메뉴 건너뛰기




Volumn 18, Issue 12, 1998, Pages 7499-7509

Identification and characterization of pancreatic eukaryotic initiation factor 2 α-subunit kinase, PEK, involved in translational control

Author keywords

[No Author keywords available]

Indexed keywords

INITIATION FACTOR 2; MESSENGER RNA; PROTEIN KINASE; PROTEIN SUBUNIT;

EID: 0031755020     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/mcb.18.12.7499     Document Type: Article
Times cited : (698)

References (53)
  • 1
    • 0026085424 scopus 로고
    • Suppression of ribosomal reinitiation at upstream open reading frames in amino acid-starved cells forms the basis of GCN4 translational control
    • Abastado, J. P., P. F. Miller, B. M. Jackson, and A. G. Hinnebusch. 1991. Suppression of ribosomal reinitiation at upstream open reading frames in amino acid-starved cells forms the basis of GCN4 translational control. Mol. Cell. Biol. 11:486-496.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 486-496
    • Abastado, J.P.1    Miller, P.F.2    Jackson, B.M.3    Hinnebusch, A.G.4
  • 2
    • 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., R. Jagus, E. F. Meurs, A. G. Hovanessian, and M. G. Katze. 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
  • 3
    • 0003043563 scopus 로고
    • Islets of langerhans: Morphology and its implications
    • C. R. Kahn and G. C. Weir (ed.), Lea & Febiger, Piladelphia, Pa
    • Bonner-Weir, S., and F. E. Smith. 1994. Islets of langerhans: morphology and its implications, p. 15-28. In C. R. Kahn and G. C. Weir (ed.), Joslin's diabetes mellitus, 13th ed. Lea & Febiger, Piladelphia, Pa.
    • (1994) Joslin's Diabetes Mellitus, 13th Ed. , pp. 15-28
    • Bonner-Weir, S.1    Smith, F.E.2
  • 4
    • 0000615498 scopus 로고
    • Plasmid vectors carrying the replication origin of filamentous single-stranded phages
    • J. K. Setlow and A. Hollaender (ed.), Plenum Press, New York, N.Y.
    • Cesareni, G., and J. Murray. 1987. Plasmid vectors carrying the replication origin of filamentous single-stranded phages, p. 135-154. In J. K. Setlow and A. Hollaender (ed.), Genetic engineering: principles and methods, vol. 9. Plenum Press, New York, N.Y.
    • (1987) Genetic Engineering: Principles and Methods , vol.9 , pp. 135-154
    • Cesareni, G.1    Murray, J.2
  • 5
    • 0028935374 scopus 로고
    • Regulation of protein synthesis by heme-regulated eIF-2 alpha kinase
    • Chen, J. J., and I. M. London. 1995. Regulation of protein synthesis by heme-regulated eIF-2 alpha kinase. Trends Biochem. Sci. 20:105-108.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 105-108
    • Chen, J.J.1    London, I.M.2
  • 6
    • 0002352428 scopus 로고    scopus 로고
    • Protein kinaes that phosphorylate eIF2 and eIF2β, and their role in eukaryotic cell translational control
    • J. W. B. Hershey, M. B. Mathews, and N. Sonenberg (ed.), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Clemens, M. J. 1996. Protein kinaes that phosphorylate eIF2 and eIF2β, and their role in eukaryotic cell translational control, p. 139-172. In J. W. B. Hershey, M. B. Mathews, and N. Sonenberg (ed.), Translational control. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1996) Translational Control , pp. 139-172
    • Clemens, M.J.1
  • 7
    • 0030267336 scopus 로고    scopus 로고
    • The eIF-2α kinases and the control of protein synthesis
    • de Haro, C., R. Mendez, and J. Santoyo. 1996 The eIF-2α kinases and the control of protein synthesis. FASEB J. 10:1378-1388.
    • (1996) FASEB J. , vol.10 , pp. 1378-1388
    • De Haro, C.1    Mendez, R.2    Santoyo, J.3
  • 8
    • 0027324505 scopus 로고
    • Mammalian eukaryotic initiation factor 2 alpha kinases functionally substitute for GCN2 protein kinase in the GCN4 translational control mechanism of yeast
    • Dever, T. E., J. J. Chen, G. N. Barber, A. M. Cigan, L. Feng, T. F. Donahue, I. M. London, M. G. Katze, and A. G. Hinnebusch. 1993. Mammalian eukaryotic initiation factor 2 alpha 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
  • 9
    • 0026556814 scopus 로고
    • Phosphorylation of initiation factor 2 alpha by protein kinase GCN2 mediates gene-specific translational control of GCN4 in yeast
    • Dever, T. E., L. Feng, R. C. Wek, A. M. Cigan, T. F. Donahue, and A. G. Hinnehusch. 1992. Phosphorylation of initiation factor 2 alpha by protein kinase GCN2 mediates gene-specific translational control of GCN4 in yeast. Cell 68:585-596.
    • (1992) Cell , vol.68 , pp. 585-596
    • Dever, T.E.1    Feng, L.2    Wek, R.C.3    Cigan, A.M.4    Donahue, T.F.5    Hinnehusch, A.G.6
  • 10
    • 0029118217 scopus 로고
    • Abrogation of translation initiation factor eIF-2 phosphorylation causes malignant transformation of NIH 3T3 cells
    • Donze, O., R. Jagus, A. E. Koromilas, J. W. Hershey, and N. Sonenberg. 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
    • Donze, O.1    Jagus, R.2    Koromilas, A.E.3    Hershey, J.W.4    Sonenberg, N.5
  • 11
    • 0026653870 scopus 로고
    • Identification of double-stranded RNA-binding domains in the interferon-induced double-stranded RNA-activated p68 kinase
    • Feng, G. S., K. Chong, A. Kumar, and B. R. Williams. 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.S.1    Chong, K.2    Kumar, A.3    Williams, B.R.4
  • 12
    • 0028122964 scopus 로고
    • Casein kinase II mediates multiple phosphorylation of Saccharomyces cerevisiae eIF-2α (encoded by SUI2), which is required for optimal function in S. cerevisiae
    • Feng, L., H. Yoon, and T. F. Donahue. 1994. Casein kinase II mediates multiple phosphorylation of Saccharomyces cerevisiae eIF-2α (encoded by SUI2), which is required for optimal function in S. cerevisiae. Mol. Cell. Biol. 14:5139-5153.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 5139-5153
    • Feng, L.1    Yoon, H.2    Donahue, T.F.3
  • 13
    • 0026639664 scopus 로고
    • Control of insulin gene expression by glucose
    • Goodison, S., S. Kenna, and S. J. Ashcroft. 1992. Control of insulin gene expression by glucose. Biochem. J. 285:563-568.
    • (1992) Biochem. J. , vol.285 , pp. 563-568
    • Goodison, S.1    Kenna, S.2    Ashcroft, S.J.3
  • 14
    • 0023655554 scopus 로고
    • Biosynthesis of insulin secretory granule membrane proteins. Control by glucose
    • Grimaldi, K. A., K. Siddle, and J. C. Hutton. 1987. Biosynthesis of insulin secretory granule membrane proteins. Control by glucose. Biochem. J. 245: 567-573.
    • (1987) Biochem. J. , vol.245 , pp. 567-573
    • Grimaldi, K.A.1    Siddle, K.2    Hutton, J.C.3
  • 15
    • 0025979251 scopus 로고
    • Insulin secretory granule biogenesis. Co-ordinate regulation of the biosynthesis of the majority of constituent proteins
    • Guest, P. C., E. M. Bailyes, N. G. Rutherford, and J. C. Hutton. 1991. Insulin secretory granule biogenesis. Co-ordinate regulation of the biosynthesis of the majority of constituent proteins. Biochem. J. 274:73-78.
    • (1991) Biochem. J. , vol.274 , pp. 73-78
    • Guest, P.C.1    Bailyes, E.M.2    Rutherford, N.G.3    Hutton, J.C.4
  • 16
    • 0024495665 scopus 로고
    • Regulation of the biosynthesis of insulin-secretory-granule proteins. Co-ordinate translational control is exerted on some, but not all, granule matrix constituents
    • Guest, P. C., C. J. Rhodes, and J. C. Hutton. 1989 Regulation of the biosynthesis of insulin-secretory-granule proteins. Co-ordinate translational control is exerted on some, but not all, granule matrix constituents. Biochem. J. 257:431-437.
    • (1989) Biochem. J. , vol.257 , pp. 431-437
    • Guest, P.C.1    Rhodes, C.J.2    Hutton, J.C.3
  • 17
    • 0029020282 scopus 로고
    • The eukaryotic protein kinase superfamily: Kinase (catalytic) domain structure and classification
    • Hanks, S. K., and T. Hunter. 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
  • 18
    • 0028695223 scopus 로고
    • The eIF-2 alpha kinases: Regulators of protein synthesis in starvation and stress
    • Review
    • Hinnebusch, A. G. 1994. The eIF-2 alpha kinases: regulators of protein synthesis in starvation and stress. Semin. Cell Biol. 5:417-426. (Review.)
    • (1994) Semin. Cell Biol. , vol.5 , pp. 417-426
    • Hinnebusch, A.G.1
  • 19
    • 0030803256 scopus 로고    scopus 로고
    • Translational regulation of yeast GCN4. A window on factors that control initiator-tRNA binding to the ribosome
    • Hinnebusch, A. G. 1997. Translational regulation of yeast GCN4. A window on factors that control initiator-tRNA binding to the ribosome. J. Biol. Chem. 272:21661-21664.
    • (1997) J. Biol. Chem. , vol.272 , pp. 21661-21664
    • Hinnebusch, A.G.1
  • 22
    • 0026701570 scopus 로고
    • Malignant transformation by a mutant of the IFN-inducible dsRNA-dependent protein kinase
    • Koromilas, A. E., S. Roy, G. N. Barber, M. G. Katze, and N. Sonenberg. 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
  • 23
    • 0025792297 scopus 로고
    • Structural features in eukaryotic mRNAs that modulate the initiation of translation
    • Kozak, M. 1991. Structural features in eukaryotic mRNAs that modulate the initiation of translation. J. Biol. Chem. 263:19867-19870.
    • (1991) J. Biol. Chem. , vol.263 , pp. 19867-19870
    • Kozak, M.1
  • 24
    • 0028290902 scopus 로고
    • The interferon-induced double-stranded RNA-activated protein kinase induces apoptosis
    • Lee, S. B., and M. Esteban. 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
  • 25
    • 0343812093 scopus 로고    scopus 로고
    • The apoptosis pathway triggered by the interferon-induced protein kinase PKR requires the third basic domain, initiates upstream of Bcl-2,. and involves ICE-like proteases
    • Lee, S. B., D. Rodriguez, J. R. Rodriguez, and M. Esteban. 1997. The apoptosis pathway triggered by the interferon-induced protein kinase PKR requires the third basic domain, initiates upstream of Bcl-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
  • 26
    • 0001016282 scopus 로고    scopus 로고
    • Interactions between viruses and the cellular machinery for protein synthesis
    • J. W. B. Hershey, M. B. Mathews, and N. Sonenberg (ed.), Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
    • Mathews, M. B. 1996. Interactions between viruses and the cellular machinery for protein synthesis, p. 505-548. In J. W. B. Hershey, M. B. Mathews, and N. Sonenberg (ed.), Translational control. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
    • (1996) Translational Control , pp. 505-548
    • Mathews, M.B.1
  • 27
    • 0001342909 scopus 로고    scopus 로고
    • Origins and targets of translational control
    • J. W. B. Hershey, M. B. Mathews, and N. Sonenberg (ed.), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Mathews, M. B., N. Sonenberg, and J. W. B. Hershey. 1996. Origins and targets of translational control, p. 1-30. In J. W. B. Hershey, M. B. Mathews, and N. Sonenberg (ed.), Translational control. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1996) Translational Control , pp. 1-30
    • Mathews, M.B.1    Sonenberg, N.2    Hershey, J.W.B.3
  • 28
    • 0002523042 scopus 로고    scopus 로고
    • The pathway and mechanism of eukaryotic protein synthesis
    • J. W. B. Hershey, M. B. Mathews, and N. Sonenberg (ed.), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Merrick, W. C., and J. W. B. Hershey. 1996. The pathway and mechanism of eukaryotic protein synthesis, p. 31-70. In J. W. B. Hershey, M. B. Mathews, and N. Sonenberg (ed.), Translational control. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1996) Translational Control , pp. 31-70
    • Merrick, W.C.1    Hershey, J.W.B.2
  • 29
    • 0027396813 scopus 로고
    • Tumor suppressor function of the interferon-induced double-stranded RNA-activated protein kinase
    • Meurs, E. F., J. Galabru, G. N. Barber, M. G. Katze, and A. G. Hovanessian. 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.F.1    Galabru, J.2    Barber, G.N.3    Katze, M.G.4    Hovanessian, A.G.5
  • 30
    • 0030665841 scopus 로고    scopus 로고
    • Molecular cloning, characterization and localization of PfPk4, an eIF-2α kinase-related enzyme from the malarial parasite Plasmodium falciparum
    • Mohrle, J. J., Y. Zhao, B. Wernli, R. M. Franklin, and B. Kappes. 1997. Molecular cloning, characterization and localization of PfPk4, an eIF-2α kinase-related enzyme from the malarial parasite Plasmodium falciparum. Biochem. J. 328:677-687.
    • (1997) Biochem. J. , vol.328 , pp. 677-687
    • Mohrle, J.J.1    Zhao, Y.2    Wernli, B.3    Franklin, R.M.4    Kappes, B.5
  • 31
    • 0022380579 scopus 로고
    • Control of insulin gene expression in pancreatic beta-cells and in an insulin-producing cell line, RIN-5F cells. I. Effects of glucose and cyclic AMP on the transcription of insulin mRNA
    • Nielsen, D. A., M. Welsh, M. J. Casadaban, and D. F. Steiner. 1985. Control of insulin gene expression in pancreatic beta-cells and in an insulin-producing cell line, RIN-5F cells. I. Effects of glucose and cyclic AMP on the transcription of insulin mRNA. J. Biol. Chem. 260:13585-13589.
    • (1985) J. Biol. Chem. , vol.260 , pp. 13585-13589
    • Nielsen, D.A.1    Welsh, M.2    Casadaban, M.J.3    Steiner, D.F.4
  • 32
    • 0027258638 scopus 로고
    • Purification and characterization of eukaryotic initiation factor (elF)-2 alpha kinases from Ehrlich ascites tumor cells
    • Olmsted, E. A., L. O'Brien, E. C. Henshaw, and R. Panniers. 1993. Purification and characterization of eukaryotic initiation factor (elF)-2 alpha 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
  • 33
    • 0031853386 scopus 로고    scopus 로고
    • Isolation of the gene encoding the Drosophila melanogaster homolog of the Saccharomyces cerevisiae GCN2 eIF-2 alpha kinase
    • Olsen, D. S., B. Jordan, D. Chen, R. C. Wek, and D. R. Cavener. 1998. Isolation of the gene encoding the Drosophila melanogaster homolog of the Saccharomyces cerevisiae GCN2 eIF-2 alpha kinase. Genetics 149:1495-1509.
    • (1998) Genetics , vol.149 , pp. 1495-1509
    • Olsen, D.S.1    Jordan, B.2    Chen, D.3    Wek, R.C.4    Cavener, D.R.5
  • 34
    • 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
  • 35
    • 0026465921 scopus 로고
    • Protein phosphorylation in translational control
    • Proud, C. G. 1992. Protein 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
  • 36
    • 0026495211 scopus 로고
    • Mutations activating the yeast elF-2α kinase GCN2: Isolation of alleles altering the domain related to histidyl-tRNA synthetases
    • Ramirez, M., R. C. Wek, C. R. Vazquez de Aldana, B. M. Jackson, B. Freeman, and A. G. Hinnebusch. 1992. Mutations activating the yeast elF-2α kinase GCN2: isolation of alleles altering the domain related to histidyl-tRNA synthetases. Mol. Cell. Biol. 12:5801-5815.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 5801-5815
    • Ramirez, M.1    Wek, R.C.2    Vazquez De Aldana, C.R.3    Jackson, B.M.4    Freeman, B.5    Hinnebusch, A.G.6
  • 37
    • 0031899816 scopus 로고    scopus 로고
    • Autopriosphorylation in the activation loop is required for full kinase activity in vivo of human and yeast eukaryotic initiation factor 2α kinases PKR and GCN2
    • Romano, P. R., M. T. Garcia-Barrio, X. Zhang, Q. Wang, D. R. Taylor, P. Zhang, C. Herring, M. B. Mathews, J. Qin, and A. G. Hinnebusch. 1998. Autopriosphorylation in the activation loop is required for full kinase activity in vivo of human and yeast eukaryotic initiation factor 2α kinases PKR and GCN2. Mol. Cell. Biol. 18:2282-2297.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 2282-2297
    • Romano, P.R.1    Garcia-Barrio, M.T.2    Zhang, X.3    Wang, Q.4    Taylor, D.R.5    Zhang, P.6    Herring, C.7    Mathews, M.B.8    Qin, J.9    Hinnebusch, A.G.10
  • 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., S. R. Green, G. N. Barber, M. B. Mathews, and A. G. Hinnebusch. 1995. Structural requirements for double-stranded RNA binding, dimerization, and activation of the human eIF-2α kinase DAI in Saccharomyces cerevisiae. Mol. Cell. Biol. 15:365-378.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 365-378
    • Romano, P.R.1    Green, S.R.2    Barber, G.N.3    Mathews, M.B.4    Hinnebusch, A.G.5
  • 39
    • 0027418321 scopus 로고
    • The eIF-2 alpha protein kinases, regulators of translation in eukaryotes from yeasts to humans
    • Review
    • Samuel, C. E. 1993. The eIF-2 alpha protein kinases, regulators of translation in eukaryotes from yeasts to humans. J. Biol. Chem. 268:7603-7606. (Review.)
    • (1993) J. Biol. Chem. , vol.268 , pp. 7603-7606
    • Samuel, C.E.1
  • 40
    • 0022555781 scopus 로고
    • Purification of double-stranded RNA-dependent protein kinase from mouse fibroblasts
    • Samuel, C. E., G. S. Knutson, M. J. Berry, J. A. Atwater, and S. R. Lasky. 1986. Purification of double-stranded RNA-dependent protein kinase from mouse fibroblasts. Methods Enzymol. 119:499-516.
    • (1986) Methods Enzymol. , vol.119 , pp. 499-516
    • Samuel, C.E.1    Knutson, G.S.2    Berry, M.J.3    Atwater, J.A.4    Lasky, S.R.5
  • 41
    • 0030911360 scopus 로고    scopus 로고
    • Cloning and characterization of a cDNA encoding a protein synthesis initiation factor-2alpha (eIF-2alpha) kinase from Drosophila melanogaster. Homology to yeast GCN2 protein kinase
    • Santoyo, J., J. Alcalde, R. Mendez, D. Pulido, and C. de Haro. 1997. Cloning and characterization of a cDNA encoding a protein synthesis initiation factor-2alpha (eIF-2alpha) kinase from Drosophila melanogaster. Homology to yeast GCN2 protein kinase. J. Biol. Chem. 272:12544-12550.
    • (1997) J. Biol. Chem. , vol.272 , pp. 12544-12550
    • Santoyo, J.1    Alcalde, J.2    Mendez, R.3    Pulido, D.4    De Haro, C.5
  • 42
    • 0031891869 scopus 로고    scopus 로고
    • Phosphorylation of eukaryotic initiation factor 2 mediates apoptosis in response to activation of the double-stranded RNA-dependent protein kinase
    • Srivastava, S. P., K. U. Kumar, and R. J. Kaufman. 1998. Phosphorylation of eukaryotic initiation factor 2 mediates apoptosis in response to activation of the double-stranded RNA-dependent protein kinase. J. Biol. Chem. 273: 2416-2423.
    • (1998) J. Biol. Chem. , vol.273 , pp. 2416-2423
    • Srivastava, S.P.1    Kumar, K.U.2    Kaufman, R.J.3
  • 43
    • 10244257563 scopus 로고    scopus 로고
    • Autophosphorylation sites participate in the activation of the double-stranded-RNA-activated protein kinase PKR
    • Taylor, D. R., S. B. Lee, P. R. Romano, D. R. Marshak, A. G. Hinnebusch, M. Esteban, and M. B. Mathews. 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    Romano, P.R.3    Marshak, D.R.4    Hinnebusch, A.G.5    Esteban, M.6    Mathews, M.B.7
  • 44
    • 0027186435 scopus 로고
    • Mutations in the alpha subunit of eukaryotic translation initiation factor 2 (eIF-2 alpha) that overcome the inhibitory effect of eIF-2 alpha phosphorylation on translation initiation
    • Vazquez de Aldana, C. R., T. E. Dever, and A. G. Hinnebusch. 1993. Mutations in the alpha subunit of eukaryotic translation initiation factor 2 (eIF-2 alpha) that overcome the inhibitory effect of eIF-2 alpha phosphorylation on translation initiation. Proc. Natl. Acad. Sci. USA 90:7215-7219.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 7215-7219
    • Vazquez De Aldana, C.R.1    Dever, T.E.2    Hinnebusch, A.G.3
  • 45
    • 0028171125 scopus 로고
    • IF-2 kinases: Regulators of general and gene-specific translation initiation
    • Review
    • Wek, R. C. 1994. eIF-2 kinases: regulators of general and gene-specific translation initiation. Trends Biochem. Sci. 19:491-496. (Review.)
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 491-496
    • Wek, R.C.1
  • 46
    • 0024381444 scopus 로고
    • Juxtaposition of domains homologous to protein kinases and histidyl-tRNA synthetases in GCN2 protein suggests a mechanism for coupling GCN4 expression to amino acid availability
    • Wek, R. C. B. M. Jackson, and A. G. Hinnebusch. 1989. Juxtaposition of domains homologous to protein kinases and histidyl-tRNA synthetases in GCN2 protein suggests a mechanism for coupling GCN4 expression to amino acid availability. Proc. Natl. Acad. Sci. USA 86:4579-4583.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 4579-4583
    • Wek, R.C.1    Jackson, B.M.2    Hinnebusch, A.G.3
  • 47
    • 0025330827 scopus 로고
    • Identification of positive-acting domains in GCN2 protein kinase required for translational activation of GCN4 expression
    • Wek, R. C., M. Ramirez, B. M. Jackson, and A. G. Hinnebusch. 1990. Identification of positive-acting domains in GCN2 protein kinase required for translational activation of GCN4 expression. Mol. Cell. Biol. 10:2820-2831.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 2820-2831
    • Wek, R.C.1    Ramirez, M.2    Jackson, B.M.3    Hinnebusch, A.G.4
  • 48
    • 0029006391 scopus 로고
    • The histidyl-tRNA synthetase-related 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., S. Zhu, and R. C. Wek. 1995. The histidyl-tRNA synthetase-related 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
  • 49
    • 0031009879 scopus 로고    scopus 로고
    • The role of the 90-kDa heat-shock protein and its associated cohorts in stabilizing the heme-regulated eIF-2alpha kinase in reticulocyte lysates during heat stress
    • Xu, Z., J. K. Pal, V. Thulasiraman, H. P. Hahn, C. J. J. Chen, and R. L. Matts. 1997. The role of the 90-kDa heat-shock protein and its associated cohorts in stabilizing the heme-regulated eIF-2alpha kinase in reticulocyte lysates during heat stress. Eur. J. Biochem. 246:461-470.
    • (1997) Eur. J. Biochem. , vol.246 , pp. 461-470
    • Xu, Z.1    Pal, J.K.2    Thulasiraman, V.3    Hahn, H.P.4    Chen, C.J.J.5    Matts, R.L.6
  • 51
    • 0030908706 scopus 로고    scopus 로고
    • Ribosome targeting of PKR is mediated by two double-stranded RNA-binding domains and facilitates in vivo phosphorylation of eukaryotic initiation factor-2
    • Zhu, S., P. R. Romano, and R. C. Wek. 1997. Ribosome targeting of PKR is mediated by two double-stranded RNA-binding domains and facilitates in vivo phosphorylation of eukaryotic initiation factor-2. J. Biol. Chem. 272: 14434-14441.
    • (1997) J. Biol. Chem. , vol.272 , pp. 14434-14441
    • Zhu, S.1    Romano, P.R.2    Wek, R.C.3
  • 52
    • 0029785485 scopus 로고    scopus 로고
    • Histidyl-tRNA synthetase-related sequences in GCN2 protein kinase regulate in vitro phosphorylation of eIF-2
    • Zhu, S., A. Y. Sobolev, and R. C. Wek. 1996. Histidyl-tRNA synthetase-related sequences in GCN2 protein kinase regulate in vitro phosphorylation of eIF-2. J. Biol. Chem. 271:24989-24994.
    • (1996) J. Biol. Chem. , vol.271 , pp. 24989-24994
    • Zhu, S.1    Sobolev, A.Y.2    Wek, R.C.3
  • 53
    • 0023021520 scopus 로고
    • Purification and characterization of a protein-tyrosine kinase from bovine thymus
    • Zioncheck, T. F., M. L. Harrison, and R. L. Geahlen. 1986. Purification and characterization of a protein-tyrosine kinase from bovine thymus. J. Biol. Chem. 261:15637-15643.
    • (1986) J. Biol. Chem. , vol.261 , pp. 15637-15643
    • Zioncheck, T.F.1    Harrison, M.L.2    Geahlen, R.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.