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Volumn 87, Issue 2, 2010, Pages 187-194

Inhibition of heat-shock protein 90 reduces Ebola virus replication

Author keywords

Ebola virus; Hsp90; Therapeutic

Indexed keywords

GELDANAMYCIN; RADICICOL; TANESPIMYCIN; ANTIVIRUS AGENT; BENZOQUINONE DERIVATIVE; ENZYME INHIBITOR; HEAT SHOCK PROTEIN 90; MACROCYCLIC LACTAM; MACROLIDE; VIRUS RNA;

EID: 77954951982     PISSN: 01663542     EISSN: 18729096     Source Type: Journal    
DOI: 10.1016/j.antiviral.2010.04.015     Document Type: Article
Times cited : (100)

References (39)
  • 1
    • 58849160500 scopus 로고    scopus 로고
    • Heat shock protein 90 as a drug target: some like it hot
    • Banerji U. Heat shock protein 90 as a drug target: some like it hot. Clin. Cancer Res. 2009, 15(1):9-14.
    • (2009) Clin. Cancer Res. , vol.15 , Issue.1 , pp. 9-14
    • Banerji, U.1
  • 3
    • 23244444185 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 DNA polymerase requires the mammalian chaperone hsp90 for proper localization to the nucleus
    • Burch A.D., Weller S.K. Herpes simplex virus type 1 DNA polymerase requires the mammalian chaperone hsp90 for proper localization to the nucleus. J. Virol. 2005, 79(16):10740-10749.
    • (2005) J. Virol. , vol.79 , Issue.16 , pp. 10740-10749
    • Burch, A.D.1    Weller, S.K.2
  • 5
    • 10044237881 scopus 로고    scopus 로고
    • Design, synthesis, and evaluation of a radicicol and geldanamycin chimera, radamide
    • Clevenger R.C., Blagg B.S. Design, synthesis, and evaluation of a radicicol and geldanamycin chimera, radamide. Org. Lett. 2004, 6(24):4459-4462.
    • (2004) Org. Lett. , vol.6 , Issue.24 , pp. 4459-4462
    • Clevenger, R.C.1    Blagg, B.S.2
  • 6
    • 34247191488 scopus 로고    scopus 로고
    • Antiviral activity and RNA polymerase degradation following Hsp90 inhibition in a range of negative strand viruses
    • Connor J.H., McKenzie M.O., Parks G.D., Lyles D.S. Antiviral activity and RNA polymerase degradation following Hsp90 inhibition in a range of negative strand viruses. Virology 2007, 362(1):109-119.
    • (2007) Virology , vol.362 , Issue.1 , pp. 109-119
    • Connor, J.H.1    McKenzie, M.O.2    Parks, G.D.3    Lyles, D.S.4
  • 7
    • 0032539680 scopus 로고    scopus 로고
    • RNA polymerase of vesicular stomatitis virus specifically associates with translation elongation factor-1 alphabetagamma for its activity
    • Das T., Mathur M., Gupta A.K., Janssen G.M., Banerjee A.K. RNA polymerase of vesicular stomatitis virus specifically associates with translation elongation factor-1 alphabetagamma for its activity. Proc. Natl. Acad. Sci. U.S.A. 1998, 95(4):1449-1454.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , Issue.4 , pp. 1449-1454
    • Das, T.1    Mathur, M.2    Gupta, A.K.3    Janssen, G.M.4    Banerjee, A.K.5
  • 8
    • 0001251439 scopus 로고
    • A new antifungal substance of fungal origin
    • Delmotte P., Delmotte-Plaque J. A new antifungal substance of fungal origin. Nature 1953, 171(4347):344.
    • (1953) Nature , vol.171 , Issue.4347 , pp. 344
    • Delmotte, P.1    Delmotte-Plaque, J.2
  • 10
    • 33846471075 scopus 로고    scopus 로고
    • Evolutionary constraints on chaperone-mediated folding provide an antiviral approach refractory to development of drug resistance
    • Geller R., Vignuzzi M., Andino R., Frydman J. Evolutionary constraints on chaperone-mediated folding provide an antiviral approach refractory to development of drug resistance. Genes Dev. 2007, 21(2):195-205.
    • (2007) Genes Dev. , vol.21 , Issue.2 , pp. 195-205
    • Geller, R.1    Vignuzzi, M.2    Andino, R.3    Frydman, J.4
  • 12
    • 0037213625 scopus 로고    scopus 로고
    • Identification of a novel tripartite complex involved in replication of vesicular stomatitis virus genome RNA
    • Gupta A.K., Shaji D., Banerjee A.K. Identification of a novel tripartite complex involved in replication of vesicular stomatitis virus genome RNA. J. Virol. 2003, 77(1):732-738.
    • (2003) J. Virol. , vol.77 , Issue.1 , pp. 732-738
    • Gupta, A.K.1    Shaji, D.2    Banerjee, A.K.3
  • 13
    • 8644249753 scopus 로고    scopus 로고
    • Requirement of heat shock protein 90 for human hepatitis B virus reverse transcriptase function
    • Hu J., Flores D., Toft D., Wang X., Nguyen D. Requirement of heat shock protein 90 for human hepatitis B virus reverse transcriptase function. J. Virol. 2004, 78(23):13122-13131.
    • (2004) J. Virol. , vol.78 , Issue.23 , pp. 13122-13131
    • Hu, J.1    Flores, D.2    Toft, D.3    Wang, X.4    Nguyen, D.5
  • 14
    • 0030035038 scopus 로고    scopus 로고
    • Hsp90 is required for the activity of a hepatitis B virus reverse transcriptase
    • Hu J., Seeger C. Hsp90 is required for the activity of a hepatitis B virus reverse transcriptase. Proc. Natl. Acad. Sci. U.S.A. 1996, 93(3):1060-1064.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , Issue.3 , pp. 1060-1064
    • Hu, J.1    Seeger, C.2
  • 15
    • 0031018112 scopus 로고    scopus 로고
    • Hepadnavirus assembly and reverse transcription require a multi-component chaperone complex which is incorporated into nucleocapsids
    • Hu J., Toft D.O., Seeger C. Hepadnavirus assembly and reverse transcription require a multi-component chaperone complex which is incorporated into nucleocapsids. EMBO J. 1997, 16(1):59-68.
    • (1997) EMBO J. , vol.16 , Issue.1 , pp. 59-68
    • Hu, J.1    Toft, D.O.2    Seeger, C.3
  • 17
    • 0036149214 scopus 로고    scopus 로고
    • Molecular chaperone Hsp90 is important for vaccinia virus growth in cells
    • Hung J.J., Chung C.S., Chang W. Molecular chaperone Hsp90 is important for vaccinia virus growth in cells. J. Virol. 2002, 76(3):1379-1390.
    • (2002) J. Virol. , vol.76 , Issue.3 , pp. 1379-1390
    • Hung, J.J.1    Chung, C.S.2    Chang, W.3
  • 18
    • 0017772897 scopus 로고
    • Isolation and partial characterisation of a new virus causing acute haemorrhagic fever in Zaire
    • Johnson K.M., Lange J.V., Webb P.A., Murphy F.A. Isolation and partial characterisation of a new virus causing acute haemorrhagic fever in Zaire. Lancet 1977, 1(8011):569-571.
    • (1977) Lancet , vol.1 , Issue.8011 , pp. 569-571
    • Johnson, K.M.1    Lange, J.V.2    Webb, P.A.3    Murphy, F.A.4
  • 19
    • 18744384675 scopus 로고    scopus 로고
    • The cellular chaperone heat shock protein 90 facilitates Flock House virus RNA replication in Drosophila cells
    • Kampmueller K.M., Miller D.J. The cellular chaperone heat shock protein 90 facilitates Flock House virus RNA replication in Drosophila cells. J. Virol. 2005, 79(11):6827-6837.
    • (2005) J. Virol. , vol.79 , Issue.11 , pp. 6827-6837
    • Kampmueller, K.M.1    Miller, D.J.2
  • 20
    • 1442349120 scopus 로고    scopus 로고
    • Geldanamycin, a ligand of heat shock protein 90, inhibits the replication of herpes simplex virus type 1 in vitro
    • Li Y.H., Tao P.Z., Liu Y.Z., Jiang J.D. Geldanamycin, a ligand of heat shock protein 90, inhibits the replication of herpes simplex virus type 1 in vitro. Antimicrob. Agents Chemother. 2004, 48(3):867-872.
    • (2004) Antimicrob. Agents Chemother. , vol.48 , Issue.3 , pp. 867-872
    • Li, Y.H.1    Tao, P.Z.2    Liu, Y.Z.3    Jiang, J.D.4
  • 21
    • 0346003805 scopus 로고    scopus 로고
    • Identification of Hsp90 as a stimulatory host factor involved in influenza virus RNA synthesis
    • Momose F., Naito T., Yano K., Sugimoto S., Morikawa Y., Nagata K. Identification of Hsp90 as a stimulatory host factor involved in influenza virus RNA synthesis. J. Biol. Chem. 2002, 277(47):45306-45314.
    • (2002) J. Biol. Chem. , vol.277 , Issue.47 , pp. 45306-45314
    • Momose, F.1    Naito, T.2    Yano, K.3    Sugimoto, S.4    Morikawa, Y.5    Nagata, K.6
  • 22
    • 33846491250 scopus 로고    scopus 로고
    • Involvement of Hsp90 in assembly and nuclear import of influenza virus RNA polymerase subunits
    • Naito T., Momose F., Kawaguchi A., Nagata K. Involvement of Hsp90 in assembly and nuclear import of influenza virus RNA polymerase subunits. J. Virol. 2007, 81(3):1339-1349.
    • (2007) J. Virol. , vol.81 , Issue.3 , pp. 1339-1349
    • Naito, T.1    Momose, F.2    Kawaguchi, A.3    Nagata, K.4
  • 24
    • 33746364784 scopus 로고    scopus 로고
    • Structure and mechanism of the Hsp90 molecular chaperone machinery
    • Pearl L.H., Prodromou C. Structure and mechanism of the Hsp90 molecular chaperone machinery. Annu. Rev. Biochem. 2006, 75:271-294.
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 271-294
    • Pearl, L.H.1    Prodromou, C.2
  • 25
    • 0037315208 scopus 로고    scopus 로고
    • Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery
    • Pratt W.B., Toft D.O. Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery. Exp. Biol. Med. (Maywood) 2003, 228(2):111-133.
    • (2003) Exp. Biol. Med. (Maywood) , vol.228 , Issue.2 , pp. 111-133
    • Pratt, W.B.1    Toft, D.O.2
  • 28
    • 0034892432 scopus 로고    scopus 로고
    • Hsp90: chaperoning signal transduction
    • Richter K., Buchner J. Hsp90: chaperoning signal transduction. J. Cell. Physiol. 2001, 188(3):281-290.
    • (2001) J. Cell. Physiol. , vol.188 , Issue.3 , pp. 281-290
    • Richter, K.1    Buchner, J.2
  • 29
  • 30
    • 0035957016 scopus 로고    scopus 로고
    • Evaluation of the role of heterogeneous nuclear ribonucleoprotein A1 as a host factor in murine coronavirus discontinuous transcription and genome replication
    • Shen X., Masters P.S. Evaluation of the role of heterogeneous nuclear ribonucleoprotein A1 as a host factor in murine coronavirus discontinuous transcription and genome replication. Proc. Natl. Acad. Sci. U.S.A. 2001, 98(5):2717-2722.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , Issue.5 , pp. 2717-2722
    • Shen, X.1    Masters, P.S.2
  • 31
    • 35548994976 scopus 로고    scopus 로고
    • Chaperone activation of the hepadnaviral reverse transcriptase for template RNA binding is established by the Hsp70 and stimulated by the Hsp90 system
    • Stahl M., Retzlaff M., Nassal M., Beck J. Chaperone activation of the hepadnaviral reverse transcriptase for template RNA binding is established by the Hsp70 and stimulated by the Hsp90 system. Nucleic Acids Res. 2007, 35(18):6124-6136.
    • (2007) Nucleic Acids Res. , vol.35 , Issue.18 , pp. 6124-6136
    • Stahl, M.1    Retzlaff, M.2    Nassal, M.3    Beck, J.4
  • 32
    • 0033524523 scopus 로고    scopus 로고
    • Viral RNA replication. With a little help from the host
    • Strauss J.H., Strauss E.G. Viral RNA replication. With a little help from the host. Science 1999, 283(5403):802-804.
    • (1999) Science , vol.283 , Issue.5403 , pp. 802-804
    • Strauss, J.H.1    Strauss, E.G.2
  • 33
    • 62149135294 scopus 로고    scopus 로고
    • Discovery and development of heat shock protein 90 inhibitors
    • Taldone T., Sun W., Chiosis G. Discovery and development of heat shock protein 90 inhibitors. Bioorg. Med. Chem. 2009, 17(6):2225-2235.
    • (2009) Bioorg. Med. Chem. , vol.17 , Issue.6 , pp. 2225-2235
    • Taldone, T.1    Sun, W.2    Chiosis, G.3
  • 34
    • 12344297305 scopus 로고    scopus 로고
    • Generation of eGFP expressing recombinant Zaire ebolavirus for analysis of early pathogenesis events and high-throughput antiviral drug screening
    • Towner J.S., Paragas J., Dover J.E., Gupta M., Goldsmith C.S., Huggins J.W., Nichol S.T. Generation of eGFP expressing recombinant Zaire ebolavirus for analysis of early pathogenesis events and high-throughput antiviral drug screening. Virology 2005, 332(1):20-27.
    • (2005) Virology , vol.332 , Issue.1 , pp. 20-27
    • Towner, J.S.1    Paragas, J.2    Dover, J.E.3    Gupta, M.4    Goldsmith, C.S.5    Huggins, J.W.6    Nichol, S.T.7
  • 35
    • 65449118855 scopus 로고    scopus 로고
    • Heat-shock protein 90 is essential for stabilization of the hepatitis C virus nonstructural protein NS3
    • Ujino S., Yamaguchi S., Shimotohno K., Takaku H. Heat-shock protein 90 is essential for stabilization of the hepatitis C virus nonstructural protein NS3. J. Biol. Chem. 2009, 284(11):6841-6846.
    • (2009) J. Biol. Chem. , vol.284 , Issue.11 , pp. 6841-6846
    • Ujino, S.1    Yamaguchi, S.2    Shimotohno, K.3    Takaku, H.4
  • 38
    • 2442666665 scopus 로고    scopus 로고
    • Transcription and replication of nonsegmented negative-strand RNA viruses
    • Whelan S.P., Barr J.N., Wertz G.W. Transcription and replication of nonsegmented negative-strand RNA viruses. Curr. Top. Microbiol. Immunol. 2004, 283:61-119.
    • (2004) Curr. Top. Microbiol. Immunol. , vol.283 , pp. 61-119
    • Whelan, S.P.1    Barr, J.N.2    Wertz, G.W.3
  • 39
    • 25844519550 scopus 로고    scopus 로고
    • HSP90 and the chaperoning of cancer
    • Whitesell L., Lindquist S.L. HSP90 and the chaperoning of cancer. Nat. Rev. Cancer 2005, 5(10):761-772.
    • (2005) Nat. Rev. Cancer , vol.5 , Issue.10 , pp. 761-772
    • Whitesell, L.1    Lindquist, S.L.2


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