메뉴 건너뛰기




Volumn 3, Issue 6, 2008, Pages

Analysis of the EIAV Rev-Responsive Element (RRE) reveals a conserved RNA motif required for high affinity REV binding in both HIV-1 and EIAV

Author keywords

[No Author keywords available]

Indexed keywords

REV PROTEIN; VIRUS RNA;

EID: 48449096205     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0002272     Document Type: Article
Times cited : (16)

References (74)
  • 1
    • 0025335833 scopus 로고
    • Cloning and functional analysis of multiply spliced mRNA species of human immunodeficiency virus type 1
    • Schwartz S, Felber BK, Benko DM, Fenyo EM, Pavlakis GN (1990) Cloning and functional analysis of multiply spliced mRNA species of human immunodeficiency virus type 1. J Virol 64: 2519-2529.
    • (1990) J Virol , vol.64 , pp. 2519-2529
    • Schwartz, S.1    Felber, B.K.2    Benko, D.M.3    Fenyo, E.M.4    Pavlakis, G.N.5
  • 2
    • 0025282286 scopus 로고
    • Cloning and characterization of cDNAs encoding equine infectious anemia virus tat and putative Rev proteins
    • Stephens RM, Derse D, Rice NR (1990) Cloning and characterization of cDNAs encoding equine infectious anemia virus tat and putative Rev proteins. J Virol 64: 3716-3725.
    • (1990) J Virol , vol.64 , pp. 3716-3725
    • Stephens, R.M.1    Derse, D.2    Rice, N.R.3
  • 3
    • 0034161419 scopus 로고    scopus 로고
    • Exonic splicing enhancers: Mechanism of action, diversity and role in human genetic diseases
    • Blencowe BJ (2000) Exonic splicing enhancers: mechanism of action, diversity and role in human genetic diseases. Trends Biochem Sci 25: 106-110.
    • (2000) Trends Biochem Sci , vol.25 , pp. 106-110
    • Blencowe, B.J.1
  • 4
    • 33745501015 scopus 로고    scopus 로고
    • General and specific functions of exonic splicing silencers in splicing control
    • Wang Z, Xiao X, Van Nostrand E, Burge CB (2006) General and specific functions of exonic splicing silencers in splicing control. Mol Cell 23: 61-70.
    • (2006) Mol Cell , vol.23 , pp. 61-70
    • Wang, Z.1    Xiao, X.2    Van Nostrand, E.3    Burge, C.B.4
  • 5
    • 0031023533 scopus 로고    scopus 로고
    • A structured retroviral RNA element that mediates nucleocytoplasmic export of intron-containing RNA
    • Ernst RK, Bray M, Rekosh D, Hammarskjold ML (1997) A structured retroviral RNA element that mediates nucleocytoplasmic export of intron-containing RNA. Mol Cell Biol 17: 135-144.
    • (1997) Mol Cell Biol , vol.17 , pp. 135-144
    • Ernst, R.K.1    Bray, M.2    Rekosh, D.3    Hammarskjold, M.L.4
  • 6
    • 0026794096 scopus 로고
    • Mechanism of action of regulatory proteins encoded by complex retroviruses
    • Cullen BR (1992) Mechanism of action of regulatory proteins encoded by complex retroviruses. Microbiol Rev 56: 375-394.
    • (1992) Microbiol Rev , vol.56 , pp. 375-394
    • Cullen, B.R.1
  • 8
    • 33644913421 scopus 로고    scopus 로고
    • Role of viral splicing elements and cellular RNA binding proteins in regulation of HIV-1 alternative RNA splicing
    • Stoltzfus CM, Madsen JM (2006) Role of viral splicing elements and cellular RNA binding proteins in regulation of HIV-1 alternative RNA splicing. Curr HIV Res 4: 43-55.
    • (2006) Curr HIV Res , vol.4 , pp. 43-55
    • Stoltzfus, C.M.1    Madsen, J.M.2
  • 9
    • 0033562095 scopus 로고    scopus 로고
    • The ins and outs of HIV Rev
    • Hope TJ (1999) The ins and outs of HIV Rev. Arch Biochem Biophys 365: 186-191.
    • (1999) Arch Biochem Biophys , vol.365 , pp. 186-191
    • Hope, T.J.1
  • 10
    • 0025810027 scopus 로고
    • Characterization of HIV-1 REV protein: Binding stoichiometry and minimal RNA substrate
    • Cook KS, Fisk GJ, Hauber J, Usman N, Daly TJ, et al. (1991) Characterization of HIV-1 REV protein: binding stoichiometry and minimal RNA substrate. Nucleic Acids Res 19: 1577-1583.
    • (1991) Nucleic Acids Res , vol.19 , pp. 1577-1583
    • Cook, K.S.1    Fisk, G.J.2    Hauber, J.3    Usman, N.4    Daly, T.J.5
  • 11
    • 0024310483 scopus 로고
    • Sequence-specific RNA binding by the HIV-1 Rev protein
    • Zapp ML, Green MR (1989) Sequence-specific RNA binding by the HIV-1 Rev protein. Nature 342: 714-716.
    • (1989) Nature , vol.342 , pp. 714-716
    • Zapp, M.L.1    Green, M.R.2
  • 12
    • 0025184516 scopus 로고
    • Interaction of the human immunodeficiency virus type 1 Rev protein with a structured region in env mRNA is dependent on multimer formation mediated through a basic stretch of amino acids
    • Olsen HS, Cochrane AW, Dillon PJ, Nalin CM, Rosen CA (1990) Interaction of the human immunodeficiency virus type 1 Rev protein with a structured region in env mRNA is dependent on multimer formation mediated through a basic stretch of amino acids. Genes Dev 4: 1357-1364.
    • (1990) Genes Dev , vol.4 , pp. 1357-1364
    • Olsen, H.S.1    Cochrane, A.W.2    Dillon, P.J.3    Nalin, C.M.4    Rosen, C.A.5
  • 13
    • 0025917131 scopus 로고
    • Oligomerization and RNA binding domains of the type 1 human immunodeficiency virus Rev protein: A dual function for an arginine-rich binding motif
    • Zapp ML, Hope TJ, Parslow TG, Green MR (1991) Oligomerization and RNA binding domains of the type 1 human immunodeficiency virus Rev protein: a dual function for an arginine-rich binding motif. Proc Natl Acad Sci U S A 88: 7734-7738.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 7734-7738
    • Zapp, M.L.1    Hope, T.J.2    Parslow, T.G.3    Green, M.R.4
  • 14
    • 0027443137 scopus 로고
    • Identification of the activation domain of equine infectious anemia virus rev
    • Fridell RA, Partin KM, Carpenter S, Cullen BR (1993) Identification of the activation domain of equine infectious anemia virus rev. J Virol 67: 7317-7323.
    • (1993) J Virol , vol.67 , pp. 7317-7323
    • Fridell, R.A.1    Partin, K.M.2    Carpenter, S.3    Cullen, B.R.4
  • 15
    • 0029880471 scopus 로고    scopus 로고
    • Nuclear export of late HIV-1 mRNAs occurs via a cellular protein export pathway
    • Fridell RA, Bogerd HP, Cullen BR (1996) Nuclear export of late HIV-1 mRNAs occurs via a cellular protein export pathway. Proc Natl Acad Sci U S A 93: 4421-4424.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 4421-4424
    • Fridell, R.A.1    Bogerd, H.P.2    Cullen, B.R.3
  • 16
    • 0025074348 scopus 로고
    • Function of the human immunodeficiency virus types 1 and 2 Rev proteins is dependent on their ability to interact with a structured region present in env gene mRNA
    • Dillon PJ, Nelbock P, Perkins A, Rosen CA (1990) Function of the human immunodeficiency virus types 1 and 2 Rev proteins is dependent on their ability to interact with a structured region present in env gene mRNA. J Virol 64: 4428-4437.
    • (1990) J Virol , vol.64 , pp. 4428-4437
    • Dillon, P.J.1    Nelbock, P.2    Perkins, A.3    Rosen, C.A.4
  • 17
    • 0025366681 scopus 로고
    • A highly conserved RNA folding region coincident with the Rev response element of primate immunodeficiency viruses
    • Le SY, Malim MH, Cullen BR, Maizel JV (1990) A highly conserved RNA folding region coincident with the Rev response element of primate immunodeficiency viruses. Nucleic Acids Res 18: 1613-1623.
    • (1990) Nucleic Acids Res , vol.18 , pp. 1613-1623
    • SY, L.1    Malim, M.H.2    Cullen, B.R.3    Maizel, J.V.4
  • 18
    • 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
  • 19
    • 0028108364 scopus 로고
    • A molecular rheostat. Co-operative rev binding to stem I of the rev-response element modulates human immunodeficiency virus type-1 late gene expression
    • Mann DA, Mikaelian I, Zemmel RW, Green SM, Lowe AD, et al. (1994) A molecular rheostat. Co-operative rev binding to stem I of the rev-response element modulates human immunodeficiency virus type-1 late gene expression. J Mol Biol 241: 193-207.
    • (1994) J Mol Biol , vol.241 , pp. 193-207
    • Mann, D.A.1    Mikaelian, I.2    Zemmel, R.W.3    Green, S.M.4    Lowe, A.D.5
  • 20
    • 0029784592 scopus 로고    scopus 로고
    • Alpha helix-RNA major groove recognition in an HIV-1 rev peptide-RRE RNA complex
    • Battiste JL, Mao H, Rao NS, Tan R, Muhandiram DR, 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    Mao, H.2    Rao, N.S.3    Tan, R.4    Muhandiram, D.R.5
  • 21
    • 0037195181 scopus 로고    scopus 로고
    • A synthetic HIV-1 Rev inhibitor interfering with the CRM1-mediated nuclear export
    • Daelemans D, Afonina E, Nilsson J, Werner G, Kjems J, et al. (2002) A synthetic HIV-1 Rev inhibitor interfering with the CRM1-mediated nuclear export. Proc Natl Acad Sci U S A 99: 14440-14445.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 14440-14445
    • Daelemans, D.1    Afonina, E.2    Nilsson, J.3    Werner, G.4    Kjems, J.5
  • 23
    • 0026778318 scopus 로고
    • Structural and functional analysis of the visna virus Rev-response element
    • Tiley LS, Cullen BR (1992) Structural and functional analysis of the visna virus Rev-response element. J Virol 66: 3609-3615.
    • (1992) J Virol , vol.66 , pp. 3609-3615
    • Tiley, L.S.1    Cullen, B.R.2
  • 24
    • 0025036273 scopus 로고
    • Nucleotide sequence and transcriptional analysis of molecular clones of CAEV which generate infectious virus
    • Saltarelli M, Querat G, Konings DA, Vigne R, Clements JE (1990) Nucleotide sequence and transcriptional analysis of molecular clones of CAEV which generate infectious virus. Virology 179: 347-364.
    • (1990) Virology , vol.179 , pp. 347-364
    • Saltarelli, M.1    Querat, G.2    Konings, D.A.3    Vigne, R.4    Clements, J.E.5
  • 25
    • 0036846922 scopus 로고    scopus 로고
    • Rev response elements (RRE) in lentiviruses: An RNAMotif algorithm-based strategy for RRE prediction
    • Lesnik EA, Sampath R, Ecker DJ (2002) Rev response elements (RRE) in lentiviruses: an RNAMotif algorithm-based strategy for RRE prediction. Med Res Rev 22: 617-636.
    • (2002) Med Res Rev , vol.22 , pp. 617-636
    • Lesnik, E.A.1    Sampath, R.2    Ecker, D.J.3
  • 26
    • 0002309133 scopus 로고    scopus 로고
    • An overview of the molecular phylogeny of lentiviruses. HIV Sequence
    • Foley BT (2000) An overview of the molecular phylogeny of lentiviruses. HIV Sequence Compendium 2000: 35-43.
    • (2000) Compendium 2000 , pp. 35-43
    • Foley, B.T.1
  • 27
    • 33645777243 scopus 로고    scopus 로고
    • Characterization of functional domains of equine infectious anemia virus Rev suggests a bipartite RNA-binding domain
    • Lee JH, Murphy SC, Belshan M, Sparks WO, Wannemuchler Y, et al. (2006) Characterization of functional domains of equine infectious anemia virus Rev suggests a bipartite RNA-binding domain. J Virol 80: 3844-3852.
    • (2006) J Virol , vol.80 , pp. 3844-3852
    • Lee, J.H.1    Murphy, S.C.2    Belshan, M.3    Sparks, W.O.4    Wannemuchler, Y.5
  • 28
    • 0031860889 scopus 로고    scopus 로고
    • Differential requirements for alternative splicing and nuclear export functions of equine infectious anemia virus Rev protein
    • Harris ME, Gontarek RR, Derse D, Hope TJ (1998) Differential requirements for alternative splicing and nuclear export functions of equine infectious anemia virus Rev protein. Mol Cell Biol 18: 3889-3899.
    • (1998) Mol Cell Biol , vol.18 , pp. 3889-3899
    • Harris, M.E.1    Gontarek, R.R.2    Derse, D.3    Hope, T.J.4
  • 29
    • 0034096383 scopus 로고    scopus 로고
    • Binding of equine infectious anemia virus rev to an exon splicing enhancer mediates alternative splicing and nuclear export of viral mRNAs
    • Belshan M, Park GS, Bilodeau P, Stoltzfus CM, Carpenter S (2000) Binding of equine infectious anemia virus rev to an exon splicing enhancer mediates alternative splicing and nuclear export of viral mRNAs. Mol Cell Biol 20: 3550-3557.
    • (2000) Mol Cell Biol , vol.20 , pp. 3550-3557
    • Belshan, M.1    Park, G.S.2    Bilodeau, P.3    Stoltzfus, C.M.4    Carpenter, S.5
  • 30
    • 2542426491 scopus 로고    scopus 로고
    • cis-Acting and trans-acting modulation of equine infectious anemia virus alternative RNA splicing
    • Liao HJ, Baker CC, Princler GL, Derse D (2004) cis-Acting and trans-acting modulation of equine infectious anemia virus alternative RNA splicing. Virology 323: 131-140.
    • (2004) Virology , vol.323 , pp. 131-140
    • Liao, H.J.1    Baker, C.C.2    Princler, G.L.3    Derse, D.4
  • 31
    • 0029935065 scopus 로고    scopus 로고
    • Interactions among SR proteins, an exonic splicing enhancer, and a lentivirus Rev protein regulate alternative splicing
    • Gontarek RR, Derse D (1996) Interactions among SR proteins, an exonic splicing enhancer, and a lentivirus Rev protein regulate alternative splicing. Mol Cell Biol 16: 2325-2331.
    • (1996) Mol Cell Biol , vol.16 , pp. 2325-2331
    • Gontarek, R.R.1    Derse, D.2
  • 32
    • 0035374453 scopus 로고    scopus 로고
    • Binding Sites for Rev and ASF/SF2 map to a 55-nucleotide purine-rich exonic element in equine infectious anemia virus RNA
    • Chung II, Derse D (2001) Binding Sites for Rev and ASF/SF2 map to a 55-nucleotide purine-rich exonic element in equine infectious anemia virus RNA. J Biol Chem 276: 18960-18967.
    • (2001) J Biol Chem , vol.276 , pp. 18960-18967
    • Chung II, D.D.1
  • 33
    • 0028355601 scopus 로고
    • Equine infectious anemia virus trans-regulatory protein Rev controls viral mRNA stability, accumulation, and alterriative splicing
    • Martarano L, Stephens R, Rice N, Deese D (1994) Equine infectious anemia virus trans-regulatory protein Rev controls viral mRNA stability, accumulation, and alterriative splicing, J Virol 68: 3102-3111.
    • (1994) J Virol , vol.68 , pp. 3102-3111
    • Martarano, L.1    Stephens, R.2    Rice, N.3    Deese, D.4
  • 34
    • 0031968989 scopus 로고    scopus 로고
    • Biological characterization of Rev variation in equine infectious anemia virus
    • Belshan M, Harris ME, Shoemaker AE, Hope TJ, Carpenter S (1998) Biological characterization of Rev variation in equine infectious anemia virus. J Virol 72: 4421-4426.
    • (1998) J Virol , vol.72 , pp. 4421-4426
    • Belshan, M.1    Harris, M.E.2    Shoemaker, A.E.3    Hope, T.J.4    Carpenter, S.5
  • 35
    • 0035916015 scopus 로고    scopus 로고
    • Belshan M, Baccam P, Oaks.JL, Sponseller BA, Murphy SC, et al. (2001) Genetic and biological variation in equine infectious anemia virus Rev correlates with variable stages of clinical disease in an experimentally infected pony. Virology 279: 185-200.
    • Belshan M, Baccam P, Oaks.JL, Sponseller BA, Murphy SC, et al. (2001) Genetic and biological variation in equine infectious anemia virus Rev correlates with variable stages of clinical disease in an experimentally infected pony. Virology 279: 185-200.
  • 36
    • 0042121256 scopus 로고    scopus 로고
    • Mfold web server for nucleic acid folding and hybridization prediction
    • Zuker M (2003) Mfold web server for nucleic acid folding and hybridization prediction. Nucleic Acids Res 31: 3406-3415.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3406-3415
    • Zuker, M.1
  • 38
    • 3242877996 scopus 로고    scopus 로고
    • Sfold web server for statistical folding and rational design of nucleic acids
    • Ding Y, Chan CY, Lawrence CE (2004) Sfold web server for statistical folding and rational design of nucleic acids. Nucleic Acids Res 32: Wl35-141.
    • (2004) Nucleic Acids Res , vol.32
    • Ding, Y.1    Chan, C.Y.2    Lawrence, C.E.3
  • 39
    • 2442626706 scopus 로고    scopus 로고
    • Incorporating chemical modification constraints into a dynamic programming algorithm for prediction of RNA secondary structure
    • Mathews DH, Disney MD, Childs JL, Schroeder SJ, Zuker M, et al. (2004) Incorporating chemical modification constraints into a dynamic programming algorithm for prediction of RNA secondary structure. Proc Natl Acad Sci U S A 101:7287-7292.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 7287-7292
    • Mathews, D.H.1    Disney, M.D.2    Childs, J.L.3    Schroeder, S.J.4    Zuker, M.5
  • 41
    • 0036301332 scopus 로고    scopus 로고
    • Secondary structure prediction for aligned RNA sequences
    • Hofacker IL, Fekete M, Stadler PF (2002) Secondary structure prediction for aligned RNA sequences. J Mol Biol 319: 1059-1066.
    • (2002) J Mol Biol , vol.319 , pp. 1059-1066
    • Hofacker, I.L.1    Fekete, M.2    Stadler, P.F.3
  • 42
    • 4143150669 scopus 로고    scopus 로고
    • Adaptive immunity is the primary force driving selection of equine infectious anemia virus envelope SU variants during acute infection
    • Mcaley RH, Leib SR, Pownder SL, McGuire TC (2004) Adaptive immunity is the primary force driving selection of equine infectious anemia virus envelope SU variants during acute infection. J Virol 78: 9295-9305.
    • (2004) J Virol , vol.78 , pp. 9295-9305
    • Mcaley, R.H.1    Leib, S.R.2    Pownder, S.L.3    McGuire, T.C.4
  • 43
    • 48449097673 scopus 로고    scopus 로고
    • Merryman CN, H. F. (1998) Footprinting and modification-interference analysis of binding sites on RNA.: New York: Oxford University Press.
    • Merryman CN, H. F. (1998) Footprinting and modification-interference analysis of binding sites on RNA.: New York: Oxford University Press.
  • 44
    • 0033655152 scopus 로고    scopus 로고
    • Directed hydroxyl radical probings of RNA from iron(II) tethered to proteins in ribonucleoprotein complexes
    • Culver GM, Noller HF (2000) Directed hydroxyl radical probings of RNA from iron(II) tethered to proteins in ribonucleoprotein complexes. Methods Enzymol 318: 461-475.
    • (2000) Methods Enzymol , vol.318 , pp. 461-475
    • Culver, G.M.1    Noller, H.F.2
  • 45
    • 0027175502 scopus 로고
    • The cardiac troponin T alternative exon contains a novel purine-rich positive splicing element
    • Xu R, Teng J, Cooper TA (1993) The cardiac troponin T alternative exon contains a novel purine-rich positive splicing element. Mol Cell Biol 13: 3660-3674.
    • (1993) Mol Cell Biol , vol.13 , pp. 3660-3674
    • Xu, R.1    Teng, J.2    Cooper, T.A.3
  • 46
    • 0036375092 scopus 로고    scopus 로고
    • RNA secondary structure and squence conservation in CI region of human immunodeficiency virus type 1 env gene
    • Peleg O, Brunak S, Trifonov EN, Nevo E, Bolshoy A (2002) RNA secondary structure and squence conservation in CI region of human immunodeficiency virus type 1 env gene. AIDS Res Hum Retroviruses 18: 867-878.
    • (2002) AIDS Res Hum Retroviruses , vol.18 , pp. 867-878
    • Peleg, O.1    Brunak, S.2    Trifonov, E.N.3    Nevo, E.4    Bolshoy, A.5
  • 47
    • 0023042012 scopus 로고
    • Information content of binding sites on nucleotide sequences
    • Schneider TD, Stormo GD, Gold L, Ehrenfeucht A (1986) Information content of binding sites on nucleotide sequences. J Mol Biol 188: 415-431.
    • (1986) J Mol Biol , vol.188 , pp. 415-431
    • Schneider, T.D.1    Stormo, G.D.2    Gold, L.3    Ehrenfeucht, A.4
  • 48
    • 0024533114 scopus 로고
    • Excess information at bacteriophage T7 genomic promoters detected by a random cloning technique
    • Schneider TD, Stormo GD (1989) Excess information at bacteriophage T7 genomic promoters detected by a random cloning technique. Nucleic Acids Res 17: 659-674.
    • (1989) Nucleic Acids Res , vol.17 , pp. 659-674
    • Schneider, T.D.1    Stormo, G.D.2
  • 49
    • 0027054380 scopus 로고
    • Features of spliceosome evolution and function inferred from an analysis of the information at human splice sites
    • Stephens RM, Schneider TD (1992) Features of spliceosome evolution and function inferred from an analysis of the information at human splice sites. J Mol Biol 228: 1124-1136.
    • (1992) J Mol Biol , vol.228 , pp. 1124-1136
    • Stephens, R.M.1    Schneider, T.D.2
  • 50
    • 0026601935 scopus 로고
    • Identification of a high-affinity RNA-binding site for the human immunodeficiency virus type 1 Rev protein
    • Tiley LS, Malim MH, Tewary HK, Stockley PG, Cullen BR (1992) Identification of a high-affinity RNA-binding site for the human immunodeficiency virus type 1 Rev protein. Proc Natl Acad Sci U S A 89: 758-762.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 758-762
    • Tiley, L.S.1    Malim, M.H.2    Tewary, H.K.3    Stockley, P.G.4    Cullen, B.R.5
  • 51
    • 0036295198 scopus 로고    scopus 로고
    • Dynalign: An algorithm for finding the secondary structure common to two RNA sequences
    • Mathews DH, Turner DH (2002) Dynalign: an algorithm for finding the secondary structure common to two RNA sequences. J Mol Biol 317: 191-203.
    • (2002) J Mol Biol , vol.317 , pp. 191-203
    • Mathews, D.H.1    Turner, D.H.2
  • 53
    • 0025166385 scopus 로고
    • HIV-1 regulator of virion expression (Rev) protein binds to an RNA stem-loop structure located within the Rev response element region
    • Heaphy S, Dingwall C, Ernberg I, Gait MJ, Green SM, et al. (1990) HIV-1 regulator of virion expression (Rev) protein binds to an RNA stem-loop structure located within the Rev response element region. Cell 60(4): 685-693.
    • (1990) Cell , vol.60 , Issue.4 , pp. 685-693
    • Heaphy, S.1    Dingwall, C.2    Ernberg, I.3    Gait, M.J.4    Green, S.M.5
  • 54
    • 0027441983 scopus 로고
    • Selective optimization of the Rev-binding element of HIV-1
    • Giver L, Bartel D, Zapp M, Pawul A, Green M, et al. (1993) Selective optimization of the Rev-binding element of HIV-1. Nucleic Acids Res 21(23): 5509-5516.
    • (1993) Nucleic Acids Res , vol.21 , Issue.23 , pp. 5509-5516
    • Giver, L.1    Bartel, D.2    Zapp, M.3    Pawul, A.4    Green, M.5
  • 55
    • 0032989115 scopus 로고    scopus 로고
    • Selection and characterization of human immunodeficiency virus type 1 mutants that are resistant to inhibition by the transdominant negative RevM10 protein
    • Hamm TE, Rekosh D, Hammarskjold ML (1999) Selection and characterization of human immunodeficiency virus type 1 mutants that are resistant to inhibition by the transdominant negative RevM10 protein. J Virol 73(7): 5741-5747.
    • (1999) J Virol , vol.73 , Issue.7 , pp. 5741-5747
    • Hamm, T.E.1    Rekosh, D.2    Hammarskjold, M.L.3
  • 56
    • 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, Kam 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(24): 6465-6472.
    • (1992) Nucleic Acids Res , vol.20 , Issue.24 , pp. 6465-6472
    • Iwai, S.1    Pritchard, C.2    Mann, D.A.3    Kam, J.4    Gait, M.J.5
  • 57
    • 0025940429 scopus 로고    scopus 로고
    • Kjems J, Frankel AD, Sharp PA (1991) Specific regulation of mRNA splicing in vitro by a peptide from HIV-1 Rev. Cell 67(1): 169-178.
    • Kjems J, Frankel AD, Sharp PA (1991) Specific regulation of mRNA splicing in vitro by a peptide from HIV-1 Rev. Cell 67(1): 169-178.
  • 58
    • 0026540537 scopus 로고
    • Specific binding of a basic peptide from HIV-1 Rev
    • Kjems J, Calnan BJ, Frankel AD, Sharp PA (1992) Specific binding of a basic peptide from HIV-1 Rev. Embo J 11(3): 1119-1129.
    • (1992) Embo J , vol.11 , Issue.3 , pp. 1119-1129
    • Kjems, J.1    Calnan, B.J.2    Frankel, A.D.3    Sharp, P.A.4
  • 59
    • 0028102988 scopus 로고
    • Inhibition of human immunodeficiency virus type 1 in human T cells by a potent Rev response clement decoy consisting of the 13-nucleotide minimal Rev-binding domain
    • Lee SW, Gallarde HF, Gilboa E, Smith C (1994) Inhibition of human immunodeficiency virus type 1 in human T cells by a potent Rev response clement decoy consisting of the 13-nucleotide minimal Rev-binding domain. J Virol 68(12): 8254-8264.
    • (1994) J Virol , vol.68 , Issue.12 , pp. 8254-8264
    • Lee, S.W.1    Gallarde, H.F.2    Gilboa, E.3    Smith, C.4
  • 60
    • 0028024260 scopus 로고
    • RNA tertiary structure of the HIV RRE domain II containing non-Watson-Crick base pairs GG and GA: Molecular modeling studies
    • Le SY, Pattabiraman N, Maizel JV Jr. (1994) RNA tertiary structure of the HIV RRE domain II containing non-Watson-Crick base pairs GG and GA: molecular modeling studies. Nucleic Acids Res 22(19): 3966-3976.
    • (1994) Nucleic Acids Res , vol.22 , Issue.19 , pp. 3966-3976
    • SY, L.1    Pattabiraman, N.2    Maizel Jr., J.V.3
  • 61
    • 3342977915 scopus 로고    scopus 로고
    • Using an RNA secondary structure partition function to determine confidence in base pairs predicted by free energy minimization
    • Mathews DH (2004) Using an RNA secondary structure partition function to determine confidence in base pairs predicted by free energy minimization. Rna 10: 1178-1190.
    • (2004) Rna , vol.10 , pp. 1178-1190
    • Mathews, D.H.1
  • 62
    • 0029286628 scopus 로고
    • Hydroxyl radical footprinting of ribosomal proteins oil 16S RNA
    • Powers T, Noller HF. (1995) Hydroxyl radical footprinting of ribosomal proteins oil 16S RNA. Rna 1: 194-209.
    • (1995) Rna , vol.1 , pp. 194-209
    • Powers, T.1    Noller, H.F.2
  • 63
    • 0035265946 scopus 로고    scopus 로고
    • Structural model for the cooperative assembly of HIV-1 Rev multimers on the RRE as deduced from analysis of assembly-defective mutants
    • Jain C, Belasco JG (2001) Structural model for the cooperative assembly of HIV-1 Rev multimers on the RRE as deduced from analysis of assembly-defective mutants. Mol Cell 7: 603-614.
    • (2001) Mol Cell , vol.7 , pp. 603-614
    • Jain, C.1    Belasco, J.G.2
  • 64
    • 0022864330 scopus 로고
    • Leutivirus genomic organization: The complete nucleotide sequence of the env gene region of equine infectious anemia virus
    • Rushlow K, Olsen K, Stiegler G, Payne SI, Montelaro RC, et al. (1986) Leutivirus genomic organization: the complete nucleotide sequence of the env gene region of equine infectious anemia virus. Virology 155: 309-321.
    • (1986) Virology , vol.155 , pp. 309-321
    • Rushlow, K.1    Olsen, K.2    Stiegler, G.3    Payne, S.I.4    Montelaro, R.C.5
  • 65
    • 0023178553 scopus 로고
    • Nucleotide sequence analysis of equine infectious anemia virus proviral DNA
    • Kawakami T, Sherman L, Dahlberg J, Gazit A, Yaniv A, et al. (1987) Nucleotide sequence analysis of equine infectious anemia virus proviral DNA. Virology 158: 300-312.
    • (1987) Virology , vol.158 , pp. 300-312
    • Kawakami, T.1    Sherman, L.2    Dahlberg, J.3    Gazit, A.4    Yaniv, A.5
  • 67
    • 0022470564 scopus 로고
    • Rapid chemical probing of conformation in 16 S ribosomal RNA and 30 S ribosomal subunits using primer extension
    • Moazed D, Stern S, Noller HF (1986) Rapid chemical probing of conformation in 16 S ribosomal RNA and 30 S ribosomal subunits using primer extension. J Mol Biol 187: 399-416.
    • (1986) J Mol Biol , vol.187 , pp. 399-416
    • Moazed, D.1    Stern, S.2    Noller, H.F.3
  • 68
    • 48449094600 scopus 로고    scopus 로고
    • http://www.graphpad.com/prism/Prism.htm.
  • 69
    • 84856043672 scopus 로고
    • A mathematical theory of communication
    • Shannon CE (1948) A mathematical theory of communication. The Bell System Technical Journal 27: 379-423, 623-656.
    • (1948) The Bell System Technical Journal , vol.27 , Issue.379-423 , pp. 623-656
    • Shannon, C.E.1
  • 71
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22: 4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 72
    • 33746320475 scopus 로고    scopus 로고
    • Revolutions in RNA secondary structure prediction
    • Mathews DH (2006) Revolutions in RNA secondary structure prediction. J Mol Biol 359: 526-532.
    • (2006) J Mol Biol , vol.359 , pp. 526-532
    • Mathews, D.H.1
  • 73
    • 33744790273 scopus 로고    scopus 로고
    • Prediction of RNA secondary structure by free energy minimization
    • Mathews DH, Turner DH (2006) Prediction of RNA secondary structure by free energy minimization. Curr Opin Struct Biol 16: 270-278.
    • (2006) Curr Opin Struct Biol , vol.16 , pp. 270-278
    • Mathews, D.H.1    Turner, D.H.2
  • 74
    • 0041620358 scopus 로고    scopus 로고
    • PSEUDOVIEWER2: Visualization of RNA pseudoknots of any type
    • Han K, Byun Y (2003) PSEUDOVIEWER2: Visualization of RNA pseudoknots of any type. Nucleic Acids Res 31: 3432-3410.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3432-3410
    • Han, K.1    Byun, Y.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.