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Volumn 10, Issue 12, 1996, Pages 1378-1387

The eIF-2α kinases and the control of protein synthesis

Author keywords

cell cycle; eIF 2 ; protein phosphorylation; protein serine kinase; translational control

Indexed keywords

HEME; INHIBITOR PROTEIN; INITIATION FACTOR; INITIATION FACTOR 2ALPHA; MESSENGER RNA; PROTEIN KINASE; SERINE; UNCLASSIFIED DRUG; PROTEIN KINASE R; PROTEIN SERINE THREONINE KINASE;

EID: 0030267336     PISSN: 08926638     EISSN: None     Source Type: Journal    
DOI: 10.1096/fasebj.10.12.8903508     Document Type: Review
Times cited : (257)

References (64)
  • 1
    • 0025832056 scopus 로고
    • Translational control in mammalian cells
    • Hershey, J. W. B. (1991) Translational control in mammalian cells. Annu. Rev. Biochem. 60, 717-755
    • (1991) Annu. Rev. Biochem. , vol.60 , pp. 717-755
    • Hershey, J.W.B.1
  • 2
    • 0026465921 scopus 로고
    • Prolein phosphorylation in translational control
    • Proud, C. G. (1992) Prolein phosphorylation in translational control. Curr. Top. Cell. Regul. 32,243-369
    • (1992) Curr. Top. Cell. Regul. , vol.32 , pp. 243-369
    • Proud, C.G.1
  • 3
    • 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
  • 4
    • 0028171125 scopus 로고
    • eIF-2 kinases: Regulators of general and gene-specific translation initiation
    • Wek, R. C. (1994) eIF-2 kinases: regulators of general and gene-specific translation initiation. Trends Biochem. Sci. 19,491-496
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 491-496
    • Wek, R.C.1
  • 5
    • 0028124985 scopus 로고
    • Control of gene expression at the level of translation initiation
    • Kaufman, R. J. (1994) Control of gene expression at the level of translation initiation. Curr. Opin. Biotechnology 5,550-557
    • (1994) Curr. Opin. Biotechnology , vol.5 , pp. 550-557
    • Kaufman, R.J.1
  • 6
    • 0028433524 scopus 로고
    • Regulation of eukaryolic protein synthesis by protein kinases that phosphorylate initiation factor eIF-2
    • Clemens, M. J. (1994) Regulation of eukaryolic protein synthesis by protein kinases that phosphorylate initiation factor eIF-2. Mol. Biol. Rep. 19, 201-210
    • (1994) Mol. Biol. Rep. , vol.19 , pp. 201-210
    • Clemens, M.J.1
  • 7
    • 0000257134 scopus 로고
    • Translational regulation in reticulocytes. the role of heme-regulated eIF-2α kinase
    • Ilan, J., ed Plenum, New York
    • Chen, J. J. (1993) Translational regulation in reticulocytes. The role of heme-regulated eIF-2α kinase. In Translational Regulation of Gene Expression 2 (Ilan, J., ed) pp. 349-372, Plenum, New York
    • (1993) Translational Regulation of Gene Expression , vol.2 , pp. 349-372
    • Chen, J.J.1
  • 8
    • 0028935374 scopus 로고
    • Regulation of protein synthesis by heme-regulated eIF-2α kinase
    • Chen, J. J., and London, I. M. (1995) Regulation of protein synthesis by heme-regulated eIF-2α kinase. Trends Biochem. Sci. 20, 105-108
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 105-108
    • Chen, J.J.1    London, I.M.2
  • 9
    • 0025931571 scopus 로고
    • Adenovirus virus-associated RNA and translational control
    • Mathews, M. B., and Shenk, T. (1991) Adenovirus virus-associated RNA and translational control. J. Virol. 65, 5657-5662
    • (1991) J. Virol. , vol.65 , pp. 5657-5662
    • Mathews, M.B.1    Shenk, T.2
  • 10
    • 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
  • 11
    • 0027490295 scopus 로고
    • Gene-specific translational control of the yeast GCN4 gene by phosphorylation of eukaryotic initiation factor 2
    • Hinnebuch, A. G. (1993) Gene-specific translational control of the yeast GCN4 gene by phosphorylation of eukaryotic initiation factor 2. Mol. Microbiol. 10,215-223
    • (1993) Mol. Microbiol. , vol.10 , pp. 215-223
    • Hinnebuch, A.G.1
  • 12
    • 0028151657 scopus 로고
    • Translational control of GCN4: An in vivo barometer of initiation-factor activity
    • Hinnebusch, A. G. (1994) Translational control of GCN4: an in vivo barometer of initiation-factor activity. Trends Biochem. Sci. 19,409-414
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 409-414
    • Hinnebusch, A.G.1
  • 13
    • 0027171069 scopus 로고
    • Translation of the yeast transcriptional activator GCN4 is stimulated by purine limitation: Implications for activation of the protein kinase GCN2
    • Rolfes, R. J., and Hinnebusch, A. G. (1993) Translation of the yeast transcriptional activator GCN4 is stimulated by purine limitation: Implications for activation of the protein kinase GCN2. Mol. Cell. Biol. 13, 5099-5111
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 5099-5111
    • Rolfes, R.J.1    Hinnebusch, A.G.2
  • 14
    • 0028582139 scopus 로고
    • The guanine nucleotide exchange factor, eIF-2B
    • Price, N., and Proud, C. G. (1994) The guanine nucleotide exchange factor, eIF-2B. Biochimie 76, 748-760
    • (1994) Biochimie , vol.76 , pp. 748-760
    • Price, N.1    Proud, C.G.2
  • 15
    • 0029020282 scopus 로고
    • The eukaryotic protein kinase superfamily: Kinase (catalytic) domain structure and classification
    • Hanks, S. K., and Hunter, T. (1995) The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification. FASEB J. 9, 576-596
    • (1995) FASEB J. , vol.9 , pp. 576-596
    • Hanks, S.K.1    Hunter, T.2
  • 16
    • 0029078852 scopus 로고
    • Functional characterization of the RMA-binding domain and motif of the double-stranded RNA-dependenl 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 RMA-binding domain and motif of the double-stranded RNA-dependenl 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
  • 17
    • 0025779365 scopus 로고
    • Cloning of the cDNA of the heme-regulated eukaryotic initiation factor 2α(eIF-2α) kinase of rabbit reticulocytes: Homology to yeast GCN2 protein kinase and human double-stranded-RNA-dependent eIF-2α kinase
    • Chen, J. J., Throop, M. S., Gehrke, L., Kuo, I., Pal, J. K., Brodsky, M., and London, I. M. (1991) Cloning of the cDNA of the heme-regulated eukaryotic initiation factor 2α(eIF-2α) kinase of rabbit reticulocytes: Homology to yeast GCN2 protein kinase and human double-stranded-RNA-dependent eIF-2α kinase. Proc. Nail. Acad. Sci. USA 88, 7729-7733
    • (1991) Proc. Nail. Acad. Sci. USA , vol.88 , pp. 7729-7733
    • Chen, J.J.1    Throop, M.S.2    Gehrke, L.3    Kuo, I.4    Pal, J.K.5    Brodsky, M.6    London, I.M.7
  • 18
    • 0028245588 scopus 로고
    • Cloning and characterization of cDNA encoding rat hemin-sensitive initiation factor2α (eIF-2α) kinase
    • Mellor, H., Flowers, K. M., Kimball, S. R., and Jefferson, L. S. (1994) Cloning and characterization of cDNA encoding rat hemin-sensitive initiation factor2α (eIF-2α) kinase J. Biol. Chem. 269,10201-10204
    • (1994) J. Biol. Chem. , vol.269 , pp. 10201-10204
    • Mellor, H.1    Flowers, K.M.2    Kimball, S.R.3    Jefferson, L.S.4
  • 19
    • 0027405813 scopus 로고
    • Regulation by heme of mitochondria! protein transport through a conserved amino acid motif
    • Lathrop, J. T., and Timko, M. P. (1993) Regulation by heme of mitochondria! protein transport through a conserved amino acid motif. Science 259, 522-525
    • (1993) Science , vol.259 , pp. 522-525
    • Lathrop, J.T.1    Timko, M.P.2
  • 20
    • 0028821439 scopus 로고
    • Heme binds to a short sequence that serves a regulatory function in diverse proteins
    • Zhang, L., and Guarente, L. (1995) Heme binds to a short sequence that serves a regulatory function in diverse proteins. EMBO J. 14, 313-320
    • (1995) EMBO J. , vol.14 , pp. 313-320
    • Zhang, L.1    Guarente, L.2
  • 21
    • 0025298202 scopus 로고
    • Molecular cloning and characterization of the human double-stranded RNA-activated protein kinase induced by interferon
    • Meurs, E., Chong, K., Calabru, 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    Calabru, J.3    Thomas, N.S.B.4    Kerr, I.M.5    Williams, B.R.G.6    Hovanessian, A.G.7
  • 22
    • 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
  • 23
    • 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 Johnston, D S. (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    Johnston, D.S.5
  • 24
    • 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 Paslore, 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    Paslore, A.5
  • 25
    • 0021066891 scopus 로고
    • Activation of the heme-stabilized translational inhibitor of reliculocyte lysales by calcium ions and phospholipid
    • de Haro, C., de Herreros, A. G., and Ochoa, S. (1983) Activation of the heme-stabilized translational inhibitor of reliculocyte lysales by calcium ions and phospholipid. Proc. Natl. Acad. Sci. USA 80,6843-6847
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 6843-6847
    • De Haro, C.1    De Herreros, A.G.2    Ochoa, S.3
  • 26
    • 0021854747 scopus 로고
    • Mechanism of activation of the heme-stabilized Iranslational inhibitorof reticulocyte lysates by calcium ions and phospholipid
    • de Herreros, A. G., de Haro, C., and Ochoa, S. (1985) Mechanism of activation of the heme-stabilized Iranslational inhibitorof reticulocyte lysates by calcium ions and phospholipid. Proc. Natl. Acad. Sci. USA 82, 3119-3123
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 3119-3123
    • De Herreros, A.G.1    De Haro, C.2    Ochoa, S.3
  • 27
    • 0021803231 scopus 로고
    • Studies on the activation of the heme-stabilized translational inhibitor of reticulocyte lysates by oxidized glutathione and NADPH depletion
    • Palomo, C., Vicente, O., Sierra, J. M., and Ochoa, S. (1985) Studies on the activation of the heme-stabilized translational inhibitor of reticulocyte lysates by oxidized glutathione and NADPH depletion. Arch. Biochem. Biophys. 239,497-507
    • (1985) Arch. Biochem. Biophys. , vol.239 , pp. 497-507
    • Palomo, C.1    Vicente, O.2    Sierra, J.M.3    Ochoa, S.4
  • 28
    • 0026778841 scopus 로고
    • Interactions of the heme-regulaled eIF-2α kinase with heat shock proteins in rabbit reticulocyle lysates
    • Malls, R. L, Xu, Z., Pal, J. K., and Chen, J. J. (1992) Interactions of the heme-regulaled eIF-2α kinase with heat shock proteins in rabbit reticulocyle lysates. J. Biol. Chem. 267, 18160-18167
    • (1992) J. Biol. Chem. , vol.267 , pp. 18160-18167
    • Malls, R.L.1    Xu, Z.2    Pal, J.K.3    Chen, J.J.4
  • 29
    • 0026725775 scopus 로고
    • Regulation of heme-controlled eukaryotic polypeptide chain initiation factor 2α-subunit kinase of reticulocyte lysales
    • Méndez, R., Moreno, A., and de Haro, C. (1992) Regulation of heme-controlled eukaryotic polypeptide chain initiation factor 2α-subunit kinase of reticulocyte lysales. J. Biol. Chem. 267,11500-11507
    • (1992) J. Biol. Chem. , vol.267 , pp. 11500-11507
    • Méndez, R.1    Moreno, A.2    De Haro, C.3
  • 30
    • 0028108282 scopus 로고
    • Casein kinase II is implicated in the regulation of heme-controlled translational inhibitor of retieulocyte lysales
    • Méndez, R., and de Haro, C. (1994) Casein kinase II is implicated in the regulation of heme-controlled translational inhibitor of retieulocyte lysales. J. Biol. Chem. 269,6170-6176
    • (1994) J. Biol. Chem. , vol.269 , pp. 6170-6176
    • Méndez, R.1    De Haro, C.2
  • 31
    • 0027451956 scopus 로고
    • The role of heat shock proteins in regulating the function, folding, and trafficking of the glucocorticoid receptor
    • Prall, W. B. (1993) The role of heat shock proteins in regulating the function, folding, and trafficking of the glucocorticoid receptor. J. Biol. Chem. 268, 21455-21458
    • (1993) J. Biol. Chem. , vol.268 , pp. 21455-21458
    • Prall, W.B.1
  • 32
    • 0025965045 scopus 로고
    • Amino acid micro-sequencing of internal tryptic peptides of heme-regulated eukaryotic initiation factor 2α subunit kinase: Homology to prolein kinases
    • Chen, J. J., Pal, J. K., Pelryshyn, R., Kuo, L, Yang, J. M., Throop, M.S., Gehrke, L., and London, I. M. (1991) Amino acid micro-sequencing of internal tryptic peptides of heme-regulated eukaryotic initiation factor 2α subunit kinase: Homology to prolein kinases. Proc. Natl. Acad. Sci. USA 88, 315-319
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 315-319
    • Chen, J.J.1    Pal, J.K.2    Pelryshyn, R.3    Kuo, L.4    Yang, J.M.5    Throop, M.S.6    Gehrke, L.7    London, I.M.8
  • 33
    • 0027282654 scopus 로고
    • Denaturared proteins inhibit translation in hemin-supplemented rabbit reticulocyte lysates by inducing the activation of the heme-regulated eIF-2α kinase
    • Matts, R. L., Hurst, R., and Xu, Z. (1993) Denaturared proteins inhibit translation in hemin-supplemented rabbit reticulocyte lysates by inducing the activation of the heme-regulated eIF-2α kinase. Biochemistry 32, 7323-7328
    • (1993) Biochemistry , vol.32 , pp. 7323-7328
    • Matts, R.L.1    Hurst, R.2    Xu, Z.3
  • 34
    • 0028070415 scopus 로고
    • Control of protein synthesis by hemin. Purification of a rabbit reticulocyte hsp70 and characterization of its regulation of the activation of the hemin-controlled eIF-2(α) kinase
    • Gross, M., Olin, A., Hessefort, S., and Bender, S. (1994) Control of protein synthesis by hemin. Purification of a rabbit reticulocyte hsp70 and characterization of its regulation of the activation of the hemin-controlled eIF-2(α) kinase. J Biol. Chem. 269, 22738-22748
    • (1994) J Biol. Chem. , vol.269 , pp. 22738-22748
    • Gross, M.1    Olin, A.2    Hessefort, S.3    Bender, S.4
  • 35
    • 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
  • 36
    • 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
  • 37
    • 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
  • 38
    • 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 Hinnebuch, 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    Hinnebuch, A.G.5
  • 40
    • 0027943267 scopus 로고
    • Activation of the double-stranded RNA (dsRNA)-aclivated human protein kinase in vivo in the absence of its dsRNA binding domain
    • Lee, S. B., Green, S. R., Malhews, M. B., and Esteban, M. (1994) Activation of the double-stranded RNA (dsRNA)-aclivated 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    Malhews, M.B.3    Esteban, M.4
  • 41
    • 0029039746 scopus 로고
    • Mechanism of Interferon action: Characterization of the intermolecular autophosphoryation of PKR, the interferon inducible, RNA-dependent protein kinase
    • Thomis, D. C., and Samuel, C. E. (1995) Mechanism of Interferon action: Characterization of the intermolecular autophosphoryation of PKR, the interferon inducible, RNA-dependent protein kinase. J. Virot. 69,5195-5198
    • (1995) J. Virot. , vol.69 , pp. 5195-5198
    • Thomis, D.C.1    Samuel, C.E.2
  • 42
    • 0027396813 scopus 로고
    • Tumor suppressor function in the interferon-induced double-stranded RNA-activated protein kinase
    • Meurs, E. F., Galabru, J., Barber, G. N., Katze, M. G., and Hovanessian, A. G. (1993) Tumor suppressor function in 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.F.1    Galabru, J.2    Barber, G.N.3    Katze, M.G.4    Hovanessian, A.G.5
  • 43
    • 0029006391 scopus 로고
    • The histidyl-lRNA synlhetaserelated sequence in the eIF-2α protein kinase GCN2 interacts with tRNA and is required for activation in response to starvation for different amino acids
    • Wek, S. A., Zhu, S., and Wek, R. C. (1995) The histidyl-lRNA synlhetaserelated sequence in the eIF-2α protein kinase GCN2 interacts with tRNA and is required for activation in response to starvation for different amino acids. Mol. Cell. Biol. 15,4497-4506
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4497-4506
    • Wek, S.A.1    Zhu, S.2    Wek, R.C.3
  • 44
    • 0029001571 scopus 로고
    • GCN20, a novel ATP binding cassette protein, and GCN1 reside in acomplex that mediates activation of the eIF-2α kinase GCN2 in amino acid-starved cells
    • Vázquez de Aldana, C. R., Marton, M. J., and Hinnebusch, A. G. (1995) GCN20, a novel ATP binding cassette protein, and GCN1 reside in acomplex that mediates activation of the eIF-2α kinase GCN2 in amino acid-starved cells. EMBO J. 14, 3184-3199
    • (1995) EMBO J. , vol.14 , pp. 3184-3199
    • Vázquez de Aldana, C.R.1    Marton, M.J.2    Hinnebusch, A.G.3
  • 46
    • 0027480747 scopus 로고
    • Purification and characterization of an initiation-factor-2 kinase from uninduced mouse erythroleukaemia cells
    • Mellor, H., Price, N. T., Oldfield, S., Sarre, T. F., and Proud, C. G. (1993) Purification and characterization of an initiation-factor-2 kinase from uninduced mouse erythroleukaemia cells. Eur. J. Biochem. 211,529-538
    • (1993) Eur. J. Biochem. , vol.211 , pp. 529-538
    • Mellor, H.1    Price, N.T.2    Oldfield, S.3    Sarre, T.F.4    Proud, C.G.5
  • 47
    • 0027258638 scopus 로고
    • Purification and characterization of eukaryotic initiation factor (eIF)-2α kinases from Ehrlich ascites tumor cells
    • Olmsted, E. A., O'Brien, L, Henshaw, E. C., and Panniers, R. (1993) Purification and characterization of eukaryotic initiation factor (eIF)-2α kinases from Ehrlich ascites tumor cells. J. Biol. Chem. 268,12552-12559
    • (1993) J. Biol. Chem. , vol.268 , pp. 12552-12559
    • Olmsted, E.A.1    O'Brien, L.2    Henshaw, E.C.3    Panniers, R.4
  • 48
    • 0028815704 scopus 로고
    • Regulation of the interferon-induced PKR: Can viruses cope?
    • Katze, M. G. (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.G.1
  • 49
    • 0026787750 scopus 로고
    • Mechanism of action of a cellular inhibitor of the dsRNA-dependent protein kinase from 3T3-442A cells
    • Judware, R., and Petryshyn, R. (1992) Mechanism of action of a cellular inhibitor of the dsRNA-dependent protein kinase from 3T3-442A cells. J. Biol. Chem. 267,21685-21690
    • (1992) J. Biol. Chem. , vol.267 , pp. 21685-21690
    • Judware, R.1    Petryshyn, R.2
  • 50
    • 0026010912 scopus 로고
    • Activation of the double-stranded RNA-dependent eIF-2αt kinase by cellular RNA from 3T3-F442A cells
    • Li, J., and Petryshyn, R. A. (1991) Activation of the double-stranded RNA-dependent eIF-2αt kinase by cellular RNA from 3T3-F442A cells. Eur. J. Biochem. 195,41-48
    • (1991) Eur. J. Biochem. , vol.195 , pp. 41-48
    • Li, J.1    Petryshyn, R.A.2
  • 51
    • 0029093904 scopus 로고
    • Interruption of myogenesis by transforming growth factor βl or EGTA inhibits expression and activity of the myogenic-associated (2′,-5′) oligoadenylate synthetase and PKR
    • Salzberg, S., Mandelbaum, M., Zalcberg, M., and Schainberg, A. (1995) Interruption of myogenesis by transforming growth factor βl or EGTA inhibits expression and activity of the myogenic-associated (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    Schainberg, A.4
  • 52
    • 0026701570 scopus 로고
    • Malignant transformation of 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 of 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
  • 53
    • 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
  • 54
    • 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
  • 55
    • 0028211253 scopus 로고
    • The 58-kilodalton inhibitor of the interferon-induced double-stranded RNA-activaled protein kinase is a tetralricopeptide repeat protein with oncogenic properties
    • Barber, G. N., Thompson, S., Lee, T. G., Strom, T., Jagus, R., Darveau, A., and Katze, M. G. (1994) The 58-kilodalton inhibitor of the interferon-induced double-stranded RNA-activaled protein kinase is a tetralricopeptide repeat protein with oncogenic properties. Proc. Natl. Acad. Sci. USA 91,4278-4282
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 4278-4282
    • Barber, G.N.1    Thompson, S.2    Lee, T.G.3    Strom, T.4    Jagus, R.5    Darveau, A.6    Katze, M.G.7
  • 56
    • 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
  • 58
    • 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
  • 59
    • 0027966119 scopus 로고
    • Interleukin 3 stimulates protein synthesis by regulating doble-stranded RNA-dependent protein kinase
    • Ito, T., Jagus, R., and May, W. S. (1994) Interleukin 3 stimulates protein synthesis by regulating doble-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
  • 60
    • 0028332026 scopus 로고
    • Double-stranded RNA-dependent protein kinase activates transcription factor NF-KB by phosphorylaling IκB
    • Kumar, A., Haque, J., Lacoste, J., Hiscott, J., and Williams, B. R. G. (1994) Double-stranded RNA-dependent protein kinase activates transcription factor NF-KB by phosphorylaling 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    Williams, B.R.G.5
  • 61
    • 0025266685 scopus 로고
    • Activation in vitro of NF-κB by phosphorylation of its inhibitor IκB
    • Ghosh, S., and Baltimore, D. (1990) Activation in vitro of NF-κB by phosphorylation of its inhibitor IκB. Nature (London) 344,678-682
    • (1990) Nature (London) , vol.344 , pp. 678-682
    • Ghosh, S.1    Baltimore, D.2
  • 63
    • 0028820772 scopus 로고
    • The interferon-inducible protein kinase PKR modulates the transcriptional activation of immunoglobulin K gene
    • Koromilas, A. E., Cantin, C., Craig, A. W. B., Jagus, R., Hiscolt, J., and Sonenberg, N. (1995) The interferon-inducible protein kinase PKR modulates the transcriptional activation of immunoglobulin K 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    Hiscolt, J.5    Sonenberg, N.6
  • 64
    • 0028559530 scopus 로고
    • Binding of eukaryotic initiation factor-2 and trans-acting factors to the 5′-untranslaled region of encephalomyocarditis virus RNA
    • Scheper, G. C., Voorma, H. O., and Thomas, A. A. M. (1994) Binding of eukaryotic initiation factor-2 and trans-acting factors to the 5′-untranslaled region of encephalomyocarditis virus RNA. Biochimie 76, 801-809
    • (1994) Biochimie , vol.76 , pp. 801-809
    • Scheper, G.C.1    Voorma, H.O.2    Thomas, A.A.M.3


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