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Volumn 86, Issue 9, 2012, Pages 4892-4905

The bovine immunodeficiency virus rev protein: Identification of a novel nuclear import pathway and nuclear export signal among retroviral Rev/Rev-like proteins

Author keywords

[No Author keywords available]

Indexed keywords

EXPORTIN 1; KARYOPHERIN ALPHA; KARYOPHERIN ALPHA3; KARYOPHERIN ALPHA5; KARYOPHERIN BETA; LEPTOMYCIN B; NUCLEAR PROTEIN; REV PROTEIN; UNCLASSIFIED DRUG;

EID: 84861324422     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.05132-11     Document Type: Article
Times cited : (11)

References (73)
  • 1
    • 0025083331 scopus 로고
    • Nuclear protein import in permeabilized mammalian cells requires soluble cytoplasmic factors
    • Adam SA, Marr RS, Gerace L. 1990. Nuclear protein import in permeabilized mammalian cells requires soluble cytoplasmic factors. J. Cell Biol. 111:807-816.
    • (1990) J. Cell Biol. , vol.111 , pp. 807-816
    • Adam, S.A.1    Marr, R.S.2    Gerace, L.3
  • 2
    • 11944274520 scopus 로고    scopus 로고
    • Nucleolar proteome dynamics
    • Andersen JS, et al. 2005. Nucleolar proteome dynamics. Nature 433: 77-83.
    • (2005) Nature , vol.433 , pp. 77-83
    • Andersen, J.S.1
  • 3
    • 33746374437 scopus 로고    scopus 로고
    • Multiple importins function as nuclear transport receptors for the Rev protein of human immunodeficiency virus type 1
    • Arnold M, Nath A, Hauber J, Kehlenbach RH. 2006. Multiple importins function as nuclear transport receptors for the Rev protein of human immunodeficiency virus type 1. J. Biol. Chem. 281:20883-20890.
    • (2006) J. Biol. Chem. , vol.281 , pp. 20883-20890
    • Arnold, M.1    Nath, A.2    Hauber, J.3    Kehlenbach, R.H.4
  • 4
    • 33947355408 scopus 로고    scopus 로고
    • Nuclear import of bovine papillomavirus type 1 E1 protein is mediated by multiple alpha importins and is negatively regulated by phosphorylation near a nuclear localization signal
    • Bian XL, Rosas-Acosta G, Wu YC, Wilson VG. 2007. Nuclear import of bovine papillomavirus type 1 E1 protein is mediated by multiple alpha importins and is negatively regulated by phosphorylation near a nuclear localization signal. J. Virol. 81:2899-2908.
    • (2007) J. Virol. , vol.81 , pp. 2899-2908
    • Bian, X.L.1    Rosas-Acosta, G.2    Wu, Y.C.3    Wilson, V.G.4
  • 5
    • 0031710231 scopus 로고    scopus 로고
    • Inhibition of human immunodeficiency virus Rev and human T-cell leukemia virus Rex function, but not Mason-Pfizer monkey virus constitutive transport element activity, by a mutant human nucleoporin targeted to Crm1
    • Bogerd HP, Echarri A, Ross TM, Cullen BR. 1998. Inhibition of human immunodeficiency virus Rev and human T-cell leukemia virus Rex function, but not Mason-Pfizer monkey virus constitutive transport element activity, by a mutant human nucleoporin targeted to Crm1. J. Virol. 72: 8627-8635.
    • (1998) J. Virol. , vol.72 , pp. 8627-8635
    • Bogerd, H.P.1    Echarri, A.2    Ross, T.M.3    Cullen, B.R.4
  • 6
    • 79953224896 scopus 로고    scopus 로고
    • Interaction of the influenza A virus polymerase PB2 C-terminal region with importin {alpha} isoforms provides insights into host adaptation and polymerase assembly
    • Boivin S, Hart DJ. 2011. Interaction of the influenza A virus polymerase PB2 C-terminal region with importin {alpha} isoforms provides insights into host adaptation and polymerase assembly. J. Biol. Chem. 286:10439-10448.
    • (2011) J. Biol. Chem. , vol.286 , pp. 10439-10448
    • Boivin, S.1    Hart, D.J.2
  • 7
    • 0028287515 scopus 로고
    • Putative nuclear localization signals (NLS) in protein transcription factors
    • Boulikas T. 1994. Putative nuclear localization signals (NLS) in protein transcription factors. J. Cell. Biochem. 55:32-58.
    • (1994) J. Cell. Biochem. , vol.55 , pp. 32-58
    • Boulikas, T.1
  • 8
    • 60349118158 scopus 로고    scopus 로고
    • Reconstitution of nuclear import in permeabilized cells
    • Cassany A, Gerace L. 2009. Reconstitution of nuclear import in permeabilized cells. Methods Mol. Biol. 464:181-205.
    • (2009) Methods Mol. Biol. , vol.464 , pp. 181-205
    • Cassany, A.1    Gerace, L.2
  • 9
    • 79960912049 scopus 로고    scopus 로고
    • Nuclear import by karyopherin-betas: recognition and inhibition
    • Chook YM, Suel KE. 2011. Nuclear import by karyopherin-betas: recognition and inhibition. Biochim. Biophys. Acta 1813:1593-1606.
    • (2011) Biochim. Biophys. Acta , vol.1813 , pp. 1593-1606
    • Chook, Y.M.1    Suel, K.E.2
  • 10
    • 0025141758 scopus 로고
    • Identification of sequences important in the nucleolar localization of human immunodeficiency virus Rev: relevance of nucleolar localization to function
    • Cochrane AW, Perkins A, Rosen CA. 1990. Identification of sequences important in the nucleolar localization of human immunodeficiency virus Rev: relevance of nucleolar localization to function. J. Virol. 64:881-885.
    • (1990) J. Virol. , vol.64 , pp. 881-885
    • Cochrane, A.W.1    Perkins, A.2    Rosen, C.A.3
  • 11
    • 34548627531 scopus 로고    scopus 로고
    • Structural biology of nucleocytoplasmic transport
    • Cook A, Bono F, Jinek M, Conti E. 2007. Structural biology of nucleocytoplasmic transport. Annu. Rev. Biochem. 76:647-671.
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 647-671
    • Cook, A.1    Bono, F.2    Jinek, M.3    Conti, E.4
  • 12
    • 77949758196 scopus 로고    scopus 로고
    • Molecular and biological aspects of the bovine immunodeficiency virus
    • Corredor AG, St-Louis MC, Archambault D. 2010. Molecular and biological aspects of the bovine immunodeficiency virus. Curr. HIV Res. 8:2-13.
    • (2010) Curr. HIV Res. , vol.8 , pp. 2-13
    • Corredor, A.G.1    St-Louis, M.C.2    Archambault, D.3
  • 13
    • 9644279587 scopus 로고    scopus 로고
    • In vivo HIV-1 Rev multimerization in the nucleolus and cytoplasm identified by fluorescence resonance energy transfer
    • Daelemans D, et al. 2004. In vivo HIV-1 Rev multimerization in the nucleolus and cytoplasm identified by fluorescence resonance energy transfer. J. Biol. Chem. 279:50167-50175.
    • (2004) J. Biol. Chem. , vol.279 , pp. 50167-50175
    • Daelemans, D.1
  • 14
    • 77953339407 scopus 로고    scopus 로고
    • The nucleocytoplasmic transport of viral proteins
    • Ding Q, Zhao L, Guo H, Zheng AC. 2010. The nucleocytoplasmic transport of viral proteins. Virol. Sin. 25:79-85.
    • (2010) Virol. Sin. , vol.25 , pp. 79-85
    • Ding, Q.1    Zhao, L.2    Guo, H.3    Zheng, A.C.4
  • 16
    • 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 WC, Mattaj IW, Luhrmann R. 1995. The HIV-1 Rev activation domain is a nuclear export signal that accesses an export pathway used by specific cellular RNAs. Cell 82:475-483.
    • (1995) Cell , vol.82 , pp. 475-483
    • Fischer, U.1    Huber, J.2    Boelens, W.C.3    Mattaj, I.W.4    Luhrmann, R.5
  • 17
    • 0030924190 scopus 로고    scopus 로고
    • CRM1 is an export receptor for leucine-rich nuclear export signals
    • Fornerod M, Ohno M, Yoshida M, Mattaj IW. 1997. CRM1 is an export receptor for leucine-rich nuclear export signals. Cell 90:1051-1060.
    • (1997) Cell , vol.90 , pp. 1051-1060
    • Fornerod, M.1    Ohno, M.2    Yoshida, M.3    Mattaj, I.W.4
  • 18
    • 0042830859 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport: taking an inventory
    • Fried H, Kutay U. 2003. Nucleocytoplasmic transport: taking an inventory. Cell. Mol. Life Sci. 60:1659-1688.
    • (2003) Cell. Mol. Life Sci. , vol.60 , pp. 1659-1688
    • Fried, H.1    Kutay, U.2
  • 19
    • 78751622104 scopus 로고    scopus 로고
    • Differential use of importin-alpha isoforms governs cell tropism and host adaptation of influenza virus
    • Gabriel G, et al. 2011. Differential use of importin-alpha isoforms governs cell tropism and host adaptation of influenza virus. Nat. Commun. 2:156.
    • (2011) Nat. Commun. , vol.2 , pp. 156
    • Gabriel, G.1
  • 20
    • 0026096530 scopus 로고
    • Yeast cell-free nuclear protein import requires ATP hydrolysis
    • Garcia-Bustos JF, Wagner P, Hall MN. 1991. Yeast cell-free nuclear protein import requires ATP hydrolysis. Exp. Cell Res. 192:213-219.
    • (1991) Exp. Cell Res. , vol.192 , pp. 213-219
    • Garcia-Bustos, J.F.1    Wagner, P.2    Hall, M.N.3
  • 21
    • 72849111075 scopus 로고    scopus 로고
    • The bovine immunodeficiency virus Rev protein: identification of a novel lentiviral bipartite nuclear localization signal harboring an atypical spacer sequence
    • Gomez Corredor A, Archambault D. 2009. The bovine immunodeficiency virus Rev protein: identification of a novel lentiviral bipartite nuclear localization signal harboring an atypical spacer sequence. J. Virol. 83:12842-12853.
    • (2009) J. Virol. , vol.83 , pp. 12842-12853
    • Gomez Corredor, A.1    Archambault, D.2
  • 22
    • 0023552557 scopus 로고
    • Characterization and molecular cloning of a bovine lentivirus related to human immunodeficiency virus
    • Gonda MA, et al. 1987. Characterization and molecular cloning of a bovine lentivirus related to human immunodeficiency virus. Nature 330: 388-391.
    • (1987) Nature , vol.330 , pp. 388-391
    • Gonda, M.A.1
  • 23
    • 0028220572 scopus 로고
    • Bovine immunodeficiency virus: molecular biology and virus-host interactions
    • Gonda MA, Luther DG, Fong SE, Tobin GJ. 1994. Bovine immunodeficiency virus: molecular biology and virus-host interactions. Virus Res. 32:155-181.
    • (1994) Virus Res , vol.32 , pp. 155-181
    • Gonda, M.A.1    Luther, D.G.2    Fong, S.E.3    Tobin, G.J.4
  • 24
    • 1842300384 scopus 로고    scopus 로고
    • A novel class of RanGTP binding proteins
    • Gorlich D, et al. 1997. A novel class of RanGTP binding proteins. J. Cell Biol. 138:65-80.
    • (1997) J. Cell Biol. , vol.138 , pp. 65-80
    • Gorlich, D.1
  • 25
    • 0029853631 scopus 로고    scopus 로고
    • Identification of different roles for RanGDP and RanGTP in nuclear protein import
    • Gorlich D, Pante N, Kutay U, Aebi U, Bischoff FR. 1996. Identification of different roles for RanGDP and RanGTP in nuclear protein import. EMBO J. 15:5584-5594.
    • (1996) EMBO J , vol.15 , pp. 5584-5594
    • Gorlich, D.1    Pante, N.2    Kutay, U.3    Aebi, U.4    Bischoff, F.R.5
  • 26
    • 79952494073 scopus 로고    scopus 로고
    • Intermolecular masking of the HIV-1 Rev NLS by the cellular protein HIC: novel insights into the regulation of Rev nuclear import
    • Gu L, et al. 2011. Intermolecular masking of the HIV-1 Rev NLS by the cellular protein HIC: novel insights into the regulation of Rev nuclear import. Retrovirology 8:17.
    • (2011) Retrovirology , vol.8 , pp. 17
    • Gu, L.1
  • 27
    • 78549264393 scopus 로고    scopus 로고
    • NES consensus redefined by structures of PKI-type and Rev-type nuclear export signals bound to CRM1
    • Guttler T, et al. 2010. NES consensus redefined by structures of PKI-type and Rev-type nuclear export signals bound to CRM1. Nat. Struct. Mol. Biol. 17:1367-1376.
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 1367-1376
    • Guttler, T.1
  • 28
    • 0031860889 scopus 로고    scopus 로고
    • Differential requirements for alternative splicing and nuclear export functions of equine infectious anemia virus Rev protein
    • Harris ME, Gontarek RR, Derse D, Hope TJ. 1998. Differential requirements for alternative splicing and nuclear export functions of equine infectious anemia virus Rev protein. Mol. Cell. Biol. 18:3889-3899.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 3889-3899
    • Harris, M.E.1    Gontarek, R.R.2    Derse, D.3    Hope, T.J.4
  • 29
    • 0034630158 scopus 로고    scopus 로고
    • A comparison of the activity, sequence specificity, and CRM1-dependence of different nuclear export signals
    • Henderson BR, Eleftheriou A. 2000. A comparison of the activity, sequence specificity, and CRM1-dependence of different nuclear export signals. Exp. Cell Res. 256:213-224.
    • (2000) Exp. Cell Res. , vol.256 , pp. 213-224
    • Henderson, B.R.1    Eleftheriou, A.2
  • 30
    • 0031578895 scopus 로고    scopus 로고
    • Interactions between HIV Rev and nuclear import and export factors: the Rev nuclear localisation signal mediates specific binding to human importin-beta
    • Henderson BR, Percipalle P. 1997. Interactions between HIV Rev and nuclear import and export factors: the Rev nuclear localisation signal mediates specific binding to human importin-beta. J. Mol. Biol. 274:693-707.
    • (1997) J. Mol. Biol. , vol.274 , pp. 693-707
    • Henderson, B.R.1    Percipalle, P.2
  • 31
    • 66849125858 scopus 로고    scopus 로고
    • The nuclear pore component Nup358 promotes transportin-dependent nuclear import
    • Hutten S, Walde S, Spillner C, Hauber J, Kehlenbach RH. 2009. The nuclear pore component Nup358 promotes transportin-dependent nuclear import. J. Cell Sci. 122:1100-1110.
    • (2009) J. Cell Sci. , vol.122 , pp. 1100-1110
    • Hutten, S.1    Walde, S.2    Spillner, C.3    Hauber, J.4    Kehlenbach, R.H.5
  • 32
    • 19444377055 scopus 로고    scopus 로고
    • A novel, mouse mammary tumor virus encoded protein with Rev-like properties
    • Indik S, Gunzburg WH, Salmons B, Rouault F. 2005. A novel, mouse mammary tumor virus encoded protein with Rev-like properties. Virology 337:1-6.
    • (2005) Virology , vol.337 , pp. 1-6
    • Indik, S.1    Gunzburg, W.H.2    Salmons, B.3    Rouault, F.4
  • 33
    • 40849142339 scopus 로고    scopus 로고
    • A functional nuclear localization signal in insulin-like growth factor binding protein-6 mediates its nuclear import
    • Iosef C, Gkourasas T, Jia CY, Li SS, Han VK. 2008. A functional nuclear localization signal in insulin-like growth factor binding protein-6 mediates its nuclear import. Endocrinology 149:1214-1226.
    • (2008) Endocrinology , vol.149 , pp. 1214-1226
    • Iosef, C.1    Gkourasas, T.2    Jia, C.Y.3    Li, S.S.4    Han, V.K.5
  • 34
    • 84884872358 scopus 로고    scopus 로고
    • Analysis of nuclear protein import and export in digitonin-permeabilized cells
    • Celis J (ed), 3rd ed, Elsevier Academic Press, Burlington MA
    • Kehlenbach RH, Paschal BM. 2006. Analysis of nuclear protein import and export in digitonin-permeabilized cells, p 267-275. In Celis J (ed), Cell biology: a laboratory handbook, 3rd ed, vol 2. Elsevier Academic Press, Burlington, MA.
    • (2006) Cell biology: a laboratory handbook , vol.2 , pp. 267-275
    • Kehlenbach, R.H.1    Paschal, B.M.2
  • 35
    • 55049137634 scopus 로고    scopus 로고
    • Caspase-mediated cleavage of importin-alpha increases its affinity for MCM and downregulates DNA synthesis by interrupting the binding ofMCMto chromatin
    • Kim BJ, Lee H. 2008. Caspase-mediated cleavage of importin-alpha increases its affinity for MCM and downregulates DNA synthesis by interrupting the binding ofMCMto chromatin. Biochim. Biophys. Acta 1783: 2287-2293.
    • (2008) Biochim. Biophys. Acta , vol.1783 , pp. 2287-2293
    • Kim, B.J.1    Lee, H.2
  • 36
    • 0141459590 scopus 로고    scopus 로고
    • Functional analysis of the interaction of the human immunodeficiency virus type 1 Rev nuclear export signal with its cofactors
    • Kiss A, Li L, Gettemeier T, Venkatesh LK. 2003. Functional analysis of the interaction of the human immunodeficiency virus type 1 Rev nuclear export signal with its cofactors. Virology 314:591-600.
    • (2003) Virology , vol.314 , pp. 591-600
    • Kiss, A.1    Li, L.2    Gettemeier, T.3    Venkatesh, L.K.4
  • 37
    • 0028964821 scopus 로고
    • Interaction of the nuclear GTP-binding protein Ran with its regulatory proteins RCC1 and RanGAP1
    • Klebe C, Bischoff FR, Ponstingl H, Wittinghofer A. 1995. Interaction of the nuclear GTP-binding protein Ran with its regulatory proteins RCC1 and RanGAP1. Biochemistry 34:639-647.
    • (1995) Biochemistry , vol.34 , pp. 639-647
    • Klebe, C.1    Bischoff, F.R.2    Ponstingl, H.3    Wittinghofer, A.4
  • 38
    • 16344379538 scopus 로고    scopus 로고
    • Importin alpha transports CaMKIV to the nucleus without utilizing importin beta
    • Kotera I, et al. 2005. Importin alpha transports CaMKIV to the nucleus without utilizing importin beta. EMBO J. 24:942-951.
    • (2005) EMBO J , vol.24 , pp. 942-951
    • Kotera, I.1
  • 39
    • 0024325692 scopus 로고
    • Functional similarity of HIV-I rev and HTLV-I rex proteins: identification of a new nucleolar-targeting signal in rev protein
    • Kubota S, et al. 1989. Functional similarity of HIV-I rev and HTLV-I rex proteins: identification of a new nucleolar-targeting signal in rev protein. Biochem. Biophys. Res. Commun. 162:963-970.
    • (1989) Biochem. Biophys. Res. Commun. , vol.162 , pp. 963-970
    • Kubota, S.1
  • 40
    • 0033529866 scopus 로고    scopus 로고
    • Leptomycin B inactivates CRM1/exportin 1 by covalent modification at a cysteine residue in the central conserved region
    • Kudo N, et al. 1999. Leptomycin B inactivates CRM1/exportin 1 by covalent modification at a cysteine residue in the central conserved region. Proc. Natl. Acad. Sci. U. S. A. 96:9112-9117.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 9112-9117
    • Kudo, N.1
  • 41
    • 14744301997 scopus 로고    scopus 로고
    • Leucine-rich nuclear-export signals: born to be weak
    • Kutay U, Guttinger S. 2005. Leucine-rich nuclear-export signals: born to be weak. Trends Cell Biol. 15:121-124.
    • (2005) Trends Cell Biol , vol.15 , pp. 121-124
    • Kutay, U.1    Guttinger, S.2
  • 42
    • 8444247065 scopus 로고    scopus 로고
    • Analysis and prediction of leucine-rich nuclear export signals
    • la Cour T, et al. 2004. Analysis and prediction of leucine-rich nuclear export signals. Protein Eng. Des. Sel. 17:527-536.
    • (2004) Protein Eng. Des. Sel. , vol.17 , pp. 527-536
    • la Cour, T.1
  • 43
    • 33645777243 scopus 로고    scopus 로고
    • Characterization of functional domains of equine infectious anemia virus Rev suggests a bipartite RNA-binding domain
    • Lee JH, et al. 2006. Characterization of functional domains of equine infectious anemia virus Rev suggests a bipartite RNA-binding domain. J. Virol. 80:3844-3852.
    • (2006) J. Virol. , vol.80 , pp. 3844-3852
    • Lee, J.H.1
  • 44
    • 77951575026 scopus 로고    scopus 로고
    • The importin beta binding domain modulates the avidity of importin beta for the nuclear pore complex
    • Lott K, Bhardwaj A, Mitrousis G, Pante N, Cingolani G. 2010. The importin beta binding domain modulates the avidity of importin beta for the nuclear pore complex. J. Biol. Chem. 285:13769-13780.
    • (2010) J. Biol. Chem. , vol.285 , pp. 13769-13780
    • Lott, K.1    Bhardwaj, A.2    Mitrousis, G.3    Pante, N.4    Cingolani, G.5
  • 45
    • 0345411605 scopus 로고    scopus 로고
    • cORF and RcRE, the Rev/Rex and RRE/RxRE homologues of the human endogenous retrovirus family HTDV/HERV-K
    • Magin C, Lower R, Lower J. 1999. cORF and RcRE, the Rev/Rex and RRE/RxRE homologues of the human endogenous retrovirus family HTDV/HERV-K. J. Virol. 73:9496-9507.
    • (1999) J. Virol. , vol.73 , pp. 9496-9507
    • Magin, C.1    Lower, R.2    Lower, J.3
  • 46
    • 0036846540 scopus 로고    scopus 로고
    • Importin alpha can migrate into the nucleus in an importin beta- and Ran-independent manner
    • Miyamoto Y, et al. 2002. Importin alpha can migrate into the nucleus in an importin beta- and Ran-independent manner.EMBOJ. 21:5833-5842.
    • (2002) EMBOJ , vol.21 , pp. 5833-5842
    • Miyamoto, Y.1
  • 47
    • 67651207674 scopus 로고    scopus 로고
    • The lactate dehydrogenase-elevating virus capsid protein is a nuclear-cytoplasmic protein
    • Mohammadi H, Sharif S, Rowland RR, Yoo D. 2009. The lactate dehydrogenase-elevating virus capsid protein is a nuclear-cytoplasmic protein. Arch. Virol. 154:1071-1080.
    • (2009) Arch. Virol. , vol.154 , pp. 1071-1080
    • Mohammadi, H.1    Sharif, S.2    Rowland, R.R.3    Yoo, D.4
  • 48
    • 69849093363 scopus 로고    scopus 로고
    • Characterisation of the passive permeability barrier of nuclear pore complexes
    • Mohr D, Frey S, Fischer T, Guttler T, Gorlich D. 2009. Characterisation of the passive permeability barrier of nuclear pore complexes. EMBO J. 28:2541-2553.
    • (2009) EMBO J , vol.28 , pp. 2541-2553
    • Mohr, D.1    Frey, S.2    Fischer, T.3    Guttler, T.4    Gorlich, D.5
  • 49
    • 0026723508 scopus 로고
    • The two steps of nuclear import, targeting to the nuclear envelope and translocation through the nuclear pore, require different cytosolic factors
    • Moore MS, Blobel G. 1992. The two steps of nuclear import, targeting to the nuclear envelope and translocation through the nuclear pore, require different cytosolic factors. Cell 69:939-950.
    • (1992) Cell , vol.69 , pp. 939-950
    • Moore, M.S.1    Blobel, G.2
  • 50
    • 77649174985 scopus 로고    scopus 로고
    • Anti-retroviral activity of TRIM5 alpha
    • Nakayama EE, Shioda T. 2010. Anti-retroviral activity of TRIM5 alpha. Rev. Med. Virol. 20:77-92.
    • (2010) Rev. Med. Virol. , vol.20 , pp. 77-92
    • Nakayama, E.E.1    Shioda, T.2
  • 51
    • 0242492517 scopus 로고    scopus 로고
    • Functional domain structure of human T-cell leukemia virus type 2 Rex
    • Narayan M, Younis I, D'Agostino DM, Green PL. 2003. Functional domain structure of human T-cell leukemia virus type 2 Rex. J. Virol. 77:12829-12840.
    • (2003) J. Virol. , vol.77 , pp. 12829-12840
    • Narayan, M.1    Younis, I.2    D'Agostino, D.M.3    Green, P.L.4
  • 52
    • 34248403282 scopus 로고    scopus 로고
    • Novel nuclear import of Vpr promoted by importin alpha is crucial for human immunodeficiency virus type 1 replication in macrophages
    • Nitahara-Kasahara Y, et al. 2007. Novel nuclear import of Vpr promoted by importin alpha is crucial for human immunodeficiency virus type 1 replication in macrophages. J. Virol. 81:5284-5293.
    • (2007) J. Virol. , vol.81 , pp. 5284-5293
    • Nitahara-Kasahara, Y.1
  • 53
    • 0024829510 scopus 로고
    • Nucleolar targeting signal of human T-cell leukemia virus type I rex-encoded protein is essential for cytoplasmic accumulation of unspliced viral mRNA
    • Nosaka T, et al. 1989. Nucleolar targeting signal of human T-cell leukemia virus type I rex-encoded protein is essential for cytoplasmic accumulation of unspliced viral mRNA. Proc. Natl. Acad. Sci. U. S. A. 86:9798-9802.
    • (1989) Proc. Natl. Acad. Sci. U. S. A. , vol.86 , pp. 9798-9802
    • Nosaka, T.1
  • 54
    • 0034623005 scopus 로고    scopus 로고
    • T- Coffee: a novel method for fast and accurate multiple sequence alignment
    • Notredame C, Higgins DG, Heringa J. 2000. T-Coffee: a novel method for fast and accurate multiple sequence alignment. J. Mol. Biol. 302:205-217.
    • (2000) J. Mol. Biol. , vol.302 , pp. 205-217
    • Notredame, C.1    Higgins, D.G.2    Heringa, J.3
  • 55
    • 0025850706 scopus 로고
    • Analysis of the transcription pattern and mapping of the putative Rev and Env splice junctions of bovine immunodeficiency-like virus
    • Oberste MS, Greenwood JD, Gonda MA. 1991. Analysis of the transcription pattern and mapping of the putative Rev and Env splice junctions of bovine immunodeficiency-like virus. J. Virol. 65:3932-3937.
    • (1991) J. Virol. , vol.65 , pp. 3932-3937
    • Oberste, M.S.1    Greenwood, J.D.2    Gonda, M.A.3
  • 56
    • 0030748907 scopus 로고    scopus 로고
    • Evidence for a role ofCRM1in signal-mediated nuclear protein export
    • Ossareh-Nazari B, Bachelerie F, Dargemont C. 1997. Evidence for a role ofCRM1in signal-mediated nuclear protein export. Science 278:141-144.
    • (1997) Science , vol.278 , pp. 141-144
    • Ossareh-Nazari, B.1    Bachelerie, F.2    Dargemont, C.3
  • 57
    • 0031818290 scopus 로고    scopus 로고
    • Leptomycin B inhibits equine infectious anemia virus Rev and feline immunodeficiency virus Rev function but not the function of the hepatitis B virus posttranscriptional regulatory element
    • Otero GC, Harris ME, Donello JE, Hope TJ. 1998. Leptomycin B inhibits equine infectious anemia virus Rev and feline immunodeficiency virus Rev function but not the function of the hepatitis B virus posttranscriptional regulatory element. J. Virol. 72:7593-7597.
    • (1998) J. Virol. , vol.72 , pp. 7593-7597
    • Otero, G.C.1    Harris, M.E.2    Donello, J.E.3    Hope, T.J.4
  • 58
    • 0032961356 scopus 로고    scopus 로고
    • Importin beta can mediate the nuclear import of an arginine-rich nuclear localization signal in the absence of importin alpha
    • Palmeri D, Malim MH. 1999. Importin beta can mediate the nuclear import of an arginine-rich nuclear localization signal in the absence of importin alpha. Mol. Cell. Biol. 19:1218-1225.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 1218-1225
    • Palmeri, D.1    Malim, M.H.2
  • 59
    • 66149126655 scopus 로고    scopus 로고
    • Active nuclear import and cytoplasmic retention of activation-induced deaminase
    • Patenaude AM, et al. 2009. Active nuclear import and cytoplasmic retention of activation-induced deaminase. Nat. Struct. Mol. Biol. 16:517-527.
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 517-527
    • Patenaude, A.M.1
  • 62
    • 0028834428 scopus 로고
    • Protein import into nuclei: association and dissociation reactions involving transport substrate, transport factors, and nucleoporins
    • Rexach M, Blobel G. 1995. Protein import into nuclei: association and dissociation reactions involving transport substrate, transport factors, and nucleoporins. Cell 83:683-692.
    • (1995) Cell , vol.83 , pp. 683-692
    • Rexach, M.1    Blobel, G.2
  • 63
    • 0030772652 scopus 로고    scopus 로고
    • Transportin-mediated nuclear import of heterogeneous nuclear RNP proteins
    • Siomi MC, et al. 1997. Transportin-mediated nuclear import of heterogeneous nuclear RNP proteins. J. Cell Biol. 138:1181-1192.
    • (1997) J. Cell Biol. , vol.138 , pp. 1181-1192
    • Siomi, M.C.1
  • 64
    • 0030985459 scopus 로고    scopus 로고
    • Exportin 1 (Crm1p) is an essential nuclear export factor
    • Stade K, Ford CS, Guthrie C, Weis K. 1997. Exportin 1 (Crm1p) is an essential nuclear export factor. Cell 90:1041-1050.
    • (1997) Cell , vol.90 , pp. 1041-1050
    • Stade, K.1    Ford, C.S.2    Guthrie, C.3    Weis, K.4
  • 65
    • 33847176295 scopus 로고    scopus 로고
    • Molecular mechanism of the nuclear protein import cycle
    • Stewart M. 2007. Molecular mechanism of the nuclear protein import cycle. Nat. Rev. Mol. Cell Biol. 8:195-208.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 195-208
    • Stewart, M.1
  • 66
    • 59649120307 scopus 로고    scopus 로고
    • Cellular proteins and HIV-1 Rev function
    • Suhasini M, Reddy TR. 2009. Cellular proteins and HIV-1 Rev function. Curr. HIV Res. 7:91-100.
    • (2009) Curr. HIV Res. , vol.7 , pp. 91-100
    • Suhasini, M.1    Reddy, T.R.2
  • 67
    • 0033178866 scopus 로고    scopus 로고
    • Getting across the nuclear pore complex
    • Talcott B, Moore MS. 1999. Getting across the nuclear pore complex. Trends Cell Biol. 9:312-318.
    • (1999) Trends Cell Biol , vol.9 , pp. 312-318
    • Talcott, B.1    Moore, M.S.2
  • 68
    • 0032911885 scopus 로고    scopus 로고
    • The arginine-rich domains present in human immunodeficiency virus type 1 Tat and Rev function as direct importin beta-dependent nuclear localization signals
    • Truant R, Cullen BR. 1999. The arginine-rich domains present in human immunodeficiency virus type 1 Tat and Rev function as direct importin beta-dependent nuclear localization signals. Mol. Cell. Biol. 19:1210-1217.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 1210-1217
    • Truant, R.1    Cullen, B.R.2
  • 69
    • 34250380367 scopus 로고    scopus 로고
    • The nuclear import of the human T lymphotropic virus type I (HTLV-1) tax protein is carrier- and energy-independent
    • Tsuji T, et al. 2007. The nuclear import of the human T lymphotropic virus type I (HTLV-1) tax protein is carrier- and energy-independent. J. Biol. Chem. 282:13875-13883.
    • (2007) J. Biol. Chem. , vol.282 , pp. 13875-13883
    • Tsuji, T.1
  • 70
    • 70349270622 scopus 로고    scopus 로고
    • Avian reovirus sigmaA localizes to the nucleolus and enters the nucleus by a nonclassical energy- and carrier-independent pathway
    • Vazquez-Iglesias L, Lostale-Seijo I, Martinez-Costas J, Benavente J. 2009. Avian reovirus sigmaA localizes to the nucleolus and enters the nucleus by a nonclassical energy- and carrier-independent pathway. J. Virol. 83:10163-10175.
    • (2009) J. Virol. , vol.83 , pp. 10163-10175
    • Vazquez-Iglesias, L.1    Lostale-Seijo, I.2    Martinez-Costas, J.3    Benavente, J.4
  • 71
    • 0029130168 scopus 로고
    • Identification of a signal for rapid export of proteins from the nucleus
    • Wen W, Meinkoth JL, Tsien RY, Taylor SS. 1995. Identification of a signal for rapid export of proteins from the nucleus. Cell 82:463-473.
    • (1995) Cell , vol.82 , pp. 463-473
    • Wen, W.1    Meinkoth, J.L.2    Tsien, R.Y.3    Taylor, S.S.4
  • 72
    • 0033539613 scopus 로고    scopus 로고
    • An ancient family of human endogenous retroviruses encodes a functional homolog of the HIV-1 Rev protein
    • Yang J, et al. 1999. An ancient family of human endogenous retroviruses encodes a functional homolog of the HIV-1 Rev protein. Proc. Natl. Acad. Sci. U. S. A. 96:13404-13408.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 13404-13408
    • Yang, J.1
  • 73
    • 0030913267 scopus 로고    scopus 로고
    • How proteins are transported from cytoplasm to the nucleus
    • Yoneda Y. 1997. How proteins are transported from cytoplasm to the nucleus. J. Biochem. 121:811-817.
    • (1997) J. Biochem. , vol.121 , pp. 811-817
    • Yoneda, Y.1


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