메뉴 건너뛰기




Volumn 479-480, Issue , 2015, Pages 555-561

Dynamic modulation of HSV chromatin drives initiation of infection and provides targets for epigenetic therapies

Author keywords

Chromatin; Demethylase; HCF 1; Herpes simplex virus; JMJD2; Latency; LSD1

Indexed keywords

CHROMATIN; TRANSCRIPTION FACTOR;

EID: 84938904549     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2015.01.026     Document Type: Review
Times cited : (45)

References (70)
  • 1
    • 53849134844 scopus 로고    scopus 로고
    • Cellular reservoirs of HIV-1 and their role in viral persistence
    • Alexaki A., Liu Y., Wigdahl B. Cellular reservoirs of HIV-1 and their role in viral persistence. Curr. HIV Res. 2008, 6:388-400.
    • (2008) Curr. HIV Res. , vol.6 , pp. 388-400
    • Alexaki, A.1    Liu, Y.2    Wigdahl, B.3
  • 3
    • 32444451768 scopus 로고    scopus 로고
    • Deacetylation of the herpes simplex virus type 1 latency-associated transcript (LAT) enhancer and a decrease in LAT abundance precede an increase in ICP0 transcriptional permissiveness at early times postexplant
    • Amelio A.L., Giordani N.V., Kubat N.J., O'Neil J E., Bloom D.C. Deacetylation of the herpes simplex virus type 1 latency-associated transcript (LAT) enhancer and a decrease in LAT abundance precede an increase in ICP0 transcriptional permissiveness at early times postexplant. J. Virol. 2006, 80:2063-2068.
    • (2006) J. Virol. , vol.80 , pp. 2063-2068
    • Amelio, A.L.1    Giordani, N.V.2    Kubat, N.J.3    O'Neil, J.E.4    Bloom, D.C.5
  • 4
    • 84903365431 scopus 로고    scopus 로고
    • Epigenetic repression of herpes simplex virus infection by the nucleosome remodeler CHD3
    • e01027-01013
    • Arbuckle J.H., Kristie T.M. Epigenetic repression of herpes simplex virus infection by the nucleosome remodeler CHD3. MBio 2014, 5:e01027-01013.
    • (2014) MBio , vol.5
    • Arbuckle, J.H.1    Kristie, T.M.2
  • 6
    • 79955122311 scopus 로고    scopus 로고
    • Cellular SNF2H chromatin-remodeling factor promotes herpes simplex virus 1 immediate-early gene expression and replication
    • e00330-00310
    • Bryant K.F., Colgrove R.C., Knipe D.M. Cellular SNF2H chromatin-remodeling factor promotes herpes simplex virus 1 immediate-early gene expression and replication. MBio 2011, 2:e00330-00310.
    • (2011) MBio , vol.2
    • Bryant, K.F.1    Colgrove, R.C.2    Knipe, D.M.3
  • 9
    • 79951990287 scopus 로고    scopus 로고
    • Curing HIV: pharmacologic approaches to target HIV-1 latency
    • Choudhary S.K., Margolis D.M. Curing HIV: pharmacologic approaches to target HIV-1 latency. Annu. Rev. Pharmacol. Toxicol. 2011, 51:397-418.
    • (2011) Annu. Rev. Pharmacol. Toxicol. , vol.51 , pp. 397-418
    • Choudhary, S.K.1    Margolis, D.M.2
  • 10
    • 84939879196 scopus 로고    scopus 로고
    • HIV-1 transcriptional regulation in the central nervous system and implications for HIV cure research
    • Churchill M.J., Cowley D.J., Wesselingh S.L., Gorry P.R., Gray L.R. HIV-1 transcriptional regulation in the central nervous system and implications for HIV cure research. J. Neurovirol. 2014, 10.1007/s13365-014-0271-5.
    • (2014) J. Neurovirol.
    • Churchill, M.J.1    Cowley, D.J.2    Wesselingh, S.L.3    Gorry, P.R.4    Gray, L.R.5
  • 11
    • 84874617418 scopus 로고    scopus 로고
    • Kinetics of facultative heterochromatin and polycomb group protein association with the herpes simplex viral genome during establishment of latent infection
    • Cliffe A.R., Coen D.M., Knipe D.M. Kinetics of facultative heterochromatin and polycomb group protein association with the herpes simplex viral genome during establishment of latent infection. MBio 2013, 4.
    • (2013) MBio , pp. 4
    • Cliffe, A.R.1    Coen, D.M.2    Knipe, D.M.3
  • 12
    • 67749108444 scopus 로고    scopus 로고
    • Transcription of the herpes simplex virus latency-associated transcript promotes the formation of facultative heterochromatin on lytic promoters
    • Cliffe A.R., Garber D.A., Knipe D.M. Transcription of the herpes simplex virus latency-associated transcript promotes the formation of facultative heterochromatin on lytic promoters. J. Virol. 2009, 83:8182-8190.
    • (2009) J. Virol. , vol.83 , pp. 8182-8190
    • Cliffe, A.R.1    Garber, D.A.2    Knipe, D.M.3
  • 13
    • 57349146688 scopus 로고    scopus 로고
    • Herpes simplex virus ICP0 promotes both histone removal and acetylation on viral DNA during lytic infection
    • Cliffe A.R., Knipe D.M. Herpes simplex virus ICP0 promotes both histone removal and acetylation on viral DNA during lytic infection. J. Virol. 2008, 82:12030-12038.
    • (2008) J. Virol. , vol.82 , pp. 12030-12038
    • Cliffe, A.R.1    Knipe, D.M.2
  • 15
    • 78149490787 scopus 로고    scopus 로고
    • Changes to euchromatin on LAT and ICP4 following reactivation are more prevalent in an efficiently reactivating strain of HSV-1
    • Creech C.C., Neumann D.M. Changes to euchromatin on LAT and ICP4 following reactivation are more prevalent in an efficiently reactivating strain of HSV-1. PloS One 2010, 5:e15416.
    • (2010) PloS One , vol.5 , pp. e15416
    • Creech, C.C.1    Neumann, D.M.2
  • 16
    • 77953955724 scopus 로고    scopus 로고
    • The death-associated protein DAXX is a novel histone chaperone involved in the replication-independent deposition of H3.3
    • Drane P., Ouararhni K., Depaux A., Shuaib M., Hamiche A. The death-associated protein DAXX is a novel histone chaperone involved in the replication-independent deposition of H3.3. Genes Dev. 2010, 24:1253-1265.
    • (2010) Genes Dev. , vol.24 , pp. 1253-1265
    • Drane, P.1    Ouararhni, K.2    Depaux, A.3    Shuaib, M.4    Hamiche, A.5
  • 17
    • 77957670263 scopus 로고    scopus 로고
    • Disruption of HDAC/CoREST/REST repressor by dnREST reduces genome silencing and increases virulence of herpes simplex virus
    • Du T., Zhou G., Khan S., Gu H., Roizman B. Disruption of HDAC/CoREST/REST repressor by dnREST reduces genome silencing and increases virulence of herpes simplex virus. Proc. Natl. Acad. Sci. USA 2010, 107:15904-15909.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 15904-15909
    • Du, T.1    Zhou, G.2    Khan, S.3    Gu, H.4    Roizman, B.5
  • 18
    • 84879510185 scopus 로고    scopus 로고
    • The spatial organization of DNA virus genomes in the nucleus
    • Everett R.D. The spatial organization of DNA virus genomes in the nucleus. PLoS Pathog. 2013, 9:e1003386.
    • (2013) PLoS Pathog. , vol.9 , pp. e1003386
    • Everett, R.D.1
  • 21
    • 79960055393 scopus 로고    scopus 로고
    • KAP-1 phosphorylation regulates CHD3 nucleosome remodeling during the DNA double-strand break response
    • Goodarzi A.A., Kurka T., Jeggo P.A. KAP-1 phosphorylation regulates CHD3 nucleosome remodeling during the DNA double-strand break response. Nat. Struct. Mol. Biol. 2011, 18:831-839.
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 831-839
    • Goodarzi, A.A.1    Kurka, T.2    Jeggo, P.A.3
  • 23
    • 19644384912 scopus 로고    scopus 로고
    • Components of the REST/CoREST/histone deacetylase repressor complex are disrupted, modified, and translocated in HSV-1-infected cells
    • Gu H., Liang Y., Mandel G., Roizman B. Components of the REST/CoREST/histone deacetylase repressor complex are disrupted, modified, and translocated in HSV-1-infected cells. Proc. Natl. Acad. Sci. USA 2005, 102:7571-7576.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 7571-7576
    • Gu, H.1    Liang, Y.2    Mandel, G.3    Roizman, B.4
  • 24
    • 36749032258 scopus 로고    scopus 로고
    • Herpes simplex virus-infected cell protein 0 blocks the silencing of viral DNA by dissociating histone deacetylases from the CoREST-REST complex
    • Gu H., Roizman B. Herpes simplex virus-infected cell protein 0 blocks the silencing of viral DNA by dissociating histone deacetylases from the CoREST-REST complex. Proc. Natl. Acad. Sci. USA 2007, 104:17134-17139.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 17134-17139
    • Gu, H.1    Roizman, B.2
  • 25
    • 84891476446 scopus 로고    scopus 로고
    • Cancer epigenetics: new therapies and new challenges
    • Hatzimichael E., Crook T. Cancer epigenetics: new therapies and new challenges. J. Drug Deliv. 2013, 2013:529312.
    • (2013) J. Drug Deliv. , vol.2013 , pp. 529312
    • Hatzimichael, E.1    Crook, T.2
  • 26
    • 84886808679 scopus 로고    scopus 로고
    • Chromatin proteins and modifications as drug targets
    • Helin K., Dhanak D. Chromatin proteins and modifications as drug targets. Nature 2013, 502:480-488.
    • (2013) Nature , vol.502 , pp. 480-488
    • Helin, K.1    Dhanak, D.2
  • 28
    • 84889573275 scopus 로고    scopus 로고
    • Histone lysine demethylases as targets for anticancer therapy
    • Hojfeldt J.W., Agger K., Helin K. Histone lysine demethylases as targets for anticancer therapy. Nat. Rev. Drug Discov. 2013, 12:917-930.
    • (2013) Nat. Rev. Drug Discov. , vol.12 , pp. 917-930
    • Hojfeldt, J.W.1    Agger, K.2    Helin, K.3
  • 30
    • 4444317361 scopus 로고    scopus 로고
    • Heterochromatin and ND10 are cell-cycle regulated and phosphorylation-dependent alternate nuclear sites of the transcription repressor Daxx and SWI/SNF protein ATRX
    • Ishov A.M., Vladimirova O.V., Maul G.G. Heterochromatin and ND10 are cell-cycle regulated and phosphorylation-dependent alternate nuclear sites of the transcription repressor Daxx and SWI/SNF protein ATRX. J. Cell Sci. 2004, 117:3807-3820.
    • (2004) J. Cell Sci. , vol.117 , pp. 3807-3820
    • Ishov, A.M.1    Vladimirova, O.V.2    Maul, G.G.3
  • 31
    • 84912108081 scopus 로고    scopus 로고
    • IFI16 restricts HSV-1 replication by accumulating on the HSV-1 genome, repressing HSV-1 gene expression, and directly or indirectly modulating histone modifications
    • Johnson K.E., Bottero V., Flaherty S., Dutta S., Singh V.V., Chandran B. IFI16 restricts HSV-1 replication by accumulating on the HSV-1 genome, repressing HSV-1 gene expression, and directly or indirectly modulating histone modifications. PLoS Pathog. 2014, 10:e1004503.
    • (2014) PLoS Pathog. , vol.10 , pp. e1004503
    • Johnson, K.E.1    Bottero, V.2    Flaherty, S.3    Dutta, S.4    Singh, V.V.5    Chandran, B.6
  • 32
    • 78049294795 scopus 로고    scopus 로고
    • Circadian CLOCK histone acetyl transferase localizes at ND10 nuclear bodies and enables herpes simplex virus gene expression
    • Kalamvoki M., Roizman B. Circadian CLOCK histone acetyl transferase localizes at ND10 nuclear bodies and enables herpes simplex virus gene expression. Proc. Natl. Acad. Sci. USA 2010, 107:17721-17726.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 17721-17726
    • Kalamvoki, M.1    Roizman, B.2
  • 33
    • 39149132854 scopus 로고    scopus 로고
    • Chromatin control of herpes simplex virus lytic and latent infection
    • Knipe D.M., Cliffe A. Chromatin control of herpes simplex virus lytic and latent infection. Nat. Rev. Microbiol. 2008, 6:211-221.
    • (2008) Nat. Rev. Microbiol. , vol.6 , pp. 211-221
    • Knipe, D.M.1    Cliffe, A.2
  • 35
    • 77949273931 scopus 로고    scopus 로고
    • Control of alpha-herpesvirus IE gene expression by HCF-1 coupled chromatin modification activities
    • Kristie T.M., Liang Y., Vogel J.L. Control of alpha-herpesvirus IE gene expression by HCF-1 coupled chromatin modification activities. Biochim. Biophys. Acta 2010, 1799:257-265.
    • (2010) Biochim. Biophys. Acta , vol.1799 , pp. 257-265
    • Kristie, T.M.1    Liang, Y.2    Vogel, J.L.3
  • 36
    • 0033573922 scopus 로고    scopus 로고
    • Nuclear localization of the C1 factor (host cell factor) in sensory neurons correlates with reactivation of herpes simplex virus from latency
    • Kristie T.M., Vogel J.L., Sears A.E. Nuclear localization of the C1 factor (host cell factor) in sensory neurons correlates with reactivation of herpes simplex virus from latency. Proc. Natl. Acad. Sci. USA 1999, 96:1229-1233.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 1229-1233
    • Kristie, T.M.1    Vogel, J.L.2    Sears, A.E.3
  • 37
    • 7644226143 scopus 로고    scopus 로고
    • The herpes simplex virus type 1 latency-associated transcript (LAT) enhancer/rcr is hyperacetylated during latency independently of LAT transcription
    • Kubat N.J., Amelio A.L., Giordani N.V., Bloom D.C. The herpes simplex virus type 1 latency-associated transcript (LAT) enhancer/rcr is hyperacetylated during latency independently of LAT transcription. J. Virol. 2004, 78:12508-12518.
    • (2004) J. Virol. , vol.78 , pp. 12508-12518
    • Kubat, N.J.1    Amelio, A.L.2    Giordani, N.V.3    Bloom, D.C.4
  • 38
    • 64049113388 scopus 로고    scopus 로고
    • Transcriptional coactivators are not required for herpes simplex virus type 1 immediate-early gene expression in vitro
    • Kutluay S.B., DeVos S.L., Klomp J.E., Triezenberg S.J. Transcriptional coactivators are not required for herpes simplex virus type 1 immediate-early gene expression in vitro. J. Virol. 2009, 83:3436-3449.
    • (2009) J. Virol. , vol.83 , pp. 3436-3449
    • Kutluay, S.B.1    DeVos, S.L.2    Klomp, J.E.3    Triezenberg, S.J.4
  • 39
    • 67749137595 scopus 로고    scopus 로고
    • The polycomb group protein Bmi1 binds to the herpes simplex virus 1 latent genome and maintains repressive histone marks during latency
    • Kwiatkowski D.L., Thompson H.W., Bloom D.C. The polycomb group protein Bmi1 binds to the herpes simplex virus 1 latent genome and maintains repressive histone marks during latency. J. Virol. 2009, 83:8173-8181.
    • (2009) J. Virol. , vol.83 , pp. 8173-8181
    • Kwiatkowski, D.L.1    Thompson, H.W.2    Bloom, D.C.3
  • 40
    • 75449106558 scopus 로고    scopus 로고
    • During lytic infections, herpes simplex virus type 1 DNA is in complexes with the properties of unstable nucleosomes
    • Lacasse J.J., Schang L.M. During lytic infections, herpes simplex virus type 1 DNA is in complexes with the properties of unstable nucleosomes. J. Virol. 2010, 84:1920-1933.
    • (2010) J. Virol. , vol.84 , pp. 1920-1933
    • Lacasse, J.J.1    Schang, L.M.2
  • 41
    • 84869039149 scopus 로고    scopus 로고
    • Herpes simplex virus 1 DNA is in unstable nucleosomes throughout the lytic infection cycle, and the instability of the nucleosomes is independent of DNA replication
    • Lacasse J.J., Schang L.M. Herpes simplex virus 1 DNA is in unstable nucleosomes throughout the lytic infection cycle, and the instability of the nucleosomes is independent of DNA replication. J. Virol. 2012, 86:11287-11300.
    • (2012) J. Virol. , vol.86 , pp. 11287-11300
    • Lacasse, J.J.1    Schang, L.M.2
  • 42
    • 25144519737 scopus 로고    scopus 로고
    • An essential role for CoREST in nucleosomal histone 3 lysine 4 demethylation
    • Lee M.G., Wynder C., Cooch N., Shiekhattar R. An essential role for CoREST in nucleosomal histone 3 lysine 4 demethylation. Nature 2005, 437:432-435.
    • (2005) Nature , vol.437 , pp. 432-435
    • Lee, M.G.1    Wynder, C.2    Cooch, N.3    Shiekhattar, R.4
  • 44
    • 84874598620 scopus 로고    scopus 로고
    • A novel selective LSD1/KDM1A inhibitor epigenetically blocks herpes simplex virus lytic replication and reactivation from latency
    • e00558-00512
    • Liang Y., Quenelle D., Vogel J.L., Mascaro C., Ortega A., Kristie T.M. A novel selective LSD1/KDM1A inhibitor epigenetically blocks herpes simplex virus lytic replication and reactivation from latency. MBio 2013, 4:e00558-00512.
    • (2013) MBio , vol.4
    • Liang, Y.1    Quenelle, D.2    Vogel, J.L.3    Mascaro, C.4    Ortega, A.5    Kristie, T.M.6
  • 46
    • 70449122130 scopus 로고    scopus 로고
    • Inhibition of the histone demethylase LSD1 blocks alpha-herpesvirus lytic replication and reactivation from latency
    • Liang Y., Vogel J.L., Narayanan A., Peng H., Kristie T.M. Inhibition of the histone demethylase LSD1 blocks alpha-herpesvirus lytic replication and reactivation from latency. Nat. Med. 2009, 15:1312-1317.
    • (2009) Nat. Med. , vol.15 , pp. 1312-1317
    • Liang, Y.1    Vogel, J.L.2    Narayanan, A.3    Peng, H.4    Kristie, T.M.5
  • 48
    • 77950515413 scopus 로고    scopus 로고
    • Regulation of ICP0-null mutant herpes simplex virus type 1 infection by ND10 components ATRX and hDaxx
    • Lukashchuk V., Everett R.D. Regulation of ICP0-null mutant herpes simplex virus type 1 infection by ND10 components ATRX and hDaxx. J. Virol. 2010, 84:4026-4040.
    • (2010) J. Virol. , vol.84 , pp. 4026-4040
    • Lukashchuk, V.1    Everett, R.D.2
  • 50
    • 12544254340 scopus 로고    scopus 로고
    • Combinatorial transcription of herpes simplex virus and varicella zoster virus immediate early genes is strictly determined by the cellular coactivator HCF-1
    • Narayanan A., Nogueira M.L., Ruyechan W.T., Kristie T.M. Combinatorial transcription of herpes simplex virus and varicella zoster virus immediate early genes is strictly determined by the cellular coactivator HCF-1. J. Biol. Chem. 2005, 280:1369-1375.
    • (2005) J. Biol. Chem. , vol.280 , pp. 1369-1375
    • Narayanan, A.1    Nogueira, M.L.2    Ruyechan, W.T.3    Kristie, T.M.4
  • 51
    • 34547467103 scopus 로고    scopus 로고
    • The coactivator host cell factor-1 mediates Set1 and MLL1 H3K4 trimethylation at herpesvirus immediate early promoters for initiation of infection
    • Narayanan A., Ruyechan W.T., Kristie T.M. The coactivator host cell factor-1 mediates Set1 and MLL1 H3K4 trimethylation at herpesvirus immediate early promoters for initiation of infection. Proc. Natl. Acad. Sci. USA 2007, 104:10835-10840.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 10835-10840
    • Narayanan, A.1    Ruyechan, W.T.2    Kristie, T.M.3
  • 53
    • 36348963706 scopus 로고    scopus 로고
    • In vivo changes in the patterns of chromatin structure associated with the latent herpes simplex virus type 1 genome in mouse trigeminal ganglia can be detected at early times after butyrate treatment
    • Neumann D.M., Bhattacharjee P.S., Giordani N.V., Bloom D.C., Hill J.M. In vivo changes in the patterns of chromatin structure associated with the latent herpes simplex virus type 1 genome in mouse trigeminal ganglia can be detected at early times after butyrate treatment. J. Virol. 2007, 81:13248-13253.
    • (2007) J. Virol. , vol.81 , pp. 13248-13253
    • Neumann, D.M.1    Bhattacharjee, P.S.2    Giordani, N.V.3    Bloom, D.C.4    Hill, J.M.5
  • 54
    • 84903365434 scopus 로고    scopus 로고
    • A targeted RNA interference screen reveals novel epigenetic factors that regulate herpesviral gene expression
    • e01086-01013
    • Oh H.S., Bryant K.F., Nieland T.J., Mazumder A., Bagul M., Bathe M., Root D.E., Knipe D.M. A targeted RNA interference screen reveals novel epigenetic factors that regulate herpesviral gene expression. MBio 2014, 5:e01086-01013.
    • (2014) MBio , vol.5
    • Oh, H.S.1    Bryant, K.F.2    Nieland, T.J.3    Mazumder, A.4    Bagul, M.5    Bathe, M.6    Root, D.E.7    Knipe, D.M.8
  • 55
    • 84869145571 scopus 로고    scopus 로고
    • Chromatin assembly on herpes simplex virus 1 DNA early during a lytic infection is Asf1a dependent
    • Oh J., Ruskoski N., Fraser N.W. Chromatin assembly on herpes simplex virus 1 DNA early during a lytic infection is Asf1a dependent. J. Virol. 2012, 86:12313-12321.
    • (2012) J. Virol. , vol.86 , pp. 12313-12321
    • Oh, J.1    Ruskoski, N.2    Fraser, N.W.3
  • 56
  • 57
    • 64749093273 scopus 로고    scopus 로고
    • Direct binding of CoREST1 to SUMO-2/3 contributes to gene-specific repression by the LSD1/CoREST1/HDAC complex
    • Ouyang J., Shi Y., Valin A., Xuan Y., Gill G. Direct binding of CoREST1 to SUMO-2/3 contributes to gene-specific repression by the LSD1/CoREST1/HDAC complex. Mol. Cell 2009, 34:145-154.
    • (2009) Mol. Cell , vol.34 , pp. 145-154
    • Ouyang, J.1    Shi, Y.2    Valin, A.3    Xuan, Y.4    Gill, G.5
  • 58
    • 59749104270 scopus 로고    scopus 로고
    • The histone variant H3.3 regulates gene expression during lytic infection with herpes simplex virus type 1
    • Placek B.J., Huang J., Kent J.R., Dorsey J., Rice L., Fraser N.W., Berger S.L. The histone variant H3.3 regulates gene expression during lytic infection with herpes simplex virus type 1. J. Virol. 2009, 83:1416-1421.
    • (2009) J. Virol. , vol.83 , pp. 1416-1421
    • Placek, B.J.1    Huang, J.2    Kent, J.R.3    Dorsey, J.4    Rice, L.5    Fraser, N.W.6    Berger, S.L.7
  • 59
    • 84922122211 scopus 로고    scopus 로고
    • PML nuclear bodies: regulation, function and therapeutic perspectives
    • Sahin U., Lallemand-Breitenbach V., de The H. PML nuclear bodies: regulation, function and therapeutic perspectives. J. Pathol. 2014, 234:289-291.
    • (2014) J. Pathol. , vol.234 , pp. 289-291
    • Sahin, U.1    Lallemand-Breitenbach, V.2    de The, H.3
  • 60
    • 0037089626 scopus 로고    scopus 로고
    • SETDB1: a novel KAP-1-associated histone H3, lysine 9-specific methyltransferase that contributes to HP1-mediated silencing of euchromatic genes by KRAB zinc-finger proteins
    • Schultz D.C., Ayyanathan K., Negorev D., Maul G.G., Rauscher F.J. SETDB1: a novel KAP-1-associated histone H3, lysine 9-specific methyltransferase that contributes to HP1-mediated silencing of euchromatic genes by KRAB zinc-finger proteins. Genes Dev. 2002, 16:919-932.
    • (2002) Genes Dev. , vol.16 , pp. 919-932
    • Schultz, D.C.1    Ayyanathan, K.2    Negorev, D.3    Maul, G.G.4    Rauscher, F.J.5
  • 61
    • 0035118229 scopus 로고    scopus 로고
    • Targeting histone deacetylase complexes via KRAB-zinc finger proteins: the PHD and bromodomains of KAP-1 form a cooperative unit that recruits a novel isoform of the Mi-2alpha subunit of NuRD
    • Schultz D.C., Friedman J.R., Rauscher F.J. Targeting histone deacetylase complexes via KRAB-zinc finger proteins: the PHD and bromodomains of KAP-1 form a cooperative unit that recruits a novel isoform of the Mi-2alpha subunit of NuRD. Genes Dev. 2001, 15:428-443.
    • (2001) Genes Dev. , vol.15 , pp. 428-443
    • Schultz, D.C.1    Friedman, J.R.2    Rauscher, F.J.3
  • 63
    • 24944535335 scopus 로고    scopus 로고
    • Regulation of LSD1 histone demethylase activity by its associated factors
    • Shi Y.J., Matson C., Lan F., Iwase S., Baba T., Shi Y. Regulation of LSD1 histone demethylase activity by its associated factors. Mol. Cell 2005, 19:857-864.
    • (2005) Mol. Cell , vol.19 , pp. 857-864
    • Shi, Y.J.1    Matson, C.2    Lan, F.3    Iwase, S.4    Baba, T.5    Shi, Y.6
  • 65
    • 44949265263 scopus 로고    scopus 로고
    • Role for A-type lamins in herpesviral DNA targeting and heterochromatin modulation
    • Silva L., Cliffe A., Chang L., Knipe D.M. Role for A-type lamins in herpesviral DNA targeting and heterochromatin modulation. PLoS Pathog. 2008, 4:e1000071.
    • (2008) PLoS Pathog. , vol.4 , pp. e1000071
    • Silva, L.1    Cliffe, A.2    Chang, L.3    Knipe, D.M.4
  • 66
    • 84878191253 scopus 로고    scopus 로고
    • The dynamics of HCF-1 modulation of herpes simplex virus chromatin during initiation of infection
    • Vogel J.L., Kristie T.M. The dynamics of HCF-1 modulation of herpes simplex virus chromatin during initiation of infection. Viruses 2013, 5:1272-1291.
    • (2013) Viruses , vol.5 , pp. 1272-1291
    • Vogel, J.L.1    Kristie, T.M.2
  • 67
    • 27644466623 scopus 로고    scopus 로고
    • Herpesviral latency-associated transcript gene promotes assembly of heterochromatin on viral lytic-gene promoters in latent infection
    • Wang Q.Y., Zhou C., Johnson K.E., Colgrove R.C., Coen D.M., Knipe D.M. Herpesviral latency-associated transcript gene promotes assembly of heterochromatin on viral lytic-gene promoters in latent infection. Proc. Natl. Acad. Sci. USA 2005, 102:16055-16059.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 16055-16059
    • Wang, Q.Y.1    Zhou, C.2    Johnson, K.E.3    Colgrove, R.C.4    Coen, D.M.5    Knipe, D.M.6
  • 68
    • 69449105987 scopus 로고    scopus 로고
    • Recruitment of the transcriptional coactivator HCF-1 to viral immediate-early promoters during initiation of reactivation from latency of herpes simplex virus type 1
    • Whitlow Z., Kristie T.M. Recruitment of the transcriptional coactivator HCF-1 to viral immediate-early promoters during initiation of reactivation from latency of herpes simplex virus type 1. J. Virol. 2009, 83:9591-9595.
    • (2009) J. Virol. , vol.83 , pp. 9591-9595
    • Whitlow, Z.1    Kristie, T.M.2
  • 70
    • 0037382574 scopus 로고    scopus 로고
    • Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1
    • Wysocka J., Myers M.P., Laherty C.D., Eisenman R.N., Herr W. Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1. Genes Dev. 2003, 17:896-911.
    • (2003) Genes Dev. , vol.17 , pp. 896-911
    • Wysocka, J.1    Myers, M.P.2    Laherty, C.D.3    Eisenman, R.N.4    Herr, W.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.