메뉴 건너뛰기




Volumn 18, Issue 12, 1998, Pages 7304-7316

Inhibition of double-stranded RNA-dependent protein kinase PKR by vaccinia virus E3: Role of complex formation and the E3 N-terminal domain

Author keywords

[No Author keywords available]

Indexed keywords

DOUBLE STRANDED RNA; INITIATION FACTOR 2; INTERFERON; PROTEIN KINASE; RNA BINDING PROTEIN; VIRUS PROTEIN;

EID: 0031723958     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.18.12.7304     Document Type: Article
Times cited : (169)

References (55)
  • 1
    • 0024394966 scopus 로고
    • Vaccinia specific kinase inhibitory factor prevents translational inhibition by double-stranded RNA in rabbit reticulocyte lysate
    • Akkaraju, G. R., P. Whitaker-Dowling, I. S. Younger, and R. Jagus. 1989. Vaccinia specific kinase inhibitory factor prevents translational inhibition by double-stranded RNA in rabbit reticulocyte lysate. J. Biol. Chem. 264: 10321-10325.
    • (1989) J. Biol. Chem. , vol.264 , pp. 10321-10325
    • Akkaraju, G.R.1    Whitaker-Dowling, P.2    Younger, I.S.3    Jagus, R.4
  • 2
    • 0028936838 scopus 로고
    • Reversal of the interferon-sensitive phenotype of a vaccinia virus lacking E3L by expression of the reovirus S4 gene
    • Beattie, E., K. L. Denzler, J. Tartaglia, M. E. Perkus, E. Paoletti, and B. L. Jacobs. 1995. Reversal of the interferon-sensitive phenotype of a vaccinia virus lacking E3L by expression of the reovirus S4 gene. J. Virol. 69:499-505.
    • (1995) J. Virol. , vol.69 , pp. 499-505
    • Beattie, E.1    Denzler, K.L.2    Tartaglia, J.3    Perkus, M.E.4    Paoletti, E.5    Jacobs, B.L.6
  • 4
    • 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., C. Neuveut, R. F. Chun, S. M. Smith, C. E. Samuel, A. Gatignol, and K. T. Jeang. 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    Neuveut, C.2    Chun, R.F.3    Smith, S.M.4    Samuel, C.E.5    Gatignol, A.6    Jeang, K.T.7
  • 5
    • 0030989529 scopus 로고    scopus 로고
    • Characterization of the solution complex between the interferon-induced, double-stranded RNA-activated protein kinase and HIV-1 trans-activating region RNA
    • Carpick, B. W., V. Graziano, D. Schneider, R. K. Maitra, X. Lee, and B. R. G. Williams. 1997. Characterization of the solution complex between the interferon-induced, double-stranded RNA-activated protein kinase and HIV-1 trans-activating region RNA. J. Biol. Chem. 272:9510-9516.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9510-9516
    • Carpick, B.W.1    Graziano, V.2    Schneider, D.3    Maitra, R.K.4    Lee, X.5    Williams, B.R.G.6
  • 6
    • 0027163011 scopus 로고
    • Recombinant vaccinia virus K3L gene product prevents activation of double-stranded RNA-dependent, initiation factor 2α-specific protein kinase
    • Carroll, K., O. Elroy-Stein, B. Moss, and R. Jagus. 1993. Recombinant vaccinia virus K3L gene product prevents activation of double-stranded RNA-dependent, initiation factor 2α-specific protein kinase. J. Biol. Chem. 268:12837-12842.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12837-12842
    • Carroll, K.1    Elroy-Stein, O.2    Moss, B.3    Jagus, R.4
  • 7
    • 0000615498 scopus 로고
    • Plasmid vectors carrying the replication origin of filamentous single-stranded phages
    • J. K. Setlow and A. Hollaender (ed.), Plenum Press, New York, N.Y.
    • Cesareni, G., and J. A. H. Murray. 1987. Plasmid vectors carrying the replication origin of filamentous single-stranded phages, p. 135-154. In J. K. Setlow and A. Hollaender (ed.), Genetic engineering: principals and methods, vol. 9. Plenum Press, New York, N.Y.
    • (1987) Genetic Engineering: Principals and Methods , vol.9 , pp. 135-154
    • Cesareni, G.1    Murray, J.A.H.2
  • 8
    • 0026751682 scopus 로고
    • The E3L gene of vaccinia virus encodes an inhibitor of the interferon-induced, double-stranded RNA-dependent protein kinase
    • Chang, H. W., J. C. Watson, and B. L. Jacobs. 1992. The E3L gene of vaccinia virus encodes an inhibitor of the interferon-induced, double-stranded RNA-dependent protein kinase. Proc. Natl. Acad. Sci. USA 89: 4825-4829.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4825-4829
    • Chang, H.W.1    Watson, J.C.2    Jacobs, B.L.3
  • 9
    • 0027163047 scopus 로고
    • Identification of a conserved motif that is necessary for binding of the vaccinia virus E3L gene products to double-stranded
    • Chang, H.-W., and B. L. Jacobs. 1993. Identification of a conserved motif that is necessary for binding of the vaccinia virus E3L gene products to double-stranded. Virology 194:537-547.
    • (1993) Virology , vol.194 , pp. 537-547
    • Chang, H.-W.1    Jacobs, B.L.2
  • 10
    • 0029133407 scopus 로고
    • Rescue of vaccinia virus lacking the E3L gene by mutants of E3L
    • Chang, H.-W., L. H. Uribe, and B. L. Jacobs. 1995. Rescue of vaccinia virus lacking the E3L gene by mutants of E3L. J. Virol. 69:6605-6608.
    • (1995) J. Virol. , vol.69 , pp. 6605-6608
    • Chang, H.-W.1    Uribe, L.H.2    Jacobs, B.L.3
  • 12
    • 0002352428 scopus 로고    scopus 로고
    • Protein kinases that phosphorylate eIF2 and eIF2B, and their role in eukaryotic cell translational control
    • J. W. B. Hershey, M. B. Mathews, and N. Sonenberg (ed.), Cold Spring Harbor Laboratory Press, Plainview, N.Y.
    • Clemens, M. J. 1996. Protein kinases that phosphorylate eIF2 and eIF2B, and their role in eukaryotic cell translational control, p. 139-172. In J. W. B. Hershey, M. B. Mathews, and N. Sonenberg (ed.), Translational control. Cold Spring Harbor Laboratory Press, Plainview, N.Y.
    • (1996) Translational Control , pp. 139-172
    • Clemens, M.J.1
  • 14
    • 0029785474 scopus 로고    scopus 로고
    • The kinase insert domain of interferon-induced protein kinase PKR is required for activity but not for interaction with the pseudosubstrate K3L
    • Craig, A. W. B., G. P. Cosentino, O. Donze, and N. Sonenberg. 1996. The kinase insert domain of interferon-induced protein kinase PKR is required for activity but not for interaction with the pseudosubstrate K3L. J. Biol. Chem. 271:24526-24533.
    • (1996) J. Biol. Chem. , vol.271 , pp. 24526-24533
    • Craig, A.W.B.1    Cosentino, G.P.2    Donze, O.3    Sonenberg, N.4
  • 15
    • 0027407080 scopus 로고
    • The E3L and K3L vaccinia virus gene products stimulate translation through inhibition of the double-stranded RNA-dependent protein kinase by different mechanisms
    • Davies, M. V., H. W. Chang, B. L. Jacobs, and R. J. Kaufman. 1993 The E3L and K3L vaccinia virus gene products stimulate translation through inhibition of the double-stranded RNA-dependent protein kinase by different mechanisms. J. Virol. 67:1688-1692.
    • (1993) J. Virol. , vol.67 , pp. 1688-1692
    • Davies, M.V.1    Chang, H.W.2    Jacobs, B.L.3    Kaufman, R.J.4
  • 17
    • 0026556814 scopus 로고
    • Phosphorylation of initiation factor 2α by protein kinase GCN2 mediates gene-specific translational control of GCN4 in yeast
    • Dever, T. E., L. Feng, R. C. Wek, A. M. Cigan, T. D. Donahue, and A. G. Hinnebusch. 1992. Phosphorylation of initiation factor 2α by protein kinase GCN2 mediates gene-specific translational control of GCN4 in yeast. Cell 68:585-596.
    • (1992) Cell , vol.68 , pp. 585-596
    • Dever, T.E.1    Feng, L.2    Wek, R.C.3    Cigan, A.M.4    Donahue, T.D.5    Hinnebusch, A.G.6
  • 18
    • 0032516048 scopus 로고    scopus 로고
    • Disruption of cellular translational control by a viral truncated eukaryotic translation initiation factor 2α kinase homolog
    • Dever, T. E., R. Sripriya, J. R. McLachlin, J. Lu, J. R. Fabian, S. R. Kimball, and L. K. Miller. 1998. Disruption of cellular translational control by a viral truncated eukaryotic translation initiation factor 2α kinase homolog. Proc. Natl. Acad. Sci. USA 95:4164-4169.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 4164-4169
    • Dever, T.E.1    Sripriya, R.2    McLachlin, J.R.3    Lu, J.4    Fabian, J.R.5    Kimball, S.R.6    Miller, L.K.7
  • 19
    • 0028263738 scopus 로고
    • Construction of an improved host strain for two hybrid screening
    • Feilotter, H. E., G. J. Hannon, C. J. Ruddell, and D. Beach. 1994. Construction of an improved host strain for two hybrid screening. Nucleic Acids Res. 22:1502-1503.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 1502-1503
    • Feilotter, H.E.1    Hannon, G.J.2    Ruddell, C.J.3    Beach, D.4
  • 20
    • 8944219769 scopus 로고    scopus 로고
    • IPK and vaccinia virus K3L is mediated by unique domains: Implications for kinase regulation
    • IPK and vaccinia virus K3L is mediated by unique domains: implications for kinase regulation. Mol. Cell. Biol. 16:4172-4181.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 4172-4181
    • Gale, M.1    Tan, S.-L.2    Wambach, M.3    Katze, M.G.4
  • 21
    • 0343924357 scopus 로고    scopus 로고
    • Evidence that hepatitis C virus resistance to interferon is mediated through repression of the PKR protein kinase by the nonstructural 5A protein
    • Gale, M. J., M. J. Korth, N. M. Tang, S. L. Tab, D. A. Hopkins, T. E. Dever, S. J. Polyak, D. R. Gretch, and M. G. Katze. 1997. Evidence that hepatitis C virus resistance to interferon is mediated through repression of the PKR protein kinase by the nonstructural 5A protein. Virology 230:217-227.
    • (1997) Virology , vol.230 , pp. 217-227
    • Gale, M.J.1    Korth, M.J.2    Tang, N.M.3    Tab, S.L.4    Hopkins, D.A.5    Dever, T.E.6    Polyak, S.J.7    Gretch, D.R.8    Katze, M.G.9
  • 22
    • 0031916702 scopus 로고    scopus 로고
    • The orf virus OV20.0L gene product is involved in interferon resistance and inhibits an interferon-inducible, double-stranded RNA-dependent kinase
    • Haig, D. M., C. J. McInnes, J. Thomson, A. Wood, K. Bunyan, and A. Mercer. 1998. The orf virus OV20.0L gene product is involved in interferon resistance and inhibits an interferon-inducible, double-stranded RNA-dependent kinase. Immunology 93:335-340.
    • (1998) Immunology , vol.93 , pp. 335-340
    • Haig, D.M.1    McInnes, C.J.2    Thomson, J.3    Wood, A.4    Bunyan, K.5    Mercer, A.6
  • 23
    • 0029963273 scopus 로고    scopus 로고
    • Physical and functional characterization of the double-stranded RNA binding protein encoded by the vaccinia virus E3 gene
    • Ho, C. K., and S. Shuman. 1996. Physical and functional characterization of the double-stranded RNA binding protein encoded by the vaccinia virus E3 gene. Virology 217:272-284.
    • (1996) Virology , vol.217 , pp. 272-284
    • Ho, C.K.1    Shuman, S.2
  • 24
    • 0025598302 scopus 로고
    • Sequence requirements for coiled coils: Analysis with lambda repressor-GCN4 leucine zipper fusions
    • Hu, J. C., E. K. O'Shea, P. S. Kim, and R. T. Sauer. 1990. Sequence requirements for coiled coils: analysis with lambda repressor-GCN4 leucine zipper fusions. Science 250:1400-1403.
    • (1990) Science , vol.250 , pp. 1400-1403
    • Hu, J.C.1    O'Shea, E.K.2    Kim, P.S.3    Sauer, R.T.4
  • 25
    • 0016669608 scopus 로고
    • The characteristics of inhibition of protein synthesis by double-stranded ribonucleic acid in reticulocyte lysates
    • Hunter, T., T. Hunt, R. J. Jackson, and H. D. Robertson. 1975. The characteristics of inhibition of protein synthesis by double-stranded ribonucleic acid in reticulocyte lysates. J. Biol. Chem. 250:409-417.
    • (1975) J. Biol. Chem. , vol.250 , pp. 409-417
    • Hunter, T.1    Hunt, T.2    Jackson, R.J.3    Robertson, H.D.4
  • 26
    • 0020529962 scopus 로고
    • Transformation of intact yeast cells treated with alkali cations
    • Ito, H., Y. Fukada, K. Murata, and A. Kimura. 1983. Transformation of intact yeast cells treated with alkali cations. J. Bacteriol. 153:163-168.
    • (1983) J. Bacteriol. , vol.153 , pp. 163-168
    • Ito, H.1    Fukada, Y.2    Murata, K.3    Kimura, A.4
  • 27
    • 0028589116 scopus 로고
    • Proteins that interact with PKR
    • Jagus, R., and M. M. Gray. 1994. Proteins that interact with PKR. Biochimie 76:779-791.
    • (1994) Biochimie , vol.76 , pp. 779-791
    • Jagus, R.1    Gray, M.M.2
  • 28
    • 0030927170 scopus 로고    scopus 로고
    • Regulation of the protein kinase PKR by the vaccinia virus pseudosubstrate inhibitor K3L is dependent on residues conserved between the K3L protein and the PKR substrate elF2α
    • Kawagishi-Kobayashi, M., J. B. Silverman, T. K. Ung, and T. E. Dever. 1997. Regulation of the protein kinase PKR by the vaccinia virus pseudosubstrate inhibitor K3L is dependent on residues conserved between the K3L protein and the PKR substrate elF2α. Mol. Cell. Biol. 17:4146-4158.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 4146-4158
    • Kawagishi-Kobayashi, M.1    Silverman, J.B.2    Ung, T.K.3    Dever, T.E.4
  • 29
    • 0024549254 scopus 로고
    • Purification and activation of the double-stranded RNA-dependent eIF-2 kinase DAI
    • Kostura, M., and M. B. Mathews. 1989. Purification and activation of the double-stranded RNA-dependent eIF-2 kinase DAI. Mol. Cell. Biol. 9:1576-1586.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 1576-1586
    • Kostura, M.1    Mathews, M.B.2
  • 30
    • 0020570527 scopus 로고
    • Comparison of initiation of protein synthesis in procaryotes, eucaryotes, and organelles
    • Kozak, M. 1983. Comparison of initiation of protein synthesis in procaryotes, eucaryotes, and organelles. Microbiol. Rev. 47:1-45.
    • (1983) Microbiol. Rev. , vol.47 , pp. 1-45
    • Kozak, M.1
  • 31
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 33
    • 0028362126 scopus 로고
    • Products of the porcine N5P3 gene bind specifically to double-stranded RNA and inhibit activation of the interferon-induced protein kinase. PKR
    • Langland, J. O., S. M. Pettiford, B. Jiang, and B. L. Jacobs. 1994. Products of the porcine N5P3 gene bind specifically to double-stranded RNA and inhibit activation of the interferon-induced protein kinase. PKR. J. Virol. 68: 3821-3829.
    • (1994) J. Virol. , vol.68 , pp. 3821-3829
    • Langland, J.O.1    Pettiford, S.M.2    Jiang, B.3    Jacobs, B.L.4
  • 34
    • 0000519248 scopus 로고
    • Viral evasion of cellular defense mechanisms: Regulation of the protein kinase DAI by RNA effectors
    • Mathews, M. B. 1993. Viral evasion of cellular defense mechanisms: regulation of the protein kinase DAI by RNA effectors. Semin. Virol. 4:247-257.
    • (1993) Semin. Virol. , vol.4 , pp. 247-257
    • Mathews, M.B.1
  • 35
    • 0028796512 scopus 로고
    • Mutational analysis of the double-stranded RNA (dsRNA) binding domain of the dsRNA-activated protein kinase, PKR
    • McMillan, N. A., B. W. Carpick, B. Hollis, W. M. Toone, M. Zamanian-Daryoush, and B. R. G. Williams. 1995. Mutational analysis of the double-stranded RNA (dsRNA) binding domain of the dsRNA-activated protein kinase, PKR. J. Biol. Chem. 270:2601-2606.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2601-2606
    • McMillan, N.A.1    Carpick, B.W.2    Hollis, B.3    Toone, W.M.4    Zamanian-Daryoush, M.5    Williams, B.R.G.6
  • 36
    • 0030030724 scopus 로고    scopus 로고
    • Mechanism of interferon action. Biochemical and genetic evidence for the intermolecular association of the RNA-dependent protein kinase PkR from human cells
    • Ortega, L. G., M. D. McCotter, G. L. Henry, S. J. McCormack, D. C. Thomis, and C. E. Samuel. 1996. Mechanism of interferon action. Biochemical and genetic evidence for the intermolecular association of the RNA-dependent protein kinase PkR from human cells. Virology 215:31-39.
    • (1996) Virology , vol.215 , pp. 31-39
    • Ortega, L.G.1    McCotter, M.D.2    Henry, G.L.3    McCormack, S.J.4    Thomis, D.C.5    Samuel, C.E.6
  • 38
    • 0029115903 scopus 로고
    • The interferon-inducible double-stranded RNA-activated protein kinase self-associates in vitro and in vivo
    • Patel, R. C., P. Stanton, N. M. J. McMillan, B. R. G. Williams, and G. C. Sen. 1995. The interferon-inducible double-stranded RNA-activated protein kinase self-associates in vitro and in vivo. Proc. Natl. Acad. Sci. USA 92:8283-8287.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8283-8287
    • Patel, R.C.1    Stanton, P.2    McMillan, N.M.J.3    Williams, B.R.G.4    Sen, G.C.5
  • 39
    • 0029841348 scopus 로고    scopus 로고
    • Specific mutations near the amino terminus of double-stranded RNA-dependent protein kinase (PKR) differentially affect its double-stranded RNA binding and dimerization properties
    • Patel, R. C., P. Stanton, and G. C. Sen. 1996. Specific mutations near the amino terminus of double-stranded RNA-dependent protein kinase (PKR) differentially affect its double-stranded RNA binding and dimerization properties. J. Biol. Chem. 271:25657-25663.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25657-25663
    • Patel, R.C.1    Stanton, P.2    Sen, G.C.3
  • 40
    • 0031020341 scopus 로고    scopus 로고
    • Homologous segments in three subunits of the guanine nucleotide exchange factor eIF2B mediate translational regulation by phosphorylation of eIF2
    • Pavitt, G. D., W. Yang, and A. G. Hinnebusch. 1997. Homologous segments in three subunits of the guanine nucleotide exchange factor eIF2B mediate translational regulation by phosphorylation of eIF2. Mol. Cell. Biol. 17: 1298-1313.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 1298-1313
    • Pavitt, G.D.1    Yang, W.2    Hinnebusch, A.G.3
  • 41
    • 0028924758 scopus 로고
    • Structural requirements for double-stranded RNA binding, dimerization, and activation of the human eIF-2α kinase DAI in Saccharomyces cerevisiae
    • Romano, P. R., S. R. Green, G. N. Barber, M. B. Mathews, and A. G. Hinnebusch. 1995. Structural requirements for double-stranded RNA binding, dimerization, and activation of the human eIF-2α kinase DAI in Saccharomyces cerevisiae. Mol. Cell. Biol. 15:365-378.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 365-378
    • Romano, P.R.1    Green, S.R.2    Barber, G.N.3    Mathews, M.B.4    Hinnebusch, A.G.5
  • 42
    • 0029078852 scopus 로고
    • Functional characterization of the RNA-binding domain and motif of the double-stranded RNA-dependent protein kinase DAI (PKR)
    • Schmedt, C., S. R. Green, L. Manche, D. R. Taylor, Y. Ma, and M. B. Mathews. 1995. Functional characterization of the RNA-binding domain and motif of the double-stranded RNA-dependent protein kinase DAI (PKR). J. Mol. Biol. 249:29-44.
    • (1995) J. Mol. Biol. , vol.249 , pp. 29-44
    • Schmedt, C.1    Green, S.R.2    Manche, L.3    Taylor, D.R.4    Ma, Y.5    Mathews, M.B.6
  • 43
    • 85038554659 scopus 로고    scopus 로고
    • The vaccinia virus E3L gene product interacts with both the regulatory and substrate binding regions of PKR: Implications for PKR autoregulation
    • in press
    • Sharp, T. V., A. Romashko, F. Moonan, B. Joshi, G. N. Barber, and R. Jagus. The vaccinia virus E3L gene product interacts with both the regulatory and substrate binding regions of PKR: implications for PKR autoregulation. Virology, in press.
    • Virology
    • Sharp, T.V.1    Romashko, A.2    Moonan, F.3    Joshi, B.4    Barber, G.N.5    Jagus, R.6
  • 45
    • 0031555657 scopus 로고    scopus 로고
    • Complementation of deletion of the vaccinia virus E3L gene by the Escherichia coli RNase III gene
    • Shors, T., and B. L. Jacobs. 1997. Complementation of deletion of the vaccinia virus E3L gene by the Escherichia coli RNase III gene. Virology 227: 77-87.
    • (1997) Virology , vol.227 , pp. 77-87
    • Shors, T.1    Jacobs, B.L.2
  • 47
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski, R, S., and P. Hieter. 1989. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122:19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 50
    • 0025947970 scopus 로고
    • Characterization of a vaccinia virus-encoded double-stranded RNA-binding protein that may be involved in inhibition of the double-stranded RNA-dependent protein kinase
    • Watson, J. C., H. W. C hang, and B. L. Jacobs. 1991. Characterization of a vaccinia virus-encoded double-stranded RNA-binding protein that may be involved in inhibition of the double-stranded RNA-dependent protein kinase. Virology 185:206-216.
    • (1991) Virology , vol.185 , pp. 206-216
    • Watson, J.C.1    Hang, H.W.C.2    Jacobs, B.L.3
  • 51
    • 0030030997 scopus 로고    scopus 로고
    • Double-stranded (ds) RNA binding and not dimerization correlates with the activation of the dsRNA-dependent protein kinase (PKR)
    • Wu, S., and R. J. Kaufman. 1996. Double-stranded (ds) RNA binding and not dimerization correlates with the activation of the dsRNA-dependent protein kinase (PKR). J. Biol. Chem. 271:1756-1763.
    • (1996) J. Biol. Chem. , vol.271 , pp. 1756-1763
    • Wu, S.1    Kaufman, R.J.2
  • 52
    • 0031021425 scopus 로고    scopus 로고
    • A model for the double-stranded RNA (dsRNA)-dependent dimerization and activation of the dsRNA-activated protein kinase PKR
    • Wu, S., and R. J. Kaufman. 1997. A model for the double-stranded RNA (dsRNA)-dependent dimerization and activation of the dsRNA-activated protein kinase PKR. J. Biol. Chem. 272:1291-1296.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1291-1296
    • Wu, S.1    Kaufman, R.J.2
  • 53
    • 0024368864 scopus 로고
    • Precise gene fusion by PCR
    • Yon, J., and M. Fried. 1988. Precise gene fusion by PCR. Nucleic Acids Res. 17:4895.
    • (1988) Nucleic Acids Res. , vol.17 , pp. 4895
    • Yon, J.1    Fried, M.2
  • 54
    • 0027255150 scopus 로고
    • Nuclear localization of a double-stranded RNA-binding protein encoded by the vaccinia virus E3L gene
    • Yuwen, H., J. H. Cox, J. W. Yewdell, J. R. Bennink, and B. Moss. 1993. Nuclear localization of a double-stranded RNA-binding protein encoded by the vaccinia virus E3L gene. Virology 195:732-744.
    • (1993) Virology , vol.195 , pp. 732-744
    • Yuwen, H.1    Cox, J.H.2    Yewdell, J.W.3    Bennink, J.R.4    Moss, B.5
  • 55
    • 0030908706 scopus 로고    scopus 로고
    • Ribosome targeting of PKR is mediated by two double-stranded RNA-binding domains and facilitates in vivo phosphorylation of eukaryotic initiation factor-2
    • Zhu, S., P. R. Romano, and R. C. Wek. 1997. Ribosome targeting of PKR is mediated by two double-stranded RNA-binding domains and facilitates in vivo phosphorylation of eukaryotic initiation factor-2. J. Biol. Chem. 272: 14434-14441.
    • (1997) J. Biol. Chem. , vol.272 , pp. 14434-14441
    • Zhu, S.1    Romano, P.R.2    Wek, R.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.