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Volumn 76, Issue 3, 2012, Pages 652-666

The multiple functions of TRBP, at the hub of cell responses to viruses, stress, and cancer

Author keywords

[No Author keywords available]

Indexed keywords

INTERFERON; MICRORNA; RNA BINDING PROTEIN; TRANS ACTIVATION RESPONSE RNA BINDING PROTEIN 1; TRANS ACTIVATION RESPONSE RNA BINDING PROTEIN 2; UNCLASSIFIED DRUG;

EID: 84865727711     PISSN: 10922172     EISSN: 10985557     Source Type: Journal    
DOI: 10.1128/MMBR.00012-12     Document Type: Review
Times cited : (76)

References (148)
  • 1
    • 77956400067 scopus 로고    scopus 로고
    • Hepatitis C virus controls interferon production through PKR activation
    • doi:10.1371/journal.pone.0010575
    • Arnaud N, et al. 2010. Hepatitis C virus controls interferon production through PKR activation. PLoS One 5 :e10575. doi:10.1371/journal.pone.0010575.
    • (2010) PLoS One , vol.5
    • Arnaud, N.1
  • 2
    • 11444253965 scopus 로고    scopus 로고
    • HIV-1 TAR RNA: The target of molecular interactions between the virus and its host
    • Bannwarth S, Gatignol A. 2005. HIV-1 TAR RNA: the target of molecular interactions between the virus and its host. Curr. HIV Res. 3:61-71.
    • (2005) Curr. HIV Res. , vol.3 , pp. 61-71
    • Bannwarth, S.1    Gatignol, A.2
  • 3
    • 29444445480 scopus 로고    scopus 로고
    • Cell-specific regulation of TRBP1 promoter by NF-Y transcription factor in lymphocytes and astrocytes
    • Bannwarth S, et al. 2006. Cell-specific regulation of TRBP1 promoter by NF-Y transcription factor in lymphocytes and astrocytes. J. Mol. Biol. 355:898-910.
    • (2006) J. Mol. Biol. , vol.355 , pp. 898-910
    • Bannwarth, S.1
  • 4
    • 0035966060 scopus 로고    scopus 로고
    • Organization of the human tarbp2 gene reveals two promoters that are repressed in an astrocytic cell line
    • Bannwarth S, et al. 2001. Organization of the human tarbp2 gene reveals two promoters that are repressed in an astrocytic cell line. J. Biol. Chem. 276:48803-48813.
    • (2001) J. Biol. Chem. , vol.276 , pp. 48803-48813
    • Bannwarth, S.1
  • 5
    • 62549152238 scopus 로고    scopus 로고
    • The NFAR's (nuclear factors associated with dsRNA): Evolutionarily conserved members of the dsRNA binding protein family
    • Barber GN. 2009. The NFAR's (nuclear factors associated with dsRNA): evolutionarily conserved members of the dsRNA binding protein family. RNA Biol. 6:35-39.
    • (2009) RNA Biol. , vol.6 , pp. 35-39
    • Barber, G.N.1
  • 6
    • 0028407347 scopus 로고
    • Binding properties of newly identified Xenopus proteins containing dsRNA-binding motifs
    • Bass BL, Hurst SR, Singer JD. 1994. Binding properties of newly identified Xenopus proteins containing dsRNA-binding motifs. Curr. Biol. 4:301-314.
    • (1994) Curr. Biol. , vol.4 , pp. 301-314
    • Bass, B.L.1    Hurst, S.R.2    Singer, J.D.3
  • 7
    • 0141816689 scopus 로고    scopus 로고
    • Additive activity between the trans-activation response RNA-binding protein, TRBP2, and cyclin T1 on HIV type 1 expression and viral production in murine cells
    • Battisti PL, et al. 2003. Additive activity between the trans-activation response RNA-binding protein, TRBP2, and cyclin T1 on HIV type 1 expression and viral production in murine cells. AIDS Res. Hum. Retroviruses 19:767-778.
    • (2003) AIDS Res. Hum. Retroviruses , vol.19 , pp. 767-778
    • Battisti, P.L.1
  • 8
    • 0031014063 scopus 로고    scopus 로고
    • Oncogenic potential of TAR RNA binding protein TRBP and its regulatory interaction with RNA-dependent protein kinase PKR
    • Benkirane M, et al. 1997. Oncogenic potential of TAR RNA binding protein TRBP and its regulatory interaction with RNA-dependent protein kinase PKR. EMBO J. 16:611-624.
    • (1997) EMBO J. , vol.16 , pp. 611-624
    • Benkirane, M.1
  • 9
    • 19344370167 scopus 로고    scopus 로고
    • Evidence that HIV-1 encodes an siRNA and a suppressor ofRNAsilencing
    • Bennasser Y, Le SY, Benkirane M, Jeang KT. 2005. Evidence that HIV-1 encodes an siRNA and a suppressor ofRNAsilencing. Immunity 22:607-619.
    • (2005) Immunity , vol.22 , pp. 607-619
    • Bennasser, Y.1    Le, S.Y.2    Benkirane, M.3    Jeang, K.T.4
  • 10
    • 33748775175 scopus 로고    scopus 로고
    • HIV-1 TAR RNA subverts RNA interference in transfected cells through sequestration of TAR RNA-binding protein, TRBP
    • Bennasser Y, Yeung ML, Jeang KT. 2006. HIV-1 TAR RNA subverts RNA interference in transfected cells through sequestration of TAR RNA-binding protein, TRBP. J. Biol. Chem. 281:27674-27678.
    • (2006) J. Biol. Chem. , vol.281 , pp. 27674-27678
    • Bennasser, Y.1    Yeung, M.L.2    Jeang, K.T.3
  • 11
    • 5644234968 scopus 로고    scopus 로고
    • Serine 18 phosphorylation of RAX, the PKR activator, is required for PKR activation and consequent translation inhibition
    • Bennett RL, Blalock WL, May WS. 2004. Serine 18 phosphorylation of RAX, the PKR activator, is required for PKR activation and consequent translation inhibition. J. Biol. Chem. 279:42687-42693.
    • (2004) J. Biol. Chem. , vol.279 , pp. 42687-42693
    • Bennett, R.L.1    Blalock, W.L.2    May, W.S.3
  • 12
    • 0028807795 scopus 로고
    • Expression of TAR RNA-binding protein in baculovirus and co-immunoprecipitation with insect cell protein kinase
    • Blair ED, et al. 1995. Expression of TAR RNA-binding protein in baculovirus and co-immunoprecipitation with insect cell protein kinase. J. Biomed. Sci. 2:322-329.
    • (1995) J. Biomed. Sci. , vol.2 , pp. 322-329
    • Blair, E.D.1
  • 14
    • 79956081671 scopus 로고    scopus 로고
    • On the nature of in vivo requirements for rde-4 in RNAi and developmental pathways in C. elegans
    • Blanchard D, et al. 2011. On the nature of in vivo requirements for rde-4 in RNAi and developmental pathways in C. elegans. RNA Biol. 8:458-467.
    • (2011) RNA Biol. , vol.8 , pp. 458-467
    • Blanchard, D.1
  • 15
    • 1642523400 scopus 로고    scopus 로고
    • New tools for gene manipulation in chicken embryos
    • Bourikas D, Stoeckli ET. 2003. New tools for gene manipulation in chicken embryos. Oligonucleotides 13:411-419.
    • (2003) Oligonucleotides , vol.13 , pp. 411-419
    • Bourikas, D.1    Stoeckli, E.T.2
  • 16
    • 0034072921 scopus 로고    scopus 로고
    • Temporal control of protein synthesis during spermatogenesis
    • Braun RE. 2000. Temporal control of protein synthesis during spermatogenesis. Int. J. Androl. 23(Suppl 2):92-94.
    • (2000) Int. J. Androl. , vol.23 , Issue.SUPPL. 2 , pp. 92-94
    • Braun, R.E.1
  • 18
    • 71049153709 scopus 로고    scopus 로고
    • Cancer/testis (CT) antigens: Potential targets for immunotherapy
    • Caballero OL, Chen YT. 2009. Cancer/testis (CT) antigens: potential targets for immunotherapy. Cancer Sci. 100:2014-2021.
    • (2009) Cancer Sci. , vol.100 , pp. 2014-2021
    • Caballero, O.L.1    Chen, Y.T.2
  • 19
    • 34548548614 scopus 로고    scopus 로고
    • Combinatorial delivery of small interfering RNAs reduces RNAi efficacy by selective incorporation into RISC
    • Castanotto D, et al. 2007. Combinatorial delivery of small interfering RNAs reduces RNAi efficacy by selective incorporation into RISC. Nucleic Acids Res. 35:5154-5164.
    • (2007) Nucleic Acids Res. , vol.35 , pp. 5154-5164
    • Castanotto, D.1
  • 21
    • 18444380595 scopus 로고    scopus 로고
    • The double-stranded RNA-binding motif, a versatile macromolecular docking platform
    • Chang KY, Ramos A. 2005. The double-stranded RNA-binding motif, a versatile macromolecular docking platform. FEBS J. 272:2109-2117.
    • (2005) FEBS J. , vol.272 , pp. 2109-2117
    • Chang, K.Y.1    Ramos, A.2
  • 22
    • 23644433363 scopus 로고    scopus 로고
    • TRBP recruits the Dicer complex to Ago2 for microRNA processing and gene silencing
    • Chendrimada TP, et al. 2005. TRBP recruits the Dicer complex to Ago2 for microRNA processing and gene silencing. Nature 436:740-744.
    • (2005) Nature , vol.436 , pp. 740-744
    • Chendrimada, T.P.1
  • 23
    • 80052870811 scopus 로고    scopus 로고
    • A proteomic study of TAR-RNA binding protein (TRBP)-associated factors
    • Chi YH, Semmes OJ, Jeang KT. 2011. A proteomic study of TAR-RNA binding protein (TRBP)-associated factors. Cell Biosci. 1:9.
    • (2011) Cell Biosci. , vol.1 , pp. 9
    • Chi, Y.H.1    Semmes, O.J.2    Jeang, K.T.3
  • 24
    • 34248353881 scopus 로고    scopus 로고
    • Small interfering RNAs against the TAR RNA binding protein, TRBP, a Dicer cofactor, inhibit human immunodeficiency virus type 1 long terminal repeat expression and viral production
    • Christensen HS, et al. 2007. Small interfering RNAs against the TAR RNA binding protein, TRBP, a Dicer cofactor, inhibit human immunodeficiency virus type 1 long terminal repeat expression and viral production. J. Virol. 81:5121-5131.
    • (2007) J. Virol. , vol.81 , pp. 5121-5131
    • Christensen, H.S.1
  • 25
    • 70349283034 scopus 로고    scopus 로고
    • ADAR1 interacts with PKR during human immunodeficiency virus infection of lymphocytes and contributes to viral replication
    • Clerzius G, et al. 2009. ADAR1 interacts with PKR during human immunodeficiency virus infection of lymphocytes and contributes to viral replication. J. Virol. 83:10119-10128.
    • (2009) J. Virol. , vol.83 , pp. 10119-10128
    • Clerzius, G.1
  • 26
    • 79551616928 scopus 로고    scopus 로고
    • Multiple levels of PKR inhibition during HIV-1 replication
    • Clerzius G, Gélinas JF, Gatignol A. 2011. Multiple levels of PKR inhibition during HIV-1 replication. Rev. Med. Virol. 21:42-53.
    • (2011) Rev. Med. Virol. , vol.21 , pp. 42-53
    • Clerzius, G.1    Gélinas, J.F.2    Gatignol, A.3
  • 27
    • 0028865525 scopus 로고
    • Double-stranded-RNA-dependent protein kinase and TAR RNA-binding protein form homo- and heterodimers in vivo
    • Cosentino GP, et al. 1995. Double-stranded-RNA-dependent protein kinase and TAR RNA-binding protein form homo- and heterodimers in vivo. Proc. Natl. Acad. Sci. U. S. A. 92:9445-9449.
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 9445-9449
    • Cosentino, G.P.1
  • 28
    • 58149463628 scopus 로고    scopus 로고
    • TRBP control of PACT-induced phosphorylation of protein kinase R is reversed by stress
    • Daher A, et al. 2009. TRBP control of PACT-induced phosphorylation of protein kinase R is reversed by stress. Mol. Cell. Biol. 29:254-265.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 254-265
    • Daher, A.1
  • 29
    • 0035823590 scopus 로고    scopus 로고
    • Two dimerization domains in the trans-activation response RNA-binding protein (TRBP) individually reverse the protein kinase R inhibition of HIV-1 long terminal repeat expression
    • Daher A, et al. 2001. Two dimerization domains in the trans-activation response RNA-binding protein (TRBP) individually reverse the protein kinase R inhibition of HIV-1 long terminal repeat expression. J. Biol. Chem. 276:33899-33905.
    • (2001) J. Biol. Chem. , vol.276 , pp. 33899-33905
    • Daher, A.1
  • 30
    • 66249134258 scopus 로고    scopus 로고
    • Characterization of the TRBP domain required for dicer interaction and function in RNA interference
    • Daniels SM, et al. 2009. Characterization of the TRBP domain required for dicer interaction and function in RNA interference. BMC Mol. Biol. 10:38.
    • (2009) BMC Mol. Biol. , vol.10 , pp. 38
    • Daniels, S.M.1
  • 31
    • 0034052232 scopus 로고    scopus 로고
    • Analysis of a binding difference between the two dsRNA-binding domains in TRBP reveals the modular function of a KR-helix motif
    • Daviet L, et al. 2000. Analysis of a binding difference between the two dsRNA-binding domains in TRBP reveals the modular function of a KR-helix motif. Eur. J. Biochem. 267:2419-2431.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 2419-2431
    • Daviet, L.1
  • 32
    • 2242464840 scopus 로고    scopus 로고
    • The draft genome of Ciona intestinalis: Insights into chordate and vertebrate origins
    • Dehal P, et al. 2002. The draft genome of Ciona intestinalis: insights into chordate and vertebrate origins. Science 298:2157-2167.
    • (2002) Science , vol.298 , pp. 2157-2167
    • Dehal, P.1
  • 33
    • 1542510099 scopus 로고    scopus 로고
    • Theoretical foundation of the balanced minimum evolution method of phylogenetic inference and its relationship to weighted least-squares tree fitting
    • Desper R, Gascuel O. 2004. Theoretical foundation of the balanced minimum evolution method of phylogenetic inference and its relationship to weighted least-squares tree fitting. Mol. Biol. Evol. 21:587-598.
    • (2004) Mol. Biol. Evol. , vol.21 , pp. 587-598
    • Desper, R.1    Gascuel, O.2
  • 34
    • 21344457676 scopus 로고    scopus 로고
    • Lentivirus-mediated transduction of PKR into CD34(+) hematopoietic stem cells inhibits HIV-1 replication in differentiated T cell progeny
    • Dimitrova DI, et al. 2005. Lentivirus-mediated transduction of PKR into CD34(+) hematopoietic stem cells inhibits HIV-1 replication in differentiated T cell progeny. J. Interferon Cytokine Res. 25:345-360.
    • (2005) J. Interferon Cytokine Res. , vol.25 , pp. 345-360
    • Dimitrova, D.I.1
  • 35
    • 0030972471 scopus 로고    scopus 로고
    • Specific repression of Tax trans-activation by TAR RNA-binding protein TRBP
    • Donzeau M, Winnacker EL, Meisterernst M. 1997. Specific repression of Tax trans-activation by TAR RNA-binding protein TRBP. J. Virol. 71:2628-2635.
    • (1997) J. Virol. , vol.71 , pp. 2628-2635
    • Donzeau, M.1    Winnacker, E.L.2    Meisterernst, M.3
  • 36
    • 0038813691 scopus 로고    scopus 로고
    • The TAR RNA-binding protein, TRBP, stimulates the expression of TAR-containing RNAs in vitro and in vivo independently of its ability to inhibit the dsRNA-dependent kinase PKR
    • Dorin D, et al. 2003. The TAR RNA-binding protein, TRBP, stimulates the expression of TAR-containing RNAs in vitro and in vivo independently of its ability to inhibit the dsRNA-dependent kinase PKR. J. Biol. Chem. 278:4440-4448.
    • (2003) J. Biol. Chem. , vol.278 , pp. 4440-4448
    • Dorin, D.1
  • 37
    • 0036966283 scopus 로고    scopus 로고
    • New and old roles of the double-stranded RNA-binding domain
    • Doyle M, Jantsch MF. 2002. New and old roles of the double-stranded RNA-binding domain. J. Struct. Biol. 140:147-153.
    • (2002) J. Struct. Biol. , vol.140 , pp. 147-153
    • Doyle, M.1    Jantsch, M.F.2
  • 38
    • 0033773221 scopus 로고    scopus 로고
    • Characterization of TRBP1 and TRBP2. Stable stem-loop structure at the 5′ end of TRBP2 mRNA resembles HIV-1 TAR and is not found in its processed pseudogene
    • Duarte M, et al. 2000. Characterization of TRBP1 and TRBP2. Stable stem-loop structure at the 5′ end of TRBP2 mRNA resembles HIV-1 TAR and is not found in its processed pseudogene. J. Biomed. Sci. 7:494-506.
    • (2000) J. Biomed. Sci. , vol.7 , pp. 494-506
    • Duarte, M.1
  • 39
    • 78650904206 scopus 로고    scopus 로고
    • Long-term inhibition of HIV-1 replication with RNA interference against cellular cofactors
    • Eekels JJ, Geerts D, Jeeninga RE, Berkhout B. 2011. Long-term inhibition of HIV-1 replication with RNA interference against cellular cofactors. Antiviral Res. 89:43-53.
    • (2011) Antiviral Res. , vol.89 , pp. 43-53
    • Eekels, J.J.1    Geerts, D.2    Jeeninga, R.E.3    Berkhout, B.4
  • 40
    • 0032568856 scopus 로고    scopus 로고
    • An Arg/Lys-rich core peptide mimics TRBP binding to the HIV-1 TAR RNA upper-stem/loop
    • Erard M, Barker DG, Amalric F, Jeang KT, Gatignol A. 1998. An Arg/Lys-rich core peptide mimics TRBP binding to the HIV-1 TAR RNA upper-stem/loop. J. Mol. Biol. 279:1085-1099.
    • (1998) J. Mol. Biol. , vol.279 , pp. 1085-1099
    • Erard, M.1    Barker, D.G.2    Amalric, F.3    Jeang, K.T.4    Gatignol, A.5
  • 41
    • 77953629046 scopus 로고    scopus 로고
    • Regulation of mRNA translation and stability by microRNAs
    • Fabian MR, Sonenberg N, Filipowicz W. 2010. Regulation of mRNA translation and stability by microRNAs. Annu. Rev. Biochem. 79:351-379.
    • (2010) Annu. Rev. Biochem. , vol.79 , pp. 351-379
    • Fabian, M.R.1    Sonenberg, N.2    Filipowicz, W.3
  • 42
    • 79952390996 scopus 로고    scopus 로고
    • Ebolavirus proteins suppress the effects of small interfering RNA by direct interaction with the mammalian RNA interference pathway
    • Fabozzi G, Nabel CS, Dolan MA, Sullivan NJ. 2011. Ebolavirus proteins suppress the effects of small interfering RNA by direct interaction with the mammalian RNA interference pathway. J. Virol. 85:2512-2523.
    • (2011) J. Virol. , vol.85 , pp. 2512-2523
    • Fabozzi, G.1    Nabel, C.S.2    Dolan, M.A.3    Sullivan, N.J.4
  • 43
    • 0032545933 scopus 로고    scopus 로고
    • Potent and specific genetic interference by double-stranded RNA in Caenorhabditis elegans
    • Fire A, et al. 1998. Potent and specific genetic interference by double-stranded RNA in Caenorhabditis elegans. Nature 391:806-811.
    • (1998) Nature , vol.391 , pp. 806-811
    • Fire, A.1
  • 44
    • 22744433240 scopus 로고    scopus 로고
    • Normal microRNA maturation and germline stem cell maintenance requires Loquacious, a double-stranded RNA-binding domain protein
    • doi:10.1371/journal.pbio.0030236
    • Förstemann K, et al. 2005. Normal microRNA maturation and germline stem cell maintenance requires Loquacious, a double-stranded RNA-binding domain protein. PLoS Biol. 3 :e236. doi:10.1371/journal.pbio.0030236.
    • (2005) PLoS Biol. , vol.3
    • Förstemann, K.1
  • 45
    • 78149416948 scopus 로고    scopus 로고
    • The activity and expression of microRNAs in prostate cancers
    • Fu X, Xue C, Huang Y, Xie Y, Li Y. 2010. The activity and expression of microRNAs in prostate cancers. Mol. Biosyst. 6:2561-2572.
    • (2010) Mol. Biosyst. , vol.6 , pp. 2561-2572
    • Fu, X.1    Xue, C.2    Huang, Y.3    Xie, Y.4    Li, Y.5
  • 46
    • 0343431521 scopus 로고    scopus 로고
    • Translational control of viral gene expression in eukaryotes
    • Gale M, Jr, Tan SL, Katze MG. 2000. Translational control of viral gene expression in eukaryotes. Microbiol. Mol. Biol. Rev. 64:239-280.
    • (2000) Microbiol. Mol. Biol. Rev. , vol.64 , pp. 239-280
    • Gale Jr., M.1    Tan, S.L.2    Katze, M.G.3
  • 47
    • 75149139029 scopus 로고    scopus 로고
    • Hepatitis C virus blocks interferon effector function by inducing protein kinase R phosphorylation
    • Garaigorta U, Chisari FV. 2009. Hepatitis C virus blocks interferon effector function by inducing protein kinase R phosphorylation. Cell Host Microbe 6:513-522.
    • (2009) Cell Host Microbe , vol.6 , pp. 513-522
    • Garaigorta, U.1    Chisari, F.V.2
  • 48
    • 33845627785 scopus 로고    scopus 로고
    • Impact of protein kinase PKR in cell biology: From antiviral to antiproliferative action
    • García MA, et al. 2006. Impact of protein kinase PKR in cell biology: from antiviral to antiproliferative action. Microbiol. Mol. Biol. Rev. 70:1032-1060.
    • (2006) Microbiol. Mol. Biol. Rev. , vol.70 , pp. 1032-1060
    • García, M.A.1
  • 49
    • 34347225099 scopus 로고    scopus 로고
    • The dsRNA protein kinase PKR: Virus and cell control
    • García MA, Meurs EF, Esteban M. 2007. The dsRNA protein kinase PKR: virus and cell control. Biochimie 89:799-811.
    • (2007) Biochimie , vol.89 , pp. 799-811
    • García, M.A.1    Meurs, E.F.2    Esteban, M.3
  • 50
    • 77957561284 scopus 로고    scopus 로고
    • Reassessing the TARBP2 mutation rate in hereditary nonpolyposis colorectal cancer
    • Garre P, Perez-Segura P, Diaz-Rubio E, Caldes T, de la Hoya M. 2010. Reassessing the TARBP2 mutation rate in hereditary nonpolyposis colorectal cancer. Nat. Genet. 42:817-818.
    • (2010) Nat. Genet. , vol.42 , pp. 817-818
    • Garre, P.1    Perez-Segura, P.2    Diaz-Rubio, E.3    Caldes, T.4    De La Hoya, M.5
  • 51
    • 0027478445 scopus 로고
    • Relatedness of an RNA-binding motif in human immunodeficiency virus type 1 TAR RNA-binding protein TRBP to human P1/dsI kinase and Drosophila staufen
    • Gatignol A, Buckler C, Jeang KT. 1993. Relatedness of an RNA-binding motif in human immunodeficiency virus type 1 TAR RNA-binding protein TRBP to human P1/dsI kinase and Drosophila staufen. Mol. Cell. Biol. 13:2193-2202.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 2193-2202
    • Gatignol, A.1    Buckler, C.2    Jeang, K.T.3
  • 52
    • 0025876881 scopus 로고
    • Characterization of a human TAR RNA-binding protein that activates the HIV-1 LTR
    • Gatignol A, Buckler-White A, Berkhout B, Jeang KT. 1991. Characterization of a human TAR RNA-binding protein that activates the HIV-1 LTR. Science 251:1597-1600.
    • (1991) Science , vol.251 , pp. 1597-1600
    • Gatignol, A.1    Buckler-White, A.2    Berkhout, B.3    Jeang, K.T.4
  • 53
    • 0029693144 scopus 로고    scopus 로고
    • Sequential steps in Tat trans-activation of HIV-1 mediated through cellular DNA, RNA, and protein binding factors
    • Gatignol A, Duarte M, Daviet L, Chang YN, Jeang KT. 1996. Sequential steps in Tat trans-activation of HIV-1 mediated through cellular DNA, RNA, and protein binding factors. Gene Expr. 5:217-228.
    • (1996) Gene Expr. , vol.5 , pp. 217-228
    • Gatignol, A.1    Duarte, M.2    Daviet, L.3    Chang, Y.N.4    Jeang, K.T.5
  • 55
    • 27744458277 scopus 로고    scopus 로고
    • Dual role of TRBP in HIV replication and RNA interference: Viral diversion of a cellular pathway or evasion from antiviral immunity?
    • doi:10.1186/1742-4690-2-65
    • Gatignol A, Lainé S, Clerzius G. 2005. Dual role of TRBP in HIV replication and RNA interference: viral diversion of a cellular pathway or evasion from antiviral immunity? Retrovirology 2:65. doi:10.1186/1742-4690-2-65.
    • (2005) Retrovirology , vol.2 , pp. 65
    • Gatignol, A.1    Lainé, S.2    Clerzius, G.3
  • 56
    • 80052339434 scopus 로고    scopus 로고
    • Enhancement of replication of RNA viruses by ADAR1 via RNA editing and inhibition of RNA-activated protein kinase
    • Gélinas JF, Clerzius G, Shaw E, Gatignol A. 2011. Enhancement of replication of RNA viruses by ADAR1 via RNA editing and inhibition of RNA-activated protein kinase. J. Virol. 85:8460-8466.
    • (2011) J. Virol. , vol.85 , pp. 8460-8466
    • Gélinas, J.F.1    Clerzius, G.2    Shaw, E.3    Gatignol, A.4
  • 57
    • 0032889273 scopus 로고    scopus 로고
    • Diminished production of human immunodeficiency virus type 1 in astrocytes results from inefficient translation of gag, env, and nef mRNAs despite efficient expression of Tat and Rev
    • Gorry PR, et al. 1999. Diminished production of human immunodeficiency virus type 1 in astrocytes results from inefficient translation of gag, env, and nef mRNAs despite efficient expression of Tat and Rev. J. Virol. 73:352-361.
    • (1999) J. Virol. , vol.73 , pp. 352-361
    • Gorry, P.R.1
  • 58
    • 2142708770 scopus 로고    scopus 로고
    • Astrocyte infection by HIV-1: Mechanisms of restricted virus replication, and role in the pathogenesis of HIV-1-associated dementia
    • Gorry PR, et al. 2003. Astrocyte infection by HIV-1: mechanisms of restricted virus replication, and role in the pathogenesis of HIV-1-associated dementia. Curr. HIV Res. 1:463-473.
    • (2003) Curr. HIV Res. , vol.1 , pp. 463-473
    • Gorry, P.R.1
  • 60
    • 27744537851 scopus 로고    scopus 로고
    • Human RISC couples microRNA biogenesis and posttranscriptional gene silencing
    • Gregory RI, Chendrimada TP, Cooch N, Shiekhattar R. 2005. Human RISC couples microRNA biogenesis and posttranscriptional gene silencing. Cell 123:631-640.
    • (2005) Cell , vol.123 , pp. 631-640
    • Gregory, R.I.1    Chendrimada, T.P.2    Cooch, N.3    Shiekhattar, R.4
  • 61
    • 0028818963 scopus 로고
    • Estimation of the number of amino acid substitutions per site when the substitution rate varies among sites
    • Grishin NV. 1995. Estimation of the number of amino acid substitutions per site when the substitution rate varies among sites. J. Mol. Evol. 41:675-679.
    • (1995) J. Mol. Evol. , vol.41 , pp. 675-679
    • Grishin, N.V.1
  • 62
    • 79952070466 scopus 로고    scopus 로고
    • Virus-encoded microRNAs
    • Grundhoff A, Sullivan CS. 2011. Virus-encoded microRNAs. Virology 411:325-343.
    • (2011) Virology , vol.411 , pp. 325-343
    • Grundhoff, A.1    Sullivan, C.S.2
  • 63
    • 79959366354 scopus 로고    scopus 로고
    • Thermodynamic stability of small hairpin RNAs highly influences the loading process of different mammalian Argonautes
    • Gu S, et al. 2011. Thermodynamic stability of small hairpin RNAs highly influences the loading process of different mammalian Argonautes. Proc. Natl. Acad. Sci. U. S. A. 108:9208-9213.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 9208-9213
    • Gu, S.1
  • 64
    • 0142247418 scopus 로고    scopus 로고
    • The carboxy-terminal, M3 motifs of PACT and TRBP have opposite effects on PKR activity
    • Gupta V, Huang X, Patel RC. 2003. The carboxy-terminal, M3 motifs of PACT and TRBP have opposite effects on PKR activity. Virology 315:283-291.
    • (2003) Virology , vol.315 , pp. 283-291
    • Gupta, V.1    Huang, X.2    Patel, R.C.3
  • 65
    • 27144550559 scopus 로고    scopus 로고
    • TRBP, a regulator of cellular PKR and HIV-1 virus expression, interacts with Dicer and functions in RNA silencing
    • Haase AD, et al. 2005. TRBP, a regulator of cellular PKR and HIV-1 virus expression, interacts with Dicer and functions in RNA silencing. EMBO Rep. 6:961-967.
    • (2005) EMBO Rep. , vol.6 , pp. 961-967
    • Haase, A.D.1
  • 66
    • 4444248655 scopus 로고    scopus 로고
    • Oligomerization activity of a double-stranded RNA-binding domain
    • Hitti EG, Sallacz NB, Schoft VK, Jantsch MF. 2004. Oligomerization activity of a double-stranded RNA-binding domain. FEBS Lett. 574:25-30.
    • (2004) FEBS Lett. , vol.574 , pp. 25-30
    • Hitti, E.G.1    Sallacz, N.B.2    Schoft, V.K.3    Jantsch, M.F.4
  • 67
    • 43549096196 scopus 로고    scopus 로고
    • The Argonaute protein family
    • Hock J, Meister G. 2008. The Argonaute protein family. Genome Biol. 9:210.
    • (2008) Genome Biol. , vol.9 , pp. 210
    • Hock, J.1    Meister, G.2
  • 68
    • 0037103840 scopus 로고    scopus 로고
    • The C-terminal, third conserved motif of the protein activator PACT plays an essential role in the activation of double-stranded-RNA-dependent protein kinase (PKR)
    • Huang X, Hutchins B, Patel RC. 2002. The C-terminal, third conserved motif of the protein activator PACT plays an essential role in the activation of double-stranded-RNA-dependent protein kinase (PKR). Biochem. J. 366:175-186.
    • (2002) Biochem. J. , vol.366 , pp. 175-186
    • Huang, X.1    Hutchins, B.2    Patel, R.C.3
  • 69
    • 37549014207 scopus 로고    scopus 로고
    • Argonaute proteins: Key players in RNA silencing
    • Hutvagner G, Simard MJ. 2008. Argonaute proteins: key players in RNA silencing. Nat. Rev. Mol. Cell Biol. 9:22-32.
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 22-32
    • Hutvagner, G.1    Simard, M.J.2
  • 70
    • 0033056848 scopus 로고    scopus 로고
    • RAX, a cellular activator for double-stranded RNA-dependent protein kinase during stress signaling
    • Ito T, Yang M, May WS. 1999. RAX, a cellular activator for double-stranded RNA-dependent protein kinase during stress signaling. J. Biol. Chem. 274:15427-15432.
    • (1999) J. Biol. Chem. , vol.274 , pp. 15427-15432
    • Ito, T.1    Yang, M.2    May, W.S.3
  • 72
    • 79960658055 scopus 로고    scopus 로고
    • Inhibition of RNase L and RNA-dependent protein kinase (PKR) by sunitinib impairs antiviral innate immunity
    • Jha BK, et al. 2011. Inhibition of RNase L and RNA-dependent protein kinase (PKR) by sunitinib impairs antiviral innate immunity. J. Biol. Chem. 286:26319-26326.
    • (2011) J. Biol. Chem. , vol.286 , pp. 26319-26326
    • Jha, B.K.1
  • 73
    • 24644483623 scopus 로고    scopus 로고
    • Modulation of hepatitis C virus RNA abundance by a liver-specific microRNA
    • Jopling CL, Yi M, Lancaster AM, Lemon SM, Sarnow P. 2005. Modulation of hepatitis C virus RNA abundance by a liver-specific microRNA. Science 309:1577-1581.
    • (2005) Science , vol.309 , pp. 1577-1581
    • Jopling, C.L.1    Yi, M.2    Lancaster, A.M.3    Lemon, S.M.4    Sarnow, P.5
  • 74
    • 79751485564 scopus 로고    scopus 로고
    • The many faces of RNAi
    • Ketting RF. 2011. The many faces of RNAi. Dev. Cell 20:148-161.
    • (2011) Dev. Cell , vol.20 , pp. 148-161
    • Ketting, R.F.1
  • 76
    • 33748368912 scopus 로고    scopus 로고
    • Argonaute-1 directs siRNA-mediated transcriptional gene silencing in human cells
    • Kim DH, Villeneuve LM, Morris KV, Rossi JJ. 2006. Argonaute-1 directs siRNA-mediated transcriptional gene silencing in human cells. Nat. Struct. Mol. Biol. 13:793-797.
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 793-797
    • Kim, D.H.1    Villeneuve, L.M.2    Morris, K.V.3    Rossi, J.J.4
  • 77
    • 77952756515 scopus 로고    scopus 로고
    • Somatic mutations and losses of expression of microRNA regulation-related genes AGO2 and TNRC6A in gastric and colorectal cancers
    • Kim MS, et al. 2010. Somatic mutations and losses of expression of microRNA regulation-related genes AGO2 and TNRC6A in gastric and colorectal cancers. J. Pathol. 221:139-146.
    • (2010) J. Pathol. , vol.221 , pp. 139-146
    • Kim, M.S.1
  • 78
    • 70350442453 scopus 로고    scopus 로고
    • Effect of siRNA terminal mismatches on TRBP and Dicer binding and silencing efficacy
    • Kini HK, Walton SP. 2009. Effect of siRNA terminal mismatches on TRBP and Dicer binding and silencing efficacy. FEBS J. 276:6576-6585.
    • (2009) FEBS J. , vol.276 , pp. 6576-6585
    • Kini, H.K.1    Walton, S.P.2
  • 79
    • 34547115237 scopus 로고    scopus 로고
    • Human TRBP and PACT directly interact with each other and associate with dicer to facilitate the production of small interfering RNA
    • Kok KH, Ng MH, Ching YP, Jin DY. 2007. Human TRBP and PACT directly interact with each other and associate with dicer to facilitate the production of small interfering RNA. J. Biol. Chem. 282:17649-17657.
    • (2007) J. Biol. Chem. , vol.282 , pp. 17649-17657
    • Kok, K.H.1    Ng, M.H.2    Ching, Y.P.3    Jin, D.Y.4
  • 80
    • 0026701570 scopus 로고
    • Malignant transformation by a mutant of the IFN-inducible dsRNA-dependent protein kinase
    • Koromilas AE, Roy S, Barber GN, Katze MG, Sonenberg N. 1992. Malignant transformation by a mutant of the IFN-inducible dsRNA-dependent protein kinase. Science 257:1685-1689.
    • (1992) Science , vol.257 , pp. 1685-1689
    • Koromilas, A.E.1    Roy, S.2    Barber, G.N.3    Katze, M.G.4    Sonenberg, N.5
  • 81
    • 82755170606 scopus 로고    scopus 로고
    • The role of Dicer protein partners in the processing of microRNA precursors
    • doi:10.1371/journal.pone.0028548
    • Koscianska E, Starega-Roslan J, Krzyzosiak WJ. 2011. The role of Dicer protein partners in the processing of microRNA precursors. PLoS One 6:e28548. doi:10.1371/journal.pone.0028548.
    • (2011) PLoS One , vol.6
    • Koscianska, E.1    Starega-Roslan, J.2    Krzyzosiak, W.J.3
  • 82
    • 0028952477 scopus 로고
    • Genetic mapping in human and mouse of the locus encoding TRBP, a protein that binds the TAR region of the human immunodeficiency virus (HIV-1)
    • Kozak CA, Gatignol A, Graham K, Jeang KT, McBride OW. 1995. Genetic mapping in human and mouse of the locus encoding TRBP, a protein that binds the TAR region of the human immunodeficiency virus (HIV-1). Genomics 25:66-72.
    • (1995) Genomics , vol.25 , pp. 66-72
    • Kozak, C.A.1    Gatignol, A.2    Graham, K.3    Jeang, K.T.4    McBride, O.W.5
  • 83
    • 77955902024 scopus 로고    scopus 로고
    • The widespread regulation of microRNA biogenesis, function and decay
    • Krol J, Loedige I, Filipowicz W. 2010. The widespread regulation of microRNA biogenesis, function and decay. Nat. Rev. Genet. 11:597-610.
    • (2010) Nat. Rev. Genet. , vol.11 , pp. 597-610
    • Krol, J.1    Loedige, I.2    Filipowicz, W.3
  • 84
    • 45849141942 scopus 로고    scopus 로고
    • Interactions between the double-stranded RNA-binding proteins TRBP and PACT define the Medipal domain that mediates protein-protein interactions
    • Laraki G, et al. 2008. Interactions between the double-stranded RNA-binding proteins TRBP and PACT define the Medipal domain that mediates protein-protein interactions. RNA Biol. 5:92-103.
    • (2008) RNA Biol. , vol.5 , pp. 92-103
    • Laraki, G.1
  • 85
    • 70349767012 scopus 로고    scopus 로고
    • Structure of the human Dicer-TRBP complex by electron microscopy
    • Lau PW, Potter CS, Carragher B, MacRae IJ. 2009. Structure of the human Dicer-TRBP complex by electron microscopy. Structure 17:1326-1332.
    • (2009) Structure , vol.17 , pp. 1326-1332
    • Lau, P.W.1    Potter, C.S.2    Carragher, B.3    MacRae, I.J.4
  • 86
    • 17644363376 scopus 로고    scopus 로고
    • A cellular microRNA mediates antiviral defense in human cells
    • Lecellier CH, et al. 2005. A cellular microRNA mediates antiviral defense in human cells. Science 308:557-560.
    • (2005) Science , vol.308 , pp. 557-560
    • Lecellier, C.H.1
  • 87
    • 3142702108 scopus 로고    scopus 로고
    • Merlin, a tumor suppressor, interacts with transactivation-responsive RNA-binding protein and inhibits its oncogenic activity
    • Lee JY, et al. 2004. Merlin, a tumor suppressor, interacts with transactivation-responsive RNA-binding protein and inhibits its oncogenic activity. J. Biol. Chem. 279:30265-30273.
    • (2004) J. Biol. Chem. , vol.279 , pp. 30265-30273
    • Lee, J.Y.1
  • 88
    • 33644527303 scopus 로고    scopus 로고
    • Merlin facilitates ubiquitination and degradation of transactivation- responsive RNA-binding protein
    • Lee JY, et al. 2006. Merlin facilitates ubiquitination and degradation of transactivation-responsive RNA-binding protein. Oncogene 25:1143-1152.
    • (2006) Oncogene , vol.25 , pp. 1143-1152
    • Lee, J.Y.1
  • 89
    • 0029977347 scopus 로고    scopus 로고
    • A testis cytoplasmic RNA-binding protein that has the properties of a translational repressor
    • Lee K, Fajardo MA, Braun RE. 1996. A testis cytoplasmic RNA-binding protein that has the properties of a translational repressor. Mol. Cell. Biol. 16:3023-3034.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 3023-3034
    • Lee, K.1    Fajardo, M.A.2    Braun, R.E.3
  • 90
    • 32544460452 scopus 로고    scopus 로고
    • The role of PACT in the RNA silencing pathway
    • Lee Y, et al. 2006. The role of PACT in the RNA silencing pathway. EMBO J. 25:522-532.
    • (2006) EMBO J. , vol.25 , pp. 522-532
    • Lee, Y.1
  • 91
    • 0346786216 scopus 로고    scopus 로고
    • PACT-mediated enhancement of reporter gene expression at the translational level
    • Li S, Sen GC. 2003. PACT-mediated enhancement of reporter gene expression at the translational level. J. Interferon Cytokine Res. 23:689-697.
    • (2003) J. Interferon Cytokine Res. , vol.23 , pp. 689-697
    • Li, S.1    Sen, G.C.2
  • 92
    • 70350005156 scopus 로고    scopus 로고
    • Binding and cleavage specificities of human Argonaute2
    • Lima WF, et al. 2009. Binding and cleavage specificities of human Argonaute2. J. Biol. Chem. 284:26017-26028.
    • (2009) J. Biol. Chem. , vol.284 , pp. 26017-26028
    • Lima, W.F.1
  • 93
    • 77953635299 scopus 로고    scopus 로고
    • Biochemical principles of small RNA pathways
    • Liu Q, Paroo Z. 2010. Biochemical principles of small RNA pathways. Annu. Rev. Biochem. 79:295-319.
    • (2010) Annu. Rev. Biochem. , vol.79 , pp. 295-319
    • Liu, Q.1    Paroo, Z.2
  • 94
    • 0141868916 scopus 로고    scopus 로고
    • R2D2, a bridge between the initiation and effector steps of the Drosophila RNAi pathway
    • Liu Q, et al. 2003. R2D2, a bridge between the initiation and effector steps of the Drosophila RNAi pathway. Science 301:1921-1925.
    • (2003) Science , vol.301 , pp. 1921-1925
    • Liu, Q.1
  • 95
    • 44649136660 scopus 로고    scopus 로고
    • Autoinhibition of human dicer by its internal helicase domain
    • Ma E, MacRae IJ, Kirsch JF, Doudna JA. 2008. Autoinhibition of human dicer by its internal helicase domain. J. Mol. Biol. 380:237-243.
    • (2008) J. Mol. Biol. , vol.380 , pp. 237-243
    • Ma, E.1    MacRae, I.J.2    Kirsch, J.F.3    Doudna, J.A.4
  • 98
    • 30644463858 scopus 로고    scopus 로고
    • Inhibition of anatid herpes virus-1 replication by small interfering RNAs in cell culture system
    • Mallanna SK, et al. 2006. Inhibition of anatid herpes virus-1 replication by small interfering RNAs in cell culture system. Virus Res. 115:192-197.
    • (2006) Virus Res. , vol.115 , pp. 192-197
    • Mallanna, S.K.1
  • 99
    • 29144431656 scopus 로고    scopus 로고
    • A human, ATP-independent, RISC assembly machine fueled by pre-miRNA
    • Maniataki E, Mourelatos Z. 2005. A human, ATP-independent, RISC assembly machine fueled by pre-miRNA. Genes Dev. 19:2979-2990.
    • (2005) Genes Dev. , vol.19 , pp. 2979-2990
    • Maniataki, E.1    Mourelatos, Z.2
  • 100
    • 79952717616 scopus 로고    scopus 로고
    • Small molecule enoxacin is a cancer-specific growth inhibitor that acts by enhancing TAR RNA-binding protein 2-mediated microRNA processing
    • Melo S, et al. 2011. Small molecule enoxacin is a cancer-specific growth inhibitor that acts by enhancing TAR RNA-binding protein 2-mediated microRNA processing. Proc. Natl. Acad. Sci. U. S. A. 108:4394-4399.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 4394-4399
    • Melo, S.1
  • 101
    • 61349127117 scopus 로고    scopus 로고
    • A TARBP2 mutation in human cancer impairs microRNA processing and DICER1 function
    • Melo SA, et al. 2009. A TARBP2 mutation in human cancer impairs microRNA processing and DICER1 function. Nat. Genet. 41:365-370.
    • (2009) Nat. Genet. , vol.41 , pp. 365-370
    • Melo, S.A.1
  • 102
    • 0025298202 scopus 로고
    • Molecular cloning and characterization of the human double-stranded RNA-activated protein kinase induced by interferon
    • Meurs E, et al. 1990. Molecular cloning and characterization of the human double-stranded RNA-activated protein kinase induced by interferon. Cell 62:379-390.
    • (1990) Cell , vol.62 , pp. 379-390
    • Meurs, E.1
  • 104
    • 77952509193 scopus 로고    scopus 로고
    • Uncovering the PKR pathway's potential for treatment of tumors
    • Mounir Z, Koromilas AE. 2010. Uncovering the PKR pathway's potential for treatment of tumors. Future Oncol. 6:643-645.
    • (2010) Future Oncol. , vol.6 , pp. 643-645
    • Mounir, Z.1    Koromilas, A.E.2
  • 105
    • 41749116632 scopus 로고    scopus 로고
    • The evolution of core proteins involved in microRNA biogenesis
    • Murphy D, Dancis B, Brown JR. 2008. The evolution of core proteins involved in microRNA biogenesis. BMC Evol. Biol. 8:92.
    • (2008) BMC Evol. Biol. , vol.8 , pp. 92
    • Murphy, D.1    Dancis, B.2    Brown, J.R.3
  • 106
    • 33846073016 scopus 로고    scopus 로고
    • Double-stranded RNA deaminase ADAR1 increases host susceptibility to virus infection
    • Nie Y, Hammond GL, Yang JH. 2007. Double-stranded RNA deaminase ADAR1 increases host susceptibility to virus infection. J. Virol. 81:917-923.
    • (2007) J. Virol. , vol.81 , pp. 917-923
    • Nie, Y.1    Hammond, G.L.2    Yang, J.H.3
  • 107
    • 77952293063 scopus 로고    scopus 로고
    • Functions and regulation of RNA editing by ADAR deaminases
    • Nishikura K. 2010. Functions and regulation of RNA editing by ADAR deaminases. Annu. Rev. Biochem. 79:321-349.
    • (2010) Annu. Rev. Biochem. , vol.79 , pp. 321-349
    • Nishikura, K.1
  • 108
    • 79959872313 scopus 로고    scopus 로고
    • siRNA repositioning for guide strand selection by human Dicer complexes
    • Noland CL, Ma E, Doudna JA. 2011. siRNA repositioning for guide strand selection by human Dicer complexes. Mol. Cell 43:110-121.
    • (2011) Mol. Cell , vol.43 , pp. 110-121
    • Noland, C.L.1    Ma, E.2    Doudna, J.A.3
  • 109
    • 26444619796 scopus 로고    scopus 로고
    • Low TRBP levels support an innate human immunodeficiency virus type 1 resistance in astrocytes by enhancing the PKR antiviral response
    • Ong CL, et al. 2005. Low TRBP levels support an innate human immunodeficiency virus type 1 resistance in astrocytes by enhancing the PKR antiviral response. J. Virol. 79:12763-12772.
    • (2005) J. Virol. , vol.79 , pp. 12763-12772
    • Ong, C.L.1
  • 110
    • 34249857539 scopus 로고    scopus 로고
    • COBALT: Constraint-based alignment tool for multiple protein sequences
    • Papadopoulos JS, Agarwala R. 2007. COBALT: constraint-based alignment tool for multiple protein sequences. Bioinformatics 23:1073-1079.
    • (2007) Bioinformatics , vol.23 , pp. 1073-1079
    • Papadopoulos, J.S.1    Agarwala, R.2
  • 111
    • 67749145232 scopus 로고    scopus 로고
    • Hsp90 regulates the function of argonaute 2 and its recruitment to stress granules and P-bodies
    • Pare JM, et al. 2009. Hsp90 regulates the function of argonaute 2 and its recruitment to stress granules and P-bodies. Mol. Biol. Cell 20:3273-3284.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 3273-3284
    • Pare, J.M.1
  • 112
    • 0028242864 scopus 로고
    • TAR RNA-binding protein is an inhibitor of the interferon-induced protein kinase PKR
    • Park H, et al. 1994. TAR RNA-binding protein is an inhibitor of the interferon-induced protein kinase PKR. Proc. Natl. Acad. Sci. U. S. A. 91:4713-4717.
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 4713-4717
    • Park, H.1
  • 113
    • 56249098241 scopus 로고    scopus 로고
    • dsRNA binding properties of RDE-4 and TRBP reflect their distinct roles in RNAi
    • Parker GS, Maity TS, Bass BL. 2008. dsRNA binding properties of RDE-4 and TRBP reflect their distinct roles in RNAi. J. Mol. Biol. 384:967-979.
    • (2008) J. Mol. Biol. , vol.384 , pp. 967-979
    • Parker, G.S.1    Maity, T.S.2    Bass, B.L.3
  • 114
    • 70349577785 scopus 로고    scopus 로고
    • Phosphorylation of the human microRNA-generating complex mediates MAPK/Erk signaling
    • Paroo Z, Ye X, Chen S, Liu Q. 2009. Phosphorylation of the human microRNA-generating complex mediates MAPK/Erk signaling. Cell 139:112-122.
    • (2009) Cell , vol.139 , pp. 112-122
    • Paroo, Z.1    Ye, X.2    Chen, S.3    Liu, Q.4
  • 115
    • 0034531395 scopus 로고    scopus 로고
    • PACT, a stress-modulated cellular activator of interferon-induced double-stranded RNA-activated protein kinase, PKR
    • Patel CV, Handy I, Goldsmith T, Patel RC. 2000. PACT, a stress-modulated cellular activator of interferon-induced double-stranded RNA-activated protein kinase, PKR. J. Biol. Chem. 275:37993-37998.
    • (2000) J. Biol. Chem. , vol.275 , pp. 37993-37998
    • Patel, C.V.1    Handy, I.2    Goldsmith, T.3    Patel, R.C.4
  • 116
    • 0032480017 scopus 로고    scopus 로고
    • PACT, a protein activator of the interferon-induced protein kinase, PKR
    • Patel RC, Sen GC. 1998. PACT, a protein activator of the interferon-induced protein kinase, PKR. EMBO J. 17:4379-4390.
    • (1998) EMBO J. , vol.17 , pp. 4379-4390
    • Patel, R.C.1    Sen, G.C.2
  • 117
    • 70349260534 scopus 로고    scopus 로고
    • The interferon system and vaccinia virus evasion mechanisms
    • Perdiguero B, Esteban M. 2009. The interferon system and vaccinia virus evasion mechanisms. J. Interferon Cytokine Res. 29:581-598.
    • (2009) J. Interferon Cytokine Res. , vol.29 , pp. 581-598
    • Perdiguero, B.1    Esteban, M.2
  • 118
    • 64549113058 scopus 로고    scopus 로고
    • Protein components of the microRNA pathway and human diseases
    • Perron MP, Provost P. 2009. Protein components of the microRNA pathway and human diseases. Methods Mol. Biol. 487:369-385.
    • (2009) Methods Mol. Biol. , vol.487 , pp. 369-385
    • Perron, M.P.1    Provost, P.2
  • 119
    • 0035012516 scopus 로고    scopus 로고
    • Modular structure of PACT: Distinct domains for binding and activating PKR
    • Peters GA, Hartmann R, Qin J, Sen GC. 2001. Modular structure of PACT: distinct domains for binding and activating PKR. Mol. Cell. Biol. 21:1908-1920.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 1908-1920
    • Peters, G.A.1    Hartmann, R.2    Qin, J.3    Sen, G.C.4
  • 120
    • 33845746006 scopus 로고    scopus 로고
    • Phosphorylation of specific serine residues in the PKR activation domain of PACT is essential for its ability to mediate apoptosis
    • Peters GA, Li S, Sen GC. 2006. Phosphorylation of specific serine residues in the PKR activation domain of PACT is essential for its ability to mediate apoptosis. J. Biol. Chem. 281:35129-35136.
    • (2006) J. Biol. Chem. , vol.281 , pp. 35129-35136
    • Peters, G.A.1    Li, S.2    Sen, G.C.3
  • 121
    • 78651488459 scopus 로고    scopus 로고
    • The role of protein kinase R in the interferon response
    • Pindel A, Sadler A. 2011. The role of protein kinase R in the interferon response. J. Interferon Cytokine Res. 31:59-70.
    • (2011) J. Interferon Cytokine Res. , vol.31 , pp. 59-70
    • Pindel, A.1    Sadler, A.2
  • 122
    • 27344452745 scopus 로고    scopus 로고
    • Mammalian Dicer finds a partner
    • Rossi JJ. 2005. Mammalian Dicer finds a partner. EMBO Rep. 6:927-929.
    • (2005) EMBO Rep. , vol.6 , pp. 927-929
    • Rossi, J.J.1
  • 123
    • 0027245423 scopus 로고
    • Alteration in a new gene encoding a putative membrane-organizing protein causes neuro-fibromatosis type 2
    • Rouleau GA, et al. 1993. Alteration in a new gene encoding a putative membrane-organizing protein causes neuro-fibromatosis type 2. Nature 363:515-521.
    • (1993) Nature , vol.363 , pp. 515-521
    • Rouleau, G.A.1
  • 124
    • 33645812734 scopus 로고    scopus 로고
    • A role of the double-stranded RNA-binding protein PACT in mouse ear development and hearing
    • Rowe TM, Rizzi M, Hirose K, Peters GA, Sen GC. 2006. A role of the double-stranded RNA-binding protein PACT in mouse ear development and hearing. Proc. Natl. Acad. Sci. U. S. A. 103:5823-5828.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 5823-5828
    • Rowe, T.M.1    Rizzi, M.2    Hirose, K.3    Peters, G.A.4    Sen, G.C.5
  • 126
    • 79952358406 scopus 로고    scopus 로고
    • A role for human Dicer in pre-RISC loading of siRNAs
    • Sakurai K, et al. 2011. A role for human Dicer in pre-RISC loading of siRNAs. Nucleic Acids Res. 39:1510-1525.
    • (2011) Nucleic Acids Res. , vol.39 , pp. 1510-1525
    • Sakurai, K.1
  • 127
    • 81255164734 scopus 로고    scopus 로고
    • The cellular TAR RNA binding protein, TRBP, promotes HIV-1 replication primarily by inhibiting the activation of double-stranded RNA-dependent kinase PKR
    • Sanghvi VR, Steel LF. 2011. The cellular TAR RNA binding protein, TRBP, promotes HIV-1 replication primarily by inhibiting the activation of double-stranded RNA-dependent kinase PKR. J. Virol. 85:12614-12621.
    • (2011) J. Virol. , vol.85 , pp. 12614-12621
    • Sanghvi, V.R.1    Steel, L.F.2
  • 128
    • 79952240422 scopus 로고    scopus 로고
    • A re-examination of global suppression of RNA interference by HIV-1
    • doi:10.1371/journal.pone.0017246
    • Sanghvi VR, Steel LF. 2011. A re-examination of global suppression of RNA interference by HIV-1. PLoS One 6 : e17246. doi:10.1371/journal.pone.0017246.
    • (2011) PLoS One , vol.6
    • Sanghvi, V.R.1    Steel, L.F.2
  • 129
    • 0037711199 scopus 로고    scopus 로고
    • The dsRNA binding protein family: Critical roles, diverse cellular functions
    • Saunders LR, Barber GN. 2003. The dsRNA binding protein family: critical roles, diverse cellular functions. FASEB J. 17:961-983.
    • (2003) FASEB J. , vol.17 , pp. 961-983
    • Saunders, L.R.1    Barber, G.N.2
  • 130
    • 36549076495 scopus 로고    scopus 로고
    • The merlin interacting proteins reveal multiple targets for NF2 therapy
    • Scoles DR. 2008. The merlin interacting proteins reveal multiple targets for NF2 therapy. Biochim. Biophys. Acta 1785:32-54.
    • (2008) Biochim. Biophys. Acta , vol.1785 , pp. 32-54
    • Scoles, D.R.1
  • 131
    • 49449096792 scopus 로고    scopus 로고
    • A small molecule enhances RNA interference and promotes microRNA processing
    • Shan G, et al. 2008. A small molecule enhances RNA interference and promotes microRNA processing. Nat. Biotechnol. 26:933-940.
    • (2008) Nat. Biotechnol. , vol.26 , pp. 933-940
    • Shan, G.1
  • 132
    • 0035101944 scopus 로고    scopus 로고
    • Expression of the TAR RNA binding protein in human testis
    • Siffroi JP, et al. 2001. Expression of the TAR RNA binding protein in human testis. Mol. Hum. Reprod. 7:219-225.
    • (2001) Mol. Hum. Reprod. , vol.7 , pp. 219-225
    • Siffroi, J.P.1
  • 133
    • 79958158639 scopus 로고    scopus 로고
    • Stress-induced phosphorylation of PACT reduces its interaction with TRBP and leads to PKR activation
    • Singh M, Castillo D, Patel CV, Patel RC. 2011. Stress-induced phosphorylation of PACT reduces its interaction with TRBP and leads to PKR activation. Biochemistry 50:4550-4560.
    • (2011) Biochemistry , vol.50 , pp. 4550-4560
    • Singh, M.1    Castillo, D.2    Patel, C.V.3    Patel, R.C.4
  • 134
    • 56649091439 scopus 로고    scopus 로고
    • A role for the Dicer helicase domain in the processing of thermodynamically unstable hairpin RNAs
    • Soifer HS, et al. 2008. A role for the Dicer helicase domain in the processing of thermodynamically unstable hairpin RNAs. Nucleic Acids Res. 36:6511-6522.
    • (2008) Nucleic Acids Res. , vol.36 , pp. 6511-6522
    • Soifer, H.S.1
  • 136
    • 79955411900 scopus 로고    scopus 로고
    • Small RNAs in early mammalian development: From gametes to gastrulation
    • Suh N, Blelloch R. 2011. Small RNAs in early mammalian development: from gametes to gastrulation. Development 138:1653-1661.
    • (2011) Development , vol.138 , pp. 1653-1661
    • Suh, N.1    Blelloch, R.2
  • 137
    • 79954616114 scopus 로고    scopus 로고
    • Reconstitution of human RNA interference in budding yeast
    • doi:10.1093/nar/gkq1321
    • Suk K, et al. 2011. Reconstitution of human RNA interference in budding yeast. Nucleic Acids Res. 39:e43. doi:10.1093/nar/gkq1321.
    • (2011) Nucleic Acids Res. , vol.39
    • Suk, K.1
  • 138
    • 0037188904 scopus 로고    scopus 로고
    • The dsRNA binding protein RDE-4 interacts with RDE-1, DCR-1, and a DExH-box helicase to direct RNAi in C. elegans
    • Tabara H, Yigit E, Siomi H, Mello CC. 2002. The dsRNA binding protein RDE-4 interacts with RDE-1, DCR-1, and a DExH-box helicase to direct RNAi in C. elegans. Cell 109:861-871.
    • (2002) Cell , vol.109 , pp. 861-871
    • Tabara, H.1    Yigit, E.2    Siomi, H.3    Mello, C.C.4
  • 139
    • 78650235515 scopus 로고    scopus 로고
    • Tracking a century of global expansion and evolution of HIV to drive understanding and to combat disease
    • Tebit DM, Arts EJ. 2011. Tracking a century of global expansion and evolution of HIV to drive understanding and to combat disease. Lancet Infect. Dis. 11:45-56.
    • (2011) Lancet Infect. Dis. , vol.11 , pp. 45-56
    • Tebit, D.M.1    Arts, E.J.2
  • 140
    • 0027405720 scopus 로고
    • A novel moesin-, ezrin-, radixin-like gene is a candidate for the neurofibromatosis 2 tumor suppressor
    • Trofatter JA, et al. 1993. A novel moesin-, ezrin-, radixin-like gene is a candidate for the neurofibromatosis 2 tumor suppressor. Cell 72:791-800.
    • (1993) Cell , vol.72 , pp. 791-800
    • Trofatter, J.A.1
  • 141
    • 28044457638 scopus 로고    scopus 로고
    • Gene therapy with E2F-1 up-regulates the protein kinase PKR and inhibits growth of leiomyosarcoma in vivo
    • Vorburger SA, et al. 2005. Gene therapy with E2F-1 up-regulates the protein kinase PKR and inhibits growth of leiomyosarcoma in vivo. Mol. Cancer Ther. 4:1710-1716.
    • (2005) Mol. Cancer Ther. , vol.4 , pp. 1710-1716
    • Vorburger, S.A.1
  • 142
    • 70350783745 scopus 로고    scopus 로고
    • Structural insights into RNA processing by the human RISC-loading complex
    • Wang HW, et al. 2009. Structural insights into RNA processing by the human RISC-loading complex. Nat. Struct. Mol. Biol. 16:1148-1153.
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 1148-1153
    • Wang, H.W.1
  • 143
    • 84862972550 scopus 로고    scopus 로고
    • TRBP and eIF6 homologue in Marsupenaeus japonicus play crucial roles in antiviral response
    • doi:10.1371/journal.pone.0030057
    • Wang S, Chen AJ, Shi LJ, Zhao XF, Wang JX. 2012. TRBP and eIF6 homologue in Marsupenaeus japonicus play crucial roles in antiviral response. PLoS One 7:e30057. doi:10.1371/journal.pone.0030057.
    • (2012) PLoS One , vol.7
    • Wang, S.1    Chen, A.J.2    Shi, L.J.3    Zhao, X.F.4    Wang, J.X.5
  • 144
    • 66949167063 scopus 로고    scopus 로고
    • TRBP homolog interacts with eukaryotic initiation factor 6 (eIF6) in Fenneropenaeus chinensis
    • Wang S, Liu N, Chen AJ, Zhao XF, Wang JX. 2009. TRBP homolog interacts with eukaryotic initiation factor 6 (eIF6) in Fenneropenaeus chinensis. J. Immunol. 182:5250-5258.
    • (2009) J. Immunol. , vol.182 , pp. 5250-5258
    • Wang, S.1    Liu, N.2    Chen, A.J.3    Zhao, X.F.4    Wang, J.X.5
  • 145
    • 0345628581 scopus 로고    scopus 로고
    • Mammalian staufen is a double-stranded-RNA- And tubulin-binding protein which localizes to the rough endoplasmic reticulum
    • Wickham L, Duchaine T, Luo M, Nabi IR, DesGroseillers L. 1999. Mammalian staufen is a double-stranded-RNA- and tubulin-binding protein which localizes to the rough endoplasmic reticulum. Mol. Cell Biol. 19:2220-2230.
    • (1999) Mol. Cell Biol. , vol.19 , pp. 2220-2230
    • Wickham, L.1    Duchaine, T.2    Luo, M.3    Nabi, I.R.4    DesGroseillers, L.5
  • 146
    • 78650763143 scopus 로고    scopus 로고
    • Structures of the first and second double-stranded RNA-binding domains of human TAR RNA-binding protein
    • Yamashita S, et al. 2011. Structures of the first and second double-stranded RNA-binding domains of human TAR RNA-binding protein. Protein Sci. 20:118-130.
    • (2011) Protein Sci. , vol.20 , pp. 118-130
    • Yamashita, S.1
  • 147
    • 0031807391 scopus 로고    scopus 로고
    • The gene encoding PRBP, the mouse homolog of human TRBP, maps to distal chromosome 15
    • Zhong J, Edelhoff S, Disteche C, Braun RE. 1998. The gene encoding PRBP, the mouse homolog of human TRBP, maps to distal chromosome 15. Mamm. Genome 9:413-414.
    • (1998) Mamm. Genome , vol.9 , pp. 413-414
    • Zhong, J.1    Edelhoff, S.2    Disteche, C.3    Braun, R.E.4
  • 148
    • 0033052048 scopus 로고    scopus 로고
    • A double-stranded RNA binding protein required for activation of repressed messages in mammalian germ cells
    • Zhong J, Peters AH, Lee K, Braun RE. 1999. A double-stranded RNA binding protein required for activation of repressed messages in mammalian germ cells. Nat. Genet. 22:171-174.
    • (1999) Nat. Genet. , vol.22 , pp. 171-174
    • Zhong, J.1    Peters, A.H.2    Lee, K.3    Braun, R.E.4


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