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Volumn 6, Issue , 2016, Pages

Human Heat shock protein 40 (Hsp40/DnaJB1) promotes influenza A virus replication by assisting nuclear import of viral ribonucleoproteins

Author keywords

[No Author keywords available]

Indexed keywords

2 PYRROLIDONE DERIVATIVE; BENZHYDRYL DERIVATIVE; HEAT SHOCK PROTEIN 40; KNK 437; PROTEIN BINDING; RIBONUCLEOPROTEIN; SMALL INTERFERING RNA; VIRAL PROTEIN;

EID: 84954146631     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep19063     Document Type: Article
Times cited : (48)

References (65)
  • 1
    • 77954242392 scopus 로고    scopus 로고
    • Viral interaction with molecular chaperones: Role in regulating viral infection
    • Xiao, A., Wong, J. & Luo, H. Viral interaction with molecular chaperones: role in regulating viral infection. Arch Virol 155(7), 1021(2010).
    • (2010) Arch Virol , vol.155 , Issue.7 , pp. 1021
    • Xiao, A.1    Wong, J.2    Luo, H.3
  • 2
    • 0033521588 scopus 로고    scopus 로고
    • In vivo newly translated polypeptides are sequestered in a protected folding environment
    • Thulasiraman, V., Yang, C. F. & Frydman, J. In vivo newly translated polypeptides are sequestered in a protected folding environment. EMBO J 18(1), 85 (1999).
    • (1999) EMBO J , vol.18 , Issue.1 , pp. 85
    • Thulasiraman, V.1    Yang, C.F.2    Frydman, J.3
  • 3
    • 9644280977 scopus 로고    scopus 로고
    • Cooperation of molecular chaperones with the ubiquitin/proteasome system
    • Esser, C., Alberti, S. & Hohfeld, J. Cooperation of molecular chaperones with the ubiquitin/proteasome system. BiochimBiophysActa 1695(1-3), 171 (2004).
    • (2004) BiochimBiophysActa , vol.1695 , Issue.1-3 , pp. 171
    • Esser, C.1    Alberti, S.2    Hohfeld, J.3
  • 4
    • 84871737427 scopus 로고    scopus 로고
    • The prenyl-binding protein PrBP/delta: A chaperone participating in intracellular trafficking
    • Zhang, H., Constantine, R., Frederick, J. M. & Baehr, W. The prenyl-binding protein PrBP/delta: a chaperone participating in intracellular trafficking. Vision Res 75, 19 (2012).
    • (2012) Vision Res , vol.75 , pp. 19
    • Zhang, H.1    Constantine, R.2    Frederick, J.M.3    Baehr, W.4
  • 5
    • 0030112452 scopus 로고    scopus 로고
    • Evidence for a role of Hsp70 in the regulation of the heat shock response in mammalian cells
    • Baler, R., Zou, J. & Voellmy, R. Evidence for a role of Hsp70 in the regulation of the heat shock response in mammalian cells. Cell Stress Chaperones 1(1), 33 (1996).
    • (1996) Cell Stress Chaperones , vol.1 , Issue.1 , pp. 33
    • Baler, R.1    Zou, J.2    Voellmy, R.3
  • 6
    • 0036194651 scopus 로고    scopus 로고
    • Heat shock cognate protein 70 is involved in rotavirus cell entry
    • Guerrero, C. A. et al. Heat shock cognate protein 70 is involved in rotavirus cell entry. J Virol 76(8), 4096 (2002).
    • (2002) J Virol , vol.76 , Issue.8 , pp. 4096
    • Guerrero, C.A.1
  • 7
    • 0035923585 scopus 로고    scopus 로고
    • Host cell factor requirement for hepatitis C virus enzyme maturation
    • Waxman, L. et al. Host cell factor requirement for hepatitis C virus enzyme maturation. Proc Natl Acad Sci USA 98(24), 13931 (2001).
    • (2001) Proc Natl Acad Sci USA , vol.98 , Issue.24 , pp. 13931
    • Waxman, L.1
  • 8
    • 84878180356 scopus 로고    scopus 로고
    • Nuclear transport of Epstein-Barr virus DNA polymerase is dependent on the BMRF1 polymerase processivity factor and molecular chaperone Hsp90
    • Kawashima, D. et al. Nuclear transport of Epstein-Barr virus DNA polymerase is dependent on the BMRF1 polymerase processivity factor and molecular chaperone Hsp90. J Virol 87(11), 6482 (2013).
    • (2013) J Virol , vol.87 , Issue.11 , pp. 6482
    • Kawashima, D.1
  • 9
    • 28844505342 scopus 로고    scopus 로고
    • Heat shock protein 40 is necessary for human immunodeficiency virus-1 Nef-mediated enhancement of viral gene expression and replication
    • Kumar, M. & Mitra, D. Heat shock protein 40 is necessary for human immunodeficiency virus-1 Nef-mediated enhancement of viral gene expression and replication. J Biol Chem 280(48), 40041 (2005).
    • (2005) J Biol Chem , vol.280 , Issue.48 , pp. 40041
    • Kumar, M.1    Mitra, D.2
  • 10
    • 79958838725 scopus 로고    scopus 로고
    • Influenza A virus nucleoprotein exploits Hsp40 to inhibit PKR activation
    • Sharma, K. et al. Influenza A virus nucleoprotein exploits Hsp40 to inhibit PKR activation. PLoS One 6(6), e20215 (2011).
    • (2011) PLoS One , vol.6 , Issue.6
    • Sharma, K.1
  • 11
    • 33745622377 scopus 로고    scopus 로고
    • Negative regulation of hepatitis B virus replication by cellular Hsp40/DnaJ proteins through destabilization of viral core and X proteins
    • Sohn, S. Y., Kim, S. B., Kim, J. & Ahn, B. Y. Negative regulation of hepatitis B virus replication by cellular Hsp40/DnaJ proteins through destabilization of viral core and X proteins. J Gen Virol 87(Pt 7), 1883 (2006).
    • (2006) J Gen Virol , vol.87 , pp. 1883
    • Sohn, S.Y.1    Kim, S.B.2    Kim, J.3    Ahn, B.Y.4
  • 12
    • 84861302576 scopus 로고    scopus 로고
    • Hsp70 protein positively regulates rabies virus infection
    • Lahaye, X., Vidy, A., Fouquet, B. & Blondel, D. Hsp70 protein positively regulates rabies virus infection. J Virol 86(9), 4743 (2012).
    • (2012) J Virol , vol.86 , Issue.9 , pp. 4743
    • Lahaye, X.1    Vidy, A.2    Fouquet, B.3    Blondel, D.4
  • 13
    • 72849128415 scopus 로고    scopus 로고
    • A targeted analysis of cellular chaperones reveals contrasting roles for heat shock protein 70 in flock house virus RNA replication
    • Weeks, S. A. et al. A targeted analysis of cellular chaperones reveals contrasting roles for heat shock protein 70 in flock house virus RNA replication. J Virol 84(1), 330 (2013).
    • (2013) J Virol , vol.84 , Issue.1 , pp. 330
    • Weeks, S.A.1
  • 14
    • 0015414910 scopus 로고
    • Structure of the ribonucleoprotein of influenza virus
    • Compans, R. W., Content, J. & Duesberg, P. H. Structure of the ribonucleoprotein of influenza virus. J Virol 10(4), 795 (1972).
    • (1972) J Virol , vol.10 , Issue.4 , pp. 795
    • Compans, R.W.1    Content, J.2    Duesberg, P.H.3
  • 15
    • 0020074251 scopus 로고
    • Studies on the helical nucleocapsid of influenza virus
    • Heggeness, M. H. et al. Studies on the helical nucleocapsid of influenza virus. Virology 118(2), 466 (1982).
    • (1982) Virology , vol.118 , Issue.2 , pp. 466
    • Heggeness, M.H.1
  • 16
    • 67650917906 scopus 로고    scopus 로고
    • The structure of a biologically active influenza virus ribonucleoprotein complex
    • Coloma, R. et al. The structure of a biologically active influenza virus ribonucleoprotein complex. PLoS Pathog 5(6), e1000491 (2009).
    • (2009) PLoS Pathog , vol.5 , Issue.6
    • Coloma, R.1
  • 17
    • 84871460710 scopus 로고    scopus 로고
    • The structure of native influenza virion ribonucleoproteins
    • Arranz, R. et al. The structure of native influenza virion ribonucleoproteins. Science 338(6114), 1634 (2012).
    • (2012) Science , vol.338 , Issue.6114 , pp. 1634
    • Arranz, R.1
  • 18
    • 0032505542 scopus 로고    scopus 로고
    • A classical bipartite nuclear localization signal on Thogoto and influenza A virus nucleoproteins
    • Weber, F., Kochs, G., Gruber, S. & Haller, O. A classical bipartite nuclear localization signal on Thogoto and influenza A virus nucleoproteins. Virology 250(1), 9 (1998).
    • (1998) Virology , vol.250 , Issue.1 , pp. 9
    • Weber, F.1    Kochs, G.2    Gruber, S.3    Haller, O.4
  • 19
    • 14544270958 scopus 로고    scopus 로고
    • An unconventional NLS is critical for the nuclear import of the influenza A virus nucleoprotein and ribonucleoprotein
    • Cros, J. F., Garcia-Sastre, A. & Palese, P. An unconventional NLS is critical for the nuclear import of the influenza A virus nucleoprotein and ribonucleoprotein. Traffic 6(3), 205 (2005).
    • (2005) Traffic , vol.6 , Issue.3 , pp. 205
    • Cros, J.F.1    Garcia-Sastre, A.2    Palese, P.3
  • 20
    • 33845724694 scopus 로고    scopus 로고
    • Contributions of two nuclear localization signals of influenza A virus nucleoprotein to viral replication
    • Ozawa, M. et al. Contributions of two nuclear localization signals of influenza A virus nucleoprotein to viral replication. J Virol 81(1), 30 (2007).
    • (2007) J Virol , vol.81 , Issue.1 , pp. 30
    • Ozawa, M.1
  • 21
    • 34250363900 scopus 로고    scopus 로고
    • Nuclear import of influenza A viral ribonucleoprotein complexes is mediated by two nuclear localization sequences on viral nucleoprotein
    • Wu, W. W., Sun, Y. H. & Pante, N., Nuclear import of influenza A viral ribonucleoprotein complexes is mediated by two nuclear localization sequences on viral nucleoprotein. Virol J 4, 49 (2007).
    • (2007) Virol J , vol.4 , pp. 49
    • Wu, W.W.1    Sun, Y.H.2    Pante, N.3
  • 22
    • 0029130751 scopus 로고
    • Nuclear import of influenza virus RNA can be mediated by viral nucleoprotein and transport factors required for protein import
    • O'Neill, R. E. et al. Nuclear import of influenza virus RNA can be mediated by viral nucleoprotein and transport factors required for protein import. J Biol Chem 270(39), 22701 (1995).
    • (1995) J Biol Chem , vol.270 , Issue.39 , pp. 22701
    • O'Neill, R.E.1
  • 23
    • 0031058042 scopus 로고    scopus 로고
    • The NPI-1/NPI-3 (karyopherin alpha) binding site on the influenza a virus nucleoprotein NP is a nonconventional nuclear localization signal
    • Wang, P., Palese, P. & O'Neill, R. E. The NPI-1/NPI-3 (karyopherin alpha) binding site on the influenza a virus nucleoprotein NP is a nonconventional nuclear localization signal. J Virol 71(3), 1850 (1997).
    • (1997) J Virol , vol.71 , Issue.3 , pp. 1850
    • Wang, P.1    Palese, P.2    O'Neill, R.E.3
  • 24
    • 33845406669 scopus 로고    scopus 로고
    • Role of ran binding protein 5 in nuclear import and assembly of the influenza virus RNA polymerase complex
    • Deng, T. et al. Role of ran binding protein 5 in nuclear import and assembly of the influenza virus RNA polymerase complex. J Virol 80(24), 11911 (2006).
    • (2006) J Virol , vol.80 , Issue.24 , pp. 11911
    • Deng, T.1
  • 25
    • 0041344551 scopus 로고    scopus 로고
    • Importin alpha nuclear localization signal binding sites for STAT1, STAT2 and influenza A virus nucleoprotein
    • Melen, K. et al. Importin alpha nuclear localization signal binding sites for STAT1, STAT2 and influenza A virus nucleoprotein. J Biol Chem 278(30), 28193 (2003).
    • (2003) J Biol Chem , vol.278 , Issue.30 , pp. 28193
    • Melen, K.1
  • 26
    • 0032472328 scopus 로고    scopus 로고
    • The influenza virus NEP (NS2 protein) mediates the nuclear export of viral ribonucleoproteins
    • O'Neill, R. E., Talon, J. & Palese, P. The influenza virus NEP (NS2 protein) mediates the nuclear export of viral ribonucleoproteins. The EMBO journal 17, 288-296, doi: 10.1093/emboj/17.1.288 (1998).
    • (1998) The EMBO Journal , vol.17 , pp. 288-296
    • O'Neill, R.E.1    Talon, J.2    Palese, P.3
  • 27
    • 84904497401 scopus 로고    scopus 로고
    • The nuclear export protein of H5N1 influenza A viruses recruits Matrix 1 (M1) protein to the viral ribonucleoprotein to mediate nuclear export
    • Brunotte, L. et al. The nuclear export protein of H5N1 influenza A viruses recruits Matrix 1 (M1) protein to the viral ribonucleoprotein to mediate nuclear export. The Journal of biological chemistry 289, 20067-20077, doi: 10.1074/jbc.M114.569178 (2014).
    • (2014) The Journal of Biological Chemistry , vol.289 , pp. 20067-20077
    • Brunotte, L.1
  • 28
    • 0034749515 scopus 로고    scopus 로고
    • Interaction of the influenza virus nucleoprotein with the cellular CRM1-mediated nuclear export pathway
    • Elton, D. et al. Interaction of the influenza virus nucleoprotein with the cellular CRM1-mediated nuclear export pathway. J Virol 75(1), 408 (2001).
    • (2001) J Virol , vol.75 , Issue.1 , pp. 408
    • Elton, D.1
  • 29
    • 0032568541 scopus 로고    scopus 로고
    • Role of the J-domain in the cooperation of Hsp40 with Hsp70
    • Greene, M. K., Maskos, K. & Landry, S. J. Role of the J-domain in the cooperation of Hsp40 with Hsp70. Proc Natl Acad Sci USA 95(11), 6108 (1998).
    • (1998) Proc Natl Acad Sci USA , vol.95 , Issue.11 , pp. 6108
    • Greene, M.K.1    Maskos, K.2    Landry, S.J.3
  • 30
    • 38349158107 scopus 로고    scopus 로고
    • Hsp40 facilitates nuclear import of the human immunodeficiency virus type 2 Vpx-mediated preintegration complex
    • Cheng, X., Belshan, M. & Ratner, L. Hsp40 facilitates nuclear import of the human immunodeficiency virus type 2 Vpx-mediated preintegration complex. J Virol 82(3), 1229 (2008).
    • (2008) J Virol , vol.82 , Issue.3 , pp. 1229
    • Cheng, X.1    Belshan, M.2    Ratner, L.3
  • 31
    • 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 81(3), 1339 (2007).
    • (2007) J Virol , vol.81 , Issue.3 , pp. 1339
    • Naito, T.1    Momose, F.2    Kawaguchi, A.3    Nagata, K.4
  • 32
    • 84896283707 scopus 로고    scopus 로고
    • Heat shock protein 70 modulates influenza A virus polymerase activity
    • Manzoor, R. et al. Heat shock protein 70 modulates influenza A virus polymerase activity. J Biol Chem 289(11), 7599 (2014).
    • (2014) J Biol Chem , vol.289 , Issue.11 , pp. 7599
    • Manzoor, R.1
  • 33
    • 0032981158 scopus 로고    scopus 로고
    • Modulation of nuclear localization of the influenza virus nucleoprotein through interaction with actin filaments
    • Digard, P. et al. Modulation of nuclear localization of the influenza virus nucleoprotein through interaction with actin filaments. J Virol 73(3), 2222 (1999).
    • (1999) J Virol , vol.73 , Issue.3 , pp. 2222
    • Digard, P.1
  • 34
    • 0035133124 scopus 로고    scopus 로고
    • Cellular splicing factor RAF-2p48/NPI-5/BAT1/UAP56 interacts with the influenza virus nucleoprotein and enhances viral RNA synthesis
    • Momose, F. et al. Cellular splicing factor RAF-2p48/NPI-5/BAT1/UAP56 interacts with the influenza virus nucleoprotein and enhances viral RNA synthesis. J Virol 75(4), 1899 (2001).
    • (2001) J Virol , vol.75 , Issue.4 , pp. 1899
    • Momose, F.1
  • 35
    • 84875875621 scopus 로고    scopus 로고
    • Influenza A virus nucleoprotein induces apoptosis in human airway epithelial cells: Implications of a novel interaction between nucleoprotein and host protein Clusterin
    • Tripathi, S. et al. Influenza A virus nucleoprotein induces apoptosis in human airway epithelial cells: implications of a novel interaction between nucleoprotein and host protein Clusterin. Cell Death Dis 4, e562 (2013).
    • (2013) Cell Death Dis , vol.4 , pp. e562
    • Tripathi, S.1
  • 36
    • 84884490302 scopus 로고    scopus 로고
    • Highly pathogenic avian influenza virus nucleoprotein interacts with TREX complex adaptor protein Aly/REF
    • Balasubramaniam, V. R. et al., Highly pathogenic avian influenza virus nucleoprotein interacts with TREX complex adaptor protein Aly/REF. PLoS One 8(9), e72429 (2013).
    • (2013) PLoS One , vol.8 , Issue.9
    • Balasubramaniam, V.R.1
  • 37
    • 84903820178 scopus 로고    scopus 로고
    • Influenza A viral nucleoprotein interacts with cytoskeleton scaffolding protein alpha-actinin-4 for viral replication
    • Sharma, S. et al. Influenza A viral nucleoprotein interacts with cytoskeleton scaffolding protein alpha-actinin-4 for viral replication. FEBS J 281(13), 2899 (2014).
    • (2014) FEBS J , vol.281 , Issue.13 , pp. 2899
    • Sharma, S.1
  • 38
    • 0014693884 scopus 로고
    • Distinct subunits of the ribonucleoprotein of influenza virus
    • Duesberg, P. H. Distinct subunits of the ribonucleoprotein of influenza virus. J Mol Biol 42(3), 485 (1969).
    • (1969) J Mol Biol , vol.42 , Issue.3 , pp. 485
    • Duesberg, P.H.1
  • 39
    • 0014591650 scopus 로고
    • And characterization of the ribonucleoprotein of influenza virus
    • Pons, M. W., Schulze, I. T., Hirst, G. K. & Hauser, R. Isolation and characterization of the ribonucleoprotein of influenza virus. Virology 39(2), 250 (1969).
    • (1969) Virology , vol.39 , Issue.2 , pp. 250
    • Pons, M.W.1    Schulze, I.T.2    Hirst, G.K.3    Hauser, R.I.4
  • 40
    • 0028275669 scopus 로고
    • Structure of influenza virus RNP. I. Influenza virus nucleoprotein melts secondary structure in panhandle RNA and exposes the bases to the solvent
    • Baudin, F., Bach, C., Cusack, S. & Ruigrok, R. W. Structure of influenza virus RNP. I. Influenza virus nucleoprotein melts secondary structure in panhandle RNA and exposes the bases to the solvent. EMBO J 13(13), 3158 (1994).
    • (1994) EMBO J , vol.13 , Issue.13 , pp. 3158
    • Baudin, F.1    Bach, C.2    Cusack, S.3    Ruigrok, R.W.4
  • 41
    • 0031469912 scopus 로고    scopus 로고
    • Hsp70 and Hsp40 chaperone activities in the cytoplasm and the nucleus of mammalian cells
    • Michels, A. A. et al. Hsp70 and Hsp40 chaperone activities in the cytoplasm and the nucleus of mammalian cells. J Biol Chem 272(52), 33283 (1997).
    • (1997) J Biol Chem , vol.272 , Issue.52 , pp. 33283
    • Michels, A.A.1
  • 42
    • 0014740350 scopus 로고
    • Developmental sequence and intracellular sites of synthesis of three structural protein antigens of influenza A2 virus
    • Maeno, K. & Kilbourne, E. D. Developmental sequence and intracellular sites of synthesis of three structural protein antigens of influenza A2 virus. Journal of virology 5, 153-164 (1970).
    • (1970) Journal of Virology , vol.5 , pp. 153-164
    • Maeno, K.1    Kilbourne, E.D.2
  • 43
    • 79960994652 scopus 로고    scopus 로고
    • Lysosome-associated membrane glycoprotein 3 is involved in influenza A virus replication in human lung epithelial (A549) cells
    • Zhou, Z. et al. Lysosome-associated membrane glycoprotein 3 is involved in influenza A virus replication in human lung epithelial (A549) cells. Virology journal 8, 384, doi: 10.1186/1743-422X-8-384 (2011).
    • (2011) Virology Journal , vol.8 , pp. 384
    • Zhou, Z.1
  • 44
    • 0028131905 scopus 로고
    • Molecular dissection of influenza virus nucleoprotein: Deletion mapping of the RNA binding domain
    • Kobayashi, M. et al. Molecular dissection of influenza virus nucleoprotein: deletion mapping of the RNA binding domain. J Virol 68(12), 8433 (1994).
    • (1994) J Virol , vol.68 , Issue.12 , pp. 8433
    • Kobayashi, M.1
  • 45
    • 0029069869 scopus 로고
    • Identification of an RNA binding region within the N-terminal third of the influenza A virus nucleoprotein
    • Albo, C., Valencia, A. & Portela, A. Identification of an RNA binding region within the N-terminal third of the influenza A virus nucleoprotein. J Virol 69(6), 3799 (1995).
    • (1995) J Virol , vol.69 , Issue.6 , pp. 3799
    • Albo, C.1    Valencia, A.2    Portela, A.3
  • 46
    • 0033587599 scopus 로고    scopus 로고
    • Oligomerization of the influenza virus nucleoprotein: Identification of positive and negative sequence elements
    • Elton, D., Medcalf, E., Bishop, K. & Digard, P. Oligomerization of the influenza virus nucleoprotein: identification of positive and negative sequence elements. Virology 260(1), 190 (1999).
    • (1999) Virology , vol.260 , Issue.1 , pp. 190
    • Elton, D.1    Medcalf, E.2    Bishop, K.3    Digard, P.4
  • 47
    • 33845890539 scopus 로고    scopus 로고
    • The mechanism by which influenza A virus nucleoprotein forms oligomers and binds RNA
    • Ye, Q., Krug, R. M. & Tao, Y. J. The mechanism by which influenza A virus nucleoprotein forms oligomers and binds RNA. Nature 444(7122), 1078 (2006).
    • (2006) Nature , vol.444 , Issue.7122 , pp. 1078
    • Ye, Q.1    Krug, R.M.2    Tao, Y.J.3
  • 48
    • 54049146687 scopus 로고    scopus 로고
    • Structure of the influenza virus A H5N1 nucleoprotein: Implications for RNA binding, oligomerization, and vaccine design
    • Ng, A. K. et al. Structure of the influenza virus A H5N1 nucleoprotein: implications for RNA binding, oligomerization, and vaccine design. FASEB J 22(10), 3638 (2008).
    • (2008) FASEB J , vol.22 , Issue.10 , pp. 3638
    • Ng, A.K.1
  • 49
    • 0034212740 scopus 로고    scopus 로고
    • Benzylidene lactam compound, KNK437, a novel inhibitor of acquisition of thermotolerance and heat shock protein induction in human colon carcinoma cells
    • Yokota, S., Kitahara, M. & Nagata, K. Benzylidene lactam compound, KNK437, a novel inhibitor of acquisition of thermotolerance and heat shock protein induction in human colon carcinoma cells. Cancer Res 60(11), 2942 (2000).
    • (2000) Cancer Res , vol.60 , Issue.11 , pp. 2942
    • Yokota, S.1    Kitahara, M.2    Nagata, K.3
  • 50
    • 77953259427 scopus 로고    scopus 로고
    • Identification of influenza A nucleoprotein as an antiviral target
    • Kao, R. Y. et al. Identification of influenza A nucleoprotein as an antiviral target. Nat Biotechnol 28(6), 600 (2010).
    • (2010) Nat Biotechnol , vol.28 , Issue.6 , pp. 600
    • Kao, R.Y.1
  • 51
    • 44949093451 scopus 로고    scopus 로고
    • Genetic compatibility and virulence of reassortants derived from contemporary avian H5N1 and human H3N2 influenza A viruses
    • Chen, L. M. et al. Genetic compatibility and virulence of reassortants derived from contemporary avian H5N1 and human H3N2 influenza A viruses. PLoS Pathog 4(5), e1000072 (2008).
    • (2008) PLoS Pathog , vol.4 , Issue.5
    • Chen, L.M.1
  • 52
    • 79952189030 scopus 로고    scopus 로고
    • Strand-specific real-time RT-PCR for distinguishing influenza vRNA, cRNA, and mRNA
    • Kawakami, E. et al. Strand-specific real-time RT-PCR for distinguishing influenza vRNA, cRNA, and mRNA. Journal of virological methods 173, 1-6, doi: 10.1016/j.jviromet.2010.12.014 (2011).
    • (2011) Journal of Virological Methods , vol.173 , pp. 1-6
    • Kawakami, E.1
  • 53
    • 0023935635 scopus 로고
    • Effect of dimethylsulfoxide (DMSO) on virus replication and maturation
    • Scholtissek, C. & Muller, K. Effect of dimethylsulfoxide (DMSO) on virus replication and maturation. Arch Virol 100(1-2), 27 (1988).
    • (1988) Arch Virol , vol.100 , Issue.1-2 , pp. 27
    • Scholtissek, C.1    Muller, K.2
  • 54
    • 0024263928 scopus 로고
    • RNA polymerase of influenza virus: Role of NP in RNA chain elongation
    • Honda, A., Ueda, K., Nagata, K. & Ishihama, A. RNA polymerase of influenza virus: role of NP in RNA chain elongation. Journal of biochemistry 104, 1021-1026 (1988).
    • (1988) Journal of Biochemistry , vol.104 , pp. 1021-1026
    • Honda, A.1    Ueda, K.2    Nagata, K.3    Ishihama, A.4
  • 55
    • 0037418322 scopus 로고    scopus 로고
    • RNA interference of influenza virus production by directly targeting mRNA for degradation and indirectly inhibiting all viral RNA transcription
    • Ge, Q. et al. RNA interference of influenza virus production by directly targeting mRNA for degradation and indirectly inhibiting all viral RNA transcription. Proceedings of the National Academy of Sciences of the United States of America 100, 2718-2723, doi: 10.1073/pnas.0437841100 (2003).
    • (2003) Proceedings of the National Academy of Sciences of the United States of America , vol.100 , pp. 2718-2723
    • Ge, Q.1
  • 56
    • 0029998889 scopus 로고    scopus 로고
    • Nuclear trafficking of influenza virus ribonuleoproteins in heterokaryons
    • Whittaker, G., Bui, M. & Helenius, A. Nuclear trafficking of influenza virus ribonuleoproteins in heterokaryons. Journal of virology 70, 2743-2756 (1996).
    • (1996) Journal of Virology , vol.70 , pp. 2743-2756
    • Whittaker, G.1    Bui, M.2    Helenius, A.3
  • 57
    • 84861325395 scopus 로고    scopus 로고
    • Identification and characterization of three novel nuclear export signals in the influenza A virus nucleoprotein
    • Yu, M. et al. Identification and characterization of three novel nuclear export signals in the influenza A virus nucleoprotein. Journal of virology 86, 4970-4980, doi: 10.1128/JVI.06159-11 (2012).
    • (2012) Journal of Virology , vol.86 , pp. 4970-4980
    • Yu, M.1
  • 58
    • 0026006258 scopus 로고
    • Nuclear transport of influenza virus ribonucleoproteins: The viral matrix protein (M1) promotes export and inhibits import
    • Martin, K. & Helenius, A. Nuclear transport of influenza virus ribonucleoproteins: the viral matrix protein (M1) promotes export and inhibits import. Cell 67, 117-130 (1991).
    • (1991) Cell , vol.67 , pp. 117-130
    • Martin, K.1    Helenius, A.2
  • 59
    • 0030731422 scopus 로고    scopus 로고
    • Nuclear import and export of influenza virus nucleoprotein
    • Neumann, G., Castrucci, M. R. & Kawaoka, Y. Nuclear import and export of influenza virus nucleoprotein. Journal of virology 71, 9690-9700 (1997).
    • (1997) Journal of Virology , vol.71 , pp. 9690-9700
    • Neumann, G.1    Castrucci, M.R.2    Kawaoka, Y.3
  • 60
    • 84870786354 scopus 로고    scopus 로고
    • A Hsp40 chaperone protein interacts with and modulates the cellular distribution of the primase protein of human cytomegalovirus
    • Pei, Y. et al. A Hsp40 chaperone protein interacts with and modulates the cellular distribution of the primase protein of human cytomegalovirus. PLoS pathogens 8, e1002968, doi: 10.1371/journal.ppat.1002968 (2012).
    • (2012) PLoS Pathogens , vol.8
    • Pei, Y.1
  • 61
    • 84862888248 scopus 로고    scopus 로고
    • Neuronal hypoxia induces Hsp40-mediated nuclear import of type 3 deiodinase as an adaptive mechanism to reduce cellular metabolism
    • Jo, S. et al. Neuronal hypoxia induces Hsp40-mediated nuclear import of type 3 deiodinase as an adaptive mechanism to reduce cellular metabolism. The Journal of neuroscience: the official journal of the Society for Neuroscience 32, 8491-8500, doi: 10.1523/JNEUROSCI.6514-11.2012 (2012).
    • (2012) The Journal of Neuroscience: the Official Journal of the Society for Neuroscience , vol.32 , pp. 8491-8500
    • Jo, S.1
  • 62
    • 67649845784 scopus 로고    scopus 로고
    • Systematic identification of cell cycle-dependent yeast nucleocytoplasmic shuttling proteins by prediction of composite motifs
    • Kosugi, S., Hasebe, M., Tomita, M. & Yanagawa, H. Systematic identification of cell cycle-dependent yeast nucleocytoplasmic shuttling proteins by prediction of composite motifs. Proc Natl Acad Sci USA 106(25), 10171 (2009).
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.25 , pp. 10171
    • Kosugi, S.1    Hasebe, M.2    Tomita, M.3    Yanagawa, H.4
  • 63
    • 84911478240 scopus 로고    scopus 로고
    • DnaJA1/Hsp40 is co-opted by influenza A virus to enhance its viral RNA polymerase activity
    • Cao, M. et al. DnaJA1/Hsp40 is co-opted by influenza A virus to enhance its viral RNA polymerase activity. J Virol 88(24), 14078 (2014).
    • (2014) J Virol , vol.88 , Issue.24 , pp. 14078
    • Cao, M.1
  • 64
    • 67649217159 scopus 로고    scopus 로고
    • Inhibiting the transcription factor HSF1 as an anticancer strategy
    • Whitesell, L. & Lindquist, S. Inhibiting the transcription factor HSF1 as an anticancer strategy. Expert Opin Ther Targets 13(4), 469 (2009).
    • (2009) Expert Opin Ther Targets , vol.13 , Issue.4 , pp. 469
    • Whitesell, L.1    Lindquist, S.2
  • 65
    • 84865618692 scopus 로고    scopus 로고
    • Inhibition of HSP70: A challenging anti-cancer strategy
    • Goloudina, A. R., Demidov, O. N. & Garrido, C. Inhibition of HSP70: a challenging anti-cancer strategy. Cancer Lett 325(2), 117 (2012).
    • (2012) Cancer Lett , vol.325 , Issue.2 , pp. 117
    • Goloudina, A.R.1    Demidov, O.N.2    Garrido, C.3


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