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Volumn 17, Issue 9, 1997, Pages 503-524

The double-stranded RNA-dependent protein kinase PKR: Structure and function

Author keywords

[No Author keywords available]

Indexed keywords

DOUBLE STRANDED RNA; ENZYME ACTIVATOR; GROWTH FACTOR; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERFERON; INTERLEUKIN 3; PLATELET DERIVED GROWTH FACTOR; PROTEIN KINASE; PROTEIN KINASE INHIBITOR; RNA BINDING PROTEIN; TRANSCRIPTION FACTOR; TRANSFORMING GROWTH FACTOR BETA;

EID: 0030725442     PISSN: 10799907     EISSN: None     Source Type: Journal    
DOI: 10.1089/jir.1997.17.503     Document Type: Review
Times cited : (530)

References (224)
  • 1
    • 0016669608 scopus 로고
    • The characteristics of inhibition of protein synthesis by double-stranded ribonucleic acid in reticulocyte lysates
    • HUNTER, T., HUNT, T., JACKSON, R.J., and ROBERTSON, H.D. (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
  • 2
    • 0016781908 scopus 로고
    • Inhibition of protein synthesis in rabbit reticulocyte lysates by double-stranded RNA and oxidized glutathione: Indirect mode of action on polypeptide chain initiation
    • CLEMENS, M.J., SAFER, B., MERRICK, W.C., ANDERSON, W.F., and LONDON, I.M. (1975). Inhibition of protein synthesis in rabbit reticulocyte lysates by double-stranded RNA and oxidized glutathione: indirect mode of action on polypeptide chain initiation. Proc. Natl. Acad. Sci. USA 72, 1286-1290.
    • (1975) Proc. Natl. Acad. Sci. USA , vol.72 , pp. 1286-1290
    • Clemens, M.J.1    Safer, B.2    Merrick, W.C.3    Anderson, W.F.4    London, I.M.5
  • 3
    • 0017370502 scopus 로고
    • Phosphorylation of initiation factor eIF-2 and control of reticulocyte protein synthesis
    • FARRELL, P.J., BALKOW, K., HUNT, T., JACKSON, R.J., and TRACHSEL, H. (1977). Phosphorylation of initiation factor eIF-2 and control of reticulocyte protein synthesis. Cell 11, 187-200.
    • (1977) Cell , vol.11 , pp. 187-200
    • Farrell, P.J.1    Balkow, K.2    Hunt, T.3    Jackson, R.J.4    Trachsel, H.5
  • 4
    • 0017890248 scopus 로고
    • Regulation of protein synthesis: Activation by double-stranded RNA of a protein kinase that phosphorylates eukaryotic initiation factor 2
    • LEVIN, D., and LONDON, I.M. (1978). Regulation of protein synthesis: activation by double-stranded RNA of a protein kinase that phosphorylates eukaryotic initiation factor 2. Proc. Natl. Acad. Sci. USA 75, 1121-1125.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 1121-1125
    • Levin, D.1    London, I.M.2
  • 5
    • 0019222257 scopus 로고
    • Characterization of a double-stranded RNA-activated kinase that phosphorylates alpha subunit of eukaryotic initiation factor 2 (eIF-2α) in reticulocyte lysates
    • LEVIN, D.H., PETRYSHYN, R., and LONDON, I.M. (1980). Characterization of a double-stranded RNA-activated kinase that phosphorylates alpha subunit of eukaryotic initiation factor 2 (eIF-2α) in reticulocyte lysates. Proc. Natl. Acad. Sci. USA 77, 832-836.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 832-836
    • Levin, D.H.1    Petryshyn, R.2    London, I.M.3
  • 6
    • 0002864972 scopus 로고
    • Interferon action: Two distinct pathways for inhibition of protein synthesis by double-stranded RNA
    • FARRELL, P.J., SEN, G.C., DUBOIS, M.F., RATNER, L., SLATTERY, E., and LENGYEL, P. (1978). Interferon action: two distinct pathways for inhibition of protein synthesis by double-stranded RNA. Proc. Natl. Acad. Sci. USA 75, 5893-5897.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 5893-5897
    • Farrell, P.J.1    Sen, G.C.2    Dubois, M.F.3    Ratner, L.4    Slattery, E.5    Lengyel, P.6
  • 7
    • 0017180822 scopus 로고
    • Interferon-induced inhibition of protein synthesis in L-cell extracts: An ATP-dependent step in the activation of an inhibitor by double-stranded RNA
    • ROBERTS, W.K., CLEMENS, M.J., and KERR, I.M. (1976). Interferon-induced inhibition of protein synthesis in L-cell extracts: an ATP-dependent step in the activation of an inhibitor by double-stranded RNA. Proc. Natl. Acad. Sci. USA 73, 3136-3140.
    • (1976) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 3136-3140
    • Roberts, W.K.1    Clemens, M.J.2    Kerr, I.M.3
  • 8
    • 0017177570 scopus 로고
    • Specific phosphorylation in vitro of a protein associated with ribosomes of interferon-treated mouse L cells
    • ZILBERSTEIN, A., FEDERMANN, P., SCHULMAN, L., and REVEL, M. (1976). Specific phosphorylation in vitro of a protein associated with ribosomes of interferon-treated mouse L cells. FEBS Lett. 68, 119-124.
    • (1976) FEBS Lett. , vol.68 , pp. 119-124
    • Zilberstein, A.1    Federmann, P.2    Schulman, L.3    Revel, M.4
  • 9
    • 0040350202 scopus 로고
    • Mechanism of interferon action: Phosphorylation of protein synthesis initiation factor eIF-2 in interferon-treated human cells by a ribosome-associated kinase possessing site specificity similar to hemin regulated rabbit reticulocyte kinase
    • SAMUEL, C.E. (1979). Mechanism of interferon action: phosphorylation of protein synthesis initiation factor eIF-2 in interferon-treated human cells by a ribosome-associated kinase possessing site specificity similar to hemin regulated rabbit reticulocyte kinase. Proc. Natl. Acd. Sci. USA 76, 600-604.
    • (1979) Proc. Natl. Acd. Sci. USA , vol.76 , pp. 600-604
    • Samuel, C.E.1
  • 10
    • 0021689391 scopus 로고
    • Mechanism of interferon action. Increased phosphorylation of protein synthesis initiation factor eIF-2(alpha) in interferon-treated, reovirus-infected mouse L929 fibroblasts in vitro and in vivo
    • SAMUEL, C.E., DUNCAN, R., KNUTSON, G.S., and HERSHEY, J.W.B. (1984). Mechanism of interferon action. Increased phosphorylation of protein synthesis initiation factor eIF-2(alpha) in interferon-treated, reovirus-infected mouse L929 fibroblasts in vitro and in vivo. J. Biol. Chem. 259, 13451-13457.
    • (1984) J. Biol. Chem. , vol.259 , pp. 13451-13457
    • Samuel, C.E.1    Duncan, R.2    Knutson, G.S.3    Hershey, J.W.B.4
  • 11
    • 0021815202 scopus 로고
    • Double-stranded RNA-dependent protein kinase and 2-5A system are both activated in interferon-treated, encephalomyocarditis virus-infected HeLa cells
    • RICE, A.P., DUNCAN, R., HERSHEY, J.W.B., and KERR, I.M. (1985). Double-stranded RNA-dependent protein kinase and 2-5A system are both activated in interferon-treated, encephalomyocarditis virus-infected HeLa cells. J. Virol. 54, 894-898.
    • (1985) J. Virol. , vol.54 , pp. 894-898
    • Rice, A.P.1    Duncan, R.2    Hershey, J.W.B.3    Kerr, I.M.4
  • 12
    • 0021275744 scopus 로고
    • Further characterization of the protein kinase activity mediated by interferon in mouse and human cells
    • KRUST, B., GALABRU, J., and HOVANESSIAN, A.G. (1984). Further characterization of the protein kinase activity mediated by interferon in mouse and human cells. J. Biol. Chem. 259, 8494-8496.
    • (1984) J. Biol. Chem. , vol.259 , pp. 8494-8496
    • Krust, B.1    Galabru, J.2    Hovanessian, A.G.3
  • 13
    • 0024833410 scopus 로고
    • The double-stranded RNA-activated protein kinase induced by interferon: dsRNA-PK
    • HOVANESSIAN, A.G. (1989). The double-stranded RNA-activated protein kinase induced by interferon: dsRNA-PK. J. Interferon Res. 9, 641-647.
    • (1989) J. Interferon Res. , vol.9 , pp. 641-647
    • Hovanessian, A.G.1
  • 15
    • 0027418321 scopus 로고
    • The eIF-2α protein kinases, regulators of translation in eukaryotes from yeasts to humans
    • SAMUEL, C.E. (1993). The eIF-2α protein kinases, regulators of translation in eukaryotes from yeasts to humans. J. Biol. Chem. 268, 7603-7606.
    • (1993) J. Biol. Chem. , vol.268 , pp. 7603-7606
    • Samuel, C.E.1
  • 16
    • 0028433524 scopus 로고
    • Regulation of eukaryotic protein synthesis by protein kinases that phosphorylate initiation factor eIF-2
    • CLEMENS, M.J. (1994). Regulation of eukaryotic protein synthesis by protein kinases that phosphorylate initiation factor eIF-2. Mol. Biol. Reports 19, 201-210.
    • (1994) Mol. Biol. Reports , vol.19 , pp. 201-210
    • Clemens, M.J.1
  • 17
    • 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 (eds.) Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • CLEMENS, M.J. (1996). Protein kinases that phosphorylate eIF2 and eIF2B, and their role in eukaryotic cell translational control. In: Translational Control. J.W.B. Hershey, M.B. Mathews, and N. Sonenberg (eds.) Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press, pp. 139-172.
    • (1996) Translational Control , pp. 139-172
    • Clemens, M.J.1
  • 18
    • 0029328380 scopus 로고
    • Identification of a plant-encoded analog of PKR, the mammalian double-strnaded RNA-dependent protein kinase
    • LANGLAND, J.O., JIN, S., JACOBS, B.L., and ROTH, D.A. (1995). Identification of a plant-encoded analog of PKR, the mammalian double-strnaded RNA-dependent protein kinase. Plant Physiol. 108, 1259-1267.
    • (1995) Plant Physiol. , vol.108 , pp. 1259-1267
    • Langland, J.O.1    Jin, S.2    Jacobs, B.L.3    Roth, D.A.4
  • 19
    • 0030047484 scopus 로고    scopus 로고
    • Phosphorylation of plant eukaryotic initiation factor-2 by the plant-encoded double-stranded RNA-dependent protein kinase, pPKR, and inhibition of protein synthesis in vitro
    • LANGLAND, J.O., LANGLAND, L.A., BROWNING, K.S., and ROTH, D.A. (1996). Phosphorylation of plant eukaryotic initiation factor-2 by the plant-encoded double-stranded RNA-dependent protein kinase, pPKR, and inhibition of protein synthesis in vitro. J. Biol. Chem. 271, 4539-4544.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4539-4544
    • Langland, J.O.1    Langland, L.A.2    Browning, K.S.3    Roth, D.A.4
  • 20
    • 0030267336 scopus 로고    scopus 로고
    • The eIF-2α kinases and the control of protein synthesis
    • DE HARO, C., MÉNDEZ, R., and SANTOYO, J. (1996). The eIF-2α kinases and the control of protein synthesis. FASEB J. 10, 1378-1387.
    • (1996) FASEB J. , vol.10 , pp. 1378-1387
    • De Haro, C.1    Méndez, R.2    Santoyo, J.3
  • 22
    • 0029046288 scopus 로고
    • The interferon system: A review with emphasis on the role of PKR in growth control
    • JARAMILLO, M.L., ABRAHAM, N., and BELL, J.C. (1995). The interferon system: a review with emphasis on the role of PKR in growth control. Cancer Invest. 13, 327-338.
    • (1995) Cancer Invest. , vol.13 , pp. 327-338
    • Jaramillo, M.L.1    Abraham, N.2    Bell, J.C.3
  • 23
    • 0029007407 scopus 로고
    • PKR: A new name and new roles
    • PROUD, C.G. (1995). PKR: a new name and new roles. Trends Biochem. Sci. 20, 241-246.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 241-246
    • Proud, C.G.1
  • 24
    • 0028797781 scopus 로고
    • The role of the dsRNA-activated kinase, PKR, in signal transduction
    • WILLIAMS, B.R.G. (1995). The role of the dsRNA-activated kinase, PKR, in signal transduction. Semin. Virol. 6, 191-202.
    • (1995) Semin. Virol. , vol.6 , pp. 191-202
    • Williams, B.R.G.1
  • 25
    • 0030585155 scopus 로고    scopus 로고
    • When two strands are better than one: The mediators and modulators of the cellular responses to double-stranded RNA
    • JACOBS, B.L., and LANGLAND, J.O. (1996). When two strands are better than one: the mediators and modulators of the cellular responses to double-stranded RNA. Virology 219, 339-349.
    • (1996) Virology , vol.219 , pp. 339-349
    • Jacobs, B.L.1    Langland, J.O.2
  • 27
    • 0030440591 scopus 로고    scopus 로고
    • The regulation of the protein kinase PKR by RNA
    • ROBERTSON, H.D., and MATHEWS, M.B. (1996). The regulation of the protein kinase PKR by RNA. Biochimie 78, 909-914.
    • (1996) Biochimie , vol.78 , pp. 909-914
    • Robertson, H.D.1    Mathews, M.B.2
  • 28
    • 0027999025 scopus 로고
    • Mechanism of interferon action: Structure of the mouse PKR gene encoding the interferon-inducible RNA-dependent protein kinase
    • TANAKA, H., and SAMUEL, C.E. (1994). Mechanism of interferon action: structure of the mouse PKR gene encoding the interferon-inducible RNA-dependent protein kinase. Proc. Natl. Acad. Sci. USA 91, 7995-7999.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 7995-7999
    • Tanaka, H.1    Samuel, C.E.2
  • 29
    • 0028817525 scopus 로고
    • Sequence of the murine interferon-inducible RNA-dependent protein kinase (PKR) deduced from genomic clones
    • TANAKA, H., and SAMUEL, C.E. (1995). Sequence of the murine interferon-inducible RNA-dependent protein kinase (PKR) deduced from genomic clones. Gene 153, 283-284.
    • (1995) Gene , vol.153 , pp. 283-284
    • Tanaka, H.1    Samuel, C.E.2
  • 30
    • 0030586859 scopus 로고    scopus 로고
    • Structural organization of the human gene (PKR) encoding an interferon-inducible RNA-dependent protein kinase (PKR) and differences from its mouse homolog
    • KUHEN, K.L., SHEN, X.Y., CARLISLE, E.R., RICHARDSON, A.L., WEIER, H.U.G., TANAKA, H., and SAMUEL, C.E. (1996). Structural organization of the human gene (PKR) encoding an interferon-inducible RNA-dependent protein kinase (PKR) and differences from its mouse homolog. Genomics 36, 197-201.
    • (1996) Genomics , vol.36 , pp. 197-201
    • Kuhen, K.L.1    Shen, X.Y.2    Carlisle, E.R.3    Richardson, A.L.4    Weier, H.U.G.5    Tanaka, H.6    Samuel, C.E.7
  • 31
    • 0030608391 scopus 로고    scopus 로고
    • Mechanism of interferon action - Sequence of the human interferon-inducible RNA-dependent protein kinase (PKR) deduced from genomic clones
    • KUHEN, K.L., SHEN, X.Y., and SAMUEL, C.E. (1996). Mechanism of interferon action - sequence of the human interferon-inducible RNA-dependent protein kinase (PKR) deduced from genomic clones. Gene 178, 191-193.
    • (1996) Gene , vol.178 , pp. 191-193
    • Kuhen, K.L.1    Shen, X.Y.2    Samuel, C.E.3
  • 32
    • 0027294641 scopus 로고
    • Chromosomal assignment of the interferon-inducible double-stranded RNA-dependent protein kinase (PRKR) to human chromosome 2p21-p22 and mouse chromosome 17 E2
    • BARBER, G.N., EDELHOFF, S., KATZE, M.G., and DISTECHE, C.M. (1993). Chromosomal assignment of the interferon-inducible double-stranded RNA-dependent protein kinase (PRKR) to human chromosome 2p21-p22 and mouse chromosome 17 E2. Genomics 16, 765-767.
    • (1993) Genomics , vol.16 , pp. 765-767
    • Barber, G.N.1    Edelhoff, S.2    Katze, M.G.3    Disteche, C.M.4
  • 33
    • 0027285719 scopus 로고
    • Localization of the human interferon-induced, ds-RNA activated p68 kinase gene (PRKR) to chromosome 2p21-p22
    • SQUIRE, J., MEURS, E.F., CHONG, K.L., McMILLAN, N.A.J., HOVANESSIAN, A.G., and WILLIAMS, B.R.G. (1993). Localization of the human interferon-induced, ds-RNA activated p68 kinase gene (PRKR) to chromosome 2p21-p22. Genomics 16, 768-770.
    • (1993) Genomics , vol.16 , pp. 768-770
    • Squire, J.1    Meurs, E.F.2    Chong, K.L.3    McMillan, N.A.J.4    Hovanessian, A.G.5    Williams, B.R.G.6
  • 34
    • 0031555628 scopus 로고    scopus 로고
    • Isolation of the interferon-inducible RNA-dependent protein kinase Pkr promoter and identification of a novel DNA element within the 5′-flanking region of human and mouse Pkr genes
    • KUHEN, K.L., and SAMUEL, C.E. (1997). Isolation of the interferon-inducible RNA-dependent protein kinase Pkr promoter and identification of a novel DNA element within the 5′-flanking region of human and mouse Pkr genes. Virology 227, 119-130.
    • (1997) Virology , vol.227 , pp. 119-130
    • Kuhen, K.L.1    Samuel, C.E.2
  • 35
    • 0025298202 scopus 로고
    • Molecular cloning and characterization of the human double-stranded RNA-activated protein kinase induced by interferon
    • MEURS, E., CHONG, K., GALABRU, J., THOMAS, N.S.B., KERR, I.M., WILLIAMS, B.R.G., and HOVANESSIAN, A.G. (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    Chong, K.2    Galabru, J.3    Thomas, N.S.B.4    Kerr, I.M.5    Williams, B.R.G.6    Hovanessian, A.G.7
  • 36
    • 0027428105 scopus 로고
    • The mouse antiphosphotyrosine immunoreactive kinase, TIK, is indistinguishable from the double-stranded RNA-dependent, interferon-induced protein kinase, PKR
    • BAIER, L.J., SHORS, T., SHORS, S.T., and JACOBS, B.L. (1993). The mouse antiphosphotyrosine immunoreactive kinase, TIK, is indistinguishable from the double-stranded RNA-dependent, interferon-induced protein kinase, PKR. Nucleic Acids Res. 21, 4830-4835.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 4830-4835
    • Baier, L.J.1    Shors, T.2    Shors, S.T.3    Jacobs, B.L.4
  • 37
    • 0027938042 scopus 로고
    • Cloning and characterization of a cDNA encoding rat PKR, the double-stranded RNA-dependent eukaryotic initiation factor-2 kinase
    • MELLOR, H., FLOWERS, K.M., KIMBALL, S.R., and JEFFERSON, L.S. (1994). Cloning and characterization of a cDNA encoding rat PKR, the double-stranded RNA-dependent eukaryotic initiation factor-2 kinase. Biochim. Biophys. Acta 1219, 693-696.
    • (1994) Biochim. Biophys. Acta , vol.1219 , pp. 693-696
    • Mellor, H.1    Flowers, K.M.2    Kimball, S.R.3    Jefferson, L.S.4
  • 38
    • 0026686791 scopus 로고
    • Identification of the double-stranded RNA-binding domain of the human interferon-inducible protein kinase
    • PATEL, R.C., and SEN, G.C. (1992). Identification of the double-stranded RNA-binding domain of the human interferon-inducible protein kinase. J. Biol. Chem. 267, 7671-7676.
    • (1992) J. Biol. Chem. , vol.267 , pp. 7671-7676
    • Patel, R.C.1    Sen, G.C.2
  • 39
    • 0028243096 scopus 로고
    • Mechanism of interferon action: Motif I of the interferon-induced, RNA-dependent protein kinase (PKR) is sufficient to mediate RNA-binding activity
    • McCORMACK, S.J., ORTEGA, L.G., DOOHAN, J.P., and SAMUEL, C.E. (1994). Mechanism of interferon action: motif I of the interferon-induced, RNA-dependent protein kinase (PKR) is sufficient to mediate RNA-binding activity. Virology 198, 92-99.
    • (1994) Virology , vol.198 , pp. 92-99
    • McCormack, S.J.1    Ortega, L.G.2    Doohan, J.P.3    Samuel, C.E.4
  • 40
    • 0026042013 scopus 로고
    • Functional expression and RNA binding analysis of the interferon-induced, double-stranded RNA-activated, 68,000-Mr protein kinase in a cell-free system
    • KATZE, M.G., WAMBACH, M., WONG, M-L., GARFINKEL, M., MEURS, E., CHONG, K., WILLIAMS, B.R.G., HOVANESSIAN, A.G., and BARBER, G.N. (1991). Functional expression and RNA binding analysis of the interferon-induced, double-stranded RNA-activated, 68,000-Mr protein kinase in a cell-free system. Mol. Cell. Biol. 11, 5497-5505.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 5497-5505
    • Katze, M.G.1    Wambach, M.2    Wong, M.-L.3    Garfinkel, M.4    Meurs, E.5    Chong, K.6    Williams, B.R.G.7    Hovanessian, A.G.8    Barber, G.N.9
  • 41
    • 0027105279 scopus 로고
    • Two RNA-binding motifs in the double-stranded RNA-activated protein kinase, DAI
    • GREEN, S.R., and MATHEWS, M.B. (1992). Two RNA-binding motifs in the double-stranded RNA-activated protein kinase, DAI. Genes Dev. 6, 2478-2490.
    • (1992) Genes Dev. , vol.6 , pp. 2478-2490
    • Green, S.R.1    Mathews, M.B.2
  • 42
    • 0026716255 scopus 로고
    • Mechanism of interferon action: Identification of a RNA binding domain within the N-terminal region of the human RNA-dependent P1/eIF-2α protein kinase
    • McCORMACK, S.J., THOMIS, D.C., and SAMUEL, C.E. (1992). Mechanism of interferon action: identification of a RNA binding domain within the N-terminal region of the human RNA-dependent P1/eIF-2α protein kinase. Virology 188, 47-56.
    • (1992) Virology , vol.188 , pp. 47-56
    • McCormack, S.J.1    Thomis, D.C.2    Samuel, C.E.3
  • 43
    • 0028241859 scopus 로고
    • Role of the amino-terminal residues of the interferon-induced protein kinase in its activation by double-stranded RNA and heparin
    • PATEL, R.C., STANTON, P., and SEN, G.C. (1994). Role of the amino-terminal residues of the interferon-induced protein kinase in its activation by double-stranded RNA and heparin. J. Biol. Chem. 269, 18593-18598.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18593-18598
    • Patel, R.C.1    Stanton, P.2    Sen, G.C.3
  • 44
    • 0029258446 scopus 로고
    • Interaction between the double-stranded RNA binding motif and RNA: Definition of the binding site for the interferon-induced protein kinase DAI (PKR) on adenovirus VA RNA
    • CLARKE, P.A., and MATHEWS, M.B. (1995). Interaction between the double-stranded RNA binding motif and RNA: definition of the binding site for the interferon-induced protein kinase DAI (PKR) on adenovirus VA RNA. RNA 1, 7-20.
    • (1995) RNA , vol.1 , pp. 7-20
    • Clarke, P.A.1    Mathews, M.B.2
  • 45
    • 0029078852 scopus 로고
    • Functional characterization of the RNA-binding domain and motif of the double-stranded RNA-dependent protein kinase DAI (PKR)
    • SCHMEDT, C., GREEN, S.R., MANCHE, L., TAYLOR, D.R., MA, Y., and MATHEWS, M.B. (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
  • 46
    • 0028796512 scopus 로고
    • Mutational analysis of the double-stranded RNA (dsRNA) binding domain of the dsRNA-activated protein kinase, PKR
    • McMILLAN, N.A.J., CARPICK, B.W., HOLLIS, B., TOONE, W.M., ZAMANIAN-DARYOUSH, M., and WILLIAMS, B.R.G. (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.J.1    Carpick, B.W.2    Hollis, B.3    Toone, W.M.4    Zamanian-Daryoush, M.5    Williams, B.R.G.6
  • 47
    • 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., STANTON, P., and SEN, G.C. (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
  • 48
    • 0030219790 scopus 로고    scopus 로고
    • Peptides derived from the interferon-induced PKR prevent activation by HIV-1 TAR RNA
    • NEKHAI, S., KUMAR, A., BOTTARO, D.P., and PETRYSHYN, R. (1996). Peptides derived from the interferon-induced PKR prevent activation by HIV-1 TAR RNA. Virology 222, 193-200.
    • (1996) Virology , vol.222 , pp. 193-200
    • Nekhai, S.1    Kumar, A.2    Bottaro, D.P.3    Petryshyn, R.4
  • 50
    • 0027102716 scopus 로고
    • Binding of influenza virus NS1 protein to dsRNA in vitro
    • HATADA, E., and FUKUDA, R. (1992). Binding of influenza virus NS1 protein to dsRNA in vitro. J. Gen. Virol. 73, 3325-3329.
    • (1992) J. Gen. Virol. , vol.73 , pp. 3325-3329
    • Hatada, E.1    Fukuda, R.2
  • 51
    • 0027163047 scopus 로고
    • Identification of a conserved motif that is necessary for binding of the vaccinia virus E3L gene products to double-stranded RNA
    • CHANG, H.-W., and JACOBS, B.L. (1993). Identification of a conserved motif that is necessary for binding of the vaccinia virus E3L gene products to double-stranded RNA. Virology 19-4, 537-547.
    • (1993) Virology , vol.194 , pp. 537-547
    • Chang, H.-W.1    Jacobs, B.L.2
  • 52
    • 0029264544 scopus 로고
    • Two basic motifs of reovirus σ3 protein are involved in double-stranded RNA binding
    • MABROUK, T., DANIS, C., and LEMAY, G. (1995). Two basic motifs of reovirus σ3 protein are involved in double-stranded RNA binding. Biochem. Cell Biol. 73, 137-145.
    • (1995) Biochem. Cell Biol. , vol.73 , pp. 137-145
    • Mabrouk, T.1    Danis, C.2    Lemay, G.3
  • 53
    • 0030009311 scopus 로고    scopus 로고
    • Mutational analysis of the vaccinia virus E3 protein defines amino acid residues involved in E3 binding to double-stranded RNA
    • HO, C.K., and SHUMAN, S. (1996). Mutational analysis of the vaccinia virus E3 protein defines amino acid residues involved in E3 binding to double-stranded RNA. J. Virol. 70, 2611-2614.
    • (1996) J. Virol. , vol.70 , pp. 2611-2614
    • Ho, C.K.1    Shuman, S.2
  • 54
    • 0028407347 scopus 로고
    • Binding properties of newly identified Xenopus proteins containing dsRNA-binding motifs
    • BASS, B.L., HURST, S.R., and SINGER, J.D. (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
  • 55
    • 0029959285 scopus 로고    scopus 로고
    • Comparative mutational analysis of the double-stranded RNA binding domains of Xenopus laevis RNA-binding protein A
    • KROVAT, B.C., and JANTSCH, M.F. (1996). Comparative mutational analysis of the double-stranded RNA binding domains of Xenopus laevis RNA-binding protein A. J. Biol. Chem. 271, 28112-28119.
    • (1996) J. Biol. Chem. , vol.271 , pp. 28112-28119
    • Krovat, B.C.1    Jantsch, M.F.2
  • 56
    • 0029041105 scopus 로고
    • NMR solution structure of a dsRNA binding domain from Drosophila staufen protein reveals homology to the N-terminal domain of ribosomal protein S5
    • BYCROFT, M., GRÜNERT, S., MURZIN, A.G., PROCTOR, M., and ST JOHNSTON, D. (1995). NMR solution structure of a dsRNA binding domain from Drosophila staufen protein reveals homology to the N-terminal domain of ribosomal protein S5. EMBO J. 14, 3563-3571.
    • (1995) EMBO J. , vol.14 , pp. 3563-3571
    • Bycroft, M.1    Grünert, S.2    Murzin, A.G.3    Proctor, M.4    St Johnston, D.5
  • 57
    • 0029944947 scopus 로고    scopus 로고
    • Detection of double-stranded RNA-protein interactions by methylene blue-mediated photo-crosslinking
    • LIU, Z-R., WILKIE, A.M., CLEMENS, M.J., and SMITH, C.W.J. (1996). Detection of double-stranded RNA-protein interactions by methylene blue-mediated photo-crosslinking. RNA 2, 611-621.
    • (1996) RNA , vol.2 , pp. 611-621
    • Liu, Z.-R.1    Wilkie, A.M.2    Clemens, M.J.3    Smith, C.W.J.4
  • 58
    • 0029058994 scopus 로고
    • Structure of the dsRNA binding domain of E. coli RNase III
    • KHARRAT, A., MACIAS, M.J., GIBSON, T.J., NILGES, M., and PASTURE, A. (1995). Structure of the dsRNA binding domain of E. coli RNase III. EMBO J. 14, 3572-3584.
    • (1995) EMBO J. , vol.14 , pp. 3572-3584
    • Kharrat, A.1    Macias, M.J.2    Gibson, T.J.3    Nilges, M.4    Pasture, A.5
  • 59
    • 0025280401 scopus 로고
    • Structural studies of protein-nucleic acid interaction: The sources of sequence-specific binding
    • STEITZ, T.A. (1990). Structural studies of protein-nucleic acid interaction: the sources of sequence-specific binding. Q. Rev. Biophys. 23, 205-280.
    • (1990) Q. Rev. Biophys. , vol.23 , pp. 205-280
    • Steitz, T.A.1
  • 60
    • 0029782652 scopus 로고    scopus 로고
    • Minor-groove recognition of double-stranded RNA by the double-stranded RNA-binding domain from the RNA-activated protein kinase PKR
    • BEVILACQUA, P.C., and CECH, T.R. (1996). Minor-groove recognition of double-stranded RNA by the double-stranded RNA-binding domain from the RNA-activated protein kinase PKR. Biochemistry 35, 9983-9994.
    • (1996) Biochemistry , vol.35 , pp. 9983-9994
    • Bevilacqua, P.C.1    Cech, T.R.2
  • 61
    • 0026713151 scopus 로고
    • Interactions between double-stranded RNA regulators and the protein kinase DAI
    • MANCHE, L., GREEN, S.R., SCHMEDT, C., and MATHEWS, M.B. (1992). Interactions between double-stranded RNA regulators and the protein kinase DAI. Mol. Cell. Biol. 12, 5238-5248.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 5238-5248
    • Manche, L.1    Green, S.R.2    Schmedt, C.3    Mathews, M.B.4
  • 62
    • 0028171125 scopus 로고
    • eIF-2 kinases: Regulators of general and genespecific translation initiation
    • WEK, R.C. (1994). eIF-2 kinases: Regulators of general and genespecific translation initiation. Trends Biochem. Sci. 19, 491-496.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 491-496
    • Wek, R.C.1
  • 64
    • 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., COSENTINO, G.P., DONZÉ, O., and SONENBERG, N. (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    Donzé, O.3    Sonenberg, N.4
  • 65
    • 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 Jr., M.1    Tan, S.L.2    Wambach, M.3    Katze, M.G.4
  • 66
    • 0029148470 scopus 로고
    • IRF-1 induced cell growth inhibition and interferon induction requires the activity of the protein kinase PKR
    • KIRCHHOFF, S., KOROMILAS, A.E., SCHAPER, F., GRASHOFF, M., SONENBERG, N., and HAUSER, H. (1995). IRF-1 induced cell growth inhibition and interferon induction requires the activity of the protein kinase PKR. Oncogene 11, 439-445.
    • (1995) Oncogene , vol.11 , pp. 439-445
    • Kirchhoff, S.1    Koromilas, A.E.2    Schaper, F.3    Grashoff, M.4    Sonenberg, N.5    Hauser, H.6
  • 67
    • 0029990084 scopus 로고    scopus 로고
    • Expression of the protein kinase PKR is modulated by IRF-1 and is reduced in 5q-associated leukemias
    • BERETTA, L., GABBAY, M., BERGER, R., HANASH, S.M., and SONENBERG, N. (1996). Expression of the protein kinase PKR is modulated by IRF-1 and is reduced in 5q-associated leukemias. Oncogene 12, 1593-1596.
    • (1996) Oncogene , vol.12 , pp. 1593-1596
    • Beretta, L.1    Gabbay, M.2    Berger, R.3    Hanash, S.M.4    Sonenberg, N.5
  • 68
    • 0023656671 scopus 로고
    • Autophoshorylation of the protein kinase dependent on double-stranded RNA
    • GALABRU, J., and HOVANESSIAN, A. (1987). Autophoshorylation of the protein kinase dependent on double-stranded RNA. J. Biol. Chem. 262, 15538-15544.
    • (1987) J. Biol. Chem. , vol.262 , pp. 15538-15544
    • Galabru, J.1    Hovanessian, A.2
  • 72
    • 0029981093 scopus 로고    scopus 로고
    • An essential role for the interferon-inducible, double-stranded RNA-activated protein kinase PKR in the tumor necrosis factor-induced apoptosis in U937 cells
    • YEUNG, M.C., LIU, J., and LAU, A.S. (1996). An essential role for the interferon-inducible, double-stranded RNA-activated protein kinase PKR in the tumor necrosis factor-induced apoptosis in U937 cells. Proc. Natl. Acad. Sci. USA 93, 12451-12455.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 12451-12455
    • Yeung, M.C.1    Liu, J.2    Lau, A.S.3
  • 73
    • 0029093904 scopus 로고
    • Interruption of myogenesis by transforming growth factor β1 or EGTA inhibits expression and activity of the myogenic-associaled (2′-5′) oligoadenylate synthetase and PKR
    • SALZBERG, S., MANDELBAUM, M., ZALCBERG, M., and SHAINBERG, A. (1995). Interruption of myogenesis by transforming growth factor β1 or EGTA inhibits expression and activity of the myogenic-associaled (2′-5′) oligoadenylate synthetase and PKR. Exp. Cell Res. 219, 223-232.
    • (1995) Exp. Cell Res. , vol.219 , pp. 223-232
    • Salzberg, S.1    Mandelbaum, M.2    Zalcberg, M.3    Shainberg, A.4
  • 74
    • 0029996422 scopus 로고    scopus 로고
    • Cloning, expression, and cellular localization of the oncogenic 58-kDa inhibitor of the RNA-activated human and mouse protein kinase
    • KORTH, M.J., LYONS, C.N., WAMBACH, M., and KATZE, M.G. (1996). Cloning, expression, and cellular localization of the oncogenic 58-kDa inhibitor of the RNA-activated human and mouse protein kinase. Gene 170, 181-188.
    • (1996) Gene , vol.170 , pp. 181-188
    • Korth, M.J.1    Lyons, C.N.2    Wambach, M.3    Katze, M.G.4
  • 75
    • 0023708282 scopus 로고
    • Influenza virus regulates protein synthesis during infection by repressing autophosphorylation and activity of the cellular 68,000-Mr protein kinase
    • KATZE, M.G., TOMITA, J., BLACK, T., KRUG, R.M., SAFER, B., and HOVANESSIAN, A. (1988). Influenza virus regulates protein synthesis during infection by repressing autophosphorylation and activity of the cellular 68,000-Mr protein kinase. J. Viral. 62, 3710-3717.
    • (1988) J. Viral. , vol.62 , pp. 3710-3717
    • Katze, M.G.1    Tomita, J.2    Black, T.3    Krug, R.M.4    Safer, B.5    Hovanessian, A.6
  • 76
    • 0030026945 scopus 로고    scopus 로고
    • The P58 cellular inhibitor complexes with the interferon-induced, double-stranded RNA-dependent protein kinase, PKR, to regulate its autophosphorylation and activity
    • POLYAK, S.J., TANG, N., WAMBACH, M., BARBER, G.N., and KATZE, M.G. (1996). The P58 cellular inhibitor complexes with the interferon-induced, double-stranded RNA-dependent protein kinase, PKR, to regulate its autophosphorylation and activity. J. Biol. Chem. 271, 1702-1707.
    • (1996) J. Biol. Chem. , vol.271 , pp. 1702-1707
    • Polyak, S.J.1    Tang, N.2    Wambach, M.3    Barber, G.N.4    Katze, M.G.5
  • 77
    • 0029855773 scopus 로고    scopus 로고
    • The 58-kDa cellular inhibitor of the double stranded RNA-dependent protein kinase requires the tetratricopeptide repeat 6 and DnaJ motifs to stimulate protein synthesis in vivo
    • TANG, N.M., HO, C.Y., and KATZE, M.G. (1996). The 58-kDa cellular inhibitor of the double stranded RNA-dependent protein kinase requires the tetratricopeptide repeat 6 and DnaJ motifs to stimulate protein synthesis in vivo. J. Biol. Chem. 271, 28660-28666.
    • (1996) J. Biol. Chem. , vol.271 , pp. 28660-28666
    • Tang, N.M.1    Ho, C.Y.2    Katze, M.G.3
  • 78
    • 0031013877 scopus 로고    scopus 로고
    • The molecular chaperone hsp40 regulates the activity of P58IPK, the cellular inhibitor of PKR
    • MELVILLE, M.W., HANSEN, W.J., FREEMAN, B.C., WELCH, W.J., and KATZE, M.G. (1997). The molecular chaperone hsp40 regulates the activity of P58IPK, the cellular inhibitor of PKR. Proc. Natl. Acad. Sci. USA 94, 97-102.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 97-102
    • Melville, M.W.1    Hansen, W.J.2    Freeman, B.C.3    Welch, W.J.4    Katze, M.G.5
  • 79
    • 0027420488 scopus 로고
    • Mechanism of interferon action: Evidence for intermolecular autophosphorylation and autoactivation of the interferon-induced, RNA-dependent protein kinase PKR
    • THOMIS, D.C., and SAMUEL, C.E. (1993). Mechanism of interferon action: evidence for intermolecular autophosphorylation and autoactivation of the interferon-induced, RNA-dependent protein kinase PKR. J. Virol. 67, 7695-7700.
    • (1993) J. Virol. , vol.67 , pp. 7695-7700
    • Thomis, D.C.1    Samuel, C.E.2
  • 80
    • 0029039746 scopus 로고
    • Mechanisms of interferon action: Characterization of the intermolecular autophosphorylation of PKR, the interferon-inducible, RNA-dependent protein kinase
    • THOMIS, D.C., and SAMUEL, C.E. (1995). Mechanisms of interferon action: characterization of the intermolecular autophosphorylation of PKR, the interferon-inducible, RNA-dependent protein kinase. J. Virol. 69, 5195-5198.
    • (1995) J. Virol. , vol.69 , pp. 5195-5198
    • Thomis, D.C.1    Samuel, C.E.2
  • 81
    • 10244257563 scopus 로고    scopus 로고
    • Autophosphorylation sites participate in the activation of the double-stranded RNA-activated protein kinase PKR
    • TAYLOR, D.R., LEE, S.B., ROMAND, P.R., MARSHAK, D.R., HINNEBUSCH, A.G., ESTEBAN, M., and MATHEWS, M.B. (1996). Autophosphorylation sites participate in the activation of the double-stranded RNA-activated protein kinase PKR. Mol. Cell. Biol. 16, 6295-6302.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6295-6302
    • Taylor, D.R.1    Lee, S.B.2    Romand, P.R.3    Marshak, D.R.4    Hinnebusch, A.G.5    Esteban, M.6    Mathews, M.B.7
  • 82
    • 0024549254 scopus 로고
    • Purification and activation of the double-stranded RNA-dependent eIF-2 kinase DAI
    • KOSTURA, M., and MATHEWS, M.B. (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
  • 83
    • 0024543242 scopus 로고
    • The binding of double-stranded RNA and adenovirus VAI RNA to the interferon-induced protein kinase
    • GALABRU, J., KATZE, M.G., ROBERT, N., and HOVANESSIAN, A.G. (1989). The binding of double-stranded RNA and adenovirus VAI RNA to the interferon-induced protein kinase. Eur. J. Biochem. 178, 581-589.
    • (1989) Eur. J. Biochem. , vol.178 , pp. 581-589
    • Galabru, J.1    Katze, M.G.2    Robert, N.3    Hovanessian, A.G.4
  • 85
    • 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., GREEN, S.R., BARBER, G.N., MATHEWS, M.B., and HINNEBUSCH, A.G. (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
  • 86
    • 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.Y., and KAUFMAN, R.J. (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.Y.1    Kaufman, R.J.2
  • 87
    • 0030989529 scopus 로고    scopus 로고
    • Characterization of the solution complex between the interferon-induced, double-stranded RNA-activated protein kinase PKR and HIV-1 TAR RNA
    • CARPICK, B.W., GRAZIANO, V., SCHNEIDER, D., MAITRA, R.K., LEE, X., and WILLIAMS, B.R.G. (1997). Characterization of the solution complex between the interferon-induced, double-stranded RNA-activated protein kinase PKR and HIV-1 TAR 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
  • 88
    • 0023948036 scopus 로고
    • Characterization of the double-stranded RNA implicated in the inhibition of protein synthesis in cells infected with a mutant adenovirus defective for VA RNAI
    • MARAN, A., and MATHEWS, M.B. (1988). Characterization of the double-stranded RNA implicated in the inhibition of protein synthesis in cells infected with a mutant adenovirus defective for VA RNAI. Virology 164, 106-113.
    • (1988) Virology , vol.164 , pp. 106-113
    • Maran, A.1    Mathews, M.B.2
  • 89
    • 0030033398 scopus 로고    scopus 로고
    • In vitro activation of the interferon-induced, double-stranded RNA-dependent protein kinase PKR by RNA, from the 3′ untranslated regions of human α-tropomyosin
    • DAVIS, S., and WATSON, J.C. (1996). In vitro activation of the interferon-induced, double-stranded RNA-dependent protein kinase PKR by RNA, from the 3′ untranslated regions of human α-tropomyosin. Proc. Natl. Acad. Sci. USA 93, 508-513.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 508-513
    • Davis, S.1    Watson, J.C.2
  • 90
    • 0024296623 scopus 로고
    • Regulation of in vitro translation by double-stranded RNA in mammalian cell mRNA preparations
    • PRATT, G., GALPINE, A.R., SHARP, N.A., PALMER, S., and CLEMENS, M.J. (1988). Regulation of in vitro translation by double-stranded RNA in mammalian cell mRNA preparations. Nucleic Acids Res. 16, 3497-3510.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 3497-3510
    • Pratt, G.1    Galpine, A.R.2    Sharp, N.A.3    Palmer, S.4    Clemens, M.J.5
  • 91
    • 0030198564 scopus 로고    scopus 로고
    • Characterization of the heparin-mediated activation of PKR, the interferon-inducible RNA-dependent protein kinase
    • GEORGE, C.X., THOMIS, D.C., McCORMACK, S.J., SVAHN, C.M., and SAMUEL, C.E. (1996). Characterization of the heparin-mediated activation of PKR, the interferon-inducible RNA-dependent protein kinase. Virology 221, 180-188.
    • (1996) Virology , vol.221 , pp. 180-188
    • George, C.X.1    Thomis, D.C.2    McCormack, S.J.3    Svahn, C.M.4    Samuel, C.E.5
  • 92
    • 0027943267 scopus 로고
    • Activation of the double-stranded RNA (dsRNA)-activated human protein kinase in vivo in the absence of its dsRNA binding domain
    • LEE, S.B., GREEN, S.R., MATHEWS, M.B., and ESTEBAN, M. (1994). Activation of the double-stranded RNA (dsRNA)-activated human protein kinase in vivo in the absence of its dsRNA binding domain. Proc. Natl. Acad. Sci. USA 91, 10551-10555.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10551-10555
    • Lee, S.B.1    Green, S.R.2    Mathews, M.B.3    Esteban, M.4
  • 93
    • 0024316945 scopus 로고
    • Identification of a 90-kDa polypeptide which associates with adenovirus VA RNAI and is phosphorylated by the double-stranded RNA-dependent protein kinase
    • RICE, A.P., KOSTURA, M., and MATHEWS, M.B. (1989). Identification of a 90-kDa polypeptide which associates with adenovirus VA RNAI and is phosphorylated by the double-stranded RNA-dependent protein kinase. J. Biol. Chem. 264, 20632-20637.
    • (1989) J. Biol. Chem. , vol.264 , pp. 20632-20637
    • Rice, A.P.1    Kostura, M.2    Mathews, M.B.3
  • 94
    • 0027966119 scopus 로고
    • Interleukin 3 stimulates protein synthesis by regulating double-stranded RNA-dependent protein kinase
    • ITO, T., JAGUS, R., and MAY, W.S. (1994). Interleukin 3 stimulates protein synthesis by regulating double-stranded RNA-dependent protein kinase. Proc. Natl. Acad. Sci. USA 91, 7455-7459.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 7455-7459
    • Ito, T.1    Jagus, R.2    May, W.S.3
  • 96
    • 0027319027 scopus 로고
    • Expression of a phosphorylation-resistant eukaryotic initiation factor 2α-subunit mitigates heat shock inhibition of protein synthe-sis
    • MURTHA-RIEL, P., DAVIES, M.V., SCHERER, B.J., CHOI, S.-Y., HERSHEY, J.W.B., and KAUFMAN, R.J. (1993). Expression of a phosphorylation-resistant eukaryotic initiation factor 2α-subunit mitigates heat shock inhibition of protein synthe-sis. J. Biol. Chem. 268, 12946-12951.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12946-12951
    • Murtha-Riel, P.1    Davies, M.V.2    Scherer, B.J.3    Choi, S.-Y.4    Hershey, J.W.B.5    Kaufman, R.J.6
  • 97
    • 0029762971 scopus 로고    scopus 로고
    • Inhibition of translational initiation by activators of the glucose-regulated stress protein and heat shock protein stress response systems - Role of the interferon-inducible double-stranded RNA-activated eukaryotic initiation factor 2α kinase
    • BROSTROM, C.O., PROSTKO, C.R., KAUFMANN, R.J., and BROSTROM, M.A. (1996). Inhibition of translational initiation by activators of the glucose-regulated stress protein and heat shock protein stress response systems - role of the interferon-inducible double-stranded RNA-activated eukaryotic initiation factor 2α kinase. J. Biol. Chem. 271, 24995-25002.
    • (1996) J. Biol. Chem. , vol.271 , pp. 24995-25002
    • Brostrom, C.O.1    Prostko, C.R.2    Kaufmann, R.J.3    Brostrom, M.A.4
  • 98
    • 0023665208 scopus 로고
    • Phosphorylation of eukaryotic initiation factor 2 during physiological stresses which affect protein synthesis
    • SCORSONE, K.A., PANNIERS, R., ROWLANDS, A.G., and HENSHAW, E.C. (1987). Phosphorylation of eukaryotic initiation factor 2 during physiological stresses which affect protein synthesis. J. Biol. Chem. 262, 14538-14543.
    • (1987) J. Biol. Chem. , vol.262 , pp. 14538-14543
    • Scorsone, K.A.1    Panniers, R.2    Rowlands, A.G.3    Henshaw, E.C.4
  • 99
    • 0023125673 scopus 로고
    • Regulation of polypeptide chain initiation in Chinese hamster ovary cells with a temperature-sensitive leucyl-tRNA synthetase
    • CLEMENS, M.J., GALPINE, A., AUSTIN, S.A., PANNIERS, R., HENSHAW, E.C., DUNCAN, R., HERSHEY, J.W.B., and POLLARD, J.W. (1987). Regulation of polypeptide chain initiation in Chinese hamster ovary cells with a temperature-sensitive leucyl-tRNA synthetase. J. Biol. Chem. 262, 767-771.
    • (1987) J. Biol. Chem. , vol.262 , pp. 767-771
    • Clemens, M.J.1    Galpine, A.2    Austin, S.A.3    Panniers, R.4    Henshaw, E.C.5    Duncan, R.6    Hershey, J.W.B.7    Pollard, J.W.8
  • 100
    • 0023753058 scopus 로고
    • Physiological stresses inhibit guanine-nucleotide-exchange factor in Ehrlich cells
    • ROWLANDS, A.G., MONTINE, K.S., HENSHAW, E.C., and PANNIERS, R. (1988). Physiological stresses inhibit guanine-nucleotide-exchange factor in Ehrlich cells. Eur. J. Biochem. 175, 93-99.
    • (1988) Eur. J. Biochem. , vol.175 , pp. 93-99
    • Rowlands, A.G.1    Montine, K.S.2    Henshaw, E.C.3    Panniers, R.4
  • 101
    • 0025326163 scopus 로고
    • Calcium-dependent regulation of protein synthesis in intact mammalian cells
    • BROSTROM, C.O., and BROSTROM, M.A. (1990). Calcium-dependent regulation of protein synthesis in intact mammalian cells. Annu. Rev. Physiol. 52, 577-590.
    • (1990) Annu. Rev. Physiol. , vol.52 , pp. 577-590
    • Brostrom, C.O.1    Brostrom, M.A.2
  • 103
    • 0027729197 scopus 로고
    • Reversible phosphorylation of eukaryotic initiation factor 2α in response to endoplasmic reticular signaling
    • PROSTKO, C.R., BROSTROM, M.A., and BROSTROM, C.O. (1993). Reversible phosphorylation of eukaryotic initiation factor 2α in response to endoplasmic reticular signaling. Mol. Cell. Biochem. 127-128, 255-265.
    • (1993) Mol. Cell. Biochem. , vol.127-128 , pp. 255-265
    • Prostko, C.R.1    Brostrom, M.A.2    Brostrom, C.O.3
  • 104
    • 0028963278 scopus 로고
    • Independent signaling of grp78 gene transcription and phosphorylation of eukaryotic initiation factor 2α by the stressed endoplasmic reticulum
    • BROSTROM, M.A., PROSTKO, C.R., GMITTER, D., and BROSTROM, C.O. (1995). Independent signaling of grp78 gene transcription and phosphorylation of eukaryotic initiation factor 2α by the stressed endoplasmic reticulum. J. Biol. Chem. 270, 4127-1132.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4127-11132
    • Brostrom, M.A.1    Prostko, C.R.2    Gmitter, D.3    Brostrom, C.O.4
  • 105
    • 0028938425 scopus 로고
    • Activation of the double-stranded RNA-regulated protein kinase by depletion of endoplasmic reticular calcium stores
    • PROSTKO, C.R., DHOLAKIA, J.N., BROSTROM, M.A., and BROSTROM, C.O. (1995). Activation of the double-stranded RNA-regulated protein kinase by depletion of endoplasmic reticular calcium stores. J. Biol. Chem. 270, 6211-6215.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6211-6215
    • Prostko, C.R.1    Dholakia, J.N.2    Brostrom, M.A.3    Brostrom, C.O.4
  • 106
    • 0029067408 scopus 로고
    • Calcium depletion from the endoplasmic reticulum activates the double-stranded RNA-dependent protein kinase (PKR) to inhibit protein synthesis
    • SRIVASTAVA, S.P., DAVIES, M.V., and KAUFMAN, R.J. (1995). Calcium depletion from the endoplasmic reticulum activates the double-stranded RNA-dependent protein kinase (PKR) to inhibit protein synthesis. J. Biol. Chem. 270, 16619-16624.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16619-16624
    • Srivastava, S.P.1    Davies, M.V.2    Kaufman, R.J.3
  • 107
    • 0030066955 scopus 로고    scopus 로고
    • Chromosomal assignment of the gene encoding the human 58-kDa inhibitor (PRKRI) of the interferon-induced dsRNA-activated protein kinase to chromosome 13q32
    • KORTH, M.J., EDELHOFF, S., DISTECHE, C.M., and KATZE, M.G. (1996). Chromosomal assignment of the gene encoding the human 58-kDa inhibitor (PRKRI) of the interferon-induced dsRNA-activated protein kinase to chromosome 13q32. Genomics 31, 238-239.
    • (1996) Genomics , vol.31 , pp. 238-239
    • Korth, M.J.1    Edelhoff, S.2    Disteche, C.M.3    Katze, M.G.4
  • 109
    • 0028290902 scopus 로고
    • The interferon-induced double-stranded RNA-activated protein kinase induces apoptosis
    • LEE, S.B., and ESTEBAN, M. (1994). The interferon-induced double-stranded RNA-activated protein kinase induces apoptosis. Virology 199, 491-496.
    • (1994) Virology , vol.199 , pp. 491-496
    • Lee, S.B.1    Esteban, M.2
  • 110
    • 0029842883 scopus 로고    scopus 로고
    • Possible involvement of double-stranded RNA-activated protein kinase in cell death by influenza virus infection
    • TAKIZAWA, T., OHASHI, K., and NAKANISHI, Y. (1996). Possible involvement of double-stranded RNA-activated protein kinase in cell death by influenza virus infection. J. Virol. 70, 8128-8132.
    • (1996) J. Virol. , vol.70 , pp. 8128-8132
    • Takizawa, T.1    Ohashi, K.2    Nakanishi, Y.3
  • 113
    • 0029115903 scopus 로고
    • The interferon-inducible double-stranded RNA-activated protein kinase self-associates in vitro and in vivo
    • PATEL, R.C., STANTON, P., McMILLAN, N.M.J., WILLIAMS, B.R.G., and SEN, G.C. (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
  • 115
    • 0024433216 scopus 로고
    • Mechanism of interferon action: Activation of the human P1/eIF-2α protein kinase by individual reovirus s-class mRNAs: s1 mRNA is a potent activator relative to s4 mRNA
    • BISCHOFF, J.R., and SAMUEL, C.E. (1989). Mechanism of interferon action: activation of the human P1/eIF-2α protein kinase by individual reovirus s-class mRNAs: s1 mRNA is a potent activator relative to s4 mRNA. Virology 172, 106-115.
    • (1989) Virology , vol.172 , pp. 106-115
    • Bischoff, J.R.1    Samuel, C.E.2
  • 116
    • 0027931144 scopus 로고
    • Mechanism of interferon action. Translational control and the RNA-dependent protein kinase (PKR): Antagonists of PKR enhance the translational activity of mRNAs that include a 161 nucleotide region from reovirus S1 mRNA
    • HENRY, G.L., McCORMACK, S.J., THOMIS, D.C., and SAMUEL, C.E. (1994). Mechanism of interferon action. Translational control and the RNA-dependent protein kinase (PKR): antagonists of PKR enhance the translational activity of mRNAs that include a 161 nucleotide region from reovirus S1 mRNA. J. Biol. Regul. Homeost. Agents 8, 15-24.
    • (1994) J. Biol. Regul. Homeost. Agents , vol.8 , pp. 15-24
    • Henry, G.L.1    McCormack, S.J.2    Thomis, D.C.3    Samuel, C.E.4
  • 117
    • 0030013732 scopus 로고    scopus 로고
    • Paradoxical interactions between human delta hepatitis agent RNA and the cellular protein kinase PKR
    • ROBERTSON, H.D., MANCHE, L., and MATHEWS, M.B. (1996). Paradoxical interactions between human delta hepatitis agent RNA and the cellular protein kinase PKR. J. Virol. 70, 5611-5617.
    • (1996) J. Virol. , vol.70 , pp. 5611-5617
    • Robertson, H.D.1    Manche, L.2    Mathews, M.B.3
  • 119
    • 0029910938 scopus 로고    scopus 로고
    • Regulation of the double-stranded RNA-dependent protein kinase PKR by RNAs encoded by a repeated sequence in the Epstein-Barr virus genome
    • ELIA, A., LAING, K.G., SCHOFIELD, A., TILLERAY, V.J., and CLEMENS, M.J. (1996). Regulation of the double-stranded RNA-dependent protein kinase PKR by RNAs encoded by a repeated sequence in the Epstein-Barr virus genome. Nucleic Acids Res. 24, 4471-4478.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 4471-4478
    • Elia, A.1    Laing, K.G.2    Schofield, A.3    Tilleray, V.J.4    Clemens, M.J.5
  • 120
    • 0026909526 scopus 로고
    • The war against the interferon-induced dsRNA-activated protein kinase: Can viruses win?
    • KATZE, M.G. (1992). The war against the interferon-induced dsRNA-activated protein kinase: can viruses win? J. Interferon Res. 12, 241-248.
    • (1992) J. Interferon Res. , vol.12 , pp. 241-248
    • Katze, M.G.1
  • 122
    • 0023304374 scopus 로고
    • The adenovirus VAI RNA complexes with the p68 protein kinase to regulate its autophosphorylation and activity
    • KATZE, M.G., DECORATO, D., SAFER, B., GALABRU, J., and HOVANESSIAN, A.G. (1987). The adenovirus VAI RNA complexes with the p68 protein kinase to regulate its autophosphorylation and activity. EMBO J. 6, 689-697.
    • (1987) EMBO J. , vol.6 , pp. 689-697
    • Katze, M.G.1    Decorato, D.2    Safer, B.3    Galabru, J.4    Hovanessian, A.G.5
  • 123
    • 0025931571 scopus 로고
    • Adenovirus virus-associated RNA and translation control
    • MATHEWS, M.B., and SHENK, T. (1991). Adenovirus virus-associated RNA and translation control. J. Virol. 65, 5657-5662.
    • (1991) J. Virol. , vol.65 , pp. 5657-5662
    • Mathews, M.B.1    Shenk, T.2
  • 124
    • 0025361887 scopus 로고
    • Interaction of adenovirus VA RNA1 with the protein kinase DAI: Nonequivalence of binding and function
    • MELLITS, K.H., KOSTURA, M., and MATHEWS, M.B. (1990). Interaction of adenovirus VA RNA1 with the protein kinase DAI: nonequivalence of binding and function. Cell 61, 843-852.
    • (1990) Cell , vol.61 , pp. 843-852
    • Mellits, K.H.1    Kostura, M.2    Mathews, M.B.3
  • 125
    • 0027988099 scopus 로고
    • Structural features of adenovirus 2 virus-associated RNA required for binding to the protein kinase DAI
    • CLARKE, P.A., PE'ERY, T., MA, Y., and MATHEWS, M.B. (1994). Structural features of adenovirus 2 virus-associated RNA required for binding to the protein kinase DAI. Nucleic Acids Res. 22, 4364-4374.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4364-4374
    • Clarke, P.A.1    Pe'ery, T.2    Ma, Y.3    Mathews, M.B.4
  • 126
    • 0026511984 scopus 로고
    • Role of the apical stem in maintaining the structure and function of adenovirus virus-associated RNA
    • MELLITS, K.H., PE'EREY, T., and MATHEWS, M.B. (1992). Role of the apical stem in maintaining the structure and function of adenovirus virus-associated RNA. J. Virol. 66, 2369-2377.
    • (1992) J. Virol. , vol.66 , pp. 2369-2377
    • Mellits, K.H.1    Pe'erey, T.2    Mathews, M.B.3
  • 127
    • 0024078349 scopus 로고
    • Effects of mutations in stem and loop regions on the structure and function of adenovirus VA RNA1
    • MELLITS, K.H., and MATHEWS, M.B. (1988). Effects of mutations in stem and loop regions on the structure and function of adenovirus VA RNA1. EMBO J. 7, 2849-2859.
    • (1988) EMBO J. , vol.7 , pp. 2849-2859
    • Mellits, K.H.1    Mathews, M.B.2
  • 128
    • 0029903806 scopus 로고    scopus 로고
    • Secondary and tertiary structure in the central domain of adenovirus type 2 VA RNAI
    • MA, Y., and MATHEWS, M.B. (1996). Secondary and tertiary structure in the central domain of adenovirus type 2 VA RNAI. RNA 2, 937-955.
    • (1996) RNA , vol.2 , pp. 937-955
    • Ma, Y.1    Mathews, M.B.2
  • 129
    • 0028298638 scopus 로고
    • In vitro analysis of virus-associated RNA I (VAI RNA): Inhibition of the double-stranded RNA-activated protein kinase PKR by VAI RNA mutants correlates with the in vivo phenotype and the structural integrity of the central domain
    • GHADGE, G.D., MALHOTRA, P., FURTADO, M.R., DHAR, R., and THIMMAPAYA, B. (1994). In vitro analysis of virus-associated RNA I (VAI RNA): inhibition of the double-stranded RNA-activated protein kinase PKR by VAI RNA mutants correlates with the in vivo phenotype and the structural integrity of the central domain. J. Virol. 68, 4137-4151.
    • (1994) J. Virol. , vol.68 , pp. 4137-4151
    • Ghadge, G.D.1    Malhotra, P.2    Furtado, M.R.3    Dhar, R.4    Thimmapaya, B.5
  • 130
    • 0025228070 scopus 로고
    • Tat-responsive region RNA of human immunodeficiency virus 1 can prevent activation of the double-stranded-RNA-activated protein kinase
    • GUNNERY, S.A., RICE, A.P., ROBERTSON, H.D., and MATHEWS, M.B. (1990). Tat-responsive region RNA of human immunodeficiency virus 1 can prevent activation of the double-stranded-RNA-activated protein kinase. Proc. Natl. Acad. Sci. USA 87, 8687-8691.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 8687-8691
    • Gunnery, S.A.1    Rice, A.P.2    Robertson, H.D.3    Mathews, M.B.4
  • 131
    • 0025129434 scopus 로고
    • Removal of double-stranded contaminants from RNA transcripts: Synthesis of adenovirus VA RNA1 from a T7 vector
    • MELLITS, K.H., PE'ERY, T., MANCHE, L., ROBERTSON, H.D., and MATHEWS, M.B. (1990). Removal of double-stranded contaminants from RNA transcripts: synthesis of adenovirus VA RNA1 from a T7 vector. Nucleic Acids Res. 18, 5401-5406.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 5401-5406
    • Mellits, K.H.1    Pe'ery, T.2    Manche, L.3    Robertson, H.D.4    Mathews, M.B.5
  • 132
    • 0026085288 scopus 로고
    • The integrity of the stem structure of human immuondeficiency virus type 1 Tat-responsive sequence RNA is required for interaction with the interferon-induced 68,000-Mr protein kinase
    • ROY, S., AGY, M., HOVANESSIAN, A.G., SONENBERG, N., and KATZE, M.G. (1991). The integrity of the stem structure of human immuondeficiency virus type 1 Tat-responsive sequence RNA is required for interaction with the interferon-induced 68,000-Mr protein kinase. J. Virol. 65, 632-640.
    • (1991) J. Virol. , vol.65 , pp. 632-640
    • Roy, S.1    Agy, M.2    Hovanessian, A.G.3    Sonenberg, N.4    Katze, M.G.5
  • 135
    • 0028589116 scopus 로고
    • Proteins that interact with PKR
    • JAGUS, R., and GRAY, M.M. (1994). Proteins that interact with PKR. Biochimie 76, 779-791.
    • (1994) Biochimie , vol.76 , pp. 779-791
    • Jagus, R.1    Gray, M.M.2
  • 136
    • 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., NEUVEUT, C., CHUN, R.F., SMITH, S.M., SAMUEL, C.E., GATIGNOL, A., and JEANG, K-T. (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
  • 138
    • 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.Y., and KAUFMAN, R.J. (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.Y.A.1    Kaufman, R.J.2
  • 139
    • 0026701570 scopus 로고
    • Malignant transformation by a mutant of the IFN-inducible dsRNA-dependent protein kinase
    • KOROMILAS, A.E., ROY, S., BARBER, G.N., KATZE, M.G., and 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
  • 140
    • 0027396813 scopus 로고
    • Tumor suppressor function of the interferon-induced double-stranded RNA-activated protein kinase
    • MEURS, E., GALABRU, J., BARBER, G.N., KATZE, M.G., and HOVANESSIAN, A.G. (1993). Tumor suppressor function of the interferon-induced double-stranded RNA-activated protein kinase. Proc. Natl. Acad. Sci. USA 90, 232-236.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 232-236
    • Meurs, E.1    Galabru, J.2    Barber, G.N.3    Katze, M.G.4    Hovanessian, A.G.5
  • 141
    • 0026653870 scopus 로고
    • Identification of double-stranded RNA-binding domains in the interferon-induced double-stranded RNA-activated p68 kinase
    • FENG, G., CHONG, K., KUMAR, A., and WILLIAMS, B.R.G. (1992). Identification of double-stranded RNA-binding domains in the interferon-induced double-stranded RNA-activated p68 kinase. Proc. Natl. Acad. Sci. USA 89, 5447-5451.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 5447-5451
    • Feng, G.1    Chong, K.2    Kumar, A.3    Williams, B.R.G.4
  • 142
    • 0027323010 scopus 로고
    • Reversal of the dsRNA-induced inhibition of protein synthesis by an inactive mutant of the protein kinase PKR
    • SHARP, T.V., XIAO, Q., JEFFREY, I., GEWERT, D.R., and CLEMENS, M.J. (1993). Reversal of the dsRNA-induced inhibition of protein synthesis by an inactive mutant of the protein kinase PKR. Eur. J. Biochem. 214, 945-948.
    • (1993) Eur. J. Biochem. , vol.214 , pp. 945-948
    • Sharp, T.V.1    Xiao, Q.2    Jeffrey, I.3    Gewert, D.R.4    Clemens, M.J.5
  • 143
    • 0029013693 scopus 로고
    • Regulation of the interferon-inducible protein kinase PKR and (2′-5′)oligo(adenylate) synthetase by a catalytically inactive PKR mutant through competition for double-stranded RNA binding
    • SHARP, T.V., XIAO, Q., JUSTESEN, J., GEWERT, D.R., and CLEMENS, M.J. (1995). Regulation of the interferon-inducible protein kinase PKR and (2′-5′)oligo(adenylate) synthetase by a catalytically inactive PKR mutant through competition for double-stranded RNA binding. Eur. J. Biochem. 230, 97-103.
    • (1995) Eur. J. Biochem. , vol.230 , pp. 97-103
    • Sharp, T.V.1    Xiao, Q.2    Justesen, J.3    Gewert, D.R.4    Clemens, M.J.5
  • 144
    • 0029122270 scopus 로고
    • Molecular mechanisms responsible for malignant transformation by regulatory and catalytic domain variants of the interferon-induced enzyme RNA-dependent protein kinase
    • BARBER, G.N., JAGUS, R., MEURS, E.F., HOVANESSIAN, A.G., and KATZE, M.G. (1995). Molecular mechanisms responsible for malignant transformation by regulatory and catalytic domain variants of the interferon-induced enzyme RNA-dependent protein kinase. J. Biol. Chem. 270, 17423-17428.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17423-17428
    • Barber, G.N.1    Jagus, R.2    Meurs, E.F.3    Hovanessian, A.G.4    Katze, M.G.5
  • 145
    • 0029061555 scopus 로고
    • Mutants of the RNA-dependent protein kinase (PKR) lacking double-stranded RNA binding domain I can act as transdominant inhibitors and induce malignant transformation
    • BARBER, G.N., WAMBACH, M., THOMPSON, S., JAGUS, R., and KATZE, M.G. (1995). Mutants of the RNA-dependent protein kinase (PKR) lacking double-stranded RNA binding domain I can act as transdominant inhibitors and induce malignant transformation. Mol. Cell. Biol. 15, 3138-3146.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3138-3146
    • Barber, G.N.1    Wambach, M.2    Thompson, S.3    Jagus, R.4    Katze, M.G.5
  • 146
    • 0029968705 scopus 로고    scopus 로고
    • Initiation of protein synthesis in eukaryotic cells
    • PAIN, V.M. (1996). Initiation of protein synthesis in eukaryotic cells. Eur. J. Biochem. 236, 747-771.
    • (1996) Eur. J. Biochem. , vol.236 , pp. 747-771
    • Pain, V.M.1
  • 147
    • 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., ROMAND, P.R., and WEK, R.C. (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    Romand, P.R.2    Wek, R.C.3
  • 148
    • 0028332026 scopus 로고
    • Double-stranded RNA-dependent protein kinase activates transcription factor NF-κB by phosphorylating IκB
    • KUMAR, A., HAQUE, J., LACOSTE, J., HISCOTT, J., and WILIAMS, B.R.G. (1994). Double-stranded RNA-dependent protein kinase activates transcription factor NF-κB by phosphorylating IκB. Proc. Natl. Acad. Sci. USA 91, 6288-6292.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 6288-6292
    • Kumar, A.1    Haque, J.2    Lacoste, J.3    Hiscott, J.4    Wiliams, B.R.G.5
  • 151
    • 17444449609 scopus 로고    scopus 로고
    • Deficient cytokine signaling in mouse embryo fibroblasts with a targeted deletion in the PKR gene: Role of IRF-1 and NF-κB
    • KUMAR, A., YANG, Y.-L., FLATI, V., DER, S., KADEREIT, S., DEB, A., HAQUE, J., REIS, L., WEISSMANN, C., and WILLIAMS, B.R.G. (1997). Deficient cytokine signaling in mouse embryo fibroblasts with a targeted deletion in the PKR gene: role of IRF-1 and NF-κB. EMBO J. 16, 406-416.
    • (1997) EMBO J. , vol.16 , pp. 406-416
    • Kumar, A.1    Yang, Y.-L.2    Flati, V.3    Der, S.4    Kadereit, S.5    Deb, A.6    Haque, J.7    Reis, L.8    Weissmann, C.9    Williams, B.R.G.10
  • 152
    • 0028820772 scopus 로고
    • The interferon-inducible protein kinase PKR modulates the transcriptional activation of immunoglobulin kappa gene
    • KOROMILAS, A.E., CANTIN, C., CRAIG, A.W.B., JAGUS, R., HISCOTT, J., and SONENBERG, N. (1995). The interferon-inducible protein kinase PKR modulates the transcriptional activation of immunoglobulin kappa gene. J. Biol. Chem. 270, 25426-25434.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25426-25434
    • Koromilas, A.E.1    Cantin, C.2    Craig, A.W.B.3    Jagus, R.4    Hiscott, J.5    Sonenberg, N.6
  • 153
    • 0343852938 scopus 로고    scopus 로고
    • Physical association between STAT1 and the interferon-inducible protein kinase PKR and implications for interferon and double-stranded RNA signaling pathways
    • WONG, A.H.T., TAM, N.W.N., YANG, Y.L., CUDDIHY, A.R., LI, S.Y., KIRCHHOFF, S., HAUSER, H., DECKER, T., and KOROMILAS, A.E. (1997). Physical association between STAT1 and the interferon-inducible protein kinase PKR and implications for interferon and double-stranded RNA signaling pathways. EMBO J. 16, 1291-1304.
    • (1997) EMBO J. , vol.16 , pp. 1291-1304
    • Wong, A.H.T.1    Tam, N.W.N.2    Yang, Y.L.3    Cuddihy, A.R.4    Li, S.Y.5    Kirchhoff, S.6    Hauser, H.7    Decker, T.8    Koromilas, A.E.9
  • 155
    • 0030928832 scopus 로고    scopus 로고
    • The Tat protein of human immunodeficiency virus type 1 is a substrate and inhibitor of the interferon-induced, virally activated protein kinase, PKR
    • BRAND, S.R., KOBAYASHI, R., and MATHEWS, M.B. (1997). The Tat protein of human immunodeficiency virus type 1 is a substrate and inhibitor of the interferon-induced, virally activated protein kinase, PKR. J. Biol. Chem. 272, 8388-8395.
    • (1997) J. Biol. Chem. , vol.272 , pp. 8388-8395
    • Brand, S.R.1    Kobayashi, R.2    Mathews, M.B.3
  • 156
    • 0027420053 scopus 로고
    • Inhibition of the dsRNA-dependent protein kinase by a peptide derived from the human immunodeficiency virus type 1 Tat protein
    • JUDWARE, R., LI, J., and PETRYSHYN, R. (1993). Inhibition of the dsRNA-dependent protein kinase by a peptide derived from the human immunodeficiency virus type 1 Tat protein. J. Interferon Res. 13, 153-160.
    • (1993) J. Interferon Res. , vol.13 , pp. 153-160
    • Judware, R.1    Li, J.2    Petryshyn, R.3
  • 157
    • 0023194764 scopus 로고
    • Four different isoforms of interferon-induced 2′,5′-oligo(A) synthetase identified by immunoblotting in human cells
    • CHEBATH, J., BENECH, P., HOVANESSIAN, A., GALABRU, J., and REVEL, M. (1987). Four different isoforms of interferon-induced 2′,5′-oligo(A) synthetase identified by immunoblotting in human cells. J. Biol. Chem. 262, 3852-3857.
    • (1987) J. Biol. Chem. , vol.262 , pp. 3852-3857
    • Chebath, J.1    Benech, P.2    Hovanessian, A.3    Galabru, J.4    Revel, M.5
  • 158
    • 0028815704 scopus 로고
    • Regulation of the interferon-induced PKR: Can viruses cope?
    • KATZE, M. (1995). Regulation of the interferon-induced PKR: can viruses cope? Trends Microbiol. 3, 75-78.
    • (1995) Trends Microbiol. , vol.3 , pp. 75-78
    • Katze, M.1
  • 159
    • 0027308224 scopus 로고
    • The interferon-induced double-stranded RNA-activated human p68 protein kinase potently inhibits protein synthesis in cultured cells
    • LEE, S.B., MELKOVA, Z., YAN, W., WILLIAMS, B.R.G., HOVANESSIAN, A.G., and ESTEBAN, M. (1993). The interferon-induced double-stranded RNA-activated human p68 protein kinase potently inhibits protein synthesis in cultured cells. Virology 192, 380-385.
    • (1993) Virology , vol.192 , pp. 380-385
    • Lee, S.B.1    Melkova, Z.2    Yan, W.3    Williams, B.R.G.4    Hovanessian, A.G.5    Esteban, M.6
  • 160
    • 0026929934 scopus 로고
    • Constitutive expression of human double-stranded RNA-activated p68 kinase in murine cells mediates phosphorylation of eukaryotic initiation factor 2 and partial resistance to encephalomyocarditis virus growth
    • MEURS, E.F., WATANABE, Y., KADEREIT, S., BARBER, G.N., KATZE, M.G., CHONG, K., WILLIAMS, B.R.G., and HOVANESSIAN, A.G. (1992). Constitutive expression of human double-stranded RNA-activated p68 kinase in murine cells mediates phosphorylation of eukaryotic initiation factor 2 and partial resistance to encephalomyocarditis virus growth. J. Virol. 66, 5805-5814.
    • (1992) J. Virol. , vol.66 , pp. 5805-5814
    • Meurs, E.F.1    Watanabe, Y.2    Kadereit, S.3    Barber, G.N.4    Katze, M.G.5    Chong, K.6    Williams, B.R.G.7    Hovanessian, A.G.8
  • 161
    • 0029051672 scopus 로고
    • Involvement of the double-stranded-RNA-dependent kinase PKR in interferon expression and interferon-mediated antiviral activity
    • DER, S.D., and LAU, A.S. (1995). Involvement of the double-stranded-RNA-dependent kinase PKR in interferon expression and interferon-mediated antiviral activity. Proc. Natl. Acad. Sci. USA 92, 8841-8845.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8841-8845
    • Der, S.D.1    Lau, A.S.2
  • 162
    • 0024326946 scopus 로고
    • Complementation of adenovirus virus-associated RNA I gene deletion by expression of a mutant eukaryotic translation initiation factor
    • DAVIES, M.V., FURTADO, M., HERSHEY, J.W.B., THIMMAPPAYA, B., and KAUFMAN, R.J. (1989). Complementation of adenovirus virus-associated RNA I gene deletion by expression of a mutant eukaryotic translation initiation factor. Proc. Natl. Acad. Sci. USA 86, 9163-9167.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 9163-9167
    • Davies, M.V.1    Furtado, M.2    Hershey, J.W.B.3    Thimmappaya, B.4    Kaufman, R.J.5
  • 163
    • 0027157746 scopus 로고
    • The interferon-induced double-stranded RNA-activated human p68 protein kinase inhibits the replication of vaccinia virus
    • LEE, S.B., and ESTEBAN, M. (1993). The interferon-induced double-stranded RNA-activated human p68 protein kinase inhibits the replication of vaccinia virus. Virology 193, 1037-1041.
    • (1993) Virology , vol.193 , pp. 1037-1041
    • Lee, S.B.1    Esteban, M.2
  • 164
    • 0029996794 scopus 로고    scopus 로고
    • Simian virus 40 large-T bypasses the translational block imposed by the phosphorylation of eIF-2α
    • SWAMINATHAN, S., RAJAN, P., SAVINOVA, O., JAGUS, R., and THIMMAPAYA, B. (1996). Simian virus 40 large-T bypasses the translational block imposed by the phosphorylation of eIF-2α. Virology 219, 321-323.
    • (1996) Virology , vol.219 , pp. 321-323
    • Swaminathan, S.1    Rajan, P.2    Savinova, O.3    Jagus, R.4    Thimmapaya, B.5
  • 165
    • 0026485045 scopus 로고
    • Suppression with a difference
    • CLEMENS, M. (1992). Suppression with a difference. Nature 360, 210-211.
    • (1992) Nature , vol.360 , pp. 210-211
    • Clemens, M.1
  • 166
    • 0027178076 scopus 로고
    • Tumor-suppressor genes: News about the interferon connection
    • LENGYEL, P. (1993). Tumor-suppressor genes: news about the interferon connection. Proc. Natl. Acad. Sci. USA 90, 5893-5895.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5893-5895
    • Lengyel, P.1
  • 167
    • 0021684617 scopus 로고
    • Growth-related expression of a double-stranded RNA-dependent protein kinase in 3T3 cells
    • PETRYSHYN, R., CHEN, J.-J., and LONDON, I.M. (1984). Growth-related expression of a double-stranded RNA-dependent protein kinase in 3T3 cells. J. Biol. Chem. 259, 14736-14742.
    • (1984) J. Biol. Chem. , vol.259 , pp. 14736-14742
    • Petryshyn, R.1    Chen, J.-J.2    London, I.M.3
  • 168
    • 0023876398 scopus 로고
    • Detection of activated double-stranded RNA-dependent protein kinase in 3T3-F442A cells
    • PETRYSHYN, R., CHEN, J.-J., and LONDON, I.M. (1988). Detection of activated double-stranded RNA-dependent protein kinase in 3T3-F442A cells. Proc. Natl. Acad. Sci. USA 85, 1427-1431.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 1427-1431
    • Petryshyn, R.1    Chen, J.-J.2    London, I.M.3
  • 169
    • 0030052279 scopus 로고    scopus 로고
    • Effect of interferon on protein translation during growth stages of 3T3 cells
    • PETRYSHYN, R., CHEN, J.J., DANLEY, L., and MATTS, R.L. (1996). Effect of interferon on protein translation during growth stages of 3T3 cells. Arch. Biochem. Biophys. 326, 290-297.
    • (1996) Arch. Biochem. Biophys. , vol.326 , pp. 290-297
    • Petryshyn, R.1    Chen, J.J.2    Danley, L.3    Matts, R.L.4
  • 170
    • 0024844263 scopus 로고
    • Serum growth factors cause rapid stimulation of protein synthesis and dephosphorylation of eIF-2 in serum deprived Ehrlich cells
    • MONTINE, K.S., and HENSHAW, E.C. (1989). Serum growth factors cause rapid stimulation of protein synthesis and dephosphorylation of eIF-2 in serum deprived Ehrlich cells. Biochim. Biophys. Acta 1014, 282-288.
    • (1989) Biochim. Biophys. Acta , vol.1014 , pp. 282-288
    • Montine, K.S.1    Henshaw, E.C.2
  • 171
    • 0028852619 scopus 로고
    • Platelet-derived growth factor signal transduction through the interferon-inducible kinase PKR. Immediate early gene induction
    • MUNDSCHAU, L.J., and FALLER, D.V. (1995). Platelet-derived growth factor signal transduction through the interferon-inducible kinase PKR. Immediate early gene induction. J. Biol. Chem. 270, 3100-3106.
    • (1995) J. Biol. Chem. , vol.270 , pp. 3100-3106
    • Mundschau, L.J.1    Faller, D.V.2
  • 172
    • 0026481080 scopus 로고
    • Oncogenic ras induces an inhibitor of double-stranded RNA-dependent eukaryotic initiation factor 2α-kinase activation
    • MUNDSCHAU, L.J., and FALLER, D.V. (1992). Oncogenic ras induces an inhibitor of double-stranded RNA-dependent eukaryotic initiation factor 2α-kinase activation. J. Biol. Chem. 267, 23092-23098.
    • (1992) J. Biol. Chem. , vol.267 , pp. 23092-23098
    • Mundschau, L.J.1    Faller, D.V.2
  • 173
    • 0026702046 scopus 로고
    • Role of protein phosphorylation in activation of interferon-stimulated gene factors
    • BANDYOPADHYAY, S.K., and SEN, G.C. (1992). Role of protein phosphorylation in activation of interferon-stimulated gene factors. J. Biol. Chem. 267, 6389-6395.
    • (1992) J. Biol. Chem. , vol.267 , pp. 6389-6395
    • Bandyopadhyay, S.K.1    Sen, G.C.2
  • 174
    • 0028977912 scopus 로고
    • Activation of the double-stranded-RNA-activated protein kinase and induction of vascular cell adhesion molecule-1 by poly(I).poly(C) in endothelial cells
    • OFFERMANN, M.K., ZIMRING, J., MELLITS, K.H., HAGAN, M.K., SHAW, R., MEDFORD, R.M., MATHEWS, M.B., GOODBOURN, S., and JAGUS, R. (1995). Activation of the double-stranded-RNA-activated protein kinase and induction of vascular cell adhesion molecule-1 by poly(I).poly(C) in endothelial cells. Eur. J. Biochem. 232, 28-36.
    • (1995) Eur. J. Biochem. , vol.232 , pp. 28-36
    • Offermann, M.K.1    Zimring, J.2    Mellits, K.H.3    Hagan, M.K.4    Shaw, R.5    Medford, R.M.6    Mathews, M.B.7    Goodbourn, S.8    Jagus, R.9
  • 175
    • 0026069531 scopus 로고
    • Overlapping elements in the guanylate-binding protein gene promoter mediate transcriptional induction by alpha and gamma interferons
    • LEW, D.J., DECKER, T., STREHLOW, I., and DARNELL, J.E. (1991). Overlapping elements in the guanylate-binding protein gene promoter mediate transcriptional induction by alpha and gamma interferons. Mol. Cell. Biol. 11, 182-191.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 182-191
    • Lew, D.J.1    Decker, T.2    Strehlow, I.3    Darnell, J.E.4
  • 176
    • 0030187883 scopus 로고    scopus 로고
    • Mechanism of the induction of apoptosis by influenza virus infection
    • TAKIZAWA, T. (1996). Mechanism of the induction of apoptosis by influenza virus infection. Nippon-Rinsho 54, 1836-1841.
    • (1996) Nippon-Rinsho , vol.54 , pp. 1836-1841
    • Takizawa, T.1
  • 178
    • 0024379787 scopus 로고
    • Induction of human interferon gene expression is associated with a nuclear factor that interacts with the NF-kappaB site of the human immunodeficiency virus enhancer
    • HISCOTT, J., ALPER, D., COHEN, L., LEBLANC, J.F., SPORTZA, L., WONG, A., and XANTHOUDAKIS, S. (1989). Induction of human interferon gene expression is associated with a nuclear factor that interacts with the NF-kappaB site of the human immunodeficiency virus enhancer. J. Virol. 63, 2557-2566.
    • (1989) J. Virol. , vol.63 , pp. 2557-2566
    • Hiscott, J.1    Alper, D.2    Cohen, L.3    Leblanc, J.F.4    Sportza, L.5    Wong, A.6    Xanthoudakis, S.7
  • 179
    • 0024516201 scopus 로고
    • The involvement of NF-kappaB in β-interferon gene regulation reveals its role as widely inducible mediator of signal transduction
    • LENARDO, M.J., FAN, C-M., MANIATIS, T., and BALTIMORE, D. (1989) The involvement of NF-kappaB in β-interferon gene regulation reveals its role as widely inducible mediator of signal transduction. Cell 57, 287-294.
    • (1989) Cell , vol.57 , pp. 287-294
    • Lenardo, M.J.1    Fan, C.-M.2    Maniatis, T.3    Baltimore, D.4
  • 180
    • 0024443096 scopus 로고
    • Double-stranded DNA activates binding of NF-βB to an inducible element in the human beta-interferon promoter
    • VISVANATHAN, K.V., and GOODBOURN, S. (1989). Double-stranded DNA activates binding of NF-βB to an inducible element in the human beta-interferon promoter. EMBO J. 8, 1129-1138.
    • (1989) EMBO J. , vol.8 , pp. 1129-1138
    • Visvanathan, K.V.1    Goodbourn, S.2
  • 181
    • 0026500204 scopus 로고
    • Critical role of a common transcription factor, IRF-1, in the regulation of IFN-β and IFN-inducible genes
    • REIS, L.F.L., HARADA, H., WOLCHOK, J.D., TANIGUCHI, T., and VILCEK, J. (1992). Critical role of a common transcription factor, IRF-1, in the regulation of IFN-β and IFN-inducible genes. EMBO J. 11, 185-193.
    • (1992) EMBO J. , vol.11 , pp. 185-193
    • Reis, L.F.L.1    Harada, H.2    Wolchok, J.D.3    Taniguchi, T.4    Vilcek, J.5
  • 182
    • 0026529289 scopus 로고
    • Identification of novel factors that bind to the PRD I region of the human beta-interferon promoter
    • WHITESIDE, S.T., VISVANATHAN, K.V., and GOODBOURN, S. (1992). Identification of novel factors that bind to the PRD I region of the human beta-interferon promoter. Nucleic Acids Res. 20, 1531-1538.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 1531-1538
    • Whiteside, S.T.1    Visvanathan, K.V.2    Goodbourn, S.3
  • 183
    • 0028172154 scopus 로고
    • NF-kappa B-independent activation of beta-interferon expression in mouse F9 embryonal carcinoma cells
    • ELLIS, M.J., and GOODBOURN, S. (1994). NF-kappa B-independent activation of beta-interferon expression in mouse F9 embryonal carcinoma cells. Nucleic Acids Res. 22, 4489-4496.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4489-4496
    • Ellis, M.J.1    Goodbourn, S.2
  • 184
    • 0029609175 scopus 로고
    • Human PKR transfected into murine cells stimulates expression of genes under control of the HIV1 or HTLV-1 LTR
    • MEURS, E.F., McMILLAN, N., WILLIAMS, B.R.G., HOVANESSIAN, A.G., and SOUTHERN, P.J. (1995). Human PKR transfected into murine cells stimulates expression of genes under control of the HIV1 or HTLV-1 LTR. Virology 214, 653-659.
    • (1995) Virology , vol.214 , pp. 653-659
    • Meurs, E.F.1    McMillan, N.2    Williams, B.R.G.3    Hovanessian, A.G.4    Southern, P.J.5
  • 185
    • 0028804388 scopus 로고
    • Potential requirement of a functional double-stranded RNA-dependent protein kinase (PKR) for the tumoricidal activation of macrophages by lipopolysaccharide or IFN-αβ, but not IFN-gamma
    • GUSELLA, G.L., MUSSO, T., ROTTSCHAFER, S.E., PULKKI, K., and VARESIO, L. (1995). Potential requirement of a functional double-stranded RNA-dependent protein kinase (PKR) for the tumoricidal activation of macrophages by lipopolysaccharide or IFN-αβ, but not IFN-gamma. J. Immunol. 154, 345-354.
    • (1995) J. Immunol. , vol.154 , pp. 345-354
    • Gusella, G.L.1    Musso, T.2    Rottschafer, S.E.3    Pulkki, K.4    Varesio, L.5
  • 186
    • 0028978241 scopus 로고
    • Transcription stimulation of the Fas-encoding gene by nuclear factor for interleukin-6 expression upon influenza virus infection
    • WADA, N., MATSUMURA, M., OHBA, Y., KOBAYASHI, N., TAKIZAWA, T., and NAKANISHI, Y. (1995). Transcription stimulation of the Fas-encoding gene by nuclear factor for interleukin-6 expression upon influenza virus infection. J. Biol. Chem. 270, 18007-18012.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18007-18012
    • Wada, N.1    Matsumura, M.2    Ohba, Y.3    Kobayashi, N.4    Takizawa, T.5    Nakanishi, Y.6
  • 187
    • 0028799943 scopus 로고
    • Characterization of specific DNA-binding factors activated by double-stranded RNA as positive regulators of interferon α/β-stimulated genes
    • DALY, C, and REICH, N.C. (1995). Characterization of specific DNA-binding factors activated by double-stranded RNA as positive regulators of interferon α/β-stimulated genes. J. Biol. Chem. 270, 23739-23746.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23739-23746
    • Daly, C.1    Reich, N.C.2
  • 188
    • 0026677031 scopus 로고
    • Double-stranded RNA and interferon-α induce transcription through different molecular mechanisms
    • DECKER, T. (1992). Double-stranded RNA and interferon-α induce transcription through different molecular mechanisms. J. Interferon Res. 12, 445-448.
    • (1992) J. Interferon Res. , vol.12 , pp. 445-448
    • Decker, T.1
  • 189
    • 0029165054 scopus 로고
    • Transcriptional induction by double-stranded RNA is mediated by interferon-stimulated response elements without activation of interferon-stimulated gene factor 3
    • BANDYOPADHYAY, S.K., LEONARD, G.T., Jr., BANDYOPADHYAY, T., STARK, G.R., and SEN, G.C. (1995). Transcriptional induction by double-stranded RNA is mediated by interferon-stimulated response elements without activation of interferon-stimulated gene factor 3. J. Biol. Chem. 270, 19624-19629.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19624-19629
    • Bandyopadhyay, S.K.1    Leonard Jr., G.T.2    Bandyopadhyay, T.3    Stark, G.R.4    Sen, G.C.5
  • 190
    • 0029658189 scopus 로고    scopus 로고
    • Transfection of IFNα in human glioblastoma cells and tumorigenicity in association with induction of PKR and OAS gene expression
    • HE, J., OLSON, J.J., EKSTRAND, A.J., SERBANESCU, A., YANG, J., OFFERMANN, M.K., and JAMES, C.D. (1996). Transfection of IFNα in human glioblastoma cells and tumorigenicity in association with induction of PKR and OAS gene expression. J. Neurosurg. 85, 1085-1090.
    • (1996) J. Neurosurg. , vol.85 , pp. 1085-1090
    • He, J.1    Olson, J.J.2    Ekstrand, A.J.3    Serbanescu, A.4    Yang, J.5    Offermann, M.K.6    James, C.D.7
  • 191
    • 0028211253 scopus 로고
    • The 58kDa inhibitor of the interferon induced dsRNA activated protein kinase is a TPR protein with oncogenic properties
    • BARBER, G.N., THOMPSON, S., LEE, T.G., STROM, T., JAGUS, R., DARVEAU, A., and KATZE, M.G. (1994). The 58kDa inhibitor of the interferon induced dsRNA activated protein kinase is a TPR protein with oncogenic properties. Proc. Natl. Acad. Sci. USA 91, 4278-1282.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 4278-11282
    • Barber, G.N.1    Thompson, S.2    Lee, T.G.3    Strom, T.4    Jagus, R.5    Darveau, A.6    Katze, M.G.7
  • 192
    • 0029118217 scopus 로고
    • Abrogation of translation initiation factor eIF-2 phosphorylation causes malignant transformation of NIH 3T3 cells
    • DONZÉ, O., JAGUS, R., KOROMILAS, A.E., HERSHEY, J.W.B., and SONENBERG, N. (1995). Abrogation of translation initiation factor eIF-2 phosphorylation causes malignant transformation of NIH 3T3 cells. EMBO J. 14, 3828-3834.
    • (1995) EMBO J. , vol.14 , pp. 3828-3834
    • Donzé, O.1    Jagus, R.2    Koromilas, A.E.3    Hershey, J.W.B.4    Sonenberg, N.5
  • 193
    • 0028558943 scopus 로고
    • Endogenous inhibitors of the dsRNA-dependent eIF-2α protein kinase PKR in normal and ras-transformed cells
    • MUNDSCHAU, L.J., and FALLER, D.V. (1994). Endogenous inhibitors of the dsRNA-dependent eIF-2α protein kinase PKR in normal and ras-transformed cells. Biochimie 76, 792-800.
    • (1994) Biochimie , vol.76 , pp. 792-800
    • Mundschau, L.J.1    Faller, D.V.2
  • 194
    • 0029817929 scopus 로고    scopus 로고
    • Double-stranded RNA-dependent protein kinase mediates c-Myc suppression induced by type I interferons
    • RAVEH, T., HOVANESSIAN, A.G., MEURS, E.F., SONENBERG, N., and KIMCHI, A. (1996). Double-stranded RNA-dependent protein kinase mediates c-Myc suppression induced by type I interferons. J. Biol. Chem. 271, 25479-25484.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25479-25484
    • Raveh, T.1    Hovanessian, A.G.2    Meurs, E.F.3    Sonenberg, N.4    Kimchi, A.5
  • 195
    • 0024600978 scopus 로고
    • Activation of interferon-regulated, dsRNA-dependent enzymes by human immunodeficiency virus-1 leader RNA
    • SENGUPTA, D.N., and SILVERMAN, R.H. (1989). Activation of interferon-regulated, dsRNA-dependent enzymes by human immunodeficiency virus-1 leader RNA. Nucleic Acids Res. 17, 969-978.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 969-978
    • Sengupta, D.N.1    Silverman, R.H.2
  • 196
    • 0028897073 scopus 로고
    • Activation of the interferon-inducible enzymes, 2′,5′-oligoadenylate synthetase and PKR by human T-cell leukemia virus type I Rex-response element
    • MORDECHAI, E., KON, N., HENDERSON, E.E., and SUHADOLNIK, R.J. (1995). Activation of the interferon-inducible enzymes, 2′,5′-oligoadenylate synthetase and PKR by human T-cell leukemia virus type I Rex-response element. Virology 206, 913-922.
    • (1995) Virology , vol.206 , pp. 913-922
    • Mordechai, E.1    Kon, N.2    Henderson, E.E.3    Suhadolnik, R.J.4
  • 197
    • 0025320261 scopus 로고
    • Biosynthesis of reovirus-specified polypeptides: 2-aminopurine increases the efficiency of translation of reovirus si mRNA but not s4 mRNA in transfected cells
    • SAMUEL, C.E., and BRODY, M.S. (1990). Biosynthesis of reovirus-specified polypeptides: 2-aminopurine increases the efficiency of translation of reovirus si mRNA but not s4 mRNA in transfected cells. Virology 176, 106-113.
    • (1990) Virology , vol.176 , pp. 106-113
    • Samuel, C.E.1    Brody, M.S.2
  • 199
    • 0029841340 scopus 로고    scopus 로고
    • A herpesvirus genetic element which affects translation in the absence of the viral GADD34 function
    • MOHR, I., and GLUZMAN, Y. (1996). A herpesvirus genetic element which affects translation in the absence of the viral GADD34 function. EMBO J. 15, 4759-4766.
    • (1996) EMBO J. , vol.15 , pp. 4759-4766
    • Mohr, I.1    Gluzman, Y.2
  • 200
    • 0026442274 scopus 로고
    • Mechanism of interferon action: Autoregulation of RNA-dependent P1/eIF-2α protein kinase (PKR) expression in transfected mammalian cells
    • THOMIS, D.C., and SAMUEL, C.E. (1992). Mechanism of interferon action: autoregulation of RNA-dependent P1/eIF-2α protein kinase (PKR) expression in transfected mammalian cells. Proc. Natl. Acad. Sci. USA 89, 10837-10841.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10837-10841
    • Thomis, D.C.1    Samuel, C.E.2
  • 201
    • 0027140480 scopus 로고
    • Tumor suppression by RNA from the 3′ untranslated region of α-tropomyosin
    • RASTINEJAD, F., CONBOY, M.J., RANDO, T.A., and BLAU, H.M. (1993). Tumor suppression by RNA from the 3′ untranslated region of α-tropomyosin. Cell 75, 1107-1117.
    • (1993) Cell , vol.75 , pp. 1107-1117
    • Rastinejad, F.1    Conboy, M.J.2    Rando, T.A.3    Blau, H.M.4
  • 202
    • 0025087879 scopus 로고
    • Epstein-Barr virus gene expression in interferon-treated cells. Implications for the regulation of protein synthesis and the antiviral state
    • CLARKE, P.A., SHARP, N.A., ARRAND, J.R., and CLEMENS, MJ. (1990). Epstein-Barr virus gene expression in interferon-treated cells. Implications for the regulation of protein synthesis and the antiviral state. Biochim. Biophys. Acta 1050, 167-173.
    • (1990) Biochim. Biophys. Acta , vol.1050 , pp. 167-173
    • Clarke, P.A.1    Sharp, N.A.2    Arrand, J.R.3    Clemens, M.J.4
  • 203
    • 0029258928 scopus 로고
    • Keeping RNA happy
    • UHLENBECK, O.C. (1995). Keeping RNA happy. RNA 1, 4-6.
    • (1995) RNA , vol.1 , pp. 4-6
    • Uhlenbeck, O.C.1
  • 204
    • 0028961190 scopus 로고
    • Two functionally distinct RNA-binding motifs in the regulatory domain of the protein kinase DAI
    • GREEN, S.R., MANCHE, L., and MATHEWS, M.B. (1995). Two functionally distinct RNA-binding motifs in the regulatory domain of the protein kinase DAI. Mol. Cell. Biol. 15, 358-364.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 358-364
    • Green, S.R.1    Manche, L.2    Mathews, M.B.3
  • 205
    • 0030424349 scopus 로고    scopus 로고
    • Semliki Forest virus capsid protein inhibits the initiation of translation by upregulating the double-stranded RNA-activated protein kinase PKR
    • FAVRE, D., STUDER, E., and MICHEL, M.R. (1996). Semliki Forest virus capsid protein inhibits the initiation of translation by upregulating the double-stranded RNA-activated protein kinase PKR. Biosci. Rep. 16, 485-511.
    • (1996) Biosci. Rep. , vol.16 , pp. 485-511
    • Favre, D.1    Studer, E.2    Michel, M.R.3
  • 206
    • 0028247651 scopus 로고
    • Cellular inhibitors of the interferon-induced, dsRNA-activated protein kinase
    • LEE, T.G., and KATZE, M.G. (1994). Cellular inhibitors of the interferon-induced, dsRNA-activated protein kinase. Prog. Mol. Subcell. Biol. 14, 48-65.
    • (1994) Prog. Mol. Subcell. Biol. , vol.14 , pp. 48-65
    • Lee, T.G.1    Katze, M.G.2
  • 207
    • 0026787750 scopus 로고
    • Mechanism of action of a cellular inhibitor of the dsRNA-dependent protein kinase from 3T3-F442A cells
    • JUDWARE, R., and PETRYSHYN, R. (1992). Mechanism of action of a cellular inhibitor of the dsRNA-dependent protein kinase from 3T3-F442A cells. J. Biol. Chem. 267, 21685-21690.
    • (1992) J. Biol. Chem. , vol.267 , pp. 21685-21690
    • Judware, R.1    Petryshyn, R.2
  • 208
    • 0027949937 scopus 로고
    • The 58,000-dalton cellular inhibitor of the interferon-induced double-stranded RNA-activated protein kinase (PKR) is a member of the tetratricopeptide repeat family of proteins
    • LEE, T.G., TANG, N., THOMPSON, S., MILLER, J., and KATZE, M.G. (1994). The 58,000-dalton cellular inhibitor of the interferon-induced double-stranded RNA-activated protein kinase (PKR) is a member of the tetratricopeptide repeat family of proteins. Mol. Cell. Biol. 14, 2331-2342.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 2331-2342
    • Lee, T.G.1    Tang, N.2    Thompson, S.3    Miller, J.4    Katze, M.G.5
  • 209
    • 0020359577 scopus 로고
    • Regulation of double-stranded RNA-activated eukaryotic initiation factor 2alpha kinase by type 2 protein phosphatase in reticulocyte lysates
    • PETRYSHYN, R., LEVIN, D.H., and LONDON, I.M. (1982). Regulation of double-stranded RNA-activated eukaryotic initiation factor 2alpha kinase by type 2 protein phosphatase in reticulocyte lysates. Proc. Natl. Acad. Sci. USA 79, 6512-6516.
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 6512-6516
    • Petryshyn, R.1    Levin, D.H.2    London, I.M.3
  • 211
    • 0028362126 scopus 로고
    • Products of the porcine group C rotavirus NSP3 gene bind specifically to double-stranded RNA and inhibit activation of the interferon-induced protein kinase PKR
    • LANGLAND, J.O., PETTIFORD, S., JIANG, B., and JACOBS, B.L. (1994). Products of the porcine group C rotavirus NSP3 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.2    Jiang, B.3    Jacobs, B.L.4
  • 212
    • 0026537228 scopus 로고
    • The vaccinia virus K3L gene product potentiates translation by inhibiting double-stranded-RNA-activated protein kinase and phosphorylation of the alpha subunit of eukaryotic initiation factor 2
    • DAVIES, M.V., ELROY-STEIN, O., JAGUS, R., MOSS, B., and KAUFMAN, R.J. (1992). The vaccinia virus K3L gene product potentiates translation by inhibiting double-stranded-RNA-activated protein kinase and phosphorylation of the alpha subunit of eukaryotic initiation factor 2. J. Virol. 66, 1943-1950.
    • (1992) J. Virol. , vol.66 , pp. 1943-1950
    • Davies, M.V.1    Elroy-Stein, O.2    Jagus, R.3    Moss, B.4    Kaufman, R.J.5
  • 213
    • 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., CHANG, H.-W., JACOBS, B.L., and KAUFMAN, R.J. (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
  • 214
    • 0027163011 scopus 로고
    • Recombinant vaccinia virus K3L gene product prevents activation of double-stranded RNA-dependent, initiation factor 2α-specific protein kinase
    • CARROLL, K., ELROY-STEIN, O., MOSS, B., and JAGUS, R. (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
  • 215
    • 0028847292 scopus 로고
    • Binding of the influenza virus NS1 protein to double-standed RNA inhibits the activation of the protein kinase that phosphorylates the eIF-2 translation initiation factor
    • LU, Y., WAMBACH, M., KATZE, M.G., and KRUG, R.M. (1995). Binding of the influenza virus NS1 protein to double-standed RNA inhibits the activation of the protein kinase that phosphorylates the eIF-2 translation initiation factor. Virology 214, 222-228.
    • (1995) Virology , vol.214 , pp. 222-228
    • Lu, Y.1    Wambach, M.2    Katze, M.G.3    Krug, R.M.4
  • 216
    • 0028217897 scopus 로고
    • The la antigen inhibits the activation of the interferon-inducible protein kinase PKR by sequestering and unwinding double-stranded RNA
    • XIAO, Q., SHARP, T.V., JEFFREY, I.W., JAMES, M.C., PRUIJN, G.J.M., VAN VENROOIJ, W.J., and CLEMENS, M.J. (1994). The La antigen inhibits the activation of the interferon-inducible protein kinase PKR by sequestering and unwinding double-stranded RNA. Nucleic Acids Res. 22, 2512-2518.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 2512-2518
    • Xiao, Q.1    Sharp, T.V.2    Jeffrey, I.W.3    James, M.C.4    Pruijn, G.J.M.5    Van Venrooij, W.J.6    Clemens, M.J.7
  • 217
    • 0030017753 scopus 로고    scopus 로고
    • A eukaryotic translation initiation factor 2-associated 67 kDa glycoprotein partially reverses protein synthesis inhibition by activated double-stranded RNA-dependent protein kinase in intact cells
    • WU, S.Y., REHEMTULLA, A., GUPTA, N.K., and KAUFMAN, R.J. (1996). A eukaryotic translation initiation factor 2-associated 67 kDa glycoprotein partially reverses protein synthesis inhibition by activated double-stranded RNA-dependent protein kinase in intact cells. Biochemistry 35, 8275-8280.
    • (1996) Biochemistry , vol.35 , pp. 8275-8280
    • Wu, S.Y.1    Rehemtulla, A.2    Gupta, N.K.3    Kaufman, R.J.4
  • 218
    • 0031017382 scopus 로고    scopus 로고
    • The gamma1 34.5 protein of herpes simplex virus 1 complexes with protein phosphatase 1alpha to dephosphorylate the alpha subunit of the eukaryotic translation initiation factor 2 and preclude the shutoff of protein synthesis by double-stranded RNA-activated protein kinase
    • HE, B., GROSS, M., and ROIZMAN, B. (1997). The gamma1 34.5 protein of herpes simplex virus 1 complexes with protein phosphatase 1alpha to dephosphorylate the alpha subunit of the eukaryotic translation initiation factor 2 and preclude the shutoff of protein synthesis by double-stranded RNA-activated protein kinase. Proc. Natl. Acad. Sci. USA 94, 843-848.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 843-848
    • He, B.1    Gross, M.2    Roizman, B.3
  • 219
    • 0028604461 scopus 로고
    • Characterization of an interferon-induced 48-kD protein immunologically related to the double-stranded RNA-activated protein kinase PKR
    • KADEREIT, S., GALABRU, J., ROBERT, N., MEURS, E.F., and HOVANESSIAN, A.G. (1994). Characterization of an interferon-induced 48-kD protein immunologically related to the double-stranded RNA-activated protein kinase PKR. J. Interferon Res. 14, 251-257.
    • (1994) J. Interferon Res. , vol.14 , pp. 251-257
    • Kadereit, S.1    Galabru, J.2    Robert, N.3    Meurs, E.F.4    Hovanessian, A.G.5
  • 220
    • 0027361282 scopus 로고
    • Molecular cloning of two new interferon-induced, highly related nuclear phosphoproteins
    • KADEREIT, S., GEWERT, D.R., GALABRU, J., HOVANESSIAN, A.G., and MEURS, E.F. (1993). Molecular cloning of two new interferon-induced, highly related nuclear phosphoproteins. J. Biol. Chem. 268, 24432-24441.
    • (1993) J. Biol. Chem. , vol.268 , pp. 24432-24441
    • Kadereit, S.1    Gewert, D.R.2    Galabru, J.3    Hovanessian, A.G.4    Meurs, E.F.5
  • 221
    • 0343812093 scopus 로고    scopus 로고
    • The apoptosis pathway triggered by the interferon-induced protein kinase PKR requires the third basic domain, initiates upstream of Bc1-2, and involves ICE-like proteases
    • LEE, S.B., RODRIGUEZ, D., RODRIGUEZ, J.R., and ESTEBAN, M. (1997). The apoptosis pathway triggered by the interferon-induced protein kinase PKR requires the third basic domain, initiates upstream of Bc1-2, and involves ICE-like proteases. Virology 231, 81-88.
    • (1997) Virology , vol.231 , pp. 81-88
    • Lee, S.B.1    Rodriguez, D.2    Rodriguez, J.R.3    Esteban, M.4
  • 222
    • 0027324505 scopus 로고
    • Mammalian eukaryotic initiation factor 2α kinases functionally substitute for GCN2 protein kinase in the GCN4 translational control mechanism of yeast
    • DEVER, T.E., CHEN, J.-J., BARBER, G.N., CIGAN, A.M., FENG, L., DONAHUE, T.F., LONDON, I.M., KATZE, M.G., and HINNEBUSCH, A.G. (1993). Mammalian eukaryotic initiation factor 2α kinases functionally substitute for GCN2 protein kinase in the GCN4 translational control mechanism of yeast. Proc. Natl. Acad. Sci. USA 90, 4616-4620.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 4616-4620
    • Dever, T.E.1    Chen, J.-J.2    Barber, G.N.3    Cigan, A.M.4    Feng, L.5    Donahue, T.F.6    London, I.M.7    Katze, M.G.8    Hinnebusch, A.G.9
  • 223
    • 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., McCOTTER, M.D., HENRY, G.L., McCORMACK, S.J., THOMIS, D.C., and SAMUEL, C.E. (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
  • 224
    • 0025267438 scopus 로고
    • Control of the interferon-induced 68-kilodalton protein kinase by the HIV-1 tat gene product
    • ROY, S., KATZE, M.G., PARKIN, N.T., EDERY, I., HOVANESSIAN, A.G., and SONENBERG, N. (1990). Control of the interferon-induced 68-kilodalton protein kinase by the HIV-1 tat gene product. Science 247, 1216-1219.
    • (1990) Science , vol.247 , pp. 1216-1219
    • Roy, S.1    Katze, M.G.2    Parkin, N.T.3    Edery, I.4    Hovanessian, A.G.5    Sonenberg, N.6


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