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Volumn 86, Issue 21, 2012, Pages 11815-11832

Flavivirus replication complex assembly revealed by DNAJC14 functional mapping

Author keywords

[No Author keywords available]

Indexed keywords

HEAT SHOCK PROTEIN 40; HYBRID PROTEIN; NONSTRUCTURAL PROTEIN 3; NONSTRUCTURAL PROTEIN 4B; PROTEIN DNAJC14; SCAFFOLD PROTEIN; UNCLASSIFIED DRUG;

EID: 84869077795     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.01022-12     Document Type: Article
Times cited : (43)

References (57)
  • 1
    • 2942715265 scopus 로고    scopus 로고
    • Characterization of the hepatitis C virus RNA replication complex associated with lipid rafts
    • Aizaki H, Lee KJ, Sung VM, Ishiko H, Lai MM. 2004. Characterization of the hepatitis C virus RNA replication complex associated with lipid rafts. Virology 324:450-461.
    • (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
    • 0035011489 scopus 로고    scopus 로고
    • Regulation of transport of the dopamine D1 receptor by a new membrane-associated ER protein
    • Bermak JC, Li M, Bullock C, Zhou QY. 2001. Regulation of transport of the dopamine D1 receptor by a new membrane-associated ER protein.Nat. Cell Biol. 3:492- 498.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 492-498
    • Bermak, J.C.1    Li, M.2    Bullock, C.3    Zhou, Q.Y.4
  • 3
    • 0036893332 scopus 로고    scopus 로고
    • Highly permissive cell lines for subgenomic and genomic hepatitis C virus RNA replication
    • Blight KJ, McKeating JA, Rice CM. 2002. Highly permissive cell lines for subgenomic and genomic hepatitis C virus RNA replication. J. Virol.76:13001-13014.
    • (2002) J. Virol. , vol.76 , pp. 13001-13014
    • Blight, K.J.1    Mckeating, J.A.2    Rice, C.M.3
  • 4
    • 0038325607 scopus 로고    scopus 로고
    • A stable full-length yellow fever virus cDNA clone and the role of conserved RNA elements in flavivirus replication
    • Bredenbeek PJ, et al. 2003. A stable full-length yellow fever virus cDNA clone and the role of conserved RNA elements in flavivirus replication. J.Gen. Virol. 84:1261-1268.
    • (2003) J.Gen. Virol. , vol.84 , pp. 1261-1268
    • Bredenbeek, P.J.1    Et al.2
  • 5
    • 0025309446 scopus 로고
    • Production of yellow fever virus proteins in infected cells: identification of discrete polyprotein species and analysis of cleavage kinetics using region-specific polyclonal antisera
    • Chambers TJ, McCourt DW, Rice CM. 1990. Production of yellow fever virus proteins in infected cells: identification of discrete polyprotein species and analysis of cleavage kinetics using region-specific polyclonal antisera.Virology 177:159 -174.
    • (1990) Virology , vol.177 , pp. 159-174
    • Chambers, T.J.1    Mccourt, D.W.2    Rice, C.M.3
  • 6
    • 0037015007 scopus 로고    scopus 로고
    • Cellular inhibitors with Fv1-like activity restrict human and simian immunodeficiency virus tropism
    • U.S. A.
    • Cowan S, et al. 2002. Cellular inhibitors with Fv1-like activity restrict human and simian immunodeficiency virus tropism. Proc. Natl. Acad.Sci. U.S.A. 99:11914 -11919.
    • (2002) Proc. Natl. Acad.Sci. , vol.99 , pp. 11914-11919
    • Cowan, S.1    Et al.2
  • 8
    • 0028832822 scopus 로고
    • Understanding, improving and using green fluorescent proteins
    • Cubitt AB, et al. 1995. Understanding, improving and using green fluorescent proteins. Trends Biochem. Sci. 20:448-455.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 448-455
    • Cubitt, A.B.1    Et al.2
  • 9
    • 77957957039 scopus 로고    scopus 로고
    • Organelle-like membrane compartmentalization of positive-strand RNA virus replication factories
    • den Boon JA, Ahlquist P. 2010. Organelle-like membrane compartmentalization of positive-strand RNA virus replication factories. Annu. Rev.Microbiol. 64:241-256.
    • (2010) Annu.Rev.Microbiol. , vol.64 , pp. 241-256
    • Den boon, J.A.1    Ahlquist, P.2
  • 10
    • 84856894606 scopus 로고    scopus 로고
    • Bromovirus RNA replication compartment formation requires concerted action of 1a's self-interacting RNA capping and helicase domains
    • Diaz A, Gallei A, Ahlquist P. 2012. Bromovirus RNA replication compartment formation requires concerted action of 1a's self-interacting RNA capping and helicase domains. J. Virol. 86:821- 834.
    • (2012) J.Virol. , vol.86 , pp. 821-834
    • Diaz, A.1    Gallei, A.2    Ahlquist, P.3
  • 11
    • 77958004276 scopus 로고    scopus 로고
    • Membrane-shaping host reticulon proteins play crucial roles in viral RNA replication compartment formation and function
    • Diaz A, Wang X, Ahlquist P. 2010. Membrane-shaping host reticulon proteins play crucial roles in viral RNA replication compartment formation and function. Proc. Natl. Acad. Sci. U.S.A. 107:16291-16296.
    • (2010) Proc.Natl.Acad.Sci. , vol.107 , pp. 16291-16296
    • Diaz, A.1    Wang, X.2    Ahlquist, P.3
  • 12
    • 20444404267 scopus 로고    scopus 로고
    • Single-molecule microscopy reveals plasma membrane microdomains created by protein-protein networks that exclude or trap signaling molecules in T cells
    • Douglass AD, Vale RD. 2005. Single-molecule microscopy reveals plasma membrane microdomains created by protein-protein networks that exclude or trap signaling molecules in T cells. Cell 121:937-950.
    • (2005) Cell , vol.121 , pp. 937-950
    • Douglass, A.D.1    Vale, R.D.2
  • 13
    • 34147219730 scopus 로고    scopus 로고
    • Claudin-1 is a hepatitis C virus co-receptor required for a late step in entry
    • Evans MJ, et al. 2007. Claudin-1 is a hepatitis C virus co-receptor required for a late step in entry. Nature 446:801- 805.
    • (2007) Nature , vol.446 , pp. 801-805
    • Evans, M.J.1    Et al.2
  • 14
    • 42049116064 scopus 로고    scopus 로고
    • Colocalization of fluorescent markers in confocal microscope images of plant cells
    • French AP, Mills S, Swarup R, Bennett MJ, Pridmore TP. 2008. Colocalization of fluorescent markers in confocal microscope images of plant cells. Nat. Protoc. 3:619-628.
    • (2008) Nat.Protoc. , vol.3 , pp. 619-628
    • French, A.P.1    Mills, S.2    Swarup, R.3    Bennett, M.J.4    Pridmore, T.P.5
  • 15
    • 77957201605 scopus 로고    scopus 로고
    • The endoplasmic reticulum provides the membrane platform for biogenesis of the flavivirus replication complex.
    • Gillespie LK, Hoenen A, Morgan G, Mackenzie JM. 2010. The endoplasmic reticulum provides the membrane platform for biogenesis of the flavivirus replication complex. J. Virol. 84:10438-10447.
    • (2010) J. Virol. , vol.84 , pp. 10438-10447
    • Gillespie, L.K.1    Hoenen, A.2    Morgan, G.3    Mackenzie, J.M.4
  • 16
    • 38849209154 scopus 로고    scopus 로고
    • Pathogenic flaviviruses
    • Gould EA, Solomon T. 2008. Pathogenic flaviviruses. Lancet 371:500-509.
    • (2008) Lancet , vol.371 , pp. 500-509
    • Gould, E.A.1    Solomon, T.2
  • 17
    • 35348925573 scopus 로고    scopus 로고
    • In Knipe DM. Howley PM (ed), Fields virology, fifth ed Lippincott Williams & Lippincott Williams &Wilkins, Philadelphia,PA Wilkins, Philadelphia,PA
    • Gubler DJ, Kuno G, Markoff L. 2007. Flaviviruses, p 1153-1252. In Knipe DM, Howley PM (ed), Fields virology, fifth ed, vol 1. Lippincott Williams & Wilkins, Philadelphia, PA.
    • (2007) Flaviviruses , pp. 1153-1252
    • Gubler, D.J.1    Kuno, G.2    Markoff, L.3
  • 18
    • 77958100661 scopus 로고    scopus 로고
    • Dengue virus nonstructural protein 3 redistributes fatty acid synthase to sites of viral replication and increases cellular fatty acid synthesis
    • Heaton NS, et al. 2010. Dengue virus nonstructural protein 3 redistributes fatty acid synthase to sites of viral replication and increases cellular fatty acid synthesis. Proc. Natl. Acad. Sci. U.S.A. 107:17345-17350.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 17345-17350
    • Heaton, N.S.1    Et al.2
  • 19
    • 78349237370 scopus 로고    scopus 로고
    • Dengue virus-induced autophagy regulates lipid metabolism
    • Heaton NS, Randall G. 2010. Dengue virus-induced autophagy regulates lipid metabolism. Cell Host Microbe 8:422- 432.
    • (2010) Cell Host Microbe , vol.8 , pp. 422-432
    • Heaton, N.S.1    Randall, G.2
  • 20
    • 79959882330 scopus 로고    scopus 로고
    • Multifaceted roles for lipids in viral infection
    • Heaton NS, Randall G. 2011. Multifaceted roles for lipids in viral infection.Trends Microbiol. 19:368 -375.
    • (2011) Trends Microbiol. , vol.19 , pp. 368-375
    • Heaton, N.S.1    Randall, G.2
  • 21
    • 77953280422 scopus 로고    scopus 로고
    • Viral reorganization of the secretory pathway generates distinct organelles for RNA replication
    • Hsu NY, et al. 2010. Viral reorganization of the secretory pathway generates distinct organelles for RNA replication. Cell 141:799-811.
    • (2010) Cell , vol.141 , pp. 799-811
    • Hsu, N.Y.1
  • 22
    • 76349104162 scopus 로고    scopus 로고
    • Real-time imaging of hepatitis C virus infection 7using a fluorescent cell-based reporter system
    • Jones CT, et al. 2010. Real-time imaging of hepatitis C virus infection 7using a fluorescent cell-based reporter system. Nat. Biotechnol. 28:167-171.
    • (2010) Nat.Biotechnol. , vol.28 , pp. 167-171
    • Jones, C.T.1
  • 23
    • 77954947810 scopus 로고    scopus 로고
    • The HSP70 chaperone machinery: J proteins as drivers of functional specificity
    • Kampinga HH, Craig EA. 2010. The HSP70 chaperone machinery: J proteins as drivers of functional specificity. Nat. Rev. Mol. Cell Biol. 11:579-592
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 579-592
    • Kampinga, H.H.1    Craig, E.A.2
  • 24
    • 0032103439 scopus 로고    scopus 로고
    • The J-domain family and the recruitment of chaperone power
    • Kelley WL. 1998. The J-domain family and the recruitment of chaperone power. Trends Biochem. Sci. 23:222-227.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 222-227
    • Kelley, W.L.1
  • 25
    • 54749157085 scopus 로고    scopus 로고
    • SARS-coronavirus replication is supported by a reticulovesicular network of modified endoplasmic reticulum
    • doi:10.1371/journal.pbio.0060226
    • Knoops K, et al. 2008. SARS-coronavirus replication is supported by a reticulovesicular network of modified endoplasmic reticulum. PLoS Biol.6:e226. doi:10.1371/journal.pbio.0060226.
    • (2008) PLoS Biol. , vol.6
    • Knoops, K.1
  • 26
    • 0036232747 scopus 로고    scopus 로고
    • Mutations in the yellow fever virus nonstructural protein NS2A selectively block production of infectious particles
    • Kümmerer BM, Rice CM. 2002. Mutations in the yellow fever virus nonstructural protein NS2A selectively block production of infectious particles. J. Virol. 76:4773- 4784.
    • (2002) J. Virol. , vol.76 , pp. 4773-4784
    • Kümmerer, B.M.1    Rice, C.M.2
  • 27
    • 31944434363 scopus 로고    scopus 로고
    • Dissection of a viral autoprotease elucidates a function of a cellular chaperone in proteolysis
    • U.S.A.
    • Lackner T, Thiel HJ, Tautz N. 2006. Dissection of a viral autoprotease elucidates a function of a cellular chaperone in proteolysis. Proc. Natl. Acad. Sci. U.S.A. 103:1510-1515.
    • (2006) Proc. Natl. Acad. Sci. , vol.103 , pp. 1510-1515
    • Lackner, T.1    Thiel, H.J.2    Tautz, N.3
  • 28
    • 13744258758 scopus 로고    scopus 로고
    • The predominant mechanism by which ribavirin exerts its antiviral activity in vitro against flaviviruses and paramyxoviruses is mediated by inhibition of IMP dehydrogenase.
    • Leyssen P, Balzarini J, De Clercq E, Neyts J. 2005. The predominant mechanism by which ribavirin exerts its antiviral activity in vitro against flaviviruses and paramyxoviruses is mediated by inhibition of IMP dehydrogenase.J. Virol. 79:1943-1947.
    • (2005) J. Virol. , vol.79 , pp. 1943-1947
    • Leyssen, P.1    Balzarini, J.2    De Clercq, E.3    Neyts, J.4
  • 29
    • 0030774240 scopus 로고    scopus 로고
    • trans-complementation of yellow fever virus NS1 reveals a role in early RNA replication
    • Lindenbach BD, Rice CM. 1997. trans-complementation of yellow fever virus NS1 reveals a role in early RNA replication. J. Virol. 71:9608-9617.
    • (1997) J. Virol. , vol.71 , pp. 9608-9617
    • Lindenbach, B.D.1    Rice, C.M.2
  • 30
    • 34748873170 scopus 로고    scopus 로고
    • Flaviviridae: the viruses and their replication
    • In (ed), Fields virology, fifth ed, Lippincott Williams &Wilkins, Philadelphia, PA
    • Lindenbach BD, Thiel H-J, Rice CM. 2007. Flaviviridae: the viruses and their replication, p 1101-1152. In Knipe DM, Howley PM (ed), Fields virology, fifth ed, vol 1. Lippincott, Williams &Wilkins, Philadelphia, PA.
    • (2007) , vol.1 , pp. 1101-1152
    • Lindenbach, B.D.1    Thiel, H.J.2    Rice, C.M.3    Knipe, D.M.4    Howley, P.M.5
  • 31
    • 74849118341 scopus 로고    scopus 로고
    • Lipid rafts as a membrane-organizing principle
    • Lingwood D, Simons K. 2010. Lipid rafts as a membrane-organizing principle. Science 327:46-50.
    • (2010) Science , vol.327 , pp. 46-50
    • Lingwood, D.1    Simons, K.2
  • 32
    • 0037150679 scopus 로고    scopus 로고
    • Visualization and functional analysis of RNA-dependent RNA polymerase lattices
    • Lyle JM, Bullitt E, Bienz K, Kirkegaard K. 2002. Visualization and functional analysis of RNA-dependent RNA polymerase lattices. Science 296:2218-2222.
    • (2002) Science , vol.296 , pp. 2218-2222
    • Lyle, J.M.1    Bullitt, E.2    Bienz, K.3    Kirkegaard, K.4
  • 33
    • 34848900462 scopus 로고    scopus 로고
    • Cholesterol manipulation by West Nile virus perturbs the cellular immune response
    • Mackenzie JM, Khromykh AA, Parton RG. 2007. Cholesterol manipulation by West Nile virus perturbs the cellular immune response. Cell Host Microbe 2:229-239.
    • (2007) Cell Host Microbe , vol.2 , pp. 229-239
    • Mackenzie, J.M.1    Khromykh, A.A.2    Parton, R.G.3
  • 34
    • 34247848008 scopus 로고    scopus 로고
    • The non-structural protein 4A of dengue virus is an integral membrane protein inducing membrane alterations in a 2K-regulated manner
    • Miller S, Kastner S, Krijnse-Locker J, Buhler S, Bartenschlager R. 2007. The non-structural protein 4A of dengue virus is an integral membrane protein inducing membrane alterations in a 2K-regulated manner. J. Biol. Chem. 282:8873-8882.
    • (2007) J. Biol. Chem. , vol.282 , pp. 8873-8882
    • Miller, S.1    Kastner, S.2    Krijnse-Locker, J.3    Buhler, S.4    Bartenschlager, R.5
  • 35
    • 42349086670 scopus 로고    scopus 로고
    • Modification of intracellular membrane structures for virus replication
    • Miller S, Krijnse-Locker J. 2008. Modification of intracellular membrane structures for virus replication. Nat. Rev. Microbiol. 6:363-374.
    • (2008) Nat. Rev. Microbiol. , vol.6 , pp. 363-374
    • Miller, S.1    Krijnse-Locker, J.2
  • 36
    • 0346118919 scopus 로고    scopus 로고
    • Hepatitis C virus non-structural proteins in the probable membranous compartment function in viral genome replication
    • Miyanari Y, et al. 2003. Hepatitis C virus non-structural proteins in the probable membranous compartment function in viral genome replication. J. Biol. Chem. 278:50301-50308.
    • (2003) J. Biol. Chem. , vol.278 , pp. 50301-50308
    • Miyanari, Y.1
  • 37
    • 84855875985 scopus 로고    scopus 로고
    • The dependence of viral RNA replication on co-opted host factors
    • Nagy PD, Pogany J. 2012. The dependence of viral RNA replication on co-opted host factors. Nat. Rev. Microbiol. 10:137-149.
    • (2012) Nat. Rev. Microbiol. , vol.10 , pp. 137-149
    • Nagy, P.D.1    Pogany, J.2
  • 38
    • 0035813034 scopus 로고    scopus 로고
    • Recombination with a cellular mRNA encoding a novel DnaJ protein results in biotype conversion in genotype 2 bovine viral diarrhea viruses
    • Neill JD, Ridpath JF. 2001. Recombination with a cellular mRNA encoding a novel DnaJ protein results in biotype conversion in genotype 2 bovine viral diarrhea viruses. Virus Res. 79:59-69.
    • (2001) Virus Res. , vol.79 , pp. 59-69
    • Neill, J.D.1    Ridpath, J.F.2
  • 39
    • 54449096215 scopus 로고    scopus 로고
    • Association of dengue virus NS1 protein with lipid rafts
    • Noisakran S, et al. 2008. Association of dengue virus NS1 protein with lipid rafts. J. Gen. Virol. 89:2492-2500.
    • (2008) J. Gen. Virol. , vol.89 , pp. 2492-2500
    • Noisakran, S.1
  • 40
    • 0035809923 scopus 로고    scopus 로고
    • Accumulation of caveolin in the endoplasmic reticulum redirects the protein to lipid storage droplets
    • Ostermeyer AG, et al. 2001. Accumulation of caveolin in the endoplasmic reticulum redirects the protein to lipid storage droplets. J. Cell Biol. 152: 1071-1078.
    • (2001) J. Cell Biol. , vol.152 , pp. 1071-1078
    • Ostermeyer, A.G.1
  • 41
    • 79960406328 scopus 로고    scopus 로고
    • NS4B self-interaction through conserved C-terminal elements is required for the establishment of functional hepatitis C virus replication complexes
    • Paul D, et al. 2011. NS4B self-interaction through conserved C-terminal elements is required for the establishment of functional hepatitis C virus replication complexes. J. Virol. 85:6963-6976.
    • (2011) J. Virol. , vol.85 , pp. 6963-6976
    • Paul, D.1
  • 42
    • 27144513392 scopus 로고    scopus 로고
    • Quantitative analysis of the hepatitis C virus replication complex
    • Quinkert D, Bartenschlager R, Lohmann V. 2005. Quantitative analysis of the hepatitis C virus replication complex. J. Virol. 79:13594-13605.
    • (2005) J. Virol. , vol.79 , pp. 13594-13605
    • Quinkert, D.1    Bartenschlager, R.2    Lohmann, V.3
  • 43
    • 78751512667 scopus 로고    scopus 로고
    • Recruitment and activation of a lipid kinase by hepatitis C virus NS5A is essential for integrity of the membranous replication compartment
    • Reiss S, et al. 2011. Recruitment and activation of a lipid kinase by hepatitis C virus NS5A is essential for integrity of the membranous replication compartment. Cell Host Microbe 9:32-45.
    • (2011) Cell Host Microbe , vol.9 , pp. 32-45
    • Reiss, S.1
  • 44
    • 0034856181 scopus 로고    scopus 로고
    • A cellular J-domain protein modulates polyprotein processing and cytopathogenicity of a pestivirus
    • Rinck G, et al. 2001. A cellular J-domain protein modulates polyprotein processing and cytopathogenicity of a pestivirus. J. Virol. 75:9470-9482.
    • (2001) J. Virol. , vol.75 , pp. 9470-9482
    • Rinck, G.1
  • 45
    • 33646167045 scopus 로고    scopus 로고
    • Regulated cleavages at the West Nile virus NS4A-2K-NS4B junctions play a major role in rearranging cytoplasmic membranes and Golgi trafficking of the NS4A protein
    • Roosendaal J, Westaway EG, Khromykh A, Mackenzie JM. 2006. Regulated cleavages at the West Nile virus NS4A-2K-NS4B junctions play a major role in rearranging cytoplasmic membranes and Golgi trafficking of the NS4A protein. J. Virol. 80:4623-4632.
    • (2006) J. Virol. , vol.80 , pp. 4623-4632
    • Roosendaal, J.1    Westaway, E.G.2    Khromykh, A.3    Mackenzie, J.M.4
  • 47
    • 0037379425 scopus 로고    scopus 로고
    • Hepatitis C virus RNA replication occurs on a detergent-resistant membrane that cofractionates with caveolin-2
    • Shi ST, Lee KJ, Aizaki H, Hwang SB, Lai MM. 2003. Hepatitis C virus RNA replication occurs on a detergent-resistant membrane that cofractionates with caveolin-2. J. Virol. 77:4160-4168.
    • (2003) J. Virol. , vol.77 , pp. 4160-4168
    • Shi, S.T.1    Lee, K.J.2    Aizaki, H.3    Hwang, S.B.4    Lai, M.M.5
  • 48
    • 79952084705 scopus 로고    scopus 로고
    • Role of cellular lipids in positive-sense RNA virus replication complex assembly and function.
    • Stapleford KA, Miller DJ. 2010. Role of cellular lipids in positive-sense RNA virus replication complex assembly and function. Viruses 2:1055-1068.
    • (2010) Viruses , vol.2 , pp. 1055-1068
    • Stapleford, K.A.1    Miller, D.J.2
  • 49
    • 39749119301 scopus 로고    scopus 로고
    • Visualization of double-stranded RNA in cells supporting hepatitis C virus RNA replication
    • Targett-Adams P, Boulant S, McLauchlan J. 2008. Visualization of double-stranded RNA in cells supporting hepatitis C virus RNA replication. J.Virol. 82:2182-2195.
    • (2008) J.Virol , vol.82 , pp. 2182-2195
    • Targett-Adams, P.1    Boulant, S.2    McLauchlan, J.3
  • 50
    • 0036253771 scopus 로고    scopus 로고
    • The Chediak-Higashi protein interacts with SNARE complex and signal transduction proteins
    • Tchernev VT, et al. 2002. The Chediak-Higashi protein interacts with SNARE complex and signal transduction proteins. Mol. Med. 8:56-64.
    • (2002) Mol. Med. , vol.8 , pp. 56-64
    • Tchernev, V.T.1
  • 51
    • 0042591335 scopus 로고    scopus 로고
    • Architecture of the flaviviral replication complex. Protease, nuclease, and detergents reveal encasement within double-layered membrane compartments
    • Uchil PD, Satchidanandam V. 2003. Architecture of the flaviviral replication complex. Protease, nuclease, and detergents reveal encasement within double-layered membrane compartments. J. Biol. Chem. 278:24388-24398.
    • (2003) J. Biol. Chem. , vol.278 , pp. 24388-24398
    • Uchil, P.D.1    Satchidanandam, V.2
  • 52
    • 46849116411 scopus 로고    scopus 로고
    • Structural and functional diversities between members of the human HSPB, HSPH, HSPA, and DNAJ chaperone families
    • Vos MJ, Hageman J, Carra S, Kampinga HH. 2008. Structural and functional diversities between members of the human HSPB, HSPH, HSPA, and DNAJ chaperone families. Biochemistry 47:7001-7011.
    • (2008) Biochemistry , vol.47 , pp. 7001-7011
    • Vos, M.J.1    Hageman, J.2    Carra, S.3    Kampinga, H.H.4
  • 53
    • 33644622698 scopus 로고    scopus 로고
    • In Chalfie M, Kain S.R. (ed)Green fluorescent protein: properties,applications, and protocols 2nd ed. John Wiley & Sons, Inc.,Hoboken N.J.
    • Ward WW. 2006. Biochemical and physical properties of green fluorescent protein, p 39-65. In Chalfie M, Kain SR (ed), Green fluorescent protein: properties, applications, and protocols, vol 47, 2nd ed. John Wiley & Sons, Inc., Hoboken, NJ.
    • (2006) Biochemical and physical properties of green fluorescent protein , vol.47
    • Ward, W.W.1
  • 54
    • 64649097038 scopus 로고    scopus 로고
    • Composition and three-dimensional architecture of the dengue virus replication and assembly sites
    • Welsch S, et al. 2009. Composition and three-dimensional architecture of the dengue virus replication and assembly sites. Cell Host Microbe 5:365-375.
    • (2009) Cell Host Microbe , vol.5 , pp. 365-375
    • Welsch, S.1
  • 55
    • 4444270620 scopus 로고    scopus 로고
    • Newly synthesized hepatitis C virus replicon RNA is protected from nuclease activity by a protease-sensitive factors
    • Yang G, et al. 2004. Newly synthesized hepatitis C virus replicon RNA is protected from nuclease activity by a protease-sensitive factor(s). J. Virol. 78:10202-10205.
    • (2004) J. Virol. , vol.78 , pp. 10202-10205
    • Yang, G.1
  • 56
    • 79551513993 scopus 로고    scopus 로고
    • Identification and characterization of the host protein DNAJC14 as a broadly active flavivirus replication modulator
    • doi:10.1371/journal.ppat.1001255
    • Yi Z, et al. 2011. Identification and characterization of the host protein DNAJC14 as a broadly active flavivirus replication modulator. PLoS Pathog. 7:e1001255. doi:10.1371/journal.ppat.1001255.
    • (2011) PLoS Pathog
    • Yi, Z.1
  • 57
    • 0034646513 scopus 로고    scopus 로고
    • HIV-1 genome nuclear import is mediated by a central DNA flap
    • Zennou V, et al. 2000. HIV-1 genome nuclear import is mediated by a central DNA flap. Cell 101:173-185.
    • (2000) Cell , vol.101 , pp. 173-185
    • Zennou, V.1


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