메뉴 건너뛰기




Volumn 287, Issue 32, 2012, Pages 26702-26714

Interleukin 6 signaling regulates promyelocytic leukemia protein gene expression in human normal and cancer cells

Author keywords

[No Author keywords available]

Indexed keywords

CANCER CELLS; CELL LINES; CULTURE MEDIA; CYTOKINES; EXPRESSION PATTERNS; GENOTOXIC STRESS; GROWTH CONDITIONS; HUMAN CELLS; INTERLEUKIN-6; LOCAL STRESS; PARACRINE; PATHOPHYSIOLOGICAL; PROMYELOCYTIC LEUKEMIA PROTEINS; PROTEIN LEVEL; SIGNALING PATHWAYS; TISSUE ADAPTATION; TUMOR SUPPRESSORS;

EID: 84864556099     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.316869     Document Type: Article
Times cited : (34)

References (83)
  • 1
    • 34548288605 scopus 로고    scopus 로고
    • Beyond repair foci: Subnuclear domains and the cellular response to DNA damage
    • Dellaire, G., and Bazett-Jones, D. P. (2007) Beyond repair foci. Subnuclear domains and the cellular response to DNA damage. Cell Cycle 6, 1864-1872 (Pubitemid 47327904)
    • (2007) Cell Cycle , vol.6 , Issue.15 , pp. 1864-1872
    • Dellaire, G.1    Bazett-Jones, D.P.2
  • 2
    • 0033848907 scopus 로고    scopus 로고
    • The puzzling multiple lives of PML and its role in the genesis of cancer
    • Ruggero, D., Wang, Z. G., and Pandolfi, P. P. (2000) The puzzling multiple lives of PML and its role in the genesis of cancer. Bioessays 22, 827-835
    • (2000) Bioessays , vol.22 , pp. 827-835
    • Ruggero, D.1    Wang, Z.G.2    Pandolfi, P.P.3
  • 3
    • 36448975490 scopus 로고    scopus 로고
    • Structure, dynamics and functions of promyelocytic leukaemia nuclear bodies
    • DOI 10.1038/nrm2277, PII NRM2277
    • Bernardi, R., and Pandolfi, P. P. (2007) Structure, dynamics, and functions of promyelocytic leukaemia nuclear bodies. Nat. Rev. Mol. Cell Biol. 8, 1006-1016 (Pubitemid 350174636)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.12 , pp. 1006-1016
    • Bernardi, R.1    Pandolfi, P.P.2
  • 4
    • 0025043959 scopus 로고
    • The t(15;17) translocation of acute promyelocytic leukaemia fuses the retinoic acid receptor α gene to a novel transcribed locus
    • de Thé, H., Chomienne, C., Lanotte, M., Degos, L., and Dejean, A. (1990) The t(15;17) translocation of acute promyelocytic leukaemia fuses the retinoic acid receptor α gene to a novel transcribed locus. Nature 347, 558-561
    • (1990) Nature , vol.347 , pp. 558-561
    • De Thé, H.1    Chomienne, C.2    Lanotte, M.3    Degos, L.4    Dejean, A.5
  • 10
    • 0029024780 scopus 로고
    • Molecular characterization of NDP52, a novel protein of the nuclear domain 10, which is redistributed upon virus infection and interferon treatment
    • Korioth, F., Gieffers, C., Maul, G. G., and Frey, J. (1995) Molecular characterization of NDP52, a novel protein of the nuclear domain 10, which is redistributed upon virus infection and interferon treatment. J. Cell Biol. 130, 1-13
    • (1995) J. Cell Biol. , vol.130 , pp. 1-13
    • Korioth, F.1    Gieffers, C.2    Maul, G.G.3    Frey, J.4
  • 13
    • 63849264344 scopus 로고    scopus 로고
    • PML links aberrant cytokine signaling and oncogenic stress to cellular senescence
    • Bourdeau, V., Baudry, D., and Ferbeyre, G. (2009) PML links aberrant cytokine signaling and oncogenic stress to cellular senescence Front. Biosci. 14, 475-485
    • (2009) Front. Biosci. , vol.14 , pp. 475-485
    • Bourdeau, V.1    Baudry, D.2    Ferbeyre, G.3
  • 14
    • 53449090838 scopus 로고    scopus 로고
    • Role of nuclear bodies in apoptosis signaling
    • Krieghoff-Henning, E., and Hofmann, T. G. (2008) Role of nuclear bodies in apoptosis signaling. Biochim. Biophys. Acta 1783, 2185-2194
    • (2008) Biochim. Biophys. Acta , vol.1783 , pp. 2185-2194
    • Krieghoff-Henning, E.1    Hofmann, T.G.2
  • 16
    • 0041856232 scopus 로고    scopus 로고
    • The promyelocytic leukemia protein protects p53 from Mdm2-mediated inhibition and degradation
    • DOI 10.1074/jbc.M301264200
    • Louria-Hayon, I., Grossman, T., Sionov, R. V., Alsheich, O., Pandolfi, P. P., and Haupt, Y. (2003) The promyelocytic leukemia protein protects p53 from Mdm2-mediated inhibition and degradation. J. Biol. Chem. 278, 33134-33141 (Pubitemid 37055760)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.35 , pp. 33134-33141
    • Louria-Hayon, I.1    Grossman, T.2    Sionov, R.V.3    Alsheich, O.4    Pandolfi, P.P.5    Haupt, Y.6
  • 17
  • 18
    • 0037667702 scopus 로고    scopus 로고
    • Rb-mediated heterochromatin formation and silencing of E2F target genes during cellular senescence
    • DOI 10.1016/S0092-8674(03)00401-X
    • Narita, M., Nũnez, S., Heard, E., Narita, M., Lin, A. W., Hearn, S. A., Spector, D. L., Hannon, G. J., and Lowe, S. W. (2003) Rb-mediated heterochromatin formation and silencing of E2F target genes during cellular senescence. Cell 113, 703-716 (Pubitemid 36724935)
    • (2003) Cell , vol.113 , Issue.6 , pp. 703-716
    • Narita, M.1    Nunez, S.2    Heard, E.3    Narita, M.4    Lin, A.W.5    Hearn, S.A.6    Spector, D.L.7    Hannon, G.J.8    Lowe, S.W.9
  • 20
    • 33947236204 scopus 로고    scopus 로고
    • Molecular dissection of formation of senescence-associated heterochromatin foci
    • DOI 10.1128/MCB.02019-06
    • Zhang, R., Chen, W., and Adams, P. D. (2007) Molecular dissection of formation of senescence-associated heterochromatin foci. Mol. Cell. Biol. 27, 2343-2358 (Pubitemid 46418486)
    • (2007) Molecular and Cellular Biology , vol.27 , Issue.6 , pp. 2343-2358
    • Zhang, R.1    Chen, W.2    Adams, P.D.3
  • 21
    • 34147143631 scopus 로고    scopus 로고
    • Definition of pRB- and p53-dependent and -independent steps in HIRA/ASF1a-mediated formation of senescence-associated heterochromatin foci
    • DOI 10.1128/MCB.01592-06
    • Ye, X., Zerlanko, B., Zhang, R., Somaiah, N., Lipinski, M., Salomoni, P., and Adams, P. D. (2007) Definition of pRB- and p53-dependent and -independent steps in HIRA/ASF1a-mediated formation of senescence-associated heterochromatin foci. Mol. Cell. Biol. 27, 2452-2465 (Pubitemid 46581338)
    • (2007) Molecular and Cellular Biology , vol.27 , Issue.7 , pp. 2452-2465
    • Ye, X.1    Zerlanko, B.2    Zhang, R.3    Somaiah, N.4    Lipinski, M.5    Salomoni, P.6    Adams, P.D.7
  • 22
    • 79851493300 scopus 로고    scopus 로고
    • Senescence-associated heterochromatin foci are dispensable for cellular senescence, occur in a cell type- And insult-dependent manner and follow expression of p16(ink4a)
    • Kosar, M., Bartkova, J., Hubackova, S., Hodny, Z., Lukas, J., and Bartek, J. (2011) Senescence-associated heterochromatin foci are dispensable for cellular senescence, occur in a cell type- and insult-dependent manner and follow expression of p16(ink4a). Cell Cycle 10, 457-468
    • (2011) Cell Cycle , vol.10 , pp. 457-468
    • Kosar, M.1    Bartkova, J.2    Hubackova, S.3    Hodny, Z.4    Lukas, J.5    Bartek, J.6
  • 24
    • 0030917324 scopus 로고    scopus 로고
    • Altered distribution of the promyelocytic leukemia-associated protein is associated with cellular senescence
    • Jiang, W. Q., and Ringertz, N. (1997) Altered distribution of the promyelocytic leukemia-associated protein is associated with cellular senescence. Cell Growth Differ. 8, 513-522
    • (1997) Cell Growth Differ. , vol.8 , pp. 513-522
    • Jiang, W.Q.1    Ringertz, N.2
  • 26
    • 77951958808 scopus 로고    scopus 로고
    • Bacterial intoxication evokes cellular senescence with persistent DNA damage and cytokine signaling
    • Blazkova, H., Krejcikova, K., Moudry, P., Frisan, T., Hodny, Z., and Bartek, J. (2010) Bacterial intoxication evokes cellular senescence with persistent DNA damage and cytokine signaling. J. Cell. Mol. Med. 14, 357-367
    • (2010) J. Cell. Mol. Med. , vol.14 , pp. 357-367
    • Blazkova, H.1    Krejcikova, K.2    Moudry, P.3    Frisan, T.4    Hodny, Z.5    Bartek, J.6
  • 29
    • 77949881221 scopus 로고    scopus 로고
    • The senescence- Associated secretory phenotype. The dark side of tumor suppression
    • Coppé, J. P., Desprez, P. Y., Krtolica, A., and Campisi, J. (2010) The senescence- associated secretory phenotype. The dark side of tumor suppression. Annu. Rev. Pathol. 5, 99-118
    • (2010) Annu. Rev. Pathol. , vol.5 , pp. 99-118
    • Coppé, J.P.1    Desprez, P.Y.2    Krtolica, A.3    Campisi, J.4
  • 30
    • 58849154235 scopus 로고    scopus 로고
    • Senescence-messaging secretome, SMS-ing cellular stress
    • Kuilman, T., and Peeper, D. S. (2009) Senescence-messaging secretome, SMS-ing cellular stress. Nat. Rev. Cancer 9, 81-94
    • (2009) Nat. Rev. Cancer , vol.9 , pp. 81-94
    • Kuilman, T.1    Peeper, D.S.2
  • 31
    • 61849107031 scopus 로고    scopus 로고
    • SASP reflects senescence
    • Young, A. R., and Narita, M. (2009) SASP reflects senescence. EMBO Rep. 10, 228-230
    • (2009) EMBO Rep. , vol.10 , pp. 228-230
    • Young, A.R.1    Narita, M.2
  • 34
    • 0037034829 scopus 로고    scopus 로고
    • PML NBs associate with the hMre11 complex and p53 at sites of irradiation induced DNA damage
    • DOI 10.1038/sj/onc/1205227
    • Carbone, R., Pearson, M., Minucci, S., and Pelicci, P. G. (2002) PML NBs associate with the hMre11 complex and p53 at sites of irradiation induced DNA damage. Oncogene 21, 1633-1640 (Pubitemid 34259026)
    • (2002) Oncogene , vol.21 , Issue.11 , pp. 1633-1640
    • Carbone, R.1    Pearson, M.2    Minucci, S.3    Pelicci, P.G.4
  • 35
    • 70449940264 scopus 로고    scopus 로고
    • High resolution imaging of changes in the structure and spatial organization of chromatin, γ-H2A.X, and the MRN complex within etoposide-induced DNA repair foci
    • Dellaire, G., Kepkay, R., and Bazett-Jones, D. P. (2009) High resolution imaging of changes in the structure and spatial organization of chromatin, γ-H2A.X, and the MRN complex within etoposide-induced DNA repair foci. Cell Cycle 8, 3750-3769
    • (2009) Cell Cycle , vol.8 , pp. 3750-3769
    • Dellaire, G.1    Kepkay, R.2    Bazett-Jones, D.P.3
  • 36
    • 4644351274 scopus 로고    scopus 로고
    • PML nuclear bodies: Dynamic sensors of DNA damage and cellular stress
    • DOI 10.1002/bies.20089
    • Dellaire, G., and Bazett-Jones, D. P. (2004) PML nuclear bodies: dynamic sensors of DNA damage and cellular stress. Bioessays 26, 963-977 (Pubitemid 39273070)
    • (2004) BioEssays , vol.26 , Issue.9 , pp. 963-977
    • Dellaire, G.1    Bazett-Jones, D.P.2
  • 41
    • 35848949304 scopus 로고    scopus 로고
    • DNA damage response as an anti-cancer barrier: Damage threshold and the concept of 'conditional haploinsufficiency'
    • Bartek, J., Lukas, J., and Bartkova, J. (2007) DNA damage response as an anti-cancer barrier. Damage threshold and the concept of "conditional haploinsufficiency." Cell Cycle 6, 2344-2347 (Pubitemid 350058685)
    • (2007) Cell Cycle , vol.6 , Issue.19 , pp. 2344-2347
    • Bartek, J.1    Lukas, J.2    Bartkova, J.3
  • 45
  • 46
    • 0024392636 scopus 로고
    • Hybridoma growth factor
    • discussion 198-199
    • Aarden, L. A. (1989) Hybridoma growth factor. Ann. N.Y. Acad. Sci. 557, 192-198, discussion 198-199
    • (1989) Ann. N.Y. Acad. Sci. , vol.557 , pp. 192-198
    • Aarden, L.A.1
  • 47
    • 33846918136 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors suppress IFNα-induced up-regulation of promyelocytic leukemia protein
    • DOI 10.1182/blood-2006-02-003418
    • Vlasáková, J., Nováková, Z., Rossmeislová, L., Kahle, M., Hozák, P., and Hodny, Z. (2007) Histone deacetylase inhibitors suppress IFNα-induced up-regulation of promyelocytic leukemia protein. Blood 109, 1373-1380 (Pubitemid 46239567)
    • (2007) Blood , vol.109 , Issue.4 , pp. 1373-1380
    • Vlasakova, J.1    Novakova, Z.2    Rossmeislova, L.3    Kahle, M.4    Hozak, P.5    Hodny, Z.6
  • 49
    • 0032489520 scopus 로고    scopus 로고
    • DNA double-stranded breaks induce histone H2AX phosphorylation on serine 139
    • DOI 10.1074/jbc.273.10.5858
    • Rogakou, E. P., Pilch, D. R., Orr, A. H., Ivanova, V. S., and Bonner, W. M. (1998) DNA double-stranded breaks induce histone H2AX phosphorylation on serine 139. J. Biol. Chem. 273, 5858-5868 (Pubitemid 28124064)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.10 , pp. 5858-5868
    • Rogakou, E.P.1    Pilch, D.R.2    Orr, A.H.3    Ivanova, V.S.4    Bonner, W.M.5
  • 50
    • 79952083895 scopus 로고    scopus 로고
    • Interleukin-1β-induced interleukin-6 production in A549 cells is mediated by both phosphatidylinositol 3-kinase and interleukin-1receptor- associated kinase-4
    • Eda, H., Burnette, B. L., Shimada, H., Hope, H. R., and Monahan, J. B. (2011) Interleukin-1β-induced interleukin-6 production in A549 cells is mediated by both phosphatidylinositol 3-kinase and interleukin-1receptor- associated kinase-4. Cell Biol. Int. 35, 355-358
    • (2011) Cell Biol. Int. , vol.35 , pp. 355-358
    • Eda, H.1    Burnette, B.L.2    Shimada, H.3    Hope, H.R.4    Monahan, J.B.5
  • 51
    • 68149170225 scopus 로고    scopus 로고
    • Interleukin 6 secreted from adipose stromal cells promotes migration and invasion of breast cancer cells
    • Walter, M., Liang, S., Ghosh, S., Hornsby, P. J., and Li, R. (2009) Interleukin 6 secreted from adipose stromal cells promotes migration and invasion of breast cancer cells. Oncogene 28, 2745-2755
    • (2009) Oncogene , vol.28 , pp. 2745-2755
    • Walter, M.1    Liang, S.2    Ghosh, S.3    Hornsby, P.J.4    Li, R.5
  • 52
    • 0035794217 scopus 로고    scopus 로고
    • DNAbinding specificity of different STAT proteins. Comparison of in vitro specificity with natural target sites
    • Ehret, G. B., Reichenbach, P., Schindler, U., Horvath, C. M., Fritz, S., Nabholz, M., and Bucher, P. (2001)DNAbinding specificity of different STAT proteins. Comparison of in vitro specificity with natural target sites. J. Biol. Chem. 276, 6675-6688
    • (2001) J. Biol. Chem. , vol.276 , pp. 6675-6688
    • Ehret, G.B.1    Reichenbach, P.2    Schindler, U.3    Horvath, C.M.4    Fritz, S.5    Nabholz, M.6    Bucher, P.7
  • 53
    • 0030926348 scopus 로고    scopus 로고
    • Tec tyrosine kinase links the cytokine receptors to PI-3 kinase probably through JAK
    • Takahashi-Tezuka, M., Hibi, M., Fujitani, Y., Fukada, T., Yamaguchi, T., and Hirano, T. (1997) Tec tyrosine kinase links the cytokine receptors to PI 3-kinase probably through JAK. Oncogene 14, 2273-2282 (Pubitemid 27260719)
    • (1997) Oncogene , vol.14 , Issue.19 , pp. 2273-2282
    • Takahashi-Tezuka, M.1    Hibi, M.2    Fujitani, Y.3    Fukada, T.4    Yamaguchi, T.5    Hirano, T.6
  • 55
    • 0037332580 scopus 로고    scopus 로고
    • Tetrameric oligomerization of IκB kinase γ (IKKγ) is obligatory for IKK complex activity and NF-κB activation
    • DOI 10.1128/MCB.23.6.2029-2041.2003
    • Tegethoff, S., Behlke, J., and Scheidereit, C. (2003) Tetrameric oligomerization of IκB kinase γ (IKKγ) is obligatory for IKK complex activity and NF-κB activation. Mol. Cell. Biol. 23, 2029-2041 (Pubitemid 36278814)
    • (2003) Molecular and Cellular Biology , vol.23 , Issue.6 , pp. 2029-2041
    • Tegethoff, S.1    Behlke, J.2    Scheidereit, C.3
  • 56
    • 0032191176 scopus 로고    scopus 로고
    • Role of early cytokines, including α, and β interferons (IFN-α/β) in innate and adaptive immune responses to viral infections
    • Biron, C. A. (1998) Role of early cytokines, including α, and β interferons (IFN-α/β) in innate and adaptive immune responses to viral infections. Semin. Immunol. 10, 383-390
    • (1998) Semin. Immunol. , vol.10 , pp. 383-390
    • Biron, C.A.1
  • 57
    • 36849015753 scopus 로고    scopus 로고
    • Myc down-regulation as a mechanism to activate the Rb pathway in STAT5A-induced senescence
    • DOI 10.1074/jbc.M707074200
    • Mallette, F. A., Gaumont-Leclerc, M. F., Huot, G., and Ferbeyre, G. (2007) Myc down-regulation as a mechanism to activate the Rb pathway in STAT5A-induced senescence. J. Biol. Chem. 282, 34938-34944 (Pubitemid 350232462)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.48 , pp. 34938-34944
    • Mallette, F.A.1    Gaumont-Leclerc, M.-F.2    Huot, G.3    Ferbeyre, G.4
  • 58
    • 0037108863 scopus 로고    scopus 로고
    • PML is a target gene of β-catenin and plakoglobin, and coactivates β-catenin-mediated transcription
    • Shtutman, M., Zhurinsky, J., Oren, M., Levina, E., and Ben-Ze'ev, A. (2002) PML is a target gene of β-catenin and plakoglobin and coactivates β-catenin-mediated transcription. Cancer Res. 62, 5947-5954 (Pubitemid 35204758)
    • (2002) Cancer Research , vol.62 , Issue.20 , pp. 5947-5954
    • Shtutman, M.1    Zhurinsky, J.2    Oren, M.3    Levina, E.4    Ben-Ze'ev, A.5
  • 59
    • 33644821166 scopus 로고    scopus 로고
    • Interactions between DNA viruses, ND10 and the DNA damage response
    • Everett, R. D. (2006) Interactions between DNA viruses, ND10 and the DNA damage response. Cell. Microbiol. 8, 365-374
    • (2006) Cell. Microbiol. , vol.8 , pp. 365-374
    • Everett, R.D.1
  • 60
    • 0031907092 scopus 로고    scopus 로고
    • Resistance to virus infection conferred by the interferon-induced promyelocytic leukemia protein
    • Chelbi-Alix, M. K., Quignon, F., Pelicano, L., Koken, M. H., and de Thé, H. (1998) Resistance to virus infection conferred by the interferon-induced promyelocytic leukemia protein. J. Virol. 72, 1043-1051 (Pubitemid 28116883)
    • (1998) Journal of Virology , vol.72 , Issue.2 , pp. 1043-1051
    • Chelbi-Alix, M.K.1    Quignon, F.2    Pelicano, L.3    Koken, M.H.M.4    De The, H.5
  • 61
    • 0035969127 scopus 로고    scopus 로고
    • Role and fate of PML nuclear bodies in response to interferon and viral infections
    • DOI 10.1038/sj.onc.1204854
    • Regad, T., and Chelbi-Alix, M. K. (2001) Role and fate of PML nuclear bodies in response to interferon and viral infections. Oncogene 20, 7274-7286 (Pubitemid 33105016)
    • (2001) Oncogene , vol.20 , Issue.49 REV. IIS. 6 , pp. 7274-7286
    • Regad, T.1    Chelbi-Alix, M.K.2
  • 62
    • 0027769358 scopus 로고
    • Modification of discrete nuclear domains induced by herpes simplex virus type 1 immediate early gene 1 product (ICPO)
    • Maul, G. G., Guldner, H. H., and Spivack, J. G. (1993) Modification of discrete nuclear domains induced by herpes simplex virus type 1 immediate early gene 1 product (ICP0) J. Gen. Virol. 74, 2679-2690 (Pubitemid 24020661)
    • (1993) Journal of General Virology , vol.74 , Issue.12 , pp. 2679-2690
    • Maul, G.G.1    Guldner, H.H.2    Spivack, J.G.3
  • 63
    • 0028039189 scopus 로고
    • HSV-1 IE protein Vmw110 causes redistribution of PML
    • Everett, R. D., and Maul, G. G. (1994) HSV-1 IE protein Vmw110 causes redistribution of PML. EMBO J. 13, 5062-5069 (Pubitemid 24341087)
    • (1994) EMBO Journal , vol.13 , Issue.21 , pp. 5062-5069
    • Everett, R.D.1    Maul, G.G.2
  • 64
    • 0031922713 scopus 로고    scopus 로고
    • Disruption of PML-associated nuclear bodies mediated by the human cytomegalovirus major immediate early gene product
    • Wilkinson, G. W., Kelly, C., Sinclair, J. H., and Rickards, C. (1998) Disruption of PML-associated nuclear bodies mediated by the human cytomegalovirus major immediate early gene product. J. Gen. Virol. 79, 1233-1245 (Pubitemid 28203865)
    • (1998) Journal of General Virology , vol.79 , Issue.5 , pp. 1233-1245
    • Wilkinson, G.W.G.1    Kelly, C.2    Sinclair, J.H.3    Rickards, C.4
  • 65
    • 2642601103 scopus 로고    scopus 로고
    • Nuclear dots: Actors on many stages
    • Sternsdorf, T., Grötzinger, T., Jensen, K., and Will, H. (1997) Nuclear dots. Actors on many stages. Immunobiology 198, 307-331 (Pubitemid 28021406)
    • (1997) Immunobiology , vol.198 , Issue.1-3 , pp. 307-331
    • Sternsdorf, T.1    Grotzinger, T.2    Jensen, K.3    Will, H.4
  • 66
    • 0344299239 scopus 로고    scopus 로고
    • Viral immediate-early proteins abrogate the modification by SUMO-1 of PML and Sp100 proteins, correlating with nuclear body disruption
    • Müller, S., and Dejean, A. (1999) Viral immediate-early proteins abrogate the modification by SUMO-1 of PML and Sp100 proteins, correlating with nuclear body disruption. J. Virol. 73, 5137-5143 (Pubitemid 29246776)
    • (1999) Journal of Virology , vol.73 , Issue.6 , pp. 5137-5143
    • Muller, S.1    Dejean, A.2
  • 67
    • 0028841483 scopus 로고
    • Sequestration of PML and Sp100 proteins in an intranuclear viral structure during herpes simplex virus type 1 infection
    • Puvion-Dutilleul, F., Venturini, L., Guillemin, M. C., de Thé, H., and Puvion, E. (1995) Sequestration of PML and Sp100 proteins in an intranuclear viral structure during herpes simplex virus type 1 infection. Exp. Cell Res. 221, 448-461
    • (1995) Exp. Cell Res. , vol.221 , pp. 448-461
    • Puvion-Dutilleul, F.1    Venturini, L.2    Guillemin, M.C.3    De Thé, H.4    Puvion, E.5
  • 68
    • 0031743484 scopus 로고    scopus 로고
    • ND10 protein PML is recruited to herpes simplex virus type 1 prereplicative sites and replication compartments in the presence of viral DNA polymerase
    • Burkham, J., Coen, D. M., and Weller, S. K. (1998) ND10 protein PML is recruited to herpes simplex virus type 1 prereplicative sites and replication compartments in the presence of viral DNA polymerase. J. Virol. 72, 10100-10107 (Pubitemid 28520880)
    • (1998) Journal of Virology , vol.72 , Issue.12 , pp. 10100-10107
    • Burkham, J.1    Coen, D.M.2    Weller, S.K.3
  • 69
    • 0035121442 scopus 로고    scopus 로고
    • Interactions of herpes simplex virus type 1 with ND10 and recruitment of PML to replication compartments
    • DOI 10.1128/JVI.75.5.2353-2367.2001
    • Burkham, J., Coen, D. M., Hwang, C. B., and Weller, S. K. (2001) Interactions of herpes simplex virus type 1 with ND10 and recruitment of PML to replication compartments. J. Virol. 75, 2353-2367 (Pubitemid 32147574)
    • (2001) Journal of Virology , vol.75 , Issue.5 , pp. 2353-2367
    • Burkham, J.1    Coen, D.M.2    Hwang, C.B.C.3    Weller, S.K.4
  • 70
    • 16244422998 scopus 로고    scopus 로고
    • ND10 components relocate to sites associated with herpes simplex virus type 1 nucleoprotein complexes during virus infection
    • DOI 10.1128/JVI.79.8.5078-5089.2005
    • Everett, R. D., and Murray, J. (2005) ND10 components relocate to sites associated with herpes simplex virus type 1 nucleoprotein complexes during virus infection. J. Virol. 79, 5078-5089 (Pubitemid 40464258)
    • (2005) Journal of Virology , vol.79 , Issue.8 , pp. 5078-5089
    • Everett, R.D.1    Murray, J.2
  • 71
    • 33746827706 scopus 로고    scopus 로고
    • PML contributes to a cellular mechanism of repression of herpes simplex virus type 1 infection that is inactivated by ICP0
    • DOI 10.1128/JVI.00734-06
    • Everett, R. D., Rechter, S., Papior, P., Tavalai, N., Stamminger, T., and Orr, A. (2006)PMLcontributes to a cellular mechanism of repression of herpes simplex virus type 1 infection that is inactivated by ICP0. J. Virol. 80, 7995-8005 (Pubitemid 44182300)
    • (2006) Journal of Virology , vol.80 , Issue.16 , pp. 7995-8005
    • Everett, R.D.1    Rechter, S.2    Papior, P.3    Tavalai, N.4    Stamminger, T.5    Orr, A.6
  • 72
    • 0033611590 scopus 로고    scopus 로고
    • Herpes virus induced proteasome-dependent degradation of the nuclear bodies-associated PML and Sp100 proteins
    • DOI 10.1038/sj.onc.1202366
    • Chelbi-Alix, M. K., and de Thé, H. (1999) Herpes virus induced proteasome-dependent degradation of the nuclear body-associated PML and Sp100 proteins. Oncogene 18, 935-941 (Pubitemid 29086270)
    • (1999) Oncogene , vol.18 , Issue.4 , pp. 935-941
    • Chelbi-Alix, M.K.1    De The, H.2
  • 73
    • 28244483929 scopus 로고    scopus 로고
    • Hepatitis C virus core protein inhibits tumor suppressor protein promyelocytic leukemia function in human hepatoma cells
    • DOI 10.1158/0008-5472.CAN-05-0880
    • Herzer, K., Weyer, S., Krammer, P. H., Galle, P. R., and Hofmann, T. G. (2005) Hepatitis C virus core protein inhibits tumor suppressor protein promyelocytic leukemia function in human hepatoma cells. Cancer Res. 65, 10830-10837 (Pubitemid 41713350)
    • (2005) Cancer Research , vol.65 , Issue.23 , pp. 10830-10837
    • Herzer, K.1    Weyer, S.2    Krammer, P.H.3    Galle, P.R.4    Hofmann, T.G.5
  • 74
    • 0034192363 scopus 로고    scopus 로고
    • Nijmegen breakage syndrome disease protein and MRE11 at PML nuclear bodies and meiotic telomeres
    • Lombard, D. B., and Guarente, L. (2000) Nijmegen breakage syndrome disease protein and MRE11 at PML nuclear bodies and meiotic telomeres. Cancer Res. 60, 2331-2334 (Pubitemid 30262415)
    • (2000) Cancer Research , vol.60 , Issue.9 , pp. 2331-2334
    • Lombard, D.B.1    Guarente, L.2
  • 75
    • 0034749425 scopus 로고    scopus 로고
    • DNA damage-dependent nuclear dynamics of the Mre11 complex
    • Mirzoeva, O. K., and Petrini, J. H. (2001) DNA damage-dependent nuclear dynamics of the Mre11 complex. Mol. Cell. Biol. 21, 281-288
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 281-288
    • Mirzoeva, O.K.1    Petrini, J.H.2
  • 76
    • 44649101304 scopus 로고    scopus 로고
    • Oncogene-Induced Senescence Relayed by an Interleukin-Dependent Inflammatory Network
    • DOI 10.1016/j.cell.2008.03.039, PII S009286740800620X
    • Kuilman, T., Michaloglou, C., Vredeveld, L. C., Douma, S., van Doorn, R., Desmet, C. J., Aarden, L. A., Mooi, W. J., and Peeper, D. S. (2008) Oncogene-induced senescence relayed by an interleukin-dependent inflammatory network. Cell 133, 1019-1031 (Pubitemid 351787746)
    • (2008) Cell , vol.133 , Issue.6 , pp. 1019-1031
    • Kuilman, T.1    Michaloglou, C.2    Vredeveld, L.C.W.3    Douma, S.4    Van Doorn, R.5    Desmet, C.J.6    Aarden, L.A.7    Mooi, W.J.8    Peeper, D.S.9
  • 79
    • 0028913109 scopus 로고
    • A STAT protein domain that determines DNA sequence recognition suggests a novel DNA-binding domain
    • Horvath, C. M., Wen, Z., and Darnell, J. E., Jr. (1995) A STAT protein domain that determines DNA sequence recognition suggests a novel DNA-binding domain. Genes Dev. 9, 984-994
    • (1995) Genes Dev. , vol.9 , pp. 984-994
    • Horvath, C.M.1    Wen, Z.2    Darnell Jr., J.E.3
  • 80
    • 0025343895 scopus 로고
    • Activation of interleukin-6 gene expression through the NF-κB transcription factor
    • Libermann, T. A., and Baltimore, D. (1990) Activation of interleukin-6 gene expression through the NF-κB transcription factor. Mol. Cell. Biol. 10, 2327-2334
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 2327-2334
    • Libermann, T.A.1    Baltimore, D.2
  • 81
    • 0027937626 scopus 로고
    • In vivo footprinting of the IRF-1 promoter: Inducible occupation of a GAS element next to a persistent structural alteration of the DNA
    • Rein, T., Müller, M., and Zorbas, H. (1994) In vivo footprinting of the IRF-1 promoter. Inducible occupation of a GAS element next to a persistent structural alteration of the DNA. Nucleic Acids Res. 22, 3033-3037 (Pubitemid 24260632)
    • (1994) Nucleic Acids Research , vol.22 , Issue.15 , pp. 3033-3037
    • Rein, T.1    Muller, M.2    Zorbas, H.3
  • 82
    • 0028927841 scopus 로고
    • Coordinate regulation of the human TAP1 and LMP2 genes from a shared bidirectional promoter
    • Wright, K. L., White, L. C., Kelly, A., Beck, S., Trowsdale, J., and Ting, J. P. (1995) Coordinate regulation of the human TAP1 and LMP2 genes from a shared bidirectional promoter. J. Exp. Med. 181, 1459-1471
    • (1995) J. Exp. Med. , vol.181 , pp. 1459-1471
    • Wright, K.L.1    White, L.C.2    Kelly, A.3    Beck, S.4    Trowsdale, J.5    Ting, J.P.6
  • 83
    • 0242361641 scopus 로고    scopus 로고
    • Ras Induces Vascular Smooth Muscle Cell Senescence and Inflammation in Human Atherosclerosis
    • DOI 10.1161/01.CIR.0000093274.82929.22
    • Minamino, T., Yoshida, T., Tateno, K., Miyauchi, H., Zou, Y., Toko, H., and Komuro, I. (2003) Ras induces vascular smooth muscle cell senescence and inflammation in human atherosclerosis. Circulation 108, 2264-2269 (Pubitemid 37363045)
    • (2003) Circulation , vol.108 , Issue.18 , pp. 2264-2269
    • Minamino, T.1    Yoshida, T.2    Tateno, K.3    Miyauchi, H.4    Zou, Y.5    Toko, H.6    Komuro, I.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.