4): 2758-66.
    • (2003) J Biol Chem , vol.278 , Issue.4 , pp. 2758-2766
    • Kiernan, R.1    Bres, V.2    Ng, R.W.3
  • 33
    • 0035977063 scopus 로고    scopus 로고
    • Butyrate suppression of colonocyte NF-kappa B activation and cellular proteasome activity
    • Yin L, Laevsky G, Giardina C. Butyrate suppression of colonocyte NF-kappa B activation and cellular proteasome activity. J Biol Chem 2001; 276(48): 44641-6.
    • (2001) J Biol Chem , vol.276 , Issue.48 , pp. 44641-44646
    • Yin, L.1    Laevsky, G.2    Giardina, C.3
  • 34
    • 0036067845 scopus 로고    scopus 로고
    • Histone deacetylases augment cytokine induction of the iNOS gene
    • Yu Z, Zhang W, Kone BC. Histone deacetylases augment cytokine induction of the iNOS gene. J Am Soc Nephrol 2002; 13(8): 2009-17.
    • (2002) J Am Soc Nephrol , vol.13 , Issue.8 , pp. 2009-2017
    • Yu, Z.1    Zhang, W.2    Kone, B.C.3
  • 35
    • 21344464730 scopus 로고    scopus 로고
    • HDAC inhibition prevents NF-kappa B activation by suppressing proteasome activity: down-regulation of proteasome subunit expression stabilizes I kappa B alpha
    • Place RF, Noonan EJ, Giardina C. HDAC inhibition prevents NF-kappa B activation by suppressing proteasome activity: down-regulation of proteasome subunit expression stabilizes I kappa B alpha. Biochem Pharmacol 2005; 70(3): 394-406.
    • (2005) Biochem Pharmacol , vol.70 , Issue.3 , pp. 394-406
    • Place, R.F.1    Noonan, E.J.2    Giardina, C.3
  • 36
    • 13944274571 scopus 로고    scopus 로고
    • Histone deacetylase inhibition down-regulates cyclin D1 transcription by inhibiting nuclear factor-kappaB/p65 DNA binding
    • Hu J, Colburn NH. Histone deacetylase inhibition down-regulates cyclin D1 transcription by inhibiting nuclear factor-kappaB/p65 DNA binding. Mol Cancer Res 2005; 3(2): 100-9.
    • (2005) Mol Cancer Res , vol.3 , Issue.2 , pp. 100-109
    • Hu, J.1    Colburn, N.H.2
  • 37
    • 25444446426 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors suppress the induction of c-Jun and its target genes including COX-2
    • Yamaguchi K, Lantowski A, Dannenberg AJ, Subbaramaiah K. Histone deacetylase inhibitors suppress the induction of c-Jun and its target genes including COX-2. J Biol Chem 2005; 280(38): 32569-77.
    • (2005) J Biol Chem , vol.280 , Issue.38 , pp. 32569-32577
    • Yamaguchi, K.1    Lantowski, A.2    Dannenberg, A.J.3    Subbaramaiah, K.4
  • 38
    • 33744938927 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors suppress the inducibility of nuclear factor-kappaB by tumor necrosis factor-alpha receptor-1 down-regulation
    • Imre G, Gekeler V, Leja A, Beckers T, Boehm M. Histone deacetylase inhibitors suppress the inducibility of nuclear factor-kappaB by tumor necrosis factor-alpha receptor-1 down-regulation. Cancer Res 2006; 66(10): 5409-18.
    • (2006) Cancer Res , vol.66 , Issue.10 , pp. 5409-5418
    • Imre, G.1    Gekeler, V.2    Leja, A.3    Beckers, T.4    Boehm, M.5
  • 39
    • 46149104370 scopus 로고    scopus 로고
    • c-Jun controls histone modifications, NF-kappaB recruitment, and RNA polymerase II function to activate the ccl2 gene
    • Wolter S, Doerrie A, Weber A et al. c-Jun controls histone modifications, NF-kappaB recruitment, and RNA polymerase II function to activate the ccl2 gene. Mol Cell Biol 2008; 28(13): 4407-23.
    • (2008) Mol Cell Biol , vol.28 , Issue.13 , pp. 4407-4423
    • Wolter, S.1    Doerrie, A.2    Weber, A.3
  • 40
    • 33646851955 scopus 로고    scopus 로고
    • Suberoylanilide hydroxamic acid potentiates apoptosis, inhibits invasion, and abolishes osteoclastogenesis by suppressing nuclear factor-kappaB activation
    • Takada Y, Gillenwater A, Ichikawa H, Aggarwal BB. Suberoylanilide hydroxamic acid potentiates apoptosis, inhibits invasion, and abolishes osteoclastogenesis by suppressing nuclear factor-kappaB activation. J Biol Chem 2006; 281(9): 5612-22.
    • (2006) J Biol Chem , vol.281 , Issue.9 , pp. 5612-5622
    • Takada, Y.1    Gillenwater, A.2    Ichikawa, H.3    Aggarwal, B.B.4
  • 41
    • 33751161897 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor reduces monocyte adhesion to endothelium through the suppression of vascular cell adhesion molecule-1 expression
    • Inoue K, Kobayashi M, Yano K et al. Histone deacetylase inhibitor reduces monocyte adhesion to endothelium through the suppression of vascular cell adhesion molecule-1 expression. Arterioscler Thromb Vasc Biol 2006; 26(12): 2652-9.
    • (2006) Arterioscler Thromb Vasc Biol , vol.26 , Issue.12 , pp. 2652-2659
    • Inoue, K.1    Kobayashi, M.2    Yano, K.3
  • 42
    • 38049016277 scopus 로고    scopus 로고
    • A shifting paradigm: histone deacetylases and transcriptional activation
    • Smith CL. A shifting paradigm: histone deacetylases and transcriptional activation. Bioessays 2008; 30(1): 15-24.
    • (2008) Bioessays , vol.30 , Issue.1 , pp. 15-24
    • Smith, C.L.1
  • 43
    • 0037111879 scopus 로고    scopus 로고
    • Requirement of Hos2 histone deacetylase for gene activity in yeast
    • Wang A, Kurdistani SK, Grunstein M. Requirement of Hos2 histone deacetylase for gene activity in yeast. Science 2002; 298(5597): 1412-4.
    • (2002) Science , vol.298 , Issue.5597 , pp. 1412-1414
    • Wang, A.1    Kurdistani, S.K.2    Grunstein, M.3
  • 44
    • 69449102464 scopus 로고    scopus 로고
    • Genome-wide mapping of HATs and HDACs reveals distinct functions in active and inactive genes
    • Wang Z, Zang C, Cui K et al. Genome-wide mapping of HATs and HDACs reveals distinct functions in active and inactive genes. Cell 2009; 138(5): 1019-31.
    • (2009) Cell , vol.138 , Issue.5 , pp. 1019-1031
    • Wang, Z.1    Zang, C.2    Cui, K.3
  • 45
    • 0344304443 scopus 로고    scopus 로고
    • Interferon-stimulated transcription and innate antiviral immunity require deacetylase activity and histone deacetylase 1
    • Nusinzon I, Horvath CM. Interferon-stimulated transcription and innate antiviral immunity require deacetylase activity and histone deacetylase 1. Proc Natl Acad Sci U S A 2003; 100(25): 14742-7.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , Issue.25 , pp. 14742-14747
    • Nusinzon, I.1    Horvath, C.M.2
  • 46
    • 0037450634 scopus 로고    scopus 로고
    • STAT5-induced Id-1 transcription involves recruitment of HDAC1 and deacetylation of C/EBPbeta
    • Xu M, Nie L, Kim SH, Sun XH. STAT5-induced Id-1 transcription involves recruitment of HDAC1 and deacetylation of C/EBPbeta. EMBO J 2003; 22(4): 893-904.
    • (2003) EMBO J , vol.22 , Issue.4 , pp. 893-904
    • Xu, M.1    Nie, L.2    Kim, S.H.3    Sun, X.H.4
  • 47
    • 33750324764 scopus 로고    scopus 로고
    • Negative and positive regulation of gene expression by mouse histone deacetylase 1
    • Zupkovitz G, Tischler J, Posch M et al. Negative and positive regulation of gene expression by mouse histone deacetylase 1. Mol Cell Biol 2006; 26(21): 7913-28.
    • (2006) Mol Cell Biol , vol.26 , Issue.21 , pp. 7913-7928
    • Zupkovitz, G.1    Tischler, J.2    Posch, M.3
  • 48
    • 64249111489 scopus 로고    scopus 로고
    • Dimethylation of H3K4 by Set1 recruits the Set3 histone deacetylase complex to 5' transcribed regions
    • Kim T, Buratowski S. Dimethylation of H3K4 by Set1 recruits the Set3 histone deacetylase complex to 5' transcribed regions. Cell 2009; 137(2): 259-72.
    • (2009) Cell , vol.137 , Issue.2 , pp. 259-272
    • Kim, T.1    Buratowski, S.2
  • 49
    • 0042567276 scopus 로고    scopus 로고
    • Inhibition of MMTV transcription by HDAC inhibitors occurs independent of changes in chromatin remodeling and increased histone acetylation
    • Mulholland NM, Soeth E, Smith CL. Inhibition of MMTV transcription by HDAC inhibitors occurs independent of changes in chromatin remodeling and increased histone acetylation. Oncogene 2003; 22(31): 4807-18.
    • (2003) Oncogene , vol.22 , Issue.31 , pp. 4807-4818
    • Mulholland, N.M.1    Soeth, E.2    Smith, C.L.3
  • 50
    • 33744963443 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors repress the transactivation potential of hypoxia-inducible factors independently of direct acetylation of HIF-alpha
    • Fath DM, Kong X, Liang D et al. Histone deacetylase inhibitors repress the transactivation potential of hypoxia-inducible factors independently of direct acetylation of HIF-alpha. J Biol Chem 2006; 281(19): 13612-9.
    • (2006) J Biol Chem , vol.281 , Issue.19 , pp. 13612-13619
    • Fath, D.M.1    Kong, X.2    Liang, D.3
  • 51
    • 77449159578 scopus 로고    scopus 로고
    • Complex regulation of the transactivation function of hypoxia-inducible factor-1 alpha by direct interaction with two distinct domains of the CREB-binding protein/p300
    • Ruas JL, Berchner-Pfannschmidt U, Malik S et al. Complex regulation of the transactivation function of hypoxia-inducible factor-1 alpha by direct interaction with two distinct domains of the CREB-binding protein/p300. J Biol Chem 2010; 285(4): 2601-9.
    • (2010) J Biol Chem , vol.285 , Issue.4 , pp. 2601-2609
    • Ruas, J.L.1    Berchner-Pfannschmidt, U.2    Malik, S.3
  • 52
    • 33947217916 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors synergize p300 autoacetylation that regulates its transactivation activity and complex formation
    • Stiehl DP, Fath DM, Liang D, Jiang Y, Sang N. Histone deacetylase inhibitors synergize p300 autoacetylation that regulates its transactivation activity and complex formation. Cancer Res 2007; 67(5): 2256-64.
    • (2007) Cancer Res , vol.67 , Issue.5 , pp. 2256-2264
    • Stiehl, D.P.1    Fath, D.M.2    Liang, D.3    Jiang, Y.4    Sang, N.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.