메뉴 건너뛰기




Volumn 86, Issue 24, 2012, Pages 13272-13280

In vitro and in vivo analysis of the interaction between RNA helicase a and HIV-1 RNA

Author keywords

[No Author keywords available]

Indexed keywords

RNA HELICASE; RNA HELICASE A; UNCLASSIFIED DRUG; VIRUS RNA;

EID: 84870677136     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.01993-12     Document Type: Article
Times cited : (24)

References (58)
  • 1
    • 0031830844 scopus 로고    scopus 로고
    • BRCA1 protein is linked to the RNA polymerase II holoenzyme complex via RNA helicase A
    • Anderson SF, Schlegel BP, Nakajima T, Wolpin ES, Parvin JD. 1998.BRCA1 protein is linked to the RNA polymerase II holoenzyme complex via RNA helicase A. Nat. Genet. 19:254-256.
    • (1998) Nat. Genet. , vol.19 , pp. 254-256
    • Anderson, S.F.1    Schlegel, B.P.2    Nakajima, T.3    Wolpin, E.S.4    Parvin, J.D.5
  • 2
    • 0034948461 scopus 로고    scopus 로고
    • Dual roles of RNA helicase A in CREB-dependent transcription
    • Aratani S, et al. 2001. Dual roles of RNA helicase A in CREB-dependent transcription. Mol. Cell. Biol. 21:4460-4469.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 4460-4469
    • Aratani, S.1
  • 3
    • 0029784592 scopus 로고    scopus 로고
    • Alpha helix-RNA major groove recognition in an HIV-1 rev peptide-RRE RNA complex
    • Battiste JL, et al. 1996. Alpha helix-RNA major groove recognition in an HIV-1 rev peptide-RRE RNA complex. Science 273:1547-1551.
    • (1996) Science , vol.273 , pp. 1547-1551
    • Battiste, J.L.1
  • 4
    • 0027479628 scopus 로고
    • Functional sites in the 5'region of human immunodeficiency virus type 1 RNA form defined structural domains
    • Baudin F, et al. 1993. Functional sites in the 5'region of human immunodeficiency virus type 1 RNA form defined structural domains. J. Mol.Biol. 229:382-397.
    • (1993) J. Mol.Biol. , vol.229 , pp. 382-397
    • Baudin, F.1
  • 5
    • 84555189622 scopus 로고    scopus 로고
    • Analysis of co-transcriptional RNA processing by RNA-ChIP assay
    • Bittencourt D, Auboeuf D. 2012. Analysis of co-transcriptional RNA processing by RNA-ChIP assay. Methods Mol. Biol. 809:563-577.
    • (2012) Methods Mol. Biol. , vol.809 , pp. 563-577
    • Bittencourt, D.1    Auboeuf, D.2
  • 6
    • 1542581581 scopus 로고    scopus 로고
    • Noncatalytic assembly of ribonuclease III with double-stranded RNA
    • Blaszczyk J, et al. 2004. Noncatalytic assembly of ribonuclease III with double-stranded RNA. Structure 12:457- 466.
    • (2004) Structure , vol.12 , pp. 457-466
    • Blaszczyk, J.1
  • 7
    • 34547211817 scopus 로고    scopus 로고
    • The long unwinding road of RNA helicases
    • Bleichert F, Baserga SJ. 2007. The long unwinding road of RNA helicases.Mol. Cell 27:339 -352.
    • (2007) Mol. Cell , vol.27 , pp. 339-352
    • Bleichert, F.1    Baserga, S.J.2
  • 8
    • 77950493743 scopus 로고    scopus 로고
    • RNA helicase A modulates translation of HIV-1 and infectivity of progeny virions
    • Bolinger C, Sharma A, Singh D, Yu L, Boris-Lawrie K. 2010. RNA helicase A modulates translation of HIV-1 and infectivity of progeny virions.Nucleic Acids Res. 38:1686 -1696.
    • (2010) Nucleic Acids Res. , vol.38 , pp. 1686-1696
    • Bolinger, C.1    Sharma, A.2    Singh, D.3    Yu, L.4    Boris-lawrie, K.5
  • 9
    • 34250353492 scopus 로고    scopus 로고
    • RNA helicase A interacts with divergent lymphotropic retroviruses and promotes translation of human T-cell leukemia virus type 1
    • Bolinger C, et al. 2007. RNA helicase A interacts with divergent lymphotropic retroviruses and promotes translation of human T-cell leukemia virus type 1. Nucleic Acids Res. 35:2629 -2642.
    • (2007) Nucleic Acids Res. , vol.35 , pp. 2629-2642
    • Bolinger, C.1
  • 10
    • 0028129989 scopus 로고
    • Conserved structures and diversity of functions of RNA-binding proteins
    • Burd CG, Dreyfuss G. 1994. Conserved structures and diversity of functions of RNA-binding proteins. Science 265:615-621.
    • (1994) Science , vol.265 , pp. 615-621
    • Burd, C.G.1    Dreyfuss, G.2
  • 11
    • 0034674157 scopus 로고    scopus 로고
    • Differential role of the intermolecular base-pairs G292-C(75) and G293-C(74) in the reaction catalyzed by Escherichia coli RNase P RNA
    • Busch S, Kirsebom LA, Notbohm H, Hartmann RK. 2000. Differential role of the intermolecular base-pairs G292-C(75) and G293-C(74) in the reaction catalyzed by Escherichia coli RNase P RNA. J. Mol. Biol. 299:941-951.
    • (2000) J. Mol. Biol. , vol.299 , pp. 941-951
    • Busch, S.1    Kirsebom, L.A.2    Notbohm, H.3    Hartmann, R.K.4
  • 12
    • 0027237045 scopus 로고
    • Epstein-Barr virus-derived vectors for transient and stable expression of recombinant proteins
    • Cachianes G, et al. 1993. Epstein-Barr virus-derived vectors for transient and stable expression of recombinant proteins. Biotechniques 15:255-259.
    • (1993) Biotechniques , vol.15 , pp. 255-259
    • Cachianes, G.1
  • 13
    • 0036888914 scopus 로고    scopus 로고
    • RNA structure and packaging signals in the 5'leader region of the human immunodeficiency virus type 1 genome
    • Clever JL, Miranda D, Jr, Parslow TG. 2002. RNA structure and packaging signals in the 5'leader region of the human immunodeficiency virus type 1 genome. J. Virol. 76:12381-12387.
    • (2002) J. Virol. , vol.76 , pp. 12381-12387
    • Clever, J.L.1    Miranda Jr., D.2    Parslow, T.G.3
  • 14
    • 33344473656 scopus 로고    scopus 로고
    • The DEAD-box protein family of RNA helicases
    • Cordin O, Banroques J, Tanner NK, Linder P. 2006. The DEAD-box protein family of RNA helicases. Gene 367:17-37.
    • (2006) Gene , vol.367 , pp. 17-37
    • Cordin, O.1    Banroques, J.2    Tanner, N.K.3    Linder, P.4
  • 16
    • 0034192148 scopus 로고    scopus 로고
    • Proteins binding to duplexed RNA:one motif, multiple functions
    • Fierro-Monti I, Mathews MB. 2000. Proteins binding to duplexed RNA:one motif, multiple functions. Trends Biochem. Sci. 25:241-246.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 241-246
    • Fierro-monti, I.1    Mathews, M.B.2
  • 17
    • 0035937176 scopus 로고    scopus 로고
    • A role of RNA helicase A in cis-acting transactivation response element-mediated transcriptional regulation of human immunodeficiency virus type 1
    • Fujii R, et al. 2001. A role of RNA helicase A in cis-acting transactivation response element-mediated transcriptional regulation of human immunodeficiency virus type 1. J. Biol. Chem. 276:5445-5451.
    • (2001) J. Biol. Chem. , vol.276 , pp. 5445-5451
    • Fujii, R.1
  • 18
    • 33749134437 scopus 로고    scopus 로고
    • DExD/H box RNA helicases: multifunctional proteins with important roles in transcriptional regulation
    • Fuller-Pace FV. 2006. DExD/H box RNA helicases: multifunctional proteins with important roles in transcriptional regulation. Nucleic Acids Res.34:4206-4215.
    • (2006) Nucleic Acids Res. , vol.34 , pp. 4206-4215
    • Fuller-pace, F.V.1
  • 19
    • 0035975942 scopus 로고    scopus 로고
    • The DExH/D box protein HEL/UAP56 is essential for mRNA nuclear export in Drosophila
    • Gatfield D, et al. 2001. The DExH/D box protein HEL/UAP56 is essential for mRNA nuclear export in Drosophila. Curr. Biol. 11:1716 -1721.
    • (2001) Curr. Biol. , vol.11 , pp. 1716-1721
    • Gatfield, D.1
  • 20
    • 67749147464 scopus 로고    scopus 로고
    • Roles of Gag and NCp7 in facilitating tRNA(Lys)(3) annealing to viral RNA in human immunodeficiency virus type 1
    • Guo F, Saadatmand J, Niu M, Kleiman L. 2009. Roles of Gag and NCp7 in facilitating tRNA(Lys)(3) annealing to viral RNA in human immunodeficiency virus type 1. J. Virol. 83:8099-8107.
    • (2009) J. Virol. , vol.83 , pp. 8099-8107
    • Guo, F.1    Saadatmand, J.2    Niu, M.3    Kleiman, L.4
  • 21
    • 0031777343 scopus 로고    scopus 로고
    • Functional analysis of the core human immunodeficiency virus type 1 packaging signal in a permissive cell line
    • Harrison GP, Miele G, Hunter E, Lever AM. 1998. Functional analysis of the core human immunodeficiency virus type 1 packaging signal in a permissive cell line. J. Virol. 72:5886-5896.
    • (1998) J. Virol. , vol.72 , pp. 5886-5896
    • Harrison, G.P.1    Miele, G.2    Hunter, E.3    Lever, A.M.4
  • 22
    • 33744931657 scopus 로고    scopus 로고
    • RNA helicase A is necessary for translation of selected messenger RNAs
    • Hartman TR, et al. 2006. RNA helicase A is necessary for translation of selected messenger RNAs. Nat. Struct. Mol. Biol. 13:509-516.
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 509-516
    • Hartman, T.R.1
  • 23
    • 56249145093 scopus 로고    scopus 로고
    • Comparisons of RNAi approaches for validation of human RNA helicase A as an essential factor in hepatitis C virus replication
    • He QS, et al. 2008. Comparisons of RNAi approaches for validation of human RNA helicase A as an essential factor in hepatitis C virus replication.J. Virol. Methods 154:216-219.
    • (2008) J. Virol. Methods , vol.154 , pp. 216-219
    • He, Q.S.1
  • 24
    • 34748885125 scopus 로고    scopus 로고
    • Nuclear factors are involved in hepatitis C virus RNA replication
    • Isken O, et al. 2007. Nuclear factors are involved in hepatitis C virus RNA replication. RNA 13:1675-1692.
    • (2007) RNA , vol.13 , pp. 1675-1692
    • Isken, O.1
  • 25
    • 0027104999 scopus 로고
    • Recognition of the high affinity binding site in rev-response element RNA by the human immunodeficiency virus type-1 rev protein
    • Iwai S, Pritchard C, Mann DA, Karn J, Gait MJ. 1992. Recognition of the high affinity binding site in rev-response element RNA by the human immunodeficiency virus type-1 rev protein. Nucleic Acids Res. 20:6465-6472.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 6465-6472
    • Iwai, S.1    Pritchard, C.2    Mann, D.A.3    Karn, J.4    Gait, M.J.5
  • 26
    • 79956049857 scopus 로고    scopus 로고
    • Evidence that Lin28 stimulates translation by recruiting RNA helicase A to polysomes
    • Jin J, et al. 2011. Evidence that Lin28 stimulates translation by recruiting RNA helicase A to polysomes. Nucleic Acids Res. 39:3724-3734.
    • (2011) Nucleic Acids Res. , vol.39 , pp. 3724-3734
    • Jin, J.1
  • 27
    • 31144459945 scopus 로고    scopus 로고
    • Structural polymorphism of the HIV-1 leader region explored by computational methods
    • Kasprzak W, Bindewald E, Shapiro BA. 2005. Structural polymorphism of the HIV-1 leader region explored by computational methods. Nucleic Acids Res. 33:7151-7163.
    • (2005) Nucleic Acids Res. , vol.33 , pp. 7151-7163
    • Kasprzak, W.1    Bindewald, E.2    Shapiro, B.A.3
  • 28
    • 0026034946 scopus 로고
    • Structural analysis of the interaction between the human immunodeficiency virus Rev protein and the Rev response element
    • Kjems J, Brown M, Chang DD, Sharp PA. 1991. Structural analysis of the interaction between the human immunodeficiency virus Rev protein and the Rev response element. Proc. Natl. Acad. Sci. U. S. A. 88:683-687.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 683-687
    • Kjems, J.1    Brown, M.2    Chang, D.D.3    Sharp, P.A.4
  • 29
    • 33745851831 scopus 로고    scopus 로고
    • In vitro characterization of the interaction between HIV-1 Gag and human lysyl-tRNA synthetase
    • Kovaleski BJ, et al. 2006. In vitro characterization of the interaction between HIV-1 Gag and human lysyl-tRNA synthetase. J. Biol. Chem.281:19449 -19456.
    • (2006) J. Biol. Chem. , vol.281 , pp. 19449-19456
    • Kovaleski, B.J.1
  • 30
    • 70350328597 scopus 로고    scopus 로고
    • Identification of RNA helicase A as a new host factor in the replication cycle of foot-and-mouth disease virus
    • Lawrence P, Rieder E. 2009. Identification of RNA helicase A as a new host factor in the replication cycle of foot-and-mouth disease virus. J.Virol. 83:11356-11366.
    • (2009) J.Virol. , vol.83 , pp. 11356-11366
    • Lawrence, P.1    Rieder, E.2
  • 31
    • 0026726096 scopus 로고
    • A new RNA helicase isolated from HeLa cells that catalytically translocates in the 3'to 5'direction
    • Lee CG, Hurwitz J. 1992. A new RNA helicase isolated from HeLa cells that catalytically translocates in the 3'to 5'direction. J. Biol. Chem. 267:4398-4407.
    • (1992) J. Biol. Chem. , vol.267 , pp. 4398-4407
    • Lee, C.G.1    Hurwitz, J.2
  • 32
    • 0033582333 scopus 로고    scopus 로고
    • A role for RNA helicase A in post-transcriptional regulation of HIV type 1
    • Li J, et al. 1999. A role for RNA helicase A in post-transcriptional regulation of HIV type 1. Proc. Natl. Acad. Sci. U. S. A. 96:709 -714.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 709-714
    • Li, J.1
  • 33
    • 84863116521 scopus 로고    scopus 로고
    • Identification of RNA helicase A as a cellular factor that interacts with influenza A virus NS1 protein and its role in the virus life cycle
    • Lin L, et al. 2012. Identification of RNA helicase A as a cellular factor that interacts with influenza A virus NS1 protein and its role in the virus life cycle. J. Virol. 86:1942-1954.
    • (2012) J. Virol. , vol.86 , pp. 1942-1954
    • Lin, L.1
  • 34
    • 84855985830 scopus 로고    scopus 로고
    • A novel role of RNA helicase A in regulation of translation of type I collagen mRNAs
    • Manojlovic Z, Stefanovic B. 2012. A novel role of RNA helicase A in regulation of translation of type I collagen mRNAs. RNA 18:321-334.
    • (2012) RNA , vol.18 , pp. 321-334
    • Manojlovic, Z.1    Stefanovic, B.2
  • 35
    • 78651285748 scopus 로고    scopus 로고
    • CDD: a conserved domain database for the functional annotation of proteins
    • doi:10.1093/nar/gkq1189
    • Marchler-Bauer A, et al. 2011. CDD: a conserved domain database for the functional annotation of proteins. Nucleic Acids Res. 39:D225-D229. doi:10.1093/nar/gkq1189.
    • (2011) Nucleic Acids Res. , vol.39
    • Marchler-bauer, A.1
  • 36
    • 84859867090 scopus 로고    scopus 로고
    • Host cell interactome of HIV-1 Rev includes RNA helicases involved in multiple facets of virus production
    • doi:10.1074/mcp.M111.015313, M111.015313
    • Naji S, et al. 2012. Host cell interactome of HIV-1 Rev includes RNA helicases involved in multiple facets of virus production. Mol. Cell. Proteomics 11:M111.015313. doi:10.1074/mcp.M111.015313.
    • (2012) Mol. Cell. Proteomics , vol.11
    • Naji, S.1
  • 37
    • 0030967951 scopus 로고    scopus 로고
    • RNA helicase A mediates association of CBP with RNA polymerase II
    • Nakajima T, et al. 1997. RNA helicase A mediates association of CBP with RNA polymerase II. Cell 90:1107-1112.
    • (1997) Cell , vol.90 , pp. 1107-1112
    • Nakajima, T.1
  • 38
    • 1342285100 scopus 로고    scopus 로고
    • Probing alternative foldings of the HIV-1 leader RNA by antisense oligonucleotide scanning arrays
    • Ooms M, Verhoef K, Southern E, Huthoff H, Berkhout B. 2004.Probing alternative foldings of the HIV-1 leader RNA by antisense oligonucleotide scanning arrays. Nucleic Acids Res. 32:819-827.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 819-827
    • Ooms, M.1    Verhoef, K.2    Southern, E.3    Huthoff, H.4    Berkhout, B.5
  • 39
    • 9144247039 scopus 로고    scopus 로고
    • First snapshots of the HIV-1 RNA structure in infected cells and in virions
    • Paillart JC, et al. 2004. First snapshots of the HIV-1 RNA structure in infected cells and in virions. J. Biol. Chem. 279:48397-48403.
    • (2004) J. Biol. Chem. , vol.279 , pp. 48397-48403
    • Paillart, J.C.1
  • 40
    • 0037155223 scopus 로고    scopus 로고
    • In vitro evidence for a long range pseudoknot in the 5'-untranslated and matrix coding regions of HIV-1 genomic RNA
    • Paillart JC, Skripkin E, Ehresmann B, Ehresmann C, Marquet R. 2002.In vitro evidence for a long range pseudoknot in the 5'-untranslated and matrix coding regions of HIV-1 genomic RNA. J. Biol. Chem. 277:5995-6004.
    • (2002) J. Biol. Chem. , vol.277 , pp. 5995-6004
    • Paillart, J.C.1    Skripkin, E.2    Ehresmann, B.3    Ehresmann, C.4    Marquet, R.5
  • 41
    • 68149157992 scopus 로고    scopus 로고
    • Structure of the HIV-1 Rev response element alone and in complex with regulator of virion(Rev) studied by atomic force microscopy
    • Pallesen J, Dong M, Besenbacher F, Kjems J. 2009. Structure of the HIV-1 Rev response element alone and in complex with regulator of virion(Rev) studied by atomic force microscopy. FEBS J. 276:4223-4232.
    • (2009) FEBS J. , vol.276 , pp. 4223-4232
    • Pallesen, J.1    Dong, M.2    Besenbacher, F.3    Kjems, J.4
  • 42
    • 0042869614 scopus 로고    scopus 로고
    • Heterogeneity of HIV-1 Rev response element
    • Retroviruses
    • Phuphuakrat A, Auewarakul P. 2003. Heterogeneity of HIV-1 Rev response element. AIDS Res. Hum. Retroviruses 19:569-574.
    • (2003) AIDS Res. Hum. , vol.19 , pp. 569-574
    • Phuphuakrat, A.1    Auewarakul, P.2
  • 44
    • 0342723737 scopus 로고    scopus 로고
    • RNA recognition by a Staufen double-stranded RNA-binding domain
    • Ramos A, et al. 2000. RNA recognition by a Staufen double-stranded RNA-binding domain. EMBO J. 19:997-1009.
    • (2000) EMBO J. , vol.19 , pp. 997-1009
    • Ramos, A.1
  • 45
    • 79953035983 scopus 로고    scopus 로고
    • Features of double-stranded RNA-binding domains of RNA helicase A are necessary for selective recognition and translation of complex mRNAs
    • Ranji A, Shkriabai N, Kvaratskhelia M, Musier-Forsyth K, Boris-Lawrie K. 2011. Features of double-stranded RNA-binding domains of RNA helicase A are necessary for selective recognition and translation of complex mRNAs. J. Biol. Chem. 286:5328 -5337.
    • (2011) J. Biol. Chem. , vol.286 , pp. 5328-5337
    • Ranji, A.1    Shkriabai, N.2    Kvaratskhelia, M.3    Musier-forsyth, K.4    Boris-lawrie, K.5
  • 46
    • 0036674269 scopus 로고    scopus 로고
    • Large-scale proteomic analysis of the human spliceosome
    • Rappsilber J, Ryder U, Lamond AI, Mann M. 2002. Large-scale proteomic analysis of the human spliceosome. Genome Res. 12:1231-1245.
    • (2002) Genome Res. , vol.12 , pp. 1231-1245
    • Rappsilber, J.1    Ryder, U.2    Lamond, A.I.3    Mann, M.4
  • 47
    • 34248576287 scopus 로고    scopus 로고
    • RNA helicase A interacts with RISC in human cells and functions in RISC loading
    • Robb GB, Rana TM. 2007. RNA helicase A interacts with RISC in human cells and functions in RISC loading. Mol. Cell 26:523-537.
    • (2007) Mol. Cell , vol.26 , pp. 523-537
    • Robb, G.B.1    Rana, T.M.2
  • 48
    • 33744965939 scopus 로고    scopus 로고
    • Association of RNA helicase A with human immunodeficiency virus type 1 particles
    • Roy BB, et al. 2006. Association of RNA helicase A with human immunodeficiency virus type 1 particles. J. Biol. Chem. 281:12625-12635.
    • (2006) J. Biol. Chem. , vol.281 , pp. 12625-12635
    • Roy, B.B.1
  • 49
    • 0032535613 scopus 로고    scopus 로고
    • Molecular basis of double-stranded RNAprotein interactions: structure of a dsRNA-binding domain complexed with dsRNA
    • Ryter JM, Schultz SC. 1998. Molecular basis of double-stranded RNAprotein interactions: structure of a dsRNA-binding domain complexed with dsRNA. EMBO J. 17:7505-7513.
    • (1998) EMBO J. , vol.17 , pp. 7505-7513
    • Ryter, J.M.1    Schultz, S.C.2
  • 50
    • 33745289012 scopus 로고    scopus 로고
    • Oncoprotein EWS-FLI1 activity is enhanced by RNA helicase A
    • Toretsky JA, et al. 2006. Oncoprotein EWS-FLI1 activity is enhanced by RNA helicase A. Cancer Res. 66:5574-5581.
    • (2006) Cancer Res. , vol.66 , pp. 5574-5581
    • Toretsky, J.A.1
  • 51
    • 77954958169 scopus 로고    scopus 로고
    • Prp43p contains a processive helicase structural architecture with a specific regulatory domain
    • Walbott H, et al. 2010. Prp43p contains a processive helicase structural architecture with a specific regulatory domain. EMBO J. 29:2194-2204.
    • (2010) EMBO J. , vol.29 , pp. 2194-2204
    • Walbott, H.1
  • 52
    • 79960173334 scopus 로고    scopus 로고
    • Structure of a yeast RNase III dsRBD complex with a noncanonical RNA substrate provides new insights into binding specificity of dsRBDs
    • Wang Z, Hartman E, Roy K, Chanfreau G, Feigon J. 2011. Structure of a yeast RNase III dsRBD complex with a noncanonical RNA substrate provides new insights into binding specificity of dsRBDs. Structure 19:999-1010.
    • (2011) Structure , vol.19 , pp. 999-1010
    • Wang, Z.1    Hartman, E.2    Roy, K.3    Chanfreau, G.4    Feigon, J.5
  • 53
    • 68449092202 scopus 로고    scopus 로고
    • Architecture and secondary structure of an entire HIV-1 RNA genome
    • Watts JM, et al. 2009. Architecture and secondary structure of an entire HIV-1 RNA genome. Nature 460:711-716.
    • (2009) Nature , vol.460 , pp. 711-716
    • Watts, J.M.1
  • 54
    • 40849123031 scopus 로고    scopus 로고
    • High-throughput SHAPE analysis reveals structures in HIV-1 genomic RNA strongly conserved across distinct biological states
    • doi:10.1371/journal.pbio.0060096
    • Wilkinson KA, et al. 2008. High-throughput SHAPE analysis reveals structures in HIV-1 genomic RNA strongly conserved across distinct biological states. PLoS Biol. 6:e96. doi:10.1371/journal.pbio.0060096.
    • (2008) PLoS Biol. , vol.6
    • Wilkinson, K.A.1
  • 55
    • 3042704491 scopus 로고    scopus 로고
    • Structural basis for recognition of the AGNN tetraloop RNA fold by the double-stranded RNA-binding domain of Rnt1p RNase III
    • Wu H, Henras A, Chanfreau G, Feigon J. 2004. Structural basis for recognition of the AGNN tetraloop RNA fold by the double-stranded RNA-binding domain of Rnt1p RNase III. Proc. Natl. Acad. Sci. U. S. A.101:8307- 8312.
    • (2004) Proc. Natl. Acad. Sci. U.S.A , vol.101 , pp. 8307-8312
    • Wu, H.1    Henras, A.2    Chanfreau, G.3    Feigon, J.4
  • 56
    • 78951484220 scopus 로고    scopus 로고
    • Coordinate roles of Gag and RNA helicase A in promoting the annealing of formula to HIV-1 RNA
    • Xing L, Liang C, Kleiman L. 2011. Coordinate roles of Gag and RNA helicase A in promoting the annealing of formula to HIV-1 RNA. J. Virol.85:1847-1860.
    • (2011) J. Virol. , vol.85 , pp. 1847-1860
    • Xing, L.1    Liang, C.2    Kleiman, L.3
  • 57
    • 0030945449 scopus 로고    scopus 로고
    • Domain structure of human nuclear DNA helicase II (RNA helicase A)
    • Zhang S, Grosse F. 1997. Domain structure of human nuclear DNA helicase II (RNA helicase A). J. Biol. Chem. 272:11487-11494.
    • (1997) J. Biol. Chem. , vol.272 , pp. 11487-11494
    • Zhang, S.1    Grosse, F.2
  • 58
    • 80555133355 scopus 로고    scopus 로고
    • DHX9 pairs with IPS-1 to sense double-stranded RNA in myeloid dendritic cells
    • Zhang Z, Yuan B, Lu N, Facchinetti V, Liu YJ. 2011. DHX9 pairs with IPS-1 to sense double-stranded RNA in myeloid dendritic cells. J. Immunol.187:4501- 4508.
    • (2011) J. Immunol. , vol.187 , pp. 4501-4508
    • Zhang, Z.1    Yuan, B.2    Lu, N.3    Facchinetti, V.4    Liu, Y.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.