메뉴 건너뛰기




Volumn 44, Issue 9, 2016, Pages 3989-4004

The DBHS proteins SFPQ, NONO and PSPC1: A multipurpose molecular scaffold

Author keywords

[No Author keywords available]

Indexed keywords

DBHS PROTEIN; MOLECULAR SCAFFOLD; NONO PROTEIN; NUCLEAR PROTEIN; PSPC1 PROTEIN; SFPQ PROTEIN; UNCLASSIFIED DRUG; NONO PROTEIN, HUMAN; NUCLEAR MATRIX PROTEIN; OCTAMER TRANSCRIPTION FACTOR; PSPC1 PROTEIN, HUMAN; PTB ASSOCIATED SPLICING FACTOR; RNA BINDING PROTEIN; RNA SPLICING FACTOR;

EID: 84971241637     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkw271     Document Type: Review
Times cited : (214)

References (178)
  • 1
    • 0027305376 scopus 로고
    • Purification and cDNA cloning of HeLa cell p54nrb, a nuclear protein with two RNA recognition motifs and extensive homology to human splicing factor PSF and Drosophila NONA/BJ6
    • Dong, B., Horowitz, D.S., Kobayashi, R., Krainer, A.R. (1993) Purification and cDNA cloning of HeLa cell p54nrb, a nuclear protein with two RNA recognition motifs and extensive homology to human splicing factor PSF and Drosophila NONA/BJ6. Nucleic Acids Res., 21, 4085-4092.
    • (1993) Nucleic Acids Res , vol.21 , pp. 4085-4092
    • Dong, B.1    Horowitz, D.S.2    Kobayashi, R.3    Krainer, A.R.4
  • 2
    • 84957537176 scopus 로고    scopus 로고
    • Caenorhabditis elegans NONO-1: Insights into DBHS protein structure, architecture and function
    • Knott, G.J., Lee, M., Passon, D.M., Fox, A.H., Bond, C.S. (2015) Caenorhabditis elegans NONO-1: Insights into DBHS protein structure, architecture and function. Protein Sci., 24, 2033-2043.
    • (2015) Protein Sci , vol.24 , pp. 2033-2043
    • Knott, G.J.1    Lee, M.2    Passon, D.M.3    Fox, A.H.4    Bond, C.S.5
  • 3
    • 0037032415 scopus 로고    scopus 로고
    • PSF and p54(nrb)/NonO-multi-functional nuclear proteins
    • Shav-Tal, Y., Zipori, D. (2002) PSF and p54(nrb)/NonO-multi-functional nuclear proteins. FEBS Lett., 531, 109-114.
    • (2002) FEBS Lett , vol.531 , pp. 109-114
    • Shav-Tal, Y.1    Zipori, D.2
  • 4
    • 69949132008 scopus 로고    scopus 로고
    • Paraspeckles: Nuclear bodies built on long noncoding RNA
    • Bond, C.S., Fox, A.H. (2009) Paraspeckles: nuclear bodies built on long noncoding RNA. J. Cell. Biol., 186, 637-644.
    • (2009) J. Cell. Biol , vol.186 , pp. 637-644
    • Bond, C.S.1    Fox, A.H.2
  • 5
    • 77958181349 scopus 로고    scopus 로고
    • Paraspeckles cold spring harbor
    • Fox, A.H., Lamond, A.I. (2010) Paraspeckles. Cold Spring Harbor Perspect. Biol., 2, a000687.
    • (2010) Perspect. Biol , vol.2 , pp. a000687
    • Fox, A.H.1    Lamond, A.I.2
  • 6
    • 84894091178 scopus 로고    scopus 로고
    • The RNA/DNA-binding protein PSF relocates to cell membrane and contributes cells' sensitivity to antitumor drug, doxorubicin
    • Ren, S., She, M., Li, M., Zhou, Q., Liu, R., Lu, H., Yang, C., Xiong, D. (2014) The RNA/DNA-binding protein PSF relocates to cell membrane and contributes cells' sensitivity to antitumor drug, doxorubicin. Cytometry A, 85, 231-241.
    • (2014) Cytometry A , vol.85 , pp. 231-241
    • Ren, S.1    She, M.2    Li, M.3    Zhou, Q.4    Liu, R.5    Lu, H.6    Yang, C.7    Xiong, D.8
  • 7
    • 84926149481 scopus 로고    scopus 로고
    • Interaction and colocalization of HERMES/RBPMS with NonO, PSF, G3BP1 in neuronal cytoplasmic RNP granules in mouse retinal line cells
    • Furukawa, M.T., Sakamoto, H., Inoue, K. (2015) Interaction and colocalization of HERMES/RBPMS with NonO, PSF, G3BP1 in neuronal cytoplasmic RNP granules in mouse retinal line cells. Genes Cells, 20, 257-266.
    • (2015) Genes Cells , vol.20 , pp. 257-266
    • Furukawa, M.T.1    Sakamoto, H.2    Inoue, K.3
  • 10
    • 84873521914 scopus 로고    scopus 로고
    • RRM-RNA Recognition: NMR or crystallography.and new findings
    • Daubner, G.M., Clery, A., Allain, F.H. (2013) RRM-RNA recognition: NMR or crystallography.and new findings. Curr. Opin. Struct. Biol., 23, 100-108.
    • (2013) Curr. Opin. Struct. Biol , vol.23 , pp. 100-108
    • Daubner, G.M.1    Clery, A.2    Allain, F.H.3
  • 11
    • 84859467060 scopus 로고    scopus 로고
    • Structure of the heterodimer of human NONO and paraspeckle protein component 1 and analysis of its role in subnuclear body formation
    • Passon, D.M., Lee, M., Rackham, O., Stanley, W.A., Sadowska, A., Filipovska, A., Fox, A.H., Bond, C.S. (2012) Structure of the heterodimer of human NONO and paraspeckle protein component 1 and analysis of its role in subnuclear body formation. Proc. Natl. Acad. Sci. U.S.A., 109, 4846-4850.
    • (2012) Proc. Natl. Acad. Sci. U.S.A , vol.109 , pp. 4846-4850
    • Passon, D.M.1    Lee, M.2    Rackham, O.3    Stanley, W.A.4    Sadowska, A.5    Filipovska, A.6    Fox, A.H.7    Bond, C.S.8
  • 12
    • 84930505834 scopus 로고    scopus 로고
    • The structure of human SFPQ reveals a coiled-coil mediated polymer essential for functional aggregation in gene regulation
    • Lee, M., Sadowska, A., Bekere, I., Ho, D., Gully, B.S., Lu, Y., Iyer, K.S., Trewhella, J., Fox, A.H., Bond, C.S. (2015) The structure of human SFPQ reveals a coiled-coil mediated polymer essential for functional aggregation in gene regulation. Nucleic Acids Res., 43, 3826-3840.
    • (2015) Nucleic Acids Res , vol.43 , pp. 3826-3840
    • Lee, M.1    Sadowska, A.2    Bekere, I.3    Ho, D.4    Gully, B.S.5    Lu, Y.6    Iyer, K.S.7    Trewhella, J.8    Fox, A.H.9    Bond, C.S.10
  • 17
    • 27644541914 scopus 로고    scopus 로고
    • P54nrb forms a heterodimer with PSP1 that localizes to paraspeckles in an RNA-dependent manner
    • Fox, A.H., Bond, C.S., Lamond, A.I. (2005) P54nrb forms a heterodimer with PSP1 that localizes to paraspeckles in an RNA-dependent manner. Mol. Biol Cell, 16, 5304-5315.
    • (2005) Mol. Biol Cell , vol.16 , pp. 5304-5315
    • Fox, A.H.1    Bond, C.S.2    Lamond, A.I.3
  • 18
    • 33747609562 scopus 로고    scopus 로고
    • PSPC1, NONO, SFPQ are expressed in mouse Sertoli cells and may function as coregulators of androgen receptor-mediated transcription
    • Kuwahara, S., Ikei, A., Taguchi, Y., Tabuchi, Y., Fujimoto, N., Obinata, M., Uesugi, S., Kurihara, Y. (2006) PSPC1, NONO, SFPQ are expressed in mouse Sertoli cells and may function as coregulators of androgen receptor-mediated transcription. Biol. Reprod., 75, 352-359.
    • (2006) Biol. Reprod , vol.75 , pp. 352-359
    • Kuwahara, S.1    Ikei, A.2    Taguchi, Y.3    Tabuchi, Y.4    Fujimoto, N.5    Obinata, M.6    Uesugi, S.7    Kurihara, Y.8
  • 19
    • 80955123973 scopus 로고    scopus 로고
    • Construct optimization for studying protein complexes: Obtaining diffraction-quality crystals of the pseudosymmetric PSPC1-NONO heterodimer
    • Lee, M., Passon, D.M., Hennig, S., Fox, A.H., Bond, C.S. (2011) Construct optimization for studying protein complexes: obtaining diffraction-quality crystals of the pseudosymmetric PSPC1-NONO heterodimer. Acta Crystallogr. Sect. D Biol. Crystallogr., 67, 981-987.
    • (2011) Acta Crystallogr. Sect. D Biol. Crystallogr , vol.67 , pp. 981-987
    • Lee, M.1    Passon, D.M.2    Hennig, S.3    Fox, A.H.4    Bond, C.S.5
  • 20
    • 0142011032 scopus 로고    scopus 로고
    • The Hrp65 self-interaction is mediated by an evolutionarily conserved domain and is required for nuclear import of Hrp65 isoforms that lack a nuclear localization signal
    • Kiesler, E., Miralles, F., Ostlund Farrants, A.K., Visa, N. (2003) The Hrp65 self-interaction is mediated by an evolutionarily conserved domain and is required for nuclear import of Hrp65 isoforms that lack a nuclear localization signal. J. Cell Sci., 116, 3949-3956.
    • (2003) J. Cell Sci , vol.116 , pp. 3949-3956
    • Kiesler, E.1    Miralles, F.2    Ostlund Farrants, A.K.3    Visa, N.4
  • 21
    • 0035298137 scopus 로고    scopus 로고
    • Molecular characterization of Ct-hrp65: Identification of two novel isoforms originated by alternative splicing
    • Miralles, F., Visa, N. (2001) Molecular characterization of Ct-hrp65: identification of two novel isoforms originated by alternative splicing. Exp. Cell Res., 264, 284-295.
    • (2001) Exp. Cell Res , vol.264 , pp. 284-295
    • Miralles, F.1    Visa, N.2
  • 22
    • 72149107079 scopus 로고    scopus 로고
    • Hnrnp M interacts with PSF and p54(nrb) and co-localizes within defined nuclear structures
    • Marko, M., Leichter, M., Patrinou-Georgoula, M., Guialis, A. (2010) hnRNP M interacts with PSF and p54(nrb) and co-localizes within defined nuclear structures. Exp. Cell Res., 316, 390-400.
    • (2010) Exp. Cell Res , vol.316 , pp. 390-400
    • Marko, M.1    Leichter, M.2    Patrinou-Georgoula, M.3    Guialis, A.4
  • 23
    • 84964315984 scopus 로고    scopus 로고
    • Double-strand break repair deficiency in NONO knockout murine embryonic fibroblasts and compensation by spontaneous upregulation of the PSPC1 paralog
    • Li, S., Li, Z., Shu, F.J., Xiong, H., Phillips, A.C., Dynan, W.S. (2014) Double-strand break repair deficiency in NONO knockout murine embryonic fibroblasts and compensation by spontaneous upregulation of the PSPC1 paralog. Nucleic Acids Res., 42, 9771-9780.
    • (2014) Nucleic Acids Res , vol.42 , pp. 9771-9780
    • Li, S.1    Li, Z.2    Shu, F.J.3    Xiong, H.4    Phillips, A.C.5    Dynan, W.S.6
  • 24
    • 84901275965 scopus 로고    scopus 로고
    • Paraspeckle protein 1 (PSPC1) is involved in the cisplatin induced DNA damage response-role in G1/S checkpoint
    • Gao, X., Kong, L., Lu, X., Zhang, G., Chi, L., Jiang, Y., Wu, Y., Yan, C., Duerksen-Hughes, P., Zhu, X. et al. (2014) Paraspeckle protein 1 (PSPC1) is involved in the cisplatin induced DNA damage response-role in G1/S checkpoint. PLoS One, 9, e97174.
    • (2014) PLoS One , vol.9 , pp. e97174
    • Gao, X.1    Kong, L.2    Lu, X.3    Zhang, G.4    Chi, L.5    Jiang, Y.6    Wu, Y.7    Yan, C.8    Duerksen-Hughes, P.9    Zhu, X.10
  • 26
    • 0026595254 scopus 로고
    • The dissonance mutation at the No-on-transient-A locus of Drosophila-melanogaster-genetic-control of courtship song and visual behaviors by a protein with putative Rna-binding motifs
    • Rendahl, K.G., Jones, K.R., Kulkarni, S.J., Bagully, S.H., Hall, J.C. (1992) The dissonance mutation at the No-on-transient-a locus of Drosophila-melanogaster-genetic-control of courtship song and visual behaviors by a protein with putative Rna-binding motifs. J. Neurosci., 12, 390-407.
    • (1992) J. Neurosci , vol.12 , pp. 390-407
    • Rendahl, K.G.1    Jones, K.R.2    Kulkarni, S.J.3    Bagully, S.H.4    Hall, J.C.5
  • 27
    • 34248579021 scopus 로고    scopus 로고
    • Whitesnake/sfpq is required for cell survival and neuronal development in the zebrafish
    • Lowery, L.A., Rubin, J., Sive, H. (2007) Whitesnake/sfpq is required for cell survival and neuronal development in the zebrafish. Dev. Dyn., 236, 1347-1357.
    • (2007) Dev. Dyn , vol.236 , pp. 1347-1357
    • Lowery, L.A.1    Rubin, J.2    Sive, H.3
  • 28
    • 17444424974 scopus 로고    scopus 로고
    • The structure of alpha-helical coiled coils
    • Lupas, A.N., Gruber, M. (2005) The structure of alpha-helical coiled coils. Adv. Protein Chem., 70, 37-78.
    • (2005) Adv. Protein Chem , vol.70 , pp. 37-78
    • Lupas, A.N.1    Gruber, M.2
  • 29
    • 84947425549 scopus 로고    scopus 로고
    • A conserved charged single alpha-helix with a putative steric role in paraspeckle formation
    • Dobson, L., Nyitray, L., Gaspari, Z. (2015) A conserved charged single alpha-helix with a putative steric role in paraspeckle formation. RNA, 21, 2023-2029.
    • (2015) RNA , vol.21 , pp. 2023-2029
    • Dobson, L.1    Nyitray, L.2    Gaspari, Z.3
  • 30
    • 0037311925 scopus 로고    scopus 로고
    • Centrosomes: Coiled-Coils organize the cell center
    • Salisbury, J.L. (2003) Centrosomes: coiled-coils organize the cell center. Curr. Biol., 13, R88-R90.
    • (2003) Curr. Biol , vol.13 , pp. R88-R90
    • Salisbury, J.L.1
  • 32
    • 0027245959 scopus 로고
    • Cloning and characterization of PSF, a novel Pre-mRNA splicing factor
    • Patton, J.G., Porro, E.B., Galceran, J., Tempst, P., Nadal-Ginard, B. (1993) Cloning and characterization of PSF, a novel pre-mRNA splicing factor. Genes Dev., 7, 393-406.
    • (1993) Genes Dev , vol.7 , pp. 393-406
    • Patton, J.G.1    Porro, E.B.2    Galceran, J.3    Tempst, P.4    Nadal-Ginard, B.5
  • 33
    • 0027328533 scopus 로고
    • NonO, a Non-POU-Domain-Containing, octamer-binding protein, is the mammalian homolog of Drosophila nonAdiss
    • Yang, Y.S., Hanke, J.H., Carayannopoulos, L., Craft, C.M., Capra, J.D., Tucker, P.W. (1993) NonO, a non-POU-domain-containing, octamer-binding protein, is the mammalian homolog of Drosophila nonAdiss. Mol. Cell. Biol., 13, 5593-5603.
    • (1993) Mol. Cell. Biol , vol.13 , pp. 5593-5603
    • Yang, Y.S.1    Hanke, J.H.2    Carayannopoulos, L.3    Craft, C.M.4    Capra, J.D.5    Tucker, P.W.6
  • 34
    • 0027401652 scopus 로고
    • Purification and characterization of a DNA-binding heterodimer of 52 and 100 kDa from HeLa cells
    • Zhang, W.W., Zhang, L.X., Busch, R.K., Farres, J., Busch, H. (1993) Purification and characterization of a DNA-binding heterodimer of 52 and 100 kDa from HeLa cells. Biochem. J., 290, 267-272.
    • (1993) Biochem. J , vol.290 , pp. 267-272
    • Zhang, W.W.1    Zhang, L.X.2    Busch, R.K.3    Farres, J.4    Busch, H.5
  • 36
    • 0029991768 scopus 로고    scopus 로고
    • The transcription factor Spi-1/PU.1 binds RNA and interferes with the RNA-binding protein p54nrb
    • Hallier, M., Tavitian, A., Moreau-Gachelin, F. (1996) The transcription factor Spi-1/PU.1 binds RNA and interferes with the RNA-binding protein p54nrb. J. Biol. Chem., 271, 11177-11181.
    • (1996) J. Biol. Chem , vol.271 , pp. 11177-11181
    • Hallier, M.1    Tavitian, A.2    Moreau-Gachelin, F.3
  • 37
    • 0031039425 scopus 로고    scopus 로고
    • The intracisternal A-particle proximal enhancer-binding protein activates transcription and is identical to the RNA-and DNA-binding protein p54nrb/NonO
    • Basu, A., Dong, B., Krainer, A.R., Howe, C.C. (1997) The intracisternal A-particle proximal enhancer-binding protein activates transcription and is identical to the RNA-and DNA-binding protein p54nrb/NonO. Mol. Cell. Biol., 17, 677-686.
    • (1997) Mol. Cell. Biol , vol.17 , pp. 677-686
    • Basu, A.1    Dong, B.2    Krainer, A.R.3    Howe, C.C.4
  • 38
    • 0035943347 scopus 로고    scopus 로고
    • The fate of dsRNA in the nucleus: A p54(nrb)-containing complex retention of promiscuously mediates the nuclear A-to-I edited RNAs
    • Zhang, Z., Carmichael, G.G. (2001) The fate of dsRNA in the nucleus: A p54(nrb)-containing complex retention of promiscuously mediates the nuclear A-to-I edited RNAs. Cell, 106, 465-475.
    • (2001) Cell , vol.106 , pp. 465-475
    • Zhang, Z.1    Carmichael, G.G.2
  • 39
    • 70349269113 scopus 로고    scopus 로고
    • Transcriptional activity of the murine retinol-binding protein gene is regulated by a multiprotein complex containing HMGA1, p54 nrb/NonO, protein-associated splicing factor (PSF) and steroidogenic factor 1 (SF1)/liver receptor homologue 1 (LRH-1)
    • Bianconcini, A., Lupo, A., Capone, S., Quadro, L., Monti, M., Zurlo, D., Fucci, A., Sabatino, L., Brunetti, A., Chiefari, E. et al. (2009) Transcriptional activity of the murine retinol-binding protein gene is regulated by a multiprotein complex containing HMGA1, p54 nrb/NonO, protein-associated splicing factor (PSF) and steroidogenic factor 1 (SF1)/liver receptor homologue 1 (LRH-1). Int. J. Biochem. Cell Biol., 41, 2189-2203.
    • (2009) Int. J. Biochem. Cell Biol , vol.41 , pp. 2189-2203
    • Bianconcini, A.1    Lupo, A.2    Capone, S.3    Quadro, L.4    Monti, M.5    Zurlo, D.6    Fucci, A.7    Sabatino, L.8    Brunetti, A.9    Chiefari, E.10
  • 40
    • 77951296232 scopus 로고    scopus 로고
    • Identification of protein interaction regions of VINC/NEAT1/Men epsilon RNA
    • Murthy, U.M., Rangarajan, P.N. (2010) Identification of protein interaction regions of VINC/NEAT1/Men epsilon RNA. FEBS Lett., 584, 1531-1535.
    • (2010) FEBS Lett , vol.584 , pp. 1531-1535
    • Murthy, U.M.1    Rangarajan, P.N.2
  • 42
    • 50649093361 scopus 로고    scopus 로고
    • Poly(ADP-ribose) binds to the splicing factor ASF/SF2 and regulates its phosphorylation by DNA topoisomerase i
    • Malanga, M., Czubaty, A., Girstun, A., Staron, K., Althaus, F.R. (2008) Poly(ADP-ribose) binds to the splicing factor ASF/SF2 and regulates its phosphorylation by DNA topoisomerase I. J. Biol. Chem., 283, 19991-19998.
    • (2008) J. Biol. Chem , vol.283 , pp. 19991-19998
    • Malanga, M.1    Czubaty, A.2    Girstun, A.3    Staron, K.4    Althaus, F.R.5
  • 44
    • 2442435550 scopus 로고    scopus 로고
    • P54(nrb) associates with the 5 ' splice site within large transcription/splicing complexes
    • Kameoka, S., Duque, P., Konarska, M.M. (2004) P54(nrb) associates with the 5 ' splice site within large transcription/splicing complexes. EMBO J., 23, 1782-1791.
    • (2004) EMBO J , vol.23 , pp. 1782-1791
    • Kameoka, S.1    Duque, P.2    Konarska, M.M.3
  • 45
    • 80855123708 scopus 로고    scopus 로고
    • PSF suppresses tau exon 10 inclusion by interacting with a stem-loop structure downstream of exon 10
    • Ray, P., Kar, A., Fushimi, K., Havlioglu, N., Chen, X., Wu, J.Y. (2011) PSF suppresses tau exon 10 inclusion by interacting with a stem-loop structure downstream of exon 10. J. Mol. Neurosci., 45, 453-466.
    • (2011) J. Mol. Neurosci , vol.45 , pp. 453-466
    • Ray, P.1    Kar, A.2    Fushimi, K.3    Havlioglu, N.4    Chen, X.5    Wu, J.Y.6
  • 46
    • 33751000460 scopus 로고    scopus 로고
    • Binding of the polypyrimidine tract-binding protein-associated splicing factor (PSF) to the hepatitis delta virus RNA
    • Greco-Stewart, V.S., Thibault, C.S.L., Pelchat, M. (2006) Binding of the polypyrimidine tract-binding protein-associated splicing factor (PSF) to the hepatitis delta virus RNA. Virology, 356, 35-44.
    • (2006) Virology , vol.356 , pp. 35-44
    • Greco-Stewart, V.S.1    Thibault, C.S.L.2    Pelchat, M.3
  • 47
    • 84879745156 scopus 로고    scopus 로고
    • STAU1 binding 3' UTR IRAlus complements nuclear retention to protect cells from PKR-mediated translational shutdown
    • Elbarbary, R.A., Li, W., Tian, B., Maquat, L.E. (2013) STAU1 binding 3' UTR IRAlus complements nuclear retention to protect cells from PKR-mediated translational shutdown. Genes Dev., 27, 1495-1510.
    • (2013) Genes Dev , vol.27 , pp. 1495-1510
    • Elbarbary, R.A.1    Li, W.2    Tian, B.3    Maquat, L.E.4
  • 50
    • 78651316335 scopus 로고    scopus 로고
    • The splicing-factor related protein SFPQ/PSF interacts with RAD51D and is necessary for homology-directed repair and sister chromatid cohesion
    • Rajesh, C., Baker, D.K., Pierce, A.J., Pittman, D.L. (2011) The splicing-factor related protein SFPQ/PSF interacts with RAD51D and is necessary for homology-directed repair and sister chromatid cohesion. Nucleic Acids Res., 39, 132-145.
    • (2011) Nucleic Acids Res , vol.39 , pp. 132-145
    • Rajesh, C.1    Baker, D.K.2    Pierce, A.J.3    Pittman, D.L.4
  • 51
    • 73449109487 scopus 로고    scopus 로고
    • Analysis of arginine and lysine methylation utilizing peptide separations at neutral pH and electron transfer dissociation mass spectrometry
    • Snijders, A.P., Hung, M.L., Wilson, S.A., Dickman, M.J. (2010) Analysis of arginine and lysine methylation utilizing peptide separations at neutral pH and electron transfer dissociation mass spectrometry. J. Am. Soc. Mass Spectrom., 21, 88-96.
    • (2010) J. Am. Soc. Mass Spectrom , vol.21 , pp. 88-96
    • Snijders, A.P.1    Hung, M.L.2    Wilson, S.A.3    Dickman, M.J.4
  • 52
    • 84884906084 scopus 로고    scopus 로고
    • Site-specific characterization of the Asp-and Glu-ADP-ribosylated proteome
    • Zhang, Y., Wang, J., Ding, M., Yu, Y. (2013) Site-specific characterization of the Asp-and Glu-ADP-ribosylated proteome. Nat. Methods, 10, 981-984.
    • (2013) Nat. Methods , vol.10 , pp. 981-984
    • Zhang, Y.1    Wang, J.2    Ding, M.3    Yu, Y.4
  • 53
    • 84949196425 scopus 로고    scopus 로고
    • Transcriptional regulators form diverse groups with context-dependent regulatory functions
    • Stampfel, G., Kazmar, T., Frank, O., Wienerroither, S., Reiter, F., Stark, A. (2015) Transcriptional regulators form diverse groups with context-dependent regulatory functions. Nature, 528, 147-151.
    • (2015) Nature , vol.528 , pp. 147-151
    • Stampfel, G.1    Kazmar, T.2    Frank, O.3    Wienerroither, S.4    Reiter, F.5    Stark, A.6
  • 54
    • 17144407579 scopus 로고    scopus 로고
    • Identification and characterization of the protein-associated splicing factor as a negative co-regulator of the progesterone receptor
    • Dong, X., Shylnova, O., Challis, J.R., Lye, S.J. (2005) Identification and characterization of the protein-associated splicing factor as a negative co-regulator of the progesterone receptor. J. Biol. Chem., 280, 13329-13340.
    • (2005) J. Biol. Chem , vol.280 , pp. 13329-13340
    • Dong, X.1    Shylnova, O.2    Challis, J.R.3    Lye, S.J.4
  • 55
    • 34347332370 scopus 로고    scopus 로고
    • Transcriptional activity of androgen receptor is modulated by two RNA splicing factors
    • Dong, X., Sweet, J., Challis, J.R., Brown, T., Lye, S.J. (2007) Transcriptional activity of androgen receptor is modulated by two RNA splicing factors, PSF and p54nrb. Mol. Cell. Biol., 27, 4863-4875.
    • (2007) PSF and p54nrb. Mol. Cell. Biol , vol.27 , pp. 4863-4875
    • Dong, X.1    Sweet, J.2    Challis, J.R.3    Brown, T.4    Lye, S.J.5
  • 56
    • 67749145286 scopus 로고    scopus 로고
    • P54Nrb is a transcriptional corepressor of the progesterone receptor that modulates transcription of the labor-associated gene, connexin 43 (Gja1
    • Dong, X., Yu, C., Shynlova, O., Challis, J.R., Rennie, P.S., Lye, S.J. (2009) p54nrb is a transcriptional corepressor of the progesterone receptor that modulates transcription of the labor-associated gene, connexin 43 (Gja1). Mol. Endocrinol., 23, 1147-1160.
    • (2009) Mol. Endocrinol , vol.23 , pp. 1147-1160
    • Dong, X.1    Yu, C.2    Shynlova, O.3    Challis, J.R.4    Rennie, P.S.5    Lye, S.J.6
  • 57
    • 0035106562 scopus 로고    scopus 로고
    • PSF is a novel corepressor that mediates its effect through Sin3A and the DNA binding domain of nuclear hormone receptors
    • Mathur, M., Tucker, P.W., Samuels, H.H. (2001) PSF is a novel corepressor that mediates its effect through Sin3A and the DNA binding domain of nuclear hormone receptors. Mol. Cell. Biol., 21, 2298-2311.
    • (2001) Mol. Cell. Biol , vol.21 , pp. 2298-2311
    • Mathur, M.1    Tucker, P.W.2    Samuels, H.H.3
  • 58
    • 0036212259 scopus 로고    scopus 로고
    • Transcriptional activation of human CYP17 in H295R adrenocortical cells depends on complex formation among p54(nrb)/NonO, protein-associated splicing factor, SF-1, a complex that also participates in repression of transcription
    • Sewer, M.B., Nguyen, V.Q., Huang, C.J., Tucker, P.W., Kagawa, N., Waterman, M.R. (2002) Transcriptional activation of human CYP17 in H295R adrenocortical cells depends on complex formation among p54(nrb)/NonO, protein-associated splicing factor, SF-1, a complex that also participates in repression of transcription. Endocrinology, 143, 1280-1290.
    • (2002) Endocrinology , vol.143 , pp. 1280-1290
    • Sewer, M.B.1    Nguyen, V.Q.2    Huang, C.J.3    Tucker, P.W.4    Kagawa, N.5    Waterman, M.R.6
  • 59
    • 0036933009 scopus 로고    scopus 로고
    • Transcriptional complexes at the CYP17 CRS
    • Sewer, M.B., Waterman, M.R. (2002) Transcriptional complexes at the CYP17 CRS. Endocr. Res., 28, 551-558.
    • (2002) Endocr. Res , vol.28 , pp. 551-558
    • Sewer, M.B.1    Waterman, M.R.2
  • 60
    • 0036228795 scopus 로고    scopus 로고
    • Adrenocorticotropin/cyclic adenosine 3', 5'-monophosphate-mediated transcription of the human CYP17 gene in the adrenal cortex is dependent on phosphatase activity
    • Sewer, M.B., Waterman, M.R. (2002) Adrenocorticotropin/cyclic adenosine 3', 5'-monophosphate-mediated transcription of the human CYP17 gene in the adrenal cortex is dependent on phosphatase activity. Endocrinology, 143, 1769-1777.
    • (2002) Endocrinology , vol.143 , pp. 1769-1777
    • Sewer, M.B.1    Waterman, M.R.2
  • 61
    • 79959366611 scopus 로고    scopus 로고
    • A molecular mechanism for circadian clock negative feedback
    • Duong, H.A., Robles, M.S., Knutti, D., Weitz, C.J. (2011) A molecular mechanism for circadian clock negative feedback. Science, 332, 1436-1439.
    • (2011) Science , vol.332 , pp. 1436-1439
    • Duong, H.A.1    Robles, M.S.2    Knutti, D.3    Weitz, C.J.4
  • 62
    • 0034463165 scopus 로고    scopus 로고
    • Polypyrimidine tract-binding protein-associated splicing factor is a negative regulator of transcriptional activity of the porcine p450scc insulin-like growth factor response element
    • Urban, R.J., Bodenburg, Y., Kurosky, A., Wood, T.G., Gasic, S. (2000) Polypyrimidine tract-binding protein-associated splicing factor is a negative regulator of transcriptional activity of the porcine p450scc insulin-like growth factor response element. Mol. Endocrinol., 14, 774-782.
    • (2000) Mol. Endocrinol , vol.14 , pp. 774-782
    • Urban, R.J.1    Bodenburg, Y.2    Kurosky, A.3    Wood, T.G.4    Gasic, S.5
  • 63
    • 0036710172 scopus 로고    scopus 로고
    • NH2 terminus of PTB-associated splicing factor binds to the porcine P450scc IGF-I response element
    • Urban, R.J., Bodenburg, Y.H., Wood, T.G. (2002) NH2 terminus of PTB-associated splicing factor binds to the porcine P450scc IGF-I response element. Am. J. Physiol. Endocrinol. Metab., 283, E423-427.
    • (2002) Am. J. Physiol. Endocrinol. Metab , vol.283 , pp. E423-427
    • Urban, R.J.1    Bodenburg, Y.H.2    Wood, T.G.3
  • 64
    • 0347635470 scopus 로고    scopus 로고
    • Binding of mouse VL30 retrotransposon RNA to PSF protein induces genes repressed by PSF: Effects on steroidogenesis and oncogenesis
    • Song, X., Sui, A., Garen, A. (2004) Binding of mouse VL30 retrotransposon RNA to PSF protein induces genes repressed by PSF: effects on steroidogenesis and oncogenesis. Proc. Natl. Acad. Sci. U.S.A., 101, 621-626.
    • (2004) Proc. Natl. Acad. Sci. U.S.A , vol.101 , pp. 621-626
    • Song, X.1    Sui, A.2    Garen, A.3
  • 65
    • 24644431794 scopus 로고    scopus 로고
    • Roles of PSF protein and VL30 RNA in reversible gene regulation
    • Song, X., Sun, Y., Garen, A. (2005) Roles of PSF protein and VL30 RNA in reversible gene regulation. Proc. Natl. Acad. Sci. U.S.A., 102, 12189-12193.
    • (2005) Proc. Natl. Acad. Sci. U.S.A , vol.102 , pp. 12189-12193
    • Song, X.1    Sun, Y.2    Garen, A.3
  • 66
    • 80052548693 scopus 로고    scopus 로고
    • Rasd1 modulates the coactivator function of NonO in the cyclic AMP pathway
    • Ong, S.A., Tan, J.J., Tew, W.L., Chen, K.S. (2011) Rasd1 modulates the coactivator function of NonO in the cyclic AMP pathway. PLoS One, 6, e24401.
    • (2011) PLoS One , vol.6 , pp. e24401
    • Ong, S.A.1    Tan, J.J.2    Tew, W.L.3    Chen, K.S.4
  • 67
    • 27744565350 scopus 로고    scopus 로고
    • Functional analysis of the promoter of the mitochondrial phosphate carrier human gene: Identification of activator and repressor elements and their transcription factors
    • Iacobazzi, V., Infantino, V., Costanzo, P., Izzo, P., Palmieri, F. (2005) Functional analysis of the promoter of the mitochondrial phosphate carrier human gene: identification of activator and repressor elements and their transcription factors. Biochem. J., 391, 613-621.
    • (2005) Biochem. J , vol.391 , pp. 613-621
    • Iacobazzi, V.1    Infantino, V.2    Costanzo, P.3    Izzo, P.4    Palmieri, F.5
  • 68
    • 84893452948 scopus 로고    scopus 로고
    • Long noncoding RNA NEAT1-dependent SFPQ relocation from promoter region to paraspeckle mediates IL8 expression upon immune stimuli
    • Imamura, K., Imamachi, N., Akizuki, G., Kumakura, M., Kawaguchi, A., Nagata, K., Kato, A., Kawaguchi, Y., Sato, H., Yoneda, M. et al. (2014) Long noncoding RNA NEAT1-dependent SFPQ relocation from promoter region to paraspeckle mediates IL8 expression upon immune stimuli. Mol. Cell, 53, 393-406.
    • (2014) Mol. Cell , vol.53 , pp. 393-406
    • Imamura, K.1    Imamachi, N.2    Akizuki, G.3    Kumakura, M.4    Kawaguchi, A.5    Nagata, K.6    Kato, A.7    Kawaguchi, Y.8    Sato, H.9    Yoneda, M.10
  • 71
    • 84897911847 scopus 로고    scopus 로고
    • The transcription-splicing protein NonO/p54nrb and three NonO-interacting proteins bind to distal enhancer region and augment rhodopsin expression
    • Yadav, S.P., Hao, H., Yang, H.J., Kautzmann, M.A., Brooks, M., Nellissery, J., Klocke, B., Seifert, M., Swaroop, A. (2014) The transcription-splicing protein NonO/p54nrb and three NonO-interacting proteins bind to distal enhancer region and augment rhodopsin expression. Hum. Mol. Genet., 23, 2132-2144.
    • (2014) Hum. Mol. Genet , vol.23 , pp. 2132-2144
    • Yadav, S.P.1    Hao, H.2    Yang, H.J.3    Kautzmann, M.A.4    Brooks, M.5    Nellissery, J.6    Klocke, B.7    Seifert, M.8    Swaroop, A.9
  • 72
    • 84872863771 scopus 로고    scopus 로고
    • NonO binds to the CpG island of oct4 promoter and functions as a transcriptional activator of oct4 gene expression
    • Park, Y., Lee, J.M., Hwang, M.Y., Son, G.H., Geum, D. (2013) NonO binds to the CpG island of oct4 promoter and functions as a transcriptional activator of oct4 gene expression. Mol. Cell, 35, 61-69.
    • (2013) Mol. Cell , vol.35 , pp. 61-69
    • Park, Y.1    Lee, J.M.2    Hwang, M.Y.3    Son, G.H.4    Geum, D.5
  • 74
    • 56249117359 scopus 로고    scopus 로고
    • Interaction of SOCS3 with NonO attenuates IL-1beta-dependent MUC8 gene expression
    • Song, K.S., Kim, K., Chung, K.C., Seol, J.H., Yoon, J.H. (2008) Interaction of SOCS3 with NonO attenuates IL-1beta-dependent MUC8 gene expression. Biochem. Biophys. Res. Commun., 377, 946-951.
    • (2008) Biochem. Biophys. Res. Commun , vol.377 , pp. 946-951
    • Song, K.S.1    Kim, K.2    Chung, K.C.3    Seol, J.H.4    Yoon, J.H.5
  • 76
    • 64549121554 scopus 로고    scopus 로고
    • Pitx3 potentiates Nurr1 in dopamine neuron terminal differentiation through release of SMRT-mediated repression
    • Jacobs, F.M., van Erp, S., van der Linden, A.J., von Oerthel, L., Burbach, J.P., Smidt, M.P. (2009) Pitx3 potentiates Nurr1 in dopamine neuron terminal differentiation through release of SMRT-mediated repression. Development, 136, 531-540.
    • (2009) Development , vol.136 , pp. 531-540
    • Jacobs, F.M.1    Van Erp, S.2    Van Der Linden, A.J.3    Von Oerthel, L.4    Burbach, J.P.5    Smidt, M.P.6
  • 77
    • 84871885736 scopus 로고    scopus 로고
    • LMX1B is part of a transcriptional complex with PSPC1 and PSF
    • Hoekstra, E.J., Mesman, S., de Munnik, W.A., Smidt, M.P. (2013) LMX1B is part of a transcriptional complex with PSPC1 and PSF. PLoS One, 8, e53122.
    • (2013) PLoS One , vol.8 , pp. e53122
    • Hoekstra, E.J.1    Mesman, S.2    De Munnik, W.A.3    Smidt, M.P.4
  • 79
    • 0041630631 scopus 로고    scopus 로고
    • P54Nrb acts as a transcriptional coactivator for activation function 1 of the human androgen receptor
    • Ishitani, K., Yoshida, T., Kitagawa, H., Ohta, H., Nozawa, S., Kato, S. (2003) p54nrb acts as a transcriptional coactivator for activation function 1 of the human androgen receptor. Biochem. Biophys. Res. Commun., 306, 660-665.
    • (2003) Biochem. Biophys. Res. Commun , vol.306 , pp. 660-665
    • Ishitani, K.1    Yoshida, T.2    Kitagawa, H.3    Ohta, H.4    Nozawa, S.5    Kato, S.6
  • 80
    • 22144483767 scopus 로고    scopus 로고
    • A pp32-retinoblastoma protein complex modulates androgen receptor-mediated transcription and associates with components of the splicing machinery
    • Adegbola, O., Pasternack, G.R. (2005) A pp32-retinoblastoma protein complex modulates androgen receptor-mediated transcription and associates with components of the splicing machinery. Biochem. Biophys. Res. Commun., 334, 702-708.
    • (2005) Biochem. Biophys. Res. Commun , vol.334 , pp. 702-708
    • Adegbola, O.1    Pasternack, G.R.2
  • 81
    • 0036715543 scopus 로고    scopus 로고
    • Splicing and transcription-associated proteins PSF and p54(nrb)/NonO bind to the RNA polymerase II CTD
    • Emili, A., Shales, M., McCracken, S., Xie, W.J., Tucker, P.W., Kobayashi, R., Blencowe, B.J., Ingles, C.J. (2002) Splicing and transcription-associated proteins PSF and p54(nrb)/NonO bind to the RNA polymerase II CTD. RNA, 8, 1102-1111.
    • (2002) RNA , vol.8 , pp. 1102-1111
    • Emili, A.1    Shales, M.2    McCracken, S.3    Xie, W.J.4    Tucker, P.W.5    Kobayashi, R.6    Blencowe, B.J.7    Ingles, C.J.8
  • 83
    • 23944495664 scopus 로고    scopus 로고
    • The growing pre-mRNA recruits actin and chromatin-modifying factors to transcriptionally active genes
    • Sjolinder, M., Bjork, P., Soderberg, E., Sabri, N., Farrants, A.K.O., Visa, N. (2005) The growing pre-mRNA recruits actin and chromatin-modifying factors to transcriptionally active genes. Genes Dev., 19, 1871-1884.
    • (2005) Genes Dev , vol.19 , pp. 1871-1884
    • Sjolinder, M.1    Bjork, P.2    Soderberg, E.3    Sabri, N.4    Farrants, A.K.O.5    Visa, N.6
  • 84
    • 34447550769 scopus 로고    scopus 로고
    • The multifunctional protein p54nrb/PSF recruits the exonuclease XRN2 to facilitate pre-mRNA 3' processing and transcription termination
    • Kaneko, S., Rozenblatt-Rosen, O., Meyerson, M., Manley, J.L. (2007) The multifunctional protein p54nrb/PSF recruits the exonuclease XRN2 to facilitate pre-mRNA 3' processing and transcription termination. Genes Dev., 21, 1779-1789.
    • (2007) Genes Dev , vol.21 , pp. 1779-1789
    • Kaneko, S.1    Rozenblatt-Rosen, O.2    Meyerson, M.3    Manley, J.L.4
  • 85
    • 84860725581 scopus 로고    scopus 로고
    • Functional coupling of transcription and splicing
    • Montes, M., Becerra, S., Sanchez-Alvarez, M., Sune, C. (2012) Functional coupling of transcription and splicing. Gene, 501, 104-117.
    • (2012) Gene , vol.501 , pp. 104-117
    • Montes, M.1    Becerra, S.2    Sanchez-Alvarez, M.3    Sune, C.4
  • 87
    • 0028360767 scopus 로고
    • A novel set of spliceosome-associated proteins and the essential splicing factor PSF bind stably to pre-mRNA prior to catalytic step II of the splicing reaction
    • Gozani, O., Patton, J.G., Reed, R. (1994) A novel set of spliceosome-associated proteins and the essential splicing factor PSF bind stably to pre-mRNA prior to catalytic step II of the splicing reaction. EMBO J., 13, 3356-3367.
    • (1994) EMBO J , vol.13 , pp. 3356-3367
    • Gozani, O.1    Patton, J.G.2    Reed, R.3
  • 88
    • 0031760528 scopus 로고    scopus 로고
    • The snRNP-free U1A (SF-A) complex(es): Identification of the largest subunit as PSF, the polypyrimidine-tract binding protein-associated splicing factor
    • Lutz, C.S., Cooke, C., O'Connor, J.P., Kobayashi, R., Alwine, J.C. (1998) The snRNP-free U1A (SF-A) complex(es): identification of the largest subunit as PSF, the polypyrimidine-tract binding protein-associated splicing factor. RNA, 4, 1493-1499.
    • (1998) RNA , vol.4 , pp. 1493-1499
    • Lutz, C.S.1    Cooke, C.2    O'Connor, J.P.3    Kobayashi, R.4    Alwine, J.C.5
  • 89
    • 33748987646 scopus 로고    scopus 로고
    • The splicing factor PSF is part of a large complex that assembles in the absence of pre-mRNA and contains all five snRNPs
    • Peng, R., Hawkins, I., Link, A.J., Patton, J.G. (2006) The splicing factor PSF is part of a large complex that assembles in the absence of pre-mRNA and contains all five snRNPs. RNA Biol., 3, 69-76.
    • (2006) RNA Biol , vol.3 , pp. 69-76
    • Peng, R.1    Hawkins, I.2    Link, A.J.3    Patton, J.G.4
  • 90
    • 77957377260 scopus 로고    scopus 로고
    • Phosphorylation-dependent regulation of PSF by GSK3 controls CD45 alternative splicing
    • Heyd, F., Lynch, K.W. (2010) Phosphorylation-dependent regulation of PSF by GSK3 controls CD45 alternative splicing. Mol. Cell, 40, 126-137.
    • (2010) Mol. Cell , vol.40 , pp. 126-137
    • Heyd, F.1    Lynch, K.W.2
  • 91
    • 79955611181 scopus 로고    scopus 로고
    • Fox-3 and PSF interact to activate neural cell-specific alternative splicing
    • Kim, K.K., Kim, Y.C., Adelstein, R.S., Kawamoto, S. (2011) Fox-3 and PSF interact to activate neural cell-specific alternative splicing. Nucleic Acids Res., 39, 3064-3078.
    • (2011) Nucleic Acids Res , vol.39 , pp. 3064-3078
    • Kim, K.K.1    Kim, Y.C.2    Adelstein, R.S.3    Kawamoto, S.4
  • 93
    • 84924872930 scopus 로고    scopus 로고
    • P54Nrb/NONO regulates cyclic AMP-dependent glucocorticoid production by modulating phosphodiesterase mRNA splicing and degradation
    • Lu, J.Y., Sewer, M.B. (2015) p54nrb/NONO regulates cyclic AMP-dependent glucocorticoid production by modulating phosphodiesterase mRNA splicing and degradation. Mol. Cell. Biol., 35, 1223-1237.
    • (2015) Mol. Cell. Biol , vol.35 , pp. 1223-1237
    • Lu, J.Y.1    Sewer, M.B.2
  • 94
    • 38049153326 scopus 로고    scopus 로고
    • The PSF.p54nrb complex is a novel Mnk substrate that binds the mRNA for tumor necrosis factor alpha
    • Buxade, M., Morrice, N., Krebs, D.L., Proud, C.G. (2008) The PSF.p54nrb complex is a novel Mnk substrate that binds the mRNA for tumor necrosis factor alpha. J. Biol. Chem., 283, 57-65.
    • (2008) J. Biol. Chem , vol.283 , pp. 57-65
    • Buxade, M.1    Morrice, N.2    Krebs, D.L.3    Proud, C.G.4
  • 95
    • 29844444075 scopus 로고    scopus 로고
    • P54Nrb is a component of the snRNP-free U1A (SF-A) complex that promotes pre-mRNA cleavage during polyadenylation
    • Liang, S., Lutz, C.S. (2006) p54nrb is a component of the snRNP-free U1A (SF-A) complex that promotes pre-mRNA cleavage during polyadenylation. RNA, 12, 111-121.
    • (2006) RNA , vol.12 , pp. 111-121
    • Liang, S.1    Lutz, C.S.2
  • 96
    • 34250797537 scopus 로고    scopus 로고
    • Specific trans-acting proteins interact with auxiliary RNA polyadenylation elements in the COX-2 3'-UTR
    • Hall-Pogar, T., Liang, S., Hague, L.K., Lutz, C.S. (2007) Specific trans-acting proteins interact with auxiliary RNA polyadenylation elements in the COX-2 3'-UTR. RNA, 13, 1103-1115.
    • (2007) RNA , vol.13 , pp. 1103-1115
    • Hall-Pogar, T.1    Liang, S.2    Hague, L.K.3    Lutz, C.S.4
  • 97
    • 80555130977 scopus 로고    scopus 로고
    • PSF controls expression of histone variants and cellular viability in thymocytes
    • Heyd, F., Lynch, K.W. (2011) PSF controls expression of histone variants and cellular viability in thymocytes. Biochem. Biophys. Res. Commun., 414, 743-749.
    • (2011) Biochem. Biophys. Res. Commun , vol.414 , pp. 743-749
    • Heyd, F.1    Lynch, K.W.2
  • 99
    • 4143088149 scopus 로고    scopus 로고
    • Kinesin transports RNA: Isolation and characterization of an RNA-transporting granule
    • Kanai, Y., Dohmae, N., Hirokawa, N. (2004) Kinesin transports RNA: isolation and characterization of an RNA-transporting granule. Neuron, 43, 513-525.
    • (2004) Neuron , vol.43 , pp. 513-525
    • Kanai, Y.1    Dohmae, N.2    Hirokawa, N.3
  • 100
    • 84899023073 scopus 로고    scopus 로고
    • P54Nrb/NonO and PSF promote U snRNA nuclear export by accelerating its export complex assembly
    • Izumi, H., McCloskey, A., Shinmyozu, K., Ohno, M. (2014) p54nrb/NonO and PSF promote U snRNA nuclear export by accelerating its export complex assembly. Nucleic Acids Res., 42, 3998-4007.
    • (2014) Nucleic Acids Res , vol.42 , pp. 3998-4007
    • Izumi, H.1    McCloskey, A.2    Shinmyozu, K.3    Ohno, M.4
  • 102
    • 84875154496 scopus 로고    scopus 로고
    • Annexin A2 and PSF proteins interact with p53 IRES and regulate translation of p53 mRNA
    • Sharathchandra, A., Lal, R., Khan, D., Das, S. (2012) Annexin A2 and PSF proteins interact with p53 IRES and regulate translation of p53 mRNA. RNA Biol., 9, 1429-1439.
    • (2012) RNA Biol , vol.9 , pp. 1429-1439
    • Sharathchandra, A.1    Lal, R.2    Khan, D.3    Das, S.4
  • 104
    • 1642499384 scopus 로고    scopus 로고
    • L-Myc protein synthesis is initiated by internal ribosome entry
    • Jopling, C.L., Spriggs, K.A., Mitchell, S.A., Stoneley, M., Willis, A.E. (2004) L-Myc protein synthesis is initiated by internal ribosome entry. RNA, 10, 287-298.
    • (2004) RNA , vol.10 , pp. 287-298
    • Jopling, C.L.1    Spriggs, K.A.2    Mitchell, S.A.3    Stoneley, M.4    Willis, A.E.5
  • 105
    • 84865628181 scopus 로고    scopus 로고
    • Paraspeckle nuclear bodies-useful uselessness?
    • Nakagawa, S., Hirose, T. (2012) Paraspeckle nuclear bodies-useful uselessness? Cell. Mol. Life Sci., 69, 3027-3036.
    • (2012) Cell. Mol. Life Sci , vol.69 , pp. 3027-3036
    • Nakagawa, S.1    Hirose, T.2
  • 106
    • 62549117314 scopus 로고    scopus 로고
    • An architectural role for a nuclear noncoding RNA: NEAT1 RNA Is essential for the structure of paraspeckles
    • Clemson, C.M., Hutchinson, J.N., Sara, S.A., Ensminger, A.W., Fox, A.H., Chess, A., Lawrence, J.B. (2009) An architectural role for a nuclear noncoding RNA: NEAT1 RNA Is essential for the structure of paraspeckles. Mol. Cell, 33, 717-726.
    • (2009) Mol. Cell , vol.33 , pp. 717-726
    • Clemson, C.M.1    Hutchinson, J.N.2    Sara, S.A.3    Ensminger, A.W.4    Fox, A.H.5    Chess, A.6    Lawrence, J.B.7
  • 107
    • 62449319486 scopus 로고    scopus 로고
    • MEN epsilon/beta noncoding RNAs are essential for structural integrity of nuclear paraspeckles
    • Sasaki, Y.T.F., Ideue, T., Sano, M., Mituyama, T., Hirose, T. (2009) MEN epsilon/beta noncoding RNAs are essential for structural integrity of nuclear paraspeckles. Proc. Natl. Acad. Sci. U.S.A., 106, 2525-2530.
    • (2009) Proc. Natl. Acad. Sci. U.S.A , vol.106 , pp. 2525-2530
    • Sasaki, Y.T.F.1    Ideue, T.2    Sano, M.3    Mituyama, T.4    Hirose, T.5
  • 108
    • 61849113891 scopus 로고    scopus 로고
    • MEN epsilon/beta nuclear-retained non-coding RNAs are up-regulated upon muscle differentiation and are essential components of paraspeckles
    • Sunwoo, H., Dinger, M.E., Wilusz, J.E., Amaral, P.P., Mattick, J.S., Spector, D.L. (2009) MEN epsilon/beta nuclear-retained non-coding RNAs are up-regulated upon muscle differentiation and are essential components of paraspeckles. Genome Res., 19, 347-359.
    • (2009) Genome Res , vol.19 , pp. 347-359
    • Sunwoo, H.1    Dinger, M.E.2    Wilusz, J.E.3    Amaral, P.P.4    Mattick, J.S.5    Spector, D.L.6
  • 110
    • 47049122843 scopus 로고    scopus 로고
    • Alu element-mediated gene silencing
    • Chen, L.L., DeCerbo, J.N., Carmichael, G.G. (2008) Alu element-mediated gene silencing. EMBO J., 27, 1694-1705.
    • (2008) EMBO J , vol.27 , pp. 1694-1705
    • Chen, L.L.1    DeCerbo, J.N.2    Carmichael, G.G.3
  • 111
    • 74049109300 scopus 로고    scopus 로고
    • How to build a paraspeckle
    • Sasaki, Y.T.F., Hirose, T. (2009) How to build a paraspeckle. Genome Biol., 10, 227.
    • (2009) Genome Biol , vol.10 , pp. 227
    • Sasaki, Y.T.F.1    Hirose, T.2
  • 112
    • 68949200866 scopus 로고    scopus 로고
    • A NEAT way of regulating nuclear export of mRNAs
    • Scadden, D. (2009) A NEAT way of regulating nuclear export of mRNAs. Mol. Cell, 35, 395-396.
    • (2009) Mol. Cell , vol.35 , pp. 395-396
    • Scadden, D.1
  • 113
    • 34247222090 scopus 로고    scopus 로고
    • Subnuclear localization and dynamics of the Pre-mRNA 3' end processing factor mammalian cleavage factor i 68-kDa subunit
    • Cardinale, S., Cisterna, B., Bonetti, P., Aringhieri, C., Biggiogera, M., Barabino, S.M. (2007) Subnuclear localization and dynamics of the Pre-mRNA 3' end processing factor mammalian cleavage factor I 68-kDa subunit. Mol. Biol. Cell, 18, 1282-1292.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 1282-1292
    • Cardinale, S.1    Cisterna, B.2    Bonetti, P.3    Aringhieri, C.4    Biggiogera, M.5    Barabino, S.M.6
  • 114
    • 79951853518 scopus 로고    scopus 로고
    • Sequences in PSF/SFPQ mediate radioresistance and recruitment of PSF/SFPQ-containing complexes to DNA damage sites in human cells
    • Ha, K., Takeda, Y., Dynan, W.S. (2011) Sequences in PSF/SFPQ mediate radioresistance and recruitment of PSF/SFPQ-containing complexes to DNA damage sites in human cells. DNA Rep., 10, 252-259.
    • (2011) DNA Rep , vol.10 , pp. 252-259
    • Ha, K.1    Takeda, Y.2    Dynan, W.S.3
  • 115
    • 84867575580 scopus 로고    scopus 로고
    • Alternative 3'-end processing of long noncoding RNA initiates construction of nuclear paraspeckles
    • Naganuma, T., Nakagawa, S., Tanigawa, A., Sasaki, Y.F., Goshima, N., Hirose, T. (2012) Alternative 3'-end processing of long noncoding RNA initiates construction of nuclear paraspeckles. EMBO J., 31, 4020-4034.
    • (2012) EMBO J , vol.31 , pp. 4020-4034
    • Naganuma, T.1    Nakagawa, S.2    Tanigawa, A.3    Sasaki, Y.F.4    Goshima, N.5    Hirose, T.6
  • 116
    • 0028941466 scopus 로고
    • Characterization of two nuclear mammalian homologous DNA-pairing activities that do not require associated exonuclease activity
    • Akhmedov, A.T., Bertrand, P., Corteggiani, E., Lopez, B.S. (1995) Characterization of two nuclear mammalian homologous DNA-pairing activities that do not require associated exonuclease activity. Proc. Natl. Acad. Sci. U.S.A., 92, 1729-1733.
    • (1995) Proc. Natl. Acad. Sci. U.S.A , vol.92 , pp. 1729-1733
    • Akhmedov, A.T.1    Bertrand, P.2    Corteggiani, E.3    Lopez, B.S.4
  • 117
  • 118
    • 0034663495 scopus 로고    scopus 로고
    • Human 100-kDa homologous DNA-pairing protein is the splicing factor PSF and promotes DNA strand invasion
    • Akhmedov, A.T., Lopez, B.S. (2000) Human 100-kDa homologous DNA-pairing protein is the splicing factor PSF and promotes DNA strand invasion. Nucleic Acids Res., 28, 3022-3030.
    • (2000) Nucleic Acids Res , vol.28 , pp. 3022-3030
    • Akhmedov, A.T.1    Lopez, B.S.2
  • 119
    • 0034720780 scopus 로고    scopus 로고
    • PSF/p54(nrb) stimulates jumping of DNA topoisomerase i between separate DNA helices
    • Straub, T., Knudsen, B.R., Boege, F. (2000) PSF/p54(nrb) stimulates "jumping" of DNA topoisomerase I between separate DNA helices. Biochemistry, 39, 7552-7558.
    • (2000) Biochemistry , vol.39 , pp. 7552-7558
    • Straub, T.1    Knudsen, B.R.2    Boege, F.3
  • 120
    • 14044257206 scopus 로고    scopus 로고
    • Identification of the polypyrimidine tract binding protein-associated splicing factor.p54(nrb) complex as a candidate DNA double-strand break rejoining factor
    • Bladen, C.L., Udayakumar, D., Takeda, Y., Dynan, W.S. (2005) Identification of the polypyrimidine tract binding protein-associated splicing factor.p54(nrb) complex as a candidate DNA double-strand break rejoining factor. J. Biol. Chem., 280, 5205-5210.
    • (2005) J. Biol. Chem , vol.280 , pp. 5205-5210
    • Bladen, C.L.1    Udayakumar, D.2    Takeda, Y.3    Dynan, W.S.4
  • 121
    • 67949123271 scopus 로고    scopus 로고
    • Human PSF binds to RAD51 and modulates its homologous-pairing and strand-exchange activities
    • Morozumi, Y., Takizawa, Y., Takaku, M., Kurumizaka, H. (2009) Human PSF binds to RAD51 and modulates its homologous-pairing and strand-exchange activities. Nucleic Acids Res., 37, 4296-4307.
    • (2009) Nucleic Acids Res , vol.37 , pp. 4296-4307
    • Morozumi, Y.1    Takizawa, Y.2    Takaku, M.3    Kurumizaka, H.4
  • 123
    • 77953564663 scopus 로고    scopus 로고
    • Involvement of Matrin 3 and SFPQ/NONO in the DNA damage response
    • Salton, M., Lerenthal, Y., Wang, S.Y., Chen, D.J., Shiloh, Y. (2010) Involvement of Matrin 3 and SFPQ/NONO in the DNA damage response. Cell Cycle, 9, 1568-1576.
    • (2010) Cell Cycle , vol.9 , pp. 1568-1576
    • Salton, M.1    Lerenthal, Y.2    Wang, S.Y.3    Chen, D.J.4    Shiloh, Y.5
  • 124
    • 73349143041 scopus 로고    scopus 로고
    • Involvement of p54(nrb), a PSF partner protein, in DNA double-strand break repair and radioresistance
    • Li, S., Kuhne, W.W., Kulharya, A., Hudson, F.Z., Ha, K., Cao, Z., Dynan, W.S. (2009) Involvement of p54(nrb), a PSF partner protein, in DNA double-strand break repair and radioresistance. Nucleic Acids Res., 37, 6746-6753.
    • (2009) Nucleic Acids Res , vol.37 , pp. 6746-6753
    • Li, S.1    Kuhne, W.W.2    Kulharya, A.3    Hudson, F.Z.4    Ha, K.5    Cao, Z.6    Dynan, W.S.7
  • 125
    • 84936890941 scopus 로고    scopus 로고
    • Characterization of DNA binding and pairing activities associated with the native SFPQ.NONO DNA repair protein complex
    • Udayakumar, D., Dynan, W.S. (2015) Characterization of DNA binding and pairing activities associated with the native SFPQ.NONO DNA repair protein complex. Biochem. Biophys. Res. Commun., 463, 473-478.
    • (2015) Biochem. Biophys. Res. Commun , vol.463 , pp. 473-478
    • Udayakumar, D.1    Dynan, W.S.2
  • 126
    • 85012081784 scopus 로고    scopus 로고
    • The RNA Splicing Response to DNA Damage
    • Shkreta, L., Chabot, B. (2015) The RNA Splicing Response to DNA Damage. Biomolecules, 5, 2935-2977.
    • (2015) Biomolecules , vol.5 , pp. 2935-2977
    • Shkreta, L.1    Chabot, B.2
  • 128
    • 84862196500 scopus 로고    scopus 로고
    • Poly(ADP-ribose) regulates Post-Transcriptional gene regulation in the cytoplasm
    • Leung, A., Todorova, T.,o, Y., Chang, P. (2012) Poly(ADP-ribose) regulates post-transcriptional gene regulation in the cytoplasm. RNA Biol., 9, 542-548.
    • (2012) RNA Biol , vol.9 , pp. 542-548
    • Leung, A.1    Todorova, T.O.Y.2    Chang, P.3
  • 129
    • 84902322535 scopus 로고    scopus 로고
    • Poly(ADP-ribose): An organizer of cellular architecture
    • Leung, A.K. (2014) Poly(ADP-ribose): an organizer of cellular architecture. J. Cell. Biol., 205, 613-619.
    • (2014) J. Cell. Biol , vol.205 , pp. 613-619
    • Leung, A.K.1
  • 131
  • 133
  • 137
    • 48749084615 scopus 로고    scopus 로고
    • The complex of TFII-I, PARP1, SFPQ proteins regulates the DYX1C1 gene implicated in neuronal migration and dyslexia
    • Tapia-Paez, I., Tammimies, K., Massinen, S., Roy, A.L., Kere, J. (2008) The complex of TFII-I, PARP1, SFPQ proteins regulates the DYX1C1 gene implicated in neuronal migration and dyslexia. FASEB J., 22, 3001-3009.
    • (2008) FASEB J , vol.22 , pp. 3001-3009
    • Tapia-Paez, I.1    Tammimies, K.2    Massinen, S.3    Roy, A.L.4    Kere, J.5
  • 138
    • 84920473846 scopus 로고    scopus 로고
    • Quantitative proteomics reveals dynamic interaction of c-Jun N-terminal kinase (JNK) with RNA transport granule proteins splicing factor proline-and glutamine-rich (Sfpq) and non-POU domain-containing octamer-binding protein (Nono) during neuronal differentiation
    • Sury, M.D., McShane, E., Hernandez-Miranda, L.R., Birchmeier, C., Selbach, M. (2015) Quantitative proteomics reveals dynamic interaction of c-Jun N-terminal kinase (JNK) with RNA transport granule proteins splicing factor proline-and glutamine-rich (Sfpq) and non-POU domain-containing octamer-binding protein (Nono) during neuronal differentiation. Mol. Cell. Proteomics, 14, 50-65.
    • (2015) Mol. Cell. Proteomics , vol.14 , pp. 50-65
    • Sury, M.D.1    McShane, E.2    Hernandez-Miranda, L.R.3    Birchmeier, C.4    Selbach, M.5
  • 139
    • 20944437573 scopus 로고    scopus 로고
    • The Parkinson's disease-associated DJ-1 protein is a transcriptional co-activator that protects against neuronal apoptosis
    • Xu, J., Zhong, N., Wang, H., Elias, J.E., Kim, C.Y., Woldman, I., Pifl, C., Gygi, S.P., Geula, C., Yankner, B.A. (2005) The Parkinson's disease-associated DJ-1 protein is a transcriptional co-activator that protects against neuronal apoptosis. Hum. Mol. Genet., 14, 1231-1241.
    • (2005) Hum. Mol. Genet , vol.14 , pp. 1231-1241
    • Xu, J.1    Zhong, N.2    Wang, H.3    Elias, J.E.4    Kim, C.Y.5    Woldman, I.6    Pifl, C.7    Gygi, S.P.8    Geula, C.9    Yankner, B.A.10
  • 140
    • 84864437328 scopus 로고    scopus 로고
    • Expression and function of myometrial PSF suggest a role in progesterone withdrawal and the initiation of labor
    • Xie, N., Liu, L., Li, Y., Yu, C., Lam, S., Shynlova, O., Gleave, M., Challis, J.R., Lye, S., Dong, X. (2012) Expression and function of myometrial PSF suggest a role in progesterone withdrawal and the initiation of labor. Mol. Endocrinol., 26, 1370-1379.
    • (2012) Mol. Endocrinol , vol.26 , pp. 1370-1379
    • Xie, N.1    Liu, L.2    Li, Y.3    Yu, C.4    Lam, S.5    Shynlova, O.6    Gleave, M.7    Challis, J.R.8    Lye, S.9    Dong, X.10
  • 141
    • 77957355995 scopus 로고    scopus 로고
    • Quantitative proteomics using SILAC coupled to LC-MS/MS reveals changes in the nucleolar proteome in influenza A virus-infected cells
    • Emmott, E., Wise, H., Loucaides, E.M., Matthews, D.A., Digard, P., Hiscox, J.A. (2010) Quantitative proteomics using SILAC coupled to LC-MS/MS reveals changes in the nucleolar proteome in influenza A virus-infected cells. J. Proteome Res., 9, 5335-5345.
    • (2010) J. Proteome Res , vol.9 , pp. 5335-5345
    • Emmott, E.1    Wise, H.2    Loucaides, E.M.3    Matthews, D.A.4    Digard, P.5    Hiscox, J.A.6
  • 142
    • 81755166636 scopus 로고    scopus 로고
    • The splicing factor proline-glutamine rich (SFPQ/PSF) is involved in influenza virus transcription
    • Landeras-Bueno, S., Jorba, N., Perez-Cidoncha, M., Ortin, J. (2011) The splicing factor proline-glutamine rich (SFPQ/PSF) is involved in influenza virus transcription. PLoS Pathog., 7, e1002397.
    • (2011) PLoS Pathog , vol.7 , pp. e1002397
    • Landeras-Bueno, S.1    Jorba, N.2    Perez-Cidoncha, M.3    Ortin, J.4
  • 143
    • 84871676628 scopus 로고    scopus 로고
    • HIV-1 pre-mRNA commitment to Rev mediated export through PSF and Matrin 3
    • Kula, A., Gharu, L., Marcello, A. (2013) HIV-1 pre-mRNA commitment to Rev mediated export through PSF and Matrin 3. Virology, 435, 329-340.
    • (2013) Virology , vol.435 , pp. 329-340
    • Kula, A.1    Gharu, L.2    Marcello, A.3
  • 144
    • 84938865013 scopus 로고    scopus 로고
    • Non-POU Domain-Containing Octamer-Binding protein negatively regulates HIV-1 Infection in CD4(+) T Cells
    • Gelais, C.S., Roger, J., Wu, L. (2015) Non-POU Domain-Containing Octamer-Binding Protein Negatively Regulates HIV-1 Infection in CD4(+) T Cells. Aids Res. Hum. Retrov., 31, 806-816.
    • (2015) Aids Res. Hum. Retrov , vol.31 , pp. 806-816
    • Gelais, C.S.1    Roger, J.2    Wu, L.3
  • 145
    • 84931074878 scopus 로고    scopus 로고
    • New noncoding lytic transcripts derived from the Epstein-barr virus latency origin of replication, orip, are hyperedited, bind the paraspeckle protein, nono/p54nrb, support viral lytic transcription
    • Cao, S., Moss, W., O'Grady, T., Concha, M., Strong, M.J., Wang, X., Yu, Y., Baddoo, M., Zhang, K., Fewell, C. et al. (2015) New Noncoding Lytic Transcripts Derived from the Epstein-Barr Virus Latency Origin of Replication, oriP, Are Hyperedited, Bind the Paraspeckle Protein, NONO/p54nrb, Support Viral Lytic Transcription. J. Virol., 89, 7120-7132.
    • (2015) J. Virol , vol.89 , pp. 7120-7132
    • Cao, S.1    Moss, W.2    O'Grady, T.3    Concha, M.4    Strong, M.J.5    Wang, X.6    Yu, Y.7    Baddoo, M.8    Zhang, K.9    Fewell, C.10
  • 146
    • 84962245224 scopus 로고    scopus 로고
    • EBV noncoding RNA EBER2 interacts with host RNA-binding proteins to regulate viral gene expression
    • Lee, N., Yario, T.A., Gao, J.S., Steitz, J.A. (2016) EBV noncoding RNA EBER2 interacts with host RNA-binding proteins to regulate viral gene expression. Proc. Natl. Acad. Sci. U.S.A., 113, 3221-3226.
    • (2016) Proc. Natl. Acad. Sci. U.S.A , vol.113 , pp. 3221-3226
    • Lee, N.1    Yario, T.A.2    Gao, J.S.3    Steitz, J.A.4
  • 147
  • 148
    • 84906090333 scopus 로고    scopus 로고
    • Long Non-Coding RNA MALAT1 promotes tumour growth and metastasis in colorectal cancer through binding to SFPQ and releasing oncogene PTBP2 from SFPQ/PTBP2 complex
    • Ji, Q., Zhang, L., Liu, X., Zhou, L., Wang, W., Han, Z., Sui, H., Tang, Y., Wang, Y., Liu, N. et al. (2014) Long non-coding RNA MALAT1 promotes tumour growth and metastasis in colorectal cancer through binding to SFPQ and releasing oncogene PTBP2 from SFPQ/PTBP2 complex. Br. J. Cancer, 111, 736-748.
    • (2014) Br. J. Cancer , vol.111 , pp. 736-748
    • Ji, Q.1    Zhang, L.2    Liu, X.3    Zhou, L.4    Wang, W.5    Han, Z.6    Sui, H.7    Tang, Y.8    Wang, Y.9    Liu, N.10
  • 149
    • 79961199011 scopus 로고    scopus 로고
    • P54Nrb is a new regulator of progression of malignant melanoma
    • Schiffner, S., Zimara, N., Schmid, R., Bosserhoff, A.K. (2011) p54nrb is a new regulator of progression of malignant melanoma. Carcinogenesis, 32, 1176-1182.
    • (2011) Carcinogenesis , vol.32 , pp. 1176-1182
    • Schiffner, S.1    Zimara, N.2    Schmid, R.3    Bosserhoff, A.K.4
  • 152
    • 84935421424 scopus 로고    scopus 로고
    • P54/NONO regulates lipid metabolism and breast cancer growth through SREBP-1A
    • Zhu, Z., Zhao, X., Zhao, L., Yang, H., Liu, L., Li, J., Wu, J., Yang, F., Huang, G., Liu, J. (2015) p54/NONO regulates lipid metabolism and breast cancer growth through SREBP-1A. Oncogene, 35, 1399-1410.
    • (2015) Oncogene , vol.35 , pp. 1399-1410
    • Zhu, Z.1    Zhao, X.2    Zhao, L.3    Yang, H.4    Liu, L.5    Li, J.6    Wu, J.7    Yang, F.8    Huang, G.9    Liu, J.10
  • 155
    • 82355173271 scopus 로고    scopus 로고
    • Proteomic analysis of 1alpha, 25-dihydroxyvitamin D3 action on human colon cancer cells reveals a link to splicing regulation
    • Cristobo, I., Larriba, M.J., de los Rios, V., Garcia, F., Munoz, A., Casal, J.I. (2011) Proteomic analysis of 1alpha, 25-dihydroxyvitamin D3 action on human colon cancer cells reveals a link to splicing regulation. J. Proteomics, 75, 384-397.
    • (2011) J. Proteomics , vol.75 , pp. 384-397
    • Cristobo, I.1    Larriba, M.J.2    Delos Rios, V.3    Garcia, F.4    Munoz, A.5    Casal, J.I.6
  • 156
    • 82055171670 scopus 로고    scopus 로고
    • NONO and RALY proteins are required for YB-1 oxaliplatin induced resistance in colon adenocarcinoma cell lines
    • Tsofack, S.P., Garand, C., Sereduk, C., Chow, D., Aziz, M., Guay, D., Yin, H.H., Lebel, M. (2011) NONO and RALY proteins are required for YB-1 oxaliplatin induced resistance in colon adenocarcinoma cell lines. Mol. Cancer, 10, 145.
    • (2011) Mol. Cancer , vol.10 , pp. 145
    • Tsofack, S.P.1    Garand, C.2    Sereduk, C.3    Chow, D.4    Aziz, M.5    Guay, D.6    Yin, H.H.7    Lebel, M.8
  • 157
    • 0037457643 scopus 로고    scopus 로고
    • 55 kDa nuclear matrix protein (nmt55) mRNA is expressed in human prostate cancer tissue and is associated with the androgen receptor
    • Ishiguro, H., Uemura, H., Fujinami, K., Ikeda, N., Ohta, S., Kubota, Y. (2003) 55 kDa nuclear matrix protein (nmt55) mRNA is expressed in human prostate cancer tissue and is associated with the androgen receptor. Int. J. Cancer, 105, 26-32.
    • (2003) Int. J. Cancer , vol.105 , pp. 26-32
    • Ishiguro, H.1    Uemura, H.2    Fujinami, K.3    Ikeda, N.4    Ohta, S.5    Kubota, Y.6
  • 158
    • 79957822818 scopus 로고    scopus 로고
    • Infiltration of tumour-associated macrophages in prostate biopsy specimens is predictive of disease progression after hormonal therapy for prostate cancer
    • Nonomura, N., Takayama, H., Nakayama, M., Nakai, Y., Kawashima, A., Mukai, M., Nagahara, A., Aozasa, K., Tsujimura, A. (2011) Infiltration of tumour-associated macrophages in prostate biopsy specimens is predictive of disease progression after hormonal therapy for prostate cancer. BJU Int., 107, 1918-1922.
    • (2011) BJU Int , vol.107 , pp. 1918-1922
    • Nonomura, N.1    Takayama, H.2    Nakayama, M.3    Nakai, Y.4    Kawashima, A.5    Mukai, M.6    Nagahara, A.7    Aozasa, K.8    Tsujimura, A.9
  • 159
    • 33846214715 scopus 로고    scopus 로고
    • Role of PSF-TFE3 oncoprotein in the development of papillary renal cell carcinomas
    • Mathur, M., Samuels, H.H. (2007) Role of PSF-TFE3 oncoprotein in the development of papillary renal cell carcinomas. Oncogene, 26, 277-283.
    • (2007) Oncogene , vol.26 , pp. 277-283
    • Mathur, M.1    Samuels, H.H.2
  • 162
    • 84971236174 scopus 로고    scopus 로고
    • TRAP150 interacts with the RNA-binding domain of PSF and antagonizes splicing of numerous PSF-target genes in T cells
    • Yarosh, C.A., Tapescu, I., Thompson, M.G., Qiu, J., Mallory, M.J., Fu, X.D., Lynch, K.W. (2015) TRAP150 interacts with the RNA-binding domain of PSF and antagonizes splicing of numerous PSF-target genes in T cells. Nucleic Acids Res., 43, 9006-9016.
    • (2015) Nucleic Acids Res , vol.43 , pp. 9006-9016
    • Yarosh, C.A.1    Tapescu, I.2    Thompson, M.G.3    Qiu, J.4    Mallory, M.J.5    Fu, X.D.6    Lynch, K.W.7
  • 163
    • 84936792294 scopus 로고    scopus 로고
    • 2'-Fluoro-modified phosphorothioate oligonucleotide can cause rapid degradation of P54nrb and PSF
    • Shen, W., Liang, X.H., Sun, H., Crooke, S.T. (2015) 2'-Fluoro-modified phosphorothioate oligonucleotide can cause rapid degradation of P54nrb and PSF. Nucleic Acids Res., 43, 4569-4578.
    • (2015) Nucleic Acids Res , vol.43 , pp. 4569-4578
    • Shen, W.1    Liang, X.H.2    Sun, H.3    Crooke, S.T.4
  • 164
    • 13444259420 scopus 로고    scopus 로고
    • The multifunctional nuclear protein p54nrb is multiphosphorylated in mitosis and interacts with the mitotic regulator Pin1
    • Proteau, A., Blier, S., Albert, A.L., Lavoie, S.B., Traish, A.M., Vincent, M. (2005) The multifunctional nuclear protein p54nrb is multiphosphorylated in mitosis and interacts with the mitotic regulator Pin1. J. Mol. Biol., 346, 1163-1172.
    • (2005) J. Mol. Biol , vol.346 , pp. 1163-1172
    • Proteau, A.1    Blier, S.2    Albert, A.L.3    Lavoie, S.B.4    Traish, A.M.5    Vincent, M.6
  • 165
    • 79959849578 scopus 로고    scopus 로고
    • Consensus PP1 binding motifs regulate transcriptional corepression and alternative RNA splicing activities of the steroid receptor coregulators, p54nrb and PSF
    • Liu, L., Xie, N., Rennie, P., Challis, J.R., Gleave, M., Lye, S.J., Dong, X. (2011) Consensus PP1 binding motifs regulate transcriptional corepression and alternative RNA splicing activities of the steroid receptor coregulators, p54nrb and PSF. Mol. Endocrinol., 25, 1197-1210.
    • (2011) Mol. Endocrinol , vol.25 , pp. 1197-1210
    • Liu, L.1    Xie, N.2    Rennie, P.3    Challis, J.R.4    Gleave, M.5    Lye, S.J.6    Dong, X.7
  • 166
    • 0034823538 scopus 로고    scopus 로고
    • Identification of tyrosine-phosphorylated proteins associated with the nuclear envelope
    • Otto, H., Dreger, M., Bengtsson, L., Hucho, F. (2001) Identification of tyrosine-phosphorylated proteins associated with the nuclear envelope. Eur. J. Biochem., 268, 420-428.
    • (2001) Eur. J. Biochem , vol.268 , pp. 420-428
    • Otto, H.1    Dreger, M.2    Bengtsson, L.3    Hucho, F.4
  • 168
    • 67349211222 scopus 로고    scopus 로고
    • BRK phosphorylates PSF promoting its cytoplasmic localization and cell cycle arrest
    • Lukong, K.E., Huot, M.E., Richard, S. (2009) BRK phosphorylates PSF promoting its cytoplasmic localization and cell cycle arrest. Cell Signal., 21, 1415-1422.
    • (2009) Cell Signal , vol.21 , pp. 1415-1422
    • Lukong, K.E.1    Huot, M.E.2    Richard, S.3
  • 169
    • 0035159666 scopus 로고    scopus 로고
    • Nuclear relocalization of the pre-mRNA splicing factor PSF during apoptosis involves hyperphosphorylation, masking of antigenic epitopes, changes in protein interactions
    • Shav-Tal, Y., Cohen, M., Lapter, S., Dye, B., Patton, J.G., Vandekerckhove, J., Zipori, D. (2001) Nuclear relocalization of the pre-mRNA splicing factor PSF during apoptosis involves hyperphosphorylation, masking of antigenic epitopes, changes in protein interactions. Mol. Biol. Cell., 12, 2328-2340.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2328-2340
    • Shav-Tal, Y.1    Cohen, M.2    Lapter, S.3    Dye, B.4    Patton, J.G.5    Vandekerckhove, J.6    Zipori, D.7
  • 170
    • 84925242210 scopus 로고    scopus 로고
    • Protein arginine methyltransferase CARM1 attenuates the paraspeckle-mediated nuclear retention of mRNAs containing IRAlus
    • Hu, S.B., Xiang, J.F., Li, X., Xu, Y., Xue, W., Huang, M., Wong, C.C., Sagum, C.A., Bedford, M.T., Yang, L. et al. (2015) Protein arginine methyltransferase CARM1 attenuates the paraspeckle-mediated nuclear retention of mRNAs containing IRAlus. Genes Dev., 29, 630-645.
    • (2015) Genes Dev , vol.29 , pp. 630-645
    • Hu, S.B.1    Xiang, J.F.2    Li, X.3    Xu, Y.4    Xue, W.5    Huang, M.6    Wong, C.C.7    Sagum, C.A.8    Bedford, M.T.9    Yang, L.10
  • 171
    • 18744375196 scopus 로고    scopus 로고
    • Identifying and quantifying in vivo methylation sites by heavy methyl SILAC
    • Ong, S.E., Mittler, G., Mann, M. (2004) Identifying and quantifying in vivo methylation sites by heavy methyl SILAC. Nat. Methods, 1, 119-126.
    • (2004) Nat. Methods , vol.1 , pp. 119-126
    • Ong, S.E.1    Mittler, G.2    Mann, M.3
  • 172
    • 33746355607 scopus 로고    scopus 로고
    • DJ-1 transcriptionally up-regulates the human tyrosine hydroxylase by inhibiting the sumoylation of pyrimidine tract-binding protein-associated splicing factor
    • Zhong, N., Kim, C.Y., Rizzu, P., Geula, C., Porter, D.R., Pothos, E.N., Squitieri, F., Heutink, P., Xu, J. (2006) DJ-1 transcriptionally up-regulates the human tyrosine hydroxylase by inhibiting the sumoylation of pyrimidine tract-binding protein-associated splicing factor. J. Biol. Chem., 281, 20940-20948.
    • (2006) J. Biol. Chem , vol.281 , pp. 20940-20948
    • Zhong, N.1    Kim, C.Y.2    Rizzu, P.3    Geula, C.4    Porter, D.R.5    Pothos, E.N.6    Squitieri, F.7    Heutink, P.8    Xu, J.9
  • 173
    • 44649130038 scopus 로고    scopus 로고
    • Transcriptional control by PARP-1: Chromatin modulation, enhancer-binding, coregulation, insulation
    • Kraus, W.L. (2008) Transcriptional control by PARP-1: chromatin modulation, enhancer-binding, coregulation, insulation. Curr. Opin. Cell. Biol., 20, 294-302.
    • (2008) Curr. Opin. Cell. Biol , vol.20 , pp. 294-302
    • Kraus, W.L.1
  • 174
    • 84881219867 scopus 로고    scopus 로고
    • Post-transcriptional regulation by poly(ADP-ribosyl)ation of the RNA-binding proteins
    • Ji, Y., Tulin, A.V. (2013) Post-transcriptional regulation by poly(ADP-ribosyl)ation of the RNA-binding proteins. Int. J. Mol. Sci., 14, 16168-16183.
    • (2013) Int. J. Mol. Sci , vol.14 , pp. 16168-16183
    • Ji, Y.1    Tulin, A.V.2
  • 175
    • 84886719040 scopus 로고    scopus 로고
    • PARP-1 and gene regulation: Progress and puzzles
    • Kraus, W.L., Hottiger, M.O. (2013) PARP-1 and gene regulation: progress and puzzles. Mol. Aspects Med., 34, 1109-1123.
    • (2013) Mol. Aspects Med , vol.34 , pp. 1109-1123
    • Kraus, W.L.1    Hottiger, M.O.2
  • 176
    • 84937622587 scopus 로고    scopus 로고
    • RNA regulation by poly(ADP-Ribose) polymerases
    • Bock, F.J., Todorova, T.T., Chang, P. (2015) RNA regulation by poly(ADP-Ribose) polymerases. Mol. Cell, 58, 959-969.
    • (2015) Mol. Cell , vol.58 , pp. 959-969
    • Bock, F.J.1    Todorova, T.T.2    Chang, P.3
  • 177
    • 0024549825 scopus 로고
    • Cloning and characterization of a myoblast cell surface antigen defined by 24.1D5 monoclonal antibody
    • Gower, H.J., Moore, S.E., Dickson, G., Elsom, V.L., Nayak, R., Walsh, F.S. (1989) Cloning and characterization of a myoblast cell surface antigen defined by 24.1D5 monoclonal antibody. Development, 105, 723-731.
    • (1989) Development , vol.105 , pp. 723-731
    • Gower, H.J.1    Moore, S.E.2    Dickson, G.3    Elsom, V.L.4    Nayak, R.5    Walsh, F.S.6
  • 178
    • 34548127017 scopus 로고    scopus 로고
    • PSF is an IbeA-binding protein contributing to meningitic Escherichia coli K1 invasion of human brain microvascular endothelial cells
    • Zou, Y., He, L., Wu, C.H., Cao, H., Xie, Z.H., Ouyang, Y., Wang, Y., Jong, A., Huang, S.H. (2007) PSF is an IbeA-binding protein contributing to meningitic Escherichia coli K1 invasion of human brain microvascular endothelial cells. Med. Microbiol. Immunol., 196, 135-143.
    • (2007) Med. Microbiol. Immunol , vol.196 , pp. 135-143
    • Zou, Y.1    He, L.2    Wu, C.H.3    Cao, H.4    Xie, Z.H.5    Ouyang, Y.6    Wang, Y.7    Jong, A.8    Huang, S.H.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.