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Volumn 31, Issue 1, 1999, Pages 175-189

Abnormal levels and minimal activity of the dsRNA-activated protein kinase, PKR, in breast carcinoma cells

Author keywords

Apoptosis; Breast cancer; PKR; Translational regulation

Indexed keywords

DOUBLE STRANDED RNA; HEPARIN; INITIATION FACTOR 2; INTERFERON; PROTEIN INHIBITOR; PROTEIN KINASE;

EID: 0032967979     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1357-2725(98)00140-X     Document Type: Article
Times cited : (39)

References (88)
  • 1
    • 0030725442 scopus 로고    scopus 로고
    • The double-stranded RNA-dependent protein kinase PKR: Structure and function
    • M.J. Clemens, A. Elia, The double-stranded RNA-dependent protein kinase PKR: structure and function, J. Interferon Cytokine Res. 17 (1997) 503-524.
    • (1997) J. Interferon Cytokine Res. , vol.17 , pp. 503-524
    • Clemens, M.J.1    Elia, A.2
  • 2
    • 0030440591 scopus 로고    scopus 로고
    • The regulation of the protein kinase PKR by RNA
    • H.D. Robertson, M.B. Mathews, The regulation of the protein kinase PKR by RNA, Biochimie 78 (1996) 909-914.
    • (1996) Biochimie , vol.78 , pp. 909-914
    • Robertson, H.D.1    Mathews, M.B.2
  • 3
    • 0029968705 scopus 로고    scopus 로고
    • Initiation of protein synthesis in eukaryotic cells
    • V.M. Pain, Initiation of protein synthesis in eukaryotic cells, Eur. J. Biochem. 236 (1996) 747-771.
    • (1996) Eur. J. Biochem. , vol.236 , pp. 747-771
    • Pain, V.M.1
  • 4
    • 0030267336 scopus 로고    scopus 로고
    • The eIF2α kinases and the control of protein synthesis
    • C. DeHaro, The eIF2α kinases and the control of protein synthesis, FASEB J. 10 (1996) 1378-1387.
    • (1996) FASEB J. , vol.10 , pp. 1378-1387
    • Deharo, C.1
  • 5
    • 0028290902 scopus 로고
    • The interferon-induced double-stranded RNA-activated protein kinase induces apoptosis
    • S.B. Lee, M. Esteban, The interferon-induced double-stranded RNA-activated protein kinase induces apoptosis, Virol. 199 (1994) 491-496.
    • (1994) Virol. , vol.199 , pp. 491-496
    • Lee, S.B.1    Esteban, M.2
  • 6
    • 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
    • S.B. Lee, D. Rodriguez, J.R. Rodriguez, M. Esteban, 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 (1997) 81-88.
    • (1997) Virology , vol.231 , pp. 81-88
    • Lee, S.B.1    Rodriguez, D.2    Rodriguez, J.R.3    Esteban, M.4
  • 7
    • 0030992545 scopus 로고    scopus 로고
    • A dsRNA-activated protein kinase-dependent pathway mediating stress-induced apoptosis
    • S.D. Der, Y.L. Yang, C. Weissman, B.R. Williams, A dsRNA-activated protein kinase-dependent pathway mediating stress-induced apoptosis, Proc. Natl. Acad. Sci. 94 (1997) 3279-3283.
    • (1997) Proc. Natl. Acad. Sci. , vol.94 , pp. 3279-3283
    • Der, S.D.1    Yang, Y.L.2    Weissman, C.3    Williams, B.R.4
  • 8
    • 0031891869 scopus 로고    scopus 로고
    • Phosphorylation of eIF2 mediates apoptosis in response to activation of PKR
    • S.P. Srivastava, K.U. Kumar, R.J. Kaufman, Phosphorylation of eIF2 mediates apoptosis in response to activation of PKR, J. Biol. Chem. 273 (1998) 2416-2423.
    • (1998) J. Biol. Chem. , vol.273 , pp. 2416-2423
    • Srivastava, S.P.1    Kumar, K.U.2    Kaufman, R.J.3
  • 9
    • 25044477096 scopus 로고    scopus 로고
    • Activation of the dsRNA-dependent protein kinase, PKR, induces apoptosis and employs the death signal transducer FADD
    • in press
    • S. Balachandran, N. Kim, W.-C. Yeh, T.W. Mak, K. Bhalla, G.N. Barber, Activation of the dsRNA-dependent protein kinase, PKR, induces apoptosis and employs the death signal transducer FADD. EMBO J., in press.
    • EMBO J.
    • Balachandran, S.1    Kim, N.2    Yeh, W.-C.3    Mak, T.W.4    Bhalla, K.5    Barber, G.N.6
  • 11
    • 0026701570 scopus 로고
    • Malignant transformation by a mutant of the IFN-inducible dsRNA-dependent protein kinase
    • A.E. Koromilas, S. Roy, G.N. Barber, M. Katze, N. Sonenberg, Malignant transformation by a mutant of the IFN-inducible dsRNA-dependent protein kinase, Science 257 (1992) 1685-1689.
    • (1992) Science , vol.257 , pp. 1685-1689
    • Koromilas, A.E.1    Roy, S.2    Barber, G.N.3    Katze, M.4    Sonenberg, N.5
  • 12
  • 13
    • 0029061555 scopus 로고
    • Mutants of PKR lacking dsRNA binding domain I can act as transdominant inhibitors and induce malignant transformation
    • G. Barber, M. Wambach, S. Thompson, R. Jagus, M.G. Katze, Mutants of PKR lacking dsRNA binding domain I can act as transdominant inhibitors and induce malignant transformation, Mol. Cell. Biol. 15 (1995) 3138-3146.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3138-3146
    • Barber, G.1    Wambach, M.2    Thompson, S.3    Jagus, R.4    Katze, M.G.5
  • 14
    • 0029122270 scopus 로고
    • Molecular mechanisms responsible for malignant transformation by regulatory and catalytic domain variants of PKR
    • G.N. Barber, R. Jagus, E.F. Meurs, A. Hovanessian, M.G. Katze, Molecular mechanisms responsible for malignant transformation by regulatory and catalytic domain variants of PKR, J. Biol. Chem. 270 (1995) 17423-17428.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17423-17428
    • Barber, G.N.1    Jagus, R.2    Meurs, E.F.3    Hovanessian, A.4    Katze, M.G.5
  • 16
    • 0029118217 scopus 로고
    • Abrogation of translation initiation factor eIF-2 phosphorylation
    • O. Donze, R. Jagus, A.E. Koromilas, J.W.B. Hershey, N. Sonenberg, Abrogation of translation initiation factor eIF-2 phosphorylation, EMBO J. 14 (1995) 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    Sonenberg, N.5
  • 18
    • 0028978183 scopus 로고
    • Mice lacking p21CIP1/WAF1 undergo normal development, but are defective in G1 checkpoint control
    • C. Deng, P. Zhang, J.W. Harper, S.J. Elledge, P. Leder, Mice lacking p21CIP1/WAF1 undergo normal development, but are defective in G1 checkpoint control, Cell 82 (1995) 675-684.
    • (1995) Cell , vol.82 , pp. 675-684
    • Deng, C.1    Zhang, P.2    Harper, J.W.3    Elledge, S.J.4    Leder, P.5
  • 19
    • 1842374435 scopus 로고    scopus 로고
    • Cyclin dependent kinase inhibitors
    • J.W. Harper, Cyclin dependent kinase inhibitors, Cancer Surv. 29 (1997) 91-107.
    • (1997) Cancer Surv. , vol.29 , pp. 91-107
    • Harper, J.W.1
  • 20
    • 0031306844 scopus 로고    scopus 로고
    • The regulation of cyclin-dependent kinase inhibitors (CKIs)
    • M. Peter, The regulation of cyclin-dependent kinase inhibitors (CKIs), Progr. Cell Cycle Res. 3 (1997) 99-108.
    • (1997) Progr. Cell Cycle Res. , vol.3 , pp. 99-108
    • Peter, M.1
  • 21
    • 0029658030 scopus 로고    scopus 로고
    • The absence of p21Cip1/WAF1 alters keratinocyte growth and differentiation and promotes ras-tumor progression
    • C. Missero, F. Di Cunto, H. Kiyokawa, A. Koff, G.P. Dotto, The absence of p21Cip1/WAF1 alters keratinocyte growth and differentiation and promotes ras-tumor progression, Genes Dev. 10 (1996) 3065-3075.
    • (1996) Genes Dev. , vol.10 , pp. 3065-3075
    • Missero, C.1    Di Cunto, F.2    Kiyokawa, H.3    Koff, A.4    Dotto, G.P.5
  • 22
    • 0027179117 scopus 로고
    • Multiple steps in carcinogenesis involving alterations of multiple tumor suppressor genes
    • J. Yokota, T. Sugimura, Multiple steps in carcinogenesis involving alterations of multiple tumor suppressor genes, FASEB J. 7 (1993) 920-925.
    • (1993) FASEB J. , vol.7 , pp. 920-925
    • Yokota, J.1    Sugimura, T.2
  • 23
    • 0027272839 scopus 로고
    • Expression of p68 protein kinase as recognized by the monoclonal antibody TJ4C4 during human fetal development
    • G.K. Haines, G. Ghadge, J.A. Radosevich, Expression of p68 protein kinase as recognized by the monoclonal antibody TJ4C4 during human fetal development, Tumor Biol. 14 (1993) 95-104.
    • (1993) Tumor Biol. , vol.14 , pp. 95-104
    • Haines, G.K.1    Ghadge, G.2    Radosevich, J.A.3
  • 24
    • 0026669650 scopus 로고
    • Expression of PKR (p68) recognized by the monoclonal antibody TJ4C4 in human lung neoplasms
    • G.K. Haines, G.D. Ghadge, B. Thimmapaya, J.A. Radosevich, Expression of PKR (p68) recognized by the monoclonal antibody TJ4C4 in human lung neoplasms, Virch. Arch. B Cell Pathol. 62 (1992) 151-158.
    • (1992) Virch. Arch. B Cell Pathol. , vol.62 , pp. 151-158
    • Haines, G.K.1    Ghadge, G.D.2    Thimmapaya, B.3    Radosevich, J.A.4
  • 27
    • 0031456383 scopus 로고    scopus 로고
    • Elevated apoptotic cell population in patients with chronic fatigue syndrome: The pivotal role of protein kinase RNA
    • A. Vojdani, M. Ghoneum, P.C. Choppa, L. Magtoto, C.W. Lapp, Elevated apoptotic cell population in patients with chronic fatigue syndrome: the pivotal role of protein kinase RNA, J. Intern. Med. 242 (1997) 465-478.
    • (1997) J. Intern. Med. , vol.242 , pp. 465-478
    • Vojdani, A.1    Ghoneum, M.2    Choppa, P.C.3    Magtoto, L.4    Lapp, C.W.5
  • 29
    • 0031458299 scopus 로고    scopus 로고
    • Interferon-responsive protein kinase (p68) and proliferating cell nuclear antigen are inversely distributed in head and neck squamous cell carcinoma
    • G.K. Haines, R.J. Panos, P.M. Bak, T. Brown, M. Zielinski, J. Leyland, J.A. Radosevich, Interferon-responsive protein kinase (p68) and proliferating cell nuclear antigen are inversely distributed in head and neck squamous cell carcinoma, Tumor Biol. 19 (1998) 52-59.
    • (1998) Tumor Biol. , vol.19 , pp. 52-59
    • Haines, G.K.1    Panos, R.J.2    Bak, P.M.3    Brown, T.4    Zielinski, M.5    Leyland, J.6    Radosevich, J.A.7
  • 32
    • 0021275744 scopus 로고
    • Further characterization of the protein kinase activity mediated by interferon in mouse and human cells
    • B. Krust, J. Galabru, A.G. Hovanessian, Further characterization of the protein kinase activity mediated by interferon in mouse and human cells, J. Biol. Chem. 259 (1984) 8494-8498.
    • (1984) J. Biol. Chem. , vol.259 , pp. 8494-8498
    • Krust, B.1    Galabru, J.2    Hovanessian, A.G.3
  • 33
    • 0023665208 scopus 로고
    • Phosphorylation of eIF-2 during physiological stresses which affect protein synthesis
    • K.A. Scorsone, R. Panniers, A.G. Rowlands, E.C. Henshaw, Phosphorylation of eIF-2 during physiological stresses which affect protein synthesis, J. Biol. Chem. 262 (1987) 14538-14543.
    • (1987) J. Biol. Chem. , vol.262 , pp. 14538-14543
    • Scorsone, K.A.1    Panniers, R.2    Rowlands, A.G.3    Henshaw, E.C.4
  • 34
    • 0023708282 scopus 로고
    • Influenza virus regulates protein synthesis by repressing the autophosphorylation of PKR
    • M.G. Katze, J. Tomita, T. Black, B. Safer, A.G. Hovanessian, Influenza virus regulates protein synthesis by repressing the autophosphorylation of PKR, J. Virol. 62 (1988) 3710-3717.
    • (1988) J. Virol. , vol.62 , pp. 3710-3717
    • Katze, M.G.1    Tomita, J.2    Black, T.3    Safer, B.4    Hovanessian, A.G.5
  • 35
    • 0027163011 scopus 로고
    • Recombinant vaccinia virus K3L gene product prevents activation of double-stranded RNA-dependent initiation factor 2 alpha-specific protein kinase
    • K. Carroll, O. Elroy-Stein, B. Moss, R. Jagus, Recombinant vaccinia virus K3L gene product prevents activation of double-stranded RNA-dependent initiation factor 2 alpha-specific protein kinase, J. Biol. Chem. 268 (1993) 12837-12842.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12837-12842
    • Carroll, K.1    Elroy-Stein, O.2    Moss, B.3    Jagus, R.4
  • 36
    • 0024593159 scopus 로고
    • Cellular PKR is highly phosphorylated and activated yet significantly degraded during polio virus infection
    • T.L. Black, B. Safer, A.G. Hovanessian, M.G. Katze, Cellular PKR is highly phosphorylated and activated yet significantly degraded during polio virus infection, J. Virol. 63 (1989) 2244-2251.
    • (1989) J. Virol. , vol.63 , pp. 2244-2251
    • Black, T.L.1    Safer, B.2    Hovanessian, A.G.3    Katze, M.G.4
  • 37
    • 0344333720 scopus 로고
    • Purification of eIF-2:eIF-2B complex and its nucleotide exchange activity
    • A. Konieczny, B. Safer, Purification of eIF-2:eIF-2B complex and its nucleotide exchange activity, J. Biol. Chem. 258 (1982) 3402-3408.
    • (1982) J. Biol. Chem. , vol.258 , pp. 3402-3408
    • Konieczny, A.1    Safer, B.2
  • 38
    • 0031009311 scopus 로고    scopus 로고
    • Use of vertical slab gel isoelectric focusing and immunoblotting to evaluate steady state levels of eIF2α phosphorylation in cells
    • O. Savinova, R. Jagus, Use of vertical slab gel isoelectric focusing and immunoblotting to evaluate steady state levels of eIF2α phosphorylation in cells, Methods 11 (1997) 419-425.
    • (1997) Methods , vol.11 , pp. 419-425
    • Savinova, O.1    Jagus, R.2
  • 39
    • 0029070762 scopus 로고
    • Elevated levels of eIF4E mRNa in a broad spectrum of transformed cell lines
    • Y. Miyagi, A. Sugiyama, A. Asai, T. Okazaki, Y. Kuchino, S.J. Kerr, Elevated levels of eIF4E mRNA in a broad spectrum of transformed cell lines, Cancer Lett. 91 (1995) 247-252.
    • (1995) Cancer Lett. , vol.91 , pp. 247-252
    • Miyagi, Y.1    Sugiyama, A.2    Asai, A.3    Okazaki, T.4    Kuchino, Y.5    Kerr, S.J.6
  • 40
    • 0027289462 scopus 로고
    • Increased expression of eukaryotic initiation factors eIF-4E and eIF-2α in response to growth induction by c-myc
    • I.B. Rosenwald, D.B. Rhoads, L.D. Callanan, K.J. Isselbacher, E.V. Schmidt, Increased expression of eukaryotic initiation factors eIF-4E and eIF-2α in response to growth induction by c-myc, Proc. Natl. Acad. Sci. 90 (1993) 6175-6178.
    • (1993) Proc. Natl. Acad. Sci. , vol.90 , pp. 6175-6178
    • Rosenwald, I.B.1    Rhoads, D.B.2    Callanan, L.D.3    Isselbacher, K.J.4    Schmidt, E.V.5
  • 41
    • 0030111237 scopus 로고    scopus 로고
    • Deregulation of protein synthesis as a mechanism of neoplastic transformation
    • I.B. Rosenwald, Deregulation of protein synthesis as a mechanism of neoplastic transformation, BioEssays 18 (1996) 243-250.
    • (1996) BioEssays , vol.18 , pp. 243-250
    • Rosenwald, I.B.1
  • 42
    • 0029873363 scopus 로고    scopus 로고
    • Upregulated expression of the genes encoding eIF4E and eIF2α in transformed cells
    • I.B. Rosenwald, Upregulated expression of the genes encoding eIF4E and eIF2α in transformed cells, Cancer Lett. 102 (1996) 113-123.
    • (1996) Cancer Lett. , vol.102 , pp. 113-123
    • Rosenwald, I.B.1
  • 43
    • 0344074151 scopus 로고    scopus 로고
    • Expression of a translationally regulated, dominant-negative C/EBPβ isoform and upregulation of eIF2α are correlated with neoplastic transformation of mammary epithelial cells
    • B. Raught, A.-C. Gingras, A. James, D. Medina, N. Sonenberg, J.M. Rosen, Expression of a translationally regulated, dominant-negative C/EBPβ isoform and upregulation of eIF2α are correlated with neoplastic transformation of mammary epithelial cells, Cancer Lett. 59 (1996) 4382-4386.
    • (1996) Cancer Lett. , vol.59 , pp. 4382-4386
    • Raught, B.1    Gingras, A.-C.2    James, A.3    Medina, D.4    Sonenberg, N.5    Rosen, J.M.6
  • 44
    • 0027399614 scopus 로고
    • C-myc oncogene expression in estrogen-dependent and -independent breast cancer
    • R.P. Shiu, P.H. Watson, D. Dubik, c-myc oncogene expression in estrogen-dependent and -independent breast cancer, Clin. Chem. 39 (1993) 353-355.
    • (1993) Clin. Chem. , vol.39 , pp. 353-355
    • Shiu, R.P.1    Watson, P.H.2    Dubik, D.3
  • 45
    • 0028305728 scopus 로고
    • A key transcription factor for eIF2α is strongly homologous to developmental transcription factors and may link metabolic genes to cellular growth and development
    • B.J. Efiok, J.A. Chiorini, B. Safer, A key transcription factor for eIF2α is strongly homologous to developmental transcription factors and may link metabolic genes to cellular growth and development, J. Biol. Chem. 269 (1994) 18921-18930.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18921-18930
    • Efiok, B.J.1    Chiorini, J.A.2    Safer, B.3
  • 47
    • 0029996794 scopus 로고    scopus 로고
    • SV40 large-T antigen bypasses the translational block imposed by the phosphorylation of eIF2α
    • S. Swaminathan, P. Rajan, O. Savinova, R. Jagus, B. Thimmapaya, SV40 large-T antigen bypasses the translational block imposed by the phosphorylation of eIF2α, Virology 219 (1996) 321-323.
    • (1996) Virology , vol.219 , pp. 321-323
    • Swaminathan, S.1    Rajan, P.2    Savinova, O.3    Jagus, R.4    Thimmapaya, B.5
  • 48
    • 0028820772 scopus 로고
    • The interferon-inducible protein kinase, PKR, mediates the transcriptional activation of the immunoglobulin κ gene
    • A. Koromilas, C. Cantin, A. Craig, R. Jagus, J. Hiscott, N. Sonenberg, The interferon-inducible protein kinase, PKR, mediates the transcriptional activation of the immunoglobulin κ gene, J. Biol. Chem. 270 (1995) 25426-25434.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25426-25434
    • Koromilas, A.1    Cantin, C.2    Craig, A.3    Jagus, R.4    Hiscott, J.5    Sonenberg, N.6
  • 50
    • 17544376424 scopus 로고    scopus 로고
    • Modulations of IFN-inducible gene expression by retinoic acid: Upregulation of STAT1 in IFN-unresponsive cells
    • V. Kolla, D.J. Lindner, W. Xiao, E.C. Borden, D.V. Kalvakolanu, Modulations of IFN-inducible gene expression by retinoic acid: upregulation of STAT1 in IFN-unresponsive cells, J. Biol. Chem. 271 (1996) 10508-10514.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10508-10514
    • Kolla, V.1    Lindner, D.J.2    Xiao, W.3    Borden, E.C.4    Kalvakolanu, D.V.5
  • 51
    • 0023696578 scopus 로고
    • A heat-sensitive inhibitor in poliovirus-infected cells which selectively blocks phosphorylation of eIF-2α by PKR
    • L.J. Ransome, A. Dasgupta, A heat-sensitive inhibitor in poliovirus-infected cells which selectively blocks phosphorylation of eIF-2α by PKR, J. Virol. 62 (1988) 3551-3557.
    • (1988) J. Virol. , vol.62 , pp. 3551-3557
    • Ransome, L.J.1    Dasgupta, A.2
  • 52
    • 0025298202 scopus 로고
    • Molecular cloning and characterization of the double-stranded, RNA-activated protein kinase induced by interferon
    • E. Meurs, K. Chong, J. Galabru, N.S. Thomas, I.M. Kerr, B.R.G. Williams, A.G. Hovanessian, Molecular cloning and characterization of the double-stranded, RNA-activated protein kinase induced by interferon, Cell 62 (1990) 379-390
    • (1990) Cell , vol.62 , pp. 379-390
    • Meurs, E.1    Chong, K.2    Galabru, J.3    Thomas, N.S.4    Kerr, I.M.5    Williams, B.R.G.6    Hovanessian, A.G.7
  • 53
    • 0024078349 scopus 로고
    • Effects of mutations in stem and loop regions on the structure and function of adenovirus VA RNA
    • K. Mellits, M.B. Mathews, Effects of mutations in stem and loop regions on the structure and function of adenovirus VA RNA, EMBO J. 7 (1988) 2849-2859.
    • (1988) EMBO J. , vol.7 , pp. 2849-2859
    • Mellits, K.1    Mathews, M.B.2
  • 54
    • 0025746604 scopus 로고
    • Functional expression and characterization of interferon-induced double-stranded RNA activated P68 protein kinase from Escherichia coli
    • G.N. Barber, T. Tomita, A.G. Hovanessian, E. Meurs, M.G. Katze, Functional expression and characterization of interferon-induced double-stranded RNA activated P68 protein kinase from Escherichia coli, Biochem. 30 (1991) 10356-10361.
    • (1991) Biochem. , vol.30 , pp. 10356-10361
    • Barber, G.N.1    Tomita, T.2    Hovanessian, A.G.3    Meurs, E.4    Katze, M.G.5
  • 55
    • 0025361887 scopus 로고
    • Interaction of adenovirus VAI RNA with PKR: Nonequivalence of binding and function
    • K.H. Mellits, M. Kostura, M.B. Mathews, Interaction of adenovirus VAI RNA with PKR: nonequivalence of binding and function, Cell 61 (1990) 843-852.
    • (1990) Cell , vol.61 , pp. 843-852
    • Mellits, K.H.1    Kostura, M.2    Mathews, M.B.3
  • 56
    • 0027487288 scopus 로고
    • Comparative analysis of the regulation of PKR by Epstein-Barr virus RNAs, EBER-1 and EBER-2 and adenovirus VA1 RNA
    • T.V. Sharp, Q. Xiao, D.R. Gewert, M.J. Clemens, Comparative analysis of the regulation of PKR by Epstein-Barr virus RNAs, EBER-1 and EBER-2 and adenovirus VA1 RNA, Nucleic Acids Res. 21 (1993) 4483-4489.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 4483-4489
    • Sharp, T.V.1    Xiao, Q.2    Gewert, D.R.3    Clemens, M.J.4
  • 57
    • 0026511984 scopus 로고
    • Role of the apical stem in maintaining structure and function of adenovirus-associated RNAs
    • K.H. Mellits, T. Pe'ery, M.B. Mathews, Role of the apical stem in maintaining structure and function of adenovirus-associated RNAs, J. Virol. 66 (1992) 2369-2377.
    • (1992) J. Virol. , vol.66 , pp. 2369-2377
    • Mellits, K.H.1    PE'Ery, T.2    Mathews, M.B.3
  • 58
    • 0000335423 scopus 로고
    • Games viruses play: A strategic initiative against PKR
    • M.G. Katze, Games viruses play: a strategic initiative against PKR, Seminars Virol. 4 (1993) 259-268.
    • (1993) Seminars Virol. , vol.4 , pp. 259-268
    • Katze, M.G.1
  • 59
    • 0028589116 scopus 로고
    • Proteins that interact with PKR
    • R. Jagus, M.E. Gray, Proteins that interact with PKR, Biochimie 76 (1994) 779-791.
    • (1994) Biochimie , vol.76 , pp. 779-791
    • Jagus, R.1    Gray, M.E.2
  • 60
    • 0030585155 scopus 로고    scopus 로고
    • When two strands are better than one: The mediators and modulators of the cellular responses to double-stranded RNA
    • B.L. Jacobs, J.O. Langland, When two strands are better than one: the mediators and modulators of the cellular responses to double-stranded RNA, Virology 219 (1996) 339-349.
    • (1996) Virology , vol.219 , pp. 339-349
    • Jacobs, B.L.1    Langland, J.O.2
  • 61
    • 0025180598 scopus 로고
    • Purification and partial characterization of an inhibitor of PKR during influenza virus infection
    • T.G. Lee, J. Tomita, A.G. Hovanessian, M.G. Katze, Purification and partial characterization of an inhibitor of PKR during influenza virus infection, Proc. Natl. Acad. Sci. 87 (1990) 6208-6212.
    • (1990) Proc. Natl. Acad. Sci. , vol.87 , pp. 6208-6212
    • Lee, T.G.1    Tomita, J.2    Hovanessian, A.G.3    Katze, M.G.4
  • 62
    • 0026628369 scopus 로고
    • Characterization and regulation of the 58 kDa cellular inhibitor of PKR
    • T.G. Lee, J. Tomita, A.G. Hovanessian, M.G. Katze, Characterization and regulation of the 58 kDa cellular inhibitor of PKR, J. Biol. Chem. 267 (1992) 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
  • 64
    • 0027949937 scopus 로고
    • The 58-kDa cellular inhibitor of PKR is a member of the TPR family of proteins
    • T.G. Lee, N. Tang, S. Thompson, J. Miller, M.G. Katze, The 58-kDa cellular inhibitor of PKR is a member of the TPR family of proteins, Mol. Cell. Biol. 14 (1994) 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
  • 65
    • 8944219769 scopus 로고    scopus 로고
    • Interaction of the interferon-induced kinase, PKR, with inhibitory proteins p58 and vaccinia virus K3L is mediated by unique domains -implications for kinase function
    • M. Gale, S.L. Tan, M. Wambach, M.G. Katze, Interaction of the interferon-induced kinase, PKR, with inhibitory proteins p58 and vaccinia virus K3L is mediated by unique domains -implications for kinase function, Mol. Cell. Biol. 16 (1996) 4172-4181.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 4172-4181
    • Gale, M.1    Tan, S.L.2    Wambach, M.3    Katze, M.G.4
  • 66
    • 0031013877 scopus 로고    scopus 로고
    • The molecular chaperone hsp40 regulates the activity of p58, the cellular inhibitor of PKR
    • M.W. Melville, W.J. Hansen, B.C. Freeman, W.J. Welch, M.G. Katze, The molecular chaperone hsp40 regulates the activity of p58, the cellular inhibitor of PKR, Proc. Natl. Acad. Sci. 94 (1997) 97-102.
    • (1997) Proc. Natl. Acad. Sci. , vol.94 , pp. 97-102
    • Melville, M.W.1    Hansen, W.J.2    Freeman, B.C.3    Welch, W.J.4    Katze, M.G.5
  • 67
    • 2642648639 scopus 로고    scopus 로고
    • Regulation of interferon-induced protein kinase PKR: Modulation of P58IPK inhibitory function by a novel protein, P52rIPK
    • M. Gale, C.M. Blakely, D.A. Hopkins, M.W. Melville, M. Wambach, P.R. Romano, M.G. Katze, Regulation of interferon-induced protein kinase PKR: modulation of P58IPK inhibitory function by a novel protein, P52rIPK, Mol. Cell. Biol. 18 (1998) 859-871.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 859-871
    • Gale, M.1    Blakely, C.M.2    Hopkins, D.A.3    Melville, M.W.4    Wambach, M.5    Romano, P.R.6    Katze, M.G.7
  • 68
    • 0026575232 scopus 로고
    • The eIF2-associated 67-kDa polypeptide (p67) plays a critical role in the regulation of protein synthesis in animal cells
    • M.K. Ray, B. Datta, A. Chakraborty, A. Chattopadhyay, S. Meza-Keuthen, N.K. Gupta, The eIF2-associated 67-kDa polypeptide (p67) plays a critical role in the regulation of protein synthesis in animal cells, Proc. Natl. Acad. Sci. 89 (1992) 539-543.
    • (1992) Proc. Natl. Acad. Sci. , vol.89 , pp. 539-543
    • Ray, M.K.1    Datta, B.2    Chakraborty, A.3    Chattopadhyay, A.4    Meza-Keuthen, S.5    Gupta, N.K.6
  • 69
    • 0025819309 scopus 로고
    • Partial characterization of a cellular factor that regulates dsRNA-dependent eIF-2α kinase in 3T3-F442a fibroblasts
    • R. Judware, R. Petryshyn, Partial characterization of a cellular factor that regulates dsRNA-dependent eIF-2α kinase in 3T3-F442A fibroblasts, Mol. Cell. Biol. 11 (1991) 3259-3267.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 3259-3267
    • Judware, R.1    Petryshyn, R.2
  • 70
    • 0026787750 scopus 로고
    • Mechanism of action of a cellular inhibitor of the dsRNA-dependent protein kinase from 3T3-F442a cells
    • R. Judware, R. Petryshyn, Mechanism of action of a cellular inhibitor of the dsRNA-dependent protein kinase from 3T3-F442A cells, J. Biol. Chem. 267 (1992) 21685-21690.
    • (1992) J. Biol. Chem. , vol.267 , pp. 21685-21690
    • Judware, R.1    Petryshyn, R.2
  • 71
    • 0026343517 scopus 로고
    • Inhibitor of interferon-induced dsRNA-dependent protein kinase
    • S. Saito, M. Kawakita, Inhibitor of interferon-induced dsRNA-dependent protein kinase, Microbiol. Immunol. 35 (1991) 1105-1114.
    • (1991) Microbiol. Immunol. , vol.35 , pp. 1105-1114
    • Saito, S.1    Kawakita, M.2
  • 72
    • 0025223478 scopus 로고
    • Enhancement of the interferon-induced dsRNA-dependent protein kinase by Sindbis virus infection and heat-shock stress
    • S. Saito, Enhancement of the interferon-induced dsRNA-dependent protein kinase by Sindbis virus infection and heat-shock stress, Microbiol. Immunol. 34 (1990) 859-870.
    • (1990) Microbiol. Immunol. , vol.34 , pp. 859-870
    • Saito, S.1
  • 73
    • 0026481080 scopus 로고
    • Oncogenic ras induces inhibition of PKR
    • L.J. Mundschau, D.V. Faller, Oncogenic ras induces inhibition of PKR, J. Biol. Chem. 267 (1992) 23092-23098.
    • (1992) J. Biol. Chem. , vol.267 , pp. 23092-23098
    • Mundschau, L.J.1    Faller, D.V.2
  • 74
    • 0028558943 scopus 로고
    • Endogenous inhibitors of PKR in normal and ras transformed cells
    • L.J. Mundschau, D.V. Faller, Endogenous inhibitors of PKR in normal and ras transformed cells, Biochimie 76 (1994) 792-800.
    • (1994) Biochimie , vol.76 , pp. 792-800
    • Mundschau, L.J.1    Faller, D.V.2
  • 75
    • 0027966119 scopus 로고
    • IL-3 stimulates protein synthesis by regulating dsRNA-dependent protein kinase (PKR)
    • T. Ito, R. Jagus, S. May, IL-3 stimulates protein synthesis by regulating dsRNA-dependent protein kinase (PKR), Proc. Natl. Acad. Sci. 91 (1994) 7455-7459.
    • (1994) Proc. Natl. Acad. Sci. , vol.91 , pp. 7455-7459
    • Ito, T.1    Jagus, R.2    May, S.3
  • 76
    • 0029670477 scopus 로고    scopus 로고
    • Translational control of p27Kip1 accumulation during the cell cycle
    • L. Hengst, S.I. Reed, Translational control of p27Kip1 accumulation during the cell cycle, Science 271 (1996) 1861-1864.
    • (1996) Science , vol.271 , pp. 1861-1864
    • Hengst, L.1    Reed, S.I.2
  • 77
    • 15144357686 scopus 로고    scopus 로고
    • Enhanced ribosomal association of p27(Kip1) mRNa is a mechanism contributing to accumulation during growth arrest
    • S.S. Millard, J.S. Yan, H. Nguyen, M. Pagano, H. Kiyokawa, A. Koff, Enhanced ribosomal association of p27(Kip1) mRNA is a mechanism contributing to accumulation during growth arrest, J. Biol. Chem. 272 (1997) 7093-7098.
    • (1997) J. Biol. Chem. , vol.272 , pp. 7093-7098
    • Millard, S.S.1    Yan, J.S.2    Nguyen, H.3    Pagano, M.4    Kiyokawa, H.5    Koff, A.6
  • 78
    • 0026698263 scopus 로고
    • Association of human cyclin e with a periodic G1-S phase protein kinase
    • V. Dulic, S. Lee, S. Reed, Association of human cyclin E with a periodic G1-S phase protein kinase, Science 257 (1992) 1958-1961.
    • (1992) Science , vol.257 , pp. 1958-1961
    • Dulic, V.1    Lee, S.2    Reed, S.3
  • 79
    • 0028988585 scopus 로고
    • Inhibitors of mammalian G1 cyclin-dependent kinases
    • C.J. Sherr, J.M. Roberts, Inhibitors of mammalian G1 cyclin-dependent kinases, Genes Dev. 9 (1995) 1149-1163.
    • (1995) Genes Dev. , vol.9 , pp. 1149-1163
    • Sherr, C.J.1    Roberts, J.M.2
  • 81
    • 0031048716 scopus 로고    scopus 로고
    • Expression of cell cycle regulators p27 and cyclin E, alone or in combination, correlate with survival in young breast cancer patients
    • P.L. Porter, K.E. Malone, P.J. Heagerty, G. M. Alexander, L.A. Gatti, E.J. Firpo, J.R. Daling, J.M. Roberts, Expression of cell cycle regulators p27 and cyclin E, alone or in combination, correlate with survival in young breast cancer patients, Nature Med. 3 (1997) 222-225.
    • (1997) Nature Med. , vol.3 , pp. 222-225
    • Porter, P.L.1    Malone, K.E.2    Heagerty, P.J.3    Alexander, G.M.4    Gatti, L.A.5    Firpo, E.J.6    Daling, J.R.7    Roberts, J.M.8
  • 82
    • 0031283125 scopus 로고    scopus 로고
    • Overexpression of C/EBPbeta-LIP, a naturally occurring, dominant-negative transcription factor, in human breast cancer
    • C.A. Zahnow, P. Younes, R. Laucirica, J.M. Rosen, Overexpression of C/EBPbeta-LIP, a naturally occurring, dominant-negative transcription factor, in human breast cancer, J. Natl. Cancer Inst. 89 (1997) 1887-1891
    • (1997) J. Natl. Cancer Inst. , vol.89 , pp. 1887-1891
    • Zahnow, C.A.1    Younes, P.2    Laucirica, R.3    Rosen, J.M.4
  • 83
    • 0031283125 scopus 로고    scopus 로고
    • Overexpression of C/EBPbeta-LIP, a naturally occurring, dominant-negative transcription factor, in human breast cancer
    • C.A. Zahnow, P. Younes, R. Laucirica, J.M. Rosen, Overexpression of C/EBPbeta-LIP, a naturally occurring, dominant-negative transcription factor, in human breast cancer, J. Natl. Cancer Inst. 89 (1997) 1887-1891.
    • (1997) J. Natl. Cancer Inst. , vol.89 , pp. 1887-1891
    • Zahnow, C.A.1    Younes, P.2    Laucirica, R.3    Rosen, J.M.4
  • 84
    • 0028013216 scopus 로고
    • LAP (NF-IL-6), a tissue-specific transcriptional activator, is an inhibitor of hepatoma cell proliferation
    • M. Buck, H. Turler, M. Chojkier, LAP (NF-IL-6), a tissue-specific transcriptional activator, is an inhibitor of hepatoma cell proliferation, EMBO J. 13 (1994) 851-860.
    • (1994) EMBO J. , vol.13 , pp. 851-860
    • Buck, M.1    Turler, H.2    Chojkier, M.3
  • 86
    • 0029045784 scopus 로고
    • Reduced expression of proapoptotic gene BAX is associated with poor response rates to combination chemotherapy and shorter survival in women with metastatic breast adenocarcinoma
    • S. Krajewski, C. Blomqvist, K. Franssila, M. Krajewska, V.M. Wasenius, E. Niskanen, S. Nordling, J.C. Reed, Reduced expression of proapoptotic gene BAX is associated with poor response rates to combination chemotherapy and shorter survival in women with metastatic breast adenocarcinoma, Cancer Res. 55 (1995) 4471-4478.
    • (1995) Cancer Res. , vol.55 , pp. 4471-4478
    • Krajewski, S.1    Blomqvist, C.2    Franssila, K.3    Krajewska, M.4    Wasenius, V.M.5    Niskanen, E.6    Nordling, S.7    Reed, J.C.8
  • 87
    • 0030803256 scopus 로고    scopus 로고
    • Translational regulation of yeast GCN4. a window on factors that control initiator-tRNa binding to the ribosome
    • A.G. Hinnebusch, Translational regulation of yeast GCN4. A window on factors that control initiator-tRNA binding to the ribosome, J. Biol. Chem. 272 (1997) 21661-21664.
    • (1997) J. Biol. Chem. , vol.272 , pp. 21661-21664
    • Hinnebusch, A.G.1
  • 88
    • 0030162560 scopus 로고    scopus 로고
    • Balancing cell life and death: Bax, apoptosis and breast cancer
    • J.C. Reed, Balancing cell life and death: bax, apoptosis and breast cancer, J. Clin. Invest. 97 (1996) 2403-2404.
    • (1996) J. Clin. Invest. , vol.97 , pp. 2403-2404
    • Reed, J.C.1


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