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Volumn 10, Issue 4, 2008, Pages 195-204

HTLV-1 Yin and Yang: Rex and p30 master regulators of viral mRNA trafficking

Author keywords

HTLV 1; p30; Posttranscriptional regulation; Rex; RNA export

Indexed keywords

MESSENGER RNA; PROTEIN P30; REX PROTEIN; TAX PROTEIN; VIRUS RNA;

EID: 59549094794     PISSN: 11396121     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (37)

References (103)
  • 1
    • 0017708061 scopus 로고
    • Adult T-cell leukemia: Clinical and hematologic features of 16 cases
    • Uchiyama T, Yodoi J, Sagawa K, Takatsuki K, Uchino H. Adult T-cell leukemia: clinical and hematologic features of 16 cases. Blood. 1977;50:481-92.
    • (1977) Blood , vol.50 , pp. 481-492
    • Uchiyama, T.1    Yodoi, J.2    Sagawa, K.3    Takatsuki, K.4    Uchino, H.5
  • 2
    • 0019254359 scopus 로고
    • Detection and isolation of type C retrovirus particles from fresh and cultured lymphocytes cytes of a patient with cutaneous T-cell lymphoma
    • Poiesz B, Ruscetti F, Gazdar A, Bunn P, Minna J, Gallo R. Detection and isolation of type C retrovirus particles from fresh and cultured lymphocytes cytes of a patient with cutaneous T-cell lymphoma. Proc Natl Acad Sci USA. 1980;77:7415-19.
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 7415-7419
    • Poiesz, B.1    Ruscetti, F.2    Gazdar, A.3    Bunn, P.4    Minna, J.5    Gallo, R.6
  • 3
    • 0019274717 scopus 로고
    • T-cell lines established from human T-lymphocytic neoplasias by direct response to T-cell growth factor
    • Poiesz B, Ruscetti F, Mier J, Woods A, Gallo R. T-cell lines established from human T-lymphocytic neoplasias by direct response to T-cell growth factor. Proc Natl Acad Sci USA. 1980;77:6815-19.
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 6815-6819
    • Poiesz, B.1    Ruscetti, F.2    Mier, J.3    Woods, A.4    Gallo, R.5
  • 4
    • 0000904435 scopus 로고
    • Isolation and characterization of retrovirus from cell lines of human adult T-cell leukemia and its implication in the disease
    • Yoshida M, Miyoshi I, Hinuma Y. Isolation and characterization of retrovirus from cell lines of human adult T-cell leukemia and its implication in the disease. Proc Natl Acad Sci USA. 1982;79:2031-5.
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 2031-2035
    • Yoshida, M.1    Miyoshi, I.2    Hinuma, Y.3
  • 5
    • 13544259114 scopus 로고    scopus 로고
    • New therapeutic approaches for adult T-cell leukemia
    • Bazarbachi A, Ghez D, Lepelletier Y, et al. New therapeutic approaches for adult T-cell leukemia. Lancet Oncol. 2004;5:664-72.
    • (2004) Lancet Oncol , vol.5 , pp. 664-672
    • Bazarbachi, A.1    Ghez, D.2    Lepelletier, Y.3
  • 6
    • 0021995980 scopus 로고
    • Antibodies to HTLV-1 in patients with tropical spastic paraparesis
    • Gessain A, Barin F, Vernant J, et al. Antibodies to HTLV-1 in patients with tropical spastic paraparesis. Lancet. 1985;2:407-10.
    • (1985) Lancet , vol.2 , pp. 407-410
    • Gessain, A.1    Barin, F.2    Vernant, J.3
  • 7
    • 0022578349 scopus 로고
    • HTLV-1 associated myelopathy, a new clinical entity
    • Osame M, Usuku K, Izumo S, et al. HTLV-1 associated myelopathy, a new clinical entity. Lancet. 1986;1:1031-2.
    • (1986) Lancet , vol.1 , pp. 1031-1032
    • Osame, M.1    Usuku, K.2    Izumo, S.3
  • 8
    • 14644389344 scopus 로고    scopus 로고
    • Current views in HTLV-1-associated adult T-cell leukemia/ lymphoma
    • Nicot C. Current views in HTLV-1-associated adult T-cell leukemia/ lymphoma. Am J Hematol. 2005;78:232-9.
    • (2005) Am J Hematol , vol.78 , pp. 232-239
    • Nicot, C.1
  • 10
    • 25444474750 scopus 로고    scopus 로고
    • Cellular immune response to HTLV-1
    • Bangham C, Osame M. Cellular immune response to HTLV-1. Oncogene. 2005;24:6035-46.
    • (2005) Oncogene , vol.24 , pp. 6035-6046
    • Bangham, C.1    Osame, M.2
  • 11
    • 31944435791 scopus 로고    scopus 로고
    • Immunopathogenesis of HTLV-1 associated neurologic disease: Molecular, histopathologic, and immunologic approaches
    • Takenouchi N, Yao K, Jacobson S. Immunopathogenesis of HTLV-1 associated neurologic disease: molecular, histopathologic, and immunologic approaches. Front Biosci. 2004;9:2527-39.
    • (2004) Front Biosci , vol.9 , pp. 2527-2539
    • Takenouchi, N.1    Yao, K.2    Jacobson, S.3
  • 13
    • 0026515141 scopus 로고
    • Complex splicing in the HTLV family of retroviruses: Novel mRNAs and proteins produced by HTLV-1
    • Ciminale V, Pavlakis G, Derse D, Cunningham C, Felber B. Complex splicing in the HTLV family of retroviruses: novel mRNAs and proteins produced by HTLV-1. J Virol. 1992;66:1737-45.
    • (1992) J Virol , vol.66 , pp. 1737-1745
    • Ciminale, V.1    Pavlakis, G.2    Derse, D.3    Cunningham, C.4    Felber, B.5
  • 14
    • 0027362537 scopus 로고
    • Transcriptional activation of the HTLV-1 long terminal repeat by functional interaction of Tax1 and Ets1
    • Gitlin S, Dittmer J, Shin R, Brady J. Transcriptional activation of the HTLV-1 long terminal repeat by functional interaction of Tax1 and Ets1. J Virol. 1993;67:7307-16.
    • (1993) J Virol , vol.67 , pp. 7307-7316
    • Gitlin, S.1    Dittmer, J.2    Shin, R.3    Brady, J.4
  • 15
    • 25444462807 scopus 로고    scopus 로고
    • Transcriptional and post-transcriptional gene regulation of HTLV-1
    • Kashanchi F, Brady J. Transcriptional and post-transcriptional gene regulation of HTLV-1. Oncogene. 2005;24:5938-51.
    • (2005) Oncogene , vol.24 , pp. 5938-5951
    • Kashanchi, F.1    Brady, J.2
  • 16
    • 17544368687 scopus 로고    scopus 로고
    • The HTLV Rex protein
    • Younis I. Green P. The HTLV Rex protein. Front Biosci. 2005;10:431-45.
    • (2005) Front Biosci , vol.10 , pp. 431-445
    • Younis, I.1    Green, P.2
  • 17
    • 85117739578 scopus 로고    scopus 로고
    • Mesnard J, Barbeau B, Devaux C. HBZ, a new important player in the mys tery of adult T-cell leukemia. Blood. 2006;108:3979-82.
    • Mesnard J, Barbeau B, Devaux C. HBZ, a new important player in the mys tery of adult T-cell leukemia. Blood. 2006;108:3979-82.
  • 18
    • 33749497284 scopus 로고    scopus 로고
    • Coactivator-associated arginine methyltransferase 1 enhances transcriptional activity of the HTLV-1 long terminal repeat through direct interaction with Tax
    • Jeong S, Lu H, Cho W, Park H, Pise-Masison C, Brady J. Coactivator-associated arginine methyltransferase 1 enhances transcriptional activity of the HTLV-1 long terminal repeat through direct interaction with Tax. J Virol. 2006;80:10036-44.
    • (2006) J Virol , vol.80 , pp. 10036-10044
    • Jeong, S.1    Lu, H.2    Cho, W.3    Park, H.4    Pise-Masison, C.5    Brady, J.6
  • 19
    • 33745854207 scopus 로고    scopus 로고
    • TORC1 and TORC2 co-activators are required for tax activation of the HTLV-1 long terminal repeats
    • Siu Y, Chin K, Siu K, Yee Wai C, Jeang K, Jin D. TORC1 and TORC2 co-activators are required for tax activation of the HTLV-1 long terminal repeats. J Virol. 2006;80:7052-9.
    • (2006) J Virol , vol.80 , pp. 7052-7059
    • Siu, Y.1    Chin, K.2    Siu, K.3    Yee Wai, C.4    Jeang, K.5    Jin, D.6
  • 20
    • 11244303595 scopus 로고    scopus 로고
    • Enhanced activation of tax-dependent transcription of HTLV-1 long terminal repeat by TORC3
    • Koga H, Ohshima T, Shimotohno K. Enhanced activation of tax-dependent transcription of HTLV-1 long terminal repeat by TORC3. J Biol Chem. 2004;279:52978-83.
    • (2004) J Biol Chem , vol.279 , pp. 52978-52983
    • Koga, H.1    Ohshima, T.2    Shimotohno, K.3
  • 21
    • 0033499691 scopus 로고    scopus 로고
    • PCAF interacts with tax and stimulates tax transactivation in a histone acetyltransferase-independent manner
    • Jiang H, Lu H, Schiltz R, et al. PCAF interacts with tax and stimulates tax transactivation in a histone acetyltransferase-independent manner. Mol Cell Biol. 1999;19:8136-45.
    • (1999) Mol Cell Biol , vol.19 , pp. 8136-8145
    • Jiang, H.1    Lu, H.2    Schiltz, R.3
  • 22
    • 0031812011 scopus 로고    scopus 로고
    • An exposed KID-like domain in HTLV-1 Tax is responsible for the recruitment of coactivators CBP/p300
    • Harrod R, Tang Y, Nicot C, et al. An exposed KID-like domain in HTLV-1 Tax is responsible for the recruitment of coactivators CBP/p300. Mol Cell Biol. 1998;18:5052-61.
    • (1998) Mol Cell Biol , vol.18 , pp. 5052-5061
    • Harrod, R.1    Tang, Y.2    Nicot, C.3
  • 23
    • 0030797544 scopus 로고    scopus 로고
    • Anchoring of CREB binding protein to the HTLV-1 promoter: A molecular mechanism of Tax transactivation
    • Giebler H, Loring J, Van Orden K, et al. Anchoring of CREB binding protein to the HTLV-1 promoter: a molecular mechanism of Tax transactivation. Mol Cell Biol. 1997;17:5156-64.
    • (1997) Mol Cell Biol , vol.17 , pp. 5156-5164
    • Giebler, H.1    Loring, J.2    Van Orden, K.3
  • 24
    • 44149096216 scopus 로고    scopus 로고
    • HTLV-1 and apoptosis: Role in cellular transformation and recent advances in therapeutic approaches
    • Taylor J, Nicot C. HTLV-1 and apoptosis: role in cellular transformation and recent advances in therapeutic approaches. Apoptosis. 2008;13:733-47.
    • (2008) Apoptosis , vol.13 , pp. 733-747
    • Taylor, J.1    Nicot, C.2
  • 25
    • 0042467680 scopus 로고    scopus 로고
    • Cellular transformation by the HTLV-1 Tax protein, a jack-of-all-trades
    • Gatza M, Watt J, Marriott S. Cellular transformation by the HTLV-1 Tax protein, a jack-of-all-trades. Oncogene. 2003;22:5141-9.
    • (2003) Oncogene , vol.22 , pp. 5141-5149
    • Gatza, M.1    Watt, J.2    Marriott, S.3
  • 26
    • 28244499237 scopus 로고    scopus 로고
    • Inactivation of tumor suppressor genes and the progression of adult T-cell leukemia-lymphoma
    • Yamada Y, Kamihira S. Inactivation of tumor suppressor genes and the progression of adult T-cell leukemia-lymphoma. Leuk Lymphoma. 2005;46:1553-9.
    • (2005) Leuk Lymphoma , vol.46 , pp. 1553-1559
    • Yamada, Y.1    Kamihira, S.2
  • 27
    • 25444533092 scopus 로고    scopus 로고
    • Impact of HTLV-1 Tax on cell cycle progression and the cellular DNA damage repair response
    • Marriott S, Semmes O. Impact of HTLV-1 Tax on cell cycle progression and the cellular DNA damage repair response. Oncogene. 2005;24: 5986-95.
    • (2005) Oncogene , vol.24 , pp. 5986-5995
    • Marriott, S.1    Semmes, O.2
  • 28
    • 38449104105 scopus 로고    scopus 로고
    • Regulation of telomerase and telomeres: Human tumor viruses take control
    • Bellon M, Nicot C. Regulation of telomerase and telomeres: human tumor viruses take control. J Natl Cancer Inst. 2008;100:98-108.
    • (2008) J Natl Cancer Inst , vol.100 , pp. 98-108
    • Bellon, M.1    Nicot, C.2
  • 29
    • 0010293636 scopus 로고
    • Two cis-acting elements responsible for posttranscriptional trans-regulation of gene expression of HTLV-1
    • Seiki M, Inoue J, Hidaka M, Yoshida M. Two cis-acting elements responsible for posttranscriptional trans-regulation of gene expression of HTLV-1. Proc Natl Acad Sci USA. 1988;85:7124-8.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 7124-7128
    • Seiki, M.1    Inoue, J.2    Hidaka, M.3    Yoshida, M.4
  • 30
    • 0029130168 scopus 로고
    • Identification of a signal for rapid export of proteins from the nucleus
    • Wen W, Meinkoth J, Tsien R, Taylor S. Identification of a signal for rapid export of proteins from the nucleus. Cell. 1995;82:463-73.
    • (1995) Cell , vol.82 , pp. 463-473
    • Wen, W.1    Meinkoth, J.2    Tsien, R.3    Taylor, S.4
  • 31
    • 0029894726 scopus 로고    scopus 로고
    • Protein sequence requirements for function of the HTLV-1 Rex nuclear export signal delineated by a novel in vivo randomization-selection assay
    • Bogerd H, Fridell R, Benson R, Hua J, Cullen B. Protein sequence requirements for function of the HTLV-1 Rex nuclear export signal delineated by a novel in vivo randomization-selection assay. Mol Cell Biol. 1996;16:4207-14.
    • (1996) Mol Cell Biol , vol.16 , pp. 4207-4214
    • Bogerd, H.1    Fridell, R.2    Benson, R.3    Hua, J.4    Cullen, B.5
  • 32
    • 0029783724 scopus 로고    scopus 로고
    • Characterization of the nuclear export signal of HTLV-1 Rex reveals that nuclear export is mediated by position-variable hydrophobic interactions
    • Kim F, Beeche A, Hunter J, Chin D, Hope T. Characterization of the nuclear export signal of HTLV-1 Rex reveals that nuclear export is mediated by position-variable hydrophobic interactions. Mol Cell Biol. 1996;16:5147-55.
    • (1996) Mol Cell Biol , vol.16 , pp. 5147-5155
    • Kim, F.1    Beeche, A.2    Hunter, J.3    Chin, D.4    Hope, T.5
  • 33
    • 0029833093 scopus 로고    scopus 로고
    • The HTLV-1 posttranscriptional trans-activator Rex con tains a nuclear export signal
    • Palmeri D, Malim M. The HTLV-1 posttranscriptional trans-activator Rex con tains a nuclear export signal. J Virol. 1996;70:6442-5.
    • (1996) J Virol , vol.70 , pp. 6442-6445
    • Palmeri, D.1    Malim, M.2
  • 34
    • 0030748907 scopus 로고    scopus 로고
    • Evidence for a role of CRM1 in signal-mediated nuclear protein export
    • Ossareh-Nazari B, Bachelerie F, Dargemont C. Evidence for a role of CRM1 in signal-mediated nuclear protein export. Science. 1997;278:141-4.
    • (1997) Science , vol.278 , pp. 141-144
    • Ossareh-Nazari, B.1    Bachelerie, F.2    Dargemont, C.3
  • 35
    • 0030924190 scopus 로고    scopus 로고
    • CRM1 is an export receptor for leucine-rich nuclear export signals
    • Fornerod M, Ohno M, Yoshida M, Mattaj I. CRM1 is an export receptor for leucine-rich nuclear export signals. Cell. 1997;90:1051-60.
    • (1997) Cell , vol.90 , pp. 1051-1060
    • Fornerod, M.1    Ohno, M.2    Yoshida, M.3    Mattaj, I.4
  • 36
    • 0030985459 scopus 로고    scopus 로고
    • Exportin 1 (Crm1p) is an essential nu clear export factor
    • Stade K, Ford C, Guthrie C, Weis K. Exportin 1 (Crm1p) is an essential nu clear export factor. Cell. 1997;90:1041-50.
    • (1997) Cell , vol.90 , pp. 1041-1050
    • Stade, K.1    Ford, C.2    Guthrie, C.3    Weis, K.4
  • 37
    • 0026419320 scopus 로고
    • Catalysis of guanine nucleotide exchange on Ran by the mitotic regulator RCC1
    • Bischoff F, Ponstingl H. Catalysis of guanine nucleotide exchange on Ran by the mitotic regulator RCC1. Nature. 1991;354:80-2.
    • (1991) Nature , vol.354 , pp. 80-82
    • Bischoff, F.1    Ponstingl, H.2
  • 38
    • 0031878580 scopus 로고    scopus 로고
    • Involvement of human CRM1 (exportin 1) in the export and multimerization of the Rex protein of HTLV-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 HTLV-1. J Virol. 1998;72:6602-7.
    • (1998) J Virol , vol.72 , pp. 6602-6607
    • Hakata, Y.1    Umemoto, T.2    Matsushita, S.3    Shida, H.4
  • 40
    • 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, Cullen B. HIV-1 structural gene expression requires the binding of multiple Rev monomers to the viral RRE: implications for HIV-1 latency. Cell. 1991;65:241-8.
    • (1991) Cell , vol.65 , pp. 241-248
    • Malim, M.1    Cullen, B.2
  • 41
    • 0027418792 scopus 로고
    • Dominant negative mutants of HTLV-1 Rex and HIV-1 Rev fail to multimerize in vivo
    • Bogerd H, Greene W. Dominant negative mutants of HTLV-1 Rex and HIV-1 Rev fail to multimerize in vivo. J Virol. 1993;67:2496-502.
    • (1993) J Virol , vol.67 , pp. 2496-2502
    • Bogerd, H.1    Greene, W.2
  • 42
    • 0031706630 scopus 로고    scopus 로고
    • Multimer formation is not essential for nuclear export of HTLV-1 Rex transactivator protein
    • Heger P, Rosorius O, Koch C, Casari G, Grassmann R, Hauber J. Multimer formation is not essential for nuclear export of HTLV-1 Rex transactivator protein. J Virol. 1998;72:8659-68.
    • (1998) J Virol , vol.72 , pp. 8659-8668
    • Heger, P.1    Rosorius, O.2    Koch, C.3    Casari, G.4    Grassmann, R.5    Hauber, J.6
  • 43
    • 0032798427 scopus 로고    scopus 로고
    • Establishment of a seronegative HTLV-1 carrier state in rats inoculated with a syngeneic HTLV-1-immortalized T-cell line preferentially expressing Tax
    • Koya Y, Ohashi T, Kato H, et al. Establishment of a seronegative HTLV-1 carrier state in rats inoculated with a syngeneic HTLV-1-immortalized T-cell line preferentially expressing Tax. J Virol. 1999;73:6436-43.
    • (1999) J Virol , vol.73 , pp. 6436-6443
    • Koya, Y.1    Ohashi, T.2    Kato, H.3
  • 44
    • 0035158959 scopus 로고    scopus 로고
    • Rat CRM1 is responsible for the poor activity of HTLV-1 Rex protein in rat cells
    • Hakata Y, Yamada M, Shida H. Rat CRM1 is responsible for the poor activity of HTLV-1 Rex protein in rat cells. J Virol. 2001;75:11515-25.
    • (2001) J Virol , vol.75 , pp. 11515-11525
    • Hakata, Y.1    Yamada, M.2    Shida, H.3
  • 45
    • 34249785398 scopus 로고    scopus 로고
    • Enhanced replication of HTLV-1 in T-cells from transgenic rats expressing human CRM1 that is regulated in a natural manner
    • Takayanagi R, Ohashi T, Yamashita E, et al. Enhanced replication of HTLV-1 in T-cells from transgenic rats expressing human CRM1 that is regulated in a natural manner. J Virol. 2007;81:5908-18.
    • (2007) J Virol , vol.81 , pp. 5908-5918
    • Takayanagi, R.1    Ohashi, T.2    Yamashita, E.3
  • 46
    • 0242552521 scopus 로고    scopus 로고
    • A multifunctional domain in human CRM1 (exportin 1) mediates RanBP3 binding and multimerization of HTLV-1 Rex protein
    • Hakata Y, Yamada M, Shida H. A multifunctional domain in human CRM1 (exportin 1) mediates RanBP3 binding and multimerization of HTLV-1 Rex protein. Mol Cell Biol. 2003;23:8751-61.
    • (2003) Mol Cell Biol , vol.23 , pp. 8751-8761
    • Hakata, Y.1    Yamada, M.2    Shida, H.3
  • 47
    • 0028922123 scopus 로고
    • Effects of translation initiation factor eIF-5A on the functioning of HTLV-1 Rex and HIV Rev inhibited trans dominantly by a Rex mutant deficient in RNA binding
    • Katahira J, Ishizaki T, Sakai H, Adachi A, Yamamoto K, Shida H. Effects of translation initiation factor eIF-5A on the functioning of HTLV-1 Rex and HIV Rev inhibited trans dominantly by a Rex mutant deficient in RNA binding. J Virol. 1995;69:3125-33.
    • (1995) J Virol , vol.69 , pp. 3125-3133
    • Katahira, J.1    Ishizaki, T.2    Sakai, H.3    Adachi, A.4    Yamamoto, K.5    Shida, H.6
  • 48
    • 0028142897 scopus 로고
    • A single stem-loop structure within the HTLV-1 Rex response element is sufficient to mediate Rex activity in vivo
    • Grone M, Hoffmann E, Berchtold S, Cullen R, Grassmann R. A single stem-loop structure within the HTLV-1 Rex response element is sufficient to mediate Rex activity in vivo. Virology. 1994;204:144-52.
    • (1994) Virology , vol.204 , pp. 144-152
    • Grone, M.1    Hoffmann, E.2    Berchtold, S.3    Cullen, R.4    Grassmann, R.5
  • 49
    • 0024747130 scopus 로고
    • Comparative analysis of the HTLV-1 Rex and HIV-1 Rev trans-regulatory proteins and their RNA response elements
    • Hanly S, Rimsky L, Malim M, et al. Comparative analysis of the HTLV-1 Rex and HIV-1 Rev trans-regulatory proteins and their RNA response elements. Genes Dev. 1989;3:1534-44.
    • (1989) Genes Dev , vol.3 , pp. 1534-1544
    • Hanly, S.1    Rimsky, L.2    Malim, M.3
  • 50
    • 0025296036 scopus 로고
    • Structure-function ana lyses of the HTLV-1 Rex and HIV-1 Rev RNA response elements: Insights into the mechanism of Rex and Rev action
    • Ahmed Y, Hanly S, Malim M, Cullen B, Greene W. Structure-function ana lyses of the HTLV-1 Rex and HIV-1 Rev RNA response elements: insights into the mechanism of Rex and Rev action. Genes Dev. 1990;4:1014-22.
    • (1990) Genes Dev , vol.4 , pp. 1014-1022
    • Ahmed, Y.1    Hanly, S.2    Malim, M.3    Cullen, B.4    Greene, W.5
  • 51
    • 0025954618 scopus 로고
    • The HTLV-1 Rex transactivator binds directly to the HTLV-1 Rex and the HIV-1 Rev RNA response elements
    • Bogerd H, Huckaby G, Ahmed Y, Hanly S, Greene W. The HTLV-1 Rex transactivator binds directly to the HTLV-1 Rex and the HIV-1 Rev RNA response elements. Proc Natl Acad Sci USA. 1991;88:5704-8.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 5704-5708
    • Bogerd, H.1    Huckaby, G.2    Ahmed, Y.3    Hanly, S.4    Greene, W.5
  • 52
    • 0026471349 scopus 로고
    • Specific binding of the HTLV-1 Rex protein to a short RNA sequence located within the Rex-response element
    • Bogerd H, Tiley L, Cullen B. Specific binding of the HTLV-1 Rex protein to a short RNA sequence located within the Rex-response element. J Virol. 1992;66:7572-5.
    • (1992) J Virol , vol.66 , pp. 7572-7575
    • Bogerd, H.1    Tiley, L.2    Cullen, B.3
  • 53
    • 0023705436 scopus 로고
    • Functional replacement of the HIV-1 rev protein by the HTLV-1 rex protein
    • Rimsky L, Hauber J, Dukovich M, et al. Functional replacement of the HIV-1 rev protein by the HTLV-1 rex protein. Nature. 1988;335:738-40.
    • (1988) Nature , vol.335 , pp. 738-740
    • Rimsky, L.1    Hauber, J.2    Dukovich, M.3
  • 54
    • 0025879947 scopus 로고
    • The Rex regulatory protein of HTLV-1 binds specifically to its target site within the viral RNA
    • Unge T, Solomin L, Mellini M, Derse D, Felber B, Pavlakis G. The Rex regulatory protein of HTLV-1 binds specifically to its target site within the viral RNA. Proc Natl Acad Sci USA. 1991;88:7145-49.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 7145-7149
    • Unge, T.1    Solomin, L.2    Mellini, M.3    Derse, D.4    Felber, B.5    Pavlakis, G.6
  • 55
    • 0024437549 scopus 로고
    • Trans-dominant inactivation of HTLV-1 and HIV-1 gene expression by mutation of the HTLV-1 Rex transactivator
    • Rimsky L, Dodon M, Dixon E, Greene W. Trans-dominant inactivation of HTLV-1 and HIV-1 gene expression by mutation of the HTLV-1 Rex transactivator. Nature. 1989;341:453-6.
    • (1989) Nature , vol.341 , pp. 453-456
    • Rimsky, L.1    Dodon, M.2    Dixon, E.3    Greene, W.4
  • 56
    • 0025251610 scopus 로고
    • Different sites of interaction for Rev, Tev, and Rex proteins within the Rev-responsive element of HIV-1
    • Solomin L, Felber B, Pavlakis G. Different sites of interaction for Rev, Tev, and Rex proteins within the Rev-responsive element of HIV-1. J Virol. 1990;64:6010-17.
    • (1990) J Virol , vol.64 , pp. 6010-6017
    • Solomin, L.1    Felber, B.2    Pavlakis, G.3
  • 57
    • 0037166259 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonucleoprotein A1 interferes with the binding of the HTLV-1 rex regulatory protein to its response element
    • Dodon M, Hamaia S, Martin J, Gazzolo L. Heterogeneous nuclear ribonucleoprotein A1 interferes with the binding of the HTLV-1 rex regulatory protein to its response element. J Biol Chem. 2002; 277:18744-52.
    • (2002) J Biol Chem , vol.277 , pp. 18744-18752
    • Dodon, M.1    Hamaia, S.2    Martin, J.3    Gazzolo, L.4
  • 58
    • 0026092676 scopus 로고
    • The HTLV-1 Rex response element mediates a novel form of mRNA polyadenylation
    • Ahmed Y, Gilmartin G, Hanly S, Nevins J, Greene W. The HTLV-1 Rex response element mediates a novel form of mRNA polyadenylation. Cell. 1991;64:727-37.
    • (1991) Cell , vol.64 , pp. 727-737
    • Ahmed, Y.1    Gilmartin, G.2    Hanly, S.3    Nevins, J.4    Greene, W.5
  • 59
    • 0023812595 scopus 로고
    • Sequence requirements for nucleolar localization of HTLV-1 pX protein, which regulates viral RNA processing
    • Siomi H, Shida H, Nam S, Nosaka T, Maki M, Hatanaka M. Sequence requirements for nucleolar localization of HTLV-1 pX protein, which regulates viral RNA processing. Cell. 1988;55:197-209.
    • (1988) Cell , vol.55 , pp. 197-209
    • Siomi, H.1    Shida, H.2    Nam, S.3    Nosaka, T.4    Maki, M.5    Hatanaka, M.6
  • 60
    • 0027252951 scopus 로고
    • Nucleolar targeting signal of Rex protein of HTLV-1 specifically binds to nucleolar shuttle protein B-23
    • Adachi Y, Copeland T, Hatanaka M, Oroszlan S. Nucleolar targeting signal of Rex protein of HTLV-1 specifically binds to nucleolar shuttle protein B-23. J Biol Chem. 1993;268;13930-4.
    • (1993) J Biol Chem , vol.268 , pp. 13930-13934
    • Adachi, Y.1    Copeland, T.2    Hatanaka, M.3    Oroszlan, S.4
  • 61
    • 34347246707 scopus 로고    scopus 로고
    • HTLV-1 rex and p30 interactions govern the switch between virus latency and replication
    • Sinha-Datta U, Datta A, Ghorbel S, Dodon M, and Nicot C. HTLV-1 rex and p30 interactions govern the switch between virus latency and replication. J Biol Chem. 2007;282:14608-15.
    • (2007) J Biol Chem , vol.282 , pp. 14608-14615
    • Sinha-Datta, U.1    Datta, A.2    Ghorbel, S.3    Dodon, M.4    Nicot, C.5
  • 62
    • 2342668567 scopus 로고    scopus 로고
    • The HTLV-1 Rex protein induces nuclear accumulation of unspliced viral RNA by avoiding intron excision and degradation
    • Grone M, Koch C, Grassmann R. The HTLV-1 Rex protein induces nuclear accumulation of unspliced viral RNA by avoiding intron excision and degradation. Virology. 1996;218:316-25.
    • (1996) Virology , vol.218 , pp. 316-325
    • Grone, M.1    Koch, C.2    Grassmann, R.3
  • 63
    • 0025288185 scopus 로고
    • Protein kinase inhibitor H-7 blocks ac cumulation of unspliced mRNA of HTLV-1
    • Adachi Y, Nosaka T, Hatanaka M. Protein kinase inhibitor H-7 blocks ac cumulation of unspliced mRNA of HTLV-1. Biochem Biophys Res Commun. 1990;169:469-75.
    • (1990) Biochem Biophys Res Commun , vol.169 , pp. 469-475
    • Adachi, Y.1    Nosaka, T.2    Hatanaka, M.3
  • 64
    • 0026787758 scopus 로고
    • Phosphorylation of the Rex protein of HTLV-1
    • Adachi Y, Copeland T, Takahashi C, et al. Phosphorylation of the Rex protein of HTLV-1. J Biol Chem. 1992;267:21977-81.
    • (1992) J Biol Chem , vol.267 , pp. 21977-21981
    • Adachi, Y.1    Copeland, T.2    Takahashi, C.3
  • 65
    • 0027407077 scopus 로고
    • Influence of HTLV-1 tax and rex on IL-2 gene expression
    • McGuire K, Curtiss V, Larson E, Haseltine W. Influence of HTLV-1 tax and rex on IL-2 gene expression. J Virol. 1993;67:1590-9.
    • (1993) J Virol , vol.67 , pp. 1590-1599
    • McGuire, K.1    Curtiss, V.2    Larson, E.3    Haseltine, W.4
  • 66
    • 0025146986 scopus 로고
    • HTLV-1 p27rex stabilizes human IL-2 receptor-α chain mRNA
    • Kanamori H, Suzuki N, Siomi H, et al. HTLV-1 p27rex stabilizes human IL-2 receptor-α chain mRNA. EMBO J. 1990;9:4161-6.
    • (1990) EMBO J , vol.9 , pp. 4161-4166
    • Kanamori, H.1    Suzuki, N.2    Siomi, H.3
  • 67
    • 0026026598 scopus 로고
    • The nucleolar localization signal of the HTLV-1 protein p27rex is important for stabilization of IL-2 receptor-α subunit mRNA by p27rex
    • White K, Nosaka T, Kanamori H, Hatanaka M, Honjo T. The nucleolar localization signal of the HTLV-1 protein p27rex is important for stabilization of IL-2 receptor-α subunit mRNA by p27rex. Biochem Biophys Res Commun. 1991;175:98-103.
    • (1991) Biochem Biophys Res Commun , vol.175 , pp. 98-103
    • White, K.1    Nosaka, T.2    Kanamori, H.3    Hatanaka, M.4    Honjo, T.5
  • 68
    • 0029591283 scopus 로고    scopus 로고
    • Kanamori H, Kodama T, Yazaki Y. The 5′ coding sequence of IL-2 receptor-α chain mRNA mediates mRNA stabilization by HTLV-1 Rex. Immunology. 1995;86:551-5.
    • Kanamori H, Kodama T, Yazaki Y. The 5′ coding sequence of IL-2 receptor-α chain mRNA mediates mRNA stabilization by HTLV-1 Rex. Immunology. 1995;86:551-5.
  • 69
    • 0032946939 scopus 로고    scopus 로고
    • Altered expression of tyrosine kinases of the Src and Syk families in HTLV-1-infected T-cell lines
    • Weil R, Levraud J, Dodon M, et al. Altered expression of tyrosine kinases of the Src and Syk families in HTLV-1-infected T-cell lines. J Virol. 1999;73:3709-17.
    • (1999) J Virol , vol.73 , pp. 3709-3717
    • Weil, R.1    Levraud, J.2    Dodon, M.3
  • 70
    • 0025752347 scopus 로고
    • Regulation of T-cell receptor signaling by a src family protein-tyrosine kinase (p59fyn)
    • Cooke M, Abraham K, Forbush K, Perlmutter R. Regulation of T-cell receptor signaling by a src family protein-tyrosine kinase (p59fyn). Cell. 1991;65:281-91.
    • (1991) Cell , vol.65 , pp. 281-291
    • Cooke, M.1    Abraham, K.2    Forbush, K.3    Perlmutter, R.4
  • 71
    • 0035057574 scopus 로고    scopus 로고
    • Vascular cell adhesion molecule-1 induced by HTLV-1 Tax protein in T-cells stimulates proliferation of human T-lymphocytes
    • Valentin H, Hamaia S, Konig S, Gazzolo L. Vascular cell adhesion molecule-1 induced by HTLV-1 Tax protein in T-cells stimulates proliferation of human T-lymphocytes. J Gen Virol. 2001;82:831-5.
    • (2001) J Gen Virol , vol.82 , pp. 831-835
    • Valentin, H.1    Hamaia, S.2    Konig, S.3    Gazzolo, L.4
  • 72
    • 11144353813 scopus 로고    scopus 로고
    • HTLV-1-encoded p30II is a post-transcriptional negative regulator of viral replication
    • Nicot C, Dundr M, Johnson J. et al. HTLV-1-encoded p30II is a post-transcriptional negative regulator of viral replication. Nat Med. 2004;10:197-201.
    • (2004) Nat Med , vol.10 , pp. 197-201
    • Nicot, C.1    Dundr, M.2    Johnson, J.3
  • 73
    • 0036713498 scopus 로고    scopus 로고
    • Critical role of HTLV-1 accessory proteins in viral replication and pathogenesis
    • Albrecht B, Lairmore M. Critical role of HTLV-1 accessory proteins in viral replication and pathogenesis. Microbiol Mol Biol Rev. 2002;66:396-406.
    • (2002) Microbiol Mol Biol Rev , vol.66 , pp. 396-406
    • Albrecht, B.1    Lairmore, M.2
  • 74
    • 25444436726 scopus 로고    scopus 로고
    • HTLV-1 nonstructural genes and their functions
    • Nicot C, Harrod R, Ciminale V, Franchini G. HTLV-1 nonstructural genes and their functions. Oncogene. 2005;24:6026-34.
    • (2005) Oncogene , vol.24 , pp. 6026-6034
    • Nicot, C.1    Harrod, R.2    Ciminale, V.3    Franchini, G.4
  • 76
    • 0030693113 scopus 로고    scopus 로고
    • X-I and X-II open reading frames of HTLV-1 are not required for virus replication or for immortalization of primary T-cells in vitro
    • Derse D, Mikovits J, Ruscetti F. X-I and X-II open reading frames of HTLV-1 are not required for virus replication or for immortalization of primary T-cells in vitro. Virology. 1997;237:123-8.
    • (1997) Virology , vol.237 , pp. 123-128
    • Derse, D.1    Mikovits, J.2    Ruscetti, F.3
  • 77
    • 0031969651 scopus 로고    scopus 로고
    • HTLV-1 pX-I and pX-II open reading frames are dispensable for the immortalization of primary lymphocytes
    • Robek M, Wong F, Ratner L. HTLV-1 pX-I and pX-II open reading frames are dispensable for the immortalization of primary lymphocytes. J Virol. 1998;72:4458-62.
    • (1998) J Virol , vol.72 , pp. 4458-4462
    • Robek, M.1    Wong, F.2    Ratner, L.3
  • 78
    • 0345735917 scopus 로고    scopus 로고
    • Roles of viral and cellular proteins in the expression of alternatively spliced HTLV-1 pX mRNAs
    • Princler G, Julias J, Hughes S, Derse D. Roles of viral and cellular proteins in the expression of alternatively spliced HTLV-1 pX mRNAs. Virology. 2003;317:136-45.
    • (2003) Virology , vol.317 , pp. 136-145
    • Princler, G.1    Julias, J.2    Hughes, S.3    Derse, D.4
  • 79
    • 0030925885 scopus 로고    scopus 로고
    • Differential expression of alternatively spliced pX mRNAs in HTLV-I-infected cell lines
    • Cereseto A, Berneman Z, Koralnik I, Vaughn J, Franchini G, Klotman M. Differential expression of alternatively spliced pX mRNAs in HTLV-I-infected cell lines. Leukemia. 1997;11:866-70.
    • (1997) Leukemia , vol.11 , pp. 866-870
    • Cereseto, A.1    Berneman, Z.2    Koralnik, I.3    Vaughn, J.4    Franchini, G.5    Klotman, M.6
  • 80
    • 0026552635 scopus 로고
    • Expression of alternatively spliced HTLV-1 pX mRNA in infected cell lines and in primary uncultured cells from patients with ATLL and healthy carriers
    • Berneman Z, Gartenhaus R, Reitz M, et al. Expression of alternatively spliced HTLV-1 pX mRNA in infected cell lines and in primary uncultured cells from patients with ATLL and healthy carriers. Proc Natl Acad Sci USA. 1992;89:3005-9.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 3005-3009
    • Berneman, Z.1    Gartenhaus, R.2    Reitz, M.3
  • 81
    • 0034662507 scopus 로고    scopus 로고
    • The HTLV-1 orfI protein is recognized by serum antibodies from naturally infected humans and experimentally infected rabbits
    • Dekaban G, Peters A, Mulloy J, et al. The HTLV-1 orfI protein is recognized by serum antibodies from naturally infected humans and experimentally infected rabbits. Virology. 2000;274:86-93.
    • (2000) Virology , vol.274 , pp. 86-93
    • Dekaban, G.1    Peters, A.2    Mulloy, J.3
  • 82
    • 0034614907 scopus 로고    scopus 로고
    • Evidence for the chronic in vivo production of HTLV-1 Rof and Tof proteins from cytotoxic T lymphocytes directed against viral peptides
    • Pique C, Ureta-Vidal A, Gessain A, et al. Evidence for the chronic in vivo production of HTLV-1 Rof and Tof proteins from cytotoxic T lymphocytes directed against viral peptides. J Exp Med. 2000;191:567-72.
    • (2000) J Exp Med , vol.191 , pp. 567-572
    • Pique, C.1    Ureta-Vidal, A.2    Gessain, A.3
  • 83
    • 33645223273 scopus 로고    scopus 로고
    • HTLV-1 mitochondrion-localizing protein p13(II) is required for viral infectivity in vivo
    • Hiraragi H, Kim S, Phipps A, et al. HTLV-1 mitochondrion-localizing protein p13(II) is required for viral infectivity in vivo. J Virol. 2006;80:3469-76.
    • (2006) J Virol , vol.80 , pp. 3469-3476
    • Hiraragi, H.1    Kim, S.2    Phipps, A.3
  • 84
    • 1842589405 scopus 로고    scopus 로고
    • HTLV-1 open reading frame II-encoded p30II is required for in vivo replication: Evidence of in vivo reversion
    • Silverman L, Phipps A, Montgomery A, Ratner L, Lairmore M. HTLV-1 open reading frame II-encoded p30II is required for in vivo replication: evidence of in vivo reversion. J Virol. 2004;78:3837-45.
    • (2004) J Virol , vol.78 , pp. 3837-3845
    • Silverman, L.1    Phipps, A.2    Montgomery, A.3    Ratner, L.4    Lairmore, M.5
  • 85
    • 0034331210 scopus 로고    scopus 로고
    • In vitro and in vivo functional analysis of HTLV-1 pX open reading frames I and II
    • Lairmore M, Albrecht B, D'Souza C, et al. In vitro and in vivo functional analysis of HTLV-1 pX open reading frames I and II. AIDS Res Hum Retroviruses. 2000;16:1757-64.
    • (2000) AIDS Res Hum Retroviruses , vol.16 , pp. 1757-1764
    • Lairmore, M.1    Albrecht, B.2    D'Souza, C.3
  • 86
    • 0033967463 scopus 로고    scopus 로고
    • Functional role of pX open reading frame II of HTLV-1 in maintenance of viral loads in vivo
    • Bartoe J, Albrecht B, Collins N, et al. Functional role of pX open reading frame II of HTLV-1 in maintenance of viral loads in vivo. J Virol. 2000;74:1094-100.
    • (2000) J Virol , vol.74 , pp. 1094-1100
    • Bartoe, J.1    Albrecht, B.2    Collins, N.3
  • 88
    • 18144386244 scopus 로고    scopus 로고
    • HTLV-1 p30II alters cellular gene expression to selectively enhance signaling pathways that activate T lymphocytes
    • Michael B, Nair A, Hiraragi H, et al. HTLV-1 p30II alters cellular gene expression to selectively enhance signaling pathways that activate T lymphocytes. Retrovirology. 2004;1:39.
    • (2004) Retrovirology , vol.1 , pp. 39
    • Michael, B.1    Nair, A.2    Hiraragi, H.3
  • 89
    • 4644248241 scopus 로고    scopus 로고
    • Repression of HTLV type 1 and type 2 replication by a viral mRNA-encoded posttranscriptional regulator
    • Younis I, Khair L, Dundr M, Lairmore M, Franchini G, Green P. Repression of HTLV type 1 and type 2 replication by a viral mRNA-encoded posttranscriptional regulator. J Virol. 2004;78:11077-83.
    • (2004) J Virol , vol.78 , pp. 11077-11083
    • Younis, I.1    Khair, L.2    Dundr, M.3    Lairmore, M.4    Franchini, G.5    Green, P.6
  • 90
    • 0035365808 scopus 로고    scopus 로고
    • Functional architecture in the cell nucleus
    • Dundr M, Misteli T. Functional architecture in the cell nucleus. Biochem J. 2001;356:297-310.
    • (2001) Biochem J , vol.356 , pp. 297-310
    • Dundr, M.1    Misteli, T.2
  • 91
    • 0027941844 scopus 로고
    • Identification of the nucleolar targeting signal of human angiogenin
    • Moroianu J, Riordan J. Identification of the nucleolar targeting signal of human angiogenin. Biochem Biophys Res Commun. 1994;203:1765-72.
    • (1994) Biochem Biophys Res Commun , vol.203 , pp. 1765-1772
    • Moroianu, J.1    Riordan, J.2
  • 92
    • 0027733676 scopus 로고
    • Determination of the functional domains involved in nucleolar targeting of nucleolin
    • Creancier L, Prats H, Zanibellato C, Amalric F, Bugler B. Determination of the functional domains involved in nucleolar targeting of nucleolin. Mol Biol Cell. 1993;4:1239-50.
    • (1993) Mol Biol Cell , vol.4 , pp. 1239-1250
    • Creancier, L.1    Prats, H.2    Zanibellato, C.3    Amalric, F.4    Bugler, B.5
  • 93
    • 33846004438 scopus 로고    scopus 로고
    • HTLV-1 p30 nuclear/nucleolar retention is mediated through interactions with RNA and a constituent of the 60 S ribosomal subunit
    • Ghorbel S, Sinha-Datta U, Dundr M, Brown M, Franchini G, Nicot C. HTLV-1 p30 nuclear/nucleolar retention is mediated through interactions with RNA and a constituent of the 60 S ribosomal subunit. J Biol Chem. 2006;281:37150-8.
    • (2006) J Biol Chem , vol.281 , pp. 37150-37158
    • Ghorbel, S.1    Sinha-Datta, U.2    Dundr, M.3    Brown, M.4    Franchini, G.5    Nicot, C.6
  • 95
    • 33846547544 scopus 로고    scopus 로고
    • RNA viruses: Hijacking the dynamic nucleolus
    • Hiscox J. RNA viruses: hijacking the dynamic nucleolus. Nat Rev Microbiol. 2007;5:119-27.
    • (2007) Nat Rev Microbiol , vol.5 , pp. 119-127
    • Hiscox, J.1
  • 96
    • 0035983223 scopus 로고    scopus 로고
    • The nucleolus-a gateway to viral infection?
    • Hiscox J. The nucleolus-a gateway to viral infection? Arch Virol. 2002;147:1077-89.
    • (2002) Arch Virol , vol.147 , pp. 1077-1089
    • Hiscox, J.1
  • 97
    • 33645849521 scopus 로고    scopus 로고
    • Human ribosomal protein L18a interacts with HCV internal ribosome entry site
    • Dhar D, Mapa K, Pudi R, Srinivasan P, Bodhinathan K, Das S. Human ribosomal protein L18a interacts with HCV internal ribosome entry site. Arch Virol. 2006;151:509-24.
    • (2006) Arch Virol , vol.151 , pp. 509-524
    • Dhar, D.1    Mapa, K.2    Pudi, R.3    Srinivasan, P.4    Bodhinathan, K.5    Das, S.6
  • 98
    • 10344243545 scopus 로고    scopus 로고
    • Coordinated assembly of human translation initiation complexes by the HCV internal ribosome entry site RNA
    • Ji H, Fraser C, Yu Y, Leary J, Doudna J. Coordinated assembly of human translation initiation complexes by the HCV internal ribosome entry site RNA. Proc Natl Acad Sci USA. 2004;101:16990-5.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 16990-16995
    • Ji, H.1    Fraser, C.2    Yu, Y.3    Leary, J.4    Doudna, J.5
  • 99
    • 27144546116 scopus 로고    scopus 로고
    • Haas M, Geldreich A, Bureau M, et al. The open reading frame VI product of Cauliflower mosaic virus is a nucleocytoplasmic protein: its N terminus mediates its nuclear export and formation of electron-dense viroplasms. Plant Cell. 2005;17:927-43.
    • Haas M, Geldreich A, Bureau M, et al. The open reading frame VI product of Cauliflower mosaic virus is a nucleocytoplasmic protein: its N terminus mediates its nuclear export and formation of electron-dense viroplasms. Plant Cell. 2005;17:927-43.
  • 100
    • 9944254163 scopus 로고    scopus 로고
    • P6 protein of Cauliflower mosaic virus, a translation reinitiator, interacts with ribosomal protein L13 from Arabidopsis thaliana
    • Bureau M
    • Bureau M, Leh V, Haas M, et al. P6 protein of Cauliflower mosaic virus, a translation reinitiator, interacts with ribosomal protein L13 from Arabidopsis thaliana. J Gen Virol. 2004;85;3765-75.
    • (2004) J Gen Virol , vol.85 , pp. 3765-3775
    • Leh, V.1    Haas, M.2
  • 101
    • 0034606669 scopus 로고    scopus 로고
    • The cauliflower mosaic virus translational transactivator interacts with the 60S ribosomal subunit protein L18 of Arabidopsis thaliana
    • Leh V, Yot P, Keller M. The cauliflower mosaic virus translational transactivator interacts with the 60S ribosomal subunit protein L18 of Arabidopsis thaliana. Virology. 2000;266:1-7.
    • (2000) Virology , vol.266 , pp. 1-7
    • Leh, V.1    Yot, P.2    Keller, M.3
  • 102
    • 0029160316 scopus 로고
    • The roles of nucleolar structure and function in the subcellular location of the HIV-1 Rev protein
    • Dundr M, Leno G, Hammarskjold M, et al. The roles of nucleolar structure and function in the subcellular location of the HIV-1 Rev protein. J Cell Sci. 1995;108:2811-23.
    • (1995) J Cell Sci , vol.108 , pp. 2811-2823
    • Dundr, M.1    Leno, G.2    Hammarskjold, M.3
  • 103
    • 0029977285 scopus 로고    scopus 로고
    • Nucleocytoplasmic redistribution of the HTLV-1 Rex protein: Alterations by co-expression of the HTLV-1 p21x protein
    • Kubota S, Hatanaka M, Pomerantz R. Nucleocytoplasmic redistribution of the HTLV-1 Rex protein: alterations by co-expression of the HTLV-1 p21x protein. Virology. 1996;220:502-7.
    • (1996) Virology , vol.220 , pp. 502-507
    • Kubota, S.1    Hatanaka, M.2    Pomerantz, R.3


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