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Volumn 3, Issue 2, 2005, Pages 0210-0220

SIRT1 regulates HIV transcription via Tat deacetylation

Author keywords

[No Author keywords available]

Indexed keywords

NICOTINAMIDE ADENINE DINUCLEOTIDE; PROTEIN INHIBITOR; PROTEIN P300; SILENT INFORMATION REGULATOR PROTEIN 2; SIRTUIN; SIRTUIN 1; SMALL INTERFERING RNA; TRANSACTIVATOR PROTEIN; UNCLASSIFIED DRUG; VIRUS PROTEIN; HISTONE DEACETYLASE; PRIMER DNA; SIRT1 PROTEIN, HUMAN;

EID: 20144372893     PISSN: 15449173     EISSN: 15457885     Source Type: Journal    
DOI: 10.1371/journal.pbio.0030041     Document Type: Article
Times cited : (293)

References (64)
  • 1
    • 0023513563 scopus 로고
    • Anti-termination of transcription within the long terminal repeat of HIV-1 by tat gene product
    • Kao SY, Calman AF, Luciw PA, Peterlin BM (1987) Anti-termination of transcription within the long terminal repeat of HIV-1 by tat gene product. Nature 330: 489-493.
    • (1987) Nature , vol.330 , pp. 489-493
    • Kao, S.Y.1    Calman, A.F.2    Luciw, P.A.3    Peterlin, B.M.4
  • 2
    • 0024635688 scopus 로고
    • In vitro formation of short RNA polymerase II transcripts that terminate within the HIV-1 and HIV-2 promoter-proximal downstream regions
    • Toohey MG, Jones KA (1989) In vitro formation of short RNA polymerase II transcripts that terminate within the HIV-1 and HIV-2 promoter-proximal downstream regions. Genes Dev 3: 265-282.
    • (1989) Genes Dev , vol.3 , pp. 265-282
    • Toohey, M.G.1    Jones, K.A.2
  • 3
    • 0022006369 scopus 로고
    • The location of cis-acting regulatory sequences in the human T cell lymphotropic virus type III (HTLV-III/LAV) long terminal repeat
    • Rosen CA, Sodroski JG, Haseltine WA (1985) The location of cis-acting regulatory sequences in the human T cell lymphotropic virus type III (HTLV-III/LAV) long terminal repeat. Cell 41: 813-823.
    • (1985) Cell , vol.41 , pp. 813-823
    • Rosen, C.A.1    Sodroski, J.G.2    Haseltine, W.A.3
  • 4
    • 0023876147 scopus 로고
    • HIV-1 tat trans-activation requires the loop sequence within tar
    • Feng S, Holland EC (1988) HIV-1 tat trans-activation requires the loop sequence within tar. Nature 334: 165-167.
    • (1988) Nature , vol.334 , pp. 165-167
    • Feng, S.1    Holland, E.C.2
  • 5
    • 0032548918 scopus 로고    scopus 로고
    • A novel CDK9-associated C-type cyclin interacts directly with HIV-1 Tat and mediates its high-affinity, loop-specific binding to TAR RNA
    • Wei P, Garber ME, Fang SM, Fischer WH, Jones KA (1998) A novel CDK9-associated C-type cyclin interacts directly with HIV-1 Tat and mediates its high-affinity, loop-specific binding to TAR RNA. Cell 92: 451-462.
    • (1998) Cell , vol.92 , pp. 451-462
    • Wei, P.1    Garber, M.E.2    Fang, S.M.3    Fischer, W.H.4    Jones, K.A.5
  • 6
    • 15144348173 scopus 로고    scopus 로고
    • Transcription elongation factor P-TEFb is required for HIV-1 tat transactivation in vitro
    • Zhu Y, Pe'ery T, Peng J, Ramanathan Y, Marshall N, et al. (1997) Transcription elongation factor P-TEFb is required for HIV-1 tat transactivation in vitro. Genes Dev 11: 2622-2632.
    • (1997) Genes Dev , vol.11 , pp. 2622-2632
    • Zhu, Y.1    Pe'ery, T.2    Peng, J.3    Ramanathan, Y.4    Marshall, N.5
  • 7
    • 0033230613 scopus 로고    scopus 로고
    • HIV-1 tat transcriptional activity is regulated by acetylation
    • Kiernan RE, Vanhulle C, Schiltz L, Adam E, Xiao H, et al. (1999) HIV-1 tat transcriptional activity is regulated by acetylation. EMBO J 18: 6106-6118.
    • (1999) EMBO J , vol.18 , pp. 6106-6118
    • Kiernan, R.E.1    Vanhulle, C.2    Schiltz, L.3    Adam, E.4    Xiao, H.5
  • 8
    • 0033576557 scopus 로고    scopus 로고
    • Acetylation of the HIV-1 Tat protein by p300 is important for its transcriptional activity
    • Ott M, Schnolzer M, Garnica J, Fischle W, Emiliani S, et al. (1999) Acetylation of the HIV-1 Tat protein by p300 is important for its transcriptional activity. Curr Biol 9: 1489-1492.
    • (1999) Curr Biol , vol.9 , pp. 1489-1492
    • Ott, M.1    Schnolzer, M.2    Garnica, J.3    Fischle, W.4    Emiliani, S.5
  • 9
    • 0034715791 scopus 로고    scopus 로고
    • Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated HIV-1 genome and enhances binding to core histones
    • Deng L, de la Fuente C, Fu P, Wang L, Donnelly R, et al. (2000) Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated HIV-1 genome and enhances binding to core histones. Virology 277: 278-295.
    • (2000) Virology , vol.277 , pp. 278-295
    • Deng, L.1    De La Fuente, C.2    Fu, P.3    Wang, L.4    Donnelly, R.5
  • 10
    • 0035958946 scopus 로고    scopus 로고
    • The histone acetyltransferase, hGCN5, interacts with and acetylates the HIV transactivator, Tat
    • Col E, Caron C, Seigneurin-Berny D, Gracia J, Favier A, et al. (2001) The histone acetyltransferase, hGCN5, interacts with and acetylates the HIV transactivator, Tat. J Biol Chem 276: 28179-28184.
    • (2001) J Biol Chem , vol.276 , pp. 28179-28184
    • Col, E.1    Caron, C.2    Seigneurin-Berny, D.3    Gracia, J.4    Favier, A.5
  • 11
    • 0042671259 scopus 로고    scopus 로고
    • Acetylation of Tat defines a cyclinT1-independent step in HIV transactivation
    • Kaehlcke K, Dorr A, Hetzer-Egger C, Kiermer V, Henklein P, et al. (2003) Acetylation of Tat defines a cyclinT1-independent step in HIV transactivation. Mol Cell 12: 167-176.
    • (2003) Mol Cell , vol.12 , pp. 167-176
    • Kaehlcke, K.1    Dorr, A.2    Hetzer-Egger, C.3    Kiermer, V.4    Henklein, P.5
  • 12
    • 0036206045 scopus 로고    scopus 로고
    • Structural basis of lysine-acetylated HIV-1 Tat recognition by PCAF bromodomain
    • Mujtaba S, He Y, Zeng L, Farooq A, Carlson JE, et al. (2002) Structural basis of lysine-acetylated HIV-1 Tat recognition by PCAF bromodomain. Mol Cell 9: 575-586.
    • (2002) Mol Cell , vol.9 , pp. 575-586
    • Mujtaba, S.1    He, Y.2    Zeng, L.3    Farooq, A.4    Carlson, J.E.5
  • 13
    • 0037013851 scopus 로고    scopus 로고
    • Transcriptional synergy between Tat and PCAF is dependent on the binding of acetylated Tat to the PCAF bromodomain
    • Dorr A, Kiermer V, Pedal A, Rackwitz HR, Henklein P, et al. (2002) Transcriptional synergy between Tat and PCAF is dependent on the binding of acetylated Tat to the PCAF bromodomain. EMBO J 21: 2715-2723.
    • (2002) EMBO J , vol.21 , pp. 2715-2723
    • Dorr, A.1    Kiermer, V.2    Pedal, A.3    Rackwitz, H.R.4    Henklein, P.5
  • 15
    • 0037406061 scopus 로고    scopus 로고
    • Class II histone deacetylases: Versatile regulators
    • Verdin E, Dequiedt F, Kasler HG (2003) Class II histone deacetylases: Versatile regulators. Trends Genet 19: 286-293.
    • (2003) Trends Genet , vol.19 , pp. 286-293
    • Verdin, E.1    Dequiedt, F.2    Kasler, H.G.3
  • 16
    • 0035861202 scopus 로고    scopus 로고
    • The molecular biology of the SIR proteins
    • Gasser SM, Cockell MM (2001) The molecular biology of the SIR proteins. Gene 279: 1-16.
    • (2001) Gene , vol.279 , pp. 1-16
    • Gasser, S.M.1    Cockell, M.M.2
  • 17
    • 0034677535 scopus 로고    scopus 로고
    • Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
    • Imai S, Armstrong CM, Kaeberlein M, Guarente L (2000) Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase. Nature 403: 795-800.
    • (2000) Nature , vol.403 , pp. 795-800
    • Imai, S.1    Armstrong, C.M.2    Kaeberlein, M.3    Guarente, L.4
  • 18
    • 0034705129 scopus 로고    scopus 로고
    • The silencing protein SIR2 and its homologs are NAD-dependent protein deacetylases
    • Landry J, Sutton A, Tafrov ST, Heller RC, Stebbins J, et al. (2000) The silencing protein SIR2 and its homologs are NAD-dependent protein deacetylases. Proc Natl Acad Sci U S A 97: 5807-5811.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 5807-5811
    • Landry, J.1    Sutton, A.2    Tafrov, S.T.3    Heller, R.C.4    Stebbins, J.5
  • 20
    • 2942564591 scopus 로고    scopus 로고
    • Sirtuins: Sir2-related NAD-dependent protein deacetylases
    • North BJ, Verdin E (2004) Sirtuins: Sir2-related NAD-dependent protein deacetylases. Genome Biol 5: 224.
    • (2004) Genome Biol , vol.5 , pp. 224
    • North, B.J.1    Verdin, E.2
  • 21
    • 0035913911 scopus 로고    scopus 로고
    • Negative control of p53 by Sir2α promotes cell survival under stress
    • Luo J, Nikolaev AY, Imai S, Chen D, Su F, et al. (2001) Negative control of p53 by Sir2α promotes cell survival under stress. Cell 107: 137-148.
    • (2001) Cell , vol.107 , pp. 137-148
    • Luo, J.1    Nikolaev, A.Y.2    Imai, S.3    Chen, D.4    Su, F.5
  • 22
    • 0035913903 scopus 로고    scopus 로고
    • hSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase
    • Vaziri H, Dessain SK, Ng Eaton E, Imai SI, Frye RA, et al. (2001) hSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase. Cell 107: 149-159.
    • (2001) Cell , vol.107 , pp. 149-159
    • Vaziri, H.1    Dessain, S.K.2    Ng Eaton, E.3    Imai, S.I.4    Frye, R.A.5
  • 23
    • 0037093346 scopus 로고    scopus 로고
    • Human SIR2 deacetylates p53 and antagonizes PML/p53-induced cellular senescence
    • Langley E, Pearson M, Faretta M, Bauer UM, Frye RA, et al. (2002) Human SIR2 deacetylates p53 and antagonizes PML/p53-induced cellular senescence. EMBO J 21: 2383-2396.
    • (2002) EMBO J , vol.21 , pp. 2383-2396
    • Langley, E.1    Pearson, M.2    Faretta, M.3    Bauer, U.M.4    Frye, R.A.5
  • 24
    • 0035868764 scopus 로고    scopus 로고
    • I68, a subunit of TIF-IB/SL1, activates RNA polymerase I transcription
    • I68, a subunit of TIF-IB/SL1, activates RNA polymerase I transcription. EMBO J 20: 1353-1362.
    • (2001) EMBO J , vol.20 , pp. 1353-1362
    • Muth, V.1    Nadaud, S.2    Grummt, I.3    Voit, R.4
  • 25
    • 0043244921 scopus 로고    scopus 로고
    • Sir2 regulates skeletal muscle differentiation as a potential sensor of the redox state
    • Fulco M, Schiltz RL, Iezzi S, King MT, Zhao P, et al. (2003) Sir2 regulates skeletal muscle differentiation as a potential sensor of the redox state. Mol Cell 12: 51-62.
    • (2003) Mol Cell , vol.12 , pp. 51-62
    • Fulco, M.1    Schiltz, R.L.2    Iezzi, S.3    King, M.T.4    Zhao, P.5
  • 26
    • 1342264308 scopus 로고    scopus 로고
    • Mammalian SIRT1 represses forkhead transcription factors
    • Motta MC, Divecha N, Lemieux M, Kamel C, Chen D, et al. (2004) Mammalian SIRT1 represses forkhead transcription factors. Cell 116: 551-563.
    • (2004) Cell , vol.116 , pp. 551-563
    • Motta, M.C.1    Divecha, N.2    Lemieux, M.3    Kamel, C.4    Chen, D.5
  • 27
    • 12144290563 scopus 로고    scopus 로고
    • Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase
    • Brunet A, Sweeney LB, Sturgill JF, Chua KF, Greer PL, et al. (2004) Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase. Science 303: 2011-2015.
    • (2004) Science , vol.303 , pp. 2011-2015
    • Brunet, A.1    Sweeney, L.B.2    Sturgill, J.F.3    Chua, K.F.4    Greer, P.L.5
  • 28
    • 3242719545 scopus 로고    scopus 로고
    • Modulation of NF-κB-dependent transcription and cell survival by the SIRT1 deacetylase
    • Yeung F, Hoberg JE, Ramsey CS, Keller MD, Jones DR, et al. (2004) Modulation of NF-κB-dependent transcription and cell survival by the SIRT1 deacetylase. EMBO J 23: 2369-2380.
    • (2004) EMBO J , vol.23 , pp. 2369-2380
    • Yeung, F.1    Hoberg, J.E.2    Ramsey, C.S.3    Keller, M.D.4    Jones, D.R.5
  • 29
    • 3142740860 scopus 로고    scopus 로고
    • Calorie restriction promotes mammalian cell survival by inducing the SIRT1 deacetylase
    • Cohen HY, Miller C, Bitterman KJ, Wall NR, Hekking B, et al. (2004) Calorie restriction promotes mammalian cell survival by inducing the SIRT1 deacetylase. Science 305: 390-392.
    • (2004) Science , vol.305 , pp. 390-392
    • Cohen, H.Y.1    Miller, C.2    Bitterman, K.J.3    Wall, N.R.4    Hekking, B.5
  • 31
    • 0037135972 scopus 로고    scopus 로고
    • The human silent information regulator (Sir)2 homologue hSIRT3 is a mitochondrial nicotinamide adenine dinucleotide-dependent deacetylase
    • Schwer B, North BJ, Frye RA, Ott M, Verdin E (2002) The human silent information regulator (Sir)2 homologue hSIRT3 is a mitochondrial nicotinamide adenine dinucleotide-dependent deacetylase. J Cell Biol 158: 647-657.
    • (2002) J Cell Biol , vol.158 , pp. 647-657
    • Schwer, B.1    North, B.J.2    Frye, R.A.3    Ott, M.4    Verdin, E.5
  • 33
    • 4944245398 scopus 로고    scopus 로고
    • Human SirT1 interacts with histone H1 and promotes formation of facultative heterochromatin
    • Vaquero A, Scher M, Lee D, Erdjument-Bromage H, Tempst P, et al. (2004) Human SirT1 interacts with histone H1 and promotes formation of facultative heterochromatin. Mol Cell 16: 93-105.
    • (2004) Mol Cell , vol.16 , pp. 93-105
    • Vaquero, A.1    Scher, M.2    Lee, D.3    Erdjument-Bromage, H.4    Tempst, P.5
  • 35
    • 0037160097 scopus 로고    scopus 로고
    • Inhibition of silencing and accelerated aging by nicotinamide, a putative negative regulator of yeast sir2 and human SIRT1
    • Bitterman KJ, Anderson RM, Cohen HY, Latorre-Esteves M, Sinclair DA (2002) Inhibition of silencing and accelerated aging by nicotinamide, a putative negative regulator of yeast sir2 and human SIRT1. J Biol Chem 277: 45099-45107.
    • (2002) J Biol Chem , vol.277 , pp. 45099-45107
    • Bitterman, K.J.1    Anderson, R.M.2    Cohen, H.Y.3    Latorre-Esteves, M.4    Sinclair, D.A.5
  • 36
    • 0035942736 scopus 로고    scopus 로고
    • Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells
    • Elbashir SM, Harborth J, Lendeckel W, Yalcin A, Weber K, et al. (2001) Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells. Nature 411: 494-498.
    • (2001) Nature , vol.411 , pp. 494-498
    • Elbashir, S.M.1    Harborth, J.2    Lendeckel, W.3    Yalcin, A.4    Weber, K.5
  • 37
    • 0037207475 scopus 로고    scopus 로고
    • The mammalian SIR2α protein has a role in embryogenesis and gametogenesis
    • McBurney MW, Yang X, Jardine K, Hixon M, Boekelheide K, et al. (2003) The mammalian SIR2α protein has a role in embryogenesis and gametogenesis. Mol Cell Biol 23: 38-54.
    • (2003) Mol Cell Biol , vol.23 , pp. 38-54
    • McBurney, M.W.1    Yang, X.2    Jardine, K.3    Hixon, M.4    Boekelheide, K.5
  • 38
    • 0032533253 scopus 로고    scopus 로고
    • The interaction between HIV-1 Tat and human cyclin T1 requires zinc and a critical cysteine residue that is not conserved in the murine CycT1 protein
    • Garber ME, Wei P, KewalRamani VN, Mayall TP, Herrmann CH, et al. (1998) The interaction between HIV-1 Tat and human cyclin T1 requires zinc and a critical cysteine residue that is not conserved in the murine CycT1 protein. Genes Dev 12: 3512-3527.
    • (1998) Genes Dev , vol.12 , pp. 3512-3527
    • Garber, M.E.1    Wei, P.2    KewalRamani, V.N.3    Mayall, T.P.4    Herrmann, C.H.5
  • 39
    • 0032401752 scopus 로고    scopus 로고
    • Recruitment of a protein complex containing Tat and cyclin T1 to TAR governs the species specificity of HIV-1 Tat
    • Bieniasz PD, Grdina TA, Bogerd HP, Cullen BR (1998) Recruitment of a protein complex containing Tat and cyclin T1 to TAR governs the species specificity of HIV-1 Tat. EMBO J 17: 7056-7065.
    • (1998) EMBO J , vol.17 , pp. 7056-7065
    • Bieniasz, P.D.1    Grdina, T.A.2    Bogerd, H.P.3    Cullen, B.R.4
  • 40
    • 0025162336 scopus 로고
    • A bulge structure in HIV-1 TAR RNA is required for Tat binding and Tat-mediated trans-activation
    • Roy S, Delling U, Chen CH, Rosen CA, Sonenberg N (1990) A bulge structure in HIV-1 TAR RNA is required for Tat binding and Tat-mediated trans-activation. Genes Dev 4: 1365-1373.
    • (1990) Genes Dev , vol.4 , pp. 1365-1373
    • Roy, S.1    Delling, U.2    Chen, C.H.3    Rosen, C.A.4    Sonenberg, N.5
  • 43
    • 0037446948 scopus 로고    scopus 로고
    • HIV reproducibly establishes a latent infection after acute infection of T cells in vitro
    • Jordan A, Bisgrove D, Verdin E (2003) HIV reproducibly establishes a latent infection after acute infection of T cells in vitro. EMBO J 22: 1868-1877.
    • (2003) EMBO J , vol.22 , pp. 1868-1877
    • Jordan, A.1    Bisgrove, D.2    Verdin, E.3
  • 44
    • 0242322010 scopus 로고    scopus 로고
    • Involvement of the histone deacetylase SIRT1 in chicken ovalbumin upstream promoter transcription factor (COUP-TF)-interacting protein 2-mediated transcriptional repression
    • Senawong T, Peterson VJ, Avram D, Shepherd DM, Frye RA, et al. (2003) Involvement of the histone deacetylase SIRT1 in chicken ovalbumin upstream promoter transcription factor (COUP-TF)-interacting protein 2-mediated transcriptional repression. J Biol Chem 278: 43041-43050.
    • (2003) J Biol Chem , vol.278 , pp. 43041-43050
    • Senawong, T.1    Peterson, V.J.2    Avram, D.3    Shepherd, D.M.4    Frye, R.A.5
  • 45
    • 0037474507 scopus 로고    scopus 로고
    • Human Sir2-related protein SIRT1 associates with the bHLH repressors HES1 and HEY2 and is involved in HES1- and HEY2-mediated transcriptional repression
    • Takata T, Ishikawa F (2003) Human Sir2-related protein SIRT1 associates with the bHLH repressors HES1 and HEY2 and is involved in HES1- and HEY2-mediated transcriptional repression. Biochem Biophys Res Commun 301: 250-257.
    • (2003) Biochem Biophys Res Commun , vol.301 , pp. 250-257
    • Takata, T.1    Ishikawa, F.2
  • 46
    • 3042681042 scopus 로고    scopus 로고
    • Sirt1 promotes fat mobilization in white adipocytes by repressing PPAR-γ
    • Picard F, Kurtev M, Chung N, Topark-Ngarm A, Senawong T, et al. (2004) Sirt1 promotes fat mobilization in white adipocytes by repressing PPAR-γ. Nature 429: 771-776.
    • (2004) Nature , vol.429 , pp. 771-776
    • Picard, F.1    Kurtev, M.2    Chung, N.3    Topark-Ngarm, A.4    Senawong, T.5
  • 47
    • 0037377060 scopus 로고    scopus 로고
    • Ubiquitination, phosphorylation and acetylation: The molecular basis for p53 regulation
    • Brooks CL, Gu W (2003) Ubiquitination, phosphorylation and acetylation: The molecular basis for p53 regulation. Curr Opin Cell Biol 15: 164-171.
    • (2003) Curr Opin Cell Biol , vol.15 , pp. 164-171
    • Brooks, C.L.1    Gu, W.2
  • 48
    • 0141814680 scopus 로고    scopus 로고
    • Developmental defects and p53 hyperacetylation in Sir2 homolog (SIRT1)-deficient mice
    • Cheng HL, Mostoslavsky R, Saito S, Manis JP, Gu Y, et al. (2003) Developmental defects and p53 hyperacetylation in Sir2 homolog (SIRT1)-deficient mice. Proc Natl Acad Sci U S A 100: 10794-10799.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 10794-10799
    • Cheng, H.L.1    Mostoslavsky, R.2    Saito, S.3    Manis, J.P.4    Gu, Y.5
  • 49
    • 0037881853 scopus 로고    scopus 로고
    • Recruitment of human cyclin T1 to nuclear bodies through direct interaction with the PML protein
    • Marcello A, Ferrari A, Pellegrini V, Pegoraro G, Lusic M, et al. (2003) Recruitment of human cyclin T1 to nuclear bodies through direct interaction with the PML protein. EMBO J 22: 2156-2166.
    • (2003) EMBO J , vol.22 , pp. 2156-2166
    • Marcello, A.1    Ferrari, A.2    Pellegrini, V.3    Pegoraro, G.4    Lusic, M.5
  • 50
    • 0034676439 scopus 로고    scopus 로고
    • Deacetylation of p53 modulates its effect on cell growth and apoptosis
    • Luo J, Su F, Chen D, Shiloh A, Gu W (2000) Deacetylation of p53 modulates its effect on cell growth and apoptosis. Nature 408: 377-381.
    • (2000) Nature , vol.408 , pp. 377-381
    • Luo, J.1    Su, F.2    Chen, D.3    Shiloh, A.4    Gu, W.5
  • 51
    • 0033929108 scopus 로고    scopus 로고
    • The human factors YY1 and LSF repress the human immunode.ciency virus type 1 long terminal repeat via recruitment of histone deacetylase 1
    • Coull JJ, Romerio F, Sun JM, Volker JL, Galvin KM, et al. (2000) The human factors YY1 and LSF repress the human immunode.ciency virus type 1 long terminal repeat via recruitment of histone deacetylase 1. J Virol 74: 6790-6799.
    • (2000) J Virol , vol.74 , pp. 6790-6799
    • Coull, J.J.1    Romerio, F.2    Sun, J.M.3    Volker, J.L.4    Galvin, K.M.5
  • 52
    • 10744228109 scopus 로고    scopus 로고
    • HIV-1 Nef mimics an integrin receptor signal that recruits the polycomb group protein Eed to the plasma membrane
    • Witte V, Laffert B, Rosorius O, Lischka P, Blume K, et al. (2004) HIV-1 Nef mimics an integrin receptor signal that recruits the polycomb group protein Eed to the plasma membrane. Mol Cell 13: 179-190.
    • (2004) Mol Cell , vol.13 , pp. 179-190
    • Witte, V.1    Laffert, B.2    Rosorius, O.3    Lischka, P.4    Blume, K.5
  • 53
    • 0035979737 scopus 로고    scopus 로고
    • Duration of nuclear NF-κB action regulated by reversible acetylation
    • Chen L, Fischle W, Verdin E, Greene WC (2001) Duration of nuclear NF-κB action regulated by reversible acetylation. Science 293: 1653-1657.
    • (2001) Science , vol.293 , pp. 1653-1657
    • Chen, L.1    Fischle, W.2    Verdin, E.3    Greene, W.C.4
  • 54
    • 0029919356 scopus 로고    scopus 로고
    • Transcriptional activation and chromatin remodeling of the HIV-1 promoter in response to histone acetylation
    • Van Lint C, Emiliani S, Ott M, Verdin E (1996) Transcriptional activation and chromatin remodeling of the HIV-1 promoter in response to histone acetylation. EMBO J 15: 1112-1120.
    • (1996) EMBO J , vol.15 , pp. 1112-1120
    • Van Lint, C.1    Emiliani, S.2    Ott, M.3    Verdin, E.4
  • 55
    • 0029901662 scopus 로고    scopus 로고
    • A point mutation in the HIV-1 Tat responsive element is associated with postintegration latency
    • Emiliani S, Van Lint C, Fischle W, Paras P, Jr, Ott M, et al. (1996) A point mutation in the HIV-1 Tat responsive element is associated with postintegration latency. Proc Natl Acad Sci U S A 93: 6377-6381.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 6377-6381
    • Emiliani, S.1    Van Lint, C.2    Fischle, W.3    Paras Jr., P.4    Ott, M.5
  • 56
    • 0031455415 scopus 로고    scopus 로고
    • Histone acetyltransferases regulate HIV-1 enhancer activity in vitro
    • Sheridan PL, Mayall TP, Verdin E, Jones KA (1997) Histone acetyltransferases regulate HIV-1 enhancer activity in vitro. Genes Dev 11: 3327-3340.
    • (1997) Genes Dev , vol.11 , pp. 3327-3340
    • Sheridan, P.L.1    Mayall, T.P.2    Verdin, E.3    Jones, K.A.4
  • 57
    • 0033231604 scopus 로고    scopus 로고
    • Acetylation of MyoD directed by PCAF is necessary for the execution of the muscle program
    • Sartorelli V, Puri PL, Hamamori Y, Ogryzko V, Chung G, et al. (1999) Acetylation of MyoD directed by PCAF is necessary for the execution of the muscle program. Mol Cell 4: 725-734.
    • (1999) Mol Cell , vol.4 , pp. 725-734
    • Sartorelli, V.1    Puri, P.L.2    Hamamori, Y.3    Ogryzko, V.4    Chung, G.5
  • 58
    • 0031931047 scopus 로고    scopus 로고
    • Mutations in the tat gene are responsible for human immunode.ciency virus type 1 postintegration latency in the U1 cell line
    • Emiliani S, Fischle W, Ott M, Van Lint C, Amella CA, et al. (1998) Mutations in the tat gene are responsible for human immunode.ciency virus type 1 postintegration latency in the U1 cell line. J Virol 72: 1666-1670.
    • (1998) J Virol , vol.72 , pp. 1666-1670
    • Emiliani, S.1    Fischle, W.2    Ott, M.3    Van Lint, C.4    Amella, C.A.5
  • 59
    • 0032589689 scopus 로고    scopus 로고
    • Activation of PPARγ coactivator-1 through transcription factor docking
    • Puigserver P, Adelmant G, Wu Z, Fan M, Xu J, et al. (1999) Activation of PPARγ coactivator-1 through transcription factor docking. Science 286: 1368-1371.
    • (1999) Science , vol.286 , pp. 1368-1371
    • Puigserver, P.1    Adelmant, G.2    Wu, Z.3    Fan, M.4    Xu, J.5
  • 60
    • 0031054036 scopus 로고    scopus 로고
    • Immune hyperactivation of HIV-1-infected T cells mediated by Tat and the CD28 pathway
    • Ott M, Emiliani S, Van Lint C, Herbein G, Lovett J, et al. (1997) Immune hyperactivation of HIV-1-infected T cells mediated by Tat and the CD28 pathway. Science 275: 1481-1485.
    • (1997) Science , vol.275 , pp. 1481-1485
    • Ott, M.1    Emiliani, S.2    Van Lint, C.3    Herbein, G.4    Lovett, J.5
  • 61
    • 1542780457 scopus 로고
    • Condensation of monosubstituted isopropylidene malonates with mannich bases
    • Jacobs RT, Wright AD, Smith FX (1982) Condensation of monosubstituted isopropylidene malonates with mannich bases. J Org Chem 47: 3769-3772.
    • (1982) J Org Chem , vol.47 , pp. 3769-3772
    • Jacobs, R.T.1    Wright, A.D.2    Smith, F.X.3
  • 63
    • 0029996147 scopus 로고    scopus 로고
    • In vivo gene delivery and stable transduction of nondividing cells by a lentiviral vector
    • Naldini L, Blomer U, Gallay P, Ory D, Mulligan R, et al. (1996) In vivo gene delivery and stable transduction of nondividing cells by a lentiviral vector. Science 272: 263-267.
    • (1996) Science , vol.272 , pp. 263-267
    • Naldini, L.1    Blomer, U.2    Gallay, P.3    Ory, D.4    Mulligan, R.5
  • 64
    • 0030819379 scopus 로고    scopus 로고
    • Multiply attenuated lentiviral vector achieves ef.cient gene delivery in vivo
    • Zufferey R, Nagy D, Mandel RJ, Naldini L, Trono D (1997) Multiply attenuated lentiviral vector achieves ef.cient gene delivery in vivo. Nat Biotechnol 15: 871-875.
    • (1997) Nat Biotechnol , vol.15 , pp. 871-875
    • Zufferey, R.1    Nagy, D.2    Mandel, R.J.3    Naldini, L.4    Trono, D.5


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