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Volumn 44, Issue 3, 2006, Pages 463-474

CGI-55 interacts with nuclear proteins and co-localizes to p80-coilin positive-coiled bodies in the nucleus

Author keywords

Cajal bodies; Coiled bodies; Domain mapping; Immunolocalization; p80 coilin; PML NBs; Protein protein interaction; Two hybrid

Indexed keywords

HYBRID PROTEIN; NUCLEAR PROTEIN; P80 COILIN; P80-COILIN; PAI RBP1 PROTEIN, HUMAN; PAI-RBP1 PROTEIN, HUMAN; PROTEIN; RNA BINDING PROTEIN;

EID: 31744447890     PISSN: 10859195     EISSN: None     Source Type: Journal    
DOI: 10.1385/CBB:44:3:463     Document Type: Conference Paper
Times cited : (26)

References (51)
  • 1
    • 6844236392 scopus 로고    scopus 로고
    • Characterization, mapping and partial cDNA sequence of the 57-kDa intracellular Ki-1 antigen
    • Kobarg, J., Schnittger, S., Fonatsch, C., et al. (1997) Characterization, mapping and partial cDNA sequence of the 57-kDa intracellular Ki-1 antigen. Exp. Clin. Immunogenet. 14, 273-280.
    • (1997) Exp. Clin. Immunogenet. , vol.14 , pp. 273-280
    • Kobarg, J.1    Schnittger, S.2    Fonatsch, C.3
  • 2
    • 0037413848 scopus 로고    scopus 로고
    • Characterization of a new family of proteins that interact with the C-terminal region of the chromatin-remodeling factor CHD-3
    • Lemos, T. A., Passos, D. O., Nery, F. C., and Kobarg, J. (2003) Characterization of a new family of proteins that interact with the C-terminal region of the chromatin-remodeling factor CHD-3. FEBS Lett. 533, 14-20.
    • (2003) FEBS Lett. , vol.533 , pp. 14-20
    • Lemos, T.A.1    Passos, D.O.2    Nery, F.C.3    Kobarg, J.4
  • 3
    • 0035793586 scopus 로고    scopus 로고
    • Identification and cDNA cloning of a novel RNA-binding protein that interacts with the cyclic nucleotide-responsive sequence in the type-1 plasminogen activator inhibitor mRNA
    • Heaton, J. H., Dlakic, W. M., Dlakic, M., and Gelehrter, T. D. (2001) Identification and cDNA cloning of a novel RNA-binding protein that interacts with the cyclic nucleotide-responsive sequence in the type-1 plasminogen activator inhibitor mRNA. J. Biol. Chem. 276, 3341-3347.
    • (2001) J. Biol. Chem. , vol.276 , pp. 3341-3347
    • Heaton, J.H.1    Dlakic, W.M.2    Dlakic, M.3    Gelehrter, T.D.4
  • 4
    • 0034703020 scopus 로고    scopus 로고
    • Molecular characterization of a novel intracellular hyaluronan-binding protein
    • Huang, L., Grammatikakis, N., Yoneda, M., Banerjee, S. D., and Toole, B. P. (2000) Molecular characterization of a novel intracellular hyaluronan-binding protein. J. Biol. Chem. 275, 29,829-29,839.
    • (2000) J. Biol. Chem. , vol.275
    • Huang, L.1    Grammatikakis, N.2    Yoneda, M.3    Banerjee, S.D.4    Toole, B.P.5
  • 5
    • 1642565088 scopus 로고    scopus 로고
    • Ki-1/57 interacts with RACK1 and is a substrate for PMA activated PKC
    • Nery, F. C., Passos, D. O., Garcia, V. S., and Kobarg, J. (2004) Ki-1/57 interacts with RACK1 and is a substrate for PMA activated PKC. J. Biol. Chem. 279, 11,444-11,455.
    • (2004) J. Biol. Chem. , vol.279
    • Nery, F.C.1    Passos, D.O.2    Garcia, V.S.3    Kobarg, J.4
  • 6
    • 0038621377 scopus 로고    scopus 로고
    • Function of p73, not of p53, is inhibited by the physical interaction with RACK1 and its inhibitory effect is counteracted by pRB
    • Ozaki, T., Watanabe, K.-I., Nakagawa, T., Miyazaki, K., Takahashi, M., and Nakagawara, A. (2003) Function of p73, not of p53, is inhibited by the physical interaction with RACK1 and its inhibitory effect is counteracted by pRB. Oncogene 22, 3231-3242.
    • (2003) Oncogene , vol.22 , pp. 3231-3242
    • Ozaki, T.1    Watanabe, K.-I.2    Nakagawa, T.3    Miyazaki, K.4    Takahashi, M.5    Nakagawara, A.6
  • 7
    • 0033179146 scopus 로고    scopus 로고
    • Nuclear bodies: Multifaceted subdomains of the interchromatin space
    • Matera, A. G. (1999) Nuclear bodies: multifaceted subdomains of the interchromatin space. Trends Cell Biol. 9, 302-309.
    • (1999) Trends Cell Biol. , vol.9 , pp. 302-309
    • Matera, A.G.1
  • 8
    • 0027479449 scopus 로고
    • Immunocytochemical analysis of the coiled body in the cell cycle and during cell proliferation
    • Andrade, L. E. C., Tan, E. M., and Chan, E. K. L. (1993) Immunocytochemical analysis of the coiled body in the cell cycle and during cell proliferation. Proc. Natl. Acad. Sci. U.S.A. 99, 1947-1951.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 1947-1951
    • Andrade, L.E.C.1    Tan, E.M.2    Chan, E.K.L.3
  • 9
    • 0037078322 scopus 로고    scopus 로고
    • Cajal bodies and coilin-moving towards function
    • Ogg, S. C., and Lamond, A. I. (2002) Cajal bodies and coilin-moving towards function. J. Cell Biol. 14, 17-21.
    • (2002) J. Cell Biol. , vol.14 , pp. 17-21
    • Ogg, S.C.1    Lamond, A.I.2
  • 10
    • 0034186133 scopus 로고    scopus 로고
    • The transcriptional role of PML and the nuclear body
    • Zhong, S., Salomoni, P., and Pandolfi, P. (2000) The transcriptional role of PML and the nuclear body. Nat. Cell Biol. 2, E85-E90.
    • (2000) Nat. Cell Biol. , vol.2
    • Zhong, S.1    Salomoni, P.2    Pandolfi, P.3
  • 11
    • 0036314919 scopus 로고    scopus 로고
    • The topoisomerase I-binding RING protein, topors, is associated with promyelocytic leukemia nuclear bodies
    • Rasheed, Z. A., Saleem, A., Ravee, Y., Pandolfi, P. P., and Rubin, E. H. (2002) The topoisomerase I-binding RING protein, topors, is associated with promyelocytic leukemia nuclear bodies. Exp. Cell Res. 277, 152-160.
    • (2002) Exp. Cell Res. , vol.277 , pp. 152-160
    • Rasheed, Z.A.1    Saleem, A.2    Ravee, Y.3    Pandolfi, P.P.4    Rubin, E.H.5
  • 12
    • 0037169341 scopus 로고    scopus 로고
    • The role of PML in tumor suppression
    • Salomoni, P. and Pandolfi, P. P. (2002) The role of PML in tumor suppression. Cell 108, 165-170.
    • (2002) Cell , vol.108 , pp. 165-170
    • Salomoni, P.1    Pandolfi, P.P.2
  • 13
    • 0033380850 scopus 로고    scopus 로고
    • Cell cycle regulation of PML modification and ND10 composition
    • Everett, R. D., Lomonte, P., Sternsdorf, T., van Driel, R., and Orr, A. (1999) Cell cycle regulation of PML modification and ND10 composition. J. Cell Sci. 112, 4581-4588.
    • (1999) J. Cell Sci. , vol.112 , pp. 4581-4588
    • Everett, R.D.1    Lomonte, P.2    Sternsdorf, T.3    Van Driel, R.4    Orr, A.5
  • 15
    • 0036318221 scopus 로고    scopus 로고
    • Pondering the promyelocytic leukemia protein (PML) puzzle: Possible functions from PML nuclear bodies
    • Borden, K. L. (2002) Pondering the promyelocytic leukemia protein (PML) puzzle: possible functions from PML nuclear bodies. Mol. Cell. Biol. 22, 5259-5269.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 5259-5269
    • Borden, K.L.1
  • 16
    • 0031426631 scopus 로고    scopus 로고
    • Evidence for covalent modification of the nuclear dot-associated proteins PML and SP100 by PIC1/SUMO1
    • Sterndorf, T., Jensen, K., and Will, H. (1997) Evidence for covalent modification of the nuclear dot-associated proteins PML and SP100 by PIC1/SUMO1. J. Cell Biol. 139, 1621-1634.
    • (1997) J. Cell Biol. , vol.139 , pp. 1621-1634
    • Sterndorf, T.1    Jensen, K.2    Will, H.3
  • 17
    • 0032721540 scopus 로고    scopus 로고
    • PML is critical for ND10 formation and recruits the PML-interacting protein daxx to this nuclear structure when modified by SUMO-1
    • Ishov, A. M., Sotnikov, A. G., Negorev, D., et al. (1999) PML is critical for ND10 formation and recruits the PML-interacting protein daxx to this nuclear structure when modified by SUMO-1. J. Cell Biol. 147, 221-234.
    • (1999) J. Cell Biol. , vol.147 , pp. 221-234
    • Ishov, A.M.1    Sotnikov, A.G.2    Negorev, D.3
  • 18
    • 0024406857 scopus 로고
    • A novel genetic system to detect protein-protein interactions
    • Fields, S. and Song, O. (1989) A novel genetic system to detect protein-protein interactions. Nature 340, 245-246.
    • (1989) Nature , vol.340 , pp. 245-246
    • Fields, S.1    Song, O.2
  • 19
    • 0029099409 scopus 로고
    • Ras-Raf interaction: Two-hybrid analysis
    • Vojtek, A. B. and Hollenberg, S. M. (1995) Ras-Raf interaction: two-hybrid analysis. Methods Enzymol. 255, 331-342.
    • (1995) Methods Enzymol. , vol.255 , pp. 331-342
    • Vojtek, A.B.1    Hollenberg, S.M.2
  • 20
    • 0037224504 scopus 로고    scopus 로고
    • Identification and characterization of proteins that selectively interact with isoforms of the mRNA binding protein AUF1 (hnRNP D)
    • Moraes, K. C., Quaresma, A. J., Maehnss, K., and Kobarg, J. (2003) Identification and characterization of proteins that selectively interact with isoforms of the mRNA binding protein AUF1 (hnRNP D). Biol. Chem. 384, 35-37.
    • (2003) Biol. Chem. , vol.384 , pp. 35-37
    • Moraes, K.C.1    Quaresma, A.J.2    Maehnss, K.3    Kobarg, J.4
  • 21
    • 0037022564 scopus 로고    scopus 로고
    • Members of the PIAS family act as SUMO ligases for c-Jun and p53 and repress p53 activity
    • Schmidt, D. and Müller, S. (2002) Members of the PIAS family act as SUMO ligases for c-Jun and p53 and repress p53 activity. Proc. Natl. Acad. Sci. U.S.A. 99, 2872-2877.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 2872-2877
    • Schmidt, D.1    Müller, S.2
  • 22
    • 0036291475 scopus 로고    scopus 로고
    • PIAS proteins modulate transcription factors by functioning as SUMO-1 ligases
    • Kotaja, N., Karvonen, U., Janne, O. A., and Palvimo, J. J. (2002) PIAS proteins modulate transcription factors by functioning as SUMO-1 ligases. Mol. Cell Biol. 22, 5222-5234.
    • (2002) Mol. Cell Biol. , vol.22 , pp. 5222-5234
    • Kotaja, N.1    Karvonen, U.2    Janne, O.A.3    Palvimo, J.J.4
  • 23
    • 0037498052 scopus 로고    scopus 로고
    • Conjugation with the ubiquitin-related modifier SUMO-1 regulates the partitioning of PML within the nucleus
    • Müller, S., Matunis, M. J., and Dejean, A. (1998) Conjugation with the ubiquitin-related modifier SUMO-1 regulates the partitioning of PML within the nucleus. EMBO J. 17, 61-70.
    • (1998) EMBO J. , vol.17 , pp. 61-70
    • Müller, S.1    Matunis, M.J.2    Dejean, A.3
  • 25
    • 0037147346 scopus 로고    scopus 로고
    • Sumoylation of Mdm2 by protein inhibitor of activated STAT (PIAS) and RanBP2 enzymes
    • Miyauchi, Y., Yogosawa, S., Honda, R., Nishida, T., and Yasuda, H. (2002) Sumoylation of Mdm2 by protein inhibitor of activated STAT (PIAS) and RanBP2 enzymes. J. Biol. Chem. 277, 50,131-50,136.
    • (2002) J. Biol. Chem. , vol.277
    • Miyauchi, Y.1    Yogosawa, S.2    Honda, R.3    Nishida, T.4    Yasuda, H.5
  • 26
    • 0345298272 scopus 로고    scopus 로고
    • Interaction between human topoisomerase I and a novel RING-finger/arginine-serine protein
    • Haluska, P., Jr., Saleem, A., Rasheed, Z., et al. (1999) Interaction between human topoisomerase I and a novel RING-finger/arginine-serine protein. Nucleic Acids Res. 27, 2538-2544.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 2538-2544
    • Haluska Jr., P.1    Saleem, A.2    Rasheed, Z.3
  • 27
    • 0032795748 scopus 로고    scopus 로고
    • Identification of a novel gene encoding a p53-associated protein
    • Zhou, R., Wen, H., and Ao, S. Z. (1999) Identification of a novel gene encoding a p53-associated protein. Gene 235, 93-101.
    • (1999) Gene , vol.235 , pp. 93-101
    • Zhou, R.1    Wen, H.2    Ao, S.Z.3
  • 28
    • 0030200110 scopus 로고    scopus 로고
    • PEST sequences and regulation by proteolysis
    • Rechsteiner, M., Rogers, S. W. (1996) PEST sequences and regulation by proteolysis. Trends Biochem. Sci. 21, 267-271.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 267-271
    • Rechsteiner, M.1    Rogers, S.W.2
  • 29
    • 0033229827 scopus 로고    scopus 로고
    • Human Daxx regulates Fas-induced apoptosis from nuclear PML oncogenic domains (PODs)
    • Torii, S., Egan, D. A., Evans, R. A., and Reed, J. C. (1999) Human Daxx regulates Fas-induced apoptosis from nuclear PML oncogenic domains (PODs). EMBO J. 18, 6037-6049.
    • (1999) EMBO J. , vol.18 , pp. 6037-6049
    • Torii, S.1    Egan, D.A.2    Evans, R.A.3    Reed, J.C.4
  • 30
    • 0034628443 scopus 로고    scopus 로고
    • EAP1/Daxx interacts with ETS1 and represses transcriptional activation of ETS1 target genes
    • Li, R., Pei, H., Watson, D. K., and Papas, T. S. (2000) EAP1/Daxx interacts with ETS1 and represses transcriptional activation of ETS1 target genes. Oncogene 19, 745-753.
    • (2000) Oncogene , vol.19 , pp. 745-753
    • Li, R.1    Pei, H.2    Watson, D.K.3    Papas, T.S.4
  • 31
    • 0035914344 scopus 로고    scopus 로고
    • Apoptosis signal-regulating kinase 1 controls the proapoptotic function of death-associated protein (Daxx) in the cytoplasm
    • Ko, Y. G., Kang, Y. S., Park, H., et al. (2001) Apoptosis signal-regulating kinase 1 controls the proapoptotic function of death-associated protein (Daxx) in the cytoplasm. J. Biol. Chem. 276, 39,103-39,106.
    • (2001) J. Biol. Chem. , vol.276
    • Ko, Y.G.1    Kang, Y.S.2    Park, H.3
  • 32
    • 0037507271 scopus 로고    scopus 로고
    • Promyelocytic leukemia protein (PML) functions as a glucocorticoid receptor co-activator by Sequestering Daxx to the PML oncogenic domains (PODs) to enhance its trans-activation potential
    • Lin, D. Y., Lai, M. Z., Ann, D. K., and Shih, H. M. (2003) Promyelocytic leukemia protein (PML) functions as a glucocorticoid receptor co-activator by Sequestering Daxx to the PML oncogenic domains (PODs) to enhance its trans-activation potential. J. Biol. Chem. 278, 15,958-15,965.
    • (2003) J. Biol. Chem. , vol.278
    • Lin, D.Y.1    Lai, M.Z.2    Ann, D.K.3    Shih, H.M.4
  • 33
    • 0037087517 scopus 로고    scopus 로고
    • Identification of septin-interacting proteins and characterization of the Smt3/SUMO-conjugation system in Drosophila
    • Shih, H. P., Hales, K. G., Pringle, J. R., and Peifer, M. (2002) Identification of septin-interacting proteins and characterization of the Smt3/SUMO-conjugation system in Drosophila. J. Cell Sci. 115, 1259-1271.
    • (2002) J. Cell Sci. , vol.115 , pp. 1259-1271
    • Shih, H.P.1    Hales, K.G.2    Pringle, J.R.3    Peifer, M.4
  • 34
    • 0035958081 scopus 로고    scopus 로고
    • Cloning and characterization of LUN, a novel ring finger protein that is highly expressed in lung and specifically binds to a palindromic sequence
    • Chu, D., Kakazu, N., Gorrin-Rivas, M. J., et al. (2001) Cloning and characterization of LUN, a novel ring finger protein that is highly expressed in lung and specifically binds to a palindromic sequence. J. Biol. Chem. 276, 14,004-14,013.
    • (2001) J. Biol. Chem. , vol.276
    • Chu, D.1    Kakazu, N.2    Gorrin-Rivas, M.J.3
  • 35
    • 0031587883 scopus 로고    scopus 로고
    • Daxx, a novel Fas-binding protein that activates JNK and apoptosis
    • Yang, X., Khosravi-Far, R., Chang, H. Y., and Baltimore, D. (1997) Daxx, a novel Fas-binding protein that activates JNK and apoptosis. Cell 89, 1067-1076.
    • (1997) Cell , vol.89 , pp. 1067-1076
    • Yang, X.1    Khosravi-Far, R.2    Chang, H.Y.3    Baltimore, D.4
  • 36
    • 0037192813 scopus 로고    scopus 로고
    • The interaction of Pax5 (BSAP) with Daxx can result in transcriptional activation in B cells
    • Emelyanov, A. V., Kovac, C. R., Sepulveda, M. A., and Birshtein, B. K. (2002) The interaction of Pax5 (BSAP) with Daxx can result in transcriptional activation in B cells. J. Biol. Chem. 277, 11,156-11,164.
    • (2002) J. Biol. Chem. , vol.277
    • Emelyanov, A.V.1    Kovac, C.R.2    Sepulveda, M.A.3    Birshtein, B.K.4
  • 37
    • 0031847605 scopus 로고    scopus 로고
    • Interphase-specific association of intrinsic centromer protein CENP-C with Daxx, a death domain-binding protein implicated in Fas-mediated cell death
    • Pluta, A. F., Earnshaw, W. C., and Goldberg, I. G. (1998) Interphase-specific association of intrinsic centromer protein CENP-C with Daxx, a death domain-binding protein implicated in Fas-mediated cell death. J. Cell. Sci. 111, 2029-2041.
    • (1998) J. Cell. Sci. , vol.111 , pp. 2029-2041
    • Pluta, A.F.1    Earnshaw, W.C.2    Goldberg, I.G.3
  • 38
    • 0030768059 scopus 로고    scopus 로고
    • Interference with the expression of a novel human polycomb protein, hPc2, results in cellular transformation and apoptosis
    • Satijn, D. P., Olson, D. J., van der Vlag, J., et al. (1997) Interference with the expression of a novel human polycomb protein, hPc2, results in cellular transformation and apoptosis. Mol. Cell Biol. 17, 6076-6086.
    • (1997) Mol. Cell Biol. , vol.17 , pp. 6076-6086
    • Satijn, D.P.1    Olson, D.J.2    Van Der Vlag, J.3
  • 39
    • 0032169599 scopus 로고    scopus 로고
    • Inhibition of Stat1-mediated gene activation by PIAS1
    • Liu, B., Liao, J., Rao, X., et al. (1998) Inhibition of Stat1-mediated gene activation by PIAS1. Proc. Nat. Acad. Sci. U.S.A. 95, 10,626-10,631.
    • (1998) Proc. Nat. Acad. Sci. U.S.A. , vol.95
    • Liu, B.1    Liao, J.2    Rao, X.3
  • 40
    • 0034789730 scopus 로고    scopus 로고
    • Involvement of PIAS1 in the sumoylation of tumor suppressor p53
    • Kahyo, T., Nishida, T., and Yasuda, H. (2001) Involvement of PIAS1 in the sumoylation of tumor suppressor p53. Mol. Cell 8, 713-718.
    • (2001) Mol. Cell , vol.8 , pp. 713-718
    • Kahyo, T.1    Nishida, T.2    Yasuda, H.3
  • 41
    • 0035576737 scopus 로고    scopus 로고
    • A new RING for SUMO: Wrestling transcriptional responses into nuclear bodieswith PIAS family E3 SUMO ligases
    • Jackson, P. K. (2001) A new RING for SUMO: wrestling transcriptional responses into nuclear bodieswith PIAS family E3 SUMO ligases. Genes Dev. 15, 3053-3058.
    • (2001) Genes Dev. , vol.15 , pp. 3053-3058
    • Jackson, P.K.1
  • 42
    • 0033537828 scopus 로고    scopus 로고
    • Identification of the enzyme required for activation of the small ubiquitin-like protein SUMO-1
    • Desterro, J. M., Rodríguez, M. S., Kemp, G. D., and Hay, R. T. (1999) Identification of the enzyme required for activation of the small ubiquitin-like protein SUMO-1. J. Biol. Chem. 274, 10,618-10,624.
    • (1999) J. Biol. Chem. , vol.274
    • Desterro, J.M.1    Rodríguez, M.S.2    Kemp, G.D.3    Hay, R.T.4
  • 43
    • 0033060826 scopus 로고    scopus 로고
    • Molecular cloning and characterization of human AOS1 and UBA2, components of the sentrin-activating enzyme complex
    • Gong, L., Li, B., Millas, S., and Yeh, E. T. (1999) Molecular cloning and characterization of human AOS1 and UBA2, components of the sentrin-activating enzyme complex. FEBS Lett. 448, 185-189.
    • (1999) FEBS Lett. , vol.448 , pp. 185-189
    • Gong, L.1    Li, B.2    Millas, S.3    Yeh, E.T.4
  • 46
    • 15844419144 scopus 로고    scopus 로고
    • Cloning and expression of human G/T mismatch-specific thymine-DNA glycosylase
    • Neddermann, P., Gallinari, P., Lettieri, T., et al. (1996) Cloning and expression of human G/T mismatch-specific thymine-DNA glycosylase. J. Biol. Chem. 271, 12,767-12,774.
    • (1996) J. Biol. Chem. , vol.271
    • Neddermann, P.1    Gallinari, P.2    Lettieri, T.3
  • 47
    • 0020016636 scopus 로고
    • DNA repair enzymes
    • Lindahl, T. (1982) DNA repair enzymes. Annu. Rev. Biochem. 51, 61-87.
    • (1982) Annu. Rev. Biochem. , vol.51 , pp. 61-87
    • Lindahl, T.1
  • 48
    • 0037086643 scopus 로고    scopus 로고
    • Modification of the human tymine-DNA-glycosylase by ubiquitin-like proteins facilitates enzymatic turnover
    • Hardeland, U., Steinacher, R., Jiricny J., and Schär, P. (2002) Modification of the human tymine-DNA-glycosylase by ubiquitin-like proteins facilitates enzymatic turnover. EMBO J. 21, 1456-1464.
    • (2002) EMBO J. , vol.21 , pp. 1456-1464
    • Hardeland, U.1    Steinacher, R.2    Jiricny, J.3    Schär, P.4
  • 49
    • 14044278774 scopus 로고    scopus 로고
    • Noncovalent SUMO-1 binding of thymine DNA glycosylase (TDG) is required for its SUMO-1 modification and colocalization with the promyelocytic leukemia protein (PML)
    • Takahashi, H., Hatakeyama, S., Saitoh, H., and Nakayama, K. I. (2005) Noncovalent SUMO-1 binding of thymine DNA glycosylase (TDG) is required for its SUMO-1 modification and colocalization with the promyelocytic leukemia protein (PML). J. Biol. Chem. 280, 5611-5621.
    • (2005) J. Biol. Chem. , vol.280 , pp. 5611-5621
    • Takahashi, H.1    Hatakeyama, S.2    Saitoh, H.3    Nakayama, K.I.4
  • 50
    • 0029736651 scopus 로고    scopus 로고
    • PIC 1, a novel ubiquitin-like protein which interacts with the PML component of a multiprotein complex that is disrupted in acute promyelocytic leukaemia
    • Boddy M. N., Howe, K., Etkin L. D., Solomon, E., and Freemont, P. S. (1996) PIC 1, a novel ubiquitin-like protein which interacts with the PML component of a multiprotein complex that is disrupted in acute promyelocytic leukaemia. Oncogene 13, 971-982.
    • (1996) Oncogene , vol.13 , pp. 971-982
    • Boddy, M.N.1    Howe, K.2    Etkin, L.D.3    Solomon, E.4    Freemont, P.S.5
  • 51
    • 0043194033 scopus 로고    scopus 로고
    • Repression of SMAD transcriptional activity by PIASy, an inhibitor of activated STAT
    • Long, J., Matsura, I., He, D., Wang, G., Shuai, K., and Liu, F. (2003) Repression of SMAD transcriptional activity by PIASy, an inhibitor of activated STAT. Proc. Natl. Acad. Sci. U.S.A. 100, 9791-9796.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 9791-9796
    • Long, J.1    Matsura, I.2    He, D.3    Wang, G.4    Shuai, K.5    Liu, F.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.