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Volumn 10, Issue 5, 2014, Pages

Rapid Evolution of PARP Genes Suggests a Broad Role for ADP-Ribosylation in Host-Virus Conflicts

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE RIBOSE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; PARP15 PROTEIN, HUMAN; POLY(ADP-RIBOSE) POLYMERASE FAMILY MEMBER 14, HUMAN;

EID: 84901594799     PISSN: 15537390     EISSN: 15537404     Source Type: Journal    
DOI: 10.1371/journal.pgen.1004403     Document Type: Article
Times cited : (146)

References (72)
  • 1
    • 84883867139 scopus 로고    scopus 로고
    • What pathogens have taught us about posttranslational modifications
    • Salomon D, Orth K, (2013) What pathogens have taught us about posttranslational modifications. Cell Host Microbe 14: 269-279.
    • (2013) Cell Host Microbe , vol.14 , pp. 269-279
    • Salomon, D.1    Orth, K.2
  • 2
    • 78651290340 scopus 로고    scopus 로고
    • Epigenetic modulation of host: new insights into immune evasion by viruses
    • Adhya D, Basu A, (2010) Epigenetic modulation of host: new insights into immune evasion by viruses. J Biosci 35: 647-663.
    • (2010) J Biosci , vol.35 , pp. 647-663
    • Adhya, D.1    Basu, A.2
  • 3
    • 67649391002 scopus 로고    scopus 로고
    • Ubiquitination, ubiquitin-like modifiers, and deubiquitination in viral infection
    • Isaacson MK, Ploegh HL, (2009) Ubiquitination, ubiquitin-like modifiers, and deubiquitination in viral infection. Cell Host Microbe 5: 559-570.
    • (2009) Cell Host Microbe , vol.5 , pp. 559-570
    • Isaacson, M.K.1    Ploegh, H.L.2
  • 5
    • 0034023238 scopus 로고    scopus 로고
    • New functions of a long-known molecule. Emerging roles of NAD in cellular signaling
    • Ziegler M, (2000) New functions of a long-known molecule. Emerging roles of NAD in cellular signaling. Eur J Biochem 267: 1550-1564.
    • (2000) Eur J Biochem , vol.267 , pp. 1550-1564
    • Ziegler, M.1
  • 6
    • 84862758175 scopus 로고    scopus 로고
    • New insights into the molecular and cellular functions of poly(ADP-ribose) and PARPs
    • Gibson BA, Kraus WL, (2012) New insights into the molecular and cellular functions of poly(ADP-ribose) and PARPs. Nat Rev Mol Cell Biol 13: 411-424.
    • (2012) Nat Rev Mol Cell Biol , vol.13 , pp. 411-424
    • Gibson, B.A.1    Kraus, W.L.2
  • 7
    • 38449088040 scopus 로고    scopus 로고
    • The diverse biological roles of mammalian PARPS, a small but powerful family of poly-ADP-ribose polymerases
    • Hassa PO, Hottiger MO, (2008) The diverse biological roles of mammalian PARPS, a small but powerful family of poly-ADP-ribose polymerases. Front Biosci 13: 3046-3082.
    • (2008) Front Biosci , vol.13 , pp. 3046-3082
    • Hassa, P.O.1    Hottiger, M.O.2
  • 9
    • 77957743077 scopus 로고    scopus 로고
    • Evolutionary history of the poly(ADP-ribose) polymerase gene family in eukaryotes
    • Citarelli M, Teotia S, Lamb RS, (2010) Evolutionary history of the poly(ADP-ribose) polymerase gene family in eukaryotes. BMC Evol Biol 10: 308.
    • (2010) BMC Evol Biol , vol.10 , pp. 308
    • Citarelli, M.1    Teotia, S.2    Lamb, R.S.3
  • 10
    • 27644577665 scopus 로고    scopus 로고
    • In silico characterization of the family of PARP-like poly(ADP-ribosyl)transferases (pARTs)
    • Otto H, Reche PA, Bazan F, Dittmar K, Haag F, et al. (2005) In silico characterization of the family of PARP-like poly(ADP-ribosyl)transferases (pARTs). BMC Genomics 6: 139.
    • (2005) BMC Genomics , vol.6 , pp. 139
    • Otto, H.1    Reche, P.A.2    Bazan, F.3    Dittmar, K.4    Haag, F.5
  • 11
    • 84882437564 scopus 로고    scopus 로고
    • A systematic analysis of the PARP protein family identifies new functions critical for cell physiology
    • Vyas S, Chesarone-Cataldo M, Todorova T, Huang YH, Chang P, (2013) A systematic analysis of the PARP protein family identifies new functions critical for cell physiology. Nat Commun 4: 2240.
    • (2013) Nat Commun , vol.4 , pp. 2240
    • Vyas, S.1    Chesarone-Cataldo, M.2    Todorova, T.3    Huang, Y.H.4    Chang, P.5
  • 12
    • 84880324619 scopus 로고    scopus 로고
    • Expanding functions of intracellular resident mono-ADP-ribosylation in cell physiology
    • Feijs KL, Verheugd P, Luscher B, (2013) Expanding functions of intracellular resident mono-ADP-ribosylation in cell physiology. FEBS J 280: 3519-3529.
    • (2013) FEBS J , vol.280 , pp. 3519-3529
    • Feijs, K.L.1    Verheugd, P.2    Luscher, B.3
  • 13
    • 84862196500 scopus 로고    scopus 로고
    • Poly(ADP-ribose) regulates post-transcriptional gene regulation in the cytoplasm
    • Leung A, Todorova T, Ando Y, Chang P, (2012) Poly(ADP-ribose) regulates post-transcriptional gene regulation in the cytoplasm. RNA Biol 9: 542-548.
    • (2012) RNA Biol , vol.9 , pp. 542-548
    • Leung, A.1    Todorova, T.2    Ando, Y.3    Chang, P.4
  • 14
    • 84885995929 scopus 로고    scopus 로고
    • Reciprocal inhibition between intracellular antiviral signaling and the RNAi machinery in mammalian cells
    • Seo GJ, Kincaid RP, Phanaksri T, Burke JM, Pare JM, et al. (2013) Reciprocal inhibition between intracellular antiviral signaling and the RNAi machinery in mammalian cells. Cell Host Microbe 14: 435-445.
    • (2013) Cell Host Microbe , vol.14 , pp. 435-445
    • Seo, G.J.1    Kincaid, R.P.2    Phanaksri, T.3    Burke, J.M.4    Pare, J.M.5
  • 17
    • 0023876562 scopus 로고
    • Inhibition of vaccinia virus replication by nicotinamide: evidence for ADP-ribosylation of viral proteins
    • Child SJ, Franke CA, Hruby DE, (1988) Inhibition of vaccinia virus replication by nicotinamide: evidence for ADP-ribosylation of viral proteins. Virus Res 9: 119-132.
    • (1988) Virus Res , vol.9 , pp. 119-132
    • Child, S.J.1    Franke, C.A.2    Hruby, D.E.3
  • 18
    • 84862910351 scopus 로고    scopus 로고
    • Herpes simplex virus requires poly(ADP-ribose) polymerase activity for efficient replication and induces extracellular signal-related kinase-dependent phosphorylation and ICP0-dependent nuclear localization of tankyrase 1
    • Li Z, Yamauchi Y, Kamakura M, Murayama T, Goshima F, et al. (2012) Herpes simplex virus requires poly(ADP-ribose) polymerase activity for efficient replication and induces extracellular signal-related kinase-dependent phosphorylation and ICP0-dependent nuclear localization of tankyrase 1. J Virol 86: 492-503.
    • (2012) J Virol , vol.86 , pp. 492-503
    • Li, Z.1    Yamauchi, Y.2    Kamakura, M.3    Murayama, T.4    Goshima, F.5
  • 19
    • 84879415959 scopus 로고    scopus 로고
    • Macrodomain-containing proteins: regulating new intracellular functions of mono(ADP-ribosyl)ation
    • Feijs KL, Forst AH, Verheugd P, Luscher B, (2013) Macrodomain-containing proteins: regulating new intracellular functions of mono(ADP-ribosyl)ation. Nat Rev Mol Cell Biol 14: 443-451.
    • (2013) Nat Rev Mol Cell Biol , vol.14 , pp. 443-451
    • Feijs, K.L.1    Forst, A.H.2    Verheugd, P.3    Luscher, B.4
  • 20
    • 67349175974 scopus 로고    scopus 로고
    • The nsP3 macro domain is important for Sindbis virus replication in neurons and neurovirulence in mice
    • Park E, Griffin DE, (2009) The nsP3 macro domain is important for Sindbis virus replication in neurons and neurovirulence in mice. Virology 388: 305-314.
    • (2009) Virology , vol.388 , pp. 305-314
    • Park, E.1    Griffin, D.E.2
  • 21
    • 79960372663 scopus 로고    scopus 로고
    • The ADP-ribose-1"-monophosphatase domains of severe acute respiratory syndrome coronavirus and human coronavirus 229E mediate resistance to antiviral interferon responses
    • Kuri T, Eriksson KK, Putics A, Zust R, Snijder EJ, et al. (2011) The ADP-ribose-1"-monophosphatase domains of severe acute respiratory syndrome coronavirus and human coronavirus 229E mediate resistance to antiviral interferon responses. J Gen Virol 92: 1899-1905.
    • (2011) J Gen Virol , vol.92 , pp. 1899-1905
    • Kuri, T.1    Eriksson, K.K.2    Putics, A.3    Zust, R.4    Snijder, E.J.5
  • 22
    • 82955187705 scopus 로고    scopus 로고
    • Interferon-stimulated genes and their antiviral effector functions
    • Schoggins JW, Rice CM, (2011) Interferon-stimulated genes and their antiviral effector functions. Curr Opin Virol 1: 519-525.
    • (2011) Curr Opin Virol , vol.1 , pp. 519-525
    • Schoggins, J.W.1    Rice, C.M.2
  • 23
    • 0037031709 scopus 로고    scopus 로고
    • Inhibition of retroviral RNA production by ZAP, a CCCH-type zinc finger protein
    • Gao G, Guo X, Goff SP, (2002) Inhibition of retroviral RNA production by ZAP, a CCCH-type zinc finger protein. Science 297: 1703-1706.
    • (2002) Science , vol.297 , pp. 1703-1706
    • Gao, G.1    Guo, X.2    Goff, S.P.3
  • 24
    • 33847194606 scopus 로고    scopus 로고
    • Inhibition of filovirus replication by the zinc finger antiviral protein
    • Muller S, Moller P, Bick MJ, Wurr S, Becker S, et al. (2007) Inhibition of filovirus replication by the zinc finger antiviral protein. J Virol 81: 2391-2400.
    • (2007) J Virol , vol.81 , pp. 2391-2400
    • Muller, S.1    Moller, P.2    Bick, M.J.3    Wurr, S.4    Becker, S.5
  • 25
    • 0142060863 scopus 로고    scopus 로고
    • Expression of the zinc-finger antiviral protein inhibits alphavirus replication
    • Bick MJ, Carroll JW, Gao G, Goff SP, Rice CM, et al. (2003) Expression of the zinc-finger antiviral protein inhibits alphavirus replication. J Virol 77: 11555-11562.
    • (2003) J Virol , vol.77 , pp. 11555-11562
    • Bick, M.J.1    Carroll, J.W.2    Gao, G.3    Goff, S.P.4    Rice, C.M.5
  • 26
    • 84884747041 scopus 로고    scopus 로고
    • Inhibition of hepatitis B virus replication by the host zinc finger antiviral protein
    • Mao R, Nie H, Cai D, Zhang J, Liu H, et al. (2013) Inhibition of hepatitis B virus replication by the host zinc finger antiviral protein. PLoS Pathog 9: e1003494.
    • (2013) PLoS Pathog , vol.9
    • Mao, R.1    Nie, H.2    Cai, D.3    Zhang, J.4    Liu, H.5
  • 27
    • 8644267555 scopus 로고    scopus 로고
    • The zinc finger antiviral protein directly binds to specific viral mRNAs through the CCCH zinc finger motifs
    • Guo X, Carroll JW, Macdonald MR, Goff SP, Gao G, (2004) The zinc finger antiviral protein directly binds to specific viral mRNAs through the CCCH zinc finger motifs. J Virol 78: 12781-12787.
    • (2004) J Virol , vol.78 , pp. 12781-12787
    • Guo, X.1    Carroll, J.W.2    Macdonald, M.R.3    Goff, S.P.4    Gao, G.5
  • 28
    • 33846083772 scopus 로고    scopus 로고
    • The zinc-finger antiviral protein recruits the RNA processing exosome to degrade the target mRNA
    • Guo X, Ma J, Sun J, Gao G, (2007) The zinc-finger antiviral protein recruits the RNA processing exosome to degrade the target mRNA. Proc Natl Acad Sci U S A 104: 151-156.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 151-156
    • Guo, X.1    Ma, J.2    Sun, J.3    Gao, G.4
  • 29
    • 79955957616 scopus 로고    scopus 로고
    • Poly(ADP-ribose) regulates stress responses and microRNA activity in the cytoplasm
    • Leung AK, Vyas S, Rood JE, Bhutkar A, Sharp PA, et al. (2011) Poly(ADP-ribose) regulates stress responses and microRNA activity in the cytoplasm. Mol Cell 42: 489-499.
    • (2011) Mol Cell , vol.42 , pp. 489-499
    • Leung, A.K.1    Vyas, S.2    Rood, J.E.3    Bhutkar, A.4    Sharp, P.A.5
  • 30
    • 77951455708 scopus 로고    scopus 로고
    • Regulation of Epstein-Barr virus OriP replication by poly(ADP-ribose) polymerase 1
    • Tempera I, Deng Z, Atanasiu C, Chen CJ, D'Erme M, et al. (2010) Regulation of Epstein-Barr virus OriP replication by poly(ADP-ribose) polymerase 1. J Virol 84: 4988-4997.
    • (2010) J Virol , vol.84 , pp. 4988-4997
    • Tempera, I.1    Deng, Z.2    Atanasiu, C.3    Chen, C.J.4    D'Erme, M.5
  • 31
    • 4444294852 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase 1 binds to Kaposi's sarcoma-associated herpesvirus (KSHV) terminal repeat sequence and modulates KSHV replication in latency
    • Ohsaki E, Ueda K, Sakakibara S, Do E, Yada K, et al. (2004) Poly(ADP-ribose) polymerase 1 binds to Kaposi's sarcoma-associated herpesvirus (KSHV) terminal repeat sequence and modulates KSHV replication in latency. J Virol 78: 9936-9946.
    • (2004) J Virol , vol.78 , pp. 9936-9946
    • Ohsaki, E.1    Ueda, K.2    Sakakibara, S.3    Do, E.4    Yada, K.5
  • 32
    • 84874669469 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase 1 promotes transcriptional repression of integrated retroviruses
    • Bueno MT, Reyes D, Valdes L, Saheba A, Urias E, et al. (2013) Poly(ADP-ribose) polymerase 1 promotes transcriptional repression of integrated retroviruses. J Virol 87: 2496-2507.
    • (2013) J Virol , vol.87 , pp. 2496-2507
    • Bueno, M.T.1    Reyes, D.2    Valdes, L.3    Saheba, A.4    Urias, E.5
  • 33
    • 84864378884 scopus 로고    scopus 로고
    • New PARP gene with an anti-alphavirus function
    • Atasheva S, Akhrymuk M, Frolova EI, Frolov I, (2012) New PARP gene with an anti-alphavirus function. J Virol 86: 8147-8160.
    • (2012) J Virol , vol.86 , pp. 8147-8160
    • Atasheva, S.1    Akhrymuk, M.2    Frolova, E.I.3    Frolov, I.4
  • 34
    • 84867647908 scopus 로고    scopus 로고
    • Rules of engagement: molecular insights from host-virus arms races
    • Daugherty MD, Malik HS, (2012) Rules of engagement: molecular insights from host-virus arms races. Annu Rev Genet 46: 677-700.
    • (2012) Annu Rev Genet , vol.46 , pp. 677-700
    • Daugherty, M.D.1    Malik, H.S.2
  • 35
    • 84867659115 scopus 로고    scopus 로고
    • Evolution-guided identification of antiviral specificity determinants in the broadly acting interferon-induced innate immunity factor MxA
    • Mitchell PS, Patzina C, Emerman M, Haller O, Malik HS, et al. (2012) Evolution-guided identification of antiviral specificity determinants in the broadly acting interferon-induced innate immunity factor MxA. Cell Host Microbe 12: 598-604.
    • (2012) Cell Host Microbe , vol.12 , pp. 598-604
    • Mitchell, P.S.1    Patzina, C.2    Emerman, M.3    Haller, O.4    Malik, H.S.5
  • 36
    • 14544281087 scopus 로고    scopus 로고
    • Positive selection of primate TRIM5alpha identifies a critical species-specific retroviral restriction domain
    • Sawyer SL, Wu LI, Emerman M, Malik HS, (2005) Positive selection of primate TRIM5alpha identifies a critical species-specific retroviral restriction domain. Proc Natl Acad Sci U S A 102: 2832-2837.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 2832-2837
    • Sawyer, S.L.1    Wu, L.I.2    Emerman, M.3    Malik, H.S.4
  • 37
    • 38949096858 scopus 로고    scopus 로고
    • Positive selection and increased antiviral activity associated with the PARP-containing isoform of human zinc-finger antiviral protein
    • Kerns JA, Emerman M, Malik HS, (2008) Positive selection and increased antiviral activity associated with the PARP-containing isoform of human zinc-finger antiviral protein. PLoS Genet 4: e21.
    • (2008) PLoS Genet , vol.4
    • Kerns, J.A.1    Emerman, M.2    Malik, H.S.3
  • 38
    • 37849007655 scopus 로고    scopus 로고
    • Discordant evolution of the adjacent antiretroviral genes TRIM22 and TRIM5 in mammals
    • Sawyer SL, Emerman M, Malik HS, (2007) Discordant evolution of the adjacent antiretroviral genes TRIM22 and TRIM5 in mammals. PLoS Pathog 3: e197.
    • (2007) PLoS Pathog , vol.3
    • Sawyer, S.L.1    Emerman, M.2    Malik, H.S.3
  • 39
    • 84861430206 scopus 로고    scopus 로고
    • An ancient history of gene duplications, fusions and losses in the evolution of APOBEC3 mutators in mammals
    • Munk C, Willemsen A, Bravo IG, (2012) An ancient history of gene duplications, fusions and losses in the evolution of APOBEC3 mutators in mammals. BMC Evol Biol 12: 71.
    • (2012) BMC Evol Biol , vol.12 , pp. 71
    • Munk, C.1    Willemsen, A.2    Bravo, I.G.3
  • 40
    • 34547803197 scopus 로고    scopus 로고
    • PAML 4: phylogenetic analysis by maximum likelihood
    • Yang Z, (2007) PAML 4: phylogenetic analysis by maximum likelihood. Mol Biol Evol 24: 1586-1591.
    • (2007) Mol Biol Evol , vol.24 , pp. 1586-1591
    • Yang, Z.1
  • 41
    • 15844406550 scopus 로고    scopus 로고
    • HyPhy: hypothesis testing using phylogenies
    • Pond SL, Frost SD, Muse SV, (2005) HyPhy: hypothesis testing using phylogenies. Bioinformatics 21: 676-679.
    • (2005) Bioinformatics , vol.21 , pp. 676-679
    • Pond, S.L.1    Frost, S.D.2    Muse, S.V.3
  • 42
    • 80155187383 scopus 로고    scopus 로고
    • A random effects branch-site model for detecting episodic diversifying selection
    • Kosakovsky Pond SL, Murrell B, Fourment M, Frost SD, Delport W, et al. (2011) A random effects branch-site model for detecting episodic diversifying selection. Mol Biol Evol 28: 3033-3043.
    • (2011) Mol Biol Evol , vol.28 , pp. 3033-3043
    • Kosakovsky Pond, S.L.1    Murrell, B.2    Fourment, M.3    Frost, S.D.4    Delport, W.5
  • 43
    • 8544225780 scopus 로고    scopus 로고
    • Accuracy and power of statistical methods for detecting adaptive evolution in protein coding sequences and for identifying positively selected sites
    • Wong WS, Yang Z, Goldman N, Nielsen R, (2004) Accuracy and power of statistical methods for detecting adaptive evolution in protein coding sequences and for identifying positively selected sites. Genetics 168: 1041-1051.
    • (2004) Genetics , vol.168 , pp. 1041-1051
    • Wong, W.S.1    Yang, Z.2    Goldman, N.3    Nielsen, R.4
  • 45
    • 58149502680 scopus 로고    scopus 로고
    • Vaults and the major vault protein: novel roles in signal pathway regulation and immunity
    • Berger W, Steiner E, Grusch M, Elbling L, Micksche M, (2009) Vaults and the major vault protein: novel roles in signal pathway regulation and immunity. Cell Mol Life Sci 66: 43-61.
    • (2009) Cell Mol Life Sci , vol.66 , pp. 43-61
    • Berger, W.1    Steiner, E.2    Grusch, M.3    Elbling, L.4    Micksche, M.5
  • 46
    • 48449106792 scopus 로고    scopus 로고
    • The Jpred 3 secondary structure prediction server
    • Cole C, Barber JD, Barton GJ, (2008) The Jpred 3 secondary structure prediction server. Nucleic Acids Res 36: W197-201.
    • (2008) Nucleic Acids Res , vol.36
    • Cole, C.1    Barber, J.D.2    Barton, G.J.3
  • 48
    • 84874456032 scopus 로고    scopus 로고
    • Recognition of mono-ADP-ribosylated ARTD10 substrates by ARTD8 macrodomains
    • Forst AH, Karlberg T, Herzog N, Thorsell AG, Gross A, et al. (2013) Recognition of mono-ADP-ribosylated ARTD10 substrates by ARTD8 macrodomains. Structure 21: 462-475.
    • (2013) Structure , vol.21 , pp. 462-475
    • Forst, A.H.1    Karlberg, T.2    Herzog, N.3    Thorsell, A.G.4    Gross, A.5
  • 49
    • 33749387471 scopus 로고    scopus 로고
    • A family of killer toxins. Exploring the mechanism of ADP-ribosylating toxins
    • Holbourn KP, Shone CC, Acharya KR, (2006) A family of killer toxins. Exploring the mechanism of ADP-ribosylating toxins. FEBS J 273: 4579-4593.
    • (2006) FEBS J , vol.273 , pp. 4579-4593
    • Holbourn, K.P.1    Shone, C.C.2    Acharya, K.R.3
  • 50
    • 33745848147 scopus 로고    scopus 로고
    • BAL1 and BBAP are regulated by a gamma interferon-responsive bidirectional promoter and are overexpressed in diffuse large B-cell lymphomas with a prominent inflammatory infiltrate
    • Juszczynski P, Kutok JL, Li C, Mitra J, Aguiar RC, et al. (2006) BAL1 and BBAP are regulated by a gamma interferon-responsive bidirectional promoter and are overexpressed in diffuse large B-cell lymphomas with a prominent inflammatory infiltrate. Mol Cell Biol 26: 5348-5359.
    • (2006) Mol Cell Biol , vol.26 , pp. 5348-5359
    • Juszczynski, P.1    Kutok, J.L.2    Li, C.3    Mitra, J.4    Aguiar, R.C.5
  • 51
    • 79955542915 scopus 로고    scopus 로고
    • A diverse range of gene products are effectors of the type I interferon antiviral response
    • Schoggins JW, Wilson SJ, Panis M, Murphy MY, Jones CT, et al. (2011) A diverse range of gene products are effectors of the type I interferon antiviral response. Nature 472: 481-485.
    • (2011) Nature , vol.472 , pp. 481-485
    • Schoggins, J.W.1    Wilson, S.J.2    Panis, M.3    Murphy, M.Y.4    Jones, C.T.5
  • 52
    • 84857538593 scopus 로고    scopus 로고
    • Disease tolerance as a defense strategy
    • Medzhitov R, Schneider DS, Soares MP, (2012) Disease tolerance as a defense strategy. Science 335: 936-941.
    • (2012) Science , vol.335 , pp. 936-941
    • Medzhitov, R.1    Schneider, D.S.2    Soares, M.P.3
  • 54
    • 27144440476 scopus 로고    scopus 로고
    • Cardif is an adaptor protein in the RIG-I antiviral pathway and is targeted by hepatitis C virus
    • Meylan E, Curran J, Hofmann K, Moradpour D, Binder M, et al. (2005) Cardif is an adaptor protein in the RIG-I antiviral pathway and is targeted by hepatitis C virus. Nature 437: 1167-1172.
    • (2005) Nature , vol.437 , pp. 1167-1172
    • Meylan, E.1    Curran, J.2    Hofmann, K.3    Moradpour, D.4    Binder, M.5
  • 55
    • 34249855382 scopus 로고    scopus 로고
    • Disruption of innate immunity due to mitochondrial targeting of a picornaviral protease precursor
    • Yang Y, Liang Y, Qu L, Chen Z, Yi M, et al. (2007) Disruption of innate immunity due to mitochondrial targeting of a picornaviral protease precursor. Proc Natl Acad Sci U S A 104: 7253-7258.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 7253-7258
    • Yang, Y.1    Liang, Y.2    Qu, L.3    Chen, Z.4    Yi, M.5
  • 56
    • 79953279338 scopus 로고    scopus 로고
    • The coxsackievirus B 3C protease cleaves MAVS and TRIF to attenuate host type I interferon and apoptotic signaling
    • Mukherjee A, Morosky SA, Delorme-Axford E, Dybdahl-Sissoko N, Oberste MS, et al. (2011) The coxsackievirus B 3C protease cleaves MAVS and TRIF to attenuate host type I interferon and apoptotic signaling. PLoS Pathog 7: e1001311.
    • (2011) PLoS Pathog , vol.7
    • Mukherjee, A.1    Morosky, S.A.2    Delorme-Axford, E.3    Dybdahl-Sissoko, N.4    Oberste, M.S.5
  • 57
    • 70350625078 scopus 로고    scopus 로고
    • Cleavage of IPS-1 in cells infected with human rhinovirus
    • Drahos J, Racaniello VR, (2009) Cleavage of IPS-1 in cells infected with human rhinovirus. J Virol 83: 11581-11587.
    • (2009) J Virol , vol.83 , pp. 11581-11587
    • Drahos, J.1    Racaniello, V.R.2
  • 58
    • 58749102026 scopus 로고    scopus 로고
    • Protein kinase R reveals an evolutionary model for defeating viral mimicry
    • Elde NC, Child SJ, Geballe AP, Malik HS, (2009) Protein kinase R reveals an evolutionary model for defeating viral mimicry. Nature 457: 485-489.
    • (2009) Nature , vol.457 , pp. 485-489
    • Elde, N.C.1    Child, S.J.2    Geballe, A.P.3    Malik, H.S.4
  • 59
  • 60
    • 41849103099 scopus 로고    scopus 로고
    • P bodies, stress granules, and viral life cycles
    • Beckham CJ, Parker R, (2008) P bodies, stress granules, and viral life cycles. Cell Host Microbe 3: 206-212.
    • (2008) Cell Host Microbe , vol.3 , pp. 206-212
    • Beckham, C.J.1    Parker, R.2
  • 61
    • 0034672418 scopus 로고    scopus 로고
    • BAL is a novel risk-related gene in diffuse large B-cell lymphomas that enhances cellular migration
    • Aguiar RC, Yakushijin Y, Kharbanda S, Salgia R, Fletcher JA, et al. (2000) BAL is a novel risk-related gene in diffuse large B-cell lymphomas that enhances cellular migration. Blood 96: 4328-4334.
    • (2000) Blood , vol.96 , pp. 4328-4334
    • Aguiar, R.C.1    Yakushijin, Y.2    Kharbanda, S.3    Salgia, R.4    Fletcher, J.A.5
  • 62
    • 84884229615 scopus 로고    scopus 로고
    • B cell-intrinsic and -extrinsic regulation of antibody responses by PARP14, an intracellular (ADP-ribosyl)transferase
    • Cho SH, Raybuck A, Wei M, Erickson J, Nam KT, et al. (2013) B cell-intrinsic and-extrinsic regulation of antibody responses by PARP14, an intracellular (ADP-ribosyl)transferase. J Immunol 191: 3169-3178.
    • (2013) J Immunol , vol.191 , pp. 3169-3178
    • Cho, S.H.1    Raybuck, A.2    Wei, M.3    Erickson, J.4    Nam, K.T.5
  • 64
    • 0032825011 scopus 로고    scopus 로고
    • K-Estimator: calculation of the number of nucleotide substitutions per site and the confidence intervals
    • Comeron JM, (1999) K-Estimator: calculation of the number of nucleotide substitutions per site and the confidence intervals. Bioinformatics 15: 763-764.
    • (1999) Bioinformatics , vol.15 , pp. 763-764
    • Comeron, J.M.1
  • 65
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: a new generation of protein database search programs
    • Altschul SF, Madden TL, Schaffer AA, Zhang J, Zhang Z, et al. (1997) Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res 25: 3389-3402.
    • (1997) Nucleic Acids Res , vol.25 , pp. 3389-3402
    • Altschul, S.F.1    Madden, T.L.2    Schaffer, A.A.3    Zhang, J.4    Zhang, Z.5
  • 66
    • 0029654258 scopus 로고
    • A dot-matrix program with dynamic threshold control suited for genomic DNA and protein sequence analysis
    • Sonnhammer EL, Durbin R, (1995) A dot-matrix program with dynamic threshold control suited for genomic DNA and protein sequence analysis. Gene 167: GC1-10.
    • (1995) Gene , vol.167
    • Sonnhammer, E.L.1    Durbin, R.2
  • 69
    • 77950806408 scopus 로고    scopus 로고
    • New algorithms and methods to estimate maximum-likelihood phylogenies: assessing the performance of PhyML 3.0
    • Guindon S, Dufayard JF, Lefort V, Anisimova M, Hordijk W, et al. (2010) New algorithms and methods to estimate maximum-likelihood phylogenies: assessing the performance of PhyML 3.0. Syst Biol 59: 307-321.
    • (2010) Syst Biol , vol.59 , pp. 307-321
    • Guindon, S.1    Dufayard, J.F.2    Lefort, V.3    Anisimova, M.4    Hordijk, W.5
  • 70
    • 18744382506 scopus 로고    scopus 로고
    • ProtTest: selection of best-fit models of protein evolution
    • Abascal F, Zardoya R, Posada D, (2005) ProtTest: selection of best-fit models of protein evolution. Bioinformatics 21: 2104-2105.
    • (2005) Bioinformatics , vol.21 , pp. 2104-2105
    • Abascal, F.1    Zardoya, R.2    Posada, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.