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Volumn 63, Issue 2, 1998, Pages 297-304

Structure, organization, and dynamics of promyelocytic leukemia protein nuclear bodies

Author keywords

[No Author keywords available]

Indexed keywords

ONCOPROTEIN;

EID: 0032231606     PISSN: 00029297     EISSN: None     Source Type: Journal    
DOI: 10.1086/301991     Document Type: Article
Times cited : (152)

References (68)
  • 1
    • 0029590158 scopus 로고
    • Growth suppression of transformed human bronchial epithelial cells by all-trans-retinoic acid occurs through specific retinoid receptors
    • Ahn MJ, Langenfeld J, Moasser MM, Rusch V, Dmitrovsky E (1995) Growth suppression of transformed human bronchial epithelial cells by all-trans-retinoic acid occurs through specific retinoid receptors. Oncogene 11:2357-2364
    • (1995) Oncogene , vol.11 , pp. 2357-2364
    • Ahn, M.J.1    Langenfeld, J.2    Moasser, M.M.3    Rusch, V.4    Dmitrovsky, E.5
  • 2
    • 0031929684 scopus 로고    scopus 로고
    • The promyelocytic leukemia gene product (PML) forms stable complexes with the retinoblastoma protein
    • Alcalay M, Tomassoni L, Colombo E, Stoldt S, Grignani F, Fagioli M, Szekely L, et al (1998) The promyelocytic leukemia gene product (PML) forms stable complexes with the retinoblastoma protein. Mol Cell Biol 18:1084-1093
    • (1998) Mol Cell Biol , vol.18 , pp. 1084-1093
    • Alcalay, M.1    Tomassoni, L.2    Colombo, E.3    Stoldt, S.4    Grignani, F.5    Fagioli, M.6    Szekely, L.7
  • 3
    • 0026019835 scopus 로고
    • Identification of a novel nuclear domain
    • Ascoli CA, Maul GG (1991) Identification of a novel nuclear domain. J Cell Biol 112:785-795
    • (1991) J Cell Biol , vol.112 , pp. 785-795
    • Ascoli, C.A.1    Maul, G.G.2
  • 4
    • 0030796314 scopus 로고    scopus 로고
    • Surface residue mutations of the PML RING finger domain alter the formation of nuclear matrix-associated PML bodies
    • Boddy MN, Duprez E, Borden KL, Freemont PS (1997) Surface residue mutations of the PML RING finger domain alter the formation of nuclear matrix-associated PML bodies. J Cell Sci 110:2197-2205
    • (1997) J Cell Sci , vol.110 , pp. 2197-2205
    • Boddy, M.N.1    Duprez, E.2    Borden, K.L.3    Freemont, P.S.4
  • 5
    • 0029736651 scopus 로고    scopus 로고
    • PIC 1, a novel ubiquitin-like protein which interacts with the PML component of a multiprotein complex that is disrupted in acute promyelocytic leukemia
    • Boddy MN, Howe K, Etkin LD Solomon E, Freemont PS (1996) PIC 1, a novel ubiquitin-like protein which interacts with the PML component of a multiprotein complex that is disrupted in acute promyelocytic leukemia. Oncogene 13: 971-982
    • (1996) Oncogene , vol.13 , pp. 971-982
    • Boddy, M.N.1    Howe, K.2    Etkin, L.D.3    Solomon, E.4    Freemont, P.S.5
  • 6
    • 0028932963 scopus 로고
    • The solution structure of the RING finger domain from the acute promyelocytic leukemia proto-oncoprotein PML
    • Borden KL, Boddy MN, Lally J, O'Reilly NJ, Martin S, Howe K, Solomon E, et al (1995) The solution structure of the RING finger domain from the acute promyelocytic leukemia proto-oncoprotein PML. EMBO J 14:1532-1541
    • (1995) EMBO J , vol.14 , pp. 1532-1541
    • Borden, K.L.1    Boddy, M.N.2    Lally, J.3    O'Reilly, N.J.4    Martin, S.5    Howe, K.6    Solomon, E.7
  • 7
    • 2642670320 scopus 로고    scopus 로고
    • An arenavirus RING (zinc-binding) protein binds the oncoprotein promyelocyte leukemia protein (PML) and relocates PML nuclear bodies to the cytoplasm
    • Borden KL, Campbell Dwyer EJ, Salvato MS (1998) An arenavirus RING (zinc-binding) protein binds the oncoprotein promyelocyte leukemia protein (PML) and relocates PML nuclear bodies to the cytoplasm. J Virol 72:758-766
    • (1998) J Virol , vol.72 , pp. 758-766
    • Borden, K.L.1    Campbell Dwyer, E.J.2    Salvato, M.S.3
  • 8
    • 0029918562 scopus 로고    scopus 로고
    • In vivo and in vitro characterization of the B1 and B2 zinc-binding domains from the acute promyelocytic leukemia protooncoprotein PML
    • Borden KL, Lally JM, Martin SR, O'Reilly NJ, Solomon E, Freemont PS (1996) In vivo and in vitro characterization of the B1 and B2 zinc-binding domains from the acute promyelocytic leukemia protooncoprotein PML. Proc Natl Acad Sci USA 93:1601-1606
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 1601-1606
    • Borden, K.L.1    Lally, J.M.2    Martin, S.R.3    O'Reilly, N.J.4    Solomon, E.5    Freemont, P.S.6
  • 10
    • 0031800796 scopus 로고    scopus 로고
    • Ret finger protein is a normal component of PML nuclear bodies and interacts directly with PML
    • Cao T, Duprez E, Borden KL, Freemont PS, Etkin LD (1998) Ret finger protein is a normal component of PML nuclear bodies and interacts directly with PML. J Cell Sci 111: 1319-1329
    • (1998) J Cell Sci , vol.111 , pp. 1319-1329
    • Cao, T.1    Duprez, E.2    Borden, K.L.3    Freemont, P.S.4    Etkin, L.D.5
  • 11
    • 0029794132 scopus 로고    scopus 로고
    • A decade of molecular biology of retinoic acid receptors
    • Chambon P (1996) A decade of molecular biology of retinoic acid receptors. FASEB J 10:940-954
    • (1996) FASEB J , vol.10 , pp. 940-954
    • Chambon, P.1
  • 12
    • 0031907092 scopus 로고    scopus 로고
    • Resistance to virus infection conferred by the interferon-induced promyelocytic leukemia protein
    • Chelbi-Alix MK, Quignon F, Pelicano L, Koken MH, de The H (1998) Resistance to virus infection conferred by the interferon-induced promyelocytic leukemia protein. J Virol 72: 1043-1051
    • (1998) J Virol , vol.72 , pp. 1043-1051
    • Chelbi-Alix, M.K.1    Quignon, F.2    Pelicano, L.3    Koken, M.H.4    De The, H.5
  • 13
    • 0028234529 scopus 로고
    • Jak-STAT pathways and transcriptional activation in response to IFNs and other extracellular signaling proteins
    • Darnell JE Jr, Kerr IM, Stark GR (1994) Jak-STAT pathways and transcriptional activation in response to IFNs and other extracellular signaling proteins. Science 264:1415-1421
    • (1994) Science , vol.264 , pp. 1415-1421
    • Darnell Jr., J.E.1    Kerr, I.M.2    Stark, G.R.3
  • 14
    • 0029789753 scopus 로고    scopus 로고
    • Exclusion of Int-6 from PML nuclear bodies by binding to the HTLV-I Tax oncoprotein
    • Desbois C, Rousset R, Bantignies F, Jalinot P (1996) Exclusion of Int-6 from PML nuclear bodies by binding to the HTLV-I Tax oncoprotein. Science 273:951-953
    • (1996) Science , vol.273 , pp. 951-953
    • Desbois, C.1    Rousset, R.2    Bantignies, F.3    Jalinot, P.4
  • 15
    • 0030443724 scopus 로고    scopus 로고
    • The PML nuclear compartment and cancer
    • Doucas V, Evans RM (1996) The PML nuclear compartment and cancer. Biochim Biophys Acta 1288:M25-M29
    • (1996) Biochim Biophys Acta , vol.1288
    • Doucas, V.1    Evans, R.M.2
  • 17
    • 0028179010 scopus 로고
    • A novel macromolecular structure is a target of the promyelocyte-retinoic acid receptor oncoprotein
    • Dyck JA, Maul GG, Miller WH Jr, Chen JD, Kakizuka A, Evans RM (1994) A novel macromolecular structure is a target of the promyelocyte-retinoic acid receptor oncoprotein. Cell 76:333-343
    • (1994) Cell , vol.76 , pp. 333-343
    • Dyck, J.A.1    Maul, G.G.2    Miller Jr., W.H.3    Chen, J.D.4    Kakizuka, A.5    Evans, R.M.6
  • 18
    • 0031878851 scopus 로고    scopus 로고
    • The disruption of ND10 during herpes simplex virus infection correlates with the Vmw110 and proteasome-dependent loss of several PML isoforms
    • Everett RD, Freemont P, Saitoh H, Dasso M, Orr A, Kathoria M, Parkinson J (1998) The disruption of ND10 during herpes simplex virus infection correlates with the Vmw110 and proteasome-dependent loss of several PML isoforms. J Virol 72:6581-6591
    • (1998) J Virol , vol.72 , pp. 6581-6591
    • Everett, R.D.1    Freemont, P.2    Saitoh, H.3    Dasso, M.4    Orr, A.5    Kathoria, M.6    Parkinson, J.7
  • 19
    • 0028039189 scopus 로고
    • HSV-1 IE protein Vmw110 causes redistribution of PML
    • Everett RD, Maul GG (1994) HSV-1 IE protein Vmw110 causes redistribution of PML. EMBO J 13:5062-5069
    • (1994) EMBO J , vol.13 , pp. 5062-5069
    • Everett, R.D.1    Maul, G.G.2
  • 20
    • 0030895008 scopus 로고    scopus 로고
    • A novel ubiquitin-specific protease is dynamically associated with the PML nuclear domain and binds to a herpesvirus regulatory protein
    • Everett RD, Meredith M, Orr A, Cross A, Kathoria M, Parkinson J (1997) A novel ubiquitin-specific protease is dynamically associated with the PML nuclear domain and binds to a herpesvirus regulatory protein. EMBO J 16: 1519-1530
    • (1997) EMBO J , vol.16 , pp. 1519-1530
    • Everett, R.D.1    Meredith, M.2    Orr, A.3    Cross, A.4    Kathoria, M.5    Parkinson, J.6
  • 21
    • 7344248065 scopus 로고    scopus 로고
    • Cooperation between the RING and B1-B2 and coiled coil domains of PML is necessary for its effect on cell survival
    • Fagioli M, Alcalay M, Tomassoni L, Ferrucci PF, Mencarelli A, Riganelli D, Grignani F, et al (1998) Cooperation between the RING and B1-B2 and coiled coil domains of PML is necessary for its effect on cell survival. Oncogene 16: 2905-2913
    • (1998) Oncogene , vol.16 , pp. 2905-2913
    • Fagioli, M.1    Alcalay, M.2    Tomassoni, L.3    Ferrucci, P.F.4    Mencarelli, A.5    Riganelli, D.6    Grignani, F.7
  • 22
    • 0031417772 scopus 로고    scopus 로고
    • Spatial organization of large-scale chromatin domains in the nucleus: A magnified view of single chromosome territories
    • Ferreira J, Paolella G, Ramos C, Lamond AI (1997) Spatial organization of large-scale chromatin domains in the nucleus: a magnified view of single chromosome territories. J Cell Biol 139:1597-1610
    • (1997) J Cell Biol , vol.139 , pp. 1597-1610
    • Ferreira, J.1    Paolella, G.2    Ramos, C.3    Lamond, A.I.4
  • 23
  • 25
    • 17144458786 scopus 로고    scopus 로고
    • Fusion proteins of the retinoic acid receptor-α recruit histone deacetylase in promyelocytic leukemia
    • Grignani F, de Matteis S, Nervi C, Tomassoni L, Gelmetti V, Cioce M, Fanelli M, et al (1998) Fusion proteins of the retinoic acid receptor-α recruit histone deacetylase in promyelocytic leukemia. Nature 391:815-818
    • (1998) Nature , vol.391 , pp. 815-818
    • Grignani, F.1    De Matteis, S.2    Nervi, C.3    Tomassoni, L.4    Gelmetti, V.5    Cioce, M.6    Fanelli, M.7
  • 26
    • 10144237851 scopus 로고    scopus 로고
    • Effects on differentiation by the promyelocytic leukemia PML/RARα protein depend on the fusion of the PML protein dimerization and RARα DNA binding domains
    • Grignani F, Testa U, Rogaia D, Ferrucci PF, Samoggia P, Pinto A, Aldinucci D, et al (1996) Effects on differentiation by the promyelocytic leukemia PML/RARα protein depend on the fusion of the PML protein dimerization and RARα DNA binding domains. EMBO J 15:4949-4958
    • (1996) EMBO J , vol.15 , pp. 4949-4958
    • Grignani, F.1    Testa, U.2    Rogaia, D.3    Ferrucci, P.F.4    Samoggia, P.5    Pinto, A.6    Aldinucci, D.7
  • 27
    • 0031467867 scopus 로고    scopus 로고
    • Characterization of cryptic rearrangements and variant translocations in acute promyelocytic leukemia
    • Grimwade D, Gorman P, Duprez E, Howe K, Langabeer S, Oliver F, Walker H, et al (1997) Characterization of cryptic rearrangements and variant translocations in acute promyelocytic leukemia. Blood 90:4876-4885
    • (1997) Blood , vol.90 , pp. 4876-4885
    • Grimwade, D.1    Gorman, P.2    Duprez, E.3    Howe, K.4    Langabeer, S.5    Oliver, F.6    Walker, H.7
  • 28
    • 0030896978 scopus 로고    scopus 로고
    • Characterisation of the PML/ RARα rearrangement associated with t(15;17) acute promyelocytic leukemia
    • Grimwade D, Solomon E (1997) Characterisation of the PML/ RARα rearrangement associated with t(15;17) acute promyelocytic leukemia. Curr Top Microbiol Immunol 220: 81-112
    • (1997) Curr Top Microbiol Immunol , vol.220 , pp. 81-112
    • Grimwade, D.1    Solomon, E.2
  • 29
    • 0031033221 scopus 로고    scopus 로고
    • Altered myeloid development and acute leukemia in transgenic mice expressing PML/RARα under control of cathepsm G regulatory sequences
    • Grisolano JL, Wesselschmidt RL, Pelicci PG, Ley TJ (1997) Altered myeloid development and acute leukemia in transgenic mice expressing PML/RARα under control of cathepsm G regulatory sequences. Blood 89:376-387
    • (1997) Blood , vol.89 , pp. 376-387
    • Grisolano, J.L.1    Wesselschmidt, R.L.2    Pelicci, P.G.3    Ley, T.J.4
  • 30
    • 0032522962 scopus 로고    scopus 로고
    • Reduced retinoic acid-sensitivities of nuclear receptor corepressor binding to PML/ and PLZF/RARα underlie molecular pathogenesis and treatment of acute promyelocytic leukemia
    • Guidez F, Ivins S, Zhu J, Soderstrom M, Waxman S, Zelent A (1998) Reduced retinoic acid-sensitivities of nuclear receptor corepressor binding to PML/ and PLZF/RARα underlie molecular pathogenesis and treatment of acute promyelocytic leukemia. Blood 91:2634-2642
    • (1998) Blood , vol.91 , pp. 2634-2642
    • Guidez, F.1    Ivins, S.2    Zhu, J.3    Soderstrom, M.4    Waxman, S.5    Zelent, A.6
  • 31
    • 0031941912 scopus 로고    scopus 로고
    • Distinct interactions of PML/RARα and PLZF/RARα with co- Repressors determine differential responses to RA in APL
    • He LZ, Guidez F, Tribioli C, Peruzzi D, Ruthardt M, Zelent A, Pandolfi PP (1998) Distinct interactions of PML/RARα and PLZF/RARα with co-repressors determine differential responses to RA in APL. Nat Genet 18:126-135
    • (1998) Nat Genet , vol.18 , pp. 126-135
    • He, L.Z.1    Guidez, F.2    Tribioli, C.3    Peruzzi, D.4    Ruthardt, M.5    Zelent, A.6    Pandolfi, P.P.7
  • 33
    • 0029838230 scopus 로고    scopus 로고
    • The periphery of nuclear domain 10 (ND10) as site of DNA virus deposition
    • Ishov AM, Maul GG (1996) The periphery of nuclear domain 10 (ND10) as site of DNA virus deposition. J Cell Biol 134: 815-826
    • (1996) J Cell Biol , vol.134 , pp. 815-826
    • Ishov, A.M.1    Maul, G.G.2
  • 34
    • 0030840687 scopus 로고    scopus 로고
    • Human cytomegalovirus immediate early interaction with host nuclear structures: Definition of an immediate transcript environment
    • Ishov AM, Sternberg RM, Maul GG (1997) Human cytomegalovirus immediate early interaction with host nuclear structures: definition of an immediate transcript environment. J Cell Biol 138:5-6
    • (1997) J Cell Biol , vol.138 , pp. 5-6
    • Ishov, A.M.1    Sternberg, R.M.2    Maul, G.G.3
  • 35
    • 0029328590 scopus 로고
    • Nuclear organization: Uniting replication foci chromatin domains and chromosome structure
    • Jackson DA (1995) Nuclear organization: uniting replication foci chromatin domains and chromosome structure. Bioessays 17:587-591
    • (1995) Bioessays , vol.17 , pp. 587-591
    • Jackson, D.A.1
  • 36
    • 0031586596 scopus 로고    scopus 로고
    • Cystine starvation induces reversible large-body formation from nuclear bodies in T24 cells
    • Kamei H (1997) Cystine starvation induces reversible large-body formation from nuclear bodies in T24 cells. Exp Cell Res 237:207-216
    • (1997) Exp Cell Res , vol.237 , pp. 207-216
    • Kamei, H.1
  • 37
    • 0026583943 scopus 로고
    • Structure localization and transcriptional properties of two classes of retinoic acid receptor alpha fusion proteins in acute promyelocytic leukemia (APL): Structural similarities with a new family of oncoproteins
    • Kastner P, Perez A, Lutz Y, Rochette-Egly C, Gaub MP, Durand B, Lanotte M, et al (1992) Structure localization and transcriptional properties of two classes of retinoic acid receptor alpha fusion proteins in acute promyelocytic leukemia (APL): structural similarities with a new family of oncoproteins. EMBO J 11:629-642
    • (1992) EMBO J , vol.11 , pp. 629-642
    • Kastner, P.1    Perez, A.2    Lutz, Y.3    Rochette-Egly, C.4    Gaub, M.P.5    Durand, B.6    Lanotte, M.7
  • 38
    • 0028972538 scopus 로고
    • Disruption of PML-associated nuclear bodies during human cytomegalovirus infection
    • Kelly C, Van Driel R, Wilkinson GW (1995) Disruption of PML-associated nuclear bodies during human cytomegalovirus infection. J Gen Virol 76:2887-2893
    • (1995) J Gen Virol , vol.76 , pp. 2887-2893
    • Kelly, C.1    Van Driel, R.2    Wilkinson, G.W.3
  • 40
    • 0030885596 scopus 로고    scopus 로고
    • Leukemia-associated retinoic acid receptor alpha fusion partners PML and PLZF heterodimerize and colocalize to nuclear bodies
    • Koken MH, Reid A, Quignon F, Chelbi-Alix MK, Davies JM, Kabarowski JH, Zhu J, et al (1997) Leukemia-associated retinoic acid receptor alpha fusion partners PML and PLZF heterodimerize and colocalize to nuclear bodies. Proc Natl Acad Sci USA 94:10255-10260
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 10255-10260
    • Koken, M.H.1    Reid, A.2    Quignon, F.3    Chelbi-Alix, M.K.4    Davies, J.M.5    Kabarowski, J.H.6    Zhu, J.7
  • 41
    • 0030602019 scopus 로고    scopus 로고
    • The nuclear domain 10 (ND10) is disrupted by the human cytomegalovirus gene product IE1
    • Korioth F, Maul GG, Plachter B, Stamminger T, Frey J (1996) The nuclear domain 10 (ND10) is disrupted by the human cytomegalovirus gene product IE1. Exp Cell Res 229: 155-158
    • (1996) Exp Cell Res , vol.229 , pp. 155-158
    • Korioth, F.1    Maul, G.G.2    Plachter, B.3    Stamminger, T.4    Frey, J.5
  • 42
    • 0032562608 scopus 로고    scopus 로고
    • Structure and function in the nucleus
    • Lamond AI, Earnshaw WC (1998) Structure and function in the nucleus. Science 280:547-553
    • (1998) Science , vol.280 , pp. 547-553
    • Lamond, A.I.1    Earnshaw, W.C.2
  • 43
    • 0032574737 scopus 로고    scopus 로고
    • Localization of nascent RNA and CREB binding protein with the PML-containing nuclear body
    • LaMorte VJ, Dyck JA, Ochs RL, Evans RM (1998) Localization of nascent RNA and CREB binding protein with the PML-containing nuclear body. Proc Natl Acad Sci USA 95: 4991-4996
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 4991-4996
    • Lamorte, V.J.1    Dyck, J.A.2    Ochs, R.L.3    Evans, R.M.4
  • 44
    • 0032499256 scopus 로고    scopus 로고
    • Recombinant PML adenovirus suppresses growth and tumorigenicity of human breast cancer cells by inducing G1 cell cycle arrest and apoptosis
    • Le XF, Vallian S, Mu ZM, Hung MC, Chang KS (1998) Recombinant PML adenovirus suppresses growth and tumorigenicity of human breast cancer cells by inducing G1 cell cycle arrest and apoptosis. Oncogene 16:1839-1849
    • (1998) Oncogene , vol.16 , pp. 1839-1849
    • Le, X.F.1    Vallian, S.2    Mu, Z.M.3    Hung, M.C.4    Chang, K.S.5
  • 45
    • 0030027449 scopus 로고    scopus 로고
    • Analysis of the growth and transformation suppressor domains of promyelocytic leukemia gene PML
    • Le XF, Yang P, Chang KS (1996) Analysis of the growth and transformation suppressor domains of promyelocytic leukemia gene PML. J Biol Chem 271:130-135
    • (1996) J Biol Chem , vol.271 , pp. 130-135
    • Le, X.F.1    Yang, P.2    Chang, K.S.3
  • 46
    • 0032546017 scopus 로고    scopus 로고
    • Role of the histone deacetylase complex in acute promyelocytic leukemia
    • Lin RJ, Nagy L, Inoue S, Shao W, Miller WH Jr, Evans RM (1998) Role of the histone deacetylase complex in acute promyelocytic leukemia. Nature 391:811-814
    • (1998) Nature , vol.391 , pp. 811-814
    • Lin, R.J.1    Nagy, L.2    Inoue, S.3    Shao, W.4    Miller Jr., W.H.5    Evans, R.M.6
  • 47
    • 0032231895 scopus 로고    scopus 로고
    • Coiled bodies and gems: Janus or Gemini?
    • in this issue
    • Matera AG, Frey MR (1998) Coiled bodies and gems: Janus or Gemini? Am J Hum Genet 63:317-321 (in this issue)
    • (1998) Am J Hum Genet , vol.63 , pp. 317-321
    • Matera, A.G.1    Frey, M.R.2
  • 48
    • 0029583591 scopus 로고
    • Nuclear domain 10 (ND10) associated proteins are also present in nuclear bodies and redistribute to hundreds of nuclear sites after stress
    • Maul GG, Yu E, Ishov AM, Epstein AL (1995) Nuclear domain 10 (ND10) associated proteins are also present in nuclear bodies and redistribute to hundreds of nuclear sites after stress. J Cell Biochem 59:498-513
    • (1995) J Cell Biochem , vol.59 , pp. 498-513
    • Maul, G.G.1    Yu, E.2    Ishov, A.M.3    Epstein, A.L.4
  • 49
    • 0028095410 scopus 로고
    • PML, a growth suppressor disrupted in acute promyelocytic leukemia
    • Mu ZM, Chin KV, Liu JH, Lozano G, Chang KS (1994) PML, a growth suppressor disrupted in acute promyelocytic leukemia. Mol Cell Biol 14:6858-67
    • (1994) Mol Cell Biol , vol.14 , pp. 6858-6867
    • Mu, Z.M.1    Chin, K.V.2    Liu, J.H.3    Lozano, G.4    Chang, K.S.5
  • 50
    • 0031418659 scopus 로고    scopus 로고
    • Stable overexpression of PML alters regulation of cell cycle progression in HeLa cells
    • Mu ZM, Le XF, Vallian S, Glassman AB, Chang KS (1997) Stable overexpression of PML alters regulation of cell cycle progression in HeLa cells. Carcinogenesis 18:2063-2069
    • (1997) Carcinogenesis , vol.18 , pp. 2063-2069
    • Mu, Z.M.1    Le, X.F.2    Vallian, S.3    Glassman, A.B.4    Chang, K.S.5
  • 51
    • 0037498052 scopus 로고    scopus 로고
    • Conjugation with the ubiquitin-related modifier SUMO-1 regulates the partitioning of PML within the nucleus
    • Muller S, Matunis MJ, Dejean A (1998) Conjugation with the ubiquitin-related modifier SUMO-1 regulates the partitioning of PML within the nucleus. EMBO J 17:61-70
    • (1998) EMBO J , vol.17 , pp. 61-70
    • Muller, S.1    Matunis, M.J.2    Dejean, A.3
  • 52
    • 0029558856 scopus 로고
    • The architectural organization of nuclear metabolism
    • Nickerson JA, Blencowe BJ, Penman S (1995) The architectural organization of nuclear metabolism. Int Rev Cytol 162A: 67-123
    • (1995) Int Rev Cytol , vol.162 A , pp. 67-123
    • Nickerson, J.A.1    Blencowe, B.J.2    Penman, S.3
  • 53
    • 0028828122 scopus 로고
    • Overexpression of retinoic acid receptor alpha suppresses myeloid cell differentiation at the promyelocyte stage
    • Onodera M, Kunisada T, Nishikawa S, Sakiyama Y, Matsumoto S, Nishikawa S (1995) Overexpression of retinoic acid receptor alpha suppresses myeloid cell differentiation at the promyelocyte stage. Oncogene 11:1291-1298
    • (1995) Oncogene , vol.11 , pp. 1291-1298
    • Onodera, M.1    Kunisada, T.2    Nishikawa, S.3    Sakiyama, Y.4    Matsumoto, S.5    Nishikawa, S.6
  • 54
    • 0030324321 scopus 로고    scopus 로고
    • PML, PLZF, and NPM genes in the molecular pathogenesis of acute promyelocytic leukemia
    • Pandolfi PP (1996) PML, PLZF, and NPM genes in the molecular pathogenesis of acute promyelocytic leukemia. Haematologica 81:472-482
    • (1996) Haematologica , vol.81 , pp. 472-482
    • Pandolfi, P.P.1
  • 58
    • 0343417089 scopus 로고    scopus 로고
    • The p300/CBP family: Integrating signals with transcription factors and chromatin
    • Shikama N, Lyon J, La Thangue NB (1997) The p300/CBP family: integrating signals with transcription factors and chromatin. Trends Cell Biol 7:230-236
    • (1997) Trends Cell Biol , vol.7 , pp. 230-236
    • Shikama, N.1    Lyon, J.2    La Thangue, N.B.3
  • 59
    • 0030666001 scopus 로고    scopus 로고
    • Ataxin-1 with an expanded glutamine tract alters nuclear matrix-associated structures
    • erratum [1998] Nature 391:307
    • Skinner PJ, Koshy BT, Cummings CJ, Klement IA, Helin K, Servadio A, Zoghbi HY, et al (1997) Ataxin-1 with an expanded glutamine tract alters nuclear matrix-associated structures. Nature 389:971-974 (erratum [1998] Nature 391:307)
    • (1997) Nature , vol.389 , pp. 971-974
    • Skinner, P.J.1    Koshy, B.T.2    Cummings, C.J.3    Klement, I.A.4    Helin, K.5    Servadio, A.6    Zoghbi, H.Y.7
  • 62
    • 0023875393 scopus 로고
    • Developmentally regulated expression of a human "finger"-containing gene encoded by the 5′ half of the ret transforming gene
    • Takahashi M, Inaguma Y, Hiai H, Hirose F (1988) Developmentally regulated expression of a human "finger"-containing gene encoded by the 5′ half of the ret transforming gene. Mol Cell Biol 8:1853-1856
    • (1988) Mol Cell Biol , vol.8 , pp. 1853-1856
    • Takahashi, M.1    Inaguma, Y.2    Hiai, H.3    Hirose, F.4
  • 64
    • 0027297095 scopus 로고
    • A dominant negative retinoic acid receptor blocks neutrophil differentiation at the promyelocyte stage
    • Tsai S, Collins SJ (1993) A dominant negative retinoic acid receptor blocks neutrophil differentiation at the promyelocyte stage. Proc Natl Acad Sci USA 90:7153-7157
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 7153-7157
    • Tsai, S.1    Collins, S.J.2
  • 66
    • 0028158682 scopus 로고
    • Retinoic acid regulates aberrant nuclear localization of PML/RARα in acute promyelocytic leukemia cells
    • Weis K, Rambaud S, Lavau C, Jansen J, Carvalho T, Carmo-Fonseca M, Lamond A, et al (1994) Retinoic acid regulates aberrant nuclear localization of PML/RARα in acute promyelocytic leukemia cells. Cell 76:345-356
    • (1994) Cell , vol.76 , pp. 345-356
    • Weis, K.1    Rambaud, S.2    Lavau, C.3    Jansen, J.4    Carvalho, T.5    Carmo-Fonseca, M.6    Lamond, A.7
  • 67
    • 0030771192 scopus 로고    scopus 로고
    • Fusion of retinoic acid receptor alpha to NuMa the nuclear mitotic apparatus protein by a variant translocation in acute promyelocytic leukemia
    • Wells RA, Catzavelos C, Kamel-Reid S (1997) Fusion of retinoic acid receptor alpha to NuMA the nuclear mitotic apparatus protein by a variant translocation in acute promyelocytic leukemia. Nat Genet 17:109-113
    • (1997) Nat Genet , vol.17 , pp. 109-113
    • Wells, R.A.1    Catzavelos, C.2    Kamel-Reid, S.3
  • 68
    • 0030890942 scopus 로고    scopus 로고
    • Arsenic-induced PML targeting onto nuclear bodies: Implications for the treatment of acute promyelocytic leukemia
    • Zhu J, Koken MH, Quignon F, Chelbi-Alix MK, Degos L, Wang ZY, Chen Z, et al (1997) Arsenic-induced PML targeting onto nuclear bodies: implications for the treatment of acute promyelocytic leukemia. Proc Natl Acad Sci USA 94:3978-3983
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 3978-3983
    • Zhu, J.1    Koken, M.H.2    Quignon, F.3    Chelbi-Alix, M.K.4    Degos, L.5    Wang, Z.Y.6    Chen, Z.7


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