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Volumn 85, Issue 6, 2011, Pages 3020-3024

Effects of microtubule modulators on HIV-1 infection of transformed and resting CD4 T cells

Author keywords

[No Author keywords available]

Indexed keywords

COLCHICINE; NOCODAZOLE; PACLITAXEL; VINBLASTINE; ZIDOVUDINE;

EID: 79952369523     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.02462-10     Document Type: Article
Times cited : (34)

References (50)
  • 1
    • 0030835321 scopus 로고    scopus 로고
    • Pseudotyping human immunodeficiency virus type 1 (HIV-1) by the glycoprotein of vesicular stomatitis virus targets HIV-1 entry to an endocytic pathway and suppresses both the requirement for nef and the sensitivity to Cyclosporin A
    • Aiken, C. 1997. Pseudotyping human immunodeficiency virus type 1 (HIV-1) by the glycoprotein of vesicular stomatitis virus targets HIV-1 entry to an endocytic pathway and suppresses both the requirement for Nef and the sensitivity to cyclosporin A. J. Virol. 71:5871-5877. (Pubitemid 27304923)
    • (1997) Journal of Virology , vol.71 , Issue.8 , pp. 5871-5877
    • Aiken, C.1
  • 2
    • 0030743974 scopus 로고    scopus 로고
    • The effects of vinblastine on the expression of human immunodeficiency virus type 1 long terminal repeat
    • Akan, E., C. M. Chang-Liu, J. Watanabe, K. Ishizawa, and G. E. Woloschak. 1997. The effects of vinblastine on the expression of human immunodeficiency virus type 1 long terminal repeat. Leuk. Res. 21:459-464.
    • (1997) Leuk. Res. , vol.21 , pp. 459-464
    • Akan, E.1    Chang-Liu, C.M.2    Watanabe, J.3    Ishizawa, K.4    Woloschak, G.E.5
  • 3
    • 0035009245 scopus 로고    scopus 로고
    • Endocytic traffic in polarized epithelial cells: Role of the actin and microtubule cytoskeleton
    • DOI 10.1034/j.1600-0854.2001.020301.x
    • Apodaca, G. 2001. Endocytic traffic in polarized epithelial cells: role of the actin and microtubule cytoskeleton. Traffic 2:149-159. (Pubitemid 32487546)
    • (2001) Traffic , vol.2 , Issue.3 , pp. 149-159
    • Apodaca, G.1
  • 5
    • 0031584820 scopus 로고    scopus 로고
    • Differential effects of colchicine and its B-ring modified analog MTPT on the assembly-independent GTPase activity of purified beta-tubulin isoforms from bovine brain
    • Banerjee, A. 1997. Differential effects of colchicine and its B-ring modified analog MTPT on the assembly-independent GTPase activity of purified beta-tubulin isoforms from bovine brain. Biochem. Biophys. Res. Commun. 231:698-700.
    • (1997) Biochem. Biophys. Res. Commun. , vol.231 , pp. 698-700
    • Banerjee, A.1
  • 6
    • 57549112904 scopus 로고    scopus 로고
    • An experimental and computational study of effects of microtubule stabilization on T-cell polarity
    • Baratt, A., S. N. Arkhipov, and I. V. Maly. 2008. An experimental and computational study of effects of microtubule stabilization on T-cell polarity. PLoS One 3:e3861.
    • (2008) PLoS One , vol.3
    • Baratt, A.1    Arkhipov, S.N.2    Maly, I.V.3
  • 7
    • 62149083847 scopus 로고    scopus 로고
    • Moesin is required for HIV-1-induced CD4-CXCR4 interaction, F-actin redistribution, membrane fusion and viral infection in lymphocytes
    • Barrero-Villar, M., et al. 2009. Moesin is required for HIV-1-induced CD4-CXCR4 interaction, F-actin redistribution, membrane fusion and viral infection in lymphocytes. J. Cell Sci. 122:103-113.
    • (2009) J. Cell Sci. , vol.122 , pp. 103-113
    • Barrero-Villar, M.1
  • 8
    • 0034681423 scopus 로고    scopus 로고
    • Effects of jasplakinolide on the kinetics of actin polymerization. An explanation for certain in vivo observations
    • Bubb, M. R., I. Spector, B. B. Beyer, and K. M. Fosen. 2000. Effects of jasplakinolide on the kinetics of actin polymerization. An explanation for certain in vivo observations. J. Biol. Chem. 275:5163-5170.
    • (2000) J. Biol. Chem. , vol.275 , pp. 5163-5170
    • Bubb, M.R.1    Spector, I.2    Beyer, B.B.3    Fosen, K.M.4
  • 9
    • 0031775745 scopus 로고    scopus 로고
    • Establishment of a functional human immunodeficiency virus type 1 (HIV-1) reverse transcription complex involves the cytoskeleton
    • Bukrinskaya, A., B. Brichacek, A. Mann, and M. Stevenson. 1998. Establishment of a functional human immunodeficiency virus type 1 (HIV-1) reverse transcription complex involves the cytoskeleton. J. Exp. Med. 188:2113-2125.
    • (1998) J. Exp. Med. , vol.188 , pp. 2113-2125
    • Bukrinskaya, A.1    Brichacek, B.2    Mann, A.3    Stevenson, M.4
  • 10
    • 2442707757 scopus 로고    scopus 로고
    • Disruption of the actin cytoskeleton can complement the ability of Nef to enhance human immunodeficiency virus type 1 infectivity
    • Campbell, E. M., R. Nunez, and T. J. Hope. 2004. Disruption of the actin cytoskeleton can complement the ability of Nef to enhance human immunodeficiency virus type 1 infectivity. J. Virol. 78:5745-5755.
    • (2004) J. Virol. , vol.78 , pp. 5745-5755
    • Campbell, E.M.1    Nunez, R.2    Hope, T.J.3
  • 11
    • 0035088135 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 particles pseudotyped with envelope proteins that fuse at low pH no longer require Nef for optimal infectivity
    • DOI 10.1128/JVI.75.8.4014-4018.2001
    • Chazal, N., G. Singer, C. Aiken, M. L. Hammarskjold, and D. Rekosh. 2001. Human immunodeficiency virus type 1 particles pseudotyped with envelope proteins that fuse at low pH no longer require Nef for optimal infectivity. J. Virol. 75:4014-4018. (Pubitemid 32246414)
    • (2001) Journal of Virology , vol.75 , Issue.8 , pp. 4014-4018
    • Chazal, N.1    Singer, G.2    Aiken, C.3    Hammarskjold, M.-L.4    Rekosh, D.5
  • 12
    • 0027481248 scopus 로고
    • Microtubules are not an essential component of phytohemagglutinin- dependent signal transduction in Jurkat T lymphocytes
    • Dupuis, G., J. Martel, B. Bastin, J. Dion, and M. D. Payet. 1993. Microtubules are not an essential component of phytohemagglutinin-dependent signal transduction in Jurkat T lymphocytes. Cell Immunol. 146:38-51.
    • (1993) Cell Immunol. , vol.146 , pp. 38-51
    • Dupuis, G.1    Martel, J.2    Bastin, B.3    Dion, J.4    Payet, M.D.5
  • 13
    • 0030852135 scopus 로고    scopus 로고
    • Association of human immunodeficiency virus Nef protein with actin is myristoylation dependent and influences its subcellular localization
    • Fackler, O. T., et al. 1997. Association of human immunodeficiency virus Nef protein with actin is myristoylation dependent and influences its subcellular localization. Eur. J. Biochem. 247:843-851.
    • (1997) Eur. J. Biochem. , vol.247 , pp. 843-851
    • Fackler, O.T.1
  • 14
    • 33746292619 scopus 로고    scopus 로고
    • Interactions of human retroviruses with the host cell cytoskeleton
    • Fackler, O. T., and H. G. Krausslich. 2006. Interactions of human retroviruses with the host cell cytoskeleton. Curr. Opin. Microbiol. 9:409-415.
    • (2006) Curr. Opin. Microbiol. , vol.9 , pp. 409-415
    • Fackler, O.T.1    Krausslich, H.G.2
  • 15
    • 0036827862 scopus 로고    scopus 로고
    • Inhibition of endosomal/lysosomal degradation increases the infectivity of human immunodeficiency virus
    • Fredericksen, B. L., B. L. Wei, J. Yao, T. Luo, and J. V. Garcia. 2002. Inhibition of endosomal/lysosomal degradation increases the infectivity of human immunodeficiency virus. J. Virol. 76:11440-11446.
    • (2002) J. Virol. , vol.76 , pp. 11440-11446
    • Fredericksen, B.L.1    Wei, B.L.2    Yao, J.3    Luo, T.4    Garcia, J.V.5
  • 16
    • 0028934998 scopus 로고
    • The large subunit of HIV-1 reverse transcriptase interacts with beta-actin
    • Hottiger, M., et al. 1995. The large subunit of HIV-1 reverse transcriptase interacts with beta-actin. Nucleic Acids Res. 23:736-741.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 736-741
    • Hottiger, M.1
  • 17
    • 0032524614 scopus 로고    scopus 로고
    • Nocodazole inhibits signal transduction by the T cell antigen receptor
    • Huby, R. D., A. Weiss, and S. C. Ley. 1998. Nocodazole inhibits signal transduction by the T cell antigen receptor. J. Biol. Chem. 273:12024-12031.
    • (1998) J. Biol. Chem. , vol.273 , pp. 12024-12031
    • Huby, R.D.1    Weiss, A.2    Ley, S.C.3
  • 18
    • 0031902924 scopus 로고    scopus 로고
    • Actin-dependent receptor colocalization required for human immunodeficiency virus entry into host cells
    • Iyengar, S., J. E. Hildreth, and D. H. Schwartz. 1998. Actin-dependent receptor colocalization required for human immunodeficiency virus entry into host cells. J. Virol. 72:5251-5255.
    • (1998) J. Virol. , vol.72 , pp. 5251-5255
    • Iyengar, S.1    Hildreth, J.E.2    Schwartz, D.H.3
  • 19
    • 34347379258 scopus 로고    scopus 로고
    • Filamin-A regulates actin-dependent clustering of HIV receptors
    • Jimenez-Baranda, S., et al. 2007. Filamin-A regulates actin-dependent clustering of HIV receptors. Nat. Cell Biol. 9:838-846.
    • (2007) Nat. Cell Biol. , vol.9 , pp. 838-846
    • Jimenez-Baranda, S.1
  • 20
    • 34249823098 scopus 로고    scopus 로고
    • Requirement for an intact T-cell actin and tubulin cytoskeleton for efficient assembly and spread of human immunodeficiency virus type 1
    • Jolly, C., I. Mitar, and Q. J. Sattentau. 2007. Requirement for an intact T-cell actin and tubulin cytoskeleton for efficient assembly and spread of human immunodeficiency virus type 1. J. Virol. 81:5547-5560.
    • (2007) J. Virol. , vol.81 , pp. 5547-5560
    • Jolly, C.1    Mitar, I.2    Sattentau, Q.J.3
  • 21
    • 0031610542 scopus 로고    scopus 로고
    • [22] Use of drugs to study role of microtubule assembly dynamics in living cells
    • DOI 10.1016/S0076-6879(98)98024-7
    • Jordan, M. A., and L. Wilson. 1998. Use of drugs to study role of microtubule assembly dynamics in living cells. Methods Enzymol. 298:252-276. (Pubitemid 28450758)
    • (1998) Methods in Enzymology , vol.298 , pp. 252-276
    • Jordan, M.A.1    Wilson, L.2
  • 23
    • 70349240755 scopus 로고    scopus 로고
    • HIV infection of T cells: Actin-in and actin-out
    • Liu, Y., N. V. Belkina, and S. Shaw. 2009. HIV infection of T cells: actin-in and actin-out. Sci. Signal 2:pe23.
    • (2009) Sci. Signal , vol.2
    • Liu, Y.1    Belkina, N.V.2    Shaw, S.3
  • 24
    • 0030008570 scopus 로고    scopus 로고
    • Interaction of vinca alkaloids with tubulin: A comparison of vinblastine, vincristine, and vinorelbine
    • Lobert, S., B. Vulevic, and J. J. Correia. 1996. Interaction of vinca alkaloids with tubulin: a comparison of vinblastine, vincristine, and vinorelbine. Biochemistry 35:6806-6814.
    • (1996) Biochemistry , vol.35 , pp. 6806-6814
    • Lobert, S.1    Vulevic, B.2    Correia, J.J.3
  • 26
    • 0025976944 scopus 로고
    • Tubulin sulfhydryl groups as probes and targets for antimitotic and antimicrotubule agents
    • Luduena, R. F., and M. C. Roach. 1991. Tubulin sulfhydryl groups as probes and targets for antimitotic and antimicrotubule agents. Pharmacol. Ther. 49:133-152.
    • (1991) Pharmacol. Ther. , vol.49 , pp. 133-152
    • Luduena, R.F.1    Roach, M.C.2
  • 28
    • 34548021883 scopus 로고    scopus 로고
    • Retroviral proteins that interact with the host cell cytoskeleton
    • Naghavi, M. H., and S. P. Goff. 2007. Retroviral proteins that interact with the host cell cytoskeleton. Curr. Opin. Immunol. 19:402-407.
    • (2007) Curr. Opin. Immunol. , vol.19 , pp. 402-407
    • Naghavi, M.H.1    Goff, S.P.2
  • 30
    • 0027496255 scopus 로고
    • Myristoylation-enhanced binding of the HIV-1 Nef protein to T cell skeletal matrix
    • Niederman, T. M., W. R. Hastings, and L. Ratner. 1993. Myristoylation-enhanced binding of the HIV-1 Nef protein to T cell skeletal matrix. Virology 197:420-425.
    • (1993) Virology , vol.197 , pp. 420-425
    • Niederman, T.M.1    Hastings, W.R.2    Ratner, L.3
  • 31
    • 77954980510 scopus 로고    scopus 로고
    • Actin-based motility drives baculovirus transit to the nucleus and cell surface
    • Ohkawa, T., L. E. Volkman, and M. D. Welch. 2010. Actin-based motility drives baculovirus transit to the nucleus and cell surface. J. Cell Biol. 190:187-195.
    • (2010) J. Cell Biol. , vol.190 , pp. 187-195
    • Ohkawa, T.1    Volkman, L.E.2    Welch, M.D.3
  • 32
    • 0035144435 scopus 로고    scopus 로고
    • Viral transport and the cytoskeleton
    • Ploubidou, A., and M. Way. 2001. Viral transport and the cytoskeleton. Curr. Opin. Cell Biol. 13:97-105.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 97-105
    • Ploubidou, A.1    Way, M.2
  • 33
    • 2942635074 scopus 로고    scopus 로고
    • Actin cytoskeletal reorganizations and coreceptor-mediated activation of Rac during human immunodeficiency virus-induced cell fusion
    • DOI 10.1128/JVI.78.13.7138-7147.2004
    • Pontow, S. E., N. V. Heyden, S. Wei, and L. Ratner. 2004. Actin cytoskeletal reorganizations and coreceptor-mediated activation of Rac during human immunodeficiency virus-induced cell fusion. J. Virol. 78:7138-7147. (Pubitemid 38781552)
    • (2004) Journal of Virology , vol.78 , Issue.13 , pp. 7138-7147
    • Pontow, S.E.1    Heyden, N.V.2    Wei, S.3    Ratner, L.4
  • 34
    • 0032516066 scopus 로고    scopus 로고
    • The C terminus of beta-tubulin regulates vinblastine-induced tubulin polymerization
    • Rai, S. S., and J. Wolff. 1998. The C terminus of beta-tubulin regulates vinblastine-induced tubulin polymerization. Proc. Natl. Acad. Sci. U. S. A. 95:4253-4257.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 4253-4257
    • Rai, S.S.1    Wolff, J.2
  • 35
    • 0029941433 scopus 로고    scopus 로고
    • HIV-1 Gag protein associates with F-actin present in microfilaments
    • DOI 10.1006/viro.1996.0343
    • Rey, O., J. Canon, and P. Krogstad. 1996. HIV-1 Gag protein associates with F-actin present in microfilaments. Virology 220:530-534. (Pubitemid 26202362)
    • (1996) Virology , vol.220 , Issue.2 , pp. 530-534
    • Rey, O.1    Canon, J.2    Krogstad, P.3
  • 36
    • 0018387446 scopus 로고
    • Promotion of microtubule assembly in vitro by taxol
    • Schiff, P. B., J. Fant, and S. B. Horwitz. 1979. Promotion of microtubule assembly in vitro by taxol. Nature 277:665-667.
    • (1979) Nature , vol.277 , pp. 665-667
    • Schiff, P.B.1    Fant, J.2    Horwitz, S.B.3
  • 37
    • 68549123450 scopus 로고    scopus 로고
    • HIV-1 Nef interferes with host cell motility by deregulation of Cofilin
    • Stolp, B., et al. 2009. HIV-1 Nef interferes with host cell motility by deregulation of Cofilin. Cell Host Microbe 6:174-186.
    • (2009) Cell Host Microbe , vol.6 , pp. 174-186
    • Stolp, B.1
  • 38
    • 33847139800 scopus 로고    scopus 로고
    • The road to chromatin - Nuclear entry of retroviruses
    • Suzuki, Y., and R. Craigie. 2007. The road to chromatin - nuclear entry of retroviruses. Nat. Rev. Microbiol. 5:187-196.
    • (2007) Nat. Rev. Microbiol. , vol.5 , pp. 187-196
    • Suzuki, Y.1    Craigie, R.2
  • 39
    • 0029122108 scopus 로고
    • RAW264 macrophages stably transfected with an HIV-1 LTR reporter gene provide a sensitive bioassay for analysis of signalling pathways in macrophages stimulated with lipopolysaccharide, TNF-alpha or taxol
    • Sweet, M. J., and D. A. Hume. 1995. RAW264 macrophages stably transfected with an HIV-1 LTR reporter gene provide a sensitive bioassay for analysis of signalling pathways in macrophages stimulated with lipopolysaccharide, TNF-alpha or taxol. J. Inflamm. 45:126-135.
    • (1995) J. Inflamm. , vol.45 , pp. 126-135
    • Sweet, M.J.1    Hume, D.A.2
  • 40
    • 8644231282 scopus 로고    scopus 로고
    • Human cell proteins and human immunodeficiency virus DNA integration
    • Turlure, F., E. Devroe, P. A. Silver, and A. Engelman. 2004. Human cell proteins and human immunodeficiency virus DNA integration. Front. Biosci. 9:3187-3208.
    • (2004) Front. Biosci. , vol.9 , pp. 3187-3208
    • Turlure, F.1    Devroe, E.2    Silver, P.A.3    Engelman, A.4
  • 42
    • 0015211527 scopus 로고
    • Plant antitumor agents. VI. The isolation and structure of taxol, a novel antileukemic and antitumor agent from Taxus brevifolia
    • Wani, M. C., H. L. Taylor, M. E. Wall, P. Coggon, and A. T. McPhail. 1971. Plant antitumor agents. VI. The isolation and structure of taxol, a novel antileukemic and antitumor agent from Taxus brevifolia. J. Am. Chem. Soc. 93:2325-2327.
    • (1971) J. Am. Chem. Soc. , vol.93 , pp. 2325-2327
    • Wani, M.C.1    Taylor, H.L.2    Wall, M.E.3    Coggon, P.4    McPhail, A.T.5
  • 43
    • 0032982141 scopus 로고    scopus 로고
    • Actin associates with the nucleocapsid domain of the human immunodeficiency virus Gag polyprotein
    • Wilk, T., B. Gowen, and S. D. Fuller. 1999. Actin associates with the nucleocapsid domain of the human immunodeficiency virus Gag polyprotein. J. Virol. 73:1931-1940.
    • (1999) J. Virol. , vol.73 , pp. 1931-1940
    • Wilk, T.1    Gowen, B.2    Fuller, S.D.3
  • 44
    • 0019977155 scopus 로고
    • Interaction of vinblastine with steady-state microtubules in vitro
    • Wilson, L., M. A. Jordan, A. Morse, and R. L. Margolis. 1982. Interaction of vinblastine with steady-state microtubules in vitro. J. Mol. Biol. 159:125-149.
    • (1982) J. Mol. Biol. , vol.159 , pp. 125-149
    • Wilson, L.1    Jordan, M.A.2    Morse, A.3    Margolis, R.L.4
  • 45
    • 34447259569 scopus 로고    scopus 로고
    • Rev-dependent indicator T cell line
    • Wu, Y., M. H. Beddall, and J. W. Marsh. 2007. Rev-dependent indicator T cell line. Curr. HIV Res. 5:395-402.
    • (2007) Curr. HIV Res. , vol.5 , pp. 395-402
    • Wu, Y.1    Beddall, M.H.2    Marsh, J.W.3
  • 46
    • 0035943355 scopus 로고    scopus 로고
    • Selective transcription and modulation of resting T cell activity by preintegrated HIV DNA
    • Wu, Y., and J. W. Marsh. 2001. Selective transcription and modulation of resting T cell activity by preintegrated HIV DNA. Science 293:1503-1506.
    • (2001) Science , vol.293 , pp. 1503-1506
    • Wu, Y.1    Marsh, J.W.2
  • 47
    • 74549178998 scopus 로고    scopus 로고
    • Chemokine coreceptor signaling in HIV-1 infection and pathogenesis
    • Wu, Y., and A. Yoder. 2009. Chemokine coreceptor signaling in HIV-1 infection and pathogenesis. PLoS Pathog. 5:e1000520.
    • (2009) PLoS Pathog , vol.5
    • Wu, Y.1    Yoder, A.2
  • 48
    • 50249107532 scopus 로고    scopus 로고
    • HIV envelope-CXCR4 signaling activates cofilin to overcome cortical actin restriction in resting CD4 T cells
    • Yoder, A., et al. 2008. HIV envelope-CXCR4 signaling activates cofilin to overcome cortical actin restriction in resting CD4 T cells. Cell 134:782-792.
    • (2008) Cell , vol.134 , pp. 782-792
    • Yoder, A.1
  • 49
    • 73449090496 scopus 로고    scopus 로고
    • The HIV envelope but not VSV glycoprotein is capable of mediating HIV latent infection of resting CD4 T cells
    • Yu, D., W. Wang, A. Yoder, M. Spear, and Y. Wu. 2009. The HIV envelope but not VSV glycoprotein is capable of mediating HIV latent infection of resting CD4 T cells. PLoS Pathog. 5:e1000633.
    • (2009) PLoS Pathog. , vol.5
    • Yu, D.1    Wang, W.2    Yoder, A.3    Spear, M.4    Wu, Y.5
  • 50
    • 35348869756 scopus 로고    scopus 로고
    • Centrosomal pre-integration latency of HIV-1 in quiescent cells
    • Zamborlini, A., et al. 2007. Centrosomal pre-integration latency of HIV-1 in quiescent cells. Retrovirology 4:63.
    • (2007) Retrovirology , vol.4 , pp. 63
    • Zamborlini, A.1


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