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Volumn 770, Issue , 2012, Pages 59-76

TRIM involvement in transcriptional regulation

Author keywords

[No Author keywords available]

Indexed keywords

CELL NUCLEUS RECEPTOR; KRUPPEL ASSOCIATED BOX ZINC FINGER PROTEIN; PROMYELOCYTIC LEUKEMIA PROTEIN; REGULATOR PROTEIN; REPRESSOR PROTEIN; RET FINGER PROTEIN; SMAD PROTEIN; TRANSCRIPTION FACTOR; TRANSCRIPTION INTERMEDIARY FACTOR 1; TRANSCRIPTION INTERMEDIARY FACTOR 1ALPHA; TRANSCRIPTION INTERMEDIARY FACTOR 1BETA; TRANSCRIPTION INTERMEDIARY FACTOR 1GAMMA; TRIPARTITE MOTIF PROTEIN; UNCLASSIFIED DRUG; ZINC FINGER PROTEIN; PROTEIN;

EID: 84878950821     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4614-5398-7_5     Document Type: Article
Times cited : (20)

References (106)
  • 1
    • 33847070442 scopus 로고    scopus 로고
    • The role of chromatin during transcription
    • I. Li 13, Carey M, Workman JL. The role of chromatin during transcription. Cell 2007; 128:707-719.
    • (2007) Cell , vol.128 , pp. 707-719
    • Li, B.1    Carey, M.2    Workman, J.L.3
  • 2
    • 34249299791 scopus 로고    scopus 로고
    • The comple x language ofchrom atin regulation during transcription
    • Berger SL. The comple x language ofchrom atin regulation during transcription. Nature 200 7; 447:40 7-412.
    • (2007) Nature , vol.447 , pp. 407-412
    • Berger, S.L.1
  • 3
    • 0035012858 scopus 로고    scopus 로고
    • Bonus, a Drosophil a homolog of TlFI proteins, interacts with nuclear receptors and can inhibit FTZ -F i -dependent transcription
    • Beckstead R,Ortiz JA, Sanchez C, et al. Bonus, a Drosophil a homolog ofTlFI proteins, interact s with nuclear receptors and can inhibit FTZ -F I -de pe n d e nt transcription. Mol Cell 2001; 7:753-765.
    • (2001) Mol Cell , vol.7 , pp. 753-765
    • Beckstead, R.1    Ortiz, J.A.2    Sanchez, C.3
  • 4
    • 33847343312 scopus 로고    scopus 로고
    • PI-IA-4/FoxA cooperates withTAM-I/TRIMto regulate cell fate restriction in the C. Elegans foregut
    • Kiefer JC, Smith PA, Mango SE. PI-IA-4/FoxA cooperates withTAM-I/TRIMto regulate cell fate restriction in the C. elegans foregut. Dev BioI 2007; 303:611-624.
    • (2007) Dev BioI , vol.303 , pp. 611-624
    • Kiefer, J.C.1    Smith, P.A.2    Mango, S.E.3
  • 5
    • 0029030016 scopus 로고
    • The N-tcrm inal part of Tl FI, a putativ e mediator of the ligand-dependent activation function (AF-2) of nuclear receptors, is fused to B-raf in the oncogenic protein T 18
    • Lc Douarin 13, Zec hcl C, Garnier JM et al. The N-tcrm inal part of Tl FI, a putativ e mediator of the ligand-dependent activation function (AF-2) of nuclear receptors, is fused to B-raf in the oncogenic protein T 18. EM130 J 1995; 14:2020-2033.
    • (1995) EM130 J , vol.14 , pp. 2020-2033
    • Lcdouarin, B.1    Zechcl, C.2    Garnier, J.M.3
  • 6
    • 0029858585 scopus 로고    scopus 로고
    • KAP-I, a novel corepressor for the highly conserved KRAB repression domain
    • Friedman JR, Fredericks WJ, Jensen DE, et al. 1. KAP-I, a novel corepressor for the highly conserved KRAB repression domain. Genes Dev 1996; 10:2067-2078.
    • (1996) Genes Dev , Issue.10 , pp. 2067-2078
    • Friedman, J.R.1    Fredericks, W.J.2    Jensen, D.E.3
  • 7
    • 0034186133 scopus 로고    scopus 로고
    • The transcriptional control of PML and the nuclear body
    • Zhong S, Salomoni L, Pandolfi PI'. The transcriptional control of PML and the nuclear body. Nat Cell BioI 2000; 2:85-89.
    • (2000) Nat Cell BioI , vol.2 , pp. 85-89
    • Zhong, S.1    Salomoni, L.2    Pandolfi, P.L.3
  • 8
    • 0029841744 scopus 로고    scopus 로고
    • A possible involvement of Tl Fl a and Tl FI in the epigenetic control oftranscription by nuclear receptors
    • Le Douarin B, Nielsen AL, Garni er JM, et al. A possible involvement of Tl Fl a and Tl FI in the epigenetic control oftranscription by nuclear receptors. EMBO J 1996; 15:6701-6715.
    • (1996) EMBO J , vol.15 , pp. 6701-6715
    • Le Douarin, B.1    Nielsen, A.L.2    Garnier, J.M.3
  • 9
    • 0033571206 scopus 로고    scopus 로고
    • Interaction with members of the heterochromatin protein i (HPI) family and histone deacetylation are differentially involved in transcriptional silencing by members ofthe TIF i family
    • Nielsen AL, Ortiz JA, You Jet al. Interac tion with members of the heterochromatin protein I (HPI) family and histone deacetylation are differentially involved in transcriptional silencing by members ofthe TIF I family. EMBO J 1999; 18:6385-6395 .
    • (1999) EMBO J , vol.18 , pp. 6385-6395
    • Nielsen, A.L.1    Ortiz, J.A.2    You, J.3
  • 10
    • 0035118229 scopus 로고    scopus 로고
    • Targeting histone deacetylase complexes via KRA13-zinc finger proteins: The PHD and bromodomains of KAP-I form a cooperative unit that recruits a novel isoform of the Mi-2alph a subunit of NuRD
    • Schultz DC, Friedman JR, Rauscher III FJ. Targeting histone deacetylase complexes via KRA13-zinc finger proteins: the PHD and bromodomains ofKAP-I form a cooperative unit that recru its a novel isoform of the Mi-2alph a subunit ofNuRD. Genes Dev 200 I; 15:428-443
    • (2001) Genes Dev , vol.15 , pp. 428-443
    • Schultz, D.C.1    Friedman, J.R.2    Rauscher III, F.J.3
  • 11
    • 0037089626 scopus 로고    scopus 로고
    • SETDBI: A novel KAP-I-associated histone H3, lysine 9-spec ific mcthyltransferasc that contributes to HPI-mediatcd silencing of euchroma tic genes by KRA13 zinc-finger proteins
    • Schultz DC, Ayya nathan K, Negorev D, et al. SETDBI: a novel KAP-I-associated histone H3, lysine 9-spec ific mcthyltransferasc that contributes to HPI-mediatcd silencing of euchroma tic genes by KRA13 zinc-finger proteins. Genes Dev 2002; 16:919-932.
    • (2002) Genes Dev , vol.16 , pp. 919-932
    • Schultz, D.C.1    Ayya Nathan, K.2    Negorev, D.3
  • 12
    • 9144223085 scopus 로고    scopus 로고
    • TlFI0, a novel lIP I-interacting member ofthe transcriptio nal intermediary factor i (TIFI) family expressed by elongating spermatids
    • Khetchoumian K, Teletin M, Mark M, et al. TlFI0, a novel lIP I-interacting member ofthe transcriptio nal intermediary factor I (TIFI) family expressed by elongating spermatids. J BioI Chern 2004; 279: 48329-48341.
    • (2004) J BioI Chern , vol.279 , pp. 48329-48341
    • Khetchoumian, K.1    Teletin, M.2    Mark, M.3
  • 13
    • 0035099686 scopus 로고    scopus 로고
    • The growth suppressor pml represses transcript ion by functionally and physically interacting with histone deacetylases
    • Wu WS, Vallian S, Seto E, et al. The growth suppressor pml represses transcript ion by functionally and physically interacting with histone deacetylases. Mol Cell Bioi 200 I ; 21:2259-2268.
    • (2001) Mol Cell Biol , vol.21 , pp. 2259-2268
    • Wu, W.S.1    Vallian, S.2    Seto, E.3
  • 14
    • 0034671552 scopus 로고    scopus 로고
    • RET finger protein is a transcr iptional repressor and interacts with enhancer ofpolycomb that has dual tran scriptional functions
    • Shimono Y, Murakami H, Hasegawa Y, et al. RET finger protein is a transcr iptional repressor and interacts with enhancer ofpolycomb that has dual tran scriptional functions. J BioIChern 2000 ; 275:394 11-394 19.
    • (2000) J BioIChern , vol.275 , pp. 39411-39419
    • Shimono, Y.1    Murakami, H.2    Hasegawa, Y.3
  • 15
    • 3142600897 scopus 로고    scopus 로고
    • Molecular cloning, genomic structure and expression analys is of the mouse transcriptional intermedi ary factor i gamma gene
    • Yan K, Dolle L, Mark M, et al. Molecular cloning, genomic structure and expression analys is of the mouse transcriptional intermedi ary factor I gamma gene. Gene 2004; 334:3-13.
    • (2004) Gene , vol.334 , pp. 3-13
    • Yan, K.1    Dolle, L.2    Mark, M.3
  • 16
    • 0033521759 scopus 로고    scopus 로고
    • TIFly, a novel member of the transcriptional intermediary factor i family
    • Ventur ini L, You J, Stadler M, et al. TIF ly, a novel member of the transcriptional intermediary factor I family. Oncogene 1999; 18:1209-121 7.
    • (1999) Oncogene , vol.18 , pp. 1209-1217
    • Venturini, L.1    You, J.2    Stadler, M.3
  • 17
    • 0033615042 scopus 로고    scopus 로고
    • The transcription coactivator HTIFI and a related protein are fused to the RET receptor tyrosine kinase in childhood papillary thyroid carcinomas
    • Klugbauer S, Rabes HM. The transcription coactivator HTIFI and a related protein are fused to the RET receptor tyrosine kinase in childhood papillary thyroid carcinomas. Oncogene 1999; 18:4388-4 393.
    • (1999) Oncogene , vol.18 , pp. 4388-4393
    • Klugbauer, S.1    Rabes, H.M.2
  • 18
    • 36549086517 scopus 로고    scopus 로고
    • Loss of Trim24 (Tifl a) gene function confers oncogenic activity to retinoic acid receptor alpha
    • Khetchoumian K, Teletin M, Tisserand J, et al. Loss of Trim24 (Tifl a) gene function confers oncogenic activity to retinoic acid receptor alpha . Nat Genet 2007; 39:1500-1506.
    • (2007) Nat Genet , vol.39 , pp. 1500-1506
    • Khetchoumian, K.1    Teletin, M.2    Tisserand, J.3
  • 19
    • 40649125047 scopus 로고    scopus 로고
    • Arteria l calci fications and increased expression of vitamin D receptor targets in mice lacking T1Fla
    • Ignat M, Teletin M, Tisserand Jet al. Arteria l calci fications and increased expression of vitamin D receptor targets in mice lacking T1Fl a . Proc Nat! Acad Sci USA 2008; 105:2598-2603.
    • (2008) Proc Nat! Acad Sci USA , vol.105 , pp. 2598-2603
    • Ignat, M.1    Teletin, M.2    Tisserand, J.3
  • 20
    • 0033915781 scopus 로고    scopus 로고
    • Mice lacking the transcriptional corcprcssor Tlf' Ip are defective in early postimplantation development
    • Cammas F, Mark M, Dolle I', et al. Mice lacking the transcriptional corcprcssor Tlf' Ip are defective in early postimplantation development. Development 2000; 127:2955-2963.
    • (2000) Development , vol.127 , pp. 2955-2963
    • Cammas, F.1    Mark, M.2    Dolle, I.'.3
  • 21
    • 0036340070 scopus 로고    scopus 로고
    • Weber L, Cammas F, Gerard C, et al
    • Weber L, Cammas F, Gerard C, et al. Germ cell expression of the transcriptional corepressor Tl FI is required for the maintenance of spermatogenesis in the mouse. Development 2002 ; 129:2329-2337.
    • (2002) Development , vol.129 , pp. 2329-2337
  • 22
    • 33646876973 scopus 로고    scopus 로고
    • Hematopoiesis controlled by dist inct TIFly and Smad4 branches ofthe TGF pathway
    • He W, Dorn DC, Erdj ument -Bromage H, et al. Hematopoiesis controlled by dist inct TIFly and Smad4 branches ofthe TGF pathway. Cell 2006; 125:929-941.
    • (2006) Cell , vol.125 , pp. 929-941
    • He, W.1    Dorn, D.C.2    Erdjument-Bromage, H.3
  • 23
    • 17044365440 scopus 로고    scopus 로고
    • Germ-layer specification and control of cell growth by Ectodermin, a Smad4 ubiquitin ligase
    • Dupont S, Zacchigna L, Cordenonsi M, et al. Germ-layer specification and control of cell growth by Ectodermin, a Smad4 ubiquitin ligase. Cell 2005; 121:87-99.
    • (2005) Cell , vol.121 , pp. 87-99
    • Dupont, S.1    Zacchigna, L.2    Cordenonsi, M.3
  • 24
    • 19344371219 scopus 로고    scopus 로고
    • The zebrafish moonshine gene encode s transcriptional intermed iary factor i gamma, an essential regulator of hematopoiesis
    • Ransom DG, Bahary N, Niss K, et al. The zebrafish moonshine gene encode s transcriptional intermed iary factor I gamma, an essential regulator of hematopoiesis. PLoS Bioi 2004; 2:E237.
    • (2004) PLoS Bioi , vol.2
    • Ransom, D.G.1    Bahary, N.2    Niss, K.3
  • 25
    • 0034602922 scopus 로고    scopus 로고
    • Reconstitution of the KRAB-KAPI repressor complex: A model system for defining the molecular anatomy of RING-B box-coiled-coil domain-mediated protein-protein interact ions
    • Peng H, Begg GE, Schultz DC, et al. Reconstitution of the KRAB-KAPI repressor comple x: a model system for defining the molecular anatomy of RING-B box-coiled-coil domain-mediated protein-protein interact ions. J Mol BioI 2000 ; 295:1139-11 62.
    • (2000) J Mol BioI , vol.295 , pp. 1139-1162
    • Peng, H.1    Begg, G.E.2    Schultz, D.C.3
  • 26
    • 0036311183 scopus 로고    scopus 로고
    • Hctero-oligomerization among the T1F family of R13CC/TRIM domain-containing nuclearc ofactors: A potential mechanism for regulating the switch between coactivation and corepression
    • Peng 1-1, Feldman I, Rauscher FJ 3rd. Hctero-oligomerization among the T1F family of R13CC/TRIM domain-containing nuclearc ofactors: a potential mechanism for regulating the switch between coactivation and corepress ion. J Mol BioI 2002; 320:629-644.
    • (2002) J Mol BioI , vol.320 , pp. 629-644
    • Peng, I.-I.1    Feldman, I.2    Rauscher III, F.J.3
  • 27
    • 33745713437 scopus 로고    scopus 로고
    • It takes a PHD to read the histone code
    • Mellor J. It takes a PHD to read the histone code. Cell 2006; 126:22-24.
    • (2006) Cell , vol.126 , pp. 22-24
    • Mellor, J.1
  • 28
    • 34547858913 scopus 로고    scopus 로고
    • Structure and acety l-lysine recog nition of the bromodomain
    • Mujtaba S, Zeng L, Zhou MM. Structure and acety l-lysine recog nition of the bromodomain. Oncogene 2007; 26:5521-5527.
    • (2007) Oncogene , vol.26 , pp. 5521-5527
    • Mujtaba, S.1    Zeng, L.2    Zhou, M.M.3
  • 29
    • 0032568663 scopus 로고    scopus 로고
    • The putative cofactor TIFIa is a protein kinase that is hyperp hosphorylated upon interaction with liganded nuclear receptors
    • Fraser RA, Heard OJ, Adam Se tal. The putative cofactor TIFIa is a protein kinase that is hyperp hosphorylated upon interaction with liganded nuclear receptors. J Bioi Chern 1998; 27:16199-16204.
    • (1998) J Bioi Chern , vol.27 , pp. 16199-16204
    • Fraser, R.A.1    Heard, O.J.2    Adam, S.3
  • 30
    • 0034704078 scopus 로고    scopus 로고
    • A novel nuclear receptor corepressor complex, N-CoR, contains components of the mammalian SWIISNF complex and the corepressor KAP-1
    • Underh ill C, Qutob MS, Yee SP, et al. A nove l nuclear receptor corepressor complex, N-CoR, conta ins components of the mammalian SWIISNF complex and the corepressor KAP-1. J Bioi Chem 2000 ; 275:40463 -40470.
    • (2000) J Bioi Chem , vol.275 , pp. 40463-40470
    • Underhill, C.1    Qutob, M.S.2    Yee, S.P.3
  • 31
    • 33644850958 scopus 로고    scopus 로고
    • Heterochromatin protein 1: Don't j udge the book by its cover!
    • Hediger F, Gasser SM. Heterochromatin protein 1: don't j udge the book by its cover ! Curr Opin Genet Dev 2006; 16:143-150.
    • (2006) Curr Opin Genet Dev , vol.16 , pp. 143-150
    • Hediger, F.1    Gasser, S.M.2
  • 32
    • 55249118199 scopus 로고    scopus 로고
    • The heterochromatin protein 1 (HP1) family: Put away a bias toward HPI
    • Kwon SH, Workman JL. The heterochromatin protein 1 (HP1) family: put away a bias toward HPI. Mol Cells 2008; 26:217-227.
    • (2008) Mol Cells , vol.26 , pp. 217-227
    • Kwon, S.H.1    Workman, J.L.2
  • 33
    • 0033013868 scopus 로고    scopus 로고
    • KAP-1 corepressor protein interacts and colocalizes with heterochromatic and euchromatic HPI proteins: A potential role for Kriippel-associated box-zinc finger proteins in heterochromatin-mediated gene silencing
    • Ryan RF, Schultz DC, Ayya nathan K, et al. KAP-1 corepressor protein interacts and colocalizes with heterochromatic and euchromatic HPI proteins: a potential role for Kriippel-associated box-zinc finger proteins in heterochromatin-mediated gene silencing. Mol Cell Bioi 1999; 19:4366-4378 .
    • (1999) Mol Cell Bioi , vol.19 , pp. 4366-4378
    • Ryan, R.F.1    Schultz, D.C.2    Ayyanathan, K.3
  • 34
    • 0012473279 scopus 로고
    • The nuclear receptor superfamily: The second decade
    • Mange lsdorf OJ, Thummel C, Beato M, et al. The nuclear receptor superfamily: the second decade. Cell 1995; 83:835 -839 .
    • (1995) Cell , vol.83 , pp. 835-839
    • Mangelsdorf, O.J.1    Thummel, C.2    Beato, M.3
  • 35
    • 34548252291 scopus 로고    scopus 로고
    • Nuclear receptor coregulators: Judges, juries and executioners of cellular regulation
    • Lonard OM, O'Malley BW. Nuclear receptor coregu lators : j udges, ju ries and exec utioners of cellular regulation. Mol Cell 2007; 27:691-700 .
    • (2007) Mol Cell , vol.27 , pp. 691-700
    • Lonard, O.M.1    O'Malley, B.W.2
  • 36
    • 0032721510 scopus 로고    scopus 로고
    • A RA-depe ndent, tumour-growth suppressive transcription complex is the target of the PML-RARalpha and T18 oncoprot eins
    • Zhong S, Delva L, Rachez C, et al. A RA-depe ndent, tumour-growth suppressive transcription complex is the target of the PML-RARalpha and T18 oncoprot eins . Nat Genet 1999; 23:287-295.
    • (1999) Nat Genet , vol.23 , pp. 287-295
    • Zhong, S.1    Delva, L.2    Rachez, C.3
  • 37
    • 33744472469 scopus 로고    scopus 로고
    • Transcriptional intermediary factor Ia mediates physical interaction and functional synergy between the coactivator-associated arginine methyltransferase 1 and glucocorticoid receptor-interacting protein i nuclear receptor coactivators
    • Teyssier C, Ou CY, Khetchoumian K, et al. Transcriptional intermediary factor I a mediates physical interaction and functio nal synergy between the coactivator-associated arginine methyltransferase 1 and glucocorticoid receptor-interacting protein I nuclear receptor coactivators . Mol Endocrinol 2006; 20:1276-1286.
    • (2006) Mol Endocrinol , vol.20 , pp. 1276-1286
    • Teyssier, C.1    Ou, C.Y.2    Khetchoumian, K.3
  • 38
    • 57349132931 scopus 로고    scopus 로고
    • Trim24 (Tiff A): An EssentiaL 'brake ' forretinoic acid-induced transcription to prevent liver cancer
    • Khetchoumian K, Teletin M, Tisserand J, et al. Trim24 (Tiff a): an essen tia l 'b rake ' forretinoic acid-induced transcri ption to prevent liver cancer. Cell Cycle 2008; 7:3647-365 2.
    • (2008) Cell Cycle , vol.7 , pp. 3647-3652
    • Khetchoumian, K.1    Teletin, M.2    Tisserand, J.3
  • 39
    • 33745179207 scopus 로고    scopus 로고
    • A comprehensive catalog of human KRAB-assoc iated zinc finger genes: Insights into the evolutionary history of a large family oftranscriptional repressors
    • Iluntley S, Baggott OM, Hamilton AT, et al. A comprehe nsive catalog of human KRAB-assoc iated zinc finger genes: insights into the evolutionary history ofa large family oftrans criptional repressors. Genome Res 2006; 1:669-677.
    • (2006) Genome Res , vol.1 , pp. 669-677
    • Iluntley, S.1    Baggott, O.M.2    Hamilton, A.T.3
  • 40
    • 0035852733 scopus 로고    scopus 로고
    • Conserved interaction between distinct Kriippel-associated box domains and the transcriptional intermed iary factor i 13
    • Abrink M, Ortiz JA, Mark C, et al. Conserved interaction between distinct Kriippel-associated box domains and the transcriptional intermed iary factor I 13. Proc Natl Acad Sci USA 2001; 98: 1422-1426.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 1422-1426
    • Abrink, M.1    Ortiz, J.A.2    Mark, C.3
  • 41
    • 36749009119 scopus 로고    scopus 로고
    • PHD domain-mediated E3 ligase activity directs intramol ecular sumoylation of an adjacent bromodomain required for gene silencing
    • Ivanov AV, Peng H, Yurchenko V, et al. PHD domain-mediated E3 ligase activity directs intramol ecular sumoylation of an adjacent bromodomain required for gene silencing. Mol Cell 2007; 28:823 -837 .
    • (2007) Mol Cell , vol.28 , pp. 823-837
    • Ivanov, A.V.1    Peng, H.2    Yurchenko, V.3
  • 42
    • 0041624239 scopus 로고    scopus 로고
    • Regulated recruitm ent of HP1 to a euchromatic gene induces mitotically heritable, epigenetic gene silencing: A mammalian cell culture model of gene variegation
    • Ayyanathan K, Lechner MS, Bell P, et al. Regulated recruitm ent of HP1 to a euchromatic gene induces mitotically heritable, epigenetic gene silencing: a mammalian cell culture model of gene variegation. Genes Dev 2003; 17:1855-1869.
    • (2003) Genes Dev , vol.17 , pp. 1855-1869
    • Ayyanathan, K.1    Lechner, M.S.2    Bell, P.3
  • 43
    • 33751007001 scopus 로고    scopus 로고
    • The KAPI corepressor functions to coordinate the assembly ofde novo HPI-demarcated microenvironments ofheterochromatin required for KRAB zinc finger protein-mediated transcriptional repression
    • Sripathy SP, Stevens J, Schultz DC. The KAPI corepressor functions to coordinate the assembly ofde novo HPI-demarcated microenvironments ofheterochromatin required for KRAB zinc finger protein-mediated transcriptional repression. Mol Cell Bioi 2006; 26:8623 -8638 .
    • (2006) Mol Cell Bioi , vol.26 , pp. 8623-8638
    • Sripathy, S.P.1    Stevens, J.2    Schultz, D.C.3
  • 44
    • 63049088211 scopus 로고    scopus 로고
    • Disruption ofthe interaction between transcri ptional intermediary factor i 13 and heterochromatin protein i leads to a switch from DNA hyper-to hypomethylation and H3K9 to H3K27 trimethylation on the MEST promoter correlating with gene reactivation
    • Riclet R, Chendeb M, Vonesch JL, et al. Disruption ofthe interaction between transcri ptional intermediary factor I 13 and heterochromatin protein I leads to a switch from DNA hyper-to hypomethylation and H3K9 to H3K27 trimethylation on the MEST promoter correlating with gene reactivation. Mol Bioi Cell 2009; 20:296-305.
    • (2009) Mol Bioi Cell , vol.20 , pp. 296-305
    • Riclet, R.1    Chendeb, M.2    Vonesch, J.L.3
  • 45
    • 0036713129 scopus 로고    scopus 로고
    • Cell differentiation induces TIFl f3 association with centromeric heterochromatin via an HPI interaction
    • Cammas F, Oulad-Ab delgha ni M, Vonesch JL, et al. Cell differentiation induces TIFl f3 association with centrome ric heteroc hromatin via an HPI interaction. J Cell Sci 2002; 115:3439-3448.
    • (2002) J Cell Sci , vol.115 , pp. 3439-3448
    • Cammas, F.1    Oulad-Ab Delghani, M.2    Vonesch, J.L.3
  • 46
    • 4444372922 scopus 로고    scopus 로고
    • Association of the transcriptional corepressor TlF1f3 with heterochromatin protein i (l IP I): An essential role for progression through differentiation
    • Cammas F, Herzog M, Lerouge T, et al. Association of the transcriptio nal corepressor TlF1f3 with heterochromatin protein I (l IP I): an essential role for progression through differentiation. Genes Dev 2004; 18:2147-2160.
    • (2004) Genes Dev , vol.18 , pp. 2147-2160
    • Cammas, F.1    Herzog, M.2    Lerouge, T.3
  • 47
    • 34848819391 scopus 로고    scopus 로고
    • TRIM28 mediates primer binding site-targeted silencing of murine leukemia virus in embryonic cells
    • Wolf 0, Goff SP. TRIM28 mediates primer binding site-targeted silencing of murine leukemia virus in embryonic cells. Cell 2007; 131:46-57.
    • (2007) Cell , vol.131 , pp. 46-57
    • Wolf, O.1    Goff, S.P.2
  • 48
    • 42449091476 scopus 로고    scopus 로고
    • Primer binding site-depe ndent restriction of murine leukemia virus requires HPI binding by TRIM28
    • Wolf 0, Cammas F, Losson R, et al. Primer binding site-depe ndent restriction of murine leukemia virus requires HPI binding by TRIM28. J Virol 2008; 82:4675-4679 .
    • (2008) J Virol , vol.82 , pp. 4675-4679
    • Wolf, O.1    Cammas, F.2    Losson, R.3
  • 49
    • 34347353316 scopus 로고    scopus 로고
    • Genome-wide analysis ofKAPI binding suggests autoreg ulation ofKRAB-ZNFs
    • O'Geen 1-1, Squazzo SL, Lyengar S, et al. Genome-wide analysis ofKAPI binding suggests autoreg ulation ofKRAB-ZNFs. PloS Genet 2007 ; 3:e89 .
    • (2007) PloS Genet , vol.3
    • O'Geen, L.-L.1    Squazzo, S.L.2    Lyengar, S.3
  • 50
    • 25144496653 scopus 로고    scopus 로고
    • MDM2 interac tion with nuclear corep ressor KAPI contributes to p53 inactivation
    • Wang C, Ivanov A, Chen L, et al. MDM2 interac tion with nuclear corep ressor KAPI contributes to p53 inactivation. EMBO J 2005; 24:3279-3290.
    • (2005) EMBO J , vol.24 , pp. 3279-3290
    • Wang, C.1    Ivanov, A.2    Chen, L.3
  • 51
    • 35649016616 scopus 로고    scopus 로고
    • Regulation ofE2F i function by the nuclear corepressor KAPI
    • Wang C, Rauscher FJ, Cress WD, et al. Regulation ofE2F I function by the nuclear corepressor KAPI. J Bioi Chem 2007; 282:29902 -29909 .
    • (2007) J Bioi Chem , vol.282 , pp. 29902-29909
    • Wang, C.1    Rauscher, F.J.2    Cress, W.D.3
  • 52
    • 46149110511 scopus 로고    scopus 로고
    • An RNAi screen of chromatin proteins identifies Tip60-p400 as a regulator of embryonic stem cell identity
    • Fazzio TG, Huff JT, Panning B.An RNAi screen ofchromatin proteins identifies Tip60-p400 as a regulator of embryo nic stem cell identity . Cell 2008; 134:162-174.
    • (2008) Cell , vol.134 , pp. 162-174
    • Fazzio, T.G.1    Huff, J.T.2    Panning, B.3
  • 53
    • 64349096829 scopus 로고    scopus 로고
    • A geno me-wide RNAi screen identifies a new transcriptional module required for self-renewal
    • Hu G, Kim J, Xu Qet al. A geno me-wide RNAi screen identifies a new transcriptional module required for self-renewal. Genes Dev 2009; 23:837 -848.
    • (2009) Genes Dev , vol.23 , pp. 837-848
    • Hu, G.1    Kim, J.2    Xu, Q.3
  • 54
    • 0000237552 scopus 로고    scopus 로고
    • Role of PML in cell growth and retinoic acid pathway
    • Wang ZG, Delva L, Gaboli M, et al. Role of PML in cell growth and retinoic acid pathway. Science 1998; 279: 1547-1551.
    • (1998) Science , vol.279 , pp. 1547-1551
    • Wang, Z.G.1    Delva, L.2    Gaboli, M.3
  • 55
    • 0035910747 scopus 로고    scopus 로고
    • Role of promyelocytic leukemia (PML) protein in tumor suppression
    • Rego EM, Wang ZG, Peruzzi Det al. Role of promyelocytic leukemia (PML) protein in tumor suppressio n. J Exp Med 2001; 193:521-529 .
    • (2001) J Exp Med , vol.193 , pp. 521-529
    • Rego, E.M.1    Wang, Z.G.2    Peruzzi, D.3
  • 56
    • 0035969125 scopus 로고    scopus 로고
    • PML protein isoforms and the RBCCnRIM motif
    • Je nssen K, Shiels C, Freemo nt PS. PML protein isoforms and the RBCCnRIM motif. Oncogene 2001; 20:7223-7233.
    • (2001) Oncogene , vol.20 , pp. 7223-7233
    • Jenssen, K.1    Shiels, C.2    Freemont, P.S.3
  • 57
    • 36448975490 scopus 로고    scopus 로고
    • Structure, dynamics and functions of promyelocytic leukaemia nuclear bodies
    • Berna rdi R, Pandolfi PP. Structure, dynamics and functio ns of promyelocytic leukaemia nuclear bodies. Nat Rev Mol Cell Bioi 2007; 8: 1006-1016.
    • (2007) Nat Rev Mol Cell Bioi , vol.8 , pp. 1006-1016
    • Bernardi, R.1    Pandolfi, P.P.2
  • 58
    • 0035809924 scopus 로고    scopus 로고
    • The transcri ption coactivator CBP is a dynamic component of the promyelocytic leukemia nuclear body
    • Boisvert FM, Kruhlak MJ, Box AK, et al. The transcri ption coactivator CBP is a dynamic component of the promyelocytic leukemia nuclear body. J Cell BioI 200 1; 152:1099-1 106.
    • (2001) J Cell BioI , vol.152 , pp. 1099-1106
    • Boisvert, F.M.1    Kruhlak, M.J.2    Box, A.K.3
  • 59
    • 84882334254 scopus 로고    scopus 로고
    • Interactiono f SP I00 with HPI proteins: A link between the promyelocytic leukemia-associated nuclear bodies and the chromatin compartment
    • Seeler JS,MarchioA, Siuer lin Detal.lnteractionofSP I00 with HPI proteins: ali nkbetweenthe promyelocytic leukemia-associated nuclear bodies and the chromatin compartment. Mol Cell Bioi 1998; 95:73 16-7321 .
    • (1998) Mol Cell Bioi , vol.95 , Issue.73 , pp. 16-7321
    • Seeler, J.S.1    Marchio, A.2    Siuerlin, D.3
  • 60
    • 0032574737 scopus 로고    scopus 로고
    • Localization of nascent RNA and CREB binding protein with the PML-containing nuclear body
    • LaMorte V, Dyck JA, Ochs RL, et al. Localization of nascent RNA and CREB binding protein with the PML-containing nuclear body. Proc Nat! Acad Sci USA 1998; 95:499 1-4996 .
    • (1998) Proc Nat! Acad Sci USA , vol.95 , Issue.499 , pp. 1-4996
    • Lamorte, V.1    Dyck, J.A.2    Ochs, R.L.3
  • 61
    • 0034707690 scopus 로고    scopus 로고
    • Promyelocytic leukemia (PML) nuclear bodies are protein structures that do not accumulate RNA
    • Boisvert FM, Hendzel MJ, Bazeu-Jones DP. Promyelocytic leukemia (PML) nuclear bodies are protein structures that do not accumulate RNA. J Cell BioI 2000; 148:283-292.
    • (2000) J Cell BioI , vol.148 , pp. 283-292
    • Boisvert, F.M.1    Hendzel, M.J.2    Bazeu-Jones, D.P.3
  • 62
    • 1242329998 scopus 로고    scopus 로고
    • Promyelocytic leukemia nuclear bodies associat e with trans criptio nally active genomic regions
    • Wang J, Shiels C, Sasieni P, et al. Promyelocytic leukemia nuclear bodies associat e with trans criptio nally active genomic regions. J Cell Bioi 2004; 164:515-526.
    • (2004) J Cell Bioi , vol.164 , pp. 515-526
    • Wang, J.1    Shiels, C.2    Sasieni, P.3
  • 63
    • 16844373902 scopus 로고    scopus 로고
    • PML bodies: A meeting place for genomic loci
    • Ching RW, Dellaire G, Eskiw CH, et al. PML bodies: A meeting place for genomic loci. J Cell Sci 2005; 118:847-854 .
    • (2005) J Cell Sci , vol.118 , pp. 847-854
    • Ching, R.W.1    Dellaire, G.2    Eskiw, C.H.3
  • 64
    • 0028832631 scopus 로고
    • Effect of PML and PML-RAR on the transact ivation properties and subcellular distribution ofstero id hormone receptors
    • Guiochon-Mantel A, Savouret JF, Guignon, et al. Effect of PML and PML-RAR on the transact ivation properties and subcellular distribution ofstero id hormone receptors. Mol Endocrinol 1995; 9: 1791-1803 .
    • (1995) Mol Endocrinol , vol.9 , pp. 1791-1803
    • Guiochon-Mantel, A.1    Savouret, J.F.2    Guignon3
  • 65
    • 0033053037 scopus 로고    scopus 로고
    • Modulation of CREB binding protein function by the promyelocytic (PML) oncopro tein suggests a ro le for nuclear bodies in hormone signaling
    • Doucas V, Tini M, Egan DA, et al. Modulation of CREB binding protein function by the promyelocytic (PML) oncopro tein suggests a ro le for nuclear bodies in hormone signaling. Proc Nat! Acad Sci USA 1999; 96:26 27-2632.
    • (1999) Proc Nat! Acad Sci USA , vol.96 , Issue.26 , pp. 27-2632
    • Doucas, V.1    Tini, M.2    Egan, D.A.3
  • 66
    • 0034306019 scopus 로고    scopus 로고
    • The function of PML in p53-dependen t apoptosis
    • Guo A, Salomoni P, Luo J, et al. The function of PML in p53-dependen t apoptosis. Nat Cell Bioi 2000; 2:730-736.
    • (2000) Nat Cell Bioi , vol.2 , pp. 730-736
    • Guo, A.1    Salomoni, P.2    Luo, J.3
  • 67
    • 27144507300 scopus 로고    scopus 로고
    • The promyelocytic leukaemia protein tumour suppressor functions as a transc riptional regulator of p63
    • Bernasso la F, Oberst A, Melino G, et al. The promyelocytic leukaemia protein tumour suppressor functions as a transc riptional regulator of p63. Oncogene 2005; 24:6982-6986.
    • (2005) Oncogene , vol.24 , pp. 6982-6986
    • Bernasso La, F.1    Oberst, A.2    Melino, G.3
  • 68
    • 2942657482 scopus 로고    scopus 로고
    • Ubiquitin-dependent degradation of p73 is inhibited by PML
    • Bernasso la F, Salomoni L, Oberst A, et al. Ubiquitin-depe ndent degradation of p73 is inhibited by PML. J Exp Med 2004; 199:1545-1557.
    • (2004) J Exp Med , vol.199 , pp. 1545-1557
    • Bernasso La, F.1    Salomoni, L.2    Oberst, A.3
  • 69
    • 0034644274 scopus 로고    scopus 로고
    • PMLregula tes p53 acety lation and premature senesce nce induced by oncogenic Ras
    • Pearson M, Carbone R, SebastianiC, et al. PMLregula tes p53 acety lation and premature senesce nce induced by oncogenic Ras. Nature 2000; 406:207-210.
    • (2000) Nature , vol.406 , pp. 207-210
    • Pearson, M.1    Carbone, R.2    Sebastiani, C.3
  • 70
    • 0142106346 scopus 로고    scopus 로고
    • Cell ular stress and DNA damage invoke temporally distinct Mdm2, p53 and PML complexes and damage-specific nuclear relocalization
    • Kurki S, Latonen L, Laiho M. Cell ular stress and DNA damage invoke temporally distinct Mdm2, p53 and PML complexes and damage-specific nuclear relocalization. J Cell Sci 2003; 116:39 17-3925.
    • (2003) J Cell Sci , vol.116 , Issue.39 , pp. 17-3925
    • Kurki, S.1    Latonen, L.2    Laiho, M.3
  • 71
    • 3242726103 scopus 로고    scopus 로고
    • PML regulates p53 stability by sequestering Mdm2 to the nucleolus
    • Bernar di R, Scagl ioni PI', Bergmann S, et al. PML regulates p53 stability by sequestering Mdm2 to the nucleolus. Nature Cell BioI 2004; 6:665-672.
    • (2004) Nature Cell BioI , vol.6 , pp. 665-672
    • Bernardi, R.1    Scaglioni, P.L.2    Bergmann, S.3
  • 72
    • 0041856232 scopus 로고    scopus 로고
    • The promyelocytic leukemia protein protects p53 from Mdm2-mediated inhibition and degradation
    • Louria-Hayon I, Grossman T, Sionov RV, et al. The promyelocytic leukemia protein protects p53 from Mdm2-mediated inhibition and degradation. J BioI Chern 2003; 278:33134-33141.
    • (2003) J BioI Chern , vol.278 , pp. 33134-33141
    • Louria-Hayon, I.1    Grossman, T.2    Sionov, R.V.3
  • 73
    • 45949110751 scopus 로고    scopus 로고
    • PML enhances the regulation ofp53 by CK i in response to DNA damage
    • Alsheich-Bartok 0, Haupt S, Alkalay-Snir L et al. PML enhances the regulation ofp53 by CK I in response to DNA damage. Oncogene 2008; 27:3653-3661.
    • (2008) Oncogene , vol.27 , pp. 3653-3661
    • Alsheich-Bartok, O.1    Haupt, S.2    Alkalay-Snir, L.3
  • 74
    • 0037061508 scopus 로고    scopus 로고
    • Deubiquitination of p53 by I-IAUSP is an important pathway for p53 stabilization
    • Li M, Chen D, Shiloh A, et al. Deubiquitination of p53 by I-IAUSP is an important pathway for p53 stabilization . Nature 2002; 4 16:648-653.
    • (2002) Nature , vol.4 , Issue.16 , pp. 648-653
    • Li, M.1    Chen, D.2    Shiloh, A.3
  • 75
    • 0032482440 scopus 로고    scopus 로고
    • Modulation ofFos -mediatedAP-I transcription by the promyelocytic leukemia protein
    • Vallian S, Gake n JA, Gingold EB, et al. Modulation ofFos -mediatedAP-I transcription by the promyelocytic leukemia protein. Oncogene 1998; 16:2843-2853.
    • (1998) Oncogene , vol.16 , pp. 2843-2853
    • Vallian, S.1    Gaken, J.A.2    Gingold, E.B.3
  • 76
    • 0033842166 scopus 로고    scopus 로고
    • Potentiation of GATA-2 activity through interactions with the promyelocytic leukemia protein(PML) and the t(l5; 17)-generated PML-retinoicacidreceptoroncoprotein
    • Tsuzuki S, Towatari M, Siato H, et al. Potentiation of GATA-2 activity through interactions with the promyelocytic leukemia protein(PML) and the t(l5; 17)-generated PML-retinoicacidreceptoroncoprotein. Mol Cell BioI 2000; 20:6276-6286.
    • (2000) Mol Cell BioI , vol.20 , pp. 6276-6286
    • Tsuzuki, S.1    Towatari, M.2    Siato, H.3
  • 77
    • 11144219997 scopus 로고    scopus 로고
    • Physical and functional link of the leukemia-associated factors AMLI and PML
    • Nguyen LA, Pandolfi PP, Aikawa Y, et al. Physical and functional link of the leukemia-associated factors AMLI and PML. Blood 2005 ; 105:292-300 .
    • (2005) Blood , vol.105 , pp. 292-300
    • Nguyen, L.A.1    Pandolfi, P.P.2    Aikawa, Y.3
  • 78
    • 4544256756 scopus 로고    scopus 로고
    • Cytoplasmic PML function in TGF signaling
    • Lin HK,Bergmann S, Pandolfi PP.Cytoplasmic PML function in TGF -signali ng. Nature 2004; 431:205-211.
    • (2004) Nature , vol.431 , pp. 205-211
    • Lin, H.K.1    Bergmann, S.2    Pandolfi, P.P.3
  • 79
    • 33845871732 scopus 로고    scopus 로고
    • Functional interaction between PML and SATBI reg ulates chromatin-loop architecture and transcription of the MHC class i locus
    • Kumar PI', Bischof 0, Purbey PI', et al. Functional interaction between PML and SATBI reg ulates chromatin-loop architecture and transcription of the MHC class I locus. Nature Cell BioI 2004; 9:45-56.
    • (2004) Nature Cell BioI , vol.9 , pp. 45-56
    • Kumar, P.L.1    Bischof, O.2    Purbey, P.I.3
  • 80
    • 0033952527 scopus 로고    scopus 로고
    • Sequestration and inhibition of Daxx-mediated transcriptional repression by PML
    • Li L-L, Leo C, Zhu J, et al. Sequestration and inhibition of Daxx-mediated transcriptional repression by PML. Mol Cell Bioi 2000; 20:1784-1796.
    • (2000) Mol Cell Bioi , vol.20 , pp. 1784-1796
    • Li, L.-L.1    Leo, C.2    Zhu, J.3
  • 81
    • 34249005636 scopus 로고    scopus 로고
    • PML4 induces differentiation by Myc destabilization
    • Buschbec k M, Uribesalgo I, Ledl A, et al. PML4 induces differentiation by Myc destabilization. Oncogene 2007; 26:3415-3422.
    • (2007) Oncogene , vol.26 , pp. 3415-3422
    • Buschbeck, M.1    Uribesalgo, I.2    Ledl, A.3
  • 82
    • 0031574262 scopus 로고    scopus 로고
    • Transcriptional repression by the promyelocytic leukemia protein, PML
    • Vallian S, Gaken EB, Trayner, et al. Transcriptional repression by the promyelocytic leukemia protein, PML. Exp Cell Res 1997; 237:37 1-382.
    • (1997) Exp Cell Res , vol.237 , Issue.37 , pp. 1-382
    • Vallian, S.1    Gaken, E.B.2    Trayner3
  • 83
    • 0034968656 scopus 로고    scopus 로고
    • Role of PML and PML-RARu in Mad-med iated transcriptional repress ion
    • Khan MM, Nomura T, Kim H, et al. Role of PML and PML-RARu in Mad-med iated transcriptional repress ion. Mol Cell 2001; 7:1233-1243.
    • (2001) Mol Cell , vol.7 , pp. 1233-1243
    • Khan, M.M.1    Nomura, T.2    Kim, H.3
  • 84
    • 0031755628 scopus 로고    scopus 로고
    • The promyelocyti c leukemia protein interacts with Spl and inhibits its transactivation ofthe epiderma l growth factor receptor promoter
    • Vallian S, Chin KV, Chang KS. The promyelocyti c leukemia protein interacts with Spl and inhibits its transactivation ofthe epiderma l growth factor receptor promoter. Mol Cell BioI 1998; 18:7147-7156.
    • (1998) Mol Cell BioI , vol.18 , pp. 7147-7156
    • Vallian, S.1    Chin, K.V.2    Chang, K.S.3
  • 85
    • 0037198670 scopus 로고    scopus 로고
    • Promyelocytic leukemia protein PML inhibits Nur77-mediated transcription through specific functional interactions
    • Wu WS, Xu lX, Ran Ret al. Promyelocytic leukemia protein PML inhibits Nur77-mediated transcription through spec ific functional interactions. Oncogene 2002; 21:3925-3933.
    • (2002) Oncogene , vol.21 , pp. 3925-3933
    • Wu, W.S.1    Xu, L.X.2    Ran, R.3
  • 86
    • 0037200047 scopus 로고    scopus 로고
    • The promyelocytic leukemia protein represses A20-mediated transc ription
    • Wu WS, Xu lX, Chang KS. The promyelocytic leukemia protein represses A20-mediated transc ription. J BioI Chem 2002; 277:31734-3 1739.
    • (2002) J BioI Chem , vol.277 , pp. 31734-31739
    • Wu, W.S.1    Lx, X.2    Chang, K.S.3
  • 87
    • 33845473249 scopus 로고    scopus 로고
    • The promyelocytic leukemia protein functio ns as a negative reg ulator of IFN-y signaling
    • Choi YH, Bernard i R, Pandolfi PP, et al. The promyelocytic leukemia protein functio ns as a negative reg ulator of IFN-y signaling. Proc Natl Acad Sci USA 2006; 103:18715-18720.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 18715-18720
    • Choi, Y.H.1    Bernardi, R.2    Pandolfi, P.P.3
  • 88
    • 0031929684 scopus 로고    scopus 로고
    • The promyelocytic leukemia gene product (PML) forms stable complexes with the retinoblastoma protein
    • Alcaly M, Tomassoni L, Colombo E, et al. The promyelocytic leukemia gene product (PML) forms stable complexes with the retinoblastoma protein. Mol Cell BioI 1998; 18:1084-1093.
    • (1998) Mol Cell BioI , vol.18 , pp. 1084-1093
    • Alcaly, M.1    Tomassoni, L.2    Colombo, E.3
  • 89
    • 0023158426 scopus 로고
    • Ret transfo rming gene encodes a fusion protein homologous to tyrosine kinases
    • Takahashi M, CooperGM. Ret transfo rming gene encodes a fusion protein homologous to tyrosin e kinases . Mol Cell Bioi 1987; 7: 1378-1385.
    • (1987) Mol Cell Bioi , vol.7 , pp. 1378-1385
    • Takahashi, M.1    Cooper, G.M.2
  • 90
    • 0032755433 scopus 로고    scopus 로고
    • Different nuclear/cytoplasmic distrib utions of RET finger protein in different cell types
    • Tezel G, Nagasaka T, Iwahashi N, et al. Different nuclear/cytoplasmic distrib utions of RET finger protein in different cell types. Path Int 1999; 49:881-886
    • (1999) Path Int , vol.49 , pp. 881-886
    • Tezel, G.1    Nagasaka, T.2    Iwahashi, N.3
  • 91
    • 0031800796 scopus 로고    scopus 로고
    • Ret finger protein is a normal component ofPML nuclear bodies and interac ts directly with PML
    • Cao T, Duprez E, Borden KLB, et al. Ret finger protein is a normal component ofPML nuclear bodies and interac ts directly with PML. J Cell Sci 1998; I II :13 19-1329.
    • (1998) J Cell Sci , vol.3 , pp. 1319-1329
    • Cao, T.1    Duprez, E.2    Klb, B.3
  • 92
    • 0032755283 scopus 로고    scopus 로고
    • Interaction between the Ret finger protein and the Int-6 gene product and coloca lisation into nuclear bodies
    • Morris-Desbois C, Bochard V, Reynaud C, et al. Interaction between the Ret finger protein and the Int-6 gene product and coloca lisation into nuclear bodies. J Cell Sci 1999; 112:333 1-3342.
    • (1999) J Cell Sci , vol.112 , Issue.333 , pp. 1-3342
    • Morris-Desbois, C.1    Bochard, V.2    Reynaud, C.3
  • 93
    • 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 Chem 2003; 278:31902-3 1908.
    • (2003) J BioI Chem , vol.278 , pp. 31902-31908
    • Dho, S.H.1    Kwon, K.S.2
  • 94
    • 22144482659 scopus 로고    scopus 로고
    • PIAS proteins are involved in theSUMO-I modification, intracell ular translocation and transcriptional repressive activity of RET finger protein
    • Matsuura T, Shimono Y, Kawai Ket al. PIAS proteins are involved in theSUMO-I modification, intracell ular translocation and transcriptional repressive activity of RET finger protein. Exp Cell Res 2005; 308:65 -77.
    • (2005) Exp Cell Res , vol.308 , pp. 65-77
    • Matsuura, T.1    Shimono, Y.2    Kawai, K.3
  • 95
    • 33750345188 scopus 로고    scopus 로고
    • RET finger protein enhances MBD2-andMBD4-dependent transcriptional repress ion
    • Fukushige S, Kondo E,GuZ, et al. RET finger proteinenhancesMBD2-andMBD4- dependent transcriptio nal repress ion. Biochem Biophys Res Commun 2006; 351 :85-92.
    • (2006) Biochem Biophys Res Commun , vol.351 , pp. 85-92
    • Fukushige, S.1    Eguz, K.2
  • 96
    • 0346434166 scopus 로고    scopus 로고
    • Mi -2 associates with BRG i and RET finger protein at the distinct regions with transcriptional activating and repressing activities
    • Shimono Y, Murakami H, Kawai K, et al. Mi -2 associates with BRG I and RET finger protein at the distinct regions with transcriptional activating and repressing activities . J BioI Chem 2003 ; 278:5 1638-5 1645.
    • (2003) J BioI Chem , vol.278 , pp. 1638-1645
    • Shimono, Y.1    Murakami, H.2    Kawai, K.3
  • 97
    • 27144466398 scopus 로고    scopus 로고
    • RFP represses transc riptional activation by bHLH transcription factors
    • Bloor AJ, Kotsopoulou E, Hayward P, et al. RFP represses transc riptional activation by bHLH transcription factors. Oncogene 2005; 24:6729-6736.
    • (2005) Oncogene , vol.24 , pp. 6729-6736
    • Bloor, A.J.1    Kotsopoulou, E.2    Hayward, P.3
  • 98
    • 17044410129 scopus 로고    scopus 로고
    • Selectiv e ablation of Retinoblastoma protein function by the RET finger protein
    • Krutzfeldt M, Ellis M, Weekes DB, et al. Selectiv e ablation of Retinoblastoma protein function by the RET finger protein. Mol Cell 2005; 18:213-224.
    • (2005) Mol Cell , vol.18 , pp. 213-224
    • Krutzfeldt, M.1    Ellis, M.2    Weekes, D.B.3
  • 99
    • 33748448840 scopus 로고    scopus 로고
    • Novel role of the RET finger protein in estrogen receptor -mediated transcription in MCF-7 cells
    • Townson SM, Kang K, Lee AVet al. Novel role of the RET finger protein in estrogen receptor -mediated transcription in MCF-7 cells . Biochcm Biophys Res Commun 2006; 349:540-548.
    • (2006) Biochcm Biophys Res Commun , vol.349 , pp. 540-548
    • Townson, S.M.1    Kang, K.2    Lee, A.V.3
  • 100
    • 28244475343 scopus 로고    scopus 로고
    • Microspherule protein I, Mi -2 and RET finger protein associate in the nucleolus and up-regulate ribosomal gene transcription
    • ShimonoK, Shimo noY, ShimokataK, et al. Microspherule protein I, Mi -2 and RET finger protein associate in the nucleolus and up-regulate ribosomal gene transcription. J Bioi Chem 2005; 280:39436-39447 .
    • (2005) J Bioi Chem , vol.280 , pp. 39436-39447
    • Shimono Shimono, K.Y.1    Shimokata, K.2
  • 101
    • 0023988517 scopus 로고
    • RPT-I, an intracellular protein from helpe r/inducer T-cells that reg ulates gene expression of interleukin 2 receptor and human immunodeficiency virus type i
    • Patarca R, Gordon JF, Schwartz Jet al. RPT-I, an intracellular protein from helpe r/inducer T-cells that reg ulates gene expression of interleukin 2 receptor and human immunodeficiency virus type I . Proc Natl Acad Sci USA 1988; 85:2733 -2737.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 2733-2737
    • Patarca, R.1    Gordon, J.F.2    Schwartz, J.3
  • 102
    • 33750720955 scopus 로고    scopus 로고
    • PUI: An ETS family transcription factor that regulates leukemogenesis besides normal hematopoiesis
    • Gupta P, Gurudutta GU, Verma YK, et al. PU. I: an ETS family transcription factor that regulates leukemogenesis besides normal hematopoiesis. Stem Cells Dev 2006; 15:609-617.
    • (2006) Stem Cells Dev , vol.15 , pp. 609-617
    • Gupta, P.1    Gurudutta, G.U.2    Verma, Y.K.3
  • 103
    • 0242331288 scopus 로고    scopus 로고
    • Pub, a novel PU i binding protein, regulates the transcriptional activity of PU i
    • Hirose S, Nishizumi 1-1, Sakano II. Pub, a novel PU. I binding protein, regulates the transcriptional activity of PU. I. Biochem Biophys Res Commun 2003; 31 1:351-360.
    • (2003) Biochem Biophys Res Commun , vol.311 , pp. 351-360
    • Hirose, S.1    Nishizumi, L.-L.2    Sakano, I.I.3
  • 104
    • 4444301523 scopus 로고    scopus 로고
    • TRIM45, a nove l human RBCCITRIMprotein, inhibits transcriptional activities of ElK-I and AP-1
    • Wang Y, Li Y, Qi X, et al. TRIM45, a nove l human RBCCITRIMprotein, inhibits transcriptional activities of ElK-I and AP-1. Biochem Biophys Res Commun 2004; 323 :9-16.
    • (2004) Biochem Biophys Res Commun , vol.323 , pp. 9-16
    • Wang, Y.1    Li, Y.2    Qi, X.3
  • 105
    • 0027397091 scopus 로고
    • A putative zinc-binding protein on lampbrush chromosome loops
    • BelliniM, Lacroix JC, Gall JG.A putative zinc-binding protein on lampbrush chromosome loops . EMBO J 1993; 12:107-1 14.
    • (1993) EMBO J , vol.12 , pp. 107-114
    • Bellini, M.1    Lacroix, J.C.2    Gall, J.G.3
  • 106
    • 34147205884 scopus 로고    scopus 로고
    • The tripartite motif of nuclear factor 7 is required for its assoc iation with trans criptional units
    • Beenders B, Jones PL, Bellini M. The tripartite motif of nuclear factor 7 is required for its assoc iation with trans criptional units. Mol Cell BioI 2007; 27:2615-2624.
    • (2007) Mol Cell BioI , vol.27 , pp. 2615-2624
    • Beenders, B.1    Jones, P.L.2    Bellini, M.3


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