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Volumn 6, Issue 10, 2011, Pages

Viral double-strand RNA-binding proteins can enhance innate immune signaling by toll-like receptor 3

Author keywords

[No Author keywords available]

Indexed keywords

DOUBLE STRANDED RNA; LUCIFERASE; POLYINOSINIC POLYCYTIDYLIC ACID; RNA BINDING PROTEIN; RNA POLYMERASE; TOLL LIKE RECEPTOR 3; VIRUS RNA; CAPSID PROTEIN; RNA DIRECTED RNA POLYMERASE; TLR3 PROTEIN, HUMAN; VIRUS PROTEIN;

EID: 80053922801     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0025837     Document Type: Article
Times cited : (30)

References (73)
  • 1
    • 78449269327 scopus 로고    scopus 로고
    • Plant and animal sensors of conserved microbial signatures
    • Ronald PC, Beutler B, (2010) Plant and animal sensors of conserved microbial signatures. Science 330: 1061-1064.
    • (2010) Science , vol.330 , pp. 1061-1064
    • Ronald, P.C.1    Beutler, B.2
  • 2
    • 31344461659 scopus 로고    scopus 로고
    • Innate immune recognition of viral infection
    • Kawai T, Akira S, (2006) Innate immune recognition of viral infection. Nat Immunol 7: 131-137.
    • (2006) Nat Immunol , vol.7 , pp. 131-137
    • Kawai, T.1    Akira, S.2
  • 3
    • 33746028777 scopus 로고    scopus 로고
    • Intracellular pattern recognition receptors in the host response
    • Meylan E, Tschopp J, Karin M, (2006) Intracellular pattern recognition receptors in the host response. Nature 442: 39-44.
    • (2006) Nature , vol.442 , pp. 39-44
    • Meylan, E.1    Tschopp, J.2    Karin, M.3
  • 4
    • 77957997708 scopus 로고    scopus 로고
    • Preference of RIG-I for short viral RNA molecules in infected cells revealed by next-generation sequencing
    • Baum A, Sachidanandam R, Garcia-Sastre A, (2010) Preference of RIG-I for short viral RNA molecules in infected cells revealed by next-generation sequencing. Proc Natl Acad Sci U S A 107: 16303-16308.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 16303-16308
    • Baum, A.1    Sachidanandam, R.2    Garcia-Sastre, A.3
  • 5
    • 77950476766 scopus 로고    scopus 로고
    • Sensing and signaling in antiviral innate immunity
    • O'Neill LA, Bowie AG, (2010) Sensing and signaling in antiviral innate immunity. Curr Biol 20: R328-333.
    • (2010) Curr Biol , vol.20
    • O'Neill, L.A.1    Bowie, A.G.2
  • 6
    • 34548459868 scopus 로고    scopus 로고
    • Structure and function of Toll receptors and their ligands
    • Gay NJ, Gangloff M, (2007) Structure and function of Toll receptors and their ligands. Annu Rev Biochem 76: 141-165.
    • (2007) Annu Rev Biochem , vol.76 , pp. 141-165
    • Gay, N.J.1    Gangloff, M.2
  • 7
    • 33645982220 scopus 로고    scopus 로고
    • A missense mutation of the Toll-like receptor 3 gene in a patient with influenza-associated encephalopathy
    • Hidaka F, Matsuo S, Muta T, Takeshige K, Mizukami T, et al. (2006) A missense mutation of the Toll-like receptor 3 gene in a patient with influenza-associated encephalopathy. Clin Immunol 119: 188-194.
    • (2006) Clin Immunol , vol.119 , pp. 188-194
    • Hidaka, F.1    Matsuo, S.2    Muta, T.3    Takeshige, K.4    Mizukami, T.5
  • 8
    • 34548699323 scopus 로고    scopus 로고
    • TLR3 deficiency in patients with herpes simplex encephalitis
    • Zhang SY, Jouanguy E, Ugolini S, Smahi A, Elain G, et al. (2007) TLR3 deficiency in patients with herpes simplex encephalitis. Science 317: 1522-1527.
    • (2007) Science , vol.317 , pp. 1522-1527
    • Zhang, S.Y.1    Jouanguy, E.2    Ugolini, S.3    Smahi, A.4    Elain, G.5
  • 9
    • 34547126686 scopus 로고    scopus 로고
    • Effects of single nucleotide polymorphisms on Toll-like receptor 3 activity and expression in cultured cells
    • Ranjith-Kumar CT, Miller W, Sun J, Xiong J, Santos J, et al. (2007) Effects of single nucleotide polymorphisms on Toll-like receptor 3 activity and expression in cultured cells. J Biol Chem 282: 17696-17705.
    • (2007) J Biol Chem , vol.282 , pp. 17696-17705
    • Ranjith-Kumar, C.T.1    Miller, W.2    Sun, J.3    Xiong, J.4    Santos, J.5
  • 10
    • 79551469099 scopus 로고    scopus 로고
    • The L412F variant of Toll-like receptor 3 (TLR3) is associated with cutaneous candidiasis, increased susceptibility to cytomegalovirus, and autoimmunity
    • Nahum A, Dadi H, Bates A, Roifman CM, (2011) The L412F variant of Toll-like receptor 3 (TLR3) is associated with cutaneous candidiasis, increased susceptibility to cytomegalovirus, and autoimmunity. J Allergy Clin Immunol 127: 528-531.
    • (2011) J Allergy Clin Immunol , vol.127 , pp. 528-531
    • Nahum, A.1    Dadi, H.2    Bates, A.3    Roifman, C.M.4
  • 11
    • 77955425319 scopus 로고    scopus 로고
    • Dissecting TLR3 signalling in dendritic cells
    • Gauzzi MC, Del Corno M, Gessani S, (2010) Dissecting TLR3 signalling in dendritic cells. Immunobiology 215: 713-723.
    • (2010) Immunobiology , vol.215 , pp. 713-723
    • Gauzzi, M.C.1    Del Corno, M.2    Gessani, S.3
  • 14
    • 65649111529 scopus 로고    scopus 로고
    • Predicting Toll-like receptor structures and characterizing ligand binding
    • Leonard JN, Bell JK, Segal DM, (2009) Predicting Toll-like receptor structures and characterizing ligand binding. Methods Mol Biol 517: 55-67.
    • (2009) Methods Mol Biol , vol.517 , pp. 55-67
    • Leonard, J.N.1    Bell, J.K.2    Segal, D.M.3
  • 16
    • 34147116078 scopus 로고    scopus 로고
    • Biochemical and functional analyses of the human Toll-like receptor 3 ectodomain
    • Ranjith-Kumar CT, Miller W, Xiong J, Russell WK, Lamb R, et al. (2007) Biochemical and functional analyses of the human Toll-like receptor 3 ectodomain. J Biol Chem 282: 7668-7678.
    • (2007) J Biol Chem , vol.282 , pp. 7668-7678
    • Ranjith-Kumar, C.T.1    Miller, W.2    Xiong, J.3    Russell, W.K.4    Lamb, R.5
  • 18
    • 80053925779 scopus 로고    scopus 로고
    • LL37 and cationic peptides enhance TLR3 signaling by viral double-stranded RNAs (submitted)
    • Lai Y, Adhikarakunnathu S, Bhardwaj K, Ranjith-Kumar CT, Wen Y, et al. (2011) LL37 and cationic peptides enhance TLR3 signaling by viral double-stranded RNAs (submitted).
    • (2011)
    • Lai, Y.1    Adhikarakunnathu, S.2    Bhardwaj, K.3    Ranjith-Kumar, C.T.4    Wen, Y.5
  • 21
    • 0034468107 scopus 로고    scopus 로고
    • Template requirements for RNA synthesis by a recombinant hepatitis C virus RNA-dependent RNA polymerase
    • Kao CC, Yang X, Kline A, Wang QM, Barket D, et al. (2000) Template requirements for RNA synthesis by a recombinant hepatitis C virus RNA-dependent RNA polymerase. J Virol 74: 11121-11128.
    • (2000) J Virol , vol.74 , pp. 11121-11128
    • Kao, C.C.1    Yang, X.2    Kline, A.3    Wang, Q.M.4    Barket, D.5
  • 22
    • 0033989278 scopus 로고    scopus 로고
    • De novo initiation of RNA synthesis by the RNA-dependent RNA polymerase (NS5B) of hepatitis C virus
    • Luo G, Hamatake RK, Mathis DM, Racela J, Rigat KL, et al. (2000) De novo initiation of RNA synthesis by the RNA-dependent RNA polymerase (NS5B) of hepatitis C virus. J Virol 74: 851-863.
    • (2000) J Virol , vol.74 , pp. 851-863
    • Luo, G.1    Hamatake, R.K.2    Mathis, D.M.3    Racela, J.4    Rigat, K.L.5
  • 23
    • 0036893141 scopus 로고    scopus 로고
    • Mechanism of de novo initiation by the hepatitis C virus RNA-dependent RNA polymerase: role of divalent metals
    • Ranjith-Kumar CT, Kim YC, Gutshall L, Silverman C, Khandekar S, et al. (2002) Mechanism of de novo initiation by the hepatitis C virus RNA-dependent RNA polymerase: role of divalent metals. J Virol 76: 12513-12525.
    • (2002) J Virol , vol.76 , pp. 12513-12525
    • Ranjith-Kumar, C.T.1    Kim, Y.C.2    Gutshall, L.3    Silverman, C.4    Khandekar, S.5
  • 24
    • 0036892593 scopus 로고    scopus 로고
    • Requirements for de novo initiation of RNA synthesis by recombinant flaviviral RNA-dependent RNA polymerases
    • Ranjith-Kumar CT, Gutshall L, Kim MJ, Sarisky RT, Kao CC, (2002) Requirements for de novo initiation of RNA synthesis by recombinant flaviviral RNA-dependent RNA polymerases. J Virol 76: 12526-12536.
    • (2002) J Virol , vol.76 , pp. 12526-12536
    • Ranjith-Kumar, C.T.1    Gutshall, L.2    Kim, M.J.3    Sarisky, R.T.4    Kao, C.C.5
  • 25
    • 7644227543 scopus 로고    scopus 로고
    • De novo initiation pocket mutations have multiple effects on hepatitis C virus RNA-dependent RNA polymerase activities
    • Ranjith-Kumar CT, Sarisky RT, Gutshall L, Thomson M, Kao CC, (2004) De novo initiation pocket mutations have multiple effects on hepatitis C virus RNA-dependent RNA polymerase activities. J Virol 78: 12207-12217.
    • (2004) J Virol , vol.78 , pp. 12207-12217
    • Ranjith-Kumar, C.T.1    Sarisky, R.T.2    Gutshall, L.3    Thomson, M.4    Kao, C.C.5
  • 26
    • 50649091630 scopus 로고    scopus 로고
    • A locking mechanism regulates RNA synthesis and host protein interaction by the hepatitis C virus polymerase
    • Chinnaswamy S, Yarbrough I, Palaninathan S, Kumar CT, Vijayaraghavan V, et al. (2008) A locking mechanism regulates RNA synthesis and host protein interaction by the hepatitis C virus polymerase. J Biol Chem 283: 20535-20546.
    • (2008) J Biol Chem , vol.283 , pp. 20535-20546
    • Chinnaswamy, S.1    Yarbrough, I.2    Palaninathan, S.3    Kumar, C.T.4    Vijayaraghavan, V.5
  • 27
    • 77952710499 scopus 로고    scopus 로고
    • Regulation of de novo-initiated RNA synthesis in hepatitis C virus RNA-dependent RNA polymerase by intermolecular interactions
    • Chinnaswamy S, Murali A, Li P, Fujisaki K, Kao CC, (2010) Regulation of de novo-initiated RNA synthesis in hepatitis C virus RNA-dependent RNA polymerase by intermolecular interactions. J Virol 84: 5923-5935.
    • (2010) J Virol , vol.84 , pp. 5923-5935
    • Chinnaswamy, S.1    Murali, A.2    Li, P.3    Fujisaki, K.4    Kao, C.C.5
  • 28
    • 0035450225 scopus 로고    scopus 로고
    • De novo initiation of viral RNA-dependent RNA synthesis
    • Kao CC, Singh P, Ecker DJ, (2001) De novo initiation of viral RNA-dependent RNA synthesis. Virology 287: 251-260.
    • (2001) Virology , vol.287 , pp. 251-260
    • Kao, C.C.1    Singh, P.2    Ecker, D.J.3
  • 29
    • 70350309663 scopus 로고    scopus 로고
    • Structural and functional analysis of hepatitis C virus strain JFH1 polymerase
    • Simister P, Schmitt M, Geitmann M, Wicht O, Danielson UH, et al. (2009) Structural and functional analysis of hepatitis C virus strain JFH1 polymerase. J Virol 83: 11926-11939.
    • (2009) J Virol , vol.83 , pp. 11926-11939
    • Simister, P.1    Schmitt, M.2    Geitmann, M.3    Wicht, O.4    Danielson, U.H.5
  • 30
    • 79952379082 scopus 로고    scopus 로고
    • A comprehensive structure-function comparison of hepatitis C virus strain JFH1 and J6 polymerases reveals a key residue stimulating replication in cell culture across genotypes
    • Schmitt M, Scrima N, Radujkovic D, Caillet-Saguy C, Simister PC, et al. (2011) A comprehensive structure-function comparison of hepatitis C virus strain JFH1 and J6 polymerases reveals a key residue stimulating replication in cell culture across genotypes. J Virol 85: 2565-2581.
    • (2011) J Virol , vol.85 , pp. 2565-2581
    • Schmitt, M.1    Scrima, N.2    Radujkovic, D.3    Caillet-Saguy, C.4    Simister, P.C.5
  • 31
    • 0034757877 scopus 로고    scopus 로고
    • Ross River virus transmission, infection, and disease: a cross-disciplinary review
    • Harley D, Sleigh A, Ritchie S, (2001) Ross River virus transmission, infection, and disease: a cross-disciplinary review. Clin Microbiol Rev 14: 909-932.
    • (2001) Clin Microbiol Rev , vol.14 , pp. 909-932
    • Harley, D.1    Sleigh, A.2    Ritchie, S.3
  • 32
    • 79953278745 scopus 로고    scopus 로고
    • The coat protein leads the way: an update on basic and applied studies with the Brome mosaic virus coat protein
    • Kao CC, Ni P, Hema M, Huang X, Dragnea B, (2011) The coat protein leads the way: an update on basic and applied studies with the Brome mosaic virus coat protein. Mol Plant Pathol 12: 403-412.
    • (2011) Mol Plant Pathol , vol.12 , pp. 403-412
    • Kao, C.C.1    Ni, P.2    Hema, M.3    Huang, X.4    Dragnea, B.5
  • 33
    • 1542316127 scopus 로고    scopus 로고
    • Hepatitis B virus infection-natural history and clinical consequences
    • Ganem D, Prince AM, (2004) Hepatitis B virus infection-natural history and clinical consequences. N Engl J Med 350: 1118-1129.
    • (2004) N Engl J Med , vol.350 , pp. 1118-1129
    • Ganem, D.1    Prince, A.M.2
  • 34
    • 80053909334 scopus 로고    scopus 로고
    • Hepadnaviruses; al KDe, editor
    • Philadelphia, PA, Lippincott Williams & Wilkins
    • Seeger C ZF, Mason WS, (2007) Hepadnaviruses; al KDe, editor. Philadelphia, PA Lippincott Williams & Wilkins pp. 2977-3029.
    • (2007) , pp. 2977-3029
    • Seeger, C.Z.F.1    Mason, W.S.2
  • 35
    • 78650754124 scopus 로고    scopus 로고
    • Virus assembly, allostery and antivirals
    • Zlotnick A, Mukhopadhyay S, (2011) Virus assembly, allostery and antivirals. Trends Microbiol 19: 14-23.
    • (2011) Trends Microbiol , vol.19 , pp. 14-23
    • Zlotnick, A.1    Mukhopadhyay, S.2
  • 36
    • 0024759051 scopus 로고
    • Effects of deletions in the N-terminal basic arm of brome mosaic virus coat protein on RNA packaging and systemic infection
    • Sacher R, Ahlquist P, (1989) Effects of deletions in the N-terminal basic arm of brome mosaic virus coat protein on RNA packaging and systemic infection. J Virol 63: 4545-4552.
    • (1989) J Virol , vol.63 , pp. 4545-4552
    • Sacher, R.1    Ahlquist, P.2
  • 37
    • 0029099051 scopus 로고
    • Biological significance of the seven amino-terminal basic residues of brome mosaic virus coat protein
    • Rao AL, Grantham GL, (1995) Biological significance of the seven amino-terminal basic residues of brome mosaic virus coat protein. Virology 211: 42-52.
    • (1995) Virology , vol.211 , pp. 42-52
    • Rao, A.L.1    Grantham, G.L.2
  • 38
    • 77953747864 scopus 로고    scopus 로고
    • Full-length hepatitis B virus core protein packages viral and heterologous RNA with similarly high levels of cooperativity
    • Porterfield JZ, Dhason MS, Loeb DD, Nassal M, Stray SJ, et al. (2010) Full-length hepatitis B virus core protein packages viral and heterologous RNA with similarly high levels of cooperativity. J Virol 84: 7174-7184.
    • (2010) J Virol , vol.84 , pp. 7174-7184
    • Porterfield, J.Z.1    Dhason, M.S.2    Loeb, D.D.3    Nassal, M.4    Stray, S.J.5
  • 39
    • 0036838225 scopus 로고    scopus 로고
    • In vitro-assembled alphavirus core-like particles maintain a structure similar to that of nucleocapsid cores in mature virus
    • Mukhopadhyay S, Chipman PR, Hong EM, Kuhn RJ, Rossmann MG, (2002) In vitro-assembled alphavirus core-like particles maintain a structure similar to that of nucleocapsid cores in mature virus. J Virol 76: 11128-11132.
    • (2002) J Virol , vol.76 , pp. 11128-11132
    • Mukhopadhyay, S.1    Chipman, P.R.2    Hong, E.M.3    Kuhn, R.J.4    Rossmann, M.G.5
  • 40
    • 33947206046 scopus 로고    scopus 로고
    • Cutting Edge: Influenza A virus activates TLR3-dependent inflammatory and RIG-I-dependent antiviral responses in human lung epithelial cells
    • Le Goffic R, Pothlichet J, Vitour D, Fujita T, Meurs E, et al. (2007) Cutting Edge: Influenza A virus activates TLR3-dependent inflammatory and RIG-I-dependent antiviral responses in human lung epithelial cells. J Immunol 178: 3368-3372.
    • (2007) J Immunol , vol.178 , pp. 3368-3372
    • Le Goffic, R.1    Pothlichet, J.2    Vitour, D.3    Fujita, T.4    Meurs, E.5
  • 41
    • 33947241758 scopus 로고    scopus 로고
    • Cytokine induction by respiratory syncytial virus and adenovirus in bronchial epithelial cells
    • Yoon JS, Kim HH, Lee Y, Lee JS, (2007) Cytokine induction by respiratory syncytial virus and adenovirus in bronchial epithelial cells. Pediatr Pulmonol 42: 277-282.
    • (2007) Pediatr Pulmonol , vol.42 , pp. 277-282
    • Yoon, J.S.1    Kim, H.H.2    Lee, Y.3    Lee, J.S.4
  • 42
    • 77958147761 scopus 로고    scopus 로고
    • Human rhinovirus-induced epithelial production of CXCL10 is dependent upon IFN regulatory factor-1
    • Zaheer RS, Proud D, (2010) Human rhinovirus-induced epithelial production of CXCL10 is dependent upon IFN regulatory factor-1. Am J Respir Cell Mol Biol 43: 413-421.
    • (2010) Am J Respir Cell Mol Biol , vol.43 , pp. 413-421
    • Zaheer, R.S.1    Proud, D.2
  • 43
    • 34447629088 scopus 로고    scopus 로고
    • Transmission of a dsRNA in bell pepper and evidence that it consists of the genome of an endornavirus
    • Valverde RA, Gutierrez DL, (2007) Transmission of a dsRNA in bell pepper and evidence that it consists of the genome of an endornavirus. Virus Genes 35: 399-403.
    • (2007) Virus Genes , vol.35 , pp. 399-403
    • Valverde, R.A.1    Gutierrez, D.L.2
  • 44
    • 33744965385 scopus 로고    scopus 로고
    • Structural and functional analyses of the human Toll-like receptor 3. Role of glycosylation
    • Sun J, Duffy KE, Ranjith-Kumar CT, Xiong J, Lamb RJ, et al. (2006) Structural and functional analyses of the human Toll-like receptor 3. Role of glycosylation. J Biol Chem 281: 11144-11151.
    • (2006) J Biol Chem , vol.281 , pp. 11144-11151
    • Sun, J.1    Duffy, K.E.2    Ranjith-Kumar, C.T.3    Xiong, J.4    Lamb, R.J.5
  • 46
    • 79952325540 scopus 로고    scopus 로고
    • Crystal structure of RIG-I C-terminal domain bound to blunt-ended double-strand RNA without 5′ triphosphate
    • Lu C, Ranjith-Kumar CT, Hao L, Kao CC, Li P, (2011) Crystal structure of RIG-I C-terminal domain bound to blunt-ended double-strand RNA without 5′ triphosphate. Nucleic Acids Res 39: 1565-1575.
    • (2011) Nucleic Acids Res , vol.39 , pp. 1565-1575
    • Lu, C.1    Ranjith-Kumar, C.T.2    Hao, L.3    Kao, C.C.4    Li, P.5
  • 47
    • 47049114564 scopus 로고    scopus 로고
    • Single-stranded oligonucleotides can inhibit cytokine production induced by human toll-like receptor 3
    • Ranjith-Kumar CT, Duffy KE, Jordan JL, Eaton-Bassiri A, Vaughan R, et al. (2008) Single-stranded oligonucleotides can inhibit cytokine production induced by human toll-like receptor 3. Mol Cell Biol 28: 4507-4519.
    • (2008) Mol Cell Biol , vol.28 , pp. 4507-4519
    • Ranjith-Kumar, C.T.1    Duffy, K.E.2    Jordan, J.L.3    Eaton-Bassiri, A.4    Vaughan, R.5
  • 48
    • 77958456917 scopus 로고    scopus 로고
    • Green tea catechin, epigallocatechin gallate, suppresses signaling by the dsRNA innate immune receptor RIG-I
    • Ranjith-Kumar CT, Lai Y, Sarisky RT, Cheng Kao C, (2010) Green tea catechin, epigallocatechin gallate, suppresses signaling by the dsRNA innate immune receptor RIG-I. PLoS One 5: e12878.
    • (2010) PLoS One , vol.5
    • Ranjith-Kumar, C.T.1    Lai, Y.2    Sarisky, R.T.3    Cheng Kao, C.4
  • 49
    • 41249083050 scopus 로고    scopus 로고
    • Structural and functional analyses of the severe acute respiratory syndrome coronavirus endoribonuclease Nsp15
    • Bhardwaj K, Palaninathan S, Alcantara JM, Yi LL, Guarino L, et al. (2008) Structural and functional analyses of the severe acute respiratory syndrome coronavirus endoribonuclease Nsp15. J Biol Chem 283: 3655-3664.
    • (2008) J Biol Chem , vol.283 , pp. 3655-3664
    • Bhardwaj, K.1    Palaninathan, S.2    Alcantara, J.M.3    Yi, L.L.4    Guarino, L.5
  • 50
    • 0037837708 scopus 로고    scopus 로고
    • Gold nanoparticles as spectroscopic enhancers for in vitro studies on single viruses
    • Dragnea B, Chen C, Kwak ES, Stein B, Kao CC, (2003) Gold nanoparticles as spectroscopic enhancers for in vitro studies on single viruses. J Am Chem Soc 125: 6374-6375.
    • (2003) J Am Chem Soc , vol.125 , pp. 6374-6375
    • Dragnea, B.1    Chen, C.2    Kwak, E.S.3    Stein, B.4    Kao, C.C.5
  • 51
    • 38049153430 scopus 로고    scopus 로고
    • Scavenger receptor class-A is a novel cell surface receptor for double-stranded RNA
    • Limmon GV, Arredouani M, McCann KL, Corn Minor RA, Kobzik L, et al. (2008) Scavenger receptor class-A is a novel cell surface receptor for double-stranded RNA. FASEB J 22: 159-167.
    • (2008) FASEB J , vol.22 , pp. 159-167
    • Limmon, G.V.1    Arredouani, M.2    McCann, K.L.3    Corn Minor, R.A.4    Kobzik, L.5
  • 52
    • 70449120118 scopus 로고    scopus 로고
    • Cell-surface accumulation of flock house virus-derived peptide leads to efficient internalization via macropinocytosis
    • Nakase I, Hirose H, Tanaka G, Tadokoro A, Kobayashi S, et al. (2009) Cell-surface accumulation of flock house virus-derived peptide leads to efficient internalization via macropinocytosis. Mol Ther 17: 1868-1876.
    • (2009) Mol Ther , vol.17 , pp. 1868-1876
    • Nakase, I.1    Hirose, H.2    Tanaka, G.3    Tadokoro, A.4    Kobayashi, S.5
  • 53
    • 78650635548 scopus 로고    scopus 로고
    • Cell-penetrating peptides derived from viral capsid proteins
    • Qi X, Droste T, Kao CC, (2011) Cell-penetrating peptides derived from viral capsid proteins. Mol Plant Microbe Interact 24: 25-36.
    • (2011) Mol Plant Microbe Interact , vol.24 , pp. 25-36
    • Qi, X.1    Droste, T.2    Kao, C.C.3
  • 54
    • 42549153337 scopus 로고    scopus 로고
    • Vaccinia virus uses macropinocytosis and apoptotic mimicry to enter host cells
    • Mercer J, Helenius A, (2008) Vaccinia virus uses macropinocytosis and apoptotic mimicry to enter host cells. Science 320: 531-535.
    • (2008) Science , vol.320 , pp. 531-535
    • Mercer, J.1    Helenius, A.2
  • 55
    • 70149101538 scopus 로고    scopus 로고
    • Nuclear entry of hepatitis B virus capsids involves disintegration to protein dimers followed by nuclear reassociation to capsids
    • Rabe B, Delaleau M, Bischof A, Foss M, Sominskaya I, et al. (2009) Nuclear entry of hepatitis B virus capsids involves disintegration to protein dimers followed by nuclear reassociation to capsids. PLoS Pathog 5: e1000563.
    • (2009) PLoS Pathog , vol.5
    • Rabe, B.1    Delaleau, M.2    Bischof, A.3    Foss, M.4    Sominskaya, I.5
  • 56
    • 0035283140 scopus 로고    scopus 로고
    • Oligomeric structures of poliovirus polymerase are important for function
    • Hobson SD, Rosenblum ES, Richards OC, Richmond K, Kirkegaard K, et al. (2001) Oligomeric structures of poliovirus polymerase are important for function. EMBO J 20: 1153-1163.
    • (2001) EMBO J , vol.20 , pp. 1153-1163
    • Hobson, S.D.1    Rosenblum, E.S.2    Richards, O.C.3    Richmond, K.4    Kirkegaard, K.5
  • 57
    • 0036194639 scopus 로고    scopus 로고
    • Oligomerization and cooperative RNA synthesis activity of hepatitis C virus RNA-dependent RNA polymerase
    • Wang QM, Hockman MA, Staschke K, Johnson RB, Case KA, et al. (2002) Oligomerization and cooperative RNA synthesis activity of hepatitis C virus RNA-dependent RNA polymerase. J Virol 76: 3865-3872.
    • (2002) J Virol , vol.76 , pp. 3865-3872
    • Wang, Q.M.1    Hockman, M.A.2    Staschke, K.3    Johnson, R.B.4    Case, K.A.5
  • 58
    • 0037127306 scopus 로고    scopus 로고
    • Oligomeric interaction of hepatitis C virus NS5B is critical for catalytic activity of RNA-dependent RNA polymerase
    • Qin W, Luo H, Nomura T, Hayashi N, Yamashita T, et al. (2002) Oligomeric interaction of hepatitis C virus NS5B is critical for catalytic activity of RNA-dependent RNA polymerase. J Biol Chem 277: 2132-2137.
    • (2002) J Biol Chem , vol.277 , pp. 2132-2137
    • Qin, W.1    Luo, H.2    Nomura, T.3    Hayashi, N.4    Yamashita, T.5
  • 59
    • 0027518457 scopus 로고
    • Ordered duplex RNA controls capsid architecture in an icosahedral animal virus
    • Fisher AJ, Johnson JE, (1993) Ordered duplex RNA controls capsid architecture in an icosahedral animal virus. Nature 361: 176-179.
    • (1993) Nature , vol.361 , pp. 176-179
    • Fisher, A.J.1    Johnson, J.E.2
  • 60
    • 0032565439 scopus 로고    scopus 로고
    • Comparison of the native CCMV virion with in vitro assembled CCMV virions by cryoelectron microscopy and image reconstruction
    • Fox JM, Wang G, Speir JA, Olson NH, Johnson JE, et al. (1998) Comparison of the native CCMV virion with in vitro assembled CCMV virions by cryoelectron microscopy and image reconstruction. Virology 244: 212-218.
    • (1998) Virology , vol.244 , pp. 212-218
    • Fox, J.M.1    Wang, G.2    Speir, J.A.3    Olson, N.H.4    Johnson, J.E.5
  • 61
    • 42349090335 scopus 로고    scopus 로고
    • Structural basis of toll-like receptor 3 signaling with double-stranded RNA
    • Liu L, Botos I, Wang Y, Leonard JN, Shiloach J, et al. (2008) Structural basis of toll-like receptor 3 signaling with double-stranded RNA. Science 320: 379-381.
    • (2008) Science , vol.320 , pp. 379-381
    • Liu, L.1    Botos, I.2    Wang, Y.3    Leonard, J.N.4    Shiloach, J.5
  • 62
    • 60749124538 scopus 로고    scopus 로고
    • Cytosolic viral sensor RIG-I is a 5′-triphosphate-dependent translocase on double-stranded RNA
    • Myong S, Cui S, Cornish PV, Kirchhofer A, Gack MU, et al. (2009) Cytosolic viral sensor RIG-I is a 5′-triphosphate-dependent translocase on double-stranded RNA. Science 323: 1070-1074.
    • (2009) Science , vol.323 , pp. 1070-1074
    • Myong, S.1    Cui, S.2    Cornish, P.V.3    Kirchhofer, A.4    Gack, M.U.5
  • 63
    • 0019459464 scopus 로고
    • Two novel classes of small ribonucleoproteins detected by antibodies associated with lupus erythematosus
    • Lerner MR, Boyle JA, Hardin JA, Steitz JA, (1981) Two novel classes of small ribonucleoproteins detected by antibodies associated with lupus erythematosus. Science 211: 400-402.
    • (1981) Science , vol.211 , pp. 400-402
    • Lerner, M.R.1    Boyle, J.A.2    Hardin, J.A.3    Steitz, J.A.4
  • 64
    • 0028362846 scopus 로고
    • Anti-5S RNA/protein (RNP) antibody levels correlate with disease activity in a patient with systemic lupus erythematosus (SLE) nephritis
    • Guialis A, Patrinou-Georgoula M, Tsifetaki N, Aidinis V, Sekeris CE, et al. (1994) Anti-5S RNA/protein (RNP) antibody levels correlate with disease activity in a patient with systemic lupus erythematosus (SLE) nephritis. Clin Exp Immunol 95: 385-389.
    • (1994) Clin Exp Immunol , vol.95 , pp. 385-389
    • Guialis, A.1    Patrinou-Georgoula, M.2    Tsifetaki, N.3    Aidinis, V.4    Sekeris, C.E.5
  • 65
    • 67749135880 scopus 로고    scopus 로고
    • Endosomal TLR signaling is required for anti-nucleic acid and rheumatoid factor autoantibodies in lupus
    • Kono DH, Haraldsson MK, Lawson BR, Pollard KM, Koh YT, et al. (2009) Endosomal TLR signaling is required for anti-nucleic acid and rheumatoid factor autoantibodies in lupus. Proc Natl Acad Sci U S A 106: 12061-12066.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 12061-12066
    • Kono, D.H.1    Haraldsson, M.K.2    Lawson, B.R.3    Pollard, K.M.4    Koh, Y.T.5
  • 66
    • 0036120573 scopus 로고    scopus 로고
    • Structural analysis of the hepatitis C virus RNA polymerase in complex with ribonucleotides
    • Bressanelli S, Tomei L, Rey FA, De Francesco R, (2002) Structural analysis of the hepatitis C virus RNA polymerase in complex with ribonucleotides. J Virol 76: 3482-3492.
    • (2002) J Virol , vol.76 , pp. 3482-3492
    • Bressanelli, S.1    Tomei, L.2    Rey, F.A.3    de Francesco, R.4
  • 67
    • 34848920059 scopus 로고    scopus 로고
    • Hepatitis C virus induces E6AP-dependent degradation of the retinoblastoma protein
    • Munakata T, Liang Y, Kim S, McGivern DR, Huibregtse J, et al. (2007) Hepatitis C virus induces E6AP-dependent degradation of the retinoblastoma protein. PLoS Pathog 3: 1335-1347.
    • (2007) PLoS Pathog , vol.3 , pp. 1335-1347
    • Munakata, T.1    Liang, Y.2    Kim, S.3    McGivern, D.R.4    Huibregtse, J.5
  • 68
    • 29144483321 scopus 로고    scopus 로고
    • Down-regulation of the retinoblastoma tumor suppressor by the hepatitis C virus NS5B RNA-dependent RNA polymerase
    • Munakata T, Nakamura M, Liang Y, Li K, Lemon SM, (2005) Down-regulation of the retinoblastoma tumor suppressor by the hepatitis C virus NS5B RNA-dependent RNA polymerase. Proc Natl Acad Sci U S A 102: 18159-18164.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 18159-18164
    • Munakata, T.1    Nakamura, M.2    Liang, Y.3    Li, K.4    Lemon, S.M.5
  • 69
    • 33644816016 scopus 로고    scopus 로고
    • Hepatitis C virus NS5B delays cell cycle progression by inducing interferon-beta via Toll-like receptor 3 signaling pathway without replicating viral genomes
    • Naka K, Dansako H, Kobayashi N, Ikeda M, Kato N, (2006) Hepatitis C virus NS5B delays cell cycle progression by inducing interferon-beta via Toll-like receptor 3 signaling pathway without replicating viral genomes. Virology 346: 348-362.
    • (2006) Virology , vol.346 , pp. 348-362
    • Naka, K.1    Dansako, H.2    Kobayashi, N.3    Ikeda, M.4    Kato, N.5
  • 70
    • 79960689739 scopus 로고    scopus 로고
    • A Cell-Based Assay for RNA Synthesis by the HCV Polymerase Reveals New Insights on Mechanism of Polymerase Inhibitors and Modulation by NS5A
    • Ranjith-Kumar CT, Wen Y, Baxter N, Bhardwaj K, Cheng Kao C, (2011) A Cell-Based Assay for RNA Synthesis by the HCV Polymerase Reveals New Insights on Mechanism of Polymerase Inhibitors and Modulation by NS5A. PLoS One 6: e22575.
    • (2011) PLoS One , vol.6
    • Ranjith-Kumar, C.T.1    Wen, Y.2    Baxter, N.3    Bhardwaj, K.4    Cheng Kao, C.5
  • 71
    • 7644226241 scopus 로고    scopus 로고
    • Hepatitis C core and nonstructural 3 proteins trigger toll-like receptor 2-mediated pathways and inflammatory activation
    • Dolganiuc A, Oak S, Kodys K, Golenbock DT, Finberg RW, et al. (2004) Hepatitis C core and nonstructural 3 proteins trigger toll-like receptor 2-mediated pathways and inflammatory activation. Gastroenterology 127: 1513-1524.
    • (2004) Gastroenterology , vol.127 , pp. 1513-1524
    • Dolganiuc, A.1    Oak, S.2    Kodys, K.3    Golenbock, D.T.4    Finberg, R.W.5
  • 72
    • 37249005205 scopus 로고    scopus 로고
    • The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability
    • Niesen FH, Berglund H, Vedadi M, (2007) The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability. Nat Protoc 2: 2212-2221.
    • (2007) Nat Protoc , vol.2 , pp. 2212-2221
    • Niesen, F.H.1    Berglund, H.2    Vedadi, M.3
  • 73
    • 4944240246 scopus 로고    scopus 로고
    • Corticosteroid and cytokines synergistically enhance Toll-like receptor 2 expression in respiratory epithelial cells
    • Homma T, Kato A, Hashimoto N, Batchelor J, Yoshikawa M, et al. (2004) Corticosteroid and cytokines synergistically enhance Toll-like receptor 2 expression in respiratory epithelial cells. Am J Respir Cell Mol Biol 31: 463-469.
    • (2004) Am J Respir Cell Mol Biol , vol.31 , pp. 463-469
    • Homma, T.1    Kato, A.2    Hashimoto, N.3    Batchelor, J.4    Yoshikawa, M.5


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