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Volumn 5, Issue 8, 2013, Pages 1901-1923

Kaposi's sarcoma-associated herpesvirus ORF57 protein: Exploiting all stages of viral mRNA processing

Author keywords

Herpesvirus; Kshv; mRNA export; mRNA stability; ORF57; Trex

Indexed keywords

CARRIER PROTEIN; EXPORTIN 1; MESSENGER RNA; OPEN READING FRAME 57 PROTEIN; TRANSCIPTION COUPLED EXPORT PROTEIN; UNCLASSIFIED DRUG; VIRUS PROTEIN;

EID: 84880812273     PISSN: 19994915     EISSN: None     Source Type: Journal    
DOI: 10.3390/v5081901     Document Type: Review
Times cited : (21)

References (134)
  • 3
    • 0029069445 scopus 로고
    • Kaposi's sarcoma-associated herpesvirus-like DNA sequences in AIDS-related body-cavity-based lymphomas
    • Cesarman, E.; Chang, Y.; Moore, P.S.; Said, J.W.; Knowles, D.M. Kaposi's sarcoma-associated herpesvirus-like DNA sequences in AIDS-related body-cavity-based lymphomas. N. Engl. J. Med. 1995, 332, 1186-1191.
    • (1995) N. Engl. J. Med , vol.332 , pp. 1186-1191
    • Cesarman, E.1    Chang, Y.2    Moore, P.S.3    Said, J.W.4    Knowles, D.M.5
  • 4
    • 0028588064 scopus 로고
    • Identification of herpesvirus-like DNA sequences in AIDS-associated Kaposi's sarcoma
    • Chang, Y.; Cesarman, E.; Pessin, M.S.; Lee, F.; Culpepper, J.; Knowles, D.M.; Moore, P.S. Identification of herpesvirus-like DNA sequences in AIDS-associated Kaposi's sarcoma. Science 1994, 266, 1865-1869.
    • (1994) Science , vol.266 , pp. 1865-1869
    • Chang, Y.1    Cesarman, E.2    Pessin, M.S.3    Lee, F.4    Culpepper, J.5    Knowles, D.M.6    Moore, P.S.7
  • 6
    • 0023710041 scopus 로고
    • Penn, I. Secondary neoplasms as a consequence of transplantation and cancer therapy
    • Penn, I. Secondary neoplasms as a consequence of transplantation and cancer therapy. Cancer Detect. Prev. 1988, 12, 39-57.
    • (1988) Cancer Detect. Prev , vol.12 , pp. 39-57
  • 7
    • 77951192990 scopus 로고    scopus 로고
    • KSHV and the pathogenesis of Kaposi sarcoma: Listening to human biology and medicine
    • Ganem, D. KSHV and the pathogenesis of Kaposi sarcoma: Listening to human biology and medicine. J. Clin. Invest. 2010, 120, 939-949.
    • (2010) J. Clin. Invest , vol.120 , pp. 939-949
    • Ganem, D.1
  • 9
    • 79952232330 scopus 로고    scopus 로고
    • Active lytic infection of human primary tonsillar B cells by KSHV and its noncytolytic control by activated CD4+ T cells
    • Myoung, J.; Ganem, D. Active lytic infection of human primary tonsillar B cells by KSHV and its noncytolytic control by activated CD4+ T cells. J. Clin. Invest. 2011, 121, 1130-1140.
    • (2011) J. Clin. Invest , vol.121 , pp. 1130-1140
    • Myoung, J.1    Ganem, D.2
  • 10
    • 1842588762 scopus 로고    scopus 로고
    • Wild-type Kaposi's sarcoma-associated herpesvirus isolated from the oropharynx of immune-competent individuals has tropism for cultured oral epithelial cells
    • Duus, K.M.; Lentchitsky, V.; Wagenaar, T.; Grose, C.; Webster-Cyriaque, J. Wild-type Kaposi's sarcoma-associated herpesvirus isolated from the oropharynx of immune-competent individuals has tropism for cultured oral epithelial cells. J. Virol. 2004, 78, 4074-4084.
    • (2004) J. Virol , vol.78 , pp. 4074-4084
    • Duus, K.M.1    Lentchitsky, V.2    Wagenaar, T.3    Grose, C.4    Webster-Cyriaque, J.5
  • 14
    • 34250010253 scopus 로고    scopus 로고
    • EBV and its replication
    • 5th ed.; Knipe, D.M., Howley, P.M., Eds.; Lippincott, Williams and Wilkins: Philadelphia, PA, USA
    • Kieff, E.; Rickinson, A. EBV and its replication. In Fields' Virology, 5th ed.; Knipe, D.M., Howley, P.M., Eds.; Lippincott, Williams and Wilkins: Philadelphia, PA, USA, 2007; pp. 2603-2654.
    • (2007) Fields' Virology , pp. 2603-2654
    • Kieff, E.1    Rickinson, A.2
  • 15
    • 77957121811 scopus 로고    scopus 로고
    • Kaposi's sarcoma and its associated herpesvirus
    • Mesri, E.A.; Cesarman, E.; Boshoff, C. Kaposi's sarcoma and its associated herpesvirus. Nat. Rev. Cancer 2010, 10, 707-719.
    • (2010) Nat. Rev. Cancer , vol.10 , pp. 707-719
    • Mesri, E.A.1    Cesarman, E.2    Boshoff, C.3
  • 16
    • 67650492477 scopus 로고    scopus 로고
    • Mechanisms of nuclear mRNA quality control
    • Fasken, M.B.; Corbett, A.H. Mechanisms of nuclear mRNA quality control. RNA Biol. 2009, 6, 237-241.
    • (2009) RNA Biol , vol.6 , pp. 237-241
    • Fasken, M.B.1    Corbett, A.H.2
  • 17
    • 0035807308 scopus 로고    scopus 로고
    • Quality control of mRNA 3'-end processing is linked to the nuclear exosome
    • Hilleren, P.; McCarthy, T.; Rosbash, M.; Parker, R.; Jensen, T.H. Quality control of mRNA 3'-end processing is linked to the nuclear exosome. Nature 2001, 413, 538-542.
    • (2001) Nature , vol.413 , pp. 538-542
    • Hilleren, P.1    McCarthy, T.2    Rosbash, M.3    Parker, R.4    Jensen, T.H.5
  • 18
    • 0034544815 scopus 로고    scopus 로고
    • Pre-mRNA processing factors are required for nuclear export
    • Brodsky, A.S.; Silver, P.A. Pre-mRNA processing factors are required for nuclear export. RNA 2000, 6, 1737-1749.
    • (2000) RNA , vol.6 , pp. 1737-1749
    • Brodsky, A.S.1    Silver, P.A.2
  • 19
    • 0036829415 scopus 로고    scopus 로고
    • Intron status and 3'-end formation control cotranscriptional export of mRNA
    • Lei, E.P.; Silver, P.A. Intron status and 3'-end formation control cotranscriptional export of mRNA. Genes Dev. 2002, 16, 2761-2766.
    • (2002) Genes Dev , vol.16 , pp. 2761-2766
    • Lei, E.P.1    Silver, P.A.2
  • 20
    • 0036889142 scopus 로고    scopus 로고
    • Interactions between mRNA export commitment, 3'-end quality control, and nuclear degradation
    • Libri, D.; Dower, K.; Boulay, J.; Thomsen, R.; Rosbash, M.; Jensen, T.H. Interactions between mRNA export commitment, 3'-end quality control, and nuclear degradation. Mol. Cell. Biol. 2002, 22, 8254-8266.
    • (2002) Mol. Cell. Biol , vol.22 , pp. 8254-8266
    • Libri, D.1    Dower, K.2    Boulay, J.3    Thomsen, R.4    Rosbash, M.5    Jensen, T.H.6
  • 21
    • 0036889334 scopus 로고    scopus 로고
    • Stable mRNP formation and export require cotranscriptional recruitment of the mRNA export factors Yra1p and Sub2p by Hpr1p
    • Zenklusen, D.; Vinciguerra, P.; Wyss, J.-C.; Stutz, F. Stable mRNP formation and export require cotranscriptional recruitment of the mRNA export factors Yra1p and Sub2p by Hpr1p. Mol. Cell. Biol. 2002, 22, 8241-8253.
    • (2002) Mol. Cell. Biol , vol.22 , pp. 8241-8253
    • Zenklusen, D.1    Vinciguerra, P.2    Wyss, J.-C.3    Stutz, F.4
  • 22
    • 33845626622 scopus 로고    scopus 로고
    • Human mRNA export machinery recruited to the 5' end of mRNA
    • Cheng, H.; Dufu, K.; Lee, C.S.; Hsu, J.L.; Dias, A.; Reed, R. Human mRNA export machinery recruited to the 5' end of mRNA. Cell 2006, 127, 1389-1400.
    • (2006) Cell , vol.127 , pp. 1389-1400
    • Cheng, H.1    Dufu, K.2    Lee, C.S.3    Hsu, J.L.4    Dias, A.5    Reed, R.6
  • 23
    • 22344438756 scopus 로고    scopus 로고
    • Recruitment of the human TREX complex to mRNA during splicing
    • Masuda, S.; Das, R.; Cheng, H.; Hurt, E.; Dorman, N.; Reed, R. Recruitment of the human TREX complex to mRNA during splicing. Genes Dev. 2005, 19, 1512-1517.
    • (2005) Genes Dev , vol.19 , pp. 1512-1517
    • Masuda, S.1    Das, R.2    Cheng, H.3    Hurt, E.4    Dorman, N.5    Reed, R.6
  • 24
    • 0034699472 scopus 로고    scopus 로고
    • The protein Aly links pre-messenger-RNA splicing to nuclear export in metazoans
    • Zhou, Z.; Luo, M.J.; Straesser, K.; Katahira, J.; Hurt, E.; Reed, R. The protein Aly links pre-messenger-RNA splicing to nuclear export in metazoans. Nature 2000, 407, 401-405.
    • (2000) Nature , vol.407 , pp. 401-405
    • Zhou, Z.1    Luo, M.J.2    Straesser, K.3    Katahira, J.4    Hurt, E.5    Reed, R.6
  • 25
    • 0037154964 scopus 로고    scopus 로고
    • A conserved mRNA export machinery coupled to pre-mRNA splicing
    • Reed, R.; Hurt, E. A conserved mRNA export machinery coupled to pre-mRNA splicing. Cell 2002, 108, 523-531.
    • (2002) Cell , vol.108 , pp. 523-531
    • Reed, R.1    Hurt, E.2
  • 26
    • 19344363274 scopus 로고    scopus 로고
    • Cotranscriptional mRNP assembly: From the DNA to the nuclear pore
    • Aguilera, A. Cotranscriptional mRNP assembly: From the DNA to the nuclear pore. Curr. Opin. Cell Biol. 2005, 17, 242-250.
    • (2005) Curr. Opin. Cell Biol , vol.17 , pp. 242-250
    • Aguilera, A.1
  • 27
    • 34648816826 scopus 로고    scopus 로고
    • Exporting RNA from the nucleus to the cytoplasm
    • Kohler, A.; Hurt, E. Exporting RNA from the nucleus to the cytoplasm. Nat. Rev. Mol. Cell Biol. 2007, 8, 761-773.
    • (2007) Nat. Rev. Mol. Cell Biol , vol.8 , pp. 761-773
    • Kohler, A.1    Hurt, E.2
  • 28
    • 77956850226 scopus 로고    scopus 로고
    • ATP is required for interactions between UAP56 and two conserved mRNA export proteins, Aly and CIP29, to assemble the TREX complex
    • Dufu, K.; Livingstone, M.J.; Seebacher, J.; Gygi, S.P.; Wilson, S.A.; Reed, R. ATP is required for interactions between UAP56 and two conserved mRNA export proteins, Aly and CIP29, to assemble the TREX complex. Genes Dev. 2010, 24, 2043-2053.
    • (2010) Genes Dev , vol.24 , pp. 2043-2053
    • Dufu, K.1    Livingstone, M.J.2    Seebacher, J.3    Gygi, S.P.4    Wilson, S.A.5    Reed, R.6
  • 31
    • 84865279780 scopus 로고    scopus 로고
    • The proteins PDIP3 and ZC11A associate with the human TREX complex in an ATP-dependent manner and function in mRNA export
    • Folco, E.G.; Lee, C.S.; Dufu, K.; Yamazaki, T.; Reed, R. The proteins PDIP3 and ZC11A associate with the human TREX complex in an ATP-dependent manner and function in mRNA export. PLoS One 2012, 7, e43804.
    • (2012) PLoS One , vol.7
    • Folco, E.G.1    Lee, C.S.2    Dufu, K.3    Yamazaki, T.4    Reed, R.5
  • 32
    • 33751094078 scopus 로고    scopus 로고
    • The solution structure of REF2-I reveals interdomain interactions and regions involved in binding mRNA export factors and RNA
    • Golovanov, A.P.; Hautbergue, G.M.; Tintaru, A.M.; Lian, L.-Y.; Wilson, S.A. The solution structure of REF2-I reveals interdomain interactions and regions involved in binding mRNA export factors and RNA. RNA 2006, 12, 1933-1948.
    • (2006) RNA , vol.12 , pp. 1933-1948
    • Golovanov, A.P.1    Hautbergue, G.M.2    Tintaru, A.M.3    Lian, L.-Y.4    Wilson, S.A.5
  • 33
    • 77955625496 scopus 로고    scopus 로고
    • The closely related RNA helicases, UAP56 and URH49, preferentially form distinct mRNA export machineries and coordinately regulate mitotic progression
    • Yamazaki, T.; Fujiwara, N.; Yukinaga, H.; Ebisuya, M.; Shiki, T.; Kurihara, T.; Kioka, N.; Kambe, T.; Nagao, M.; Nishida, E. The closely related RNA helicases, UAP56 and URH49, preferentially form distinct mRNA export machineries and coordinately regulate mitotic progression. Mol. Biol. Cell 2010, 21, 2953-2965.
    • (2010) Mol. Biol. Cell , vol.21 , pp. 2953-2965
    • Yamazaki, T.1    Fujiwara, N.2    Yukinaga, H.3    Ebisuya, M.4    Shiki, T.5    Kurihara, T.6    Kioka, N.7    Kambe, T.8    Nagao, M.9    Nishida, E.10
  • 34
    • 37849054264 scopus 로고    scopus 로고
    • ATP-dependent recruitment of export factor Aly/REF onto intron-less mRNAs by RNA helicase UAP56
    • Taniguchi, I.; Ohno, M. ATP-dependent recruitment of export factor Aly/REF onto intron-less mRNAs by RNA helicase UAP56. Mol. Cell. Biol. 2008, 28, 601-608.
    • (2008) Mol. Cell. Biol , vol.28 , pp. 601-608
    • Taniguchi, I.1    Ohno, M.2
  • 35
    • 84875455758 scopus 로고    scopus 로고
    • Aly and THO are required for assembly of the human TREX complex and association of TREX components with the spliced mRNA
    • Chi, B.; Wang, Q.; Wu, G.; Tan, M.; Wang, L.; Shi, M.; Chang, X.; Cheng, H. Aly and THO are required for assembly of the human TREX complex and association of TREX components with the spliced mRNA. Nucleic Acids Res. 2013, 41, 1294-1306.
    • (2013) Nucleic Acids Res , vol.41 , pp. 1294-1306
    • Chi, B.1    Wang, Q.2    Wu, G.3    Tan, M.4    Wang, L.5    Shi, M.6    Chang, X.7    Cheng, H.8
  • 36
    • 19344374094 scopus 로고    scopus 로고
    • TREX, SR proteins and export of mRNA
    • Reed, R.; Cheng, H. TREX, SR proteins and export of mRNA. Curr. Opin. Cell Biol. 2005, 17, 269-273.
    • (2005) Curr. Opin. Cell Biol , vol.17 , pp. 269-273
    • Reed, R.1    Cheng, H.2
  • 37
    • 0042658190 scopus 로고    scopus 로고
    • Nuclear mRNA export: Insights from virology
    • Cullen, B.R. Nuclear mRNA export: Insights from virology. Trends Biochem. Sci. 2003, 28, 419-424.
    • (2003) Trends Biochem. Sci , vol.28 , pp. 419-424
    • Cullen, B.R.1
  • 38
    • 0038697629 scopus 로고    scopus 로고
    • The interplay of nuclear mRNP assembly, mRNA surveillance and export
    • Stutz, F.; Izaurralde, E. The interplay of nuclear mRNP assembly, mRNA surveillance and export. Trends Cell Biol. 2003, 13, 319-327.
    • (2003) Trends Cell Biol , vol.13 , pp. 319-327
    • Stutz, F.1    Izaurralde, E.2
  • 39
    • 81055126291 scopus 로고    scopus 로고
    • Export and stability of naturally intron-less mRNAs require specific coding region sequences and the TREX mRNA export complex
    • Lei, H.; Dias, A.P.; Reed, R. Export and stability of naturally intron-less mRNAs require specific coding region sequences and the TREX mRNA export complex. Proc. Natl. Acad. Sci. USA 2011, 108, 17985-17990.
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 17985-17990
    • Lei, H.1    Dias, A.P.2    Reed, R.3
  • 40
    • 84876359822 scopus 로고    scopus 로고
    • Evidence that a consensus element found in naturally intron-less mRNAs promotes mRNA export
    • Lei, H.; Zhai, B.; Yin, S.; Gygi, S.; Reed, R. Evidence that a consensus element found in naturally intron-less mRNAs promotes mRNA export. Nucleic Acids Res. 2013, 41, 2517-2525.
    • (2013) Nucleic Acids Res , vol.41 , pp. 2517-2525
    • Lei, H.1    Zhai, B.2    Yin, S.3    Gygi, S.4    Reed, R.5
  • 41
    • 0033788228 scopus 로고    scopus 로고
    • The ends of the affair: Capping and polyadenylation
    • Shatkin, A.J.; Manley, J.L. The ends of the affair: Capping and polyadenylation. Nat. Struct. Mol. Biol. 2000, 7, 838-842.
    • (2000) Nat. Struct. Mol. Biol , vol.7 , pp. 838-842
    • Shatkin, A.J.1    Manley, J.L.2
  • 42
    • 0036645697 scopus 로고    scopus 로고
    • The exon junction complex is detected on CBP80-bound but not eIF4E-bound mRNA in mammalian cells: Dynamics of mRNP remodeling
    • Lejeune, F.; Ishigaki, Y.; Li, X.; Maquat, L.E. The exon junction complex is detected on CBP80-bound but not eIF4E-bound mRNA in mammalian cells: Dynamics of mRNP remodeling. EMBO J. 2002, 21, 3536-3545.
    • (2002) EMBO J , vol.21 , pp. 3536-3545
    • Lejeune, F.1    Ishigaki, Y.2    Li, X.3    Maquat, L.E.4
  • 43
    • 0035846138 scopus 로고    scopus 로고
    • Pre-mRNA splicing and mRNA export linked by direct interactions between UAP56 and Aly
    • Luo, M.-J.; Zhou, Z.; Magni, K.; Christoforides, C.; Rappsilber, J.; Mann, M.; Reed, R. Pre-mRNA splicing and mRNA export linked by direct interactions between UAP56 and Aly. Nature 2001, 413, 644-647.
    • (2001) Nature , vol.413 , pp. 644-647
    • Luo, M.-J.1    Zhou, Z.2    Magni, K.3    Christoforides, C.4    Rappsilber, J.5    Mann, M.6    Reed, R.7
  • 44
    • 0034672093 scopus 로고    scopus 로고
    • The spliceosome deposits multiple proteins 20-24 nucleotides upstream of mRNA exon-exon junctions
    • Le Hir, H.; Izaurralde, E.; Maquat, L.E.; Moore, M.J. The spliceosome deposits multiple proteins 20-24 nucleotides upstream of mRNA exon-exon junctions. EMBO J. 2000, 19, 6860-6869.
    • (2000) EMBO J , vol.19 , pp. 6860-6869
    • Le Hir, H.1    Izaurralde, E.2    Maquat, L.E.3    Moore, M.J.4
  • 45
    • 34248585758 scopus 로고    scopus 로고
    • The nuclear nurture and cytoplasmic nature of localized mRNPs
    • Giorgi, C.; Moore, M.J. The nuclear nurture and cytoplasmic nature of localized mRNPs. Semin. Cell Dev. Biol. 2007, 18, 186-193.
    • (2007) Semin. Cell Dev. Biol , vol.18 , pp. 186-193
    • Giorgi, C.1    Moore, M.J.2
  • 46
    • 0942268832 scopus 로고    scopus 로고
    • Splicing enhances translation in mammalian cells: An additional function of the exon junction complex
    • Nott, A.; le Hir, H.; Moore, M.J. Splicing enhances translation in mammalian cells: An additional function of the exon junction complex. Genes Dev. 2004, 18, 210-222.
    • (2004) Genes Dev , vol.18 , pp. 210-222
    • Nott, A.1    Le Hir, H.2    Moore, M.J.3
  • 47
    • 34247197937 scopus 로고    scopus 로고
    • The nonsense-mediated decay RNA surveillance pathway
    • Chang, Y.-F.; Imam, J.S.; Wilkinson, M.F. The nonsense-mediated decay RNA surveillance pathway. Annu. Rev. Biochem. 2007, 76, 51-74.
    • (2007) Annu. Rev. Biochem , vol.76 , pp. 51-74
    • Chang, Y.-F.1    Imam, J.S.2    Wilkinson, M.F.3
  • 48
    • 36849049323 scopus 로고    scopus 로고
    • PYM binds the cytoplasmic exon-junction complex and ribosomes to enhance translation of spliced mRNAs
    • Diem, M.D.; Chan, C.C.; Younis, I.; Dreyfuss, G. PYM binds the cytoplasmic exon-junction complex and ribosomes to enhance translation of spliced mRNAs. Nat. Struct. Mol. Biol. 2007, 14, 1173-1179.
    • (2007) Nat. Struct. Mol. Biol , vol.14 , pp. 1173-1179
    • Diem, M.D.1    Chan, C.C.2    Younis, I.3    Dreyfuss, G.4
  • 49
    • 41949101770 scopus 로고    scopus 로고
    • SKAR links pre-mRNA splicing to mTOR/S6K1-mediated enhanced translation efficiency of spliced mRNAs
    • Ma, X.M.; Yoon, S.O.; Richardson, C.J.; Julich, K.; Blenis, J. SKAR links pre-mRNA splicing to mTOR/S6K1-mediated enhanced translation efficiency of spliced mRNAs. Cell 2008, 133, 303-313.
    • (2008) Cell , vol.133 , pp. 303-313
    • Ma, X.M.1    Yoon, S.O.2    Richardson, C.J.3    Julich, K.4    Blenis, J.5
  • 52
    • 62049085851 scopus 로고    scopus 로고
    • Adaptor Aly and co-adaptor Thoc5 function in the Tap-p15-mediated nuclear export of HSP70 mRNA
    • Katahira, J.; Inoue, H.; Hurt, E.; Yoneda, Y. Adaptor Aly and co-adaptor Thoc5 function in the Tap-p15-mediated nuclear export of HSP70 mRNA. EMBO J. 2009, 28, 556-567.
    • (2009) EMBO J , vol.28 , pp. 556-567
    • Katahira, J.1    Inoue, H.2    Hurt, E.3    Yoneda, Y.4
  • 53
    • 0344211508 scopus 로고    scopus 로고
    • SR splicing factors serve as adapter proteins for TAP-dependent mRNA export
    • Huang, Y.; Gattoni, R.; Stevenin, J.; Steitz, J.A. SR splicing factors serve as adapter proteins for TAP-dependent mRNA export. Mol. Cell 2003, 11, 837-843.
    • (2003) Mol. Cell , vol.11 , pp. 837-843
    • Huang, Y.1    Gattoni, R.2    Stevenin, J.3    Steitz, J.A.4
  • 54
    • 58649121693 scopus 로고    scopus 로고
    • Cotranscriptional recruitment of the mRNA export factor Yra1 by direct interaction with the 3' end processing factor Pcf11
    • Johnson, S.A.; Cubberley, G.; Bentley, D.L. Cotranscriptional recruitment of the mRNA export factor Yra1 by direct interaction with the 3' end processing factor Pcf11. Mol. Cell 2009, 33, 215-226.
    • (2009) Mol. Cell , vol.33 , pp. 215-226
    • Johnson, S.A.1    Cubberley, G.2    Bentley, D.L.3
  • 56
    • 84863182811 scopus 로고    scopus 로고
    • The interaction of Pcf11 and Clp1 is needed for mRNA 3'-end formation and is modulated by amino acids in the ATP-binding site
    • Ghazy, M.A.; Gordon, J.M.B.; Lee, S.D.; Singh, B.N.; Bohm, A.; Hampsey, M.; Moore, C. The interaction of Pcf11 and Clp1 is needed for mRNA 3'-end formation and is modulated by amino acids in the ATP-binding site. Nucleic Acids Res. 2012, 40, 1214-1225.
    • (2012) Nucleic Acids Res , vol.40 , pp. 1214-1225
    • Ghazy, M.A.1    Gordon, J.M.B.2    Lee, S.D.3    Singh, B.N.4    Bohm, A.5    Hampsey, M.6    Moore, C.7
  • 58
    • 84880824954 scopus 로고    scopus 로고
    • Human TREX component Thoc5 affects alternative polyadenylation site choice by recruiting mammalian cleavage factor I
    • doi: 10.1093/nar/gkt414
    • Katahira, J.; Okuzaki, D.; Inoue, H.; Yoneda, Y.; Maehara, K.; Ohkawa, Y. Human TREX component Thoc5 affects alternative polyadenylation site choice by recruiting mammalian cleavage factor I. Nucleic Acids Res. 2013, doi: 10.1093/nar/gkt414.
    • (2013) Nucleic Acids Res
    • Katahira, J.1    Okuzaki, D.2    Inoue, H.3    Yoneda, Y.4    Maehara, K.5    Ohkawa, Y.6
  • 59
    • 80052979140 scopus 로고    scopus 로고
    • Mechanisms and consequences of alternative polyadenylation
    • Di Giammartino, D.C.; Nishida, K.; Manley, J.L. Mechanisms and consequences of alternative polyadenylation. Mol. Cell 2011, 43, 853-866.
    • (2011) Mol. Cell , vol.43 , pp. 853-866
    • Di Giammartino, D.C.1    Nishida, K.2    Manley, J.L.3
  • 63
    • 33846702294 scopus 로고    scopus 로고
    • Ratcheting mRNA out of the nucleus
    • Stewart, M. Ratcheting mRNA out of the nucleus. Mol. Cell 2007, 25, 327-330.
    • (2007) Mol. Cell , vol.25 , pp. 327-330
    • Stewart, M.1
  • 64
    • 0027955795 scopus 로고
    • A small element from the Mason-Pfizer monkey virus genome makes human immunodeficiency virus type 1 expression and replication Rev-independent
    • Bray, M.; Prasad, S.; Dubay, J.W.; Hunter, E.; Jeang, K.T.; Rekosh, D.; Hammarskjöld, M.L. A small element from the Mason-Pfizer monkey virus genome makes human immunodeficiency virus type 1 expression and replication Rev-independent. Proc. Natl. Acad. Sci. USA 1994, 91, 1256-1260.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 1256-1260
    • Bray, M.1    Prasad, S.2    Dubay, J.W.3    Hunter, E.4    Jeang, K.T.5    Rekosh, D.6    Hammarskjöld, M.L.7
  • 66
    • 77951049855 scopus 로고    scopus 로고
    • Individual influenza A virus mRNAs show differential dependence on cellular NXF1/TAP for their nuclear export
    • Read, E.K.C.; Digard, P. Individual influenza A virus mRNAs show differential dependence on cellular NXF1/TAP for their nuclear export. J. Gen. Virol. 2010, 91, 1290-1301.
    • (2010) J. Gen. Virol , vol.91 , pp. 1290-1301
    • Read, E.K.C.1    Digard, P.2
  • 67
    • 0037443026 scopus 로고    scopus 로고
    • Nuclear RNA export
    • Cullen, B.R. Nuclear RNA export. J. Cell Sci. 2003, 116, 587-597.
    • (2003) J. Cell Sci , vol.116 , pp. 587-597
    • Cullen, B.R.1
  • 68
    • 0030701840 scopus 로고    scopus 로고
    • Molecular cloning and cell cycle-dependent expression of mammalian CRM1, a protein involved in nuclear export of proteins
    • Kudo, N.; Khochbin, S.; Nishi, K.; Kitano, K.; Yanagida, M.; Yoshida, M.; Horinouchi, S. Molecular cloning and cell cycle-dependent expression of mammalian CRM1, a protein involved in nuclear export of proteins. J. Biol. Chem. 1997, 272, 29742-29751.
    • (1997) J. Biol. Chem , vol.272 , pp. 29742-29751
    • Kudo, N.1    Khochbin, S.2    Nishi, K.3    Kitano, K.4    Yanagida, M.5    Yoshida, M.6    Horinouchi, S.7
  • 70
    • 0034597057 scopus 로고    scopus 로고
    • Protein ligands to HuR modulate its interaction with target mRNAs in vivo
    • Brennan, C.M.; Gallouzi, I.-E.; Steitz, J.A. Protein ligands to HuR modulate its interaction with target mRNAs in vivo. J. Cell Biol. 2000, 151, 1-14.
    • (2000) J. Cell Biol , vol.151 , pp. 1-14
    • Brennan, C.M.1    Gallouzi, I.-E.2    Steitz, J.A.3
  • 71
    • 0034671768 scopus 로고    scopus 로고
    • Phosphorylation-dependent regulation of cyclin D1 nuclear export and cyclin D1-dependent cellular transformation
    • Alt, J.R.; Cleveland, J.L.; Hannink, M.; Diehl, J.A. Phosphorylation-dependent regulation of cyclin D1 nuclear export and cyclin D1-dependent cellular transformation. Genes Dev. 2000, 14, 3102-3114.
    • (2000) Genes Dev , vol.14 , pp. 3102-3114
    • Alt, J.R.1    Cleveland, J.L.2    Hannink, M.3    Diehl, J.A.4
  • 72
    • 0030924190 scopus 로고    scopus 로고
    • CRM1 is an export receptor for leucine-rich nuclear export signals
    • Fornerod, M.; Ohno, M.; Yoshida, M.; Mattaj, I.W. CRM1 is an export receptor for leucine-rich nuclear export signals. Cell 1997, 90, 1051-1060.
    • (1997) Cell , vol.90 , pp. 1051-1060
    • Fornerod, M.1    Ohno, M.2    Yoshida, M.3    Mattaj, I.W.4
  • 73
    • 0029130169 scopus 로고
    • The HIV-1 Rev activation domain is a nuclear export signal that accesses an export pathway used by specific cellular RNAs
    • Fischer, U.; Huber, J.; Boelens, W.C.; Mattajt, L.W.; Lührmann, R. The HIV-1 Rev activation domain is a nuclear export signal that accesses an export pathway used by specific cellular RNAs. Cell 1995, 82, 475-483.
    • (1995) Cell , vol.82 , pp. 475-483
    • Fischer, U.1    Huber, J.2    Boelens, W.C.3    Mattajt, L.W.4    Lührmann, R.5
  • 74
    • 0027376308 scopus 로고
    • The GTP-binding protein Ran/TC4 is required for protein import into the nucleus
    • Moore, M.S.; Blobel, G. The GTP-binding protein Ran/TC4 is required for protein import into the nucleus. Nature 1993, 365, 661-663.
    • (1993) Nature , vol.365 , pp. 661-663
    • Moore, M.S.1    Blobel, G.2
  • 75
    • 0032483384 scopus 로고    scopus 로고
    • Ran and nuclear transport
    • Moore, M.S. Ran and nuclear transport. J. Biol. Chem. 1998, 273, 22857-22860.
    • (1998) J. Biol. Chem , vol.273 , pp. 22857-22860
    • Moore, M.S.1
  • 76
    • 0033279841 scopus 로고    scopus 로고
    • Transport between the cell nucleus and the cytoplasm
    • Görlich, D.; Kutay, U. Transport between the cell nucleus and the cytoplasm. Annu. Rev. Cell Dev. Biol. 1999, 15, 607-660.
    • (1999) Annu. Rev. Cell Dev. Biol , vol.15 , pp. 607-660
    • Görlich, D.1    Kutay, U.2
  • 77
    • 0025818452 scopus 로고
    • HIV-1 structural gene expression requires the binding of multiple Rev monomers to the viral RRE: Implications for HIV-1 latency
    • Malim, M.H.; Cullen, B.R. HIV-1 structural gene expression requires the binding of multiple Rev monomers to the viral RRE: Implications for HIV-1 latency. Cell 1991, 65, 241-248.
    • (1991) Cell , vol.65 , pp. 241-248
    • Malim, M.H.1    Cullen, B.R.2
  • 78
    • 0024518918 scopus 로고
    • The HIV-1 rev trans-activator acts through a structured target sequence to activate nuclear export of unspliced viral mRNA
    • Malim, M.H.; Hauber, J.; Le, S.-Y.; Maizel, J.V.; Cullen, B.R. The HIV-1 rev trans-activator acts through a structured target sequence to activate nuclear export of unspliced viral mRNA. Nature 1989, 338, 254-257.
    • (1989) Nature , vol.338 , pp. 254-257
    • Malim, M.H.1    Hauber, J.2    Le, S.-Y.3    Maizel, J.V.4    Cullen, B.R.5
  • 79
    • 0031878580 scopus 로고    scopus 로고
    • Involvement of human CRM1 (exportin 1) in the export and multimerization of the Rex protein of human T-cell leukemia virus type 1
    • Hakata, Y.; Umemoto, T.; Matsushita, S.; Shida, H. Involvement of human CRM1 (exportin 1) in the export and multimerization of the Rex protein of human T-cell leukemia virus type 1. J. Virol. 1998, 72, 6602-6607.
    • (1998) J. Virol , vol.72 , pp. 6602-6607
    • Hakata, Y.1    Umemoto, T.2    Matsushita, S.3    Shida, H.4
  • 80
    • 84875852858 scopus 로고    scopus 로고
    • HTLV-1 Rex: The courier of viral messages, making use of the host vehicle
    • Nakano, K.; Watanabe, T. HTLV-1 Rex: The courier of viral messages, making use of the host vehicle. Front. Microbiol. 2012, 3, e330.
    • (2012) Front. Microbiol , vol.3
    • Nakano, K.1    Watanabe, T.2
  • 81
    • 84875774017 scopus 로고    scopus 로고
    • Role of nucleocytoplasmic RNA transport during the life cycle of retroviruses
    • Shida, H. Role of nucleocytoplasmic RNA transport during the life cycle of retroviruses. Front. Microbiol. 2012, 3, e179.
    • (2012) Front. Microbiol , vol.3
    • Shida, H.1
  • 82
    • 84860852545 scopus 로고    scopus 로고
    • Nuclear envelope budding enables large ribonucleoprotein particle export during synaptic Wnt signaling
    • Speese, S.D.; Ashley, J.; Jokhi, V.; Nunnari, J.; Barria, R.; Li, Y.; Ataman, B.; Koon, A.; Chang, Y.-T.; Li, Q. Nuclear envelope budding enables large ribonucleoprotein particle export during synaptic Wnt signaling. Cell 2012, 149, 832-846.
    • (2012) Cell , vol.149 , pp. 832-846
    • Speese, S.D.1    Ashley, J.2    Jokhi, V.3    Nunnari, J.4    Barria, R.5    Li, Y.6    Ataman, B.7    Koon, A.8    Chang, Y.-T.9    Li, Q.10
  • 83
    • 0036347096 scopus 로고    scopus 로고
    • Life at the edge: The nuclear envelope and human disease
    • Burke, B.; Stewart, C.L. Life at the edge: The nuclear envelope and human disease. Nat. Rev. Mol. Cell Biol. 2002, 3, 575-585.
    • (2002) Nat. Rev. Mol. Cell Biol , vol.3 , pp. 575-585
    • Burke, B.1    Stewart, C.L.2
  • 85
  • 86
    • 77953302554 scopus 로고    scopus 로고
    • Escape of herpesviruses from the nucleus
    • Lee, C.-P.; Chen, M.-R. Escape of herpesviruses from the nucleus. Rev. Med. Virol. 2010, 20, 214-230.
    • (2010) Rev. Med. Virol , vol.20 , pp. 214-230
    • Lee, C.-P.1    Chen, M.-R.2
  • 87
    • 55449092922 scopus 로고    scopus 로고
    • Recruitment of the complete hTREX complex is required for Kaposi's sarcoma-associated herpesvirus intron-less mRNA nuclear export and virus replication
    • Boyne, J.R.; Colgan, K.J.; Whitehouse, A. Recruitment of the complete hTREX complex is required for Kaposi's sarcoma-associated herpesvirus intron-less mRNA nuclear export and virus replication. PLoS Pathog. 2008, 4, e1000194.
    • (2008) PLoS Pathog , vol.4
    • Boyne, J.R.1    Colgan, K.J.2    Whitehouse, A.3
  • 88
    • 71749109176 scopus 로고    scopus 로고
    • Nucleolar disruption impairs Kaposi's sarcoma-associated herpesvirus ORF57-mediated nuclear export of intron-less viral mRNAs
    • Boyne, J.R.; Whitehouse, A. Nucleolar disruption impairs Kaposi's sarcoma-associated herpesvirus ORF57-mediated nuclear export of intron-less viral mRNAs. FEBS Lett. 2009, 583, 3549-3556.
    • (2009) FEBS Lett , vol.583 , pp. 3549-3556
    • Boyne, J.R.1    Whitehouse, A.2
  • 89
    • 79960396328 scopus 로고    scopus 로고
    • Mutation of a C-terminal motif affects Kaposi's sarcoma-associated herpesvirus ORF57 RNA binding, nuclear trafficking, and multimerization
    • Taylor, A.; Jackson, B.R.; Noerenberg, M.; Hughes, D.J.; Boyne, J.R.; Verow, M.; Harris, M.; Whitehouse, A. Mutation of a C-terminal motif affects Kaposi's sarcoma-associated herpesvirus ORF57 RNA binding, nuclear trafficking, and multimerization. J. Virol. 2011, 85, 7881-7891.
    • (2011) J. Virol , vol.85 , pp. 7881-7891
    • Taylor, A.1    Jackson, B.R.2    Noerenberg, M.3    Hughes, D.J.4    Boyne, J.R.5    Verow, M.6    Harris, M.7    Whitehouse, A.8
  • 90
    • 3542999242 scopus 로고    scopus 로고
    • The evolutionarily conserved Kaposi's sarcoma-associated herpesvirus ORF57 protein interacts with REF protein and acts as an RNA export factor
    • Malik, P.; Blackbourn, D.J.; Clements, J.B. The evolutionarily conserved Kaposi's sarcoma-associated herpesvirus ORF57 protein interacts with REF protein and acts as an RNA export factor. J. Biol. Chem. 2004, 279, 33001-33011.
    • (2004) J. Biol. Chem , vol.279 , pp. 33001-33011
    • Malik, P.1    Blackbourn, D.J.2    Clements, J.B.3
  • 91
    • 40149095094 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus ORF57 functions as a viral splicing factor and promotes expression of intron-containing viral lytic genes in spliceosome-mediated RNA splicing
    • Majerciak, V.; Yamanegi, K.; Allemand, E.; Kruhlak, M.; Krainer, A.R.; Zheng, Z.M., Kaposi's sarcoma-associated herpesvirus ORF57 functions as a viral splicing factor and promotes expression of intron-containing viral lytic genes in spliceosome-mediated RNA splicing. J. Virol. 2008, 82, 2792-2801.
    • (2008) J. Virol , vol.82 , pp. 2792-2801
    • Majerciak, V.1    Yamanegi, K.2    Allemand, E.3    Kruhlak, M.4    Krainer, A.R.5    Zheng, Z.M.6
  • 92
    • 52049115835 scopus 로고    scopus 로고
    • The many roles of the regulatory protein ICP27 during herpes simplex virus infection
    • Sandri-Goldin, R.M. The many roles of the regulatory protein ICP27 during herpes simplex virus infection. Front. Biosci. 2008, 13, 5241-5256.
    • (2008) Front. Biosci , vol.13 , pp. 5241-5256
    • Sandri-Goldin, R.M.1
  • 93
    • 0032521214 scopus 로고    scopus 로고
    • ICP27 mediates HSV RNA export by shuttling through a leucine-rich nuclear export signal and binding viral intron-less RNAs through an RGG motif
    • Sandri-Goldin, R.M. ICP27 mediates HSV RNA export by shuttling through a leucine-rich nuclear export signal and binding viral intron-less RNAs through an RGG motif. Genes Dev. 1998, 12, 868-879.
    • (1998) Genes Dev , vol.12 , pp. 868-879
    • Sandri-Goldin, R.M.1
  • 94
    • 0031743482 scopus 로고    scopus 로고
    • Mta has properties of an RNA export protein and increases cytoplasmic accumulation of Epstein-Barr virus replication gene mRNA
    • Semmes, O.J.; Chen, L.; Sarisky, R.T.; Gao, Z.; Zhong, L.; Hayward, S.D. Mta has properties of an RNA export protein and increases cytoplasmic accumulation of Epstein-Barr virus replication gene mRNA. J. Virol. 1998, 72, 9526-9534.
    • (1998) J. Virol , vol.72 , pp. 9526-9534
    • Semmes, O.J.1    Chen, L.2    Sarisky, R.T.3    Gao, Z.4    Zhong, L.5    Hayward, S.D.6
  • 95
    • 0346365296 scopus 로고    scopus 로고
    • Functional analysis of Epstein-Barr virus SM protein: Identification of amino acids essential for structure, transactivation, splicing inhibition, and virion production
    • Ruvolo, V.; Sun, L.; Howard, K.; Sung, S.; Delecluse, H.J.; Hammerschmidt, W.; Swaminathan, S. Functional analysis of Epstein-Barr virus SM protein: Identification of amino acids essential for structure, transactivation, splicing inhibition, and virion production. J. Virol. 2004, 78, 340-352.
    • (2004) J. Virol , vol.78 , pp. 340-352
    • Ruvolo, V.1    Sun, L.2    Howard, K.3    Sung, S.4    Delecluse, H.J.5    Hammerschmidt, W.6    Swaminathan, S.7
  • 96
    • 38449102461 scopus 로고    scopus 로고
    • The human cytomegalovirus regulatory protein UL69 and its effect on mRNA export
    • Toth, Z.; Stamminger, T. The human cytomegalovirus regulatory protein UL69 and its effect on mRNA export. Front. Biosci. 2008, 13, 2939-2949.
    • (2008) Front. Biosci , vol.13 , pp. 2939-2949
    • Toth, Z.1    Stamminger, T.2
  • 98
    • 33750053559 scopus 로고    scopus 로고
    • Nucleolar trafficking is essential for nuclear export of intron-less herpesvirus mRNA
    • Boyne, J.R.; Whitehouse, A. Nucleolar trafficking is essential for nuclear export of intron-less herpesvirus mRNA. Proc. Natl. Acad. Sci. USA 2006, 103, 15190-15195.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 15190-15195
    • Boyne, J.R.1    Whitehouse, A.2
  • 99
    • 38449087806 scopus 로고    scopus 로고
    • Herpesvirus saimiri ORF57: A post-transcriptional regulatory protein
    • Boyne, J.R.; Colgan, K.J.; Whitehouse, A. Herpesvirus saimiri ORF57: A post-transcriptional regulatory protein. Front. Biosci. 2008, 13, 2928-2938.
    • (2008) Front. Biosci , vol.13 , pp. 2928-2938
    • Boyne, J.R.1    Colgan, K.J.2    Whitehouse, A.3
  • 100
    • 67649220993 scopus 로고    scopus 로고
    • Uncoupling of hTREX demonstrates that UAP56 and hTHO-complex recruitment onto herpesvirus saimiri intron-less transcripts is required for replication
    • Colgan, K.J.; Boyne, J.R.; Whitehouse, A. Uncoupling of hTREX demonstrates that UAP56 and hTHO-complex recruitment onto herpesvirus saimiri intron-less transcripts is required for replication. J. Gen. Virol. 2009, 90, 1455-1460.
    • (2009) J. Gen. Virol , vol.90 , pp. 1455-1460
    • Colgan, K.J.1    Boyne, J.R.2    Whitehouse, A.3
  • 101
    • 0033832979 scopus 로고    scopus 로고
    • The carboxy terminus of the herpesvirus saimiri ORF 57 gene contains domains that are required for transactivation and transrepression
    • Goodwin, D.J.; Hall, K.T.; Giles, M.S.; Calderwood, M.A.; Markham, A.F.; Whitehouse, A. The carboxy terminus of the herpesvirus saimiri ORF 57 gene contains domains that are required for transactivation and transrepression. J. Gen. Virol. 2000, 81, 2253-2265.
    • (2000) J. Gen. Virol , vol.81 , pp. 2253-2265
    • Goodwin, D.J.1    Hall, K.T.2    Giles, M.S.3    Calderwood, M.A.4    Markham, A.F.5    Whitehouse, A.6
  • 102
    • 77950439778 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus ORF57 protein binds and protects a nuclear noncoding RNA from cellular RNA decay pathways
    • Sahin, B.B.; Patel, D.; Conrad, N.K. Kaposi's sarcoma-associated herpesvirus ORF57 protein binds and protects a nuclear noncoding RNA from cellular RNA decay pathways. PLoS Pathog. 2010, 6, e1000799.
    • (2010) PLoS Pathog , vol.6
    • Sahin, B.B.1    Patel, D.2    Conrad, N.K.3
  • 103
    • 4043147875 scopus 로고    scopus 로고
    • Functional co-operation between the Kaposi's sarcoma-associated herpesvirus ORF57 and ORF50 regulatory proteins
    • Malik, P.; Blackbourn, D.J.; Cheng, M.F.; Hayward, G.S.; Clements, J.B. Functional co-operation between the Kaposi's sarcoma-associated herpesvirus ORF57 and ORF50 regulatory proteins. J. Gen. Virol. 2004, 85, 2155-2166.
    • (2004) J. Gen. Virol , vol.85 , pp. 2155-2166
    • Malik, P.1    Blackbourn, D.J.2    Cheng, M.F.3    Hayward, G.S.4    Clements, J.B.5
  • 104
    • 77953123485 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus ORF57 protein interacts with PYM to enhance translation of viral intron-less mRNAs
    • Boyne, J.R.; Jackson, B.R.; Taylor, A.; Macnab, S.A.; Whitehouse, A. Kaposi's sarcoma-associated herpesvirus ORF57 protein interacts with PYM to enhance translation of viral intron-less mRNAs. EMBO J. 2010, 29, 1851-1864.
    • (2010) EMBO J , vol.29 , pp. 1851-1864
    • Boyne, J.R.1    Jackson, B.R.2    Taylor, A.3    Macnab, S.A.4    Whitehouse, A.5
  • 106
    • 33751280939 scopus 로고    scopus 로고
    • The Kaposi's sarcoma-associated herpesvirus ORF57 protein: A pleurotropic regulator of gene expression
    • Malik, P.; Schirmer, E.C. The Kaposi's sarcoma-associated herpesvirus ORF57 protein: A pleurotropic regulator of gene expression. Biochem. Soc. Trans. 2006, 34, 705-710.
    • (2006) Biochem. Soc. Trans , vol.34 , pp. 705-710
    • Malik, P.1    Schirmer, E.C.2
  • 107
    • 84865289392 scopus 로고    scopus 로고
    • The Kaposi's sarcoma-associated herpesvirus ORF57 protein and its multiple roles in mRNA biogenesis
    • Jackson, B.R.; Noerenberg, M.; Whitehouse, A. The Kaposi's sarcoma-associated herpesvirus ORF57 protein and its multiple roles in mRNA biogenesis. Front. Microbiol. 2012, 3, e59.
    • (2012) Front. Microbiol , vol.3
    • Jackson, B.R.1    Noerenberg, M.2    Whitehouse, A.3
  • 108
    • 33748788787 scopus 로고    scopus 로고
    • Structural and functional analyses of Kaposi sarcoma-associated herpesvirus ORF57 nuclear localization signals in living cells
    • Majerciak, V.; Yamanegi, K.; Nie, S.H.; Zheng, Z.M. Structural and functional analyses of Kaposi sarcoma-associated herpesvirus ORF57 nuclear localization signals in living cells. J. Biol. Chem. 2006, 281, 28365-28378.
    • (2006) J. Biol. Chem , vol.281 , pp. 28365-28378
    • Majerciak, V.1    Yamanegi, K.2    Nie, S.H.3    Zheng, Z.M.4
  • 110
    • 0035827596 scopus 로고    scopus 로고
    • A gamma-2 herpesvirus nucleocytoplasmic shuttle protein interacts with importin alpha 1 and alpha 5
    • Goodwin, D.J.; Whitehouse, A. A gamma-2 herpesvirus nucleocytoplasmic shuttle protein interacts with importin alpha 1 and alpha 5. J. Biol. Chem. 2001, 276, 19905-19912.
    • (2001) J. Biol. Chem , vol.276 , pp. 19905-19912
    • Goodwin, D.J.1    Whitehouse, A.2
  • 111
    • 17644394248 scopus 로고    scopus 로고
    • The prototype gamma-2 herpesvirus nucleocytoplasmic shuttling protein, ORF 57, transports viral RNA through the cellular mRNA export pathway
    • Williams, B.J.; Boyne, J.R.; Goodwin, D.J.; Roaden, L.; Hautbergue, G.M.; Wilson, S.A.; Whitehouse, A. The prototype gamma-2 herpesvirus nucleocytoplasmic shuttling protein, ORF 57, transports viral RNA through the cellular mRNA export pathway. Biochem. J. 2005, 387, 295-308.
    • (2005) Biochem. J , vol.387 , pp. 295-308
    • Williams, B.J.1    Boyne, J.R.2    Goodwin, D.J.3    Roaden, L.4    Hautbergue, G.M.5    Wilson, S.A.6    Whitehouse, A.7
  • 112
    • 84866169180 scopus 로고    scopus 로고
    • Binding of cellular export factor REF/Aly by Kaposi's sarcoma-associated herpesvirus (KSHV) ORF57 protein is not required for efficient KSHV lytic replication
    • Li, D.-J.; Verma, D.; Swaminathan, S. Binding of cellular export factor REF/Aly by Kaposi's sarcoma-associated herpesvirus (KSHV) ORF57 protein is not required for efficient KSHV lytic replication. J. Virol. 2012, 86, 9866-9874.
    • (2012) J. Virol , vol.86 , pp. 9866-9874
    • Li, D.-J.1    Verma, D.2    Swaminathan, S.3
  • 113
    • 35348914370 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus ORF57 protein enhances mRNA accumulation independently of effects on nuclear RNA export
    • Nekorchuk, M.; Han, Z.; Hsieh, T.T.; Swaminathan, S. Kaposi's sarcoma-associated herpesvirus ORF57 protein enhances mRNA accumulation independently of effects on nuclear RNA export. J. Virol. 2007, 81, 9990-9998.
    • (2007) J. Virol , vol.81 , pp. 9990-9998
    • Nekorchuk, M.1    Han, Z.2    Hsieh, T.T.3    Swaminathan, S.4
  • 114
    • 78951490537 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus ORF57 interacts with cellular RNA export cofactors RBM15 and OTT3 to promote expression of viral ORF59
    • Majerciak, V.; Uranishi, H.; Kruhlak, M.; Pilkington, G.R.; Massimelli, M.J.; Bear, J.; Pavlakis, G.N.; Felber, B.K.; Zheng, Z.-M. Kaposi's sarcoma-associated herpesvirus ORF57 interacts with cellular RNA export cofactors RBM15 and OTT3 to promote expression of viral ORF59. J. Virol. 2011, 85, 1528-1540.
    • (2011) J. Virol , vol.85 , pp. 1528-1540
    • Majerciak, V.1    Uranishi, H.2    Kruhlak, M.3    Pilkington, G.R.4    Massimelli, M.J.5    Bear, J.6    Pavlakis, G.N.7    Felber, B.K.8    Zheng, Z.-M.9
  • 115
    • 84880371226 scopus 로고    scopus 로고
    • The interaction of the cellular export adaptor protein Aly/REF with ICP27 contributes to the efficiency of herpes simplex virus 1 mRNA export
    • Tian, X.; Devi-Rao, G.; Golovanov, A.P.; Sandri-Goldin, R.M. The interaction of the cellular export adaptor protein Aly/REF with ICP27 contributes to the efficiency of herpes simplex virus 1 mRNA export. J. Virol. 2013, 87, 7210-7217.
    • (2013) J. Virol , vol.87 , pp. 7210-7217
    • Tian, X.1    Devi-Rao, G.2    Golovanov, A.P.3    Sandri-Goldin, R.M.4
  • 117
    • 67449086121 scopus 로고    scopus 로고
    • The cellular RNA export receptor TAP/NXF1 is required for ICP27-mediated export of herpes simplex virus 1 RNA, but the TREX complex adaptor protein Aly/REF appears to be dispensable
    • Johnson, L.A.; Li, L.; Sandri-Goldin, R.M. The cellular RNA export receptor TAP/NXF1 is required for ICP27-mediated export of herpes simplex virus 1 RNA, but the TREX complex adaptor protein Aly/REF appears to be dispensable. J. Virol. 2009, 83, 6335-6346.
    • (2009) J. Virol , vol.83 , pp. 6335-6346
    • Johnson, L.A.1    Li, L.2    Sandri-Goldin, R.M.3
  • 118
    • 0037414768 scopus 로고    scopus 로고
    • A novel nuclear export signal and a REF interaction domain both promote mRNA export by the Epstein-Barr virus EB2 protein
    • Hiriart, E.; Farjot, G.; Gruffat, H.; Nguyen, M.V.C.; Sergeant, A.; Manet, E. A novel nuclear export signal and a REF interaction domain both promote mRNA export by the Epstein-Barr virus EB2 protein. J. Biol. Chem. 2003, 278, 335-342.
    • (2003) J. Biol. Chem , vol.278 , pp. 335-342
    • Hiriart, E.1    Farjot, G.2    Gruffat, H.3    Nguyen, M.V.C.4    Sergeant, A.5    Manet, E.6
  • 119
    • 33644518219 scopus 로고    scopus 로고
    • The UL69 transactivator protein of human cytomegalovirus interacts with DEXD/H-box RNA helicase UAP56 to promote cytoplasmic accumulation of unspliced RNA
    • Lischka, P.; Toth, Z.; Thomas, M.; Mueller, R.; Stamminger, T. The UL69 transactivator protein of human cytomegalovirus interacts with DEXD/H-box RNA helicase UAP56 to promote cytoplasmic accumulation of unspliced RNA. Mol. Cell. Biol. 2006, 26, 1631-1643.
    • (2006) Mol. Cell. Biol , vol.26 , pp. 1631-1643
    • Lischka, P.1    Toth, Z.2    Thomas, M.3    Mueller, R.4    Stamminger, T.5
  • 120
    • 84860008720 scopus 로고    scopus 로고
    • Viral factors reveal a role for REF/Aly in nuclear RNA stability
    • Stubbs, S.H.; Hunter, O.V.; Hoover, A.; Conrad, N.K. Viral factors reveal a role for REF/Aly in nuclear RNA stability. Mol. Cell. Biol. 2012, 32, 1260-1270.
    • (2012) Mol. Cell. Biol , vol.32 , pp. 1260-1270
    • Stubbs, S.H.1    Hunter, O.V.2    Hoover, A.3    Conrad, N.K.4
  • 121
    • 80052955255 scopus 로고    scopus 로고
    • Delineation of a core RNA element required for Kaposi's sarcoma-associated herpesvirus ORF57 binding and activity
    • Sei, E.; Conrad, N.K. Delineation of a core RNA element required for Kaposi's sarcoma-associated herpesvirus ORF57 binding and activity. Virology 2011, 419, 107-116.
    • (2011) Virology , vol.419 , pp. 107-116
    • Sei, E.1    Conrad, N.K.2
  • 122
    • 80054796475 scopus 로고    scopus 로고
    • Stability of a long noncoding viral RNA depends on a 9-nt core element at the RNA 5' end to interact with viral ORF57 and cellular PABPC1
    • Massimelli, M.J.; Kang, J.-G.; Majerciak, V.; Le, S.-Y.; Liewehr, D.; Steinberg, S.; Zheng, Z.M. Stability of a long noncoding viral RNA depends on a 9-nt core element at the RNA 5' end to interact with viral ORF57 and cellular PABPC1. Int. J. Biol. Sci. 2011, 7, 1145-1160.
    • (2011) Int. J. Biol. Sci , vol.7 , pp. 1145-1160
    • Massimelli, M.J.1    Kang, J.-G.2    Majerciak, V.3    Le, S.-Y.4    Liewehr, D.5    Steinberg, S.6    Zheng, Z.M.7
  • 123
    • 79952386909 scopus 로고    scopus 로고
    • Kaposi sarcoma-associated herpesvirus ORF57 promotes escape of viral and human interleukin-6 from microRNA-mediated suppression
    • Kang, J.G.; Pripuzova, N.; Majerciak, V.; Kruhlak, M.; Le, S.Y.; Zheng, Z.M. Kaposi sarcoma-associated herpesvirus ORF57 promotes escape of viral and human interleukin-6 from microRNA-mediated suppression. J. Virol. 2011, 85, 2620-2630.
    • (2011) J. Virol , vol.85 , pp. 2620-2630
    • Kang, J.G.1    Pripuzova, N.2    Majerciak, V.3    Kruhlak, M.4    Le, S.Y.5    Zheng, Z.M.6
  • 124
    • 84871992043 scopus 로고    scopus 로고
    • Interplay between polyadenylate-binding protein 1 and Kaposi's sarcoma-associated herpesvirus ORF57 in accumulation of polyadenylated nuclear RNA, a viral long noncoding RNA
    • Massimelli, M.J.; Majerciak, V.; Kruhlak, M.; Zheng, Z.-M. Interplay between polyadenylate-binding protein 1 and Kaposi's sarcoma-associated herpesvirus ORF57 in accumulation of polyadenylated nuclear RNA, a viral long noncoding RNA. J. Virol. 2013, 87, 243-256.
    • (2013) J. Virol , vol.87 , pp. 243-256
    • Massimelli, M.J.1    Majerciak, V.2    Kruhlak, M.3    Zheng, Z.-M.4
  • 125
    • 0034076058 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus open reading frame 57 encodes a posttranscriptional regulator with multiple distinct activities
    • Kirshner, J.R.; Lukac, D.M.; Chang, J.; Ganem, D. Kaposi's sarcoma-associated herpesvirus open reading frame 57 encodes a posttranscriptional regulator with multiple distinct activities. J. Virol. 2000, 74, 3586-3597.
    • (2000) J. Virol , vol.74 , pp. 3586-3597
    • Kirshner, J.R.1    Lukac, D.M.2    Chang, J.3    Ganem, D.4
  • 126
    • 67449101832 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus RTA promotes degradation of the Hey1 repressor protein through the ubiquitin proteasome pathway
    • Gould, F.; Harrison, S.M.; Hewitt, E.W.; Whitehouse, A. Kaposi's sarcoma-associated herpesvirus RTA promotes degradation of the Hey1 repressor protein through the ubiquitin proteasome pathway. J. Virol. 2009, 83, 6727-6738.
    • (2009) J. Virol , vol.83 , pp. 6727-6738
    • Gould, F.1    Harrison, S.M.2    Hewitt, E.W.3    Whitehouse, A.4
  • 127
    • 33645744610 scopus 로고    scopus 로고
    • KSHV infection and the pathogenesis of Kaposi's sarcoma
    • Ganem, D. KSHV infection and the pathogenesis of Kaposi's sarcoma. Annu. Rev. Pathol. 2006, 1, 273-296.
    • (2006) Annu. Rev. Pathol , vol.1 , pp. 273-296
    • Ganem, D.1
  • 128
    • 0038653408 scopus 로고    scopus 로고
    • Molecular genetics of Kaposi's sarcoma-associated herpesvirus (human herpesvirus-8) epidemiology and pathogenesis
    • Dourmishev, L.A.; Dourmishev, A.L.; Palmeri, D.; Schwartz, R.A.; Lukac, D.M. Molecular genetics of Kaposi's sarcoma-associated herpesvirus (human herpesvirus-8) epidemiology and pathogenesis. Microbiol. Mol. Biol. Rev. 2003, 67, 175-212.
    • (2003) Microbiol. Mol. Biol. Rev , vol.67 , pp. 175-212
    • Dourmishev, L.A.1    Dourmishev, A.L.2    Palmeri, D.3    Schwartz, R.A.4    Lukac, D.M.5
  • 129
    • 37049020932 scopus 로고    scopus 로고
    • Promoter- and cell-specific transcriptional transactivation by the Kaposi's sarcoma-associated herpesvirus ORF57/Mta protein
    • Palmeri, D.; Spadavecchia, S.; Carroll, K.D.; Lukac, D.M. Promoter- and cell-specific transcriptional transactivation by the Kaposi's sarcoma-associated herpesvirus ORF57/Mta protein. J. Virol. 2007, 81, 13299-13314.
    • (2007) J. Virol , vol.81 , pp. 13299-13314
    • Palmeri, D.1    Spadavecchia, S.2    Carroll, K.D.3    Lukac, D.M.4
  • 130
    • 84875545697 scopus 로고    scopus 로고
    • Chromatin immunoprecipitation and microarray analysis suggest functional cooperation between kaposi's sarcoma-associated herpesvirus ORF57 and K-bZIP
    • Hunter, O.V.; Sei, E.; Richardson, R.B.; Conrad, N.K. Chromatin immunoprecipitation and microarray analysis suggest functional cooperation between kaposi's sarcoma-associated herpesvirus ORF57 and K-bZIP. J. Virol. 2013, 87, 4005-4016.
    • (2013) J. Virol , vol.87 , pp. 4005-4016
    • Hunter, O.V.1    Sei, E.2    Richardson, R.B.3    Conrad, N.K.4
  • 131
    • 77956854995 scopus 로고    scopus 로고
    • ORF57: Master regulator of KSHV mRNA biogenesis
    • Boyne, J.R.; Jackson, B.R.; Whitehouse, A. ORF57: Master regulator of KSHV mRNA biogenesis. Cell Cycle 2010, 9, 2702-2703.
    • (2010) Cell Cycle , vol.9 , pp. 2702-2703
    • Boyne, J.R.1    Jackson, B.R.2    Whitehouse, A.3
  • 132
    • 47049128026 scopus 로고    scopus 로고
    • Epstein-Barr virus SM protein functions as an alternative splicing factor
    • Verma, D.; Swaminathan, S. Epstein-Barr virus SM protein functions as an alternative splicing factor. J. Virol. 2008, 82, 7180-7188.
    • (2008) J. Virol , vol.82 , pp. 7180-7188
    • Verma, D.1    Swaminathan, S.2
  • 133
    • 33646735179 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus lytic gene ORF57 is essential for infectious virion production
    • Han, Z.; Swaminathan, S. Kaposi's sarcoma-associated herpesvirus lytic gene ORF57 is essential for infectious virion production. J. Virol. 2006, 80, 5251-5260.
    • (2006) J. Virol , vol.80 , pp. 5251-5260
    • Han, Z.1    Swaminathan, S.2


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