메뉴 건너뛰기




Volumn 19, Issue 1, 2005, Pages 111-122

Cyclophilin B is a functional regulator of hepatitis C virus RNA polymerase

Author keywords

[No Author keywords available]

Indexed keywords

CYCLOPHILIN B; RNA POLYMERASE; VIRUS RNA;

EID: 21244433445     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2005.05.014     Document Type: Article
Times cited : (400)

References (48)
  • 1
    • 2942715265 scopus 로고    scopus 로고
    • Characterization of the hepatitis C virus RNA replication complex associated with lipid rafts
    • H. Aizaki, K.J. Lee, V.M. Sung, H. Ishiko, and M.M. Lai Characterization of the hepatitis C virus RNA replication complex associated with lipid rafts Virology 324 2004 450 461
    • (2004) Virology , vol.324 , pp. 450-461
    • Aizaki, H.1    Lee, K.J.2    Sung, V.M.3    Ishiko, H.4    Lai, M.M.5
  • 2
    • 0034877411 scopus 로고    scopus 로고
    • Novel cell culture systems for the hepatitis C virus
    • R. Bartenschlager, and V. Lohmann Novel cell culture systems for the hepatitis C virus Antiviral Res. 52 2001 1 17
    • (2001) Antiviral Res. , vol.52 , pp. 1-17
    • Bartenschlager, R.1    Lohmann, V.2
  • 3
    • 0028965266 scopus 로고
    • Mode of action of SDZ NIM 811, a nonimmunosuppressive cyclosporin a analog with activity against human immunodeficiency virus (HIV) type 1: Interference with HIV protein-cyclophilin a interactions
    • A. Billich, F. Hammerschmid, P. Peichl, R. Wenger, G. Zenke, V. Quesniaux, and B. Rosenwirth Mode of action of SDZ NIM 811, a nonimmunosuppressive cyclosporin A analog with activity against human immunodeficiency virus (HIV) type 1: interference with HIV protein-cyclophilin A interactions J. Virol. 69 1995 2451 2461
    • (1995) J. Virol. , vol.69 , pp. 2451-2461
    • Billich, A.1    Hammerschmid, F.2    Peichl, P.3    Wenger, R.4    Zenke, G.5    Quesniaux, V.6    Rosenwirth, B.7
  • 4
    • 0035869011 scopus 로고    scopus 로고
    • Cyclophilin a regulates HIV-1 infectivity, as demonstrated by gene targeting in human T cells
    • D. Braaten, and J. Luban Cyclophilin A regulates HIV-1 infectivity, as demonstrated by gene targeting in human T cells EMBO J. 20 2001 1300 1309
    • (2001) EMBO J. , vol.20 , pp. 1300-1309
    • Braaten, D.1    Luban, J.2
  • 5
    • 0027323876 scopus 로고
    • Identification of the immunophilins capable of mediating inhibition of signal transduction by cyclosporin a and FK506: Roles of calcineurin binding and cellular location
    • R.J. Bram, D.T. Hung, P.K. Martin, S.L. Schreiber, and G.R. Crabtree Identification of the immunophilins capable of mediating inhibition of signal transduction by cyclosporin A and FK506: roles of calcineurin binding and cellular location Mol. Cell. Biol. 13 1993 4760 4769
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 4760-4769
    • Bram, R.J.1    Hung, D.T.2    Martin, P.K.3    Schreiber, S.L.4    Crabtree, G.R.5
  • 6
    • 0037133154 scopus 로고    scopus 로고
    • Regulation of the tyrosine kinase Itk by the peptidyl-prolyl isomerase cyclophilin a
    • K.N. Brazin, R.J. Mallis, D.B. Fulton, and A.H. Andreotti Regulation of the tyrosine kinase Itk by the peptidyl-prolyl isomerase cyclophilin A Proc. Natl. Acad. Sci. USA 99 2002 1899 1904
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 1899-1904
    • Brazin, K.N.1    Mallis, R.J.2    Fulton, D.B.3    Andreotti, A.H.4
  • 7
    • 4143074548 scopus 로고    scopus 로고
    • Cyclophilin a regulates TCR signal strength in CD4+ T cells via a proline-directed conformational switch in Itk
    • J. Colgan, M. Asmal, M. Neagu, B. Yu, J. Schneidkraut, Y. Lee, E. Sokolskaja, A. Andreotti, and J. Luban Cyclophilin A regulates TCR signal strength in CD4+ T cells via a proline-directed conformational switch in Itk Immunity 21 2004 189 201
    • (2004) Immunity , vol.21 , pp. 189-201
    • Colgan, J.1    Asmal, M.2    Neagu, M.3    Yu, B.4    Schneidkraut, J.5    Lee, Y.6    Sokolskaja, E.7    Andreotti, A.8    Luban, J.9
  • 8
    • 0029807530 scopus 로고    scopus 로고
    • A cyclophilin function in Hsp90-dependent signal transduction
    • A.A. Duina, H.C. Chang, J.A. Marsh, S. Lindquist, and R.F. Gaber A cyclophilin function in Hsp90-dependent signal transduction Science 274 1996 1713 1715
    • (1996) Science , vol.274 , pp. 1713-1715
    • Duina, A.A.1    Chang, H.C.2    Marsh, J.A.3    Lindquist, S.4    Gaber, R.F.5
  • 9
    • 0036100578 scopus 로고    scopus 로고
    • Expression of hepatitis C virus proteins induces distinct membrane alterations including a candidate viral replication complex
    • D. Egger, B. Wolk, R. Gosert, L. Bianchi, H.E. Blum, D. Moradpour, and K. Bienz Expression of hepatitis C virus proteins induces distinct membrane alterations including a candidate viral replication complex J. Virol. 76 2002 5974 5984
    • (2002) J. Virol. , vol.76 , pp. 5974-5984
    • Egger, D.1    Wolk, B.2    Gosert, R.3    Bianchi, L.4    Blum, H.E.5    Moradpour, D.6    Bienz, K.7
  • 10
    • 0141507081 scopus 로고    scopus 로고
    • Replication of hepatitis C virus RNA occurs in a membrane-bound replication complex containing nonstructural viral proteins and RNA
    • N. El-Hage, and G. Luo Replication of hepatitis C virus RNA occurs in a membrane-bound replication complex containing nonstructural viral proteins and RNA J. Gen. Virol. 84 2003 2761 2769
    • (2003) J. Gen. Virol. , vol.84 , pp. 2761-2769
    • El-Hage, N.1    Luo, G.2
  • 11
    • 0032502955 scopus 로고    scopus 로고
    • The mode of action of peptidyl prolyl cis/trans isomerases in vivo: Binding vs. catalysis
    • G. Fischer, T. Tradler, and T. Zarnt The mode of action of peptidyl prolyl cis/trans isomerases in vivo: binding vs. catalysis FEBS Lett. 426 1998 17 20
    • (1998) FEBS Lett. , vol.426 , pp. 17-20
    • Fischer, G.1    Tradler, T.2    Zarnt, T.3
  • 12
    • 0027940713 scopus 로고
    • Specific incorporation of cyclophilin a into HIV-1 virions
    • E.K. Franke, H.E. Yuan, and J. Luban Specific incorporation of cyclophilin A into HIV-1 virions Nature 372 1994 359 362
    • (1994) Nature , vol.372 , pp. 359-362
    • Franke, E.K.1    Yuan, H.E.2    Luban, J.3
  • 13
    • 0036327097 scopus 로고    scopus 로고
    • Nuclear DNA helicase II is recruited to IFN-alpha-activated transcription sites at PML nuclear bodies
    • B. Fuchsova, P. Novak, J. Kafkova, and P. Hozak Nuclear DNA helicase II is recruited to IFN-alpha-activated transcription sites at PML nuclear bodies J. Cell Biol. 158 2002 463 473
    • (2002) J. Cell Biol. , vol.158 , pp. 463-473
    • Fuchsova, B.1    Novak, P.2    Kafkova, J.3    Hozak, P.4
  • 14
    • 1842457783 scopus 로고    scopus 로고
    • Interactions between viral nonstructural proteins and host protein hVAP-33 mediate the formation of hepatitis C virus RNA replication complex on lipid raft
    • L. Gao, H. Aizaki, J.W. He, and M.M. Lai Interactions between viral nonstructural proteins and host protein hVAP-33 mediate the formation of hepatitis C virus RNA replication complex on lipid raft J. Virol. 78 2004 3480 3488
    • (2004) J. Virol. , vol.78 , pp. 3480-3488
    • Gao, L.1    Aizaki, H.2    He, J.W.3    Lai, M.M.4
  • 15
    • 0345144016 scopus 로고    scopus 로고
    • Identification of the hepatitis C virus RNA replication complex in Huh-7 cells harboring subgenomic replicons
    • R. Gosert, D. Egger, V. Lohmann, R. Bartenschlager, H.E. Blum, K. Bienz, and D. Moradpour Identification of the hepatitis C virus RNA replication complex in Huh-7 cells harboring subgenomic replicons J. Virol. 77 2003 5487 5492
    • (2003) J. Virol. , vol.77 , pp. 5487-5492
    • Gosert, R.1    Egger, D.2    Lohmann, V.3    Bartenschlager, R.4    Blum, H.E.5    Bienz, K.6    Moradpour, D.7
  • 16
    • 0027476809 scopus 로고
    • Expression and identification of hepatitis C virus polyprotein cleavage products
    • A. Grakoui, C. Wychowski, C. Lin, S.M. Feinstone, and C.M. Rice Expression and identification of hepatitis C virus polyprotein cleavage products J. Virol. 67 1993 1385 1395
    • (1993) J. Virol. , vol.67 , pp. 1385-1395
    • Grakoui, A.1    Wychowski, C.2    Lin, C.3    Feinstone, S.M.4    Rice, C.M.5
  • 18
    • 0032898362 scopus 로고    scopus 로고
    • Expression of hepatitis C virus NS5B protein: Characterization of its RNA polymerase activity and RNA binding
    • K. Ishii, Y. Tanaka, C.C. Yap, H. Aizaki, Y. Matsuura, and T. Miyamura Expression of hepatitis C virus NS5B protein: characterization of its RNA polymerase activity and RNA binding Hepatology 29 1999 1227 1235
    • (1999) Hepatology , vol.29 , pp. 1227-1235
    • Ishii, K.1    Tanaka, Y.2    Yap, C.C.3    Aizaki, H.4    Matsuura, Y.5    Miyamura, T.6
  • 19
    • 4644328613 scopus 로고    scopus 로고
    • Cis-acting RNA signals in the NS5B C-terminal coding sequence of the hepatitis C virus genome
    • H. Lee, H. Shin, E. Wimmer, and A.V. Paul cis-acting RNA signals in the NS5B C-terminal coding sequence of the hepatitis C virus genome J. Virol. 78 2004 10865 10877
    • (2004) J. Virol. , vol.78 , pp. 10865-10877
    • Lee, H.1    Shin, H.2    Wimmer, E.3    Paul, A.V.4
  • 21
    • 1842289764 scopus 로고    scopus 로고
    • Biochemical properties of hepatitis C virus NS5B RNA-dependent RNA polymerase and identification of amino acid sequence motifs essential for enzymatic activity
    • V. Lohmann, F. Korner, U. Herian, and R. Bartenschlager Biochemical properties of hepatitis C virus NS5B RNA-dependent RNA polymerase and identification of amino acid sequence motifs essential for enzymatic activity J. Virol. 71 1997 8416 8428
    • (1997) J. Virol. , vol.71 , pp. 8416-8428
    • Lohmann, V.1    Korner, F.2    Herian, U.3    Bartenschlager, R.4
  • 23
    • 0037057583 scopus 로고    scopus 로고
    • Cyclosporins: Structure-activity relationships for the inhibition of the human MDR1 P-glycoprotein ABC transporter
    • F. Loor, F. Tiberghien, T. Wenandy, A. Didier, and R. Traber Cyclosporins: structure-activity relationships for the inhibition of the human MDR1 P-glycoprotein ABC transporter J. Med. Chem. 45 2002 4598 4612
    • (2002) J. Med. Chem. , vol.45 , pp. 4598-4612
    • Loor, F.1    Tiberghien, F.2    Wenandy, T.3    Didier, A.4    Traber, R.5
  • 24
    • 0027207885 scopus 로고
    • Human immunodeficiency virus type 1 Gag protein binds to cyclophilins a and B
    • J. Luban, K.L. Bossolt, E.K. Franke, G.V. Kalpana, and S.P. Goff Human immunodeficiency virus type 1 Gag protein binds to cyclophilins A and B Cell 73 1993 1067 1078
    • (1993) Cell , vol.73 , pp. 1067-1078
    • Luban, J.1    Bossolt, K.L.2    Franke, E.K.3    Kalpana, G.V.4    Goff, S.P.5
  • 25
    • 0346118919 scopus 로고    scopus 로고
    • Hepatitis C virus non-structural proteins in the probable membranous compartment function in viral genome replication
    • Y. Miyanari, M. Hijikata, M. Yamaji, M. Hosaka, H. Takahashi, and K. Shimotohno Hepatitis C virus non-structural proteins in the probable membranous compartment function in viral genome replication J. Biol. Chem. 278 2003 50301 50308
    • (2003) J. Biol. Chem. , vol.278 , pp. 50301-50308
    • Miyanari, Y.1    Hijikata, M.2    Yamaji, M.3    Hosaka, M.4    Takahashi, H.5    Shimotohno, K.6
  • 29
    • 0242406997 scopus 로고    scopus 로고
    • Brome mosaic virus RNA replication: Revealing the role of the host in RNA virus replication
    • A.O. Noueiry, and P. Ahlquist Brome mosaic virus RNA replication: revealing the role of the host in RNA virus replication Annu. Rev. Phytopathol. 41 2003 77 98
    • (2003) Annu. Rev. Phytopathol. , vol.41 , pp. 77-98
    • Noueiry, A.O.1    Ahlquist, P.2
  • 30
    • 0028227015 scopus 로고
    • Cyclophilin B trafficking through the secretory pathway is altered by binding of cyclosporin a
    • E.R. Price, M. Jin, D. Lim, S. Pati, C.T. Walsh, and F.D. McKeon Cyclophilin B trafficking through the secretory pathway is altered by binding of cyclosporin A Proc. Natl. Acad. Sci. USA 91 1994 3931 3935
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 3931-3935
    • Price, E.R.1    Jin, M.2    Lim, D.3    Pati, S.4    Walsh, C.T.5    McKeon, F.D.6
  • 31
    • 0035120615 scopus 로고    scopus 로고
    • Mutational analysis of the structure and functions of hepatitis C virus RNA-dependent RNA polymerase
    • W. Qin, T. Yamashita, Y. Shirota, Y. Lin, W. Wei, and S. Murakami Mutational analysis of the structure and functions of hepatitis C virus RNA-dependent RNA polymerase Hepatology 33 2001 728 737
    • (2001) Hepatology , vol.33 , pp. 728-737
    • Qin, W.1    Yamashita, T.2    Shirota, Y.3    Lin, Y.4    Wei, W.5    Murakami, S.6
  • 32
    • 0029910198 scopus 로고    scopus 로고
    • Brome mosaic virus helicase- and polymerase-like proteins colocalize on the endoplasmic reticulum at sites of viral RNA synthesis
    • M.A. Restrepo-Hartwig, and P. Ahlquist Brome mosaic virus helicase- and polymerase-like proteins colocalize on the endoplasmic reticulum at sites of viral RNA synthesis J. Virol. 70 1996 8908 8916
    • (1996) J. Virol. , vol.70 , pp. 8908-8916
    • Restrepo-Hartwig, M.A.1    Ahlquist, P.2
  • 33
    • 0037076393 scopus 로고    scopus 로고
    • The intranuclear prolactin/cyclophilin B complex as a transcriptional inducer
    • M.A. Rycyzyn, and C.V. Clevenger The intranuclear prolactin/cyclophilin B complex as a transcriptional inducer Proc. Natl. Acad. Sci. USA 99 2002 6790 6795
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 6790-6795
    • Rycyzyn, M.A.1    Clevenger, C.V.2
  • 36
    • 0026030568 scopus 로고
    • Chemistry and biology of the immunophilins and their immunosuppressive ligands
    • S.L. Schreiber Chemistry and biology of the immunophilins and their immunosuppressive ligands Science 251 1991 283 287
    • (1991) Science , vol.251 , pp. 283-287
    • Schreiber, S.L.1
  • 37
    • 0026625939 scopus 로고
    • Immunophilin-sensitive protein phosphatase action in cell signaling pathways
    • S.L. Schreiber Immunophilin-sensitive protein phosphatase action in cell signaling pathways Cell 70 1992 365 368
    • (1992) Cell , vol.70 , pp. 365-368
    • Schreiber, S.L.1
  • 38
    • 0030765061 scopus 로고    scopus 로고
    • Characterization of anti-Toxoplasma activity of SDZ 215-918, a cyclosporin derivative lacking immunosuppressive and peptidyl-prolyl-isomerase- inhibiting activity: Possible role of a P glycoprotein in Toxoplasma physiology
    • J.A. Silverman, M.L. Hayes, B.J. Luft, and K.A. Joiner Characterization of anti-Toxoplasma activity of SDZ 215-918, a cyclosporin derivative lacking immunosuppressive and peptidyl-prolyl-isomerase-inhibiting activity: possible role of a P glycoprotein in Toxoplasma physiology Antimicrob. Agents Chemother. 41 1997 1859 1866
    • (1997) Antimicrob. Agents Chemother. , vol.41 , pp. 1859-1866
    • Silverman, J.A.1    Hayes, M.L.2    Luft, B.J.3    Joiner, K.A.4
  • 39
    • 0032982178 scopus 로고    scopus 로고
    • Pharmacodynamics of ciclosporin a (cyclosporine)
    • N. Takahashi Pharmacodynamics of ciclosporin A (cyclosporine) Clin. Exp. Nephrol. 3 1999 S16 S26
    • (1999) Clin. Exp. Nephrol. , vol.3
    • Takahashi, N.1
  • 40
    • 0036345943 scopus 로고    scopus 로고
    • Interaction between hepatitis C virus proteins and host cell factors
    • T.L. Tellinghuisen, and C.M. Rice Interaction between hepatitis C virus proteins and host cell factors Curr. Opin. Microbiol. 5 2002 419 427
    • (2002) Curr. Opin. Microbiol. , vol.5 , pp. 419-427
    • Tellinghuisen, T.L.1    Rice, C.M.2
  • 44
    • 0035421819 scopus 로고    scopus 로고
    • Cytoplasmic localization is important for transcription factor nuclear factor-kappa B activation by hepatitis C virus core protein through its amino terminal region
    • K. Watashi, M. Hijikata, H. Marusawa, T. Doi, and K. Shimotohno Cytoplasmic localization is important for transcription factor nuclear factor-kappa B activation by hepatitis C virus core protein through its amino terminal region Virology 286 2001 391 402
    • (2001) Virology , vol.286 , pp. 391-402
    • Watashi, K.1    Hijikata, M.2    Marusawa, H.3    Doi, T.4    Shimotohno, K.5
  • 45
    • 0142182744 scopus 로고    scopus 로고
    • Cyclosporin a suppresses replication of hepatitis C virus genome in cultured hepatocytes
    • K. Watashi, M. Hijikata, M. Hosaka, M. Yamaji, and K. Shimotohno Cyclosporin A suppresses replication of hepatitis C virus genome in cultured hepatocytes Hepatology 38 2003 1282 1288
    • (2003) Hepatology , vol.38 , pp. 1282-1288
    • Watashi, K.1    Hijikata, M.2    Hosaka, M.3    Yamaji, M.4    Shimotohno, K.5
  • 46
    • 0142123224 scopus 로고    scopus 로고
    • Modulation of retinoid signaling by a cytoplasmic viral protein via sequestration of Sp110b, a potent transcriptional corepressor of retinoic acid receptor, from the nucleus
    • K. Watashi, M. Hijikata, A. Tagawa, T. Doi, H. Marusawa, and K. Shimotohno Modulation of retinoid signaling by a cytoplasmic viral protein via sequestration of Sp110b, a potent transcriptional corepressor of retinoic acid receptor, from the nucleus Mol. Cell. Biol. 23 2003 7498 7509
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 7498-7509
    • Watashi, K.1    Hijikata, M.2    Tagawa, A.3    Doi, T.4    Marusawa, H.5    Shimotohno, K.6
  • 47
    • 0141426816 scopus 로고    scopus 로고
    • Targeting NS5B RNA-dependent RNA polymerase for anti-HCV chemotherapy
    • J.Z. Wu, and Z. Hong Targeting NS5B RNA-dependent RNA polymerase for anti-HCV chemotherapy Curr. Drug Targets Infect. Disord. 3 2003 207 219
    • (2003) Curr. Drug Targets Infect. Disord. , vol.3 , pp. 207-219
    • Wu, J.Z.1    Hong, Z.2
  • 48
    • 0347634413 scopus 로고    scopus 로고
    • A cis-acting replication element in the sequence encoding the NS5B RNA-dependent RNA polymerase is required for hepatitis C virus RNA replication
    • S. You, D.D. Stump, A.D. Branch, and C.M. Rice A cis-acting replication element in the sequence encoding the NS5B RNA-dependent RNA polymerase is required for hepatitis C virus RNA replication J. Virol. 78 2004 1352 1366
    • (2004) J. Virol. , vol.78 , pp. 1352-1366
    • You, S.1    Stump, D.D.2    Branch, A.D.3    Rice, C.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.