메뉴 건너뛰기




Volumn 8, Issue 9, 2013, Pages

Heat Shock Protein 70 Is Associated with Replicase Complex of Japanese Encephalitis Virus and Positively Regulates Viral Genome Replication

Author keywords

[No Author keywords available]

Indexed keywords

DOUBLE STRANDED RNA; ELONGATION FACTOR 1ALPHA; HEAT SHOCK PROTEIN 70; NONSTRUCTURAL PROTEIN 3; NONSTRUCTURAL PROTEIN 5; RAN PROTEIN;

EID: 84884521148     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0075188     Document Type: Article
Times cited : (50)

References (45)
  • 2
    • 77952293291 scopus 로고    scopus 로고
    • Overview: Japanese encephalitis
    • doi: 10.1016/j.pneurobio.2010.01.008
    • Misra UK, Kalita J, (2010) Overview: Japanese encephalitis. Prog Neurobiol 91: 108-120. doi:10.1016/j.pneurobio.2010.01.008. PubMed: 20132860.
    • (2010) Prog Neurobiol , vol.91 , pp. 108-120
    • Misra, U.K.1    Kalita, J.2
  • 3
    • 0023497850 scopus 로고
    • Complete nucleotide sequence of the Japanese encephalitis virus genome RNA
    • doi: 10.1016/0042-6822(87)90144-9
    • Sumiyoshi H, Mori C, Fuke I, Morita K, Kuhara S, et al. (1987) Complete nucleotide sequence of the Japanese encephalitis virus genome RNA. Virology 161: 497-510. doi:10.1016/0042-6822(87)90144-9. PubMed: 3686827.
    • (1987) Virology , vol.161 , pp. 497-510
    • Sumiyoshi, H.1    Mori, C.2    Fuke, I.3    Morita, K.4    Kuhara, S.5
  • 4
    • 77954956665 scopus 로고    scopus 로고
    • Structure and functionality in flavivirus NS-proteins: perspectives for drug design
    • doi: 10.1016/j.antiviral.2009.11.009
    • Bollati M, Alvarez K, Assenberg R, Baronti C, Canard B, et al. (2010) Structure and functionality in flavivirus NS-proteins: perspectives for drug design. Antiviral Res 87: 125-148. doi:10.1016/j.antiviral.2009.11.009. PubMed: 19945487.
    • (2010) Antiviral Res , vol.87 , pp. 125-148
    • Bollati, M.1    Alvarez, K.2    Assenberg, R.3    Baronti, C.4    Canard, B.5
  • 5
    • 68649103985 scopus 로고    scopus 로고
    • New insights into flavivirus nonstructural protein 5
    • doi: 10.1016/S0065-3527(09)74002-3
    • Davidson AD, (2009) Chapter 2. New insights into flavivirus nonstructural protein 5. Adv Virus Res 74: 41-101. doi:10.1016/S0065-3527(09)74002-3. PubMed: 19698895.
    • (2009) Adv Virus Res , vol.74 , pp. 41-101
    • Davidson, A.D.1
  • 6
    • 33646735772 scopus 로고    scopus 로고
    • Nuclear localization of flavivirus RNA synthesis in infected cells
    • doi: 10.1128/JVI.01982-05
    • Uchil PD, Kumar AV, Satchidanandam V, (2006) Nuclear localization of flavivirus RNA synthesis in infected cells. J Virol 80: 5451-5464. doi:10.1128/JVI.01982-05. PubMed: 16699025.
    • (2006) J Virol , vol.80 , pp. 5451-5464
    • Uchil, P.D.1    Kumar, A.V.2    Satchidanandam, V.3
  • 7
    • 4143151721 scopus 로고    scopus 로고
    • Blocking of the alpha interferon-induced Jak-Stat signaling pathway by Japanese encephalitis virus infection
    • doi: 10.1128/JVI.78.17.9285-9294.2004
    • Lin RJ, Liao CL, Lin E, Lin YL, (2004) Blocking of the alpha interferon-induced Jak-Stat signaling pathway by Japanese encephalitis virus infection. J Virol 78: 9285-9294. doi:10.1128/JVI.78.17.9285-9294.2004. PubMed: 15308723.
    • (2004) J Virol , vol.78 , pp. 9285-9294
    • Lin, R.J.1    Liao, C.L.2    Lin, E.3    Lin, Y.L.4
  • 8
    • 33744943788 scopus 로고    scopus 로고
    • Blocking of interferon-induced Jak-Stat signaling by Japanese encephalitis virus NS5 through a protein tyrosine phosphatase-mediated mechanism
    • doi: 10.1128/JVI.02714-05
    • Lin RJ, Chang BL, Yu HP, Liao CL, Lin YL, (2006) Blocking of interferon-induced Jak-Stat signaling by Japanese encephalitis virus NS5 through a protein tyrosine phosphatase-mediated mechanism. J Virol 80: 5908-5918. doi:10.1128/JVI.02714-05. PubMed: 16731929.
    • (2006) J Virol , vol.80 , pp. 5908-5918
    • Lin, R.J.1    Chang, B.L.2    Yu, H.P.3    Liao, C.L.4    Lin, Y.L.5
  • 9
    • 77955842615 scopus 로고    scopus 로고
    • Role of host cell factors in flavivirus infection: Implications for pathogenesis and development of antiviral drugs
    • doi: 10.1016/j.antiviral.2010.04.014
    • Pastorino B, Nougairède A, Wurtz N, Gould E, de Lamballerie X, (2010) Role of host cell factors in flavivirus infection: Implications for pathogenesis and development of antiviral drugs. Antiviral Res 87: 281-294. doi:10.1016/j.antiviral.2010.04.014. PubMed: 20452379.
    • (2010) Antiviral Res , vol.87 , pp. 281-294
    • Pastorino, B.1    Nougairède, A.2    Wurtz, N.3    Gould, E.4    de Lamballerie, X.5
  • 10
    • 0033579518 scopus 로고    scopus 로고
    • Heat shock protein (Hsp) 40 mutants inhibit Hsp70 in mammalian cells
    • doi: 10.1074/jbc.274.51.36757
    • Michels AA, Kanon B, Bensaude O, Kampinga HH, (1999) Heat shock protein (Hsp) 40 mutants inhibit Hsp70 in mammalian cells. J Biol Chem 274: 36757-36763. doi:10.1074/jbc.274.51.36757. PubMed: 10593983.
    • (1999) J Biol Chem , vol.274 , pp. 36757-36763
    • Michels, A.A.1    Kanon, B.2    Bensaude, O.3    Kampinga, H.H.4
  • 11
    • 0034646511 scopus 로고    scopus 로고
    • Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine
    • doi: 10.1016/S0092-8674(00)80830-2
    • Scheufler C, Brinker A, Bourenkov G, Pegoraro S, Moroder L, et al. (2000) Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine. Cell 101: 199-210. doi:10.1016/S0092-8674(00)80830-2. PubMed: 10786835.
    • (2000) Cell , vol.101 , pp. 199-210
    • Scheufler, C.1    Brinker, A.2    Bourenkov, G.3    Pegoraro, S.4    Moroder, L.5
  • 12
    • 17044387386 scopus 로고    scopus 로고
    • Hsp70 chaperones: cellular functions and molecular mechanism
    • doi: 10.1007/s00018-004-4464-6
    • Mayer MP, Bukau B, (2005) Hsp70 chaperones: cellular functions and molecular mechanism. Cell Mol Life Sci 62: 670-684. doi:10.1007/s00018-004-4464-6. PubMed: 15770419.
    • (2005) Cell Mol Life Sci , vol.62 , pp. 670-684
    • Mayer, M.P.1    Bukau, B.2
  • 13
    • 0642377466 scopus 로고    scopus 로고
    • More than folding: localized functions of cytosolic chaperones
    • doi: 10.1016/j.tibs.2003.08.009
    • Young JC, Barral JM, Ulrich Hartl F, (2003) More than folding: localized functions of cytosolic chaperones. Trends Biochem Sci 28: 541-547. doi:10.1016/j.tibs.2003.08.009. PubMed: 14559183.
    • (2003) Trends Biochem Sci , vol.28 , pp. 541-547
    • Young, J.C.1    Barral, J.M.2    Ulrich Hartl, F.3
  • 14
    • 0037315208 scopus 로고    scopus 로고
    • Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery
    • PubMed: 12563018
    • Pratt WB, Toft DO, (2003) Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery. Exp Biol Med (Maywood) 228: 111-133. PubMed: 12563018.
    • (2003) Exp Biol Med (Maywood) , vol.228 , pp. 111-133
    • Pratt, W.B.1    Toft, D.O.2
  • 15
    • 4444296762 scopus 로고    scopus 로고
    • Heat shock protein 70 protects cells from cell cycle arrest and apoptosis induced by human immunodeficiency virus type 1 viral protein R
    • doi: 10.1128/JVI.78.18.9697-9704.2004
    • Iordanskiy S, Zhao Y, Dubrovsky L, Iordanskaya T, Chen M, et al. (2004) Heat shock protein 70 protects cells from cell cycle arrest and apoptosis induced by human immunodeficiency virus type 1 viral protein R. J Virol 78: 9697-9704. doi:10.1128/JVI.78.18.9697-9704.2004. PubMed: 15331702.
    • (2004) J Virol , vol.78 , pp. 9697-9704
    • Iordanskiy, S.1    Zhao, Y.2    Dubrovsky, L.3    Iordanskaya, T.4    Chen, M.5
  • 16
    • 33750716581 scopus 로고    scopus 로고
    • hsp72, a host determinant of measles virus neurovirulence
    • doi: 10.1128/JVI.01438-06
    • Carsillo T, Traylor Z, Choi C, Niewiesk S, Oglesbee M, (2006) hsp72, a host determinant of measles virus neurovirulence. J Virol 80: 11031-11039. doi:10.1128/JVI.01438-06. PubMed: 16971451.
    • (2006) J Virol , vol.80 , pp. 11031-11039
    • Carsillo, T.1    Traylor, Z.2    Choi, C.3    Niewiesk, S.4    Oglesbee, M.5
  • 17
    • 58149399332 scopus 로고    scopus 로고
    • In vitro assembly of the Tomato bushy stunt virus replicase requires the host Heat shock protein 70
    • doi: 10.1073/pnas.0810851105
    • Pogany J, Stork J, Li Z, Nagy PD, (2008) In vitro assembly of the Tomato bushy stunt virus replicase requires the host Heat shock protein 70. Proc Natl Acad Sci U S A 105: 19956-19961. doi:10.1073/pnas.0810851105. PubMed: 19060219.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 19956-19961
    • Pogany, J.1    Stork, J.2    Li, Z.3    Nagy, P.D.4
  • 18
    • 33846484215 scopus 로고    scopus 로고
    • Hsp70 negatively controls rotavirus protein bioavailability in caco-2 cells infected by the rotavirus RF strain
    • doi: 10.1128/JVI.01336-06
    • Broquet AH, Lenoir C, Gardet A, Sapin C, Chwetzoff S, et al. (2007) Hsp70 negatively controls rotavirus protein bioavailability in caco-2 cells infected by the rotavirus RF strain. J Virol 81: 1297-1304. doi:10.1128/JVI.01336-06. PubMed: 17079279.
    • (2007) J Virol , vol.81 , pp. 1297-1304
    • Broquet, A.H.1    Lenoir, C.2    Gardet, A.3    Sapin, C.4    Chwetzoff, S.5
  • 19
    • 0347003598 scopus 로고    scopus 로고
    • Heat shock protein 70 is related to thermal inhibition of nuclear export of the influenza virus ribonucleoprotein complex
    • doi: 10.1128/JVI.78.3.1263-1270.2004
    • Hirayama E, Atagi H, Hiraki A, Kim J, (2004) Heat shock protein 70 is related to thermal inhibition of nuclear export of the influenza virus ribonucleoprotein complex. J Virol 78: 1263-1270. doi:10.1128/JVI.78.3.1263-1270.2004. PubMed: 14722281.
    • (2004) J Virol , vol.78 , pp. 1263-1270
    • Hirayama, E.1    Atagi, H.2    Hiraki, A.3    Kim, J.4
  • 20
    • 79952076763 scopus 로고    scopus 로고
    • Heat shock protein 70 inhibits the activity of Influenza A virus ribonucleoprotein and blocks the replication of virus in vitro and in vivo
    • doi: 10.1371/journal.pone.0016546
    • Li G, Zhang J, Tong X, Liu W, Ye X, (2011) Heat shock protein 70 inhibits the activity of Influenza A virus ribonucleoprotein and blocks the replication of virus in vitro and in vivo. PLOS ONE 6: e16546. doi:10.1371/journal.pone.0016546. PubMed: 21390211.
    • (2011) PLOS ONE , vol.6
    • Li, G.1    Zhang, J.2    Tong, X.3    Liu, W.4    Ye, X.5
  • 21
    • 16244364801 scopus 로고    scopus 로고
    • Heat shock protein 90 and heat shock protein 70 are components of dengue virus receptor complex in human cells
    • doi: 10.1128/JVI.79.8.4557-4567.2005
    • Reyes-Del Valle J, Chávez-Salinas S, Medina F, Del Angel RM, (2005) Heat shock protein 90 and heat shock protein 70 are components of dengue virus receptor complex in human cells. J Virol 79: 4557-4567. doi:10.1128/JVI.79.8.4557-4567.2005. PubMed: 15795242.
    • (2005) J Virol , vol.79 , pp. 4557-4567
    • Reyes-Del Valle, J.1    Chávez-Salinas, S.2    Medina, F.3    Del Angel, R.M.4
  • 22
    • 16444378781 scopus 로고    scopus 로고
    • Recruitment of Hsp70 chaperones: a crucial part of viral survival strategies
    • doi: 10.1007/s10254-004-0025-5
    • Mayer MP, (2005) Recruitment of Hsp70 chaperones: a crucial part of viral survival strategies. Rev Physiol Biochem Pharmacol 153: 1-46. doi:10.1007/s10254-004-0025-5. PubMed: 15243813.
    • (2005) Rev Physiol Biochem Pharmacol , vol.153 , pp. 1-46
    • Mayer, M.P.1
  • 23
    • 60349109590 scopus 로고    scopus 로고
    • Heat shock protein 70 on Neuro2a cells is a putative receptor for Japanese encephalitis virus
    • doi: 10.1016/j.virol.2008.10.025
    • Das S, Laxminarayana SV, Chandra N, Ravi V, Desai A, (2009) Heat shock protein 70 on Neuro2a cells is a putative receptor for Japanese encephalitis virus. Virology 385: 47-57. doi:10.1016/j.virol.2008.10.025. PubMed: 19068261.
    • (2009) Virology , vol.385 , pp. 47-57
    • Das, S.1    Laxminarayana, S.V.2    Chandra, N.3    Ravi, V.4    Desai, A.5
  • 24
    • 83755195729 scopus 로고    scopus 로고
    • Association of heat-shock protein 70 with lipid rafts is required for Japanese encephalitis virus infection in Huh7 cells
    • doi: 10.1099/vir.0.034637-0
    • Zhu YZ, Cao MM, Wang WB, Wang W, Ren H, et al. (2012) Association of heat-shock protein 70 with lipid rafts is required for Japanese encephalitis virus infection in Huh7 cells. J Gen Virol 93: 61-71. doi:10.1099/vir.0.034637-0. PubMed: 21940409.
    • (2012) J Gen Virol , vol.93 , pp. 61-71
    • Zhu, Y.Z.1    Cao, M.M.2    Wang, W.B.3    Wang, W.4    Ren, H.5
  • 25
    • 84859964106 scopus 로고    scopus 로고
    • Monoclonal antibodies against NS3 and NS5 proteins of Japanese encephalitis virus
    • doi: 10.1089/hyb.2011.0107
    • Chen Z, Shao L, Ye J, Li Y, Huang S, et al. (2012) Monoclonal antibodies against NS3 and NS5 proteins of Japanese encephalitis virus. Hybridoma (Larchmt) 31: 137-141. doi:10.1089/hyb.2011.0107. PubMed: 22509919.
    • (2012) Hybridoma (Larchmt) , vol.31 , pp. 137-141
    • Chen, Z.1    Shao, L.2    Ye, J.3    Li, Y.4    Huang, S.5
  • 26
    • 80055111913 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonucleoprotein A2 participates in the replication of Japanese encephalitis virus through an interaction with viral proteins and RNA
    • doi: 10.1128/JVI.00846-11
    • Katoh H, Mori Y, Kambara H, Abe T, Fukuhara T, et al. (2011) Heterogeneous nuclear ribonucleoprotein A2 participates in the replication of Japanese encephalitis virus through an interaction with viral proteins and RNA. J Virol 85: 10976-10988. doi:10.1128/JVI.00846-11. PubMed: 21865391.
    • (2011) J Virol , vol.85 , pp. 10976-10988
    • Katoh, H.1    Mori, Y.2    Kambara, H.3    Abe, T.4    Fukuhara, T.5
  • 27
    • 80053936781 scopus 로고    scopus 로고
    • DnaJ homolog Hdj2 facilitates Japanese encephalitis virus replication
    • doi: 10.1186/1743-422X-8-471
    • Wang RY, Huang YR, Chong KM, Hung CY, Ke ZL, et al. (2011) DnaJ homolog Hdj2 facilitates Japanese encephalitis virus replication. Virol J 8: 471. doi:10.1186/1743-422X-8-471. PubMed: 21999493.
    • (2011) Virol J , vol.8 , pp. 471
    • Wang, R.Y.1    Huang, Y.R.2    Chong, K.M.3    Hung, C.Y.4    Ke, Z.L.5
  • 28
    • 49549092476 scopus 로고    scopus 로고
    • Mapping multiprotein complexes by affinity purification and mass spectrometry
    • doi: 10.1016/j.copbio.2008.06.002
    • Collins MO, Choudhary JS, (2008) Mapping multiprotein complexes by affinity purification and mass spectrometry. Curr Opin Biotechnol 19: 324-330. doi:10.1016/j.copbio.2008.06.002. PubMed: 18598764.
    • (2008) Curr Opin Biotechnol , vol.19 , pp. 324-330
    • Collins, M.O.1    Choudhary, J.S.2
  • 29
    • 0346094408 scopus 로고    scopus 로고
    • Recent developments in the analysis of protein complexes
    • doi: 10.1016/S0014-5793(03)01357-7
    • Dziembowski A, Séraphin B, (2004) Recent developments in the analysis of protein complexes. FEBS Lett 556: 1-6. doi:10.1016/S0014-5793(03)01357-7. PubMed: 14706816.
    • (2004) FEBS Lett , vol.556 , pp. 1-6
    • Dziembowski, A.1    Séraphin, B.2
  • 30
    • 0030761459 scopus 로고    scopus 로고
    • Translation elongation factor-1 alpha interacts with the 3' stem-loop region of West Nile virus genomic RNA
    • PubMed: 9261361
    • Blackwell JL, Brinton MA, (1997) Translation elongation factor-1 alpha interacts with the 3' stem-loop region of West Nile virus genomic RNA. J Virol 71: 6433-6444. PubMed: 9261361.
    • (1997) J Virol , vol.71 , pp. 6433-6444
    • Blackwell, J.L.1    Brinton, M.A.2
  • 31
    • 35348822495 scopus 로고    scopus 로고
    • Interaction between the cellular protein eEF1A and the 3'-terminal stem-loop of West Nile virus genomic RNA facilitates viral minus-strand RNA synthesis
    • doi: 10.1128/JVI.00531-07
    • Davis WG, Blackwell JL, Shi PY, Brinton MA, (2007) Interaction between the cellular protein eEF1A and the 3'-terminal stem-loop of West Nile virus genomic RNA facilitates viral minus-strand RNA synthesis. J Virol 81: 10172-10187. doi:10.1128/JVI.00531-07. PubMed: 17626087.
    • (2007) J Virol , vol.81 , pp. 10172-10187
    • Davis, W.G.1    Blackwell, J.L.2    Shi, P.Y.3    Brinton, M.A.4
  • 32
    • 0027959741 scopus 로고
    • Interaction of poliovirus polypeptide 3CDpro with the 5' and 3' termini of the poliovirus genome. Identification of viral and cellular cofactors needed for efficient binding
    • PubMed: 7929441
    • Harris KS, Xiang W, Alexander L, Lane WS, Paul AV, et al. (1994) Interaction of poliovirus polypeptide 3CDpro with the 5' and 3' termini of the poliovirus genome. Identification of viral and cellular cofactors needed for efficient binding. J Biol Chem 269: 27004-27014. PubMed: 7929441.
    • (1994) J Biol Chem , vol.269 , pp. 27004-27014
    • Harris, K.S.1    Xiang, W.2    Alexander, L.3    Lane, W.S.4    Paul, A.V.5
  • 33
    • 1642317212 scopus 로고    scopus 로고
    • eEF1A binding to aminoacylated viral RNA represses minus strand synthesis by TYMV RNA-dependent RNA polymerase
    • doi: 10.1016/j.virol.2003.10.028
    • Matsuda D, Yoshinari S, Dreher TW, (2004) eEF1A binding to aminoacylated viral RNA represses minus strand synthesis by TYMV RNA-dependent RNA polymerase. Virology 321: 47-56. doi:10.1016/j.virol.2003.10.028. PubMed: 15033564.
    • (2004) Virology , vol.321 , pp. 47-56
    • Matsuda, D.1    Yoshinari, S.2    Dreher, T.W.3
  • 34
    • 1942469432 scopus 로고    scopus 로고
    • Two RNA polymerase complexes from vesicular stomatitis virus-infected cells that carry out transcription and replication of genome RNA
    • doi: 10.1073/pnas.0401449101
    • Qanungo KR, Shaji D, Mathur M, Banerjee AK, (2004) Two RNA polymerase complexes from vesicular stomatitis virus-infected cells that carry out transcription and replication of genome RNA. Proc Natl Acad Sci U S A 101: 5952-5957. doi:10.1073/pnas.0401449101. PubMed: 15069200.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 5952-5957
    • Qanungo, K.R.1    Shaji, D.2    Mathur, M.3    Banerjee, A.K.4
  • 35
    • 38349187678 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport of proteins
    • doi: 10.1134/S0006297907130032
    • Sorokin AV, Kim ER, Ovchinnikov LP, (2007) Nucleocytoplasmic transport of proteins. Biochemistry (Mosc) 72: 1439-1457. doi:10.1134/S0006297907130032. PubMed: 18282135.
    • (2007) Biochemistry (Mosc) , vol.72 , pp. 1439-1457
    • Sorokin, A.V.1    Kim, E.R.2    Ovchinnikov, L.P.3
  • 36
    • 33847176295 scopus 로고    scopus 로고
    • Molecular mechanism of the nuclear protein import cycle
    • doi: 10.1038/nrm2114
    • Stewart M, (2007) Molecular mechanism of the nuclear protein import cycle. Nat Rev Mol Cell Biol 8: 195-208. doi:10.1038/nrm2114. PubMed: 17287812.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 195-208
    • Stewart, M.1
  • 37
    • 0029027850 scopus 로고
    • Association between NS3 and NS5 proteins of dengue virus type 2 in the putative RNA replicase is linked to differential phosphorylation of NS5
    • doi: 10.1074/jbc.270.32.19100
    • Kapoor M, Zhang L, Ramachandra M, Kusukawa J, Ebner KE, et al. (1995) Association between NS3 and NS5 proteins of dengue virus type 2 in the putative RNA replicase is linked to differential phosphorylation of NS5. J Biol Chem 270: 19100-19106. doi:10.1074/jbc.270.32.19100. PubMed: 7642575.
    • (1995) J Biol Chem , vol.270 , pp. 19100-19106
    • Kapoor, M.1    Zhang, L.2    Ramachandra, M.3    Kusukawa, J.4    Ebner, K.E.5
  • 38
    • 78650155438 scopus 로고    scopus 로고
    • Dengue virus infection activates cellular chaperone Hsp70 in THP-1 cells: downregulation of Hsp70 by siRNA revealed decreased viral replication
    • doi: 10.1089/vim.2010.0052
    • Padwad YS, Mishra KP, Jain M, Chanda S, Ganju L, (2010) Dengue virus infection activates cellular chaperone Hsp70 in THP-1 cells: downregulation of Hsp70 by siRNA revealed decreased viral replication. Viral Immunol 23: 557-565. doi:10.1089/vim.2010.0052. PubMed: 21142441.
    • (2010) Viral Immunol , vol.23 , pp. 557-565
    • Padwad, Y.S.1    Mishra, K.P.2    Jain, M.3    Chanda, S.4    Ganju, L.5
  • 39
    • 77956255823 scopus 로고    scopus 로고
    • Heat shock protein 72 is associated with the hepatitis C virus replicase complex and enhances viral RNA replication
    • doi: 10.1074/jbc.M110.118323
    • Chen YJ, Chen YH, Chow LP, Tsai YH, Chen PH, et al. (2010) Heat shock protein 72 is associated with the hepatitis C virus replicase complex and enhances viral RNA replication. J Biol Chem 285: 28183-28190. doi:10.1074/jbc.M110.118323. PubMed: 20601427.
    • (2010) J Biol Chem , vol.285 , pp. 28183-28190
    • Chen, Y.J.1    Chen, Y.H.2    Chow, L.P.3    Tsai, Y.H.4    Chen, P.H.5
  • 40
    • 0036223410 scopus 로고    scopus 로고
    • Japanese encephalitis virus infection initiates endoplasmic reticulum stress and an unfolded protein response
    • doi: 10.1128/JVI.76.9.4162-4171.2002
    • Su HL, Liao CL, Lin YL, (2002) Japanese encephalitis virus infection initiates endoplasmic reticulum stress and an unfolded protein response. J Virol 76: 4162-4171. doi:10.1128/JVI.76.9.4162-4171.2002. PubMed: 11932381.
    • (2002) J Virol , vol.76 , pp. 4162-4171
    • Su, H.L.1    Liao, C.L.2    Lin, Y.L.3
  • 41
    • 35148894008 scopus 로고    scopus 로고
    • West Nile virus infection activates the unfolded protein response, leading to CHOP induction and apoptosis
    • doi: 10.1128/JVI.01151-07
    • Medigeshi GR, Lancaster AM, Hirsch AJ, Briese T, Lipkin WI, et al. (2007) West Nile virus infection activates the unfolded protein response, leading to CHOP induction and apoptosis. J Virol 81: 10849-10860. doi:10.1128/JVI.01151-07. PubMed: 17686866.
    • (2007) J Virol , vol.81 , pp. 10849-10860
    • Medigeshi, G.R.1    Lancaster, A.M.2    Hirsch, A.J.3    Briese, T.4    Lipkin, W.I.5
  • 42
    • 78650287673 scopus 로고    scopus 로고
    • Dengue infection of monocytic cells activates ER stress pathways, but apoptosis is induced through both extrinsic and intrinsic pathways
    • doi: 10.1016/j.virol.2010.10.010
    • Klomporn P, Panyasrivanit M, Wikan N, Smith DR, (2011) Dengue infection of monocytic cells activates ER stress pathways, but apoptosis is induced through both extrinsic and intrinsic pathways. Virology 409: 189-197. doi:10.1016/j.virol.2010.10.010. PubMed: 21047664.
    • (2011) Virology , vol.409 , pp. 189-197
    • Klomporn, P.1    Panyasrivanit, M.2    Wikan, N.3    Smith, D.R.4
  • 43
    • 79953089155 scopus 로고    scopus 로고
    • Japanese encephalitis virus co-opts the ER-stress response protein GRP78 for viral infectivity
    • doi: 10.1186/1743-422X-8-128
    • Wu YP, Chang CM, Hung CY, Tsai MC, Schuyler SC, et al. (2011) Japanese encephalitis virus co-opts the ER-stress response protein GRP78 for viral infectivity. Virol J 8: 128. doi:10.1186/1743-422X-8-128. PubMed: 21418596.
    • (2011) Virol J , vol.8 , pp. 128
    • Wu, Y.P.1    Chang, C.M.2    Hung, C.Y.3    Tsai, M.C.4    Schuyler, S.C.5
  • 44
    • 84861302576 scopus 로고    scopus 로고
    • Hsp70 protein positively regulates rabies virus infection
    • doi: 10.1128/JVI.06501-11
    • Lahaye X, Vidy A, Fouquet B, Blondel D, (2012) Hsp70 protein positively regulates rabies virus infection. J Virol 86: 4743-4751. doi:10.1128/JVI.06501-11. PubMed: 22345440.
    • (2012) J Virol , vol.86 , pp. 4743-4751
    • Lahaye, X.1    Vidy, A.2    Fouquet, B.3    Blondel, D.4
  • 45
    • 0032983061 scopus 로고    scopus 로고
    • In vivo chaperone activity of heat shock protein 70 and thermotolerance
    • doi: 10022894
    • Nollen EA, Brunsting JF, Roelofsen H, Weber LA, Kampinga HH, (1999) In vivo chaperone activity of heat shock protein 70 and thermotolerance. Mol Cell Biol 19: 2069-2079. PubMed: 10022894.
    • (1999) Mol Cell Biol , vol.19 , pp. 2069-2079
    • Nollen, E.A.1    Brunsting, J.F.2    Roelofsen, H.3    Weber, L.A.4    Kampinga, H.H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.