The dsRNA protein kinase PKR: Virus and cell control

Biochimie

Volumn 89, Issue 6-7, 2007, Pages 799-811

  Garcia M A ^a   Meurs, E F ^b   Esteban, M ^a  

^a CENTRO NACIONAL DE BIOTECNOLOGÍA   (Spain)

^b INSTITUT PASTEUR   (France)

Author keywords

Anticellular; Antiviral; Apoptosis; dsRNA dependent enzyme; Modulation; PKR; Protein kinase; Signal transduction; Translational control

Indexed keywords

ACTIVATING TRANSCRIPTION FACTOR 3; APOPTOTIC PROTEASE ACTIVATING FACTOR 1; CASPASE 8; CASPASE 9; CELL PROTEIN; DOUBLE STRANDED RNA; FAS ASSOCIATED DEATH DOMAIN PROTEIN; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERFERON; NUCLEOPHOSMIN; PROTEIN E3L; PROTEIN K3L; PROTEIN KINASE INHIBITOR; PROTEIN KINASE R; PROTEIN MDA7; PROTEIN P53; PROTEIN P58; PROTEIN RAX; UNCLASSIFIED DRUG; VIRUS PROTEIN; VIRUS RNA;

AMINO TERMINAL SEQUENCE; CELL DIFFERENTIATION; CELL GROWTH; ENZYME ACTIVATION; ENZYME MECHANISM; ENZYME PHOSPHORYLATION; ENZYME REGULATION; GENE EXPRESSION REGULATION; GENE FUNCTION; HUMAN; MITOCHONDRIAL RESPIRATION; NONHUMAN; ONCOGENE; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN MOTIF; PROTEIN RNA BINDING; REVIEW; TRANSCRIPTION REGULATION; TRANSLATION REGULATION; VIRUS CELL INTERACTION; VIRUS INFECTION; VIRUS INHIBITION; VIRUS REPLICATION;

AMINO ACID MOTIFS; ANIMALS; ANTIVIRAL AGENTS; APOPTOSIS; CELL PROLIFERATION; EIF-2 KINASE; GENE EXPRESSION REGULATION; GENE EXPRESSION REGULATION, VIRAL; HUMANS; MODELS, BIOLOGICAL; NF-KAPPA B; PROTEIN BIOSYNTHESIS; PROTEIN STRUCTURE, TERTIARY; RNA, MESSENGER; SIGNAL TRANSDUCTION;

MAMMALIA;

EID: 34347225099     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2007.03.001     Document Type: Review

References (207)

1. Samuel C.E. Antiviral actions of interferon. Interferon-regulated cellular proteins and their surprisingly selective antiviral activities. Virology 183 1 (1991) 1-11
2. Sen G.C., and Lengyel P. The interferon system. A bird's eye view of its biochemistry. J. Biol. Chem. 267 8 (1992) 5017-5020
3. Stark G.R., Kerr I.M., Williams B.R., Silverman R.H., and Schreiber R.D. How cells respond to interferons. Annu. Rev. Biochem. 67 (1998) 227-264
4. Pestka S., Krause C.D., and Walter M.R. Interferons, interferon-like cytokines, and their receptors. Immunol. Rev. 202 (2004) 8-32
5. Garcia M.A., Gil J., Ventoso I., Guerra S., Domingo E., Rivas C., et al. Impact of protein kinase PKR in cell biology: from antiviral to antiproliferative action. Microbiol. Mol. Biol. Rev. 70 4 (2006) 1032-1060
6. Metz D.H., and Esteban M. Interferon inhibits viral protein synthesis in L cells infected with vaccinia virus. Nature 238 5364 (1972) 385-388
7. Friedman R.M., Metz D.H., Esteban R.M., Tovell D.R., Ball L.A., and Kerr I.M. Mechanism of interferon action: inhibition of viral messenger ribonucleic acid translation in L-cell extracts. J. Virol. 10 6 (1972) 1184-1198
8. Colby C., and Duesberg P.H. Double-stranded RNA in vaccinia virus infected cells. Nature 222 5197 (1969) 940-944
9. Ehrenfeld E., and Hunt T. Double-stranded poliovirus RNA inhibits initiation of protein synthesis by reticulocyte lysates. Proc. Natl. Acad. Sci. U.S.A. 68 5 (1971) 1075-1078
10. Cordell-Stewart B., and Taylor M.W. Effect of viral double-stranded RNA on mammalian cells in culture: cytotoxicity under conditions preventing viral replication and protein synthesis. J. Virol. 12 2 (1973) 360-366
11. Kerr I.M., Brown R.E., and Ball L.A. Increased sensitivity of cell-free protein synthesis to double-stranded RNA after interferon treatment. Nature 250 461 (1974) 57-59
12. Farrell P.J., Balkow K., Hunt T., Jackson R.J., and Trachsel H. Phosphorylation of initiation factor elF-2 and the control of reticulocyte protein synthesis. Cell 11 1 (1977) 187-200
13. Hovanessian A.G., and Kerr I.M. The (2′-5′) oligoadenylate (pppA2′-5′A2′-5′A) synthetase and protein kinase(s) from interferon-treated cells. Eur. J. Biochem. 93 3 (1979) 515-526
14. Krust B., Galabru J., and Hovanessian A.G. Further characterisation of the protein kinase activity mediated by interferon in mouse and human cells. J. Biol. Chem. 259 13 (1984) 8494-8498
15. Laurent A.G., Krust B., Galabru J., Svab J., and Hovanessian A.G. Monoclonal antibodies to an interferon-induced Mr 68,000 protein and their use for the detection of double-stranded RNA-dependent protein kinase in human cells. Proc. Natl. Acad. Sci. U.S.A. 82 13 (1985) 4341-4345
16. Meurs E., Chong K., Galabru J., Thomas N.S., Kerr I.M., Williams B.R., et al. Molecular cloning and characterization of the human double-stranded RNA-activated protein kinase induced by interferon. Cell 62 2 (1990) 379-390
17. Galabru J., Katze M.G., Robert N., and Hovanessian A.G. The binding of double-stranded RNA and adenovirus VAI RNA to the interferon-induced protein kinase. Eur. J. Biochem. 178 3 (1989) 581-589
18. Hovanessian A.G., Galabru J., Riviere Y., and Montagnier L. Efficiency of poly(A).poly(U) as an adjuvant. Immunol. Today 9 6 (1988) 161-162
19. Clemens M.J., Hershey J.W., Hovanessian A.C., Jacobs B.C., Katze M.G., Kaufman R.J., et al. PKR: proposed nomenclature for the RNA-dependent protein kinase induced by interferon. J. Interferon Res. 13 3 (1993) 241
20. Galabru J., and Hovanessian A. Autophosphorylation of the protein kinase dependent on double-stranded RNA. J. Biol. Chem. 262 32 (1987) 15538-15544
21. Hovanessian A.G. The double stranded RNA-activated protein kinase induced by interferon: dsRNA-PK. J. Interferon Res. 9 6 (1989) 641-647
22. Rhoads R.E. Regulation of eukaryotic protein synthesis by initiation factors. J. Biol. Chem. 268 5 (1993) 3017-3020
23. Kumar A., Haque J., Lacoste J., Hiscott J., and Williams B.R. Double-stranded RNA-dependent protein kinase activates transcription factor NF-kappa B by phosphorylating I kappa B. Proc. Natl. Acad. Sci. U.S.A. 91 14 (1994) 6288-6292
24. Koromilas A.E., Roy S., Barber G.N., Katze M.G., and Sonenberg N. Malignant transformation by a mutant of the IFN-inducible dsRNA-dependent protein kinase. Science 257 5077 (1992) 1685-1689
25. Lengyel P. Tumor-suppressor genes: news about the interferon connection. Proc. Natl. Acad. Sci. U.S.A. 90 13 (1993) 5893-5895
26. Meurs E.F., Galabru J., Barber G.N., Katze M.G., and Hovanessian A.G. Tumor suppressor function of the interferon-induced double-stranded RNA-activated protein kinase. Proc. Natl. Acad. Sci. U.S.A. 90 1 (1993) 232-236
27. Ito T., Yang M., and May W.S. RAX, a cellular activator for double-stranded RNA-dependent protein kinase during stress signaling. J. Biol. Chem. 274 22 (1999) 15427-15432
28. Patel R.C., and Sen G.C. PACT, a protein activator of the interferon-induced protein kinase, PKR. EMBO J. 17 15 (1998) 4379-4390
29. Goh K.C., deVeer M.J., and Williams B.R. The protein kinase PKR is required for p38 MAPK activation and the innate immune response to bacterial endotoxin. EMBO J. 19 16 (2000) 4292-4297
30. Jiang Z., Zamanian-Daryoush M., Nie H., Silva A.M., Williams B.R., and Li X. Poly(I-C)-induced Toll-like receptor 3 (TLR3)-mediated activation of NFkappa B and MAP kinase is through an interleukin-1 receptor-associated kinase (IRAK)-independent pathway employing the signaling components TLR3-TRAF6-TAK1-TAB2-PKR. J. Biol. Chem. 278 19 (2003) 16713-16719
31. Williams B.R. Signal integration via PKR. Sci. STKE 2001 89 (2001) RE2
32. Verma I.M., Stevenson J.K., Schwarz E.M., Van Antwerp D., and Miyamoto S. Rel/NF-kappa B/I kappa B family: intimate tales of association and dissociation. Genes Dev. 9 22 (1995) 2723-2735
33. Clemens M.J. PKR-a protein kinase regulated by double-stranded RNA. Int J. Biochem Cell Biol. 29 7 (1997) 945-949
34. Nanduri S., Carpick B., Yang Y., Williams B.R., and Qin J. 1H, 13C, 15N resonance assignment of the 20 kDa double stranded RNA binding domain of PKR. J. Biomol. NMR 12 2 (1998) 349-351
35. Dey M., Cao C., Dar A.C., Tamura T., Ozato K., Sicheri F., et al. Mechanistic link between PKR dimerization, autophosphorylation, and eIF2alpha substrate recognition. Cell 122 6 (2005) 901-913
36. Zhang F., Romano P.R., Nagamura-Inoue T., Tian B., Dever T.E., Mathews M.B., et al. Binding of double-stranded RNA to protein kinase PKR is required for dimerization and promotes critical autophosphorylation events in the activation loop. J. Biol. Chem. 276 27 (2001) 24946-24958
37. Dar A.C., Dever T.E., and Sicheri F. Higher-order substrate recognition of eIF2alpha by the RNA-dependent protein kinase PKR. Cell 122 6 (2005) 887-900
38. Guerra S., Lopez-Fernandez L.A., Garcia M.A., Zaballos A., and Esteban M. Human gene profiling in response to the active protein kinase, interferon-induced serine/threonine protein kinase (PKR), in infected cells. Involvement of the transcription factor ATF-3 IN PKR-induced apoptosis. J. Biol. Chem. 281 27 (2006) 18734-18745
39. Donze O., Deng J., Curran J., Sladek R., Picard D., and Sonenberg N. The protein kinase PKR: a molecular clock that sequentially activates survival and death programs. EMBO J. 23 3 (2004) 564-571
40. Kazemi S., Papadopoulou S., Li S., Su Q., Wang S., Yoshimura A., et al. Control of alpha subunit of eukaryotic translation initiation factor 2 (eIF2 alpha) phosphorylation by the human papillomavirus type 18 E6 oncoprotein: implications for eIF2 alpha-dependent gene expression and cell death. Mol. Cell. Biol. 24 8 (2004) 3415-3429
41. Williams B.R. PKR; a sentinel kinase for cellular stress. Oncogene 18 45 (1999) 6112-6120
42. Lee S.B., Melkova Z., Yan W., Williams B.R., Hovanessian A.G., and Esteban M. The interferon-induced double-stranded RNA-activated human p68 protein kinase potently inhibits protein synthesis in cultured cells. Virology 192 1 (1993) 380-385
43. Lee S.B., Bablanian R., and Esteban M. Regulated expression of the interferon-induced protein kinase p68 (PKR) by vaccinia virus recombinants inhibits the replication of vesicular stomatitis virus but not that of poliovirus. J. Interferon Cytokine Res. 16 12 (1996) 1073-1078
44. Balachandran S., Roberts P.C., Brown L.E., Truong H., Pattnaik A.K., Archer D.R., et al. Essential role for the dsRNA-dependent protein kinase PKR in innate immunity to viral infection. Immunity 13 1 (2000) 129-141
45. Stojdl D.F., Abraham N., Knowles S., Marius R., Brasey A., Lichty B.D., et al. The murine double-stranded RNA-dependent protein kinase PKR is required for resistance to vesicular stomatitis virus. J. Virol. 74 20 (2000) 9580-9585
46. Su Q., Wang S., Baltzis D., Qu L.K., Wong A.H., and Koromilas A.E. Tyrosine phosphorylation acts as a molecular switch to full-scale activation of the eIF2alpha RNA-dependent protein kinase. Proc. Natl. Acad. Sci. U.S.A. 103 1 (2006) 63-68
47. Hershey J.W. Translational control in mammalian cells. Annu. Rev. Biochem. 60 (1991) 717-755
48. Majumdar R., and Maitra U. Regulation of GTP hydrolysis prior to ribosomal AUG selection during eukaryotic translation initiation. EMBO J. 24 21 (2005) 3737-3746
49. Sudhakar A., Ramachandran A., Ghosh S., Hasnain S.E., Kaufman R.J., and Ramaiah K.V. Phosphorylation of serine 51 in initiation factor 2 alpha (eIF2 alpha) promotes complex formation between eIF2 alpha(P) and eIF2B and causes inhibition in the guanine nucleotide exchange activity of eIF2B. Biochemistry 39 42 (2000) 12929-12938
50. Zhu S., Romano P.R., and Wek R.C. 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 22 (1997) 14434-14441
51. Kumar K.U., Srivastava S.P., and Kaufman R.J. Double-stranded RNA-activated protein kinase (PKR) is negatively regulated by 60S ribosomal subunit protein L18. Mol. Cell. Biol. 19 2 (1999) 1116-1125
52. Wu S., Kumar K.U., and Kaufman R.J. Identification and requirement of three ribosome binding domains in dsRNA-dependent protein kinase (PKR). Biochemistry 37 39 (1998) 13816-13826
53. Kaufman R.J., Davies M.V., Pathak V.K., and Hershey J.W. The phosphorylation state of eucaryotic initiation factor 2 alters translational efficiency of specific mRNAs. Mol. Cell. Biol. 9 3 (1989) 946-958
54. Ben-Asouli Y., Banai Y., Pel-Or Y., Shir A., and Kaempfer R. Human interferon-gamma mRNA autoregulates its translation through a pseudoknot that activates the interferon-inducible protein kinase PKR. Cell 108 2 (2002) 221-232
55. Jeffrey I.W., Kadereit S., Meurs E.F., Metzger T., Bachmann M., Schwemmle M., et al. Nuclear localization of the interferon-inducible protein kinase PKR in human cells and transfected mouse cells. Exp. Cell Res. 218 1 (1995) 17-27
56. Onuki R., Bando Y., Suyama E., Katayama T., Kawasaki H., Baba T., et al. An RNA-dependent protein kinase is involved in tunicamycin-induced apoptosis and Alzheimer's disease. EMBO J. 23 4 (2004) 959-968
57. Kirchhoff S., Koromilas A.E., Schaper F., Grashoff M., Sonenberg N., and Hauser H. IRF-1 induced cell growth inhibition and interferon induction requires the activity of the protein kinase PKR. Oncogene 11 3 (1995) 439-445
58. Kumar A., Yang Y.L., Flati V., Der S., Kadereit S., Deb A., et al. Deficient cytokine signaling in mouse embryo fibroblasts with a targeted deletion in the PKR gene: role of IRF-1 and NF-kappaB. EMBO J. 16 2 (1997) 406-416
59. Ramana C.V., Grammatikakis N., Chernov M., Nguyen H., Goh K.C., Williams B.R., et al. Regulation of c-myc expression by IFN-gamma through Stat1-dependent and -independent pathways. EMBO J. 19 2 (2000) 263-272
60. Lee J.H., Park E.J., Kim O.S., Kim H.Y., Joe E.H., and Jou I. Double-stranded RNA-activated protein kinase is required for the LPS-induced activation of STAT1 inflammatory signaling in rat brain glial cells. Glia 50 1 (2005) 66-79
61. Deb A., Zamanian-Daryoush M., Xu Z., Kadereit S., and Williams B.R. Protein kinase PKR is required for platelet-derived growth factor signaling of c-fos gene expression via Erks and Stat3. EMBO J. 20 10 (2001) 2487-2496
62. Cuddihy A.R., Wong A.H., Tam N.W., Li S., and Koromilas A.E. The double-stranded RNA activated protein kinase PKR physically associates with the tumor suppressor p53 protein and phosphorylates human p53 on serine 392 in vitro. Oncogene 18 17 (1999) 2690-2702
63. Chu W.M., Ostertag D., Li Z.W., Chang L., Chen Y., Hu Y., et al. JNK2 and IKKbeta are required for activating the innate response to viral infection. Immunity 11 6 (1999) 721-731
64. Visvanathan K.V., and Goodbourn S. Double-stranded RNA activates binding of NF-kappa B to an inducible element in the human beta-interferon promoter. EMBO J. 8 4 (1989) 1129-1138
65. Maran A., Maitra R.K., Kumar A., Dong B., Xiao W., Li G., et al. Blockage of NF-kappa B signaling by selective ablation of an mRNA target by 2-5A antisense chimeras. Science 265 5173 (1994) 789-792
66. Yang Y.L., Reis L.F., Pavlovic J., Aguzzi A., Schafer R., Kumar A., et al. Deficient signaling in mice devoid of double-stranded RNA-dependent protein kinase. EMBO J. 14 24 (1995) 6095-6106
67. Gil J., Alcami J., and Esteban M. Activation of NF-kappa B by the dsRNA-dependent protein kinase, PKR involves the I kappa B kinase complex. Oncogene 19 11 (2000) 1369-1378
68. Gil J., Alcami J., and Esteban M. Induction of apoptosis by double-stranded-RNA-dependent protein kinase (PKR) involves the alpha subunit of eukaryotic translation initiation factor 2 and NF-kappaB. Mol. Cell. Biol. 19 7 (1999) 4653-4663
69. Roff M., Thompson J., Rodriguez M.S., Jacque J.M., Baleux F., Arenzana-Seisdedos F., et al. Role of IkappaBalpha ubiquitination in signal-induced activation of NFkappaB in vivo. J. Biol. Chem. 271 13 (1996) 7844-7850
70. Ghosh S., May M.J., and Kopp E.B. NF-kappa B and Rel proteins: evolutionarily conserved mediators of immune responses. Annu. Rev. Immunol. 16 (1998) 225-260
71. Ghosh S., and Karin M. Missing pieces in the NF-kappaB puzzle. Cell 109 Suppl (2002) S81-S96
72. Yamaoka S., Courtois G., Bessia C., Whiteside S.T., Weil R., Agou F., et al. Complementation cloning of NEMO, a component of the IkappaB kinase complex essential for NF-kappaB activation. Cell 93 7 (1998) 1231-1240
73. Leaman D.W., Salvekar A., Patel R., Sen G.C., and Stark G.R. A mutant cell line defective in response to double-stranded RNA and in regulating basal expression of interferon-stimulated genes. Proc. Natl. Acad. Sci. U.S.A. 95 16 (1998) 9442-9447
74. Bonnet M.C., Weil R., Dam E., Hovanessian A.G., and Meurs E.F. PKR stimulates NF-kappaB irrespective of its kinase function by interacting with the IkappaB kinase complex. Mol. Cell. Biol. 20 13 (2000) 4532-4542
75. Zamanian-Daryoush M., Mogensen T.H., DiDonato J.A., and Williams B.R. NF-kappaB activation by double-stranded-RNA-activated protein kinase (PKR) is mediated through NF-kappaB-inducing kinase and IkappaB kinase. Mol. Cell. Biol. 20 4 (2000) 1278-1290
76. Bonnet M.C., Daurat C., Ottone C., and Meurs E.F. The N-terminus of PKR is responsible for the activation of the NF-kappaB signaling pathway by interacting with the IKK complex. Cell Signal 18 11 (2006) 1865-1875
77. Gil J., Garcia M.A., Gomez-Puertas P., Guerra S., Rullas J., Nakano H., et al. TRAF family proteins link PKR with NF-kappa B activation. Mol. Cell. Biol. 24 10 (2004) 4502-4512
78. Oganesyan G., Saha S.K., Guo B., He J.Q., Shahangian A., Zarnegar B., et al. Critical role of TRAF3 in the Toll-like receptor-dependent and -independent antiviral response. Nature 439 7073 (2006) 208-211
79. Gil J., Rullas J., Garcia M.A., Alcami J., and Esteban M. The catalytic activity of dsRNA-dependent protein kinase, PKR, is required for NF-kappaB activation. Oncogene 20 3 (2001) 385-394
80. Lee T.G., Tang N., Thompson S., Miller J., and Katze M.G. 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 4 (1994) 2331-2342
81. Lee T.G., Tomita J., Hovanessian A.G., and Katze M.G. Purification and partial characterization of a cellular inhibitor of the interferon-induced protein kinase of Mr 68,000 from influenza virus-infected cells. Proc. Natl. Acad. Sci. U.S.A. 87 16 (1990) 6208-6212
82. Barber G.N., Thompson S., Lee T.G., Strom T., Jagus R., Darveau A., et al. 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. U.S.A. 91 10 (1994) 4278-4282
83. Gale Jr. M., Blakely C.M., Darveau A., Romano P.R., Korth M.J., and Katze M.G. P52rIPK regulates the molecular cochaperone P58IPK to mediate control of the RNA-dependent protein kinase in response to cytoplasmic stress. Biochemistry 41 39 (2002) 11878-11887
84. Gatignol A., Buckler-White A., Berkhout B., and Jeang K.T. Characterization of a human TAR RNA-binding protein that activates the HIV-1 LTR. Science 251 5001 (1991) 1597-1600
85. Daher A., Longuet M., Dorin D., Bois F., Segeral E., Bannwarth S., et al. Two dimerization domains in the trans-activation response RNA-binding protein (TRBP) individually reverse the protein kinase R inhibition of HIV-1 long terminal repeat expression. J. Biol. Chem. 276 36 (2001) 33899-33905
86. Ong C.L., Thorpe J.C., Gorry P.R., Bannwarth S., Jaworowski A., Howard J.L., et al. Low TRBP levels support an innate human immunodeficiency virus type 1 resistance in astrocytes by enhancing the PKR antiviral response. J. Virol. 79 20 (2005) 12763-12772
87. Edery I., Petryshyn R., and Sonenberg N. Activation of double-stranded RNA-dependent kinase (dsl) by the TAR region of HIV-1 mRNA: a novel translational control mechanism. Cell 56 2 (1989) 303-312
88. Kim I., Liu C.W., and Puglisi J.D. Specific recognition of HIV TAR RNA by the dsRNA binding domains (dsRBD1-dsRBD2) of PKR. J. Mol. Biol. 358 2 (2006) 430-442
89. Gunnery S., Green S.R., and Mathews M.B. Tat-responsive region RNA of human immunodeficiency virus type 1 stimulates protein synthesis in vivo and in vitro: relationship between structure and function. Proc. Natl. Acad. Sci. U.S.A. 89 23 (1992) 11557-11561
90. Haase A.D., Jaskiewicz L., Zhang H., Laine S., Sack R., Gatignol A., et al. TRBP, a regulator of cellular PKR and HIV-1 virus expression, interacts with Dicer and functions in RNA silencing. EMBO Rep. 6 10 (2005) 961-967
91. Benkirane M., Neuveut C., Chun R.F., Smith S.M., Samuel C.E., Gatignol A., et al. Oncogenic potential of TAR RNA binding protein TRBP and its regulatory interaction with RNA-dependent protein kinase PKR. EMBO J. 16 3 (1997) 611-624
92. Datta B., Datta R., Ghosh A., and Majumdar A. Eukaryotic initiation factor 2-associated glycoprotein, p67, shows differential effects on the activity of certain kinases during serum-starved conditions. Arch. Biochem. Biophys. 427 1 (2004) 68-78
93. Gil J., Esteban M., and Roth D. In vivo regulation of the dsRNA-dependent protein kinase PKR by the cellular glycoprotein p67. Biochemistry 39 51 (2000) 16016-16025
94. Donze O., Abbas-Terki T., and Picard D. The Hsp90 chaperone complex is both a facilitator and a repressor of the dsRNA-dependent kinase PKR. EMBO J. 20 14 (2001) 3771-3780
95. Pang Q., Christianson T.A., Keeble W., Koretsky T., and Bagby G.C. The anti-apoptotic function of Hsp70 in the interferon-inducible double-stranded RNA-dependent protein kinase-mediated death signaling pathway requires the Fanconi anemia protein. FANCC.J. Biol. Chem. 277 51 (2002) 49638-49643
96. Itahana K., Bhat K.P., Jin A., Itahana Y., Hawke D., Kobayashi R., et al. Tumor suppressor ARF degrades B23, a nucleolar protein involved in ribosome biogenesis and cell proliferation. Mol. Cell 12 5 (2003) 1151-1164
97. Chan W.Y., Liu Q.R., Borjigin J., Busch H., Rennert O.M., Tease L.A., et al. Characterization of the cDNA encoding human nucleophosmin and studies of its role in normal and abnormal growth. Biochemistry 28 3 (1989) 1033-1039
98. Falini B., Mecucci C., Tiacci E., Alcalay M., Rosati R., Pasqualucci L., et al. Cytoplasmic nucleophosmin in acute myelogenous leukemia with a normal karyotype. N. Engl. J. Med. 352 3 (2005) 254-266
99. Pang Q., Christianson T.A., Koretsky T., Carlson H., David L., Keeble W., et al. Nucleophosmin interacts with and inhibits the catalytic function of eukaryotic initiation factor 2 kinase PKR. J. Biol. Chem. 278 43 (2003) 41709-41717
100. Garcia M.A., Collado M., Munoz-Fontela C., Matheu A., Marcos-Villar L., Arroyo J., et al. Antiviral action of the tumor suppressor ARF. EMBO J. 25 18 (2006) 4284-4292
101. Bennett R.L., Blalock W.L., and May W.S. Serine 18 phosphorylation of, R.A.X., the PKR activator, is required for PKR activation and consequent translation inhibition. J. Biol. Chem. 279 41 (2004) 42687-42693
102. Peters G.A., Hartmann R., Qin J., and Sen G.C. Modular structure of PACT: distinct domains for binding and activating PKR. Mol. Cell. Biol. 21 6 (2001) 1908-1920
103. Patel C.V., Handy I., Goldsmith T., and Patel R.C. PACT, a stress-modulated cellular activator of interferon-induced double-stranded RNA-activated protein kinase. PKR.J. Biol. Chem. 275 48 (2000) 37993-37998
104. Pataer A., Vorburger S.A., Chada S., Balachandran S., Barber G.N., Roth J.A., et al. Melanoma differentiation-associated gene-7 protein physically associates with the double-stranded RNA-activated protein kinase PKR. Mol. Ther. 11 5 (2005) 717-723
105. Vorburger S.A., Hetrakul N., Xia W., Wilson-Heiner M., Mirza N., Pollock R.E., et al. Gene therapy with E2F-1 up-regulates the protein kinase PKR and inhibits growth of leiomyosarcoma in vivo. Mol. Cancer Ther. 4 11 (2005) 1710-1716
106. Goodbourn S., Didcock L., and Randall R.E. Interferons: cell signalling, immune modulation, antiviral response and virus countermeasures. J. Gen. Virol. 81 Pt 10 (2000) 2341-2364
107. He B., Gross M., and Roizman B. The gamma134.5 protein of herpes simplex virus 1 has the structural and functional attributes of a protein phosphatase 1 regulatory subunit and is present in a high molecular weight complex with the enzyme in infected cells. J. Biol. Chem. 273 33 (1998) 20737-20743
108. Cassady K.A., and Gross M. The herpes simplex virus type 1 U(S)11 protein interacts with protein kinase R in infected cells and requires a 30-amino-acid sequence adjacent to a kinase substrate domain. J. Virol. 76 5 (2002) 2029-2035
109. Poppers J., Mulvey M., Perez C., Khoo D., and Mohr I. Identification of a lytic-cycle Epstein-Barr virus gene product that can regulate PKR activation. J. Virol. 77 1 (2003) 228-236
110. Peters G.A., Khoo D., Mohr I., and Sen G.C. Inhibition of PACT-mediated activation of PKR by the herpes simplex virus type 1 Us11 protein. J. Virol. 76 21 (2002) 11054-11064
111. Burysek L., and Pitha P.M. Latently expressed human herpesvirus 8-encoded interferon regulatory factor 2 inhibits double-stranded RNA-activated protein kinase. J. Virol. 75 5 (2001) 2345-2352
112. Rivas C., Thlick A.E., Parravicini C., Moore P.S., and Chang Y. Kaposi's sarcoma-associated herpesvirus LANA2 is a B-cell-specific latent viral protein that inhibits p53. J. Virol. 75 1 (2001) 429-438
113. Esteban M., Garcia M.A., Domingo-Gil E., Arroyo J., Nombela C., and Rivas C. The latency protein LANA2 from Kaposi's sarcoma-associated herpesvirus inhibits apoptosis induced by dsRNA-activated protein kinase but not RNase L activation. J. Gen. Virol. 84 Pt 6 (2003) 1463-1470
114. Carroll K., Elroy-Stein O., Moss B., and Jagus R. Recombinant vaccinia virus K3L gene product prevents activation of double-stranded RNA-dependent, initiation factor 2 alpha-specific protein kinase. J. Biol. Chem. 268 17 (1993) 12837-12842
115. Davies M.V., Elroy-Stein O., Jagus R., Moss B., and Kaufman R.J. The vaccinia virus K3L gene product potentiates translation by inhibiting double-stranded-RNA-activated protein kinase and phosphorylation of the alpha subunit of eukaryotic initiation factor 2. J. Virol. 66 4 (1992) 1943-1950
116. Beattie E., Paoletti E., and Tartaglia J. Distinct patterns of IFN sensitivity observed in cells infected with vaccinia K3L- and E3L- mutant viruses. Virology 210 2 (1995) 254-263
117. Brandt T.A., and Jacobs B.L. Both carboxy- and amino-terminal domains of the vaccinia virus interferon resistance gene, E3L, are required for pathogenesis in a mouse model. J. Virol. 75 2 (2001) 850-856
118. Shors T., Kibler K.V., Perkins K.B., Seidler-Wulff R., Banaszak M.P., and Jacobs B.L. Complementation of vaccinia virus deleted of the E3L gene by mutants of E3L. Virology 239 2 (1997) 269-276
119. Rivas C., Gil J., Melkova Z., Esteban M., and Diaz-Guerra M. Vaccinia virus E3L protein is an inhibitor of the interferon (i.f.n.)-induced 2-5A synthetase enzyme. Virology 243 2 (1998) 406-414
120. Romano P.R., Zhang F., Tan S.L., Garcia-Barrio M.T., Katze M.G., Dever T.E., et al. Inhibition of double-stranded RNA-dependent protein kinase PKR by vaccinia virus E3: role of complex formation and the E3 N-terminal domain. Mol. Cell. Biol. 18 12 (1998) 7304-7316
121. Sharp T.V., Moonan F., Romashko A., Joshi B., Barber G.N., and Jagus R. The vaccinia virus E3L gene product interacts with both the regulatory and the substrate binding regions of PKR: implications for PKR autoregulation. Virology 250 2 (1998) 302-315
122. Garcia M.A., Guerra S., Gil J., Jimenez V., and Esteban M. Anti-apoptotic and oncogenic properties of the dsRNA-binding protein of vaccinia virus, E3L. Oncogene 21 55 (2002) 8379-8387
123. Lu Y., Wambach M., Katze M.G., and Krug R.M. Binding of the influenza virus NS1 protein to double-stranded RNA inhibits the activation of the protein kinase that phosphorylates the elF-2 translation initiation factor. Virology 214 1 (1995) 222-228
124. Hatada E., Saito S., and Fukuda R. Mutant influenza viruses with a defective NS1 protein cannot block the activation of PKR in infected cells. J. Virol. 73 3 (1999) 2425-2433
125. Bergmann M., Garcia-Sastre A., Carnero E., Pehamberger H., Wolff K., Palese P., et al. Influenza virus NS1 protein counteracts PKR-mediated inhibition of replication. J. Virol. 74 13 (2000) 6203-6206
126. Li S., Min J.Y., Krug R.M., and Sen G.C. Binding of the influenza A virus NS1 protein to PKR mediates the inhibition of its activation by either PACT or double-stranded RNA. Virology 349 1 (2006) 13-21
127. Enomoto N., Sakuma I., Asahina Y., Kurosaki M., Murakami T., Yamamoto C., et al. Comparison of full-length sequences of interferon-sensitive and resistant hepatitis C virus 1b. Sensitivity to interferon is conferred by amino acid substitutions in the NS5A region. J. Clin. Invest. 96 1 (1995) 224-230
128. Enomoto N., Sakuma I., Asahina Y., Kurosaki M., Murakami T., Yamamoto C., et al. Mutations in the nonstructural protein 5A gene and response to interferon in patients with chronic hepatitis C virus 1b infection. N. Engl. J. Med. 334 2 (1996) 77-81
129. Gale Jr. M., Blakely C.M., Kwieciszewski B., Tan S.L., Dossett M., Tang N.M., et al. Control of PKR protein kinase by hepatitis C virus nonstructural 5A protein: molecular mechanisms of kinase regulation. Mol. Cell. Biol. 18 9 (1998) 5208-5218
130. Gale Jr. M.J., Korth M.J., Tang N.M., Tan S.L., Hopkins D.A., Dever T.E., et al. Evidence that hepatitis C virus resistance to interferon is mediated through repression of the PKR protein kinase by the nonstructural 5A protein. Virology 230 2 (1997) 217-227
131. Duverlie G., Khorsi H., Castelain S., Jaillon O., Izopet J., Lunel F., et al. Sequence analysis of the NS5A protein of European hepatitis C virus 1b isolates and relation to interferon sensitivity. J. Gen. Virol. 79 Pt 6 (1998) 1373-1381
132. Zeuzem S., Lee J.H., and Roth W.K. Mutations in the nonstructural 5A gene of European hepatitis C virus isolates and response to interferon alfa. Hepatology 25 3 (1997) 740-744
133. Squadrito G., Raffa G., Restuccia T., Pollicino T., Brancatelli S., and Raimondo G. Is investigation of hepatitis C virus NS5A gene heterogeneity a tool for predicting long-lasting response to interferon therapy in patients with HCV-1b chronic hepatitis?. J. Viral Hepat. 9 5 (2002) 360-369
134. Kmieciak D., Kruszyna L., Migdalski P., Lacinski M., Juszczyk J., and Trzeciak W.H. Mutations within protein kinase R-binding domain of NS5A protein of hepatitis C virus (HCV) and specificity of HCV antibodies in pretreatment sera of HCV-chronically infected patients and their effect on the result of treatment. Jpn. J. Infect. Dis. 59 2 (2006) 92-99
135. Liang Y., Kang C.B., and Yoon H.S. Molecular and structural characterization of the domain 2 of hepatitis C virus non-structural protein 5A. Mol. Cells 22 1 (2006) 13-20
136. Taylor D.R., Shi S.T., Romano P.R., Barber G.N., and Lai M.M. Inhibition of the interferon-inducible protein kinase PKR by HCV E2 protein. Science 285 5424 (1999) 107-110
137. Pavio N., Romano P.R., Graczyk T.M., Feinstone S.M., and Taylor D.R. Protein synthesis and endoplasmic reticulum stress can be modulated by the hepatitis C virus envelope protein E2 through the eukaryotic initiation factor 2alpha kinase PERK. J. Virol. 77 6 (2003) 3578-3585
138. Pavio N., Taylor D.R., and Lai M.M. Detection of a novel unglycosylated form of hepatitis C virus E2 envelope protein that is located in the cytosol and interacts with PKR. J. Virol. 76 3 (2002) 1265-1272
139. Brazzoli M., Helenius A., Foung S.K., Houghton M., Abrignani S., and Merola M. Folding and dimerization of hepatitis C virus E1 and E2 glycoproteins in stably transfected CHO cells. Virology 332 1 (2005) 438-453
140. Gaudy C., Lambele M., Moreau A., Veillon P., Lunel F., and Goudeau A. Mutations within the hepatitis C virus genotype 1b E2-PePHD domain do not correlate with treatment outcome. J. Clin. Microbiol. 43 2 (2005) 750-754
141. Clemens M.J. Epstein-Barr virus: Inhibition of apoptosis as a mechanism of cell transformation. Int. J. Biochem. Cell Biol. 38 2 (2006) 164-169
142. Sharp T.V., Schwemmle M., Jeffrey I., Laing K., Mellor H., Proud C.G., et al. Comparative analysis of the regulation of the interferon-inducible protein kinase PKR by Epstein-Barr virus RNAs EBER-1 and EBER-2 and adenovirus VAI RNA. Nucleic Acids Res. 21 19 (1993) 4483-4490
143. Ruf I.K., Lackey K.A., Warudkar S., and Sample J.T. Protection from interferon-induced apoptosis by Epstein-Barr virus small RNAs is not mediated by inhibition of PKR. J. Virol. 79 23 (2005) 14562-14569
144. Talon J., Horvath C.M., Polley R., Basler C.F., Muster T., Palese P., et al. Activation of interferon regulatory factor 3 is inhibited by the influenza A virus NS1 protein. J. Virol. 74 17 (2000) 7989-7996
145. Wang X., Li M., Zheng H., Muster T., Palese P., Beg A.A., et al. Influenza A virus NS1 protein prevents activation of NF-kappaB and induction of alpha/beta interferon. J. Virol. 74 24 (2000) 11566-11573
146. Tan S.L., and Katze M.G. Biochemical and genetic evidence for complex formation between the influenza A virus NS1 protein and the interferon-induced PKR protein kinase. J. Interferon Cytokine Res. 18 9 (1998) 757-766
147. Falcon A.M., Fortes P., Marion R.M., Beloso A., and Ortin J. Interaction of influenza virus NS1 protein and the human homologue of Staufen in vivo and in vitro. Nucleic Acids Res. 27 11 (1999) 2241-2247
148. Brand S.R., Kobayashi R., and Mathews M.B. The Tat protein of human immunodeficiency virus type 1 is a substrate and inhibitor of the interferon-induced, virally activated protein kinase, PKR. J. Biol. Chem. 272 13 (1997) 8388-8395
149. McMillan N.A., Chun R.F., Siderovski D.P., Galabru J., Toone W.M., Samuel C.E., et al. HIV-1 Tat directly interacts with the interferon-induced, double-stranded RNA-dependent kinase, PKR. Virology 213 2 (1995) 413-424
150. Endo-Munoz L., Warby T., Harrich D., and McMillan N.A. Phosphorylation of HIV Tat by PKR increases interaction with TAR RNA and enhances transcription. Virol J. 2 (2005) 17
151. Yue Z., and Shatkin A.J. Double-stranded RNA-dependent protein kinase (PKR) is regulated by reovirus structural proteins. Virology 234 2 (1997) 364-371
152. Gonzalez-Lopez C., Martinez-Costas J., Esteban M., and Benavente J. Evidence that avian reovirus sigmaA protein is an inhibitor of the double-stranded RNA-dependent protein kinase. J. Gen. Virol. 84 Pt 6 (2003) 1629-1639
153. Jacobs B.L., and Langland J.O. Reovirus sigma 3 protein: dsRNA binding and inhibition of RNA-activated protein kinase. Curr. Top. Microbiol. Immunol. 233 Pt 1 (1998) 185-196
154. Castelli J.C., Hassel B.A., Maran A., Paranjape J., Hewitt J.A., Li X.L., et al. The role of 2′-5′ oligoadenylate-activated ribonuclease L in apoptosis. Cell Death Differ. 5 4 (1998) 313-320
155. Lee S.B., and Esteban M. The interferon-induced double-stranded RNA-activated protein kinase induces apoptosis. Virology 199 2 (1994) 491-496
156. Der S.D., Yang Y.L., Weissmann C., and Williams B.R. A double-stranded RNA-activated protein kinase-dependent pathway mediating stress-induced apoptosis. Proc. Natl. Acad. Sci. U.S.A. 94 7 (1997) 3279-3283
157. Srivastava S.P., Kumar K.U., and Kaufman R.J. Phosphorylation of eukaryotic translation initiation factor 2 mediates apoptosis in response to activation of the double-stranded RNA-dependent protein kinase. J. Biol. Chem. 273 4 (1998) 2416-2423
158. Kibler K.V., Shors T., Perkins K.B., Zeman C.C., Banaszak M.P., Biesterfeldt J., et al. Double-stranded RNA is a trigger for apoptosis in vaccinia virus-infected cells. J. Virol. 71 3 (1997) 1992-2003
159. Takizawa T., Ohashi K., and Nakanishi Y. Possible involvement of double-stranded RNA-activated protein kinase in cell death by influenza virus infection. J. Virol. 70 11 (1996) 8128-8132
160. Yeung M.C., Chang D.L., Camantigue R.E., and Lau A.S. Inhibitory role of the host apoptogenic gene PKR in the establishment of persistent infection by encephalomyocarditis virus in U937 cells. Proc. Natl. Acad. Sci. U.S.A. 96 21 (1999) 11860-11865
161. Kaufman R.J. Double-stranded RNA-activated protein kinase mediates virus-induced apoptosis: a new role for an old actor. Proc. Natl. Acad. Sci. U.S.A. 96 21 (1999) 11693-11695
162. Beretta L., Gabbay M., Berger R., Hanash S.M., and Sonenberg N. Expression of the protein kinase PKR in modulated by IRF-1 and is reduced in 5q- associated leukemias. Oncogene 12 7 (1996) 1593-1596
163. Scheuner D., Patel R., Wang F., Lee K., Kumar K., Wu J., et al. Double-stranded RNA-dependent protein kinase phosphorylation of the alpha-subunit of eukaryotic translation initiation factor 2 mediates apoptosis. J. Biol. Chem. 281 30 (2006) 21458-21468
164. Hai T., and Hartman M.G. The molecular biology and nomenclature of the activating transcription factor/cAMP responsive element binding family of transcription factors: activating transcription factor proteins and homeostasis. Gene 273 1 (2001) 1-11
165. Sionov R.V., and Haupt Y. The cellular response to p53: the decision between life and death. Oncogene 18 45 (1999) 6145-6157
166. Gil J., and Esteban M. The interferon-induced protein kinase (PKR), triggers apoptosis through FADD-mediated activation of caspase 8 in a manner independent of Fas and TNF-alpha receptors. Oncogene 19 32 (2000) 3665-3674
167. Balachandran S., Kim C.N., Yeh W.C., Mak T.W., Bhalla K., and Barber G.N. Activation of the dsRNA-dependent protein kinase, PKR, induces apoptosis through FADD-mediated death signaling. EMBO J. 17 23 (1998) 6888-6902
168. Gil J., Garcia M.A., and Esteban M. Caspase 9 activation by the dsRNA-dependent protein kinase, PKR: molecular mechanism and relevance. FEBS Lett. 529 2-3 (2002) 249-255
169. Brun A., Rivas C., Esteban M., Escribano J.M., and Alonso C. African swine fever virus gene A179L, a viral homologue of bcl-2, protects cells from programmed cell death. Virology 225 1 (1996) 227-230
170. Lee S.B., Rodriguez D., Rodriguez J.R., and Esteban M. 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 1 (1997) 81-88
171. Iordanov M.S., Ryabinina O.P., Schneider P., and Magun B.E. Two mechanisms of caspase 9 processing in double-stranded RNA- and virus-triggered apoptosis. Apoptosis 10 1 (2005) 153-166
172. Chong K.L., Feng L., Schappert K., Meurs E., Donahue T.F., Friesen J.D., et al. Human p68 kinase exhibits growth suppression in yeast and homology to the translational regulator GCN2. EMBO J. 11 4 (1992) 1553-1562
173. Donze O., Jagus R., Koromilas A.E., Hershey J.W., and Sonenberg N. Abrogation of translation initiation factor eIF-2 phosphorylation causes malignant transformation of NIH 3T3 cells. EMBO J. 14 15 (1995) 3828-3834
174. Barber G.N., Jagus R., Meurs E.F., Hovanessian A.G., and Katze M.G. 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 29 (1995) 17423-17428
175. Salzberg S., Vilchik S., Cohen S., Heller A., and Kronfeld-Kinar Y. Expression of a PKR dominant-negative mutant in myogenic cells interferes with the myogenic process. Exp. Cell Res. 254 1 (2000) 45-54
176. Morimoto H., Ozaki A., Okamura H., Yoshida K., Kitamura S., and Haneji T. Okadaic acid induces tyrosine phosphorylation of IkappaBalpha that mediated by PKR pathway in human osteoblastic MG63 cells. Mol. Cell. Biochem. 276 1-2 (2005) 211-217
177. Kuyama M., Nakanishi G., Arata J., Iwatsuki K., and Fujimoto W. Expression of double-stranded RNA-activated protein kinase in keratinocytes and keratinocytic neoplasia. J. Dermatol. 30 8 (2003) 579-589
178. Petryshyn R.A., Li J., and Judware R. Activation of the dsRNA-dependent kinase. Prog. Mol. Subcell. Biol. 14 (1994) 1-14
179. Zamanian-Daryoush M., Der S.D., and Williams B.R. Cell cycle regulation of the double stranded RNA activated protein kinase, PKR. Oncogene 18 2 (1999) 315-326
180. Abraham N., Stojdl D.F., Duncan P.I., Methot N., Ishii T., Dube M., et al. Characterization of transgenic mice with targeted disruption of the catalytic domain of the double-stranded RNA-dependent protein kinase. PKR.J. Biol. Chem. 274 9 (1999) 5953-5962
181. Baltzis D., Li S., and Koromilas A.E. Functional characterization of pkr gene products expressed in cells from mice with a targeted deletion of the N terminus or C terminus domain of PKR. J. Biol. Chem. 277 41 (2002) 38364-38372
182. Pataer A., Vorburger S.A., Barber G.N., Chada S., Mhashilkar A.M., Zou-Yang H., et al. Adenoviral transfer of the melanoma differentiation-associated gene 7 (mda7) induces apoptosis of lung cancer cells via up-regulation of the double-stranded RNA-dependent protein kinase (PKR). Cancer Res. 62 8 (2002) 2239-2243
183. Nussbaum J.M., Gunnery S., and Mathews M.B. The 3′-untranslated regions of cytoskeletal muscle mRNAs inhibit translation by activating the double-stranded RNA-dependent protein kinase PKR. Nucleic Acids Res. 30 5 (2002) 1205-1212
184. Cuddihy A.R., Li S., Tam N.W., Wong A.H., Taya Y., Abraham N., et al. Double-stranded-RNA-activated protein kinase PKR enhances transcriptional activation by tumor suppressor p53. Mol. Cell. Biol. 19 4 (1999) 2475-2484
185. Friedrich I., Ben-Bassat H., and Levitzki A. Activation of dsRNA dependent protein kinase PKR in Karpas299 does not lead to cell death. Cancer Biol Ther. 4 7 (2005) 734-739
186. Buchner J. Hsp90 & Co.-a holding for folding. Trends Biochem. Sci. 24 4 (1999) 136-141
187. Strong J.E., Coffey M.C., Tang D., Sabinin P., and Lee P.W. The molecular basis of viral oncolysis: usurpation of the Ras signaling pathway by reovirus. EMBO J. 17 12 (1998) 3351-3362
188. Mundschau L.J., and Faller D.V. Endogenous inhibitors of the dsRNA-dependent eIF-2 alpha protein kinase PKR in normal and ras-transformed cells. Biochimie 76 8 (1994) 792-800
189. Raveh T., Hovanessian A.G., Meurs E.F., Sonenberg N., and Kimchi A. Double-stranded RNA-dependent protein kinase mediates c-Myc suppression induced by type I interferons. J. Biol. Chem. 271 41 (1996) 25479-25484
190. Shang Y., Baumrucker C.R., and Green M.H. c-Myc is a major mediator of the synergistic growth inhibitory effects of retinoic acid and interferon in breast cancer cells. J. Biol. Chem. 273 46 (1998) 30608-30613
191. Lu D., Wolfgang C.D., and Hai T. Activating transcription factor 3, a stress-inducible gene, suppresses Ras-stimulated tumorigenesis. J. Biol. Chem. 281 15 (2006) 10473-10481
192. Squire J., Meurs E.F., Chong K.L., McMillan N.A., Hovanessian A.G., and Williams B.R. Localization of the human interferon-induced, ds-RNA activated p68 kinase gene (PRKR) to chromosome 2p21-p22. Genomics 16 3 (1993) 768-770
193. Barber G.N., Edelhoff S., Katze M.G., and Disteche C.M. Chromosomal assignment of the interferon-inducible double-stranded RNA-dependent protein kinase (PRKR) to human chromosome 2p21-p22 and mouse chromosome 17 E2. Genomics 16 3 (1993) 765-767
194. Haus O. The genes of interferons and interferon-related factors: localization and relationships with chromosome aberrations in cancer. Arch. Immunol. Ther. Exp. (Warsz.) 48 2 (2000) 95-100
195. Li S., and Koromilas A.E. Dominant negative function by an alternatively spliced form of the interferon-inducible protein kinase PKR. J. Biol. Chem. 276 17 (2001) 13881-13890
196. Murad J.M., Tone L.G., de Souza L.R., and De Lucca F.L. A point mutation in the RNA-binding domain I results in decrease of PKR activation in acute lymphoblastic leukemia. Blood Cells Mol. Dis. 34 1 (2005) 1-5
197. Hii S.I., Hardy L., Crough T., Payne E.J., Grimmett K., Gill D., et al. Loss of PKR activity in chronic lymphocytic leukemia. Int. J. Cancer 109 3 (2004) 329-335
198. Haines III G.K., Panos R.J., Bak P.M., Brown T., Zielinski M., Leyland J., et al. Interferon-responsive protein kinase (p68) and proliferating cell nuclear antigen are inversely distributed in head and neck squamous cell carcinoma. Tumour Biol. 19 1 (1998) 52-59
199. Haines G.K., Cajulis R., Hayden R., Duda R., Talamonti M., and Radosevich J.A. Expression of the double-stranded RNA-dependent protein kinase (p68) in human breast tissues. Tumour Biol. 17 1 (1996) 5-12
200. Delhem N., Sabile A., Gajardo R., Podevin P., Abadie A., Blaton M.A., et al. Activation of the interferon-inducible protein kinase PKR by hepatocellular carcinoma derived-hepatitis C virus core protein. Oncogene 20 41 (2001) 5836-5845
201. Nussbaum J.M., Major M., and Gunnery S. Transcriptional upregulation of interferon-induced protein kinase, PKR, in breast cancer. Cancer Lett. 196 2 (2003) 207-216
202. Kim S.H., Forman A.P., Mathews M.B., and Gunnery S. Human breast cancer cells contain elevated levels and activity of the protein kinase, PKR. Oncogene 19 27 (2000) 3086-3094
203. Kim S.H., Gunnery S., Choe J.K., and Mathews M.B. Neoplastic progression in melanoma and colon cancer is associated with increased expression and activity of the interferon-inducible protein kinase, PKR. Oncogene 21 57 (2002) 8741-8748
204. Shimada A., Shiota G., Miyata H., Kamahora T., Kawasaki H., Shiraki K., et al. Aberrant expression of double-stranded RNA-dependent protein kinase in hepatocytes of chronic hepatitis and differentiated hepatocellular carcinoma. Cancer Res. 58 19 (1998) 4434-4438
205. Terada T., Maeta H., Endo K., and Ohta T. Protein expression of double-stranded RNA-activated protein kinase in thyroid carcinomas: correlations with histologic types, pathologic parameters, and Ki-67 labeling. Hum. Pathol. 31 7 (2000) 817-821
206. Terada T., Ueyama J., Ukita Y., and Ohta T. Protein expression of double-stranded RNA-activated protein kinase (PKR) in intrahepatic bile ducts in normal adult livers, fetal livers, primary biliary cirrhosis, hepatolithiasis and intrahepatic cholangiocarcinoma. Liver 20 6 (2000) 450-457
207. Zhou Y., Gobl A., Wang S., Jacobsen M.B., Janson E.T., Haines III G.K., et al. Expression of p68 protein kinase and its prognostic significance during IFN-alpha therapy in patients with carcinoid tumours. Eur. J. Cancer 34 13 (1998) 2046-2052