메뉴 건너뛰기




Volumn 770, Issue , 2012, Pages 39-58

PML nuclear bodies and other trim-defined subcellular compartments

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; ISOPROTEIN; PROMYELOCYTIC LEUKEMIA PROTEIN; PROTEIN TIF1ALPHA; REGULATOR PROTEIN; RFP PROTEIN; TRANSCRIPTION FACTOR; TRIPARTITE MOTIF PROTEIN; UNCLASSIFIED DRUG; PROTEIN;

EID: 84878950860     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4614-5398-7_4     Document Type: Article
Times cited : (9)

References (126)
  • 1
    • 0026782376 scopus 로고
    • A novel zinc finger coiled-coil domain in a family of nuclear proteins
    • I. Reddy BA, Etkin LD, Freemont PS. A novel zinc finger coiled-coil domain in a family of nuclear proteins. Trends Biochem Sci 1992; 17(9):344-345.
    • (1992) Trends Biochem Sci , vol.17 , Issue.9 , pp. 344-345
    • Reddy, B.A.I.1    Etkin, L.D.2    Freemont, P.S.3
  • 2
    • 17744371839 scopus 로고    scopus 로고
    • The tripartite motiffamily identifies cell compartments
    • Reymond A, Meroni G, Fantozzi A, et al. The tripartite motiffamily identifies cell compartments. EMBO J 2001; 20(9):2140-2151.
    • (2001) EMBO J , vol.20 , Issue.9 , pp. 2140-2151
    • Reymond, A.1    Meroni, G.2    Fantozzi, A.3
  • 3
    • 30444452500 scopus 로고    scopus 로고
    • TRIM/RBCC, a novel class of ' single protein RING finger ' E3 ubiquitin ligases
    • Meroni G, Diez-Roux G. TRIM/RBCC, a novel class of ' single protein RING finger ' E3 ubiquitin ligases. Bioessays 2005; 27(11):1147-1157.
    • (2005) Bioessays , vol.27 , Issue.11 , pp. 1147-1157
    • Meroni, G.1    Diez-Roux, G.2
  • 4
    • 33645731002 scopus 로고    scopus 로고
    • The number of PML nuclear bodie s increases in early S phase by a fission mech anism
    • Dellaire G, Chin g RW, Dehghani H, et al. The number of PML nuclear bodie s increases in early S phase by a fission mech anism. J Ce ll Sci 2006 ; 119(Pt 6): I026-1 033.
    • (2006) J Ce Ll Sci , vol.119 , Issue.PART 6 , pp. 1026-1033
    • Dellaire, G.1    Ching, R.W.2    Dehghani, H.3
  • 5
    • 0032721540 scopus 로고    scopus 로고
    • PML is critical forNOl Oformation and recruits the PML-interacting prot ein daxx to this nuclear structure when modified by SUMO-I
    • Isho vAM, SotnikovAG, Negorev De t al. PML is critical forNOl Oformation and recruits the PML-interacting prot ein daxx to this nuclear structure when modified by SUMO-I . J Ce ll BioI 1999; 147(2):221-234.
    • (1999) J Ce Ll BioI , vol.147 , Issue.2 , pp. 221-234
    • Ishov, A.M.1    Sotnikov, A.G.2    Negorev, D.3
  • 6
    • 0343776952 scopus 로고    scopus 로고
    • Role of SUMO-I-modified PML in nucle ar body formation
    • Zhong S, Muller S, Ronche tti S, et al. Role of SUMO-I-modified PML in nucle ar body formation. Blood 2000 ; 95(9):2748-2 752.
    • (2000) Blood , vol.95 , Issue.9 , pp. 2748-2752
    • Zhong, S.1    Muller, S.2    Ronchetti, S.3
  • 7
    • 0025633966 scopus 로고
    • Isolation and characterization of cDNA encoding a human nuclear antigen predominantly recogni zed by autoa ntibodi es from patients with primary biliary cirrhosis
    • Szostecki C, Guldner HH, Netter HJ, et al. Isolation and characterization of cDNA encoding a human nuclear antigen predomin antly recogni zed by autoa ntibodi es from patients with primary biliary cirrhosis. J Immunol 1990; 145(12):4338-4347.
    • (1990) J Immunol , vol.145 , Issue.12 , pp. 4338-4347
    • Szostecki, C.1    Guldner, H.H.2    Netter, H.J.3
  • 8
    • 0035809924 scopus 로고    scopus 로고
    • The transcriptio n coactivator CBP is a dynamic component of the promyeloc ytic leukemi a nucle ar body
    • Boisvert I'M, Kruhlak MJ, Box AK, et al. The transcriptio n coactivator CBP is a dynamic component of the promyeloc ytic leukemi a nucle ar body. J Cell BioI 2001; 152(5):1099-1106.
    • (2001) J Cell BioI , vol.152 , Issue.5 , pp. 1099-1106
    • I'M, B.1    Kruhlak, M.J.2    Box, A.K.3
  • 9
    • 0033952527 scopus 로고    scopus 로고
    • Sequestration and inhibiti on of Daxx-m ediated transcriptional repression by PML
    • Li H, Leo C, Zhu J, et al. Sequestration and inhibiti on of Daxx-m ediated transcriptional repression by PML. Mol Cell Bioi 2000; 20(5): 1784-1796.
    • (2000) Mol Cell Bioi , vol.20 , Issue.5 , pp. 1784-1796
    • Li, H.1    Leo, C.2    Zhu, J.3
  • 10
    • 0031929684 scopus 로고    scopus 로고
    • The promyelocytic leukemia gene product (PML) forms stable complexes with the retinoblastoma protein
    • Alcalay M, Tomass oni L, Colombo E, et al. The promyelocytic leukemia gene product (PML) forms stable complexes with the retinoblastoma protein. Mol Cell BioI 1998; 18(2) : I084-1093
    • (1998) Mol Cell BioI , vol.18 , Issue.2
    • Alcalay, M.1    Tomassoni, L.2    Colombo, E.3
  • 11
    • 0030796314 scopus 로고    scopus 로고
    • Surfa ce residue mutations of the PML RING finger domain alter the formation of nuclear matrix-associated PML bodies
    • Boddy MN, Duprez E, Borden KL, et al. Surfa ce residue mutations of the PML RING finger domain alter the formation of nuclear matrix-associated PML bodie s. J Cell Sci 1997; 110(Pt 18):2197-2205.
    • (1997) J Cell Sci , vol.110 , Issue.PART 18 , pp. 2197-2205
    • Boddy, M.N.1    Duprez, E.2    Borden, K.L.3
  • 12
    • 0035969107 scopus 로고    scopus 로고
    • Cellular prot eins localized at and interacting within NDIOPML nuclear bodies! PODs suggest functions of a nuclear depot
    • Negorev O, Maul GG. Cellular prot eins localized at and interacting within NDIO/PML nuclear bodies! PODs suggest functions of a nuclear depot. Oncogene 200 I ; 20(49):7234-7242.
    • (2001) Oncogene , vol.20 , Issue.49 , pp. 7234-7242
    • Negorev, O.1    Maul, G.G.2
  • 13
    • 0037169341 scopus 로고    scopus 로고
    • The role of PML in tumor suppress ion
    • Salomoni L, Pandolfi PI' . The role of PML in tumor suppress ion. Ce ll 2002; 108(2): 165-170.
    • (2002) Cell , vol.108 , Issue.2 , pp. 165-170
    • Salomoni, L.1    Pandolfi, P.L.2
  • 15
    • 4644351274 scopus 로고    scopus 로고
    • PML nuclear bodie s: Dynam ic sensors of DNA damage and cellular stress
    • Dellaire G, Bazett-Jones 0L . PML nuclear bodie s: dynam ic sensors of DNA damage and cellular stress. Bioessays 2004 ; 26(9) :963-9 77.
    • (2004) Bioessays , vol.26 , Issue.9 , pp. 963-977
    • Dellaire, G.1    Bazett-Jones, O.L.2
  • 16
    • 0035147230 scopus 로고    scopus 로고
    • Inter feron gamma regulates accumulation of the proteasome activator PA28 and immunoproteasomes at nuclear PML bodies
    • Fabunm i RP, Wigley WC, Thomas Pl, et al. Inter feron gamma regulates accumulation of the proteasome activator PA28 and immunoproteasom es at nuclear PML bodies. J Ce ll Sci 2001; 114(Pt 1):29-36.
    • (2001) J Ce Ll Sci , vol.114 , Issue.PART 1 , pp. 29-36
    • Fabunmi, R.P.1    Wigley, W.C.2    Pl, T.3
  • 17
    • 0034186133 scopus 로고    scopus 로고
    • The transcription Al role of PML and the nuclear body
    • Zhong S, Salomoni L, Pandolfi PI'. The transc ription al role of pML and the nuclear body. Nat Cell BioI 2000; 2(5): E85-90.
    • (2000) Nat Cell BioI , vol.2 , Issue.5
    • Zhong, S.1    Salomoni, L.2    Pandolfi, P.L.3
  • 18
    • 0036798404 scopus 로고    scopus 로고
    • Finding a role for pML in ApL pathogenesis: A critical asses sment of potenti al PML activiti es
    • Strudwick S, Borden KL. Finding a role for pML in ApL pathogenesis: a critical asses sment of potenti al PML activiti es. Leukemia 2002; 16(10):1906-1917.
    • (2002) Leukemia , vol.16 , Issue.10 , pp. 1906-1917
    • Strudwick, S.1    Borden, K.L.2
  • 19
    • 34548501553 scopus 로고    scopus 로고
    • Are promyeloc ytic leukaemia protein nuclear bodie s a scaffold for caspas e-2 programmed cell death?
    • Sanche z-Pulido L, Valencia A, Rojas AM. Are promyeloc ytic leukaemia protein nuclear bodie s a scaffold for caspas e-2 programmed cell death? Trends Biochem Sci 200 7; 32(9):400-406.
    • (2007) Trends Biochem Sci , vol.32 , Issue.9 , pp. 400-406
    • Sanchez-Pulido, L.1    Valencia, A.2    Rojas, A.M.3
  • 20
    • 34347348272 scopus 로고    scopus 로고
    • PML and pML nuclear bodie s: Impl ications in antiviral defence
    • Everett RD, Chelb i-Alix MK. pML and pML nuclear bodie s: impl ications in antiviral defence . Biochimie 2007;89(6-7):819-830.
    • (2007) Biochimie , vol.89 , Issue.6-7 , pp. 819-830
    • Everett, R.D.1    Chelbi-Alix, M.K.2
  • 21
    • 27244444559 scopus 로고    scopus 로고
    • TRIM family proteins : Retroviral restrict ion and antiviral defence
    • Nisole S, Stoye Jp, Saib A. TRIM family proteins : retroviral restrict ion and antiviral defence. Nat Rev Microbiol 2005; 3(10) :799-808.
    • (2005) Nat Rev Microbiol , vol.3 , Issue.10 , pp. 799-808
    • Nisole, S.1    Stoye, J.P.2    Saib, A.3
  • 22
    • 0027239790 scopus 로고
    • The RING finger A novel protein sequence motif related to the zinc finger
    • Freemont PS. The RING finger. A novel protein sequence motif related to the zinc finger. Ann NY Acad Sci 1993; 684:174-192.
    • (1993) Ann NY Acad Sci , vol.684 , pp. 174-192
    • Freemont, P.S.1
  • 23
    • 0034266806 scopus 로고    scopus 로고
    • RING finger proteins: Mediators of ubiquitin ligase activity
    • Joazeiro CA, Weissman AM. RING finger protein s: mediato rs of ubiqui tin ligase activity. Cell 2000; 102(5):549-552.
    • (2000) Cell , vol.102 , Issue.5 , pp. 549-552
    • Joazeiro, C.A.1    Weissman, A.M.2
  • 24
    • 0028932963 scopus 로고
    • The solution structure of the RING finger domain from the acute promyelocytic leukaemia proto-oncoprotein PML
    • Borden KL, Boddy MN, Lally J, et al. The solution structure of the RING finger domain from the acute promyelocytic leuka emia proto-oncoprotein PML. EMBO J 1995; 14(7):1532-1541.
    • (1995) EMBO J , vol.14 , Issue.7 , pp. 1532-1541
    • Borden, K.L.1    Boddy, M.N.2    Lally, J.3
  • 25
    • 0028095410 scopus 로고
    • PML, a growth suppressor disrup ted in acute promyeloc ytic leukemia
    • Mu ZM, Chin KV, Liu JH, et al. pML, a growth suppressor disrup ted in acute promyeloc ytic leukemia. Mol Cell BioI 1994; 14(10):6858-6867.
    • (1994) Mol Cell BioI , vol.14 , Issue.10 , pp. 6858-6867
    • Mu, Z.M.1    Chin, K.V.2    Liu, J.H.3
  • 26
    • 0030027449 scopus 로고    scopus 로고
    • Analys is ofthe growth and transformation suppressor domains ofpromyeloc ytic leukemia gene
    • Le XI', Yang L, Chang KS.Analys is ofthe growth and transformation suppressor domains ofpromyeloc ytic leukemia gene, pML. J BioI Chern 1996; 271(1) :130-13 5.
    • (1996) PML J BioI Chern , vol.271 , Issue.1 , pp. 130-135
    • Le, X.I.1    Yang, L.2    Chang, K.S.3
  • 27
    • 0030817386 scopus 로고    scopus 로고
    • The promyeloc ytic leukemia protein pML has apro-apoptotic activity mediated through its RING domain
    • Borden KL, CampbellDwyer EJ, Salvato MS.The promyeloc ytic leukemia protein pML has apro-apoptotic activity mediated through its RING domain. FEBS Lett 1997; 418(1-2):30-34.
    • (1997) FEBS Lett , vol.418 , Issue.1-2 , pp. 30-34
    • Borden, K.L.1    Campbell Dwyer, E.J.2    Salvato, M.S.3
  • 28
    • 0035969127 scopus 로고    scopus 로고
    • Role and fate of 'Plvll. Nuclear bodies in response to interferon and viral infections
    • Regad T, Chelbi-Alix MK. Role and fate of'Plvll. nucle ar bodies in response to interferon and vira l infections. Oncogene 200 I ; 20(49) :72 74-7286.
    • (2001) Oncogene , vol.20 , Issue.49-72 , pp. 74-7286
    • Regad, T.1    Chelbi-Alix, M.K.2
  • 29
    • 0037180485 scopus 로고    scopus 로고
    • Control ofbiochemical reactions through supramolecular RING domain self-assembly
    • Kentsis A, Gordon RE, Borden KL. Control ofbiochemical reactions through supramolecular RING domain self-assembly. Proc Natl Acad Sci USA 2002; 99(24): 15404-15409 .
    • (2002) Proc Natl Acad Sci USA , vol.99 , Issue.24 , pp. 15404-15409
    • Kentsis, A.1    Gordon, R.E.2    Borden, K.L.3
  • 30
    • 0032463343 scopus 로고    scopus 로고
    • RING fingers and B-boxes: Zinc-binding protein-protein interac tion domains
    • Borden KL. RING fingers and B-boxe s: zinc-binding protein-protein interac tion doma ins. Biochem Cell Bioi 1998; 76(2-3):351-358.
    • (1998) Biochem Cell Bioi , vol.76 , Issue.2-3 , pp. 351-358
    • Borden, K.L.1
  • 31
    • 0029918562 scopus 로고    scopus 로고
    • In vivo and in vitro cha racteri zation of the BI and B2 zinc-binding domai ns from the acute promyelocytic leukemia protooncoprotein pML
    • Borden KL, Lally JM, Martin SR, et al. In vivo and in vitro cha racteri zation of the BI and B2 zinc-binding domai ns from the acute promyelocytic leukemia protooncoprotein pML. Proc Natl Acad Sci USA 1996; 93(4) :1601-1606.
    • (1996) Proc Natl Acad Sci USA , vol.93 , Issue.4 , pp. 1601-1606
    • Borden, K.L.1    Lally, J.M.2    Martin, S.R.3
  • 32
    • 7344248065 scopus 로고    scopus 로고
    • Cooperation betw een the RING + BI-B2 and coiled-coil domain s of pML is necess ary for its effects on cell survival
    • Fagioli M, Alcalay M, Tomassoni L, et al. Cooperation betw een the RING + BI-B2 and coiled-coil domain s of pML is necess ary for its effects on cell survival. Oncogene 1998; 16(22):2905-2913.
    • (1998) Oncogene , vol.16 , Issue.22 , pp. 2905-2913
    • Fagioli, M.1    Alcalay, M.2    Tomassoni, L.3
  • 33
    • 0035908032 scopus 로고    scopus 로고
    • Lallemand-Breiten bach V, Zhu J, Puvion F, et al
    • Lallemand-Breiten bach V, Zhu J, Puvion F, et al. Role of promyelocytic leukemia (PML) sumolation in nucle ar body formatio n, li S proteasome recru itment and As203-ind uced PML or PMLlretinoic acid receptor alpha degradation. J Exp Med 2001 ; 193(12):1361-1371.
    • (2001) J Exp Med , vol.193 , Issue.12 , pp. 1361-1371
  • 34
    • 13844269220 scopus 로고    scopus 로고
    • A sumoylation site in PMLlRARA is essential for leukemi C transformation
    • Zhu J, Zhou J, Peres L, et al. A sumoylation site in PMLlRARA is essential for leukemi c transfo rmatio n. CancerCell2005; 7(2):143-153.
    • (2005) Cancer Cell , vol.7 , Issue.2 , pp. 143-153
    • Zhu, J.1    Zhou, J.2    Peres, L.3
  • 35
    • 33646116320 scopus 로고    scopus 로고
    • Solutio n structure of the RBCC/TR im B-boxl domain of human MIDI: B-box with a RING
    • Massiah MA, Simmons BN, Short KM, et al. Solutio n structure of the RBCC/TR IM B-boxl domain of human MIDI: B-box with a RING. J Mol Bioi 2006; 358(2):532-545.
    • (2006) J Mol Bioi , vol.358 , Issue.2 , pp. 532-545
    • Massiah, M.A.1    Simmons, B.N.2    Short, K.M.3
  • 36
    • 10144237851 scopus 로고    scopus 로고
    • Effects on differ entiation by the promye locytic leukemia PMLI RARalpha protein depend on the fusion of the PML protein dimerization and RARalpha DNA binding domains
    • Grignani F, Testa U, Rogaia 0, et al. Effects on differ entiation by the promye locytic leukemia PMLI RARalpha protein depe nd on the fusion of the PML protein dimerization and RARalpha DNA binding domains. EMBO J 1996; 15(18):4949-4958.
    • (1996) EMBO J , vol.15 , Issue.18 , pp. 4949-4958
    • Grignani, F.1    Testa, U.2    Rogaia, O.3
  • 37
    • 0026583943 scopus 로고
    • Kastner L, Perez A, Lutz Y, et al
    • Kastner L, Perez A, Lutz Y, et al. Structure, localization and transcriptional propert ies of two classe s of retinoic acid receptor alpha fusion proteins in acute promyelocytic leukem ia (APL) : struct ural similaritie s with a ncw family of oncoproteins. EMBO J 1992; 11(2):629-642.
    • (1992) EMBO J , vol.11 , Issue.2 , pp. 629-642
  • 38
    • 0027328057 scopus 로고
    • PMLRAR homodimers: Distinct DNA binding properties and heteromeric interactions with RXR
    • Perez A, Kastner P, Sethi S, et al. PMLRAR homodimers: distinct DNA binding properties and heteromeric interactions with RXR. EMBO J 1993; 12(8):3 171-3182.
    • (1993) EMBO J , vol.12 , Issue.8 , pp. 3171-3182
    • Perez, A.1    Kastner, P.2    Sethi, S.3
  • 39
    • 1242272073 scopus 로고    scopus 로고
    • The coiled-coil domain is the structural determinant for mammalian homologues of Drosophila Sina-mediated degra dation of promye locytic leukemia protein and other tripartite motif proteins by the proteasome
    • Fanelli M, Fantozzi A, De Luca P, et al. The coiled-coil domain is the structural determinant for mammalian homologues of Drosophila Sina-mediated degra dation of promye locytic leukemia protein and other tripartite motif proteins by the proteasome. J Bioi Chem 2004; 279(7):5374-5379.
    • (2004) J Bioi Chem , vol.279 , Issue.7 , pp. 5374-5379
    • Fanelli, M.1    Fantozzi, A.2    De Luca, P.3
  • 40
    • 0037498052 scopus 로고    scopus 로고
    • Conjugation with the ubiquitin-related modifier SUMO-I reg ulates the partitioning ofPML within the nucleus
    • Muller S, Matunis MJ, Dejea n A. Conjugation with the ubiquitin-related modifier SUMO-I reg ulates the partitioning ofPML within the nucle us. EMBO J 1998; 17(1):61-70. 4 1
    • (1998) EMBO J , vol.17 , Issue.1 , pp. 61-70
    • Muller, S.1    Matunis, M.J.2    Dejean, A.3
  • 41
    • 0035969125 scopus 로고    scopus 로고
    • PML protein isoforms and the RBCC/TRIM motif
    • Jensen K, Shiels C, Frecmont PS. PML protein isoforms and the RBCC/TRIM motif Oncogene 2001; 20(49):72 23-7233
    • (2001) Oncogene , vol.20 , Issue.49 , pp. 7223-7233
    • Jensen, K.1    Shiels, C.2    Frecmont, P.S.3
  • 42
    • 0035929557 scopus 로고    scopus 로고
    • Polymeric cha ins ofSUMO-2 and SUMO-3 are conj ugated to protein substrates by SAEIISAE2 and Ubc9
    • Tatham MH, Jaffray E, Vaughan OA, et al. Polymeric cha ins ofSUMO-2 and SUMO-3 are conj ugated to protein substrates by SAEIISAE2 and Ubc9. J BioI Chem 2001 ; 276(38):35368-3537 4
    • (2001) J BioI Chem , vol.276 , Issue.38 , pp. 35368-35374
    • Tatham, M.H.1    Jaffray, E.2    Vaughan, O.A.3
  • 43
    • 24644522876 scopus 로고    scopus 로고
    • Stab ilization of PML nuclear loca lization by conjugation and oligome rization ofSUMO-3
    • Fu C, Ahmed K, Ding H, et al. Stab ilization of PML nuclear loca lization by conjugation and oligome rization ofSUMO-3. Oncoge ne 2005; 24(35) :5401-5 413.
    • (2005) Oncogene , vol.24 , Issue.35 , pp. 5401-5413
    • Fu, C.1    Ahmed, K.2    Ding, H.3
  • 44
    • 0032500634 scopus 로고    scopus 로고
    • Identification of three major sentrinization sites in PML
    • Kamitan i T, Kito K, Nguyen HP, et al. Identification of three major sentrinization sites in PML. J Bioi Chem 1998; 273(41):26675-26682.
    • (1998) J Bioi Chem , vol.273 , Issue.41 , pp. 26675-26682
    • Kamitani, T.1    Kito, K.2    Nguyen, H.P.3
  • 45
    • 0033034749 scopus 로고    scopus 로고
    • SUMO-I modificationofthe acute promyclocytic Icukaemia protein PML: Implications for nuclear localisation
    • Duprcz E, Saurin AJ, Desterro JM et al. SUMO-I modificationofthe acute promyclocytic Icukaemia protein PML: implications for nuclear localisation. J Cell Sci 1999; 112(Pt 3):381 -393 .
    • (1999) J Cell Sci , vol.112 , Issue.PART 3 , pp. 381-393
    • Duprcz, E.1    Saurin, A.J.2    Desterro, J.M.3
  • 46
    • 0032574737 scopus 로고    scopus 로고
    • Local ization of nascent RNA and CREB binding protein with the PML-containing nuclear body
    • LaMorte VJ, Dyck JA, Ochs RL, et al. Local ization of nascent RNA and CREB binding protein with the PML-containing nuclear body. Proc Natl Acad Sci USA 1998; 95(9) :4991-4996
    • (1998) Proc Natl Acad Sci USA , vol.95 , Issue.9 , pp. 4991-4996
    • Lamorte, V.J.1    Dyck, J.A.2    Ochs, R.L.3
  • 47
    • 0033537828 scopus 로고    scopus 로고
    • Identification of the enzyme req uired for activa tion of the small ubiquitin-like protein SUMO-I
    • Desterro JM, Rodriguez MS, Kemp GO, et al. Identification of the enzyme req uired for activa tion of the small ubiquitin-like protein SUMO-I. J Bioi Chem 1999; 274(15):10618-10624.
    • (1999) J Bioi Chem , vol.274 , Issue.15 , pp. 10618-10624
    • Desterro, J.M.1    Rodriguez, M.S.2    Kemp, G.O.3
  • 48
    • 33750447586 scopus 로고    scopus 로고
    • The mechanisms ofPML-nuclear body formation
    • Shen TH, Lin HK, Scagl ioni PP, et al. The mechanisms ofPML-nuclear body formation. Mol Ce ll 2006; 24(3) :331-339 .
    • (2006) Mol Cell , vol.24 , Issue.3 , pp. 331-339
    • Shen, T.H.1    Lin, H.K.2    Scaglioni, P.P.3
  • 50
    • 34648840192 scopus 로고    scopus 로고
    • SUMO-targ eted ubiquiti n ligases in genome stability
    • Prudden J, Pebernard S, Raffa G, et al. SUMO-targ eted ubiquiti n ligases in genome stability. EMBO J 2007 ; 26(18):4089-4 101.
    • (2007) EMBO J , vol.26 , Issue.18 , pp. 4089-4101
    • Prudden, J.1    Pebernard, S.2    Raffa, G.3
  • 51
    • 34648816891 scopus 로고    scopus 로고
    • Conserve d function of RNF4 family proteins in eukaryotes: Targeting a ubiquitin ligase to SUMOylated proteins
    • Sun H, Leverson JD, Hunter T. Conserve d function of RNF4 family proteins in eukaryotes: targeting a ubiquitin ligase to SUMOylated proteins. EMBO J 2007 ; 26(18):4 102-41 12.
    • (2007) EMBO J , vol.26 , Issue.18 , pp. 4102-4112
    • Sun, H.1    Leverson, J.D.2    Hunter, T.3
  • 52
    • 0028916423 scopus 로고
    • The PML growth-suppressor has an altered expression in human oncogenesis
    • Koken MH, Linares-Cruz G, Quignon F, et al. The PML growth-suppressor has an altered expression in human oncogenesis. Oncogene 1995; 10(7):1315-1324.
    • (1995) Oncogene , vol.10 , Issue.7 , pp. 1315-1324
    • Koken, M.H.1    Linares-Cruz, G.2    Quignon, F.3
  • 53
    • 0036170782 scopus 로고    scopus 로고
    • Metabolic-energy-dependent movement of PML bodies within the mammalian cell nucleus
    • Muratani M, Gerlic h 0, Janicki SM, et al. Metabolic-energy-dependent movement of PML bodies within the mammalian cell nucleus . Nat Cc ll Bioi 2002 ; 4(2): 106-110.
    • (2002) Nat Cc Ll Bioi , vol.4 , Issue.2 , pp. 106-110
    • Muratani, M.1    Gerlich, O.2    Janicki, S.M.3
  • 54
    • 0242550970 scopus 로고    scopus 로고
    • Size, position and dynamic behavior of PML nucle ar bodies following cell stress as a paradigm for supramolecular trafficking and assembly
    • Eskiw CH, Dellai re G, Mymryk JS, et al. Size, position and dynamic behavior of PML nucle ar bodies following cell stress as a parad igm for supramolecular trafficking and assembly. J Cell Sci 2003 ; 116(Pt 21):44 55-4466.
    • (2003) J Cell Sci , vol.116 , Issue.PART 21 , pp. 4455-4466
    • Eskiw, C.H.1    Dellaire, G.2    Mymryk, J.S.3
  • 55
    • 0033380850 scopus 로고    scopus 로고
    • Cell cycle regulation ofPML modification andNOI0 composition
    • Everett RD, Lomonte P, SternsdorfT, et al. Cell cycle regulation ofPML modification andNOI0 composition. J Cell Sci 1999; 112(Pt 24):458 1-4588 .
    • (1999) J Cell Sci , vol.112 , Issue.24 PART , pp. 4581-4588
    • Everett, R.D.1    Lomonte, P.2    Sternsdorf, T.3
  • 56
    • 33645749156 scopus 로고    scopus 로고
    • Mitotic accumulations of PML protein contribute to the re-establishment of PML nuclear bodies in GI
    • Dellaire G, Eskiw CH, Dehghani H, et al. Mitotic accumulations of PML protein contribute to the re-establishment of PML nuclear bodies in GI. J Cell Sci 2006; 119(Pt 6): 1034-1042.
    • (2006) J Cell Sci , vol.119 , Issue.PART 6 , pp. 1034-1042
    • Dellaire, G.1    Eskiw, C.H.2    Dehghani, H.3
  • 57
    • 33746073030 scopus 로고    scopus 로고
    • PML nuclear bodies are highly organ ised DNA-prot ein structures with a function in heterochromatin remodell ing at the G2 phase
    • Luciani JJ, Depetris 0, Usson Y et al. PML nuclear bodies are highly organ ised DNA-prot ein structures with a function in heterochromatin remodell ing at the G2 phase. J Cell Sci 2006; 119(Pt 12):2518-2531.
    • (2006) J Cell Sci , vol.119 , Issue.PART 12 , pp. 2518-2531
    • Luciani, J.J.1    Depetris, O.2    Usson, Y.3
  • 58
    • 35548950835 scopus 로고    scopus 로고
    • A nucleolar targeting signal in PML-I addresses PML to nucleolar caps in stressed or senescent cells
    • Condemine W, Taka hashi Y, Le Bras M, et al. A nucleolar targeting signal in PML-I addresses PML to nucleolar caps in stressed or senescent cells. J Cell Sci 2007; 120(Pt 18):32 19-3227.
    • (2007) J Cell Sci , vol.120 , Issue.PART 18 , pp. 3219-3227
    • Condemine, W.1    Taka Hashi, Y.2    Le Bras, M.3
  • 59
    • 0026578112 scopus 로고
    • Alternative splicing ofPML transcripts predicts coexpre ssion of several carboxy-terminally different protein isoforms
    • Fagioli M, Alcalay M, Pandolfi PI', et al. Alternative splicing ofPML transcripts predicts coexpre ssion of several carboxy-terminally differ ent protein isoforms. Oncogen e 1992; 7(6):1083-1091.
    • (1992) Oncogene , vol.7 , Issue.6 , pp. 1083-1091
    • Fagioli, M.1    Alcalay, M.2    Pandolfi, P.L.3
  • 60
    • 4544256756 scopus 로고    scopus 로고
    • Cytoplasmic PML function in TGF-beta signaling
    • Lin HK, Bergmann S, Pando lfi PP. Cytoplasmic PML function in TGF-beta signalling. Nature 2004; 431(7005):205-2 11.
    • (2004) Nature , vol.431 , Issue.7005 , pp. 205-211
    • Lin, H.K.1    Bergmann, S.2    Pandolfi, P.P.3
  • 61
    • 34447116912 scopus 로고    scopus 로고
    • New insights into the cytoplasmic function of PML
    • Salomoni P, Bellodi C. New insights into the cytoplasmic function of PML. Histol Histopathol 2007; 22(8):937-946.
    • (2007) Histol Histopathol , vol.22 , Issue.8 , pp. 937-946
    • Salomoni, P.1    Bellodi, C.2
  • 62
    • 0034630158 scopus 로고    scopus 로고
    • A comparison of the activity, sequence specificity and CRMI-dependence of different nuclear export signals
    • Henderso n BR, Eleftherio u A. A comparison of the activity, sequence specificity and CRMI-dependence of different nuclear export signals . Exp Cell Res 2000 ; 256 (I):2 13-224.
    • (2000) Exp Cell Res , vol.256 , Issue.1-2 , pp. 13-224
    • Henderson, B.R.1    Eleftheriou, A.2
  • 63
    • 33745728153 scopus 로고    scopus 로고
    • Chara cterization of endogenous human promyelocytic leukemia isofonn s
    • Condemine W, Takahashi Y, Zhu J, et al. Chara cterization of endogenous human promyelocytic leukemia isofonn s. Cancer Res 2006; 66 (12):6192-6198.
    • (2006) Cancer Res , vol.66 , Issue.12 , pp. 6192-6198
    • Condemine, W.1    Takahashi, Y.2    Zhu, J.3
  • 64
    • 14644394332 scopus 로고    scopus 로고
    • A role for PML3 in centrosome duplication and genome stability
    • Xu lX, lou WX, Lin P, et al. A role for PML3 in centrosome duplication and genome stability. Mol Cell 2005; 17(5):72 1-732 .
    • (2005) Mol Cell , vol.17 , Issue.5 , pp. 721-732
    • Xu, I.X.1    Lou, W.X.2    Lin, P.3
  • 65
    • 0031791875 scopus 로고    scopus 로고
    • PML is essential for multiple apoptoti c pathways
    • Wang lG, Ruggero D, Ronchetti S, et al. PML is essential for multiple apoptoti c pathways. Nat Genet 1998; 20(3) :266-272.
    • (1998) Nat Genet , vol.20 , Issue.3 , pp. 266-272
    • Lg, W.1    Ruggero, D.2    Ronchetti, S.3
  • 66
    • 0346147033 scopus 로고    scopus 로고
    • Body language: The function of PML nuclear bodies in apoptosis regulation
    • Hofmann TG, Will H. Body language: the function of PML nuclear bodies in apoptosis regulation. Cell Death Differ 2003; 10(12):1290-1299.
    • (2003) Cell Death Differ , vol.10 , Issue.12 , pp. 1290-1299
    • Hofmann, T.G.1    Will, H.2
  • 67
    • 0034669124 scopus 로고    scopus 로고
    • Regulation of P53 activity in nuclear bodies by a specific PML isoform
    • Fogal V, Gost issa M, Sandy Pet al. Regulation of p53 activity in nuclear bodies by a specific PML isoform. EMBO J 2000; 19(22):6185-6195.
    • (2000) EMBO J , vol.19 , Issue.22 , pp. 6185-6195
    • Fogal, V.1    Gostissa, M.2    Sandy, P.3
  • 68
    • 0034306019 scopus 로고    scopus 로고
    • The function of PML in p53-de pendent apoptosis
    • Guo A, Salomo ni P, Luo J, et al. The function of PML in p53-de pendent apoptos is. Nat Cell BioI 2000; 2 (I0):730-736.
    • (2000) Nat Cell BioI , vol.2 , Issue.10 , pp. 730-736
    • Guo, A.1    Salomoni, P.2    Luo, J.3
  • 69
    • 0025875679 scopus 로고
    • The PML-RAR alpha fusion mRNA generated by the t(15;17) translocation inacutepromyelocytic leukemia encodes a functionally altered RAR
    • de The H, Lavau C, Marchio A, et al. The PML-RAR alpha fusion mRNA generated by the t(15;17) translocation inacutepromyelocytic leukemia encodes a functionally altered RAR.Cell 1991;66(4):675-684.
    • (1991) Cell , vol.66 , Issue.4 , pp. 675-684
    • De The, H.1    Lavau, C.2    Marchio, A.3
  • 70
    • 0025780876 scopus 로고
    • Chromosomal translocation t(l5;17) in human acute promyelocytic leukemia fuses RAR alpha with a novel putative transcription factor, PML
    • Kakizuka A, Miller WH Jr, Umeso no K, et al. Chromosomal translocation t(l5;17) in human acute promyelocytic leukemia fuses RAR alpha with a novel putative transcription factor, PML. Cell 1991; 66(4):663-674.
    • (1991) Cell , vol.66 , Issue.4 , pp. 663-674
    • Kakizuka, A.1    Miller Jr., W.H.2    Umesono, K.3
  • 71
    • 0025917413 scopus 로고
    • Structure and origin of the acute promyelocytic leukemia myll RAR alpha eDNA and characterization of its retinoid-binding and transactivation properties
    • Pandolfi PP, Grignani F, Alcalay M, et al. Structure and origin of the acute promyelocytic leukemia myll RAR alpha eDNA and characterization of its retinoid-binding and transactivation properties. Oncogene 1991; 6(7):1285-1292.
    • (1991) Oncogene , vol.6 , Issue.7 , pp. 1285-1292
    • Pandolfi, P.P.1    Grignani, F.2    Alcalay, M.3
  • 72
    • 0026326963 scopus 로고
    • Characterization of a zinc finger gene disrupted by the t(15;17) in acute promyelocytic leukemia
    • Goddard AD, Borrow J, Freemont PS, et al. Characterization of a zinc finger gene disrupted by the t(15;17) in acute promyelocytic leukemia. Science 1991; 254(5036):1371-1374.
    • (1991) Science , vol.254 , Issue.5036 , pp. 1371-1374
    • Goddard, A.D.1    Borrow, J.2    Freemont, P.S.3
  • 73
    • 0028179010 scopus 로고
    • A novel macromo lecular structure is a target of the promyelocyteretinoic acid receptor oncoprotein
    • Dyck JA, Maul GG, Miller WH Jr, et al. A novel macromo lecular structure is a target of the promyelocyteretinoic acid receptor oncoprotein . Cell 1994; 76(2):333-343.
    • (1994) Cell , vol.76 , Issue.2 , pp. 333-343
    • Dyck, J.A.1    Maul, G.G.2    Miller Jr., W.H.3
  • 74
    • 0028293945 scopus 로고
    • The t(15;17) translocation alters a nuclear body in a retinoic acid-revers ible fashio n
    • Koken MH, Puvion-Dutilleul F, Guillemin MC, et al. The t(15;17) translocation alters a nuclear body in a retinoic acid-revers ible fashio n. EMBO J 1994; 13(5): I073-1083.
    • (1994) EMBO J , vol.13 , Issue.5
    • Koken, M.H.1    Puvion-Dutilleul, F.2    Guillemin, M.C.3
  • 75
    • 0028158682 scopus 로고
    • Retinoic acid regulates aberrant nuclear localization of PML-RAR alpha in acute promyelocytic leukemia cells
    • Weis K, Rambaud S, Lavau C, et al. Retinoic acid regulates aberrant nuclear localization of PML-RAR alpha in acute promyelocytic leukemia cells. Cell 1994; 76(2):345-356.
    • (1994) Cell , vol.76 , Issue.2 , pp. 345-356
    • Weis, K.1    Rambaud, S.2    Lavau, C.3
  • 76
    • 0027290450 scopus 로고
    • PML protein expression in hematopoietic and acute promyelocyt ic leukemia cells
    • Daniel MT, Koken M, Romag ne 0, et al. PML protein expression in hematopoietic and acute promyelocyt ic leukemia cells. Blood 1993; 82(6): 1858-1867.
    • (1993) Blood , vol.82 , Issue.6 , pp. 1858-1867
    • Daniel, M.T.1    Koken, M.2    Romagne, O.3
  • 77
    • 0023752982 scopus 로고
    • Use of all-tran s retinoic acid in the treatment of acute promyelocytic leukemia
    • Huang ME, Ye YC, Chen SR, et al. Use of all-tran s retinoic acid in the treatment of acute promyelocytic leukemia. Blood 1988; 72(2):567-572.
    • (1988) Blood , vol.72 , Issue.2 , pp. 567-572
    • Huang, M.E.1    Ye, Y.C.2    Chen, S.R.3
  • 78
    • 2942566483 scopus 로고    scopus 로고
    • Reduced intranuclear mobil ity of APL fusion proteins accompanies their mis localization and results in sequestration and decreased mobility of retinoid X receptor alpha
    • Dong S, Stenoien DL, Qiu J, et al. Reduced intranuclear mobil ity of APL fusion proteins accompanies their mis localization and results in sequestration and decreased mobility of retinoid X receptor alpha. Mol Cell BioI 2004; 24(10):4465-4475.
    • (2004) Mol Cell BioI , vol.24 , Issue.10 , pp. 4465-4475
    • Dong, S.1    Stenoien, D.L.2    Qiu, J.3
  • 79
    • 36248931601 scopus 로고    scopus 로고
    • Coiled-coi l domain of PML is essentia l for the aberrant dynamics of PML-RARalpha, resulting in sequestration and decreased mobility of SMRT
    • Huang Y, Qiu J, Chen G, et al. Coiled-coi l domain of PML is essentia l for the aberrant dynamics of PML-RARalpha, resulting in sequestration and decreased mobility of SMRT. Biochem Biophys Res Comm un 2008; 365(2) :258-265.
    • (2008) Biochem Biophys Res Commun , vol.365 , Issue.2 , pp. 258-265
    • Huang, Y.1    Qiu, J.2    Chen, G.3
  • 80
    • 33644821166 scopus 로고    scopus 로고
    • Interactions between DNA viruses, NDIO and the DNA damage response
    • Everett RD. Interactions between DNA viruses, NDIO and the DNA damage response. Cell Microbiol 2006; 8(3):365-374.
    • (2006) Cell Microbiol , vol.8 , Issue.3 , pp. 365-374
    • Everett, R.D.1
  • 81
    • 0029838230 scopus 로고    scopus 로고
    • The periphery of nuclear domain 10 (NDIO) as site of DNA virus deposition
    • lshov AM, Maul GG. The periphery of nuclear domain 10 (NDIO) as site ofDNA virus deposition. J Cell Bioi 1996; 134(4):815-826.
    • (1996) J Cell Bioi , vol.134 , Issue.4 , pp. 815-826
    • Lshov, A.M.1    Maul, G.G.2
  • 82
    • 0029862620 scopus 로고    scopus 로고
    • Nuclear domain 10 as preexisting potential replication start sites of herpes simplex virus type-I
    • Maul GG, Ishov AM, Everett RD. Nuclear domain 10 as preexisting potential replication start sites of herpes simplex virus type-I. Virology 1996; 217(1):67-75.
    • (1996) Virology , vol.217 , Issue.1 , pp. 67-75
    • Maul, G.G.1    Ishov, A.M.2    Everett, R.D.3
  • 83
    • 0029618165 scopus 로고
    • Chelb i-Alix MK, Pelicano L, Quignon F, et al
    • Chelb i-Alix MK, Pelicano L, Quignon F, et al. Induction of the PML protein by interferons in normal and API. cells. Leukemia 1995; 9 (12):2027-2033.
    • (1995) Leukemia , vol.9 , Issue.12 , pp. 2027-2033
  • 84
    • 0028979594 scopus 로고
    • The acute promyelocytic leukaemia-associated PML gene is induced by interferon
    • Lavau C, Marchio A, Fagioli Met al. The acute promyelocytic leukaemia-associated PML gene is induced by interferon. Oncogene 1995; 11(5):87 1-876 .
    • (1995) Oncogene , vol.11 , Issue.5 , pp. 871-876
    • Lavau, C.1    Marchio, A.2    Fagioli, M.3
  • 85
    • 0031907092 scopus 로고    scopus 로고
    • Resistance to virus infection conferred by the interferoninduced promyelocytic leukemia protein
    • Chelbi-Alix MK, Quignon F, Pelicano L, et al. Resistance to virus infection conferred by the interferoninduced promyelocytic leukemia protein. J Virol 1998; 72(2): I043-1051.
    • (1998) J Virol , vol.72 , Issue.2
    • Chelbi-Alix, M.K.1    Quignon, F.2    Pelicano, L.3
  • 86
    • 0029100611 scopus 로고
    • Targeti ng of adenovirus EIA and E4-0 RF3 proteins to nuclear matrix-associated PML bodies
    • Carvalho T, Seeler JS, Ohman K, et al. Targeti ng of adenovirus EIA and E4-0 RF3 proteins to nuclear matrix-assoc iated PML bodies. J Cell BioI 1995; 131(1):45-56.
    • (1995) J Cell BioI , vol.131 , Issue.1 , pp. 45-56
    • Carvalho, T.1    Seeler, J.S.2    Ohman, K.3
  • 87
    • 0030052130 scopus 로고    scopus 로고
    • Adenovirus replication is coupled with the dynamic properties of the PML nuclear structure
    • Doucas V, Ishov AM, Romo A, et al. Adenovirus replication is coupled with the dynamic properties of the PML nuclear structure. Genes Dev 1996; 10(2) :196-207.
    • (1996) Genes Dev , vol.10 , Issue.2 , pp. 196-207
    • Doucas, V.1    Ishov, A.M.2    Romo, A.3
  • 88
    • 33644768122 scopus 로고    scopus 로고
    • Lnteraction of the adenovirus type 5 E4 or O protein with promyelocytic leukemia protein isofonn II is required for ND 10 disruption
    • HoppeA, Beech SJ, DimmockJ, et al. lnteractionofthe adenovirus type 5 E4 OrO protein with promyelocytic leukemia protein isofonn II is required for ND 10 disruption. J Virol 2006; 80(6):3042-3049.
    • (2006) J Virol , vol.80 , Issue.6 , pp. 3042-3049
    • Hoppe, A.1    Beech, S.J.2    Dimmock, J.3
  • 89
    • 1542288934 scopus 로고    scopus 로고
    • The cytoplasmic body component TRIM5a lpha restricts HIV-I infection in Old World monkeys
    • Stremlau M, Owens CM, Perron MJ, et al. The cytoplasmic body compo nent TRIM5a lpha restricts HIV-I infection in Old World monkeys. Nature 2004; 427(6977):848-853.
    • (2004) Nature , vol.427 , Issue.6977 , pp. 848-853
    • Stremlau, M.1    Owens, C.M.2    Perron, M.J.3
  • 90
    • 21644450071 scopus 로고    scopus 로고
    • Human tripartite motif 5alpha domains responsib le for retrovi rus restriction activity and specificity
    • Perez-Caballero O, Hatziioannou T, Yang A, et al. Human tripartite motif 5alpha domains responsib le for retrovi rus restriction activity and specificity. J Viro12005 ; 79(14):8969-8978.
    • (2005) J Viro1 , vol.79 , Issue.14 , pp. 8969-8978
    • Perez-Caballero, O.1    Hatziioannou, T.2    Yang, A.3
  • 91
    • 34250319332 scopus 로고    scopus 로고
    • TRIM5 alpha cytop lasmic bodies are highly dynamic structures
    • Campbell EM, DoddingMP, YapMW, et al. TRIM5 alpha cytop lasmic bodies are highly dynamic structures. Mol Bioi Cell 2007 ; 18(6):2102-21 11.
    • (2007) Mol Bioi Cell , vol.18 , Issue.6 , pp. 2102-2111
    • Campbell, E.M.1    Dodding, M.P.2    Yap, M.W.3
  • 92
    • 3242726103 scopus 로고    scopus 로고
    • PML regulates p53 stability by sequestering Mdm2 to the nucleolus
    • Bernardi R, Scagl ioni PP, Bergmann S, et al. PML regulates p53 stability by sequestering Mdm2 to the nucleolus. Nat Cell BioI 2004; 6(7) :665-672 .
    • (2004) Nat Cell BioI , vol.6 , Issue.7 , pp. 665-672
    • Bernardi, R.1    Scaglioni, P.P.2    Bergmann, S.3
  • 93
    • 34249938802 scopus 로고    scopus 로고
    • PML protein assoc iation with spec ific nucleolar structures differs in normal, tumor and senescent human cells
    • Janderova-Rossmeislova L, NovakovaZ, Vlasa kova J, et al. PML protein assoc iation with spec ific nucleolar structures differs in normal, tumor and senescent human cells. J Struct BioI 2007; 159(1):56-70.
    • (2007) J Struct BioI , vol.159 , Issue.1 , pp. 56-70
    • Janderova-Rossmeislova, L.1    Novakova, Z.2    Vlasakova, J.3
  • 94
    • 2442704958 scopus 로고    scopus 로고
    • Cell cycle-dependent association of PML bodies with sites of active transcription in nuclei of mammal ian cells
    • Kiesslich A, von Mikecz A, Hemmerich P. Cell cycle-dependent associa tion ofPML bodies with sites of active trans cription in nucle i of mammal ian cells. J Struct BioI 2002;140(1-3):167-179.
    • (2002) J Struct BioI , vol.140 , Issue.1-3 , pp. 167-179
    • Kiesslich, A.1    Von Mikecz, A.2    Hemmerich, P.3
  • 95
    • 0032744386 scopus 로고    scopus 로고
    • A dynamic connection between centromeres and NOlO proteins
    • Everett RD, Earnshaw WC, Pluta AF, et al.A dynamic connection betwee n centromeres and NOlO proteins. J Cell Sci 1999; 112(Pt 20):3443-3454.
    • (1999) J Cell Sci , vol.112 , Issue.PART 20 , pp. 3443-3454
    • Everett, R.D.1    Earnshaw, W.C.2    Pluta, A.F.3
  • 96
    • 0030697342 scopus 로고    scopus 로고
    • Evidence for an alternative mechanism formaintaining telomere length in human tumors and tumor-derived cell lines
    • BryanTM, EnglezouA, Dalla-PozzaL, et al. Evidence for an alternative mechanism formaintaining telomere length in human tumors and tumor-derived cell lines. Nat Med 1997; 3(11) :1271-1274.
    • (1997) Nat Med , vol.3 , Issue.11 , pp. 1271-1274
    • Bryan, T.M.1    Englezou, A.2    Dalla-Pozza, L.3
  • 97
    • 0033672470 scopus 로고    scopus 로고
    • Telomere maintenance by recombin ation in human cells
    • Dunham MA, Neumann AA, Fasching CL, et al. Telomere maintenance by recombin ation in human cells. Nat Genet 2000; 26(4):447-450.
    • (2000) Nat Genet , vol.26 , Issue.4 , pp. 447-450
    • Dunham, M.A.1    Neumann, A.A.2    Fasching, C.L.3
  • 98
    • 0033199695 scopus 로고    scopus 로고
    • Telomerase-negative immortalized human cells contain a novel type of promyelocytic leukemia (PML) body
    • Yeager TR, Neumann AA, Englezou A, et al. Telomerase-negative immortalized human cells contain a novel type of promyelocytic leukemia (PML) body. Cancer Res 1999; 59(17):4175-4179.
    • (1999) Cancer Res , vol.59 , Issue.17 , pp. 4175-4179
    • Yeager, T.R.1    Neumann, A.A.2    Englezou, A.3
  • 99
    • 0034759620 scopus 로고    scopus 로고
    • PML bodies assoc iate specifically with the MHC gene cluster in interphase nuclei
    • Shiels C, Islam SA, Vatcheva R, et al. PML bodies assoc iate specifically with the MHC gene cluster in interphase nuclei . J Cell Sci 2001; 114(Pt 20):3705-3716.
    • (2001) J Cell Sci , vol.114 , Issue.PART 20 , pp. 3705-3716
    • Shiels, C.1    Islam, S.A.2    Vatcheva, R.3
  • 100
    • 1242329998 scopus 로고    scopus 로고
    • Promyelocytic leukemia nuclear bodies associate with transcriptionally activegeno mic regions
    • Wang J, Shiels C, Sasieni P, et al. Promyelocytic leukemia nuclear bodies assoc iate with transcriptionally active geno mic regio ns. J Cell Bioi 2004; 164(4):515-526.
    • (2004) J Cell Bioi , vol.164 , Issue.4 , pp. 515-526
    • Wang, J.1    Shiels, C.2    Sasieni, P.3
  • 101
    • 0030583287 scopus 로고    scopus 로고
    • A RING finger motif reg ulates transforming activity of the rfp/ret fusion gene
    • Hasegawa N, Iwashi ta T, Asai N, et al. A RING finger motif reg ulates transforming activity of the rfp/ret fusio n gene . Biochem Biophys Res Commun 1996; 225(2):627-63 1.
    • (1996) Biochem Biophys Res Commun , vol.225 , Issue.2 , pp. 627-631
    • Hasegawa, N.1    Iwashita, T.2    Asai, N.3
  • 102
    • 0033615042 scopus 로고    scopus 로고
    • The transcription coactivator IITIFI and a related protein are fused to the RET receptor tyrosi ne kinase in childhood papillary thyroid carcinomas
    • Klugbauer S, Rabes HM. The transcription coactivator IITIFI and a related protein are fused to the RET receptor tyrosi ne kinase in childhood papillary thyroid carcinomas. Oncogene 1999; 18(30) :4388-4393.
    • (1999) Oncogene , vol.18 , Issue.30 , pp. 4388-4393
    • Klugbauer, S.1    Rabes, H.M.2
  • 103
    • 0029030016 scopus 로고
    • The N-terminal part of Tl FI, A putative mediator of the ligand-dependent activation function (AF-2) of nuclear receptors, is fused to B-raf in the oncogenic protein T18
    • Le Douar in B, Zeche l C, Garn ier JM, et al. The N-terminal part of Tl FI, a putative mediator of the ligand-dependent activation function (AF-2) of nuclear receptors, is fused to B-raf in the oncogenic protein T18. EMBO J 1995; 14(9):2020-2033.
    • (1995) EMBO J , vol.14 , Issue.9 , pp. 2020-2033
    • Le Douarin, B.1    Zechel, C.2    Garnier, J.M.3
  • 104
    • 0032721510 scopus 로고    scopus 로고
    • A I{A-dependent tumo ur-growth suppressive transcription complex is the target oft he PML-raralpha and T18 oncoproteins
    • Zhong S, Delva L, Rachez C, et al. A I{A-depende nt, tumo ur-growth suppressiv e transcription complex is the target oft he PML-RARa lpha and T18 oncoproteins. Nat Genet 1999; 23(3):287-295 .
    • (1999) Nat Genet , vol.23 , Issue.3 , pp. 287-295
    • Zhong, S.1    Delva, L.2    Rachez, C.3
  • 105
    • 0035028618 scopus 로고    scopus 로고
    • Common properties of nuclear body protein SP IOO and TIFl alpha chromatin factor: Role of SUMO modification
    • Seeler JS, Marchio A, Losson R, et al. Common properties of nuclear body protein SP IOO and TIFlalpha chromatin factor: role ofSUMO modification. Mol Cell BioI 200 I ; 21(I 0):3314-3324.
    • (2001) Mol Cell BioI , vol.21 , Issue.10 , pp. 3314-3324
    • Seeler, J.S.1    Marchio, A.2    Losson, R.3
  • 106
    • 0029841744 scopus 로고    scopus 로고
    • A possible involvement of TlFI alpha and TIFI beta in the epigenetic control oftranscription by nuclear receptors
    • Le Douar in B, Nielsen AL, Garnier JM, et al. A possible involvement ofTlFI alpha and TIFI beta in the epigenetic control oftranscription by nuclear receptors . EMBO J 1996; 15(23):6701-6715.
    • (1996) EMBO J , vol.15 , Issue.23 , pp. 6701-6715
    • Le Douarin, B.1    Nielsen, A.L.2    Garnier, J.M.3
  • 107
    • 0036311183 scopus 로고    scopus 로고
    • Hetero-oligomerization among the TlF family of RBCC/TRIM domain-containing nuclearcofactors: A potentialmechanism forregulating the switch between coactivation and corepression
    • Peng H, Feldman I, Rauscher FJ 3rd. Hetero-oligomerization among the TlF family of RBCC/TRIM domain-containing nuclearcofactors: a potentialmechanism forregulating the switch between coactivation and corepression . J Mol BioI 2002; 320(3):629-644.
    • (2002) J Mol BioI , vol.320 , Issue.3 , pp. 629-644
    • Peng, H.1    Feldman, I.2    Rauscher III, F.J.3
  • 108
    • 34247147729 scopus 로고    scopus 로고
    • The adenovirus E4ORF3 protein binds and reorganizes the TRIM family member transcriptional intermediary factor i alpha
    • Yondola MA, Hearing P.The adenovi rus E4ORF3 protein binds and reorganizes theTRIM family member transcriptional intermediary factor I alpha. J Viro12007; 81(8):4264-4271.
    • (2007) J Viros , vol.81 , Issue.8 , pp. 4264-4271
    • Yondola, M.A.1    Hearing, P.2
  • 109
    • 0025275906 scopus 로고
    • Nuclear localization of antigens detected by a monoclonal antibody against a synthetic peptide of Rfp finger protein
    • Kikuchi T, Taka hashi M, Ueda Ret al. Nuclear localization of antigens detected by a monoclonal antibody agai nst a synthetic peptide of rfp finger protein. Hybridoma 1990; 9(2): 189-200.
    • (1990) Hybridoma , vol.9 , Issue.2 , pp. 189-200
    • Kikuchi, T.1    Takahashi, M.2    Ueda, R.3
  • 110
    • 0032755433 scopus 로고    scopus 로고
    • Different nuclear/cy toplasmic distributions of RET finger protein in different cell types
    • Tezel G, Nagasaka T, Iwahas hi N, et al. Different nuclear/cy toplasmic distributions of RET finger protein in different cell types. Patholl nt 1999; 49(10):881-886.
    • (1999) Pathollnt , vol.49 , Issue.10 , pp. 881-886
    • Tezel, G.1    Nagasaka, T.2    Iwahashi, N.3
  • 111
    • 0034671552 scopus 로고    scopus 로고
    • RET finger protein is a transcriptional repressor and interacts withenhancer ofpolycomb that has dual transcriptional functions
    • Shimono Y, Murakami II, Hasegawa Y, et al. RET finger protein is a transcriptional repressor and interacts withenhancer ofpolycomb that has dual transcriptiona l functions. J BioIChem2000;275(50):39411-39419.
    • (2000) J BioIChem , vol.275 , Issue.50 , pp. 39411-39419
    • Shimono, Y.1    Murakami, I.I.2    Hasegawa, Y.3
  • 112
    • 22144482659 scopus 로고    scopus 로고
    • PIAS proteins are involved in the SUMO-I modification, intracellular trans locat ion and transcriptional repressive activity of RET finger protein
    • Matsuura T, Shimono Y, Kawai K, et al. PIAS proteins are involved in the SUMO-I modification, intracellular trans locat ion and transcriptional repressive activity of RET finger protein. Exp Cell Res 2005; 308 (1):65-77.
    • (2005) Exp Cell Res , vol.308 , Issue.1 , pp. 65-77
    • Matsuura, T.1    Shimono, Y.2    Kawai, K.3
  • 113
    • 0035930616 scopus 로고    scopus 로고
    • Intracellular localizatio n of the ret finger protein depends on a functional nuclear export signal and protein kinase C activation
    • Harbe rs M, Nomura T, Ohno S, et al. Intracellul ar localizatio n of the Ret finger protein depends on a functional nuclear export signal and protein kinaseC activation. J BioiChern200 I; 276(51):48596 -48607 .
    • (2001) J BioiChern , vol.276 , Issue.51 , pp. 48596-48607
    • Harbers, M.1    Nomura, T.2    Ohno, S.3
  • 114
    • 0346100493 scopus 로고    scopus 로고
    • PIASSUMO: New partners in transcriptional regulation
    • Schmidt 0, Muller S. PIAS/SUMO: new partners in transc riptional regulation. Cell Mol Life Sci 2003 ; 60 (12):256 1-2574.
    • (2003) Cell Mol Life Sci , vol.60 , Issue.12 , pp. 2561-2574
    • Schmidt, O.1    Muller, S.2
  • 115
    • 0030751654 scopus 로고    scopus 로고
    • Lnvolvement of the rfp tripartite motif in protein-protein interactions and subcellular distribution
    • Cao T, Borden KL, Freemo nt PS, et al. lnvolvement of the rfp tripartite motif in protein-protein interactio ns and subce llular distribu tion. J Cell Sci 1997; 110(Pt 14):1563-1571.
    • (1997) J Cell Sci , vol.110 , Issue.PART 14 , pp. 1563-1571
    • Cao, T.1    Borden, K.L.2    Freemont, P.S.3
  • 116
    • 0031800796 scopus 로고    scopus 로고
    • Ret finger protein is a normal component ofPML nuclear bodies and interacts directly with PML
    • Cao T, Duprez E, Borden KL, et al. Ret finger protein is a normal component ofPML nuclear bodies and interacts directly with PML. J Cell Sci 1998; 111(Pt 10):1319-1329.
    • (1998) J Cell Sci , vol.111 , Issue.PART 10 , pp. 1319-1329
    • Cao, T.1    Duprez, E.2    Borden, K.L.3
  • 117
    • 0042858174 scopus 로고    scopus 로고
    • The Ret finger protein induces apoptosis via its RING finger-B box-coiled-coil motif
    • Dho SH, Kwon KS. The Ret finger protein induces apoptosis via its RING finger-B box-coiled-coil motif. J Bioi Chern 2003; 278(34):31902-3 1908.
    • (2003) J Bioi Chern , vol.278 , Issue.34 , pp. 31902-31908
    • Dho, S.H.1    Kwon, K.S.2
  • 118
    • 0032755283 scopus 로고    scopus 로고
    • Interaction between the Ret finger protein and the Int-6 gene product and colocalisation into nuclear bodies
    • Morr is-Des bois C, Bochard V, Reynaud C, et al. Interaction between the Ret finger protein and the Int-6 gene product and colocalisation into nuclear bod ies. J Cell Sci 1999; I 12(Pt 19):3331-3342.
    • (1999) J Cell Sci , vol.12 , Issue.PART 19 , pp. 3331-3342
    • Morris-Des Bois, C.1    Bochard, V.2    Reynaud, C.3
  • 119
    • 0034830955 scopus 로고    scopus 로고
    • A novel member ofthe RBCC family, Trif, expresse d specifically in the spermatids of mouse testis
    • Shyu HW, Hsu SH, Hsieh-L i HM, et al. A novel member ofthe RBCC family, Trif, expresse d specifically in the spermatids of mouse testis. Mech Dev 200 I; I08 (1-2) :2 13-2 16.
    • (2001) Mech Dev , vol.108 , Issue.1-2 , pp. 213-216
    • Shyu, H.W.1    Hsu, S.H.2    Hsieh-Li, H.M.3
  • 120
    • 0041703139 scopus 로고    scopus 로고
    • Forced expression of RNF36 induces cell apoptosis
    • Shyu HW, Hsu SH, Hsieh-L i HM, et al. Forced expression of RNF36 induces cell apoptosis. Exp Cell Res 2003; 287(2):30 1-313 .
    • (2003) Exp Cell Res , vol.287 , Issue.2 , pp. 301-313
    • Shyu, H.W.1    Hsu, S.H.2    Hsieh-Li, H.M.3
  • 121
    • 30944452960 scopus 로고    scopus 로고
    • The PHD finger, a nuclear protein-interaction domain
    • Bienz M. The PHD finger, a nucle ar protein-interactio n domain. Trends Biochem Sci 2006; 3 1(I) :35-40.
    • (2006) Trends Biochem Sci , vol.31 , Issue.1 , pp. 35-40
    • Bienz, M.1
  • 122
    • 33646842883 scopus 로고    scopus 로고
    • Subclassification of the RBCCIT RIM superfami ly reveals a nove l motif necessary for microtubule binding
    • Short KM, Cox TC. Subclassification of the RBCCIT RIM superfami ly reveals a nove l motif necessary for microtubule binding. J Bioi Chern 2006; 28 1(13):8970-8980.
    • (2006) J Bioi Chern , vol.281 , Issue.13 , pp. 8970-8980
    • Short, K.M.1    Cox, T.C.2
  • 123
    • 28244438788 scopus 로고    scopus 로고
    • Relationship between SPRY and 1330.2 protein domains. Evolution of a component of immune defence?
    • Rhodes DA, dc Bono 13, Trowsdale J. Relationship between SPRY and 1330.2 protein domains. Evo lution ofa component of immune de fence? Immu nology 2005; 116(4):41 1-41 7.
    • (2005) ImmuNology , vol.116 , Issue.4 , pp. 411-417
    • Rhodes, D.A.1    Dcbono, B.2    Trowsdale, J.3
  • 124
    • 0033918327 scopus 로고    scopus 로고
    • Gene encoding a new RlNG-13-box-Coiled-coil protein is mutated in mulibrey nanism
    • Avela K, Lipsane n-Nyman M, Idan heimo N, et al. Gene encoding a new RlNG-13-box-Coiled-coil protein is mutated in mulibrey nanism. Nat Genet 2000; 25(3):298-301.
    • (2000) Nat Genet , vol.25 , Issue.3 , pp. 298-301
    • Avela, K.1    Lipsanen-Nyman, M.2    Idanheimo, N.3
  • 125
    • 0036235857 scopus 로고    scopus 로고
    • The TRIM37 ge ne encodes a pero xi somal RING-B-box-coi led-coi l protein : Classification of mulibreynanism as a new peroxisomal disorder
    • Kall ijarvi J, Avela K, Lipsanen-Nyman M, et al. The TRIM37 ge ne encodes a pero xi somal RING-B-box-coi led-coi l protein : classification ofmulibrey nanism as a new peroxisomal diso rder. Am J Hum Genet 2002 ; 70(5) :1215 -1228.
    • (2002) Am J Hum Genet , vol.70 , Issue.5 , pp. 1215-1228
    • Kallijarvi, J.1    Avela, K.2    Lipsanen-Nyman, M.3
  • 126
    • 22144464391 scopus 로고    scopus 로고
    • TRIM37 defective in mulibrey nanism is a novel RING finger ubiquitin E3 ligase
    • Kallijarvi J, Lahtinen U, Hamalainen Ret al. TRIM37 defective in mulibrey nanism is a novel RING finger ubiquitin E3 ligase . Exp Cc ll Rcs 2005 ; 308(1) :146-155.
    • (2005) Exp Cc Ll Rcs , vol.308 , Issue.1 , pp. 146-155
    • Kallijarvi, J.1    Lahtinen, U.2    Hamalainen, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.