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Volumn 18, Issue 2, 1998, Pages 859-871

Regulation of interferon-induced protein kinase PKR: Modulation of P58(IPK) inhibitory function by a novel protein, p52(rIPK)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA2A INTERFERON; INITIATION FACTOR 2; MESSENGER RNA; PROTEIN KINASE;

EID: 2642648639     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.18.2.859     Document Type: Article
Times cited : (77)

References (92)
  • 1
    • 0028211253 scopus 로고
    • The 58-kilodalton inhibitor of the interferon-induced double-stranded RNA-activated protein kinase is a tetratricopeptide repeat protein with oncogenic properties
    • Barber, G. N., S. Thompson, T. G. Lee, T. Strom, R. Jagus, A. Darveau, and M. G. Katze. 1994. The 58-kilodalton inhibitor of the interferon-induced double-stranded RNA-activated protein kinase is a tetratricopeptide 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
  • 2
    • 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., M. Wambach, S. Thompson, R. Jagus, and M. G. Katze. 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
  • 5
    • 0029126514 scopus 로고
    • Analyzing protein-protein interactions using the two-hybrid system
    • Bartel, P. L., and S. Fields. 1995. Analyzing protein-protein interactions using the two-hybrid system. Methods Enzymol. 254:241-263.
    • (1995) Methods Enzymol. , vol.254 , pp. 241-263
    • Bartel, P.L.1    Fields, S.2
  • 6
    • 0031014063 scopus 로고    scopus 로고
    • Oncogenic potential of TAR RNA binding protein TRBP and its regulatory interaction with RNA-dependent protein kinase PKR
    • Benkirane, M., C. Neuveut, R. F. Chun, S. M. Smith, C. E. Samuel, A. Gatignol, and K.-T. Jeang. 1997. Oncogenic potential of TAR RNA binding protein TRBP and its regulatory interaction with RNA-dependent protein kinase PKR. EMBO J. 16:611-624.
    • (1997) EMBO J. , vol.16 , pp. 611-624
    • Benkirane, M.1    Neuveut, C.2    Chun, R.F.3    Smith, S.M.4    Samuel, C.E.5    Gatignol, A.6    Jeang, K.-T.7
  • 7
    • 0029762971 scopus 로고    scopus 로고
    • Inhibition of translational initiation by activators of the glucose-regulated stress protein and heat shock protein stress response systems
    • Brostrom, C. O., C. R. Prostko, R. J. Kaufman, and M. A. Brostrom. 1996. Inhibition of translational initiation by activators of the glucose-regulated stress protein and heat shock protein stress response systems. J. Biol. Chem. 271:24995-25002.
    • (1996) J. Biol. Chem. , vol.271 , pp. 24995-25002
    • Brostrom, C.O.1    Prostko, C.R.2    Kaufman, R.J.3    Brostrom, M.A.4
  • 8
    • 0027429134 scopus 로고
    • Interaction of glucocorticosteroid receptor and wild-type or mutated 90-kDa heat shock protein coexpressed in baculovirus-infected Sf9 cells
    • Cadepond, F., N. Binart, B. Chambraud, N. Jibard, G. Schweizer-Groyer, I. Segard-Maurel, and E. E. Baulieu. 1993. Interaction of glucocorticosteroid receptor and wild-type or mutated 90-kDa heat shock protein coexpressed in baculovirus-infected Sf9 cells. Proc. Natl. Acad. Sci. USA 90:10434-10438.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10434-10438
    • Cadepond, F.1    Binart, N.2    Chambraud, B.3    Jibard, N.4    Schweizer-Groyer, G.5    Segard-Maurel, I.6    Baulieu, E.E.7
  • 9
    • 0028331568 scopus 로고
    • Selective deletions in the 90 kDa heat shock protein (hsp90) impede hetero-ligomeric complex formation with the glucocorticoid receptor (GR) and hormone binding by GR
    • Cadepond, F., N. Jibard, N. Binart, G. Schweizer-Groyer, I. Segard-Maurel, and E. E. Baulieu. 1994. Selective deletions in the 90 kDa heat shock protein (hsp90) impede hetero-ligomeric complex formation with the glucocorticoid receptor (GR) and hormone binding by GR. Steroid Biochem. Mol. Biol. 48:361-367.
    • (1994) Steroid Biochem. Mol. Biol. , vol.48 , pp. 361-367
    • Cadepond, F.1    Jibard, N.2    Binart, N.3    Schweizer-Groyer, G.4    Segard-Maurel, I.5    Baulieu, E.E.6
  • 10
    • 0025745326 scopus 로고
    • Characterization of YDJ1: A yeast homologue of the bacterial dnaJ protein
    • Caplan, A. J., and M. G. Douglas. 1991. Characterization of YDJ1: a yeast homologue of the bacterial dnaJ protein. J. Cell Biol. 114:609-621.
    • (1991) J. Cell Biol. , vol.114 , pp. 609-621
    • Caplan, A.J.1    Douglas, M.G.2
  • 11
    • 0000615498 scopus 로고
    • Plasmid vectors carrying the replication origin of filamentous single-stranded phages
    • J. K. Setlow and A. Hollaender (ed.), Plenum Press, New York, N.Y.
    • Cesareni, G., and J. A. H. Murray. 1987. Plasmid vectors carrying the replication origin of filamentous single-stranded phages, p. 135-154. In J. K. Setlow and A. Hollaender (ed.), Genetic engineering: principles and methods. Plenum Press, New York, N.Y.
    • (1987) Genetic Engineering: Principles and Methods , pp. 135-154
    • Cesareni, G.1    Murray, J.A.H.2
  • 12
    • 0025779365 scopus 로고
    • Cloning of the cDNA of the heme-regulated eukaryotic initiation factor 2a (eIF-2a) kinase of rabbit reticulocytes: Homology to yeast GCN2 protein kinase and human double-stranded-RNA-dependent eIF-2a kinase
    • Chen, J., J. Pal, M. S. Throop, L. Gehrke, I. Kuo, J. K. Pal, M. Brodsky, and I. M. London. 1991. Cloning of the cDNA of the heme-regulated eukaryotic initiation factor 2a (eIF-2a) kinase of rabbit reticulocytes: homology to yeast GCN2 protein kinase and human double-stranded-RNA-dependent eIF-2a kinase. Proc. Natl. Acad. Sci. USA 88:7729-7733.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 7729-7733
    • Chen, J.1    Pal, J.2    Throop, M.S.3    Gehrke, L.4    Kuo, I.5    Pal, J.K.6    Brodsky, M.7    London, I.M.8
  • 13
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by guanidium thiocyanate-phenol-chloroform extraction
    • Chomczynski, P., and N. Sacchi. 1987. Single-step method of RNA isolation by guanidium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162:156-159.
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 15
    • 0002352428 scopus 로고    scopus 로고
    • Protein kinases that phosphorylate eIF-2 and cIF-2B, and their role in eukaryotic cell translational control
    • J. Hershey, M. Mathews, and N. Sonenberg (ed.), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Clemens, M. J. 1996. Protein kinases that phosphorylate eIF-2 and cIF-2B, and their role in eukaryotic cell translational control, p. 139-172. In J. Hershey, M. 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
  • 16
    • 0030725442 scopus 로고    scopus 로고
    • The double-stranded RNA-dcpendent protein kinase PKR - Structure and function
    • Clemens, M. J., and A. Elia. 1997. The double-stranded RNA-dcpendent protein kinase PKR - structure and function. J. Interferon Cytokine Res. 17:503-524.
    • (1997) J. Interferon Cytokine Res. , vol.17 , pp. 503-524
    • Clemens, M.J.1    Elia, A.2
  • 17
    • 0027300506 scopus 로고
    • Heat shock proteins: Molecular chaperones of protein biogenesis
    • Craig, E. A., B. D. Gambill, and R. J. Nelson. 1993. Heat shock proteins: molecular chaperones of protein biogenesis. Microbiol. Rev. 57:402-414.
    • (1993) Microbiol. Rev. , vol.57 , pp. 402-414
    • Craig, E.A.1    Gambill, B.D.2    Nelson, R.J.3
  • 18
    • 0028363670 scopus 로고
    • Mutations in Hsp83 and cdc37 impair signaling by the sevenless receptor tyrosine kinase in Drosophila
    • Cutforth, T., and G. M. Rubin. 1994. Mutations in Hsp83 and cdc37 impair signaling by the sevenless receptor tyrosine kinase in Drosophila. Cell 77: 1027-1036.
    • (1994) Cell , vol.77 , pp. 1027-1036
    • Cutforth, T.1    Rubin, G.M.2
  • 19
    • 0028353336 scopus 로고
    • DnaJ-like proteins: Molecular chaperones and specific regulators of Hsp70
    • Cyr, D. M., T. Langer, and M. G. Douglas. 1994. DnaJ-like proteins: molecular chaperones and specific regulators of Hsp70. Trends Biochem. Sci. 19:176-181.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 176-181
    • Cyr, D.M.1    Langer, T.2    Douglas, M.G.3
  • 20
    • 0030992545 scopus 로고    scopus 로고
    • A double-stranded RNA-activated protein kinase-dependent pathway mediating stress-induced apoptosis
    • Der, S. D., Y. L. Yang, C. Weissman, and B. R. Williams. 1997. A double-stranded RNA-activated protein kinase-dependent pathway mediating stress-induced apoptosis. Proc. Natl. Acad. Sci. USA 94:3279-3283.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 3279-3283
    • Der, S.D.1    Yang, Y.L.2    Weissman, C.3    Williams, B.R.4
  • 21
    • 0030907057 scopus 로고    scopus 로고
    • Using GCN4 as a reporter of eIF-2α phosphorylation and translational regulation in yeast
    • Dever, T. E. 1997. Using GCN4 as a reporter of eIF-2α phosphorylation and translational regulation in yeast. Methods Companion Methods Enzymol. 11:403-417.
    • (1997) Methods Companion Methods Enzymol. , vol.11 , pp. 403-417
    • Dever, T.E.1
  • 22
    • 0027324505 scopus 로고
    • Mammalian eukaryotic initiation factor eIF2a kinases functionally substitute for GCN2 protein kinase in the GCN4 translational control mechanism in yeast
    • Dever, T. E., J.-J. Chen, G. N. Barber, A. M. Cigan, L. Feng, T. F. Donahue, I. London, M. G. Katze, and A. G. Hinnebusch. 1994. Mammalian eukaryotic initiation factor eIF2a kinases functionally substitute for GCN2 protein kinase in the GCN4 translational control mechanism in yeast. Proc. Natl. Acad. Sci. USA 90:4616-4620.
    • (1994) 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.7    Katze, M.G.8    Hinnebusch, A.G.9
  • 23
    • 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. Hinnebusch. 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    Hinnebusch, A.G.6
  • 24
    • 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. B. Hershey, and N. Sonneberg. 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.B.4    Sonneberg, N.5
  • 25
  • 26
    • 0028981277 scopus 로고    scopus 로고
    • p53-dependent repression of CDK4 translation in TGF-heta-induced G1 cell cycle arrest
    • Ewen, M. E., C. J. Oliver, H. K. Sluss, S. J. Miller, and D. S. Peeper. 1997. p53-dependent repression of CDK4 translation in TGF-heta-induced G1 cell cycle arrest. Genes Dev. 9:204-217.
    • (1997) Genes Dev. , vol.9 , pp. 204-217
    • Ewen, M.E.1    Oliver, C.J.2    Sluss, H.K.3    Miller, S.J.4    Peeper, D.S.5
  • 27
    • 0024406857 scopus 로고
    • A novel genetic system to detect protein-protein interactions
    • Fields, S., and O. Song. 1989. A novel genetic system to detect protein-protein interactions. Nature 340:245-246.
    • (1989) Nature , vol.340 , pp. 245-246
    • Fields, S.1    Song, O.2
  • 28
    • 0031106603 scopus 로고    scopus 로고
    • Chaperones get in touch: The Hip-Hop connection
    • Frydman, J., and J. Hohfeld. 1997. Chaperones get in touch: the Hip-Hop connection. Trends Biochem. Sci. 22:87-92.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 87-92
    • Frydman, J.1    Hohfeld, J.2
  • 29
    • 0028135410 scopus 로고
    • Translational control mediates the developmental regulation of the Trypanosoma brucei Nrk protein kinase
    • Gale, M., Jr., V. Carter, and M. Parsons. 1994. Translational control mediates the developmental regulation of the Trypanosoma brucei Nrk protein kinase. J. Biol. Chem. 269:31659-31665.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31659-31665
    • Gale Jr., M.1    Carter, V.2    Parsons, M.3
  • 30
    • 0342618445 scopus 로고    scopus 로고
    • What happens inside lentivirus or influenza virus infected cells: Insights into the regulation of cellular and viral protein synthesis
    • Gale, M., Jr., and M. G. Katze. 1997. What happens inside lentivirus or influenza virus infected cells: insights into the regulation of cellular and viral protein synthesis. Methods Companion Methods Enzymol. 11:383-401.
    • (1997) Methods Companion Methods Enzymol. , vol.11 , pp. 383-401
    • Gale Jr., M.1    Katze, M.G.2
  • 31
    • 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.J.1    Tan, S.-L.2    Wambach, M.3    Katze, M.G.4
  • 32
    • 85036676954 scopus 로고    scopus 로고
    • Gale, M. J., Jr., C. M. Blakely, and M. G. Katze. Unpublished observations
    • Gale, M. J., Jr., C. M. Blakely, and M. G. Katze. Unpublished observations.
  • 33
    • 0343924357 scopus 로고    scopus 로고
    • Evidence that hepatitis C virus resistance to interferon is mediated through repression of the PKR protein kinase by the nonstructural 5A protein
    • Gale, M. J., Jr., M. J. Korth, N. M. Tang, S. L. Tan, D. A. Hopkins, T. E. Dever, S. J. Polyak, D. R. Gretch, and M. G. Katze. 1997. Evidence that hepatitis C virus resistance to interferon is mediated through repression of the PKR protein kinase by the nonstructural 5A protein. Virology 230:217-227.
    • (1997) Virology , vol.230 , pp. 217-227
    • Gale Jr., M.J.1    Korth, M.J.2    Tang, N.M.3    Tan, S.L.4    Hopkins, D.A.5    Dever, T.E.6    Polyak, S.J.7    Gretch, D.R.8    Katze, M.G.9
  • 34
    • 0030198564 scopus 로고    scopus 로고
    • Characterization of the heparin-mediated activation of PKR, the interferon-inducible RNA-dependent protein kinase
    • George, C. X., D. C. Thomis, S. J. McCormack, C. M. Svahn, and C. E. Samuel. 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
  • 35
    • 0025922586 scopus 로고
    • The TPR snap helix: A novel protein repeat motif from mitosis to transcription
    • Goebl, M., and M. Yanagida. 1991. The TPR snap helix: a novel protein repeat motif from mitosis to transcription. Trends Biochem. Sci. 16:173-177.
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 173-177
    • Goebl, M.1    Yanagida, M.2
  • 36
    • 0029670477 scopus 로고    scopus 로고
    • Kip1 accumulation during the cell cycle
    • Kip1 accumulation during the cell cycle. Science 271:1861-1864.
    • (1997) Science , vol.271 , pp. 1861-1864
    • Hengst, L.1    Reed, S.I.2
  • 37
    • 0024364170 scopus 로고
    • Sequence and regulation of a gene encoding a human 89-kilodalton heat shock protein
    • Hickey, E., S. E. Brandon, G. Smale, D. Lloyd, and L. A. Weber. 1989. Sequence and regulation of a gene encoding a human 89-kilodalton heat shock protein. Mol. Cell. Biol. 9:2615-2626.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 2615-2626
    • Hickey, E.1    Brandon, S.E.2    Smale, G.3    Lloyd, D.4    Weber, L.A.5
  • 38
    • 0028695223 scopus 로고
    • The eIF-2α kinases: Regulators of protein synthesis in starvation and stress
    • Hinnebusch, A. G. 1994. The eIF-2α kinases: regulators of protein synthesis in starvation and stress. Semin. Cell Biol. 5:417-426.
    • (1994) Semin. Cell Biol. , vol.5 , pp. 417-426
    • Hinnebusch, A.G.1
  • 39
    • 0028842615 scopus 로고
    • Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle
    • Höhfeld, J., Y. Minami, and F. U. Hartl. 1995. Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle. Cell 83:589-598.
    • (1995) Cell , vol.83 , pp. 589-598
    • Höhfeld, J.1    Minami, Y.2    Hartl, F.U.3
  • 40
    • 0031127737 scopus 로고    scopus 로고
    • Cdc37: A protein kinase chaperone?
    • Hunter, T. 1997. Cdc37: a protein kinase chaperone? Trends. Cell Biol. 7:157-161.
    • (1997) Trends. Cell Biol. , vol.7 , pp. 157-161
    • Hunter, T.1
  • 41
    • 0030933277 scopus 로고    scopus 로고
    • Oncoprotein networks
    • Hunter, T. 1997. Oncoprotein networks. Cell 88:333-346.
    • (1997) Cell , vol.88 , pp. 333-346
    • Hunter, T.1
  • 42
    • 0008988515 scopus 로고
    • The regulation of the interferon-induced dsRNA activated protein kinase in virus-infected cells by viral and cellular gene products
    • Katze, M. G. 1993. The regulation of the interferon-induced dsRNA activated protein kinase in virus-infected cells by viral and cellular gene products. Semin. Virol. 508:1-5.
    • (1993) Semin. Virol. , vol.508 , pp. 1-5
    • Katze, M.G.1
  • 43
    • 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 Microhiol. 3:75-78.
    • (1995) Trends Microhiol. , vol.3 , pp. 75-78
    • Katze, M.G.1
  • 44
    • 0002833852 scopus 로고    scopus 로고
    • Translational control in cells infected with influenza virus and reovirus
    • J. W. B. Hershey, M. B. Mathews, and N. Sonenherg (ed.), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Katze, M. G. 1996. Translational control in cells infected with influenza virus and reovirus, p. 607-630. In J. W. B. Hershey, M. B. Mathews, and N. Sonenherg (ed.), Translational control. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1996) Translational Control , pp. 607-630
    • Katze, M.G.1
  • 46
    • 0023896661 scopus 로고
    • Amino acid biosynthesis inhibitors as herbicides
    • Kishore, G. M., and D. M. Shaw. 1988. Amino acid biosynthesis inhibitors as herbicides. Annu. Rev. Biochem. 57:627-663.
    • (1988) Annu. Rev. Biochem. , vol.57 , pp. 627-663
    • Kishore, G.M.1    Shaw, D.M.2
  • 47
    • 0030927170 scopus 로고    scopus 로고
    • Regulation of the protein kinase PKR by the vaccinia virus pseudosubstrate inhibitor K3L is dependent on residues conserved between the K3L protein and the PKR substrate eIF-2α
    • Kobayashi, M., E. Locke, J. Silverman, T. Ung, and T. E. Dever. 1997. Regulation of the protein kinase PKR by the vaccinia virus pseudosubstrate inhibitor K3L is dependent on residues conserved between the K3L protein and the PKR substrate eIF-2α. Mol. Cell. Biol. 17:4146-4158.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 4146-4158
    • Kobayashi, M.1    Locke, E.2    Silverman, J.3    Ung, T.4    Dever, T.E.5
  • 48
    • 0026701570 scopus 로고
    • Malignant transformation by a mutant of the interferon-inducible dsRNA dependent protein kinase
    • Koromilas, A. E., S. Roy, G. N. Barber, M. G. Katze, and N. Sonneberg. 1992. Malignant transformation by a mutant of the interferon-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    Sonneberg, N.5
  • 49
    • 0029996422 scopus 로고    scopus 로고
    • Cloning, expression, and cellular localization of the oncogenic 5H-kDa inhibitor of the RNA-activated human and mouse protein kinase
    • Korth, M. J., C. N. Lyons, M. Wambach, and M. G. Katze. 1996. Cloning, expression, and cellular localization of the oncogenic 5H-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
  • 50
    • 0028332026 scopus 로고
    • The dsRNA-dependent protein kinase, PKR, activates transcription factor NF-kB by phosphorylating IkB
    • Kumar, A., J. Haque, J. Lacoste, J. Hiscott, and B. R. G. Williams. 1994. The dsRNA-dependent protein kinase, PKR, activates transcription factor NF-kB by phosphorylating IkB. 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
  • 51
    • 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-kB
    • Kumar, A., Y. Yang, V. Flati, S. Der, S. Kadereit, A. Deb, J. Haque, L. Reis, C. Weissmann, and B. R. G. Williams. 1997. Deficient cytokine signaling in mouse embryo fibroblasts with a targeted deletion in the PKR gene: role of IRF-1 and NF-kB. EMBO J. 16:406-413.
    • (1997) EMBO J. , vol.16 , pp. 406-413
    • Kumar, A.1    Yang, Y.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
  • 52
    • 0026075824 scopus 로고    scopus 로고
    • Chromosome 11q13 abnormalities in human cancer
    • Lammie, G. A., and G. Peters. 1997. Chromosome 11q13 abnormalities in human cancer. Cancer Cells 3:413-420.
    • (1997) Cancer Cells , vol.3 , pp. 413-420
    • Lammie, G.A.1    Peters, G.2
  • 53
    • 0345064267 scopus 로고
    • Monoclonal antibodies to interferon induced 68,000 Mr protein and their use for the detection of double-stranded RNA dependent protein kinase in human cells
    • Laurent, A. G., B. Krust, J. Galabru, J. Svab, and A. G. Hovanessian. 1985. Monoclonal antibodies to interferon induced 68,000 Mr protein and their use for the detection of double-stranded RNA dependent protein kinase in human cells. Proc. Natl. Acad. Sci. USA 82:4341-4345.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 4341-4345
    • Laurent, A.G.1    Krust, B.2    Galabru, J.3    Svab, J.4    Hovanessian, A.G.5
  • 54
    • 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., N. Tang, S. Thompson, J. Miller, and M. G. Katze. 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
  • 55
    • 0026628369 scopus 로고
    • Characterization and regulation of the 58,000-dalton cellular inhibitor of the interferon-induced, dsRNA-activated protein kinase
    • Lee, T. G., J. Tomita, A. G. Hovanessian, and M. G. Katze. 1992. Characterization and regulation of the 58,000-dalton cellular inhibitor of the interferon-induced, dsRNA-activated protein kinase. J. Biol. Chem. 267:14238-14243.
    • (1992) J. Biol. Chem. , vol.267 , pp. 14238-14243
    • Lee, T.G.1    Tomita, J.2    Hovanessian, A.G.3    Katze, M.G.4
  • 57
    • 0026778841 scopus 로고
    • Interactions of the heme-regulated eIF-2 alpha kinase with heat shock proteins in rabbit reticulocyte lysates
    • Matts, R. L., Z. Xu, J. K. Pal, and J.-J. Chen. 1992. Interactions of the heme-regulated eIF-2 alpha kinase with heat shock proteins in rabbit reticulocyte lysates. J. Biol. Chem. 267:18160-18167.
    • (1992) J. Biol. Chem. , vol.267 , pp. 18160-18167
    • Matts, R.L.1    Xu, Z.2    Pal, J.K.3    Chen, J.-J.4
  • 59
    • 0025298202 scopus 로고
    • Molecular cloning and characterization of the human double-stranded RNA-activated protein kinase induced by interferon
    • Meurs, E., K. L. Chong, J. Galabru, N. Thomas, I. Kerr, B. R. G. Williams, and A. G. Hovanessian. 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.L.2    Galabru, J.3    Thomas, N.4    Kerr, I.5    Williams, B.R.G.6    Hovanessian, A.G.7
  • 60
    • 0027396813 scopus 로고
    • Tumour suppressor function of the interteron-induced double-stranded RNA-activated 68,000-Mr protein kinase
    • Meurs, E., J. Galabru, G. N. Barber, M. G. Katze, and A. G. Hovanessian. 1993. Tumour suppressor function of the interteron-induced double-stranded RNA-activated 68,000-Mr 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
  • 61
    • 0001824746 scopus 로고
    • Progress and perspectives on the biology of heat shock proteins and molecular chaperones
    • R. I. Morimoto, A. Tissieres, and C. Georgopoulos (ed.), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Morimoto, R. I., A. Tissieres, and C. Georgopoulos. 1994. Progress and perspectives on the biology of heat shock proteins and molecular chaperones, p. 1-30. In R. I. Morimoto, A. Tissieres, and C. Georgopoulos (ed.), The biology of heat shock proteins and molecular chaperones. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1994) The Biology of Heat Shock Proteins and Molecular Chaperones , pp. 1-30
    • Morimoto, R.I.1    Tissieres, A.2    Georgopoulos, C.3
  • 63
    • 0028812847 scopus 로고
    • Genetics of chromosome 11: Loci for pediatric and adult malignancies, developmental disorders, and other diseases
    • Nowak, N. J., and T. B. Shows. 1995. Genetics of chromosome 11: loci for pediatric and adult malignancies, developmental disorders, and other diseases. Cancer Inv. 13:646-659.
    • (1995) Cancer Inv. , vol.13 , pp. 646-659
    • Nowak, N.J.1    Shows, T.B.2
  • 64
    • 0027486385 scopus 로고
    • Cloning of a cDNA for heat-shock protein hsp40, a human homologue of bacterial DnaJ
    • Ohtsuka, K. 1993. Cloning of a cDNA for heat-shock protein hsp40, a human homologue of bacterial DnaJ. Biochem. Biophys. Res. Commun. 197:235-240.
    • (1993) Biochem. Biophys. Res. Commun. , vol.197 , pp. 235-240
    • Ohtsuka, K.1
  • 65
    • 0030889218 scopus 로고    scopus 로고
    • The product of the proto-oncogene c-cbl: A negative regulator of the Syk tyrosine kinase
    • Ota, Y., and L. E. Samelson. 1997. The product of the proto-oncogene c-cbl: a negative regulator of the Syk tyrosine kinase. Science 276:418-420.
    • (1997) Science , vol.276 , pp. 418-420
    • Ota, Y.1    Samelson, L.E.2
  • 66
    • 0029889955 scopus 로고    scopus 로고
    • A model of protein targeting mediated by immunophilins and other proteins that bind to hsp90 via tetratricopeptide repeal domains
    • Owens-Grillo, J. K., M. J. Czar, K. A. Hutchinson, K. Hoffman, G. H. Perdew, and W. B. Pratt. 1996. A model of protein targeting mediated by immunophilins and other proteins that bind to hsp90 via tetratricopeptide repeal domains. J. Biol. Chem. 271:13468-13475.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13468-13475
    • Owens-Grillo, J.K.1    Czar, M.J.2    Hutchinson, K.A.3    Hoffman, K.4    Perdew, G.H.5    Pratt, W.B.6
  • 67
    • 0029115903 scopus 로고
    • The interferon-inducible double-stranded RNA-activated protein kinase self-associates in vitro and in vivo
    • Patel, R. C., P. Stanton, N. M. J. McMillan, B. R. G. Williams, and G. C. Sen. 1995. The interferon-inducible double-stranded RNA-activated protein kinase self-associates in vitro and in vivo. Proc. Natl. Acad. Sci. USA 92:8283-8287.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8283-8287
    • Patel, R.C.1    Stanton, P.2    McMillan, N.M.J.3    Williams, B.R.G.4    Sen, G.C.5
  • 68
    • 0026495863 scopus 로고    scopus 로고
    • Expression and characterization of human FKBP52, an immunophilin that associates with the 90-kDa heat shock protein and is a component of steroid receptor complexes
    • Peattie, D. A., M. W. Harding, M. A. Fleming, M. T. DeCenzo, J. A. Lippke, D. J. Livingston, and M. Benasutti. 1997. Expression and characterization of human FKBP52, an immunophilin that associates with the 90-kDa heat shock protein and is a component of steroid receptor complexes. Proc. Natl. Acad. Sci. USA 89:10974-10978.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10974-10978
    • Peattie, D.A.1    Harding, M.W.2    Fleming, M.A.3    DeCenzo, M.T.4    Lippke, J.A.5    Livingston, D.J.6    Benasutti, M.7
  • 69
    • 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., N. Tang, M. Wambach, G. N. Barber, and M. G. Katze. 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
  • 70
    • 0026587013 scopus 로고
    • Transmembrane receptors and intracellular pathways that control cell proliferation
    • Poussegur, J., and K. Seuwen. 1992. Transmembrane receptors and intracellular pathways that control cell proliferation. Annu. Rev. Physiol. 54:195-210.
    • (1992) Annu. Rev. Physiol. , vol.54 , pp. 195-210
    • Poussegur, J.1    Seuwen, K.2
  • 71
    • 0028938425 scopus 로고
    • Activation of the double-stranded RNA-regulated protein kinase by depletion of endoplasmic reticular calcium stores
    • Prostko, C. R., J. N. Dholakia, M. A. Brostrom, and C. O. Brostrom. 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
  • 72
    • 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
  • 73
    • 0028935270 scopus 로고    scopus 로고
    • Pro-inflammatory cytokines and environmental stress cause p38 mitogen-activated protein kinase activation by dual phosphorylation on tyrosine and threonine
    • Raingeaud, J., S. Gupta, J. S. Rodgers, M. Dickens, J. Han, R. J. Ulevitch, and R. J. Davis. 1997. Pro-inflammatory cytokines and environmental stress cause p38 mitogen-activated protein kinase activation by dual phosphorylation on tyrosine and threonine. J. Biol. Chem. 270:7420-7426.
    • (1997) J. Biol. Chem. , vol.270 , pp. 7420-7426
    • Raingeaud, J.1    Gupta, S.2    Rodgers, J.S.3    Dickens, M.4    Han, J.5    Ulevitch, R.J.6    Davis, R.J.7
  • 74
    • 0028924758 scopus 로고
    • Structural requirements for double-stranded RNA binding, dimerization, and activation of the human eIF-2α kinase DAI in yeast
    • 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 yeast. 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
  • 76
    • 0027365517 scopus 로고
    • Elevated levels of cyclin D1 protein in response to increased expression of eukaryotic initiation factor 4E
    • Rosenwald, I. B., A. Lazaris-Karatzas, N. Sonenberg, and E. V. Schmidt. 1993. Elevated levels of cyclin D1 protein in response to increased expression of eukaryotic initiation factor 4E. Mol. Cell. Biol. 13:7358-7363.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 7358-7363
    • Rosenwald, I.B.1    Lazaris-Karatzas, A.2    Sonenberg, N.3    Schmidt, E.V.4
  • 77
    • 0029860936 scopus 로고    scopus 로고
    • Ultraviolet light and osmotic stress: Activation of the JNK cascade through multiple growth factor and cytokine receptors
    • Rosette, C., and M. Karin. 1996. Ultraviolet light and osmotic stress: activation of the JNK cascade through multiple growth factor and cytokine receptors. Science 274:1194-1197.
    • (1996) Science , vol.274 , pp. 1194-1197
    • Rosette, C.1    Karin, M.2
  • 78
    • 0027352378 scopus 로고
    • Interferon-induced antiviral actions and their regulation
    • Sen, G. C., and R. M. Ransohoff. 1993. Interferon-induced antiviral actions and their regulation. Adv. Virus Res. 42:57.
    • (1993) Adv. Virus Res. , vol.42 , pp. 57
    • Sen, G.C.1    Ransohoff, R.M.2
  • 79
    • 0029957019 scopus 로고    scopus 로고
    • A non-enzymatic p21 protein inhibitor of stress-activated protein kinase
    • Shim, J., H. Lee, J. Park, H. Kim, and E.-J. Choi. 1997. A non-enzymatic p21 protein inhibitor of stress-activated protein kinase. Nature 381:804-807.
    • (1997) Nature , vol.381 , pp. 804-807
    • Shim, J.1    Lee, H.2    Park, J.3    Kim, H.4    Choi, E.-J.5
  • 80
    • 0023806075 scopus 로고
    • Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione-S-transferase
    • Smith, D. B., and K. S. Johnson. 1988. Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione-S-transferase. Gene 67:31-40.
    • (1988) Gene , vol.67 , pp. 31-40
    • Smith, D.B.1    Johnson, K.S.2
  • 82
    • 0027445185 scopus 로고
    • Translation factors as effectors of cell growth and tumorigenesis
    • Sonenberg, N. 1993. Translation factors as effectors of cell growth and tumorigenesis. Curr. Opin. Cell Biol. 5:955-960.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 955-960
    • Sonenberg, N.1
  • 83
    • 0000831271 scopus 로고    scopus 로고
    • mRNA 5′ cap-binding protein eIF4E and control of cell growth
    • J. Hershey, M. Mathews, and N. Sonenberg (ed.), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Sonenberg, N. 1996. mRNA 5′ cap-binding protein eIF4E and control of cell growth, p. 245-270. In J. Hershey, M. Mathews, and N. Sonenberg (ed.), Translational control. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1996) Translational Control , pp. 245-270
    • Sonenberg, N.1
  • 84
    • 0031005361 scopus 로고    scopus 로고
    • Crystal structure of an hsp90-geldanamycin complex: Targeting of a protein chaperone by an antitumor agent
    • Stebbins, C. E., A. A. Russo, C. Schneider, N. Rosen, F. V. Hartl, and N. P. Pavletich. 1997. Crystal structure of an hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent. Cell 89:239-250.
    • (1997) Cell , vol.89 , pp. 239-250
    • Stebbins, C.E.1    Russo, A.A.2    Schneider, C.3    Rosen, N.4    Hartl, F.V.5    Pavletich, N.P.6
  • 86
    • 0029855773 scopus 로고    scopus 로고
    • The 58 kDa cellular inhibitor of the dsRNA-dependent protein kinase (PKR) requires the TPR 6 and DnaJ motifs to stimulate protein synthesis in vivo
    • Tang, N. M., C. Y. Ho, and M. G. Katze. 1996. The 58 kDa cellular inhibitor of the dsRNA-dependent protein kinase (PKR) requires the TPR 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
  • 87
    • 0030997120 scopus 로고    scopus 로고
    • Hsp90 is obligatory for the heme-regulated eIF-2 alpha kinase to acquire and maintain an activable conformation
    • Uma, S., S. D. Hartson, J. J. Chen, and R. L. Matts. 1997. Hsp90 is obligatory for the heme-regulated eIF-2 alpha kinase to acquire and maintain an activable conformation. J. Biol. Chem. 272:11648-11656.
    • (1997) J. Biol. Chem. , vol.272 , pp. 11648-11656
    • Uma, S.1    Hartson, S.D.2    Chen, J.J.3    Matts, R.L.4
  • 88
    • 0030896688 scopus 로고    scopus 로고
    • The heat shock protein 83 (Hsp83) is required for Raf-mediated signalling in Drosophila
    • van der Straten, A., C. Rommel, B. Dickson, and E. Hafen. 1997. The heat shock protein 83 (Hsp83) is required for Raf-mediated signalling in Drosophila. EMBO J. 16:1961-1969.
    • (1997) EMBO J. , vol.16 , pp. 1961-1969
    • Van Der Straten, A.1    Rommel, C.2    Dickson, B.3    Hafen, E.4
  • 89
    • 0343852938 scopus 로고    scopus 로고
    • Physical interaction between STAT1 and the interferon-induced protein kinase PKR and implications for interferon and double-stranded RNA signaling pathways
    • Wong, A. H.-T., N. W. N. Tam, Y.-L. Yang, A. R. Cuddihy, S. Li, S. Kirchoff, H. Hauser, T. Decker, and A. Koromilas. 1997. Physical interaction between STAT1 and the interferon-induced 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.5    Kirchoff, S.6    Hauser, H.7    Decker, T.8    Koromilas, A.9
  • 91
    • 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., J. Liu, and A. S. Lau. 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
  • 92
    • 0029995023 scopus 로고    scopus 로고
    • Characterization of cyclophilin 40: A highly conserved protein that directly associates with Hsp90
    • Yokoi, H., H. Kondo, A. Furuya, N. Hanai, J. E. Ikeda, and H. Anazawa. 1997. Characterization of cyclophilin 40: a highly conserved protein that directly associates with Hsp90. Biol. Pharm. Bull. 19:506-511.
    • (1997) Biol. Pharm. Bull. , vol.19 , pp. 506-511
    • Yokoi, H.1    Kondo, H.2    Furuya, A.3    Hanai, N.4    Ikeda, J.E.5    Anazawa, H.6


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