The dsRNA protein kinase PKR: Virus and cell control

NF-κB AND REL PROTEINS: Evolutionarily Conserved Mediators of Immune Responses

Ghosh, S., May, M. J., & Kopp, E. B. (1998) · Annual Review of Immunology · doi:10.1146/annurev.immunol.16.1.225 · Cited by 5,182 · see citing works

HOW CELLS RESPOND TO INTERFERONS

Stark, G. R., Kerr, I. M., Williams, B. R. G., Silverman, R. H., & Schreiber, R. D. (1998) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.67.1.227 · Cited by 3,932 · see citing works

Missing Pieces in the NF-κB Puzzle

Ghosh, S., & Karin, M. (2002) · Cell · doi:10.1016/s0092-8674(02)00703-1 · Cited by 3,638 · see citing works

Cytoplasmic Nucleophosmin in Acute Myelogenous Leukemia with a Normal Karyotype

Falini, B., Mecucci, C., Tiacci, E., Alcalay, M., Rosati, R., Pasqualucci, L., La Starza, R., Diverio, D., Colombo, E., Santucci, A., et al. (2005) · New England Journal of Medicine · doi:10.1056/nejmoa041974 · Cited by 1,892 · see citing works

Interferons, interferon‐like cytokines, and their receptors

Pestka, S., Krause, C. D., & Walter, M. R. (2004) · Immunological Reviews · doi:10.1111/j.0105-2896.2004.00204.x · Cited by 1,768 · see citing works

Rel/NF-kappa B/I kappa B family: intimate tales of association and dissociation.Preprint

Verma, I. M., Stevenson, J. K., Schwarz, E. M., Antwerp, D. V., & Miyamoto, S. (1995) · Genes & Development · doi:10.1101/gad.9.22.2723 · Cited by 1,696 · see citing works

Complementation Cloning of NEMO, a Component of the IκB Kinase Complex Essential for NF-κB Activation

Yamaoka, S., Courtois, G., Chable-Bessia, C., Whiteside, S. T., Weil, R., Agou, F., Kirk, H., Kay, R. J., & Israël, A. (1998) · Cell · doi:10.1016/s0092-8674(00)81466-x · Cited by 1,077 · see citing works

TRANSLATIONAL CONTROL IN MAMMALIAN CELLS

Hershey, J. W. B. (1991) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.60.070191.003441 · Cited by 1,037 · see citing works

Molecular cloning and characterization of the human double-stranded RNA-activated protein kinase induced by interferon

MEURS, E. F., Chong, K. L., GALABRU, J., Thomas, N. S. B., Kerr, I. M., Williams, B. R. G., & Hovanessian, A. G. (1990) · Cell · doi:10.1016/0092-8674(90)90374-n · Cited by 1,017 · see citing works

Mutations in the Nonstructural Protein 5a Gene and Response to Interferon in Patients with Chronic Hepatitis C Virus 1b Infection

Enomoto, N., Sakuma, I., Asahina, Y., Kurosaki, M., Murakami, T., Yamamoto, C., Ogura, Y., Izumi, N., Marumo, F., & Sato, C. (1996) · New England Journal of Medicine · doi:10.1056/nejm199601113340203 · Cited by 997 · see citing works

Interferons: cell signalling, immune modulation, antiviral response and virus countermeasures

Goodbourn, S., Didcock, L., & Randall, R. E. (2000) · Journal of General Virology · doi:10.1099/0022-1317-81-10-2341 · Cited by 977 · see citing works

Critical role of TRAF3 in the Toll-like receptor-dependent and -independent antiviral response

Oganesyan, G., Saha, S. K., Guo, B., He, J. Q., Shahangian, A., Zarnegar, B. J., Perry, A. K., & Cheng, G. (2005) · Nature · doi:10.1038/nature04374 · Cited by 881 · see citing works

PKR; a sentinel kinase for cellular stress

Williams, B. R. (1999) · Oncogene · doi:10.1038/sj.onc.1203127 · Cited by 820 · see citing works

Impact of Protein Kinase PKR in Cell Biology: from Antiviral to Antiproliferative Action

García, M. A., Gil, J., Ventoso, I., Guerra, S., Domingo, E., Rivas, C., & Esteban, M. (2006) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00027-06 · Cited by 818 · see citing works

Evidence That Hepatitis C Virus Resistance to Interferon Is Mediated through Repression of the PKR Protein Kinase by the Nonstructural 5A Protein

Gale, M., Korth, M. J., Tang, N., Tan, S., Hopkins, D. A., Dever, T. E., Polyak, S. J., Gretch, D. R., & Katze, M. G. (1997) · Virology · doi:10.1006/viro.1997.8493 · Cited by 810 · see citing works

The molecular biology and nomenclature of the activating transcription factor/cAMP responsive element binding family of transcription factors: activating transcription factor proteins and homeostasis

Hai, T., & Hartman, M. G. (2001) · Gene · doi:10.1016/s0378-1119(01)00551-0 · Cited by 808 · see citing works

Phosphorylation of initiation factor eIF-2 and the control of reticulocyte protein synthesis

Farrell, P. J., Balkow, K., Hunt, T., Jackson, R. J., & Trachsel, H. (1977) · Cell · doi:10.1016/0092-8674(77)90330-0 · Cited by 745 · see citing works

Inhibition of the Interferon- Inducible Protein Kinase PKR by HCV E2 Protein

Taylor, D. R., Shi, S. T., Romano, P. R., Barber, G. N., & Lai, M. M. C. (1999) · Science · doi:10.1126/science.285.5424.107 · Cited by 732 · see citing works

TRBP, a regulator of cellular PKR and HIV‐1 virus expression, interacts with Dicer and functions in RNA silencing

Haase, A. D. D., Jaśkiewicz, Ł., Zhang, H., Lainé, S., Sack, R., Gatignol, A., & Filipowicz, W. (2005) · EMBO Reports · doi:10.1038/sj.embor.7400509 · Cited by 657 · see citing works

The interferon system. A bird's eye view of its biochemistry.

Sen, G. C., & Lengyel, P. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42719-6 · Cited by 633 · see citing works

Deficient signaling in mice devoid of double‐stranded RNA‐dependent protein kinase.

Yang, Y. L., Reis, L. F. L., Pavlovic, J., Aguzzi, A., Schäfer, R., Kumar, A., Williams, B. R. G., Aguet, M., & Weissmann, C. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb00300.x · Cited by 632 · see citing works

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.

Enomoto, N., Sakuma, I., Asahina, Y., Kurosaki, M., Murakami, T., Yamamoto, C., Izumi, N., Marumo, F., & Sato, C. (1995) · Journal of Clinical Investigation · doi:10.1172/jci118025 · Cited by 626 · see citing works

Hsp90 & Co. – a holding for folding

Büchner, J. (1999) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(99)01373-0 · Cited by 625 · see citing works

Antiviral actions of interferon interferon-regulated cellular proteins and their surprisingly selective antiviral activities

Samuel, C. E. (1991) · Virology · doi:10.1016/0042-6822(91)90112-o · Cited by 608 · see citing works

Control of PKR Protein Kinase by Hepatitis C Virus Nonstructural 5A Protein: Molecular Mechanisms of Kinase Regulation

Gale, M., Blakely, C. M., Kwieciszewski, B., Tan, S., Dossett, M. L., Tang, N., Korth, M. J., Polyak, S. J., Gretch, D. R., & Katze, M. G. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.9.5208 · Cited by 606 · see citing works

The cellular response to p53: the decision between life and death

Sionov, R. V., & Haupt, Y. (1999) · Oncogene · doi:10.1038/sj.onc.1203130 · Cited by 600 · see citing works

Activation of Interferon Regulatory Factor 3 Is Inhibited by the Influenza A Virus NS1 Protein

Talon, J., Horvath, C. M., Polley, R., Basler, C. F., Muster, T., Palese, P., & García‐Sastre, A. (2000) · Journal of Virology · doi:10.1128/jvi.74.17.7989-7996.2000 · Cited by 578 · see citing works

Double-stranded RNA-dependent protein kinase activates transcription factor NF-kappa B by phosphorylating I kappa B.

Kumar, A., Haque, J., Lacoste, J., Hiscott, J. B., & Williams, B. R. G. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.14.6288 · Cited by 568 · see citing works

The molecular basis of viral oncolysis: usurpation of the Ras signaling pathway by reovirus

Strong, J. E., Coffey, M. C., Tang, D., Sabinin, P., & Lee, P. W. K. (1998) · The EMBO Journal · doi:10.1093/emboj/17.12.3351 · Cited by 552 · see citing works

Influenza A Virus NS1 Protein Prevents Activation of NF-κB and Induction of Alpha/Beta Interferon

Wang, X., Li, M. O., Zheng, H., Muster, T., Palese, P., Beg, A. A., & García‐Sastre, A. (2000) · Journal of Virology · doi:10.1128/jvi.74.24.11566-11573.2000 · Cited by 536 · see citing works

Malignant transformation by a mutant of the IFN-inducible dsRNA-dependent protein kinase

Koromilas, A. E., Roy, S., Barber, G. N., Katze, M. G., & Sonenberg, N. (1992) · Science · doi:10.1126/science.1382315 · Cited by 532 · see citing works

Essential Role for the dsRNA-Dependent Protein Kinase PKR in Innate Immunity to Viral Infection

Balachandran, S., Roberts, P. C., Brown, L. E., Truong, H., Pattnaik, A. K., Archer, D. R., & Barber, G. N. (2000) · Immunity · doi:10.1016/s1074-7613(00)00014-5 · Cited by 527 · see citing works

PACT, a protein activator of the interferon‐induced protein kinase, PKR

Patel, R. C., & Sen, G. C. (1998) · The EMBO Journal · doi:10.1093/emboj/17.15.4379 · Cited by 457 · see citing works

Tumor Suppressor ARF Degrades B23, a Nucleolar Protein Involved in Ribosome Biogenesis and Cell Proliferation

Itahana, K., Bhat, K., Jin, A., Itahana, Y., Hawke, D. H., Kobayashi, R., & Zhang, Y. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00431-3 · Cited by 431 · see citing works

Tumor suppressor function of the interferon-induced double-stranded RNA-activated protein kinase.

MEURS, E. F., GALABRU, J., Barber, G. N., Katze, M. G., & Hovanessian, A. G. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.1.232 · Cited by 426 · see citing works

Signal Integration via PKR

Williams, B. R. G. (2001) · Science s STKE · doi:10.1126/stke.2001.89.re2 · Cited by 407 · see citing works

The Phosphorylation State of Eucaryotic Initiation Factor 2 Alters Translational Efficiency of Specific mRNAs

Kaufman, R. J., Davies, M. V., Pathak, V. K., & Hershey, J. W. B. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.3.946-958.1989 · Cited by 395 · see citing works

JNK2 and IKKβ Are Required for Activating the Innate Response to Viral Infection

Chu, W., Ostertag, D. G., Li, Z.-W., Chang, L., Chen, Y., Hu, Y., Williams, B. R. G., Perrault, J., & Karin, M. (1999) · Immunity · doi:10.1016/s1074-7613(00)80146-6 · Cited by 389 · see citing works

Characterization of a Human TAR RNA-Binding Protein That Activates the HIV-1 LTR

Gatignol, A., Buckler-White, A. J., Berkhout, B., & Jeang, K. (1991) · Science · doi:10.1126/science.2011739 · Cited by 389 · see citing works

A double-stranded RNA-activated protein kinase-dependent pathway mediating stress-induced apoptosis

Der, S. D., Yang, Y.-L., Weissmann, C., & Williams, B. R. G. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.7.3279 · Cited by 389 · see citing works

Binding of the Influenza Virus NS1 Protein to Double-Stranded RNA Inhibits the Activation of the Protein Kinase That Phosphorylates the eIF-2 Translation Initiation Factor

LU, Y., Wambach, M., Katze, M. G., & Krug, R. M. (1995) · Virology · doi:10.1006/viro.1995.9937 · Cited by 387 · see citing works

Activation of the dsRNA‐dependent protein kinase, PKR, induces apoptosis through FADD‐mediated death signaling

Balachandran, S., Kim, C. N., Yeh, W., Mak, T., Bhalla, K., & Barber, G. (1998) · EMBO Journal · doi:10.1093/emboj/17.23.6888 · Cited by 385 · see citing works

Phosphorylation of Eukaryotic Translation Initiation Factor 2 Mediates Apoptosis in Response to Activation of the Double-stranded RNA-dependent Protein Kinase

Srivastava, S. P., Kumar, K. U., & Kaufman, R. J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.4.2416 · Cited by 378 · see citing works

Mechanistic Link between PKR Dimerization, Autophosphorylation, and eIF2α Substrate Recognition

Dey, M., Cao, C., Dar, A. C., Tamura, T., Ozato, K., Sicheri, F., & Dever, T. E. (2005) · Cell · doi:10.1016/j.cell.2005.06.041 · Cited by 366 · see citing works

NF-κB Activation by Double-Stranded-RNA-Activated Protein Kinase (PKR) Is Mediated through NF-κB-Inducing Kinase and IκB Kinase

Zamanian-Daryoush, M., Mogensen, T. H., DiDonato, J. A., & Williams, B. R. G. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.4.1278-1290.2000 · Cited by 362 · see citing works

Influenza Virus NS1 Protein Counteracts PKR-Mediated Inhibition of Replication

Bergmann, M., Garcia-Sastre, A., Carnero, E., Pehamberger, H., Wolff, K., Palese, P., & Muster, T. (2000) · Journal of Virology · doi:10.1128/jvi.74.13.6203-6206.2000 · Cited by 362 · see citing works

Deficient cytokine signaling in mouse embryo fibroblasts with a targeted deletion in the PKR gene: role of IRF‐1 and NF‐κB

Kumar, A., Yang, Y., Flati, V., Der, S., Kadereit, S., Deb, A., Haque, J., Reis, L. F. L., Weissmann, C., & Williams, B. R. G. (1997) · The EMBO Journal · doi:10.1093/emboj/16.2.406 · Cited by 350 · see citing works

Poly(dI·dC)-induced Toll-like Receptor 3 (TLR3)-mediated Activation of NFκB and MAP Kinase Is through an Interleukin-1 Receptor-associated Kinase (IRAK)-independent Pathway Employing the Signaling Components TLR3-TRAF6-TAK1-TAB2-PKR*

Jiang, Z.-F., Zamanian-Daryoush, M., Nie, H., Silva, A. M., Williams, B., & Li, X.-X. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300562200 · Cited by 341 · see citing works

Binding of the influenza A virus NS1 protein to PKR mediates the inhibition of its activation by either PACT or double-stranded RNA

Li, S., Min, J.-Y., Krug, R. M., & Sen, G. C. (2006) · Virology · doi:10.1016/j.virol.2006.01.005 · Cited by 332 · see citing works

The Interferon-induced Double-Stranded RNA-Activated Protein Kinase Induces Apoptosis

Lee, S. B., & Estéban, M. (1994) · Virology · doi:10.1006/viro.1994.1151 · Cited by 324 · see citing works

Human p68 kinase exhibits growth suppression in yeast and homology to the translational regulator GCN2.

Chong, K. L., Feng, L., Schappert, K. T., MEURS, E. F., Donahue, T. F., Friesen, J. D., Hovanessian, A. G., & Williams, B. R. G. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05200.x · Cited by 320 · see citing works

Regulation of c‐myc expression by IFN‐γ through Stat1‐dependent and ‐independent pathways

Ramana, C. V., Grammatikakis, N., Chernov, M., Nguyen, H., Goh, K. C., Williams, B. R. G., & Stark, G. R. (2000) · The EMBO Journal · doi:10.1093/emboj/19.2.263 · Cited by 320 · see citing works

Double‐stranded RNA activates binding of NF‐kappa B to an inducible element in the human beta‐interferon promoter.

Visvanathan, K. V., & Goodbourn, S. (1989) · The EMBO Journal · doi:10.1002/j.1460-2075.1989.tb03483.x · Cited by 315 · see citing works

Autophosphorylation of the protein kinase dependent on double-stranded RNA.

GALABRU, J., & Hovanessian, A. G. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47759-9 · Cited by 303 · see citing works

Regulation of eukaryotic protein synthesis by initiation factors.

Rhoads, R. E. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53649-8 · Cited by 298 · see citing works

Kaposi's Sarcoma-Associated Herpesvirus LANA2 Is a B-Cell-Specific Latent Viral Protein That Inhibits p53

Rivas, C., Thlick, A.-E., Parravicini, C., Moore, P. S., & Chang, Y. (2001) · Journal of Virology · doi:10.1128/jvi.75.1.429-438.2001 · Cited by 296 · see citing works

Abrogation of translation initiation factor eIF‐2 phosphorylation causes malignant transformation of NIH 3T3 cells.

Donzé, O., Jagus, R., Koromilas, A. E., Hershey, J. W. B., & Sonenberg, N. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb00052.x · Cited by 288 · see citing works

The protein kinase PKR is required for p38 MAPK activation and the innate immune response to bacterial endotoxin

Goh, K. C., deVeer, M. J., & Williams, B. R. G. (2000) · The EMBO Journal · doi:10.1093/emboj/19.16.4292 · Cited by 285 · see citing works

Characterization of the cDNA encoding human nucleophosmin and studies of its role in normal and abnormal growth

Chan, W., Liu, Q., Borjigin, J., Busch, H., Rennert, O. M., Tease, L. A., & Chan, P. K. (1989) · Biochemistry · doi:10.1021/bi00429a017 · Cited by 270 · see citing works

PACT, a Stress-modulated Cellular Activator of Interferon-induced Double-stranded RNA-activated Protein Kinase, PKR

Patel, C. V., Handy, I., Goldsmith, T., & Patel, R. C. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m004762200 · Cited by 247 · see citing works

PKR Stimulates NF-κB Irrespective of Its Kinase Function by Interacting with the IκB Kinase Complex

Bonnet, M., Weil, R., Dam, E., Hovanessian, A. G., & MEURS, E. F. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.13.4532-4542.2000 · Cited by 234 · see citing works

Characterization of Transgenic Mice with Targeted Disruption of the Catalytic Domain of the Double-stranded RNA-dependent Protein Kinase, PKR

Abraham, N. B., Stojdl, D. F., Duncan, P. I., Méthot, N., Ishii, T. M., Dubé, M., Vanderhyden, B. C., Atkins, H. L., Gray, D. A., McBurney, M. W., et al. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.9.5953 · Cited by 231 · see citing works

RAX, a Cellular Activator for Double-stranded RNA-dependent Protein Kinase during Stress Signaling

Ito, T., Yang, M., & May, W. S. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.22.15427 · Cited by 224 · see citing works

Oncogenic potential of TAR RNA binding protein TRBP and its regulatory interaction with RNA‐dependent protein kinase PKR

Benkirane, M., Neuveut, C., Chun, R. F., Smith, S. M., Samuel, C. E., Gatignol, A., & Jeang, K. (1997) · The EMBO Journal · doi:10.1093/emboj/16.3.611 · Cited by 221 · see citing works

Both Carboxy- and Amino-Terminal Domains of the Vaccinia Virus Interferon Resistance Gene, E3L, Are Required for Pathogenesis in a Mouse Model

Brandt, T. A., & Jacobs, B. L. (2001) · Journal of Virology · doi:10.1128/jvi.75.2.850-856.2001 · Cited by 219 · see citing works

PKR—A protein kinase regulated by double-stranded RNA

Clemens, M. J. (1997) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(96)00169-0 · Cited by 216 · see citing works

Role of I Bα Ubiquitination in Signal-induced Activation of NF- B in Vivo

Roff, M. A., Thompson, J., Rodríguez, M. S., Jacqué, J.-M., Baleux, F., Arenzana‐Seisdedos, F., & Hay, R. T. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.13.7844 · Cited by 215 · see citing works

Blockage of NF-κB Signaling by Selective Ablation of an mRNA target by 2-5A Antisense Chimeras

Maran, A., Maitra, R. K., Kumar, A., Dong, B., Xiao, W., Li, G., Williams, B. R. G., Torrence, P. F., & Silverman, R. H. (1994) · Science · doi:10.1126/science.7914032 · Cited by 214 · see citing works

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

Davies, M. V., Elroy‐Stein, O., Jagus, R., Moss, B., & Kaufman, R. J. (1992) · Journal of Virology · doi:10.1128/jvi.66.4.1943-1950.1992 · Cited by 214 · see citing works

Human Interferon-γ mRNA Autoregulates Its Translation through a Pseudoknot that Activates the Interferon-Inducible Protein Kinase PKR

Ben-Asouli, Y., Banai, Y., Pel-Or, Y., Shir, A., & Kaempfer, R. (2002) · Cell · doi:10.1016/s0092-8674(02)00616-5 · Cited by 206 · see citing works

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

Cuddihy, A. R., Hoi-Tao Wong, A., Wai Ning Tam, N., Li, S., & Koromilas, A. E. (1999) · Oncogene · doi:10.1038/sj.onc.1202620 · Cited by 203 · see citing works

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., Tang, N., Thompson, S., Miller, J., & Katze, M. G. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.4.2331-2342.1994 · Cited by 202 · see citing works

Double-Stranded Poliovirus RNA Inhibits Initiation of Protein Synthesis by Reticulocyte Lysates

Ehrenfeld, E., & Hunt, T. (1971) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.68.5.1075 · Cited by 202 · see citing works

Activating Transcription Factor 3, a Stress-inducible Gene, Suppresses Ras-stimulated Tumorigenesis

Lü, D., Wolfgang, C. D., & Hai, T. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m509278200 · Cited by 202 · see citing works

The Double Stranded RNA-Activated Protein Kinase Induced by Interferon: dsRNA-PK

Hovanessian, A. G. (1989) · Journal of Interferon Research · doi:10.1089/jir.1989.9.641 · Cited by 201 · see citing works

Tumor-suppressor genes: news about the interferon connection.

Lengyel, P. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.13.5893 · Cited by 199 · see citing works

Induction of Apoptosis by Double-Stranded-RNA-Dependent Protein Kinase (PKR) Involves the α Subunit of Eukaryotic Translation Initiation Factor 2 and NF-κB

Gil, J., Alcamí, J., & Esteban, M. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.7.4653 · Cited by 199 · see citing works

Activation of double-stranded RNA-dependent kinase (dsl) by the TAR region of HIV-1 mRNA: A novel translational control mechanism

Edery, I., Petryshyn, R., & Sonenberg, N. (1989) · Cell · doi:10.1016/0092-8674(89)90904-5 · Cited by 196 · see citing works

The Murine Double-Stranded RNA-Dependent Protein Kinase PKR Is Required for Resistance to Vesicular Stomatitis Virus

Stojdl, D. F., Abraham, N. B., Knowles, S., Marius, R. M., Brasey, A., Lichty, B. D., Brown, E. G., Sonenberg, N., & Bell, J. C. (2000) · Journal of Virology · doi:10.1128/jvi.74.20.9580-9585.2000 · Cited by 196 · see citing works

Double-stranded RNA is a trigger for apoptosis in vaccinia virus-infected cells

Kibler, K. V., Shors, T., Perkins, K., Zeman, C., Banaszak, M. P., Biesterfeldt, J., Langland, J. O., & Jacobs, B. L. (1997) · Journal of Virology · doi:10.1128/jvi.71.3.1992-2003.1997 · Cited by 192 · see citing works

Double-stranded RNA in Vaccinia Virus Infected Cells

Colby, C., & DUESBERG, P. H. (1969) · Nature · doi:10.1038/222940a0 · Cited by 191 · see citing works

Mutations in the Nonstructural 5A Gene of European Hepatitis C Virus Isolates and Response to Interferon Alfa

Zeuzem, S., Lee, J. H., & Roth, W. K. (1997) · Hepatology · doi:10.1002/hep.510250341 · Cited by 189 · see citing works

Binding of Double-stranded RNA to Protein Kinase PKR Is Required for Dimerization and Promotes Critical Autophosphorylation Events in the Activation Loop

Zhang, F., Romano, P. R., Nagamura‐Inoue, T., Tian, B., Dever, T. E., Mathews, M. B., Ozato, K., & Hinnebusch, A. G. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102108200 · Cited by 188 · see citing works

Phosphorylation of Serine 51 in Initiation Factor 2α (eIF2α) Promotes Complex Formation between eIF2α(P) and eIF2B and Causes Inhibition in the Guanine Nucleotide Exchange Activity of eIF2B

Sudhakar, A., Ramachandran, A., Ghosh, S., Hasnain, S. E., Kaufman, R. J., & Ramaiah, K. V. A. (2000) · Biochemistry · doi:10.1021/bi0008682 · Cited by 188 · see citing works

Inhibition of Double-Stranded RNA-Dependent Protein Kinase PKR by Vaccinia Virus E3: Role of Complex Formation and the E3 N-Terminal Domain

Romano, P. R., Zhang, F., Tan, S., Garcia-Barrio, M. T., Katze, M. G., Dever, T. E., & Hinnebusch, A. G. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.12.7304 · Cited by 188 · see citing works

Recombinant vaccinia virus K3L gene product prevents activation of double-stranded RNA-dependent, initiation factor 2 alpha-specific protein kinase

Carroll, K. L., Elroy‐Stein, O., Moss, B., & Jagus, R. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)31463-7 · Cited by 184 · see citing works

The role of 2′-5′ oligoadenylate-activated ribonuclease L in apoptosis

Castelli, J. C., Hassel, B. A., Maran, A., Paranjape, J. M., Hewitt, J., Li, X.-L., Hsu, Y., Silverman, R. H., & Youle, R. J. (1998) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4400352 · Cited by 181 · see citing works

Increased sensitivity of cell-free protein synthesis to double-stranded RNA after interferon treatment

Kerr, I. M., BROWN, R. E., & Ball, L. A. (1974) · Nature · doi:10.1038/250057a0 · Cited by 180 · see citing works

Modular Structure of PACT: Distinct Domains for Binding and Activating PKR

Peters, G. A., Hartmann, R., Qin, J., & Sen, G. C. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.6.1908-1920.2001 · Cited by 178 · see citing works

Mutant Influenza Viruses with a Defective NS1 Protein Cannot Block the Activation of PKR in Infected Cells

Hatada, E., Saito, S., & Fukuda, R. (1999) · Journal of Virology · doi:10.1128/jvi.73.3.2425-2433.1999 · Cited by 177 · see citing works

Comparative analysis of the regulation of the interferoninducible protein kinase PKR by Epstein - Barr virus RNAs EBER-1 and EBER-2 and adenovirus VA, RNA

Sharp, T. V., Schwemmle, M., Jeffrey, I. W., Laing, K. G., Mellor, H., Proud, C. G., Hilse, K., & Clemens, M. J. (1993) · Nucleic Acids Research · doi:10.1093/nar/21.19.4483 · Cited by 174 · see citing works

The (2′‐5′)Oligoadenylate (pppA2′‐5′A2′‐5′A) Synthetase and Protein Kinase(s) from Interferon‐Treated Cells

Hovanessian, A. G., & Kerr, I. M. (1979) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1979.tb12850.x · Cited by 172 · see citing works

The γ134.5 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

He, B., Gross, M. S., & Roizman, B. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.33.20737 · Cited by 169 · see citing works

Purification and partial characterization of a cellular inhibitor of the interferon-induced protein kinase of Mr 68,000 from influenza virus-infected cells.

Lee, T. G., Tomita, J., Hovanessian, A. G., & Katze, M. G. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.16.6208 · Cited by 163 · see citing works

An RNA‐dependent protein kinase is involved in tunicamycin‐induced apoptosis and Alzheimer's disease

Onuki, R., Bando, Y., Suyama, E., Katayama, T., Kawasaki, H., Baba, T., Tohyama, M., & Taira, K. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600049 · Cited by 163 · see citing works

Latently Expressed Human Herpesvirus 8-Encoded Interferon Regulatory Factor 2 Inhibits Double-Stranded RNA-Activated Protein Kinase

Burýšek, L., & Pitha, P. M. (2001) · Journal of Virology · doi:10.1128/jvi.75.5.2345-2352.2001 · Cited by 157 · see citing works

Mechanism of Interferon Action: Inhibition of Viral Messenger Ribonucleic Acid Translation in L-Cell Extracts

Friedman, R. M., Metz, D. H., Estéban, M., Tovell, D. R., Ball, L. A., & Kerr, I. M. (1972) · Journal of Virology · doi:10.1128/jvi.10.6.1184-1198.1972 · Cited by 155 · see citing works

Protein Synthesis and Endoplasmic Reticulum Stress Can Be Modulated by the Hepatitis C Virus Envelope Protein E2 through the Eukaryotic Initiation Factor 2α Kinase PERK

Pavio, N., Romano, P. R., Graczyk, T. M., Feinstone, S. M., & Taylor, D. R. (2003) · Journal of Virology · doi:10.1128/jvi.77.6.3578-3585.2003 · Cited by 150 · see citing works

Vaccinia Virus E3L Protein Is an Inhibitor of the Interferon (IFN)-Induced 2-5A Synthetase Enzyme

Rivas, C., Gil, J., Mělková, Z., Estéban, M., & Díaz‐Guerra, M. (1998) · Virology · doi:10.1006/viro.1998.9072 · Cited by 149 · see citing works

HIV-1 Tat Directly Interacts with the Interferon-Induced, Double-Stranded RNA-Dependent Kinase, PKR

McMillan, N. A. J., Chun, R. F., Siderovski, D. P., GALABRU, J., Toone, W. M., Samuel, C. E., Mak, T. W., Hovanessian, A. G., Jeang, K.-T., & Williams, B. R. G. (1995) · Virology · doi:10.1006/viro.1995.0014 · Cited by 147 · see citing works

The Tat Protein of Human Immunodeficiency Virus Type 1 Is a Substrate and Inhibitor of the Interferon-induced, Virally Activated Protein Kinase, PKR

Brand, S. R., Kobayashi, R., & Mathews, M. B. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.13.8388 · Cited by 146 · see citing works

Interferon inhibits Viral Protein Synthesis in L Cells infected with Vaccinia Virus

Metz, D. H., & Estéban, M. (1972) · Nature · doi:10.1038/238385a0 · Cited by 144 · see citing works

Possible involvement of double-stranded RNA-activated protein kinase in cell death by influenza virus infection

Takizawa, T., Ohashi, K., & Nakanishi, Y. (1996) · Journal of Virology · doi:10.1128/jvi.70.11.8128-8132.1996 · Cited by 142 · see citing works

The binding of double‐stranded RNA and adenovirus VAI RNA to the interferon‐induced protein kinase

GALABRU, J., Katze, M. G., Robert, N., & Hovanessian, A. G. (1989) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1989.tb14485.x · Cited by 142 · see citing works

Double-stranded RNA-activated protein kinase mediates virus-induced apoptosis: A new role for an old actor

Kaufman, R. J. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.21.11693 · Cited by 142 · see citing works

Biochemical and Genetic Evidence for Complex Formation Between the Influenza A Virus NS1 Protein and the Interferon-induced PKR Protein Kinase

Tan, S., & Katze, M. G. (1998) · Journal of Interferon & Cytokine Research · doi:10.1089/jir.1998.18.757 · Cited by 141 · see citing works

TRAF Family Proteins Link PKR with NF-κB Activation

Gil, J., García, M. Á., Gómez‐Puertas, P., Guerra, S., Rullás, J., Nakano, H., Alcamı́, J., & Estéban, M. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.10.4502-4512.2004 · Cited by 138 · see citing works

Double-Stranded-RNA-Activated Protein Kinase PKR Enhances Transcriptional Activation by Tumor Suppressor p53

Cuddihy, A. R., Li, S., Tam, N. W. N., Wong, A. H., Taya, Y., Abraham, N., Bell, J. C., & Koromilas, A. E. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.4.2475 · Cited by 137 · see citing works

Double-stranded RNA-dependent Protein Kinase Phosphorylation of the α-Subunit of Eukaryotic Translation Initiation Factor 2 Mediates Apoptosis

Scheuner, D. L., Patel, R., Wang, F., Lee, K., Kumar, K. U., Wu, J., Nilsson, A., Karin, M., & Kaufman, R. J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m603784200 · Cited by 137 · see citing works

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.

Laurent-Crawford, A. G., Krust, B., GALABRU, J., Svab, J., & Hovanessian, A. G. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.13.4341 · Cited by 137 · see citing works

Sequence analysis of the NS5A protein of European hepatitis C virus 1b isolates and relation to interferon sensitivity.

Duverlie, G., Lunel, F., Eb, F., Jaillon, O., Izopet, J., Khorsi, H., Castelain, S., Pénin, F., & Wychowski, C. (1998) · Journal of General Virology · doi:10.1099/0022-1317-79-6-1373 · Cited by 137 · see citing works

Activation of NF-κB by the dsRNA-dependent protein kinase, PKR involves the IκB kinase complex

Gil, J., Alcamı́, J., & Estéban, M. (2000) · Oncogene · doi:10.1038/sj.onc.1203448 · Cited by 137 · see citing works

The interferon-induced protein kinase (PKR), triggers apoptosis through FADD-mediated activation of caspase 8 in a manner independent of Fas and TNF-α receptors

Gil, J., & Estéban, M. (2000) · Oncogene · doi:10.1038/sj.onc.1203710 · Cited by 128 · see citing works

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).

Pataer, A., Vorburger, S. A., Barber, G. N., Chada, S., Mhashilkar, A. M., Zou-Yang, H., Stewart, A. L., Balachandran, S., Roth, J. A., Hunt, K. K., et al. (2002) · PubMed · Cited by 127 · see citing works

The Hsp90 chaperone complex is both a facilitator and a repressor of the dsRNA‐dependent kinase PKR

Donzé, O., Abbas‐Terki, T., & Picard, D. (2001) · The EMBO Journal · doi:10.1093/emboj/20.14.3771 · Cited by 126 · see citing works

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 Proteases1

Lee, S. B., Rodrı́guez, D., Rodríguez, J. R., & Estéban, M. (1997) · Virology · doi:10.1006/viro.1997.8494 · Cited by 124 · see citing works

African Swine Fever Virus GeneA179L,a Viral Homologue ofbcl-2, Protects Cells from Programmed Cell Death

Brun, A., Rivas, C., Estéban, M., Escribano, J. M., & Alonso, C. (1996) · Virology · doi:10.1006/viro.1996.0592 · Cited by 123 · see citing works

The Vaccinia Virus E3L Gene Product Interacts with both the Regulatory and the Substrate Binding Regions of PKR: Implications for PKR Autoregulation

Sharp, T. V., Moonan, F., Romashko, A. M., Joshi, B., Barber, G. N., & Jagus, R. (1998) · Virology · doi:10.1006/viro.1998.9365 · Cited by 120 · see citing works

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., Thompson, S., Lee, T. G., Strom, T. B., Jagus, R., Darveau, A., & Katze, M. G. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.10.4278 · Cited by 119 · see citing works

Inhibition of PACT-Mediated Activation of PKR by the Herpes Simplex Virus Type 1 Us11 Protein

Peters, G. A., Khoo, D., Mohr, I., & Sen, G. C. (2002) · Journal of Virology · doi:10.1128/jvi.76.21.11054-11064.2002 · Cited by 118 · see citing works

Nuclear Localization of the Interferon-Inducible Protein Kinase PKR in Human Cells and Transfected Mouse Cells

Jeffrey, I. W., Kadereit, S., MEURS, E. F., Metzger, T. E., Bachmann, M. P., Schwemmle, M., Hovanessian, A. G., & Clemens, M. J. (1995) · Experimental Cell Research · doi:10.1006/excr.1995.1126 · Cited by 114 · see citing works

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

Cassady, K. A., & Gross, M. S. (2002) · Journal of Virology · doi:10.1128/jvi.76.5.2029-2035.2002 · Cited by 113 · see citing works

Distinct Patterns of IFN Sensitivity Observed in Cells Infected with Vaccinia K3L- and E3L- Mutant Viruses

Beattie, E., Paoletti, E., & Tartaglia, J. (1995) · Virology · doi:10.1006/viro.1995.1342 · Cited by 112 · see citing works

IRF-1 induced cell growth inhibition and interferon induction requires the activity of the protein kinase PKR.

Kirchhoff, S., Koromilas, A. E., Schaper, F., Grashoff, M., Sonenberg, N., & Häuser, H. (1995) · PubMed · Cited by 110 · see citing works

The protein kinase PKR: a molecular clock that sequentially activates survival and death programs

Donzé, O., Deng, J., Curran, J. A., SLADEK, R. M., Picard, D., & Sonenberg, N. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600078 · Cited by 107 · see citing works

Higher-Order Substrate Recognition of eIF2α by the RNA-Dependent Protein Kinase PKR

Dar, A., Dever, T., & Sicheri, F. (2005) · Cell · doi:10.1016/j.cell.2005.06.044 · Cited by 107 · see citing works

Human breast cancer cells contain elevated levels and activity of the protein kinase, PKR

Kim, S. H., Forman, A. P., Mathews, M. B., & Gunnery, S. (2000) · Oncogene · doi:10.1038/sj.onc.1203632 · Cited by 106 · see citing works

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

Pang, Q., Christianson, T. A., Keeble, W. W., Koretsky, T., & Bagby, G. C. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m209386200 · Cited by 105 · see citing works

Double-Stranded RNA-Dependent Protein Kinase (PKR) Is Regulated by Reovirus Structural Proteins

Yue, Z., & Shatkin, A. J. (1997) · Virology · doi:10.1006/viro.1997.8664 · Cited by 105 · see citing works

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

Daher, A., Longuet, M., Dorin, D., Bois, F., Ségéral, E., Bannwarth, S., Battisti, P.-L., Purcell, D. F. J., Bénarous, R., Vaquero, C., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103584200 · Cited by 105 · see citing works

Control of α Subunit of Eukaryotic Translation Initiation Factor 2 (eIF2α) Phosphorylation by the Human Papillomavirus Type 18 E6 Oncoprotein: Implications for eIF2α-Dependent Gene Expression and Cell Death

Kazemi, S., Papadopoulou, S., Li, S., Su, Q., Wang, S., Yoshimura, A., Matlashewski, G., Dever, T. E., & Koromilas, A. E. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.8.3415-3429.2004 · Cited by 99 · see citing works

Interaction of influenza virus NS1 protein and the human homologue of Staufen in vivo and in vitro

Falcón, A. M., Fortes, P., Marión, R. M., Beloso, A., & Ortı́n, J. (1999) · Nucleic Acids Research · doi:10.1093/nar/27.11.2241 · Cited by 95 · see citing works

Detection of a Novel Unglycosylated Form of Hepatitis C Virus E2 Envelope Protein That Is Located in the Cytosol and Interacts with PKR

Pavio, N., Taylor, D. R., & Lai, M. M. C. (2002) · Journal of Virology · doi:10.1128/jvi.76.3.1265-1272.2002 · Cited by 92 · see citing works

Neoplastic progression in melanoma and colon cancer is associated with increased expression and activity of the interferon-inducible protein kinase, PKR

Kim, S. H., Gunnery, S., Choe, J. K., & Mathews, M. B. (2002) · Oncogene · doi:10.1038/sj.onc.1205987 · Cited by 92 · see citing works

Double-Stranded RNA-Activated Protein Kinase (PKR) Is Negatively Regulated by 60S Ribosomal Subunit Protein L18

Kumar, K. U., Srivastava, S. P., & Kaufman, R. J. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.2.1116 · Cited by 90 · see citing works

Low TRBP Levels Support an Innate Human Immunodeficiency Virus Type 1 Resistance in Astrocytes by Enhancing the PKR Antiviral Response

Ong, C. L., Thorpe, J. C., Gorry, P. R., Bannwarth, S., Jaworowski, A., Howard, J. L., Chung, S. W. L., Campbell, S. M., Christensen, H. S., Clerzius, G., et al. (2005) · Journal of Virology · doi:10.1128/jvi.79.20.12763-12772.2005 · Cited by 83 · see citing works

Folding and dimerization of hepatitis C virus E1 and E2 glycoproteins in stably transfected CHO cells

Brazzoli, M., Helenius, A., Foung, S. K. H., Houghton, M., Abrignani, S., & Merola, M. (2005) · Virology · doi:10.1016/j.virol.2004.11.034 · Cited by 81 · see citing works

Protein kinase PKR is required for platelet‐derived growth factor signaling of c‐fos gene expression via Erks and Stat3

Deb, A., Zamanian‐Daryoush, M., Xu, Z., Kadereit, S., & Williams, B. R. G. (2001) · The EMBO Journal · doi:10.1093/emboj/20.10.2487 · Cited by 81 · see citing works

Ribosome Targeting of PKR Is Mediated by Two Double-stranded RNA-binding Domains and Facilitates in Vivo Phosphorylation of Eukaryotic Initiation Factor-2

Zhu, S., Romano, P. R., & Wek, R. C. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.22.14434 · Cited by 80 · see citing works

Molecular Mechanisms Responsible for Malignant Transformation by Regulatory and Catalytic Domain Variants of the Interferon-induced Enzyme RNA-dependent Protein Kinase

Barber, G. N., Jagus, R., MEURS, E. F., Hovanessian, A. G., & Katze, M. G. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.29.17423 · Cited by 78 · see citing works

Tyrosine phosphorylation acts as a molecular switch to full-scale activation of the eIF2α RNA-dependent protein kinase

Su, Q., Wang, S., Baltzis, D., Qu, L.-K., Wong, A. H.-T., & Koromilas, A. E. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0508207103 · Cited by 77 · see citing works

The latency protein LANA2 from Kaposi's sarcoma-associated herpesvirus inhibits apoptosis induced by dsRNA-activated protein kinase but not RNase L activation

Estéban, M., García, M. Á., Domingo-Gil, E., Arroyo, J., Nombela, C., & Rivas, C. (2003) · Journal of General Virology · doi:10.1099/vir.0.19014-0 · Cited by 76 · see citing works

Inhibitory role of the host apoptogenic gene PKR in the establishment of persistent infection by encephalomyocarditis virus in U937 cells

Yeung, M. C., Chang, D. L., Camantigue, R. E., & Lau, A. S. Y. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.21.11860 · Cited by 74 · see citing works

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

Baltzis, D., Li, S., & Koromilas, A. E. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m203564200 · Cited by 74 · see citing works

Evidence that avian reovirus σA protein is an inhibitor of the double-stranded RNA-dependent protein kinase

González-López, C., Martı́nez-Costas, J., Estéban, M., & Benavente, J. (2003) · Journal of General Virology · doi:10.1099/vir.0.19004-0 · Cited by 73 · see citing works

The catalytic activity of dsRNA-dependent protein kinase, PKR, is required for NF-κB activation

Gil, J., Rullás, J., García, M. Á., Alcamı́, J., & Estéban, M. (2001) · Oncogene · doi:10.1038/sj.onc.1204109 · Cited by 73 · see citing works

The N-terminus of PKR is responsible for the activation of the NF-κB signaling pathway by interacting with the IKK complex

Bonnet, M. C., Daurat, C., Ottone, C., & Meurs, E. F. (2006) · Cellular Signalling · doi:10.1016/j.cellsig.2006.02.010 · Cited by 71 · see citing works

Complementation of Vaccinia Virus Deleted of the E3L Gene by Mutants of E3L

Shors, T., Kibler, K. V., Perkins, K., Seidler-Wulff, R., Banaszak, M. P., & Jacobs, B. L. (1997) · Virology · doi:10.1006/viro.1997.8881 · Cited by 71 · see citing works

Activation of the interferon-inducible protein kinase PKR by Hepatocellular carcinoma derived-Hepatitis C virus core protein

Delhem, N., Sabile, A., Gajardo, R., Podevin, P., Abadie, A., Blaton, M. A., Kremsdorf, D., Beretta, L., & Bréchot, C. (2001) · Oncogene · doi:10.1038/sj.onc.1204744 · Cited by 71 · see citing works

Cell cycle regulation of the double stranded RNA activated protein kinase, PKR

Zamanian-Daryoush, M., Der, S. D., & Williams, B. R. G. (1999) · Oncogene · doi:10.1038/sj.onc.1202293 · Cited by 70 · see citing works

Protection from Interferon-Induced Apoptosis by Epstein-Barr Virus Small RNAs Is Not Mediated by Inhibition of PKR

Ruf, I. K., Lackey, K. A., Warudkar, S., & Sample, J. T. (2005) · Journal of Virology · doi:10.1128/jvi.79.23.14562-14569.2005 · Cited by 70 · see citing works

Double-stranded RNA-dependent Protein Kinase Mediates c-Myc Suppression Induced by Type I Interferons

Raveh, T. B., Hovanessian, A. G., MEURS, E. F., Sonenberg, N., & Kimchi, A. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.41.25479 · Cited by 68 · see citing works

Expression of the protein kinase PKR in modulated by IRF-1 and is reduced in 5q- associated leukemias.

Beretta, L., Gabbay, M., Berger, R., Hanash, S., & Sonenberg, N. (1996) · PubMed · Cited by 68 · see citing works

Melanoma differentiation-associated gene-7 protein physically associates with the double-stranded RNA-activated protein kinase PKR

Pataer, A., Vorburger, S. A., Chada, S., Balachandran, S., Barber, G. N., Roth, J. A., Hunt, K. K., & Swisher, S. G. (2005) · Molecular Therapy · doi:10.1016/j.ymthe.2005.01.018 · Cited by 67 · see citing works

Tat-responsive region RNA of human immunodeficiency virus type 1 stimulates protein synthesis in vivo and in vitro: relationship between structure and function.

Gunnery, S., Green, S. R., & Mathews, M. B. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.23.11557 · Cited by 65 · see citing works

Phosphorylation of HIV Tat by PKR increases interaction with TAR RNA and enhances transcription

Endo‐Munoz, L., Warby, T., Harrich, D., & McMillan, N. A. J. (2005) · Virology Journal · doi:10.1186/1743-422x-2-17 · Cited by 64 · see citing works

Serine 18 Phosphorylation of RAX, the PKR Activator, Is Required for PKR Activation and Consequent Translation Inhibition

Bennett, R. L., Blalock, W. L., & May, W. S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m403321200 · Cited by 62 · see citing works

Identification of a Lytic-Cycle Epstein-Barr Virus Gene Product That Can Regulate PKR Activation

Poppers, J., Mulvey, M., Perez, C., Khoo, D., & Mohr, I. (2002) · Journal of Virology · doi:10.1128/jvi.77.1.228-236.2003 · Cited by 62 · see citing works

The Interferon-Induced Double-Stranded RNA-Activated Human p68 Protein Kinase Potently Inhibits Protein Synthesis in Cultured Cells

Lee, S. B., Mělková, Z., Yan, W., Williams, B. R. G., Hovanessian, A. G., & Estéban, M. (1993) · Virology · doi:10.1006/viro.1993.1048 · Cited by 61 · see citing works

Further characterization of the protein kinase activity mediated by interferon in mouse and human cells.

Krust, B., GALABRU, J., & Hovanessian, A. G. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)39757-0 · Cited by 59 · see citing works

Caspase 9 activation by the dsRNA‐dependent protein kinase, PKR: molecular mechanism and relevance

Gil, J., García, M. Á., & Estéban, M. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)03348-3 · Cited by 59 · see citing works

Nucleophosmin Interacts with and Inhibits the Catalytic Function of Eukaryotic Initiation Factor 2 Kinase PKR

Pang, Q., Christianson, T. A., Koretsky, T., Carlson, H. L., David, L. L., Keeble, W. W., Faulkner, G. R., Speckhart, A., & Bagby, G. C. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301392200 · Cited by 57 · see citing works

Antiviral action of the tumor suppressor ARF

García, M. Á., Collado, M., Muñoz‐Fontela, C., Matheu, A., Marcos-Villar, L., Arroyo, J., Estéban, M., Serrano, M., & Rivas, C. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601302 · Cited by 54 · see citing works

Anti-apoptotic and oncogenic properties of the dsRNA-binding protein of vaccinia virus, E3L

García, M. Á., Guerra, S., Gil, J., Jiménez, V., & Estéban, M. (2002) · Oncogene · doi:10.1038/sj.onc.1206036 · Cited by 54 · see citing works

Specific Recognition of HIV TAR RNA by the dsRNA Binding Domains (dsRBD1–dsRBD2) of PKR

Kim, I., Liu, C. W., & Puglisi, J. D. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.01.099 · Cited by 53 · see citing works

Regulation of GTP hydrolysis prior to ribosomal AUG selection during eukaryotic translation initiation

Majumdar, R., & Maitra, U. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600844 · Cited by 53 · see citing works

Endogenous inhibitors of the dsRNA-dependent eIF-2α protein kinase PKR in normal and ras-transformed cells

Mundschau, L. J., & Faller, D. V. (1994) · Biochimie · doi:10.1016/0300-9084(94)90083-3 · Cited by 52 · see citing works

PKR: Proposed Nomenclature for the RNA-Dependent Protein Kinase Induced by Interferon

Clemens, M. J., Hershey, J. W. B., Hovanessian, A. G., Jacobs, B. C., Katze, M. G., Kaufman, R. J., Lengyel, P., Samuel, C. E., Sen, G. C., & Williams, B. R. G. (1993) · Journal of Interferon Research · doi:10.1089/jir.1993.13.241 · Cited by 51 · see citing works

Double-stranded RNA-activated protein kinase is required for the LPS-induced activation of STAT1 inflammatory signaling in rat brain glial cells

Lee, J. H., Park, E., Kim, O. S., Kim, H. Y., Joe, E.-H., & Jou, I. (2005) · Glia · doi:10.1002/glia.20156 · Cited by 50 · see citing works

Aberrant expression of double-stranded RNA-dependent protein kinase in hepatocytes of chronic hepatitis and differentiated hepatocellular carcinoma.

Shimada, A., Shiota, G., Miyata, H., Kamahora, T., Kawasaki, H., Shiraki, K., Hino, S., & Terada, T. (1998) · PubMed · Cited by 49 · see citing works

Dominant Negative Function by an Alternatively Spliced Form of the Interferon-inducible Protein Kinase PKR

Li, S., & Koromilas, A. E. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008140200 · Cited by 48 · see citing works

Expression of the Double-Stranded RNA-Dependent Protein Kinase (p68) in Human Breast Tissues

Haines, G. K., Cajulis, R. S., Hayden, R., Duda, R. B., Talamonti, M., & Radosevich, J. A. (1996) · Tumor Biology · doi:10.1159/000217961 · Cited by 47 · see citing works

Loss of PKR activity in chronic lymphocytic leukemia

Hii, S.-I., Hardy, L., Crough, T., Payne, E., Grimmett, K., Gill, D. S., & McMillan, N. A. J. (2004) · International Journal of Cancer · doi:10.1002/ijc.11714 · Cited by 47 · see citing works

Identification and Requirement of Three Ribosome Binding Domains in dsRNA-Dependent Protein Kinase (PKR)

Wu, S., Kumar, K. U., & Kaufman, R. J. (1998) · Biochemistry · doi:10.1021/bi981472h · Cited by 42 · see citing works

The 3'-untranslated regions of cytoskeletal muscle mRNAs inhibit translation by activating the double-stranded RNA-dependent protein kinase PKR

Nussbaum, J. M. (2002) · Nucleic Acids Research · doi:10.1093/nar/30.5.1205 · Cited by 42 · see citing works

Efficiency of poly (A).poly(U) as an adjuvant

Hovanessian, A. G., GALABRU, J., Rivière, Y., & Montagnier, L. (1988) · Immunology Today · doi:10.1016/0167-5699(88)91288-1 · Cited by 41 · see citing works

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

Lee, S. B., Bablanian, R., & Estéban, M. (1996) · Journal of Interferon & Cytokine Research · doi:10.1089/jir.1996.16.1073 · Cited by 40 · see citing works

Human Gene Profiling in Response to the Active Protein Kinase, Interferon-induced Serine/threonine Protein Kinase (PKR), in Infected Cells

Guerra, S., López-Fernández, L. A., García, M. A., Zaballos, A., & Esteban, M. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m511983200 · Cited by 40 · see citing works

Chromosomal Assignment of the Interferon-Inducible Double-Stranded RNA-Dependent Protein Kinase (PRKR) to Human Chromosome 2p21-p22 and Mouse Chromosome 17 E2

Barber, G. N., Edelhoff, S., Katze, M. G., & Distèche, C. M. (1993) · Genomics · doi:10.1006/geno.1993.1262 · Cited by 36 · see citing works

A mutant cell line defective in response to double-stranded RNA and in regulating basal expression of interferon-stimulated genes

Leaman, D. W., Salvekar, A., Patel, R. C., Sen, G. C., & Stark, G. R. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.16.9442 · Cited by 36 · see citing works

c-Myc Is a Major Mediator of the Synergistic Growth Inhibitory Effects of Retinoic Acid and Interferon in Breast Cancer Cells

Shang, Y., Baumrucker, C. R., & Green, M. H. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.46.30608 · Cited by 36 · see citing works

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

Terada, T., Ueyama, J., Ukita, Y., & Ohta, T. (2000) · Liver International · doi:10.1034/j.1600-0676.2000.020006450.x · Cited by 33 · see citing works

Interferon-Responsive Protein Kinase (p68) and Proliferating Cell Nuclear Antigen Are Inversely Distributed in Head and Neck Squamous Cell Carcinoma

Haines, G. K., Panos, R. J., Bak, P. M., Brown, T., Zielinski, M., Leyland, J., & Radosevich, J. A. (1998) · Tumor Biology · doi:10.1159/000029974 · Cited by 33 · see citing works

Reovirus σ3 Protein: dsRNA Binding and Inhibition of RNA-Activated Protein Kinase

Jacobs, B. L., & Langland, J. (1998) · Current topics in microbiology and immunology · doi:10.1007/978-3-642-72092-5_9 · Cited by 32 · see citing works

Molecular and Structural Characterization of the Domain 2 of Hepatitis C Virus Non-structural Protein 5A

Yu, L., Kang, C., & Yoon, H. S. (2006) · Molecules and Cells · doi:10.1016/s1016-8478(23)17385-7 · Cited by 32 · see citing works

Protein expression of double-stranded RNA-activated protein kinase in thyroid carcinomas: Correlations with histologic types, pathologic parameters, and Ki-67 labeling

Terada, T., Maeta, H., Endo, K., & Ohta, T. (2000) · Human Pathology · doi:10.1053/hupa.2000.8443 · Cited by 30 · see citing works

Mutations within the Hepatitis C Virus Genotype 1b E2-PePHD Domain Do Not Correlate with Treatment Outcome

Gaudy, C., Lambelé, M., Moreau, A., Veillon, P., Lunel, F., & Goudeau, A. (2005) · Journal of Clinical Microbiology · doi:10.1128/jcm.43.2.750-754.2005 · Cited by 30 · see citing works

Epstein-Barr virus: Inhibition of apoptosis as a mechanism of cell transformation

Clemens, M. J. (2005) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2005.09.014 · Cited by 29 · see citing works

Two mechanisms of caspase 9 processing in double-stranded RNA- and virus-triggered apoptosis

Iordanov, M. S., Ryabinina, O. P., Schneider, P., & Magun, B. E. (2005) · APOPTOSIS · doi:10.1007/s10495-005-6070-y · Cited by 29 · see citing works

The genes of interferons and interferon-related factors: localization and relationships with chromosome aberrations in cancer.

Haus, O. (2000) · PubMed · Cited by 26 · see citing works

P52rIPK Regulates the Molecular Cochaperone P58IPK To Mediate Control of the RNA-Dependent Protein Kinase in Response to Cytoplasmic Stress

Gale, M., Blakely, C. M., Darveau, A., Romano, P. R., Korth, M. J., & Katze, M. G. (2002) · Biochemistry · doi:10.1021/bi020397e · Cited by 25 · see citing works

Expression of p68 protein kinase and its prognostic significance during IFN-α therapy in patients with carcinoid tumours

Zhou, Y., Gobl, A., Wang, S., Jacobsen, M. B., Janson, E. T., Haines, G. K., Radosevich, J. A., & Öberg, K. (1998) · European Journal of Cancer · doi:10.1016/s0959-8049(98)00292-5 · Cited by 25 · see citing works

Localization of the Human Interferon-Induced, ds-RNA Activated p68 Kinase Gene (PRKR) to Chromosome 2p21-p22

Squire, J. A., MEURS, E. F., Chong, K. L., McMillan, N. A. J., Hovanessian, A. G., & Williams, B. R. G. (1993) · Genomics · doi:10.1006/geno.1993.1263 · Cited by 24 · see citing works

Expression of a PKR Dominant-Negative Mutant in Myogenic Cells Interferes with the Myogenic Process

Salzberg, S., Vilchik, S., Cohen, S., Heller, A., & Kronfeld-Kinar, Y. (2000) · Experimental Cell Research · doi:10.1006/excr.1999.4721 · Cited by 24 · see citing works

Transcriptional upregulation of interferon-induced protein kinase, PKR, in breast cancer

Nussbaum, J. M., Major, M. E., & Gunnery, S. (2003) · Cancer Letters · doi:10.1016/s0304-3835(03)00276-3 · Cited by 23 · see citing works

1H, 13C, 15N Resonance Assignment of the 20 kDa Double Stranded RNA Binding Domain of PKR

Nanduri, S., Carpick, B. W., Yang, Y., Williams, B. R. G., & Qin, J. (1998) · Journal of Biomolecular NMR · doi:10.1023/a:1008259729432 · Cited by 20 · see citing works

A point mutation in the RNA-binding domain I results in decrease of PKR activation in acute lymphoblastic leukemia

Murad, J., Tone, L. G., de Souza, L. R., & Lucca, F. L. D. (2004) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2004.08.025 · Cited by 20 · see citing works

In Vivo Regulation of the dsRNA-Dependent Protein Kinase PKR by the Cellular Glycoprotein P67

Gil, J., Estéban, M., & Roth, D. (2000) · Biochemistry · doi:10.1021/bi001754t · Cited by 20 · see citing works

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

Kmieciak, D., Kruszyna, Ł., Migdalski, P., Łaciński, M., Juszczyk, J., & Trzeciak, W. H. (2006) · Japanese Journal of Infectious Diseases · doi:10.7883/yoken.jjid.2006.92 · Cited by 20 · see citing works

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?

Squadrito, G., Raffa, G., Restuccia, T., Pollicino, T., Brancatelli, S., & Raimondo, G. (2002) · Journal of Viral Hepatitis · doi:10.1046/j.1365-2893.2002.00379.x · Cited by 19 · see citing works

Regulation of microRNA biogenesis

Ha, M., & Kim, V. N. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3838 · Cited by 5,462 · see citing works

Biogenesis of small RNAs in animals

Kim, V. N., Han, J., & Siomi, M. C. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2632 · Cited by 3,197 · see citing works

The integrated stress response

Pakos‐Zebrucka, K., Koryga, I., Mnich, K., Ljujic, M., Samali, A., & Gorman, A. M. (2016) · The EMBO Reports · doi:10.15252/embr.201642195 · Cited by 2,659 · see citing works

MicroRNA: Biogenesis, Function and Role in Cancer

MacFarlane, L.-A., & Murphy, P. R. (2010) · Current Genomics · doi:10.2174/138920210793175895 · Cited by 1,824 · see citing works

The integrated stress response: From mechanism to disease

Costa-Mattioli, M., & Walter, P. (2020) · Science · doi:10.1126/science.aat5314 · Cited by 1,617 · see citing works

RNA‐binding proteins and post‐transcriptional gene regulation

Glisovic, T., Bachorik, J. L., Yong, J., & Dreyfuss, G. (2008) · FEBS Letters · doi:10.1016/j.febslet.2008.03.004 · Cited by 1,398 · see citing works

Endoplasmic Reticulum Stress and Oxidative Stress in Cell Fate Decision and Human Disease

Cao, S. S., & Kaufman, R. J. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.5851 · Cited by 1,370 · see citing works

The eIF2α kinases: their structures and functions

Donnelly, N., Gorman, A. M., Gupta, S., & Afshin Samali, A. (2013) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-1252-6 · Cited by 860 · see citing works

The airway epithelium: soldier in the fight against respiratory viruses

Vareille, M., Kieninger, E., Edwards, M. R., & Regamey, N. (2011) · Clinical Microbiology Reviews · doi:10.1128/cmr.00014-10 · Cited by 655 · see citing works

Nanomaterial Delivery Systems for mRNA Vaccines

Buschmann, M. D., Carrasco, M. J., Alishetty, S., Paige, M., Alameh, M. G., & Weissman, D. (2021) · Vaccines · doi:10.3390/vaccines9010065 · Cited by 582 · see citing works

The landscape of mRNA nanomedicine

Huang, X., Kong, N., Zhang, X., Cao, Y., Langer, R., & Tao, W. (2022) · Nature Medicine · doi:10.1038/s41591-022-02061-1 · Cited by 511 · see citing works

Eukaryotic Initiation Factor 2 Phosphorylation and Translational Control in Metabolism

Baird, T. D., & Wek, R. C. (2012) · Advances in Nutrition · doi:10.3945/an.112.002113 · Cited by 470 · see citing works

Immunogenicity of lipid nanoparticles and its impact on the efficacy of mRNA vaccines and therapeutics

Lee, Y., Jeong, M., Park, J., Jung, H., & Lee, H. (2023) · Experimental & Molecular Medicine · doi:10.1038/s12276-023-01086-x · Cited by 477 · see citing works

How viruses hijack cell regulation

Davey, N. E., Travé, G., & Gibson, T. J. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.10.002 · Cited by 383 · see citing works

DDX1, DDX21, and DHX36 Helicases Form a Complex with the Adaptor Molecule TRIF to Sense dsRNA in Dendritic Cells

Zhang, Z., Kim, T., Bao, M., Facchinetti, V., Jung, S. Y., Ghaffari, A. A., Qin, J., Cheng, G., & Liu, Y. (2011) · Immunity · doi:10.1016/j.immuni.2011.03.027 · Cited by 376 · see citing works

Translational control in synaptic plasticity and cognitive dysfunction

Buffington, S. A., Huang, W., & Costa-Mattioli, M. (2014) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-071013-014100 · Cited by 348 · see citing works

Translation inhibition and stress granules in the antiviral immune response

McCormick, C., & Khaperskyy, D. A. (2017) · Nature reviews. Immunology · doi:10.1038/nri.2017.63 · Cited by 354 · see citing works

Genetically Engineered Microvesicles Carrying Suicide mRNA/Protein Inhibit Schwannoma Tumor Growth

Mizrak, A., Bolukbasi, M. F., Ozdener, G. B., Brenner, G. J., Madlener, S., Erkan, E. P., Ströbel, T., Breakefield, X. O., & Saydam, O. (2013) · Molecular Therapy · doi:10.1038/mt.2012.161 · Cited by 337 · see citing works

Difference in the lipid nanoparticle technology employed in three approved siRNA (Patisiran) and mRNA (COVID-19 vaccine) drugs

Suzuki, Y., & Ishihara, H. (2021) · Drug Metabolism and Pharmacokinetics · doi:10.1016/j.dmpk.2021.100424 · Cited by 304 · see citing works

A systematic approach to virus–virus interactions

DaPalma, T., Doonan, B. P., Trager, N., & Kasman, L. M. (2010) · Virus Research · doi:10.1016/j.virusres.2010.01.002 · Cited by 276 · see citing works

Both Transcriptional Regulation and Translational Control of ATF4 Are Central to the Integrated Stress Response

Dey, S., Baird, T. D., Zhou, D., Palam, L. R., Spandau, D. F., & Wek, R. C. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.167213 · Cited by 261 · see citing works

PKR: A Kinase to Remember

Gal-Ben-Ari, S., Barrera, I., Ehrlich, M., & Rosenblum, K. (2019) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2018.00480 · Cited by 258 · see citing works

RNA-binding proteins in Mendelian disease

Castelló, A., Fischer, B., Hentze, M. W., & Preiß, T. (2013) · Trends in Genetics · doi:10.1016/j.tig.2013.01.004 · Cited by 255 · see citing works

The evolutionary significance of depression in Pathogen Host Defense (PATHOS-D)

Raison, C. L., & Miller, A. H. (2013) · Molecular Psychiatry · doi:10.1038/mp.2012.2 · Cited by 253 · see citing works

NSs Protein of Rift Valley Fever Virus Induces the Specific Degradation of the Double-Stranded RNA-Dependent Protein Kinase

Habjan, M., Pichlmair, A., Elliott, R. M., Överby, A. K., Glatter, T., Gstaiger, M., Superti‐Furga, G., Unger, H., & Weber, F. (2009) · Journal of Virology · doi:10.1128/jvi.02148-08 · Cited by 253 · see citing works

Antiviral innate immunity and stress granule responses

Onomoto, K., Yoneyama, M., Fung, G., Kato, H., & Fujita, T. (2014) · Trends in Immunology · doi:10.1016/j.it.2014.07.006 · Cited by 238 · see citing works

MDA-5 Recognition of a Murine Norovirus

McCartney, S. A., Thackray, L. B., Gitlin, L., Gilfillan, S., Virgin, H. W., & Colonna, M. (2008) · PLoS Pathogens · doi:10.1371/journal.ppat.1000108 · Cited by 229 · see citing works

Suppression of PKR Promotes Network Excitability and Enhanced Cognition by Interferon-γ-Mediated Disinhibition

Zhu, P. J., Huang, W., Kalikulov, D., Yoo, J. W., Placzek, A. N., Stoica, L., Zhou, H., Bell, J. C., Friedlander, M. J., Krnjević, K., et al. (2011) · Cell · doi:10.1016/j.cell.2011.11.029 · Cited by 221 · see citing works

DHX9 Pairs with IPS-1 To Sense Double-Stranded RNA in Myeloid Dendritic Cells

Zhang, Z., Yuan, B., Lu, N., Facchinetti, V., & Liu, Y. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1101307 · Cited by 184 · see citing works

Dynamic Oscillation of Translation and Stress Granule Formation Mark the Cellular Response to Virus Infection

Ruggieri, A., Dazert, E., Metz, P., Hofmann, S., Bergeest, J.-P., Mazur, J., Bankhead, P., Hiet, M., Kallis, S., Alvisi, G., et al. (2012) · Cell Host & Microbe · doi:10.1016/j.chom.2012.05.013 · Cited by 180 · see citing works

Oxidative stress increases BACE1 protein levels through activation of the PKR-eIF2α pathway

Mouton‐Liger, F., Paquet, C., Dumurgier, J., Bouras, C., Pradier, L., Gray, F., & Hugon, J. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2012.01.009 · Cited by 176 · see citing works

Mechanisms of Mycotoxin-Induced Neurotoxicity through Oxidative Stress-Associated Pathways

Doi, K., & Uetsuka, K. (2011) · International Journal of Molecular Sciences · doi:10.3390/ijms12085213 · Cited by 174 · see citing works

The Herpes Simplex Virus 1 Us11 Protein Inhibits Autophagy through Its Interaction with the Protein Kinase PKR

Lussignol, M., Queval, C. J., Bernet‐Camard, M., Cotte-Laffitte, J., Beau, I., Codogno, P., & Esclatine, A. (2012) · Journal of Virology · doi:10.1128/jvi.01158-12 · Cited by 174 · see citing works

dsRNA-Dependent Protein Kinase PKR and its Role in Stress, Signaling and HCV Infection

Dabo, S., & MEURS, E. F. (2012) · Viruses · doi:10.3390/v4112598 · Cited by 171 · see citing works

Vorinostat and sorafenib increase ER stress, autophagy and apoptosis via ceramide-dependent CD95 and PERK activation

Park, M. A., Zhang, G., Martin, A. P., Hamed, H. A., Mitchell, C., Hylemon, P. B., Graf, M. R., Rahmani, M., Ryan, K. M., Liu, X., et al. (2008) · Cancer Biology & Therapy · doi:10.4161/cbt.7.10.6623 · Cited by 171 · see citing works

Adenosine deaminase acting on RNA (ADAR1), a suppressor of double-stranded RNA–triggered innate immune responses

Samuel, C. E. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.tm118.004166 · Cited by 172 · see citing works

Viral Subversion of Apoptotic Enzymes: Escape from Death Row

Best, S. M. (2008) · Annual Review of Microbiology · doi:10.1146/annurev.micro.62.081307.163009 · Cited by 168 · see citing works

Precursor miR-886, a novel noncoding RNA repressed in cancer, associates with PKR and modulates its activity

Lee, K., Kunkeaw, N., Jeon, S. H., Lee, I., Johnson, B. H., Kang, G., Bang, J. Y., Park, H. S., Leelayuwat, C., & Lee, Y. S. (2011) · RNA · doi:10.1261/rna.2701111 · Cited by 167 · see citing works

Designing and Building Oncolytic Viruses

Maroun, J. W., Muñoz-Alía, M. Á., Ammayappan, A., Schulze, A. J., Peng, K.-W., & Russell, S. J. (2017) · Future Virology · doi:10.2217/fvl-2016-0129 · Cited by 162 · see citing works

The fight between the teleost fish immune response and aquatic viruses

Workenhe, S. T., Rise, M. L., Kibenge, M., & Kibenge, F. S. B. (2010) · Molecular Immunology · doi:10.1016/j.molimm.2010.06.009 · Cited by 157 · see citing works

Interferon and cytokine responses to SARS-coronavirus infection

Thiel, V., & Weber, F. (2008) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2008.01.001 · Cited by 149 · see citing works

Viral modulation of programmed necrosis

Kaiser, W. J., Upton, J. W., & Mocarski, E. S. (2013) · Current Opinion in Virology · doi:10.1016/j.coviro.2013.05.019 · Cited by 149 · see citing works

Targeting endoplasmic reticulum stress in metabolic disease

Cao, S. S., & Kaufman, R. J. (2013) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2013.756471 · Cited by 149 · see citing works

Single-cell dissection of the human motor and prefrontal cortices in ALS and FTLD

Pineda, S. S., Lee, H., Fitzwalter, B. E., Mohammadi, S., Pregent, L., Gardashli, M., Mantero, J. C., Engelberg-Cook, E., DeJesus‐Hernandez, M., van Blitterswijk, M., et al. (2024) · Cell · doi:10.1016/j.cell.2024.02.031 · Cited by 150 · see citing works

The expanding roles of endoplasmic reticulum stress in virus replication and pathogenesis

Li, S., Kong, L., & Yu, X. (2013) · Critical Reviews in Microbiology · doi:10.3109/1040841x.2013.813899 · Cited by 145 · see citing works

Regulation of innate immunity by signaling pathways emerging from the endoplasmic reticulum

Martinon, F., & Glimcher, L. H. (2010) · Current Opinion in Immunology · doi:10.1016/j.coi.2010.10.016 · Cited by 144 · see citing works

Eukaryotic Initiation Factor 2 (eIF2) Signaling Regulates Proinflammatory Cytokine Expression and Bacterial Invasion

Shrestha, N., Bahnan, W., Wiley, D. J., Barber, G. N., Fields, K. A., & Schesser, K. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.375915 · Cited by 142 · see citing works

Double-stranded RNA induces disproportionate expression of thymic stromal lymphopoietin versus interferon- in bronchial epithelial cells from donors with asthma

Uller, L., Leino, M. S., Bedke, N., Sammut, D., Green, B., Lau, L., Howarth, P. H., Holgate, S. T., & Davies, D. E. (2010) · Thorax · doi:10.1136/thx.2009.125930 · Cited by 142 · see citing works

Severe Acute Respiratory Syndrome Coronavirus Triggers Apoptosis via Protein Kinase R but Is Resistant to Its Antiviral Activity

Krähling, V., Stein, D. A., Spiegel, M., Weber, F., & Mühlberger, E. (2008) · Journal of Virology · doi:10.1128/jvi.01245-08 · Cited by 141 · see citing works

Influenza A virus inhibits cytoplasmic stress granule formation

Khaperskyy, D. A., Hatchette, T. F., & McCormick, C. (2011) · The FASEB Journal · doi:10.1096/fj.11-196915 · Cited by 141 · see citing works

IFITM proteins—cellular inhibitors of viral entry

Smith, S. E., Weston, S. M., Kellam, P., & Marsh, M. (2014) · Current Opinion in Virology · doi:10.1016/j.coviro.2013.11.004 · Cited by 138 · see citing works

Editing of Cellular Self-RNAs by Adenosine Deaminase ADAR1 Suppresses Innate Immune Stress Responses

George, C. X., Ramaswami, G., Li, J. B., & Samuel, C. E. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.709014 · Cited by 138 · see citing works

Nucleoside modifications modulate activation of the protein kinase PKR in an RNA structure-specific manner

Nallagatla, S. R., & Bevilacqua, P. C. (2008) · RNA · doi:10.1261/rna.1007408 · Cited by 137 · see citing works

Targeting the ATF4 pathway in cancer therapy

Singleton, D. C., & Harris, A. L. (2012) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2012.728207 · Cited by 130 · see citing works

ADAR1 Interacts with PKR during Human Immunodeficiency Virus Infection of Lymphocytes and Contributes to Viral Replication

Clerzius, G., Gélinas, J., Daher, A., Bonnet, M., MEURS, E. F., & Gatignol, A. (2009) · Journal of Virology · doi:10.1128/jvi.02457-08 · Cited by 135 · see citing works

Regulation of innate immunity through RNA structure and the protein kinase PKR

Nallagatla, S. R., Toroney, R., & Bevilacqua, P. C. (2010) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2010.11.003 · Cited by 133 · see citing works

Integrated stress response is critical for gemcitabine resistance in pancreatic ductal adenocarcinoma

Palam, L. R., Gore, J., Craven, K. E., Wilson, J. L., & Korc, M. (2015) · Cell Death and Disease · doi:10.1038/cddis.2015.264 · Cited by 132 · see citing works

TRBP Control of PACT-Induced Phosphorylation of Protein Kinase R Is Reversed by Stress

Daher, A., Laraki, G., Singh, M., Melendez-Peña, C. E., Bannwarth, S., Peters, A. H. F. M., MEURS, E. F., Braun, R. E., Patel, R. C., & Gatignol, A. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01030-08 · Cited by 131 · see citing works

Targeting Proteotoxic Stress in Cancer: A Review of the Role that Protein Quality Control Pathways Play in Oncogenesis

Ho, M., Kavanagh, E. L., Dunne, L., Dowling, P., Zhang, L., Lindsay, S., Bazou, D., Goh, C. Y., Hanley, C., Bianchi, G., et al. (2019) · Cancers · doi:10.3390/cancers11010066 · Cited by 131 · see citing works

Dance with the Devil: Stress Granules and Signaling in Antiviral Responses

Eiermann, N., Haneke, K., Sun, Z., Stoecklin, G., & Ruggieri, A. (2020) · Viruses · doi:10.3390/v12090984 · Cited by 125 · see citing works

SARS-CoV-2 nucleocapsid protein impairs stress granule formation to promote viral replication

Zheng, Z.-Q., Wang, S.-Y., Xu, Z.-S., Fu, Y.-Z., & Wang, Y.-Y. (2021) · Cell Discovery · doi:10.1038/s41421-021-00275-0 · Cited by 127 · see citing works

Flavivirus Infection Uncouples Translation Suppression from Cellular Stress Responses

Roth, H., Magg, V., Uch, F., Mutz, P., Klein, P., Haneke, K., Lohmann, V., Bartenschlager, R. F. W., Fackler, O., Locker, N., et al. (2017) · mBio · doi:10.1128/mbio.02150-16 · Cited by 122 · see citing works

Hepatitis C Virus Controls Interferon Production through PKR Activation

Arnaud, N., Dabo, S., Maillard, P., Budkowska, A., Kalliampakou, K. I., Mavromara, P., Garcin, D., Hugon, J., Gatignol, A., Akazawa, D., et al. (2010) · PLoS ONE · doi:10.1371/journal.pone.0010575 · Cited by 120 · see citing works

Inhibition of Stress Granule Formation by Middle East Respiratory Syndrome Coronavirus 4a Accessory Protein Facilitates Viral Translation, Leading to Efficient Virus Replication

Nakagawa, K., Narayanan, K., Wada, M., & Makino, S. (2018) · Journal of Virology · doi:10.1128/jvi.00902-18 · Cited by 117 · see citing works

Induction of GADD34 Is Necessary for dsRNA-Dependent Interferon-β Production and Participates in the Control of Chikungunya Virus Infection

Clavarino, G., Cláudio, N., Couderc, T., Dalet, A., Judith, D., Camosseto, V., Schmidt, E. K., Wenger, T., Lecuit, M., Gatti, E., et al. (2012) · PLoS Pathogens · doi:10.1371/journal.ppat.1002708 · Cited by 115 · see citing works

Interactions between the double-stranded RNA-binding proteins TRBP and PACT define the Medipal domain that mediates protein-protein interactions

Laraki, G., Clerzius, G., Daher, A., Melendez-Peña, C. E., Daniels, S. M., & Gatignol, A. (2008) · RNA Biology · doi:10.4161/rna.5.2.6069 · Cited by 118 · see citing works

Human nuclear Dicer restricts the deleterious accumulation of endogenous double-stranded RNA

White, E., Schlackow, M., Kamieniarz-Gdula, K., Proudfoot, N. J., & Gullerová, M. (2014) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2827 · Cited by 118 · see citing works

Activation of the Antiviral Kinase PKR and Viral Countermeasures

Dauber, B., & Wolff, T. (2009) · Viruses · doi:10.3390/v1030523 · Cited by 117 · see citing works

TPT1/ TCTP-regulated pathways in phenotypic reprogramming

Amson, R. B., Pece, S., Marine, J., Fiore, P. P. D., & Telerman, A. (2012) · Trends in Cell Biology · doi:10.1016/j.tcb.2012.10.002 · Cited by 116 · see citing works

Allelic methylation levels of the noncoding VTRNA2-1 located on chromosome 5q31.1 predict outcome in AML

Treppendahl, M. B., Qiu, X., Helbo, A. S., Yang, X., Nandrup-Bus, C., Hother, C., Andersen, M. K., Kjeldsen, L., Möllgaard, L., Hellström‐Lindberg, E., et al. (2011) · Blood · doi:10.1182/blood-2011-06-362541 · Cited by 115 · see citing works

Evading innate immunity in nonviral mRNA delivery: don't shoot the messenger.

Devoldere, J., Dewitte, H., De Smedt, S. C., & Remaut, K. (2016) · Drug Discovery Today · doi:10.1016/j.drudis.2015.07.009 · Cited by 112 · see citing works

A Novel Intracellular Isoform of Matrix Metalloproteinase-2 Induced by Oxidative Stress Activates Innate Immunity

Lovett, D. H., Mahimkar, R., Raffaı̈, R. L., Cape, L., Maklashina, E., Cecchini, G., & Karliner, J. S. (2012) · PLoS ONE · doi:10.1371/journal.pone.0034177 · Cited by 112 · see citing works

Circular RNAs in Immune Response and Viral Infection

Yan, L., & Chen, Y. G. (2020) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2020.08.006 · Cited by 110 · see citing works

Phosphorylation of Eukaryotic Translation Initiation Factor 2α Coordinates rRNA Transcription and Translation Inhibition during Endoplasmic Reticulum Stress

DuRose, J. B., Scheuner, D. L., Kaufman, R. J., Rothblum, L. I., & Niwa, M. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00260-09 · Cited by 110 · see citing works

Blocking Double-Stranded RNA-Activated Protein Kinase PKR by Japanese Encephalitis Virus Nonstructural Protein 2A

Tu, Y.-C., Yu, C.-Y., Liang, J., Lin, E., Liao, C., & Lin, Y. (2012) · Journal of Virology · doi:10.1128/jvi.00525-12 · Cited by 108 · see citing works

Defects in interferon pathways as potential biomarkers of sensitivity to oncolytic viruses

Matveeva, O. V., & Chumakov, P. M. (2018) · Reviews in Medical Virology · doi:10.1002/rmv.2008 · Cited by 107 · see citing works

Activation of Double-stranded RNA-activated Protein Kinase (PKR) by Interferon-stimulated Gene 15 (ISG15) Modification Down-regulates Protein Translation

Okumura, F., Okumura, A. J., Uematsu, K., Hatakeyama, S., Zhang, D., & Kamura, T. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.401851 · Cited by 105 · see citing works

TCTP as therapeutic target in cancers

Acunzo, J., Baylot, V., So, A., & Rocchi, P. (2014) · Cancer Treatment Reviews · doi:10.1016/j.ctrv.2014.02.007 · Cited by 102 · see citing works

The Multiple Functions of TRBP, at the Hub of Cell Responses to Viruses, Stress, and Cancer

Daniels, S. M., & Gatignol, A. (2012) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00012-12 · Cited by 102 · see citing works

Aberrant phase separation and cancer

Taniue, K., & Akimitsu, N. (2021) · FEBS Journal · doi:10.1111/febs.15765 · Cited by 101 · see citing works

Mechanisms Employed by Herpes Simplex Virus 1 to Inhibit the Interferon Response

Paladino, P., & Mossman, K. L. (2009) · Journal of Interferon & Cytokine Research · doi:10.1089/jir.2009.0074 · Cited by 101 · see citing works

NFκB inhibitors: Strategies from poxviruses

Mohamed, M. R., & McFadden, G. (2009) · Cell Cycle · doi:10.4161/cc.8.19.9683 · Cited by 100 · see citing works

Interferon and cytokine responses to Crimean Congo hemorrhagic fever virus; an emerging and neglected viral zonoosis

Weber, F., & Mirazimi, A. (2008) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2008.11.001 · Cited by 102 · see citing works

The Anti-Hepatitis C Agent Nitazoxanide Induces Phosphorylation of Eukaryotic Initiation Factor 2α Via Protein Kinase Activated by Double-Stranded RNA Activation

Elazar, M., Liu, M. B., McKenna, S. A., Liu, P., Gehrig, E., Puglisi, J. D., Rossignol, J., & Glenn, J. S. (2009) · Gastroenterology · doi:10.1053/j.gastro.2009.07.056 · Cited by 100 · see citing works

Non-coding RNAs in homeostasis, disease and stress responses: an evolutionary perspective

Amaral, P., Dinger, M. E., & Mattick, J. S. (2013) · Briefings in Functional Genomics · doi:10.1093/bfgp/elt016 · Cited by 99 · see citing works

Macroautophagy Signaling and Regulation

Esclatine, A., Chaumorcel, M., & Codogno, P. (2009) · Current topics in microbiology and immunology · doi:10.1007/978-3-642-00302-8_2 · Cited by 99 · see citing works

Robust expression of vault RNAs induced by influenza A virus plays a critical role in suppression of PKR-mediated innate immunity

Li, F., Chen, Y., Zhang, Z., Ouyang, J., Wang, Y., Yan, R., Huang, S., Gao, G. F., Guo, G., & Chen, J. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv1078 · Cited by 97 · see citing works

Rabies Virus Infection Induces the Formation of Stress Granules Closely Connected to the Viral Factories

Nikolić, J., Civas, A., Zoé, L., Lagaudrière‐Gesbert, C., & Blondel, D. (2016) · PLoS Pathogens · doi:10.1371/journal.ppat.1005942 · Cited by 97 · see citing works

A Novel Mitochondrial MAVS/Caspase-8 Platform Links RNA Virus–Induced Innate Antiviral Signaling to Bax/Bak-Independent Apoptosis

Maadidi, S. E., Faletti, L. E., Berg, B., Wenzl, C., Wieland, K., Chen, Z. J., Maurer, U., & Borner, C. (2014) · The Journal of Immunology · doi:10.4049/jimmunol.1300842 · Cited by 95 · see citing works

Inhibiting the integrated stress response pathway prevents aberrant chondrocyte differentiation thereby alleviating chondrodysplasia

Wang, C., Tan, Z., Niu, B., Tsang, K. Y., Tai, A. C. P., Chan, W. C. W., Lo, R. L. K., Leung, K. K. H., Dung, N. W. F., Itoh, N., et al. (2018) · eLife · doi:10.7554/elife.37673 · Cited by 87 · see citing works

Enhancement of Replication of RNA Viruses by ADAR1 via RNA Editing and Inhibition of RNA-Activated Protein Kinase

Gélinas, J., Clerzius, G., Shaw, E., & Gatignol, A. (2011) · Journal of Virology · doi:10.1128/jvi.00240-11 · Cited by 95 · see citing works

Exploration of Pattern Recognition Receptor Agonists as Candidate Adjuvants

Ong, G. H., Lian, B. S. X., Kawasaki, T., & Kawai, T. (2021) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2021.745016 · Cited by 95 · see citing works

Inhibition of PKR by Viruses

Cesaro, T., & Michiels, T. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.757238 · Cited by 91 · see citing works

Innate Immunity in the Female Reproductive Tract: Role of Sex Hormones in Regulating Uterine Epithelial Cell Protection Against Pathogens

Ochiel, D. O., Fahey, J. V., Ghosh, M., Haddad, S. N., & Wira, C. R. (2008) · Current Women s Health Reviews · doi:10.2174/157340408784246395 · Cited by 90 · see citing works

An eIF2α-binding motif in protein phosphatase 1 subunit GADD34 and its viral orthologs is required to promote dephosphorylation of eIF2α

Rojas, M., Vasconcelos, G., & Dever, T. E. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1501557112 · Cited by 88 · see citing works

PfeIK1, a eukaryotic initiation factor 2α kinase of the human malaria parasite Plasmodium falciparum, regulates stress-response to amino-acid starvation

Fennell, C., Babbitt, S. E., Russo, I., Wilkes, J., Ranford-Cartwright, L. C., Goldberg, D. E., & Doerig, C. (2009) · Malaria Journal · doi:10.1186/1475-2875-8-99 · Cited by 88 · see citing works

CCCP‐induced mitochondrial dysfunction – characterization and analysis of integrated stress response to cellular signaling and homeostasis

Koncha, R. R., Ramachandran, G., Sepuri, N. B. V., & Ramaiah, K. V. A. (2021) · FEBS Journal · doi:10.1111/febs.15868 · Cited by 85 · see citing works

siRNA Functionalized Lipid Nanoparticles (LNPs) in Management of Diseases

Kalita, T., Dezfouli, S. A., Pandey, L. M., & Uludağ, H. (2022) · Pharmaceutics · doi:10.3390/pharmaceutics14112520 · Cited by 87 · see citing works

Efficiency of poly (A).poly(U) as an adjuvant

Hovanessian, A. G., GALABRU, J., Rivière, Y., & Montagnier, L. (1988) · Immunology Today · doi:10.1016/0167-5699(88)91288-1 · Cited by 41 · see citing works

266 The interferon sensitivity of tick-borne encephalitis virus is partially mediated by double-stranded RNA-dependent protein kinase

Överby, A. K., & Weber, F. (2008) · Cytokine · doi:10.1016/j.cyto.2008.07.348 · Cited by 1 · see citing works

PKR

(2008) · Springer eBooks · doi:10.1007/978-1-4020-6754-9_12924

The dsRNA-dependent protein kinase, PKR and cell death

Barber, G. N. (2005) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401643 · Cited by 90 · see citing works

Impact of Protein Kinase PKR in Cell Biology: from Antiviral to Antiproliferative Action

García, M. A., Gil, J., Ventoso, I., Guerra, S., Domingo, E., Rivas, C., & Esteban, M. (2006) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00027-06 · Cited by 818 · see citing works