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, Andrew R; Hoi-Tao Wong, Andrew; Wai Ning Tam, Nancy; Li, Suiyang; Koromilas, Antonis E

doi:10.1038/sj.onc.1202620

Cited by 204Cancer-related Molecular Pathwaysinterferon and immune responsesPI3K/AKT/mTOR signaling in cancer

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, Andrew R, Hoi-Tao Wong, Andrew, Wai Ning Tam, Nancy, Li, Suiyang, Koromilas, Antonis E·1999·Oncogene

DOI 10.1038/sj.onc.1202620

Open this paper in CoChat — free account

Abstract

The tumor suppressor p53 is a multifunctional protein that plays a critical role in modulating cellular responses upon DNA damage or other stresses. These functions of p53 are regulated both by protein-protein interactions and phosphorylation. The double-stranded RNA activated protein kinase PKR is a serine/threonine kinase that modulates protein synthesis through the phosphorylation of translation initiation factor eIF-2alpha. PKR is an interferon (IFN)-inducible protein that is thought to mediate the anti-viral and anti-proliferative effects of IFN via its capacity to inhibit protein synthesis. Here we report that PKR physically associates with p53. The interaction of PKR with p53 is enhanced by IFNs and upon conditions that p53 acquires a wild type conformation. PKR/p53 complex formation in vitro requires the N-terminal regulatory domain of PKR and the last 30 amino acids of the C-terminus of human p53. In addition, p53 may function as a substrate of PKR since phosphorylation of human p53 on serine392 is induced by activated PKR in vitro. These novel findings raise the possibility of a functional interaction between PKR and p53 in vivo, which may account, at least in part, for the ability of each protein to regulate gene expression at both the transcriptional and the translational levels.

Integrity signals

Registry

Crossref · 10.1038/sj.onc.1202620

Cites

68 of 68 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

PKR is physically associated with p53 and phosphorylated it in mouse embryo fibroblasts cells treated with IFN.
“It is known that PKR is physically associated with p53 and phosphorylated it in mouse embryo fibroblasts cells treated with IFN [64].”
From PKR, the double stranded RNA‐dependent protein kinase as a critical target in Alzheimer's disease (2009) · cites this paper as [64]

Molecular Cloning: A Laboratory Manual
Sambrook, J., Fritsch, E., & Maniatis, T. (1989) · UCLA - Biblioteca de Ciencias de la Salud · Cited by 133,589 · see citing works
Molecular cloning: A laboratory manual
Deininger, P. L. (1990) · Analytical Biochemistry · doi:10.1016/0003-2697(90)90595-z · Cited by 84,684 · see citing works
WAF1, a potential mediator of p53 tumor suppression
El-Deiry, W. S., Tokino, T., Velculescu, V. E., Levy, D. B., Parsons, R., Trent, J. M., Lin, D., Mercer, W. E., Kinzler, K. W., & Vogelstein, B. (1993) · Cell · doi:10.1016/0092-8674(93)90500-p · Cited by 8,321 · see citing works
p53, the cellular gatekeeper for growth and division
Levine, A. J. (1997) · Cell · doi:10.1016/s0092-8674(00)81871-1 · Cited by 7,693 · see citing works
The p21 Cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin-dependent kinases.
Wade Harper, J. (1993) · Cell · doi:10.1016/0092-8674(93)90499-g · Cited by 5,651 · see citing works
Tumor suppressor p53 is a direct transcriptional activator of the human bax gene
Toshiyuki, M., & Reed, J. C. (1995) · Cell · doi:10.1016/0092-8674(95)90412-3 · Cited by 4,063 · see citing works
p53: puzzle and paradigm.Preprint
Ko, L. J., & Prives, C. L. (1996) · Genes & Development · doi:10.1101/gad.10.9.1054 · Cited by 2,338 · see citing works
pEF-BOS, a powerful mammalian expression vector
Mizushima, S., & Nagata, S. (1990) · Nucleic Acids Research · doi:10.1093/nar/18.17.5322 · Cited by 1,632 · see citing works
A novel form of Epstein-Barr virus latency in normal B cells in vivo
Miyashita, E. M., Yang, B., Lam, K. M. C., Crawford, D., & Thorley‐Lawson, D. A. (1995) · Cell · doi:10.1016/0092-8674(95)90513-8 · Cited by 1,591 · see citing works
[11] Phosphopeptide mapping and phosphoamino acid analysis by two-dimensional separation on thin-layer cellulose plates
Boyle, W. J., van der Geer, P., & Hunter, T. R. (1991) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(91)01013-r · Cited by 1,452 · see citing works
Life, death, and the pursuit of apoptosis.Preprint
White, E. (1996) · Genes & Development · doi:10.1101/gad.10.1.1 · Cited by 1,300 · see citing works
Regulation of the specific DNA binding function of p53
Hupp, T. R., Meek, D. W., Midgley, C., & Lane, D. P. (1992) · Cell · doi:10.1016/0092-8674(92)90562-q · Cited by 905 · see citing works
Solubilization and Purification of Enzymatically Active Glutathione S-Transferase (pGEX) Fusion Proteins
Frangioni, J. V., & Neel, B. G. (1993) · Analytical Biochemistry · doi:10.1006/abio.1993.1170 · Cited by 883 · see citing works
Wild-type p53 mediates apoptosis by E1A, which is inhibited by E1B.Preprint
Debbas, M. E., & White, E. (1993) · Genes & Development · doi:10.1101/gad.7.4.546 · Cited by 871 · see citing works
p53-Dependent apoptosis in the absence of transcriptional activation of p53-target genes
Caelles, C., Helmberg, A., & Karin, M. (1994) · Nature · doi:10.1038/370220a0 · Cited by 843 · see citing works
Binding and modulation of p53 by p300/CBP coactivators
Lill, N. L., Grossman, S. R., Ginsberg, D., DeCaprio, J. A., & Livingston, D. M. (1997) · Nature · doi:10.1038/42981 · Cited by 693 · see citing works
Mapping of the p53 and mdm-2 Interaction Domains
Chen, J., Maréchal, V., & Levine, A. J. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.7.4107 · Cited by 689 · see citing works
Recruitment of p300/CBP in p53-Dependent Signal Pathways
Avantaggiati, M. L., Ogryzko, V. V., Gardner, K., Giordano, A., Levine, A. S., & Kelly, K. (1997) · Cell · doi:10.1016/s0092-8674(00)80304-9 · Cited by 668 · 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
The Double-Stranded RNA-Dependent Protein Kinase PKR: Structure and Function
Clemens, M. J., & Elia, A. (1997) · Journal of Interferon & Cytokine Research · doi:10.1089/jir.1997.17.503 · Cited by 605 · see citing works
Synergistic activation of transcription by CBP and p53
Gu, W., Shi, X.-L., & Roeder, R. G. (1997) · Nature · doi:10.1038/42972 · Cited by 596 · 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
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
Self-citation
Translational control
(1991) · Journal of Cellular Biochemistry · doi:10.1002/jcb.240470805 · Cited by 433 · 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
p53 and its 14 kDa C-terminal domain recognize primary DNA damage in the form of insertion/deletion mismatches
Lee, S., Elenbaas, B., Levine, A. J., & Griffith, J. D. (1995) · Cell · doi:10.1016/s0092-8674(05)80006-6 · Cited by 405 · 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
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
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
Protein Phosphorylation Controls Translation Rates
Hershey, J. W. B. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)30005-5 · Cited by 293 · see citing works
Negative feedback regulation of wild‐type p53 biosynthesis.
Mosner, J., Mummenbrauer, T., Bauer, C., Sczakiel, G., Große, F., & Deppert, W. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb00123.x · Cited by 286 · see citing works
p53 binds single-stranded DNA ends and catalyzes DNA renaturation and strand transfer.
Bakalkin, G. Y., Yakovleva, T., Selivanova, G., Magnússon, K. P., Székely, L., Владимировна, К. Е., Klein, G., Terenius, L. Y., & Wiman, K. G. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.1.413 · Cited by 274 · see citing works
p53 domains: identification and characterization of two autonomous DNA-binding regions.Preprint
Wang, Y., Reed, M. J., Wang, P., Stenger, J. E., Mayr, G. A., Anderson, M. E., Schwedes, J. F., & Tegtmeyer, P. (1993) · Genes & Development · doi:10.1101/gad.7.12b.2575 · Cited by 239 · see citing works
p53‐catalyzed annealing of complementary single‐stranded nucleic acids.
Oberosler, P., Hloch, P., Ramsperger, U., & Stahl, H. D. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb05893.x · Cited by 222 · see citing works
Functional expression and RNA binding analysis of the interferon-induced, double-stranded RNA-activated, 68,000-Mr protein kinase in a cell-free system.
Katze, M. G., Wambach, M., Wong, M., Garfinkel, M. S., MEURS, E. F., Chong, K. L., Williams, B. R. G., Hovanessian, A. G., & Barber, G. N. (1991) · Molecular and Cellular Biology · doi:10.1128/mcb.11.11.5497 · Cited by 203 · see citing works
Regulation of the Sequence-specific DNA Binding Function of p53 by Protein Kinase C and Protein Phosphatases
Takenaka, I. M., Morin, F., Seizinger, B. R., & Kley, N. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.10.5405 · Cited by 197 · see citing works
Wild‐type p53 adopts a ‘mutant’‐like conformation when bound to DNA.
Halazonetis, T. D., Davis, L. J., & Kandil, A. N. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb05743.x · Cited by 193 · see citing works
Physical association between STAT1 and the interferon‐inducible protein kinase PKR and implications for interferon and double‐stranded RNA signaling pathways
Wong, A. H.-T., Tam, N. W. N., Yang, Y.-L., Cuddihy, A., Li, S.-Y., Kirchhoff, S., Hauser, H., Decker, T., & Koromilas, A. (1997) · EMBO Journal · doi:10.1093/emboj/16.6.1291 · Cited by 187 · see citing works
Self-citation
The C-terminal domain of p53 recognizes DNA damaged by ionizing radiation.
Reed, M. J., Woelker, B., Wang, P., Wang, Y., Anderson, M. E., & Tegtmeyer, P. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.21.9455 · Cited by 187 · see citing works
Two Domains of p53 Interact with the TATA-Binding Protein, and the Adenovirus 13S E1A Protein Disrupts the Association, Relieving p53-Mediated Transcriptional Repression
Horikoshi, N., Usheva, A., Chen, J., Levine, A. J., Weinmann, R. S., & Shenk, T. E. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.1.227 · Cited by 182 · see citing works
Translational initiation factor and ribosome association with the cytoskeletal framework fraction from HeLa cells
Howe, J. G., & Hershey, J. W. B. (1984) · Cell · doi:10.1016/0092-8674(84)90303-9 · Cited by 178 · see citing works
Regulation of the interferon-induced PKR: can viruses cope?
Katze, M. G. (1995) · Trends in Microbiology · doi:10.1016/s0966-842x(00)88880-0 · Cited by 174 · see citing works
An essential role for the interferon-inducible, double-stranded RNA-activated protein kinase PKR in the tumor necrosis factor-induced apoptosis in U937 cells.
Yeung, M. C., Liu, J., & Lau, A. S. Y. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.22.12451 · Cited by 172 · see citing works
p53-dependent repression of CDK4 translation in TGF-beta-induced G1 cell-cycle arrest.Preprint
Ewen, M. E., Oliver, C. J., Sluss, H. K., Miller, S. J., & Peeper, D. S. (1995) · Genes & Development · doi:10.1101/gad.9.2.204 · Cited by 165 · see citing works
p53 binds single-stranded DNA ends through the C-terminal domain and internal DNA segments via the middle domain
Bakalkin, G. Y., Selivanova, G., Yakovleva, T., Владимировна, К. Е., Kashuba, E., Magnússon, K. P., Székely, L., Klein, G., Terenius, L. Y., & Wiman, K. G. (1995) · Nucleic Acids Research · doi:10.1093/nar/23.3.362 · Cited by 163 · see citing works
Ultraviolet radiation, but not γ radiation or etoposide-induced DNA damage, results in the phosphorylation of the murine p53 protein at serine-389
Lu, H., Taya, Y., Ikeda, M., & Levine, A. J. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6399 · Cited by 162 · see citing works
The Interferon-Inducible p202 Protein as a Modulator of Transcription: Inhibition of NF-κB, c-Fos, and c-Jun Activities
Wang, M., Ghosh, S., & Lengyel, P. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.1.359 · Cited by 148 · 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
Translational regulation of human p53 gene expression.
Fu, L., Minden, M. D., & Benchimol, S. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00812.x · Cited by 138 · see citing works
Repression of endogenous p53 transactivation function in HeLa cervical carcinoma cells by human papillomavirus type 16 E6, human mdm-2, and mutant p53
Hoppe‐Seyler, F., & Butz, K. (1993) · Journal of Virology · doi:10.1128/jvi.67.6.3111-3117.1993 · Cited by 134 · see citing works
Mutants of the RNA-Dependent Protein Kinase (PKR) Lacking Double-Stranded RNA Binding Domain I Can Act as Transdominant Inhibitors and Induce Malignant Transformation
Barber, G. N., Wambach, M., Thompson, S., Jagus, R., & Katze, M. G. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.6.3138 · Cited by 134 · 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
Participation of the human p53 3′UTR in translational repression and activation following γ‐irradiation
Fu, L., & Benchimol, S. (1997) · The EMBO Journal · doi:10.1093/emboj/16.13.4117 · Cited by 116 · see citing works
Histidyl-tRNA Synthetase-related Sequences in GCN2 Protein Kinase Regulate in Vitro Phosphorylation of eIF-2
Zhu, S., Sobolev, A. Y., & Wek, R. C. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.40.24989 · Cited by 115 · see citing works
Alternatively Spliced Forms in the Carboxy-Terminal Domain of the p53 Protein Regulate Its Ability to Promote Annealing of Complementary Single Strands of Nucleic Acids
Wu, L., Bayle, J. H., Elenbaas, B., Pavletich, N. P., & Levine, A. J. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.1.497 · Cited by 108 · see citing works
Binding of an Interferon-inducible Protein (p202) to the Retinoblastoma Protein
Choubey, D., & Lengyel, P. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.11.6134 · Cited by 105 · see citing works
Inhibition of E2F‐mediated transcription by p202.
Choubey, D., Li, S. J., Datta, B., Gutterman, J. U., & Lengyel, P. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00951.x · Cited by 104 · see citing works
Self-citation
p53 Is Covalently Linked to 5.8S rRNA
Fontoura, B. M. A., Sorokina, E. A., David, E., & Carroll, R. B. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.11.5145 · Cited by 102 · see citing works
Two Functionally Distinct RNA-Binding Motifs in the Regulatory Domain of the Protein Kinase DAI
Green, S. R., Manche, L., & Mathews, M. B. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.1.358 · Cited by 102 · see citing works
p202, an Interferon-inducible Modulator of Transcription, Inhibits Transcriptional Activation by the p53 Tumor Suppressor Protein, and a Segment from the p53-binding Protein 1 That Binds to p202 Overcomes This Inhibition
Datta, B., Li, B., Choubey, D., Nallur, G., & Lengyel, P. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.44.27544 · Cited by 102 · see citing works
The carboxyl-terminal domain of the p53 protein regulates sequence-specific DNA binding through its nonspecific nucleic acid-binding activity.
Bayle, J. H., Elenbaas, B., & Levine, A. J. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.12.5729 · Cited by 102 · see citing works
How Phosphorylation Regulates the Activity of p53
Steegenga, W. T., van der Eb, A. J., & Jochemsen, A. G. (1996) · Journal of Molecular Biology · doi:10.1006/jmbi.1996.0560 · Cited by 97 · see citing works
Cytoplasmic p53 Polypeptide Is Associated with Ribosomes
Fontoura, B. M. A., Atienza, C. A., Sorokina, E. A., Morimoto, T., & Carroll, R. B. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.6.3146 · Cited by 64 · see citing works
p53 and translational control
Ewen, M. E., & Miller, S. J. (1996) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/0304-419x(95)00010-d · Cited by 54 · see citing works
Mutagenesis in the P53 gene
Pfeifer, G. P., & Holmquist, G. P. (1997) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/s0304-419x(97)00004-8 · Cited by 38 · see citing works
Excitons in parabolic quantum dots in electric and magnetic fields
Jaziri, S., & Bennaceur, R. (1994) · Semiconductor Science and Technology · doi:10.1088/0268-1242/9/10/003 · Cited by 35 · see citing works
Interaction of the Human Protein Kinase PKR with the Mouse PKR Homolog Occurs via the N-Terminal Region of PKR and Does Not Inactivate Autophosphorylation Activity of Mouse PKR
Rende-Fournier, R., Ortega, L. G., George, C. X., & Samuel, C. E. (1997) · Virology · doi:10.1006/viro.1997.8824 · Cited by 12 · see citing works

Flagged first, then by citations

Sorted by citations

Interferons and viruses: an interplay between induction, signalling, antiviral responses and virus countermeasures
Randall, R. E., & Goodbourn, S. (2007) · Journal of General Virology · doi:10.1099/vir.0.83391-0 · Cited by 1,559 · see citing works
Post-translational modification of p53 in tumorigenesis
Bode, A. M., & Dong, Z. (2004) · Nature Reviews Cancer · doi:10.1038/nrc1455 · Cited by 1,270 · see citing works
Post‐translational modifications and activation of p53 by genotoxic stresses
Appella, E., & Anderson, C. W. (2001) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2001.02225.x · Cited by 1,071 · 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
The human homologs of checkpoint kinases Chk1 and Cds1 (Chk2) phosphorylate p53 at multiple DNA damage-inducible sites.
Shieh, S.-Y., Ahn, J., Tamai, K., Taya, Y., & Prives, C. (2000) · Genes & Development · doi:10.1101/gad.14.3.289 · Cited by 972 · 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
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
Regulation of Protein Synthesis by Hypoxia via Activation of the Endoplasmic Reticulum Kinase PERK and Phosphorylation of the Translation Initiation Factor eIF2α
Koumenis, C., Naczki, C., Koritzinsky, M., Rastani, S., Diehl, J. A., Sonenberg, N., Koromilas, A. E., & Wouters, B. G. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.21.7405-7416.2002 · Cited by 688 · see citing works
Self-citation
PKR; a sentinel kinase for cellular stress
Williams, B. R. (1999) · Oncogene · doi:10.1038/sj.onc.1203127 · Cited by 820 · see citing works
The dsRNA protein kinase PKR: Virus and cell control
García, M. A., Meurs, E. F., & Esteban, M. (2007) · Biochimie · doi:10.1016/j.biochi.2007.03.001 · Cited by 644 · see citing works
Phosphorylation by aurora kinase A induces Mdm2-mediated destabilization and inhibition of p53
Katayama, H. G., Sasai, K., Kawai, H., Yuan, Z.-M., Bondaruk, J. E., Suzuki, F., Fujii, S., Arlinghaus, R. B., Czerniak, B. A., & Sen, S. (2003) · Nature Genetics · doi:10.1038/ng1279 · Cited by 586 · see citing works
Induction of apoptosis by the dsRNA-dependent protein kinase (PKR): Mechanism of action
Gil, J., & Estéban, M. (2000) · APOPTOSIS · doi:10.1023/a:1009664109241 · Cited by 369 · 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
CAJAL BODIES: A Long History of Discovery
Cioce, M., & Lamond, A. I. (2005) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.20.010403.103738 · Cited by 359 · see citing works
GPS 5.0: An Update on the Prediction of Kinase-Specific Phosphorylation Sites in Proteins
Wang, C., Xu, H., Lin, S., Deng, W., Zhou, J., Zhang, Y. W., Shi, Y., Peng, D., & Xue, Y. (2020) · Genomics Proteomics & Bioinformatics · doi:10.1016/j.gpb.2020.01.001 · Cited by 297 · see citing works
A role for the p38 mitogen-acitvated protein kinase pathway in the transcriptional activation of p53 on genotoxic stress by chemotherapeutic agents.
Sánchez‐Prieto, R., Rojas, J. M., Taya, Y., & Gutkind, J. S. (2000) · PubMed · Cited by 264 · 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
Endoplasmic reticulum stress induces p53 cytoplasmic localization and prevents p53-dependent apoptosis by a pathway involving glycogen synthase kinase-3βPreprint
Qu, L.-K., Huang, S. H., Baltzis, D., Rivas-Estilla, A.-M., Pluquet, O., Hatzoglou, M., Koumenis, C., Taya, Y., Yoshimura, A., & Koromilas, A. E. (2004) · Genes & Development · doi:10.1101/gad.1165804 · Cited by 247 · see citing works
Self-citation
Curaxins: Anticancer Compounds That Simultaneously Suppress NF-κB and Activate p53 by Targeting FACT
Gasparian, A. V., Burkhart, C. A., Purmal, A. A., Brodsky, L., Pal, M., Saranadasa, M., Bosykh, D. A., Commane, M., Guryanova, O. A., Pal, S., et al. (2011) · Science Translational Medicine · doi:10.1126/scitranslmed.3002530 · Cited by 237 · see citing works
Dial 9-1-1 for p53: Mechanisms of p53 Activation by Cellular Stress
Ljungman, M. E. (2000) · Neoplasia · doi:10.1038/sj.neo.7900073 · Cited by 218 · see citing works
Initiation Factor eIF2α Phosphorylation in Stress Responses and Apoptosis
Clemens, M. J. (2001) · Progress in molecular and subcellular biology · doi:10.1007/978-3-662-09889-9_3 · Cited by 216 · see citing works
Structure and Function of the Protein Kinase R
Sadler, A. J., & Williams, B. R. G. (2007) · Springer eBooks · doi:10.1007/978-3-540-71329-6_13 · Cited by 203 · see citing works
p53 Signaling and Cell Cycle Checkpoints
Stewart, Z. A., & Pietenpol, J. A. (2001) · Chemical Research in Toxicology · doi:10.1021/tx000199t · Cited by 200 · see citing works
The Role of Protein Kinase R in the Interferon Response
Pindel, A., & Sadler, A. J. (2010) · Journal of Interferon & Cytokine Research · doi:10.1089/jir.2010.0099 · Cited by 182 · 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
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
Influenza Virus Infection Increases p53 Activity: Role of p53 in Cell Death and Viral Replication
Turpin, E. A., Luke, K., Jones, J. C., Tumpey, T. M., Konan, K. V., & Schultz‐Cherry, S. (2005) · Journal of Virology · doi:10.1128/jvi.79.14.8802-8811.2005 · Cited by 160 · see citing works
Strategies for manipulating the p53 pathway in the treatment of human cancer
Hupp, T. R., Lane, D. P., & Ball, K. L. (2000) · Biochemical Journal · doi:10.1042/bj3520001 · Cited by 148 · 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
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
Self-citation
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
Dual Role of p53 in Innate Antiviral Immunity
Rivas, C., Aaronson, S. A., & Muñoz‐Fontela, C. (2010) · Viruses · doi:10.3390/v2010298 · Cited by 131 · 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
Increased Sensitivity to UV Radiation in Mice with a p53 Point Mutation at Ser389
Bruins, W., Zwart, E., Attardi, L. D., Iwakuma, T., Hoogervorst, E. M., Beems, R. B., Miranda, B., van Oostrom, C. T. M., van den Berg, J., van den Aardweg, G. J., et al. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.20.8884-8894.2004 · Cited by 121 · see citing works
Roles of the translation initiation factor eIF2α serine 51 phosphorylation in cancer formation and treatment
Koromilas, A. E. (2014) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2014.12.007 · Cited by 119 · see citing works
Self-citation
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
Activated double-stranded RNA-dependent protein kinase and neuronal death in models of Alzheimer’s disease
Page, G., Rioux Bilan, A., Ingrand, S., Lafay-Chebassier, C., Pain, S., Perault Pochat, M. C., Bouras, C., Bayer, T., & Hugon, J. (2006) · Neuroscience · doi:10.1016/j.neuroscience.2006.01.047 · Cited by 116 · see citing works
Binding and Nuclear Relocalization of Protein Kinase R by Human Cytomegalovirus TRS1
Hakki, M., Marshall, E. E., Niro, K. L. D., & Geballe, A. P. (2006) · Journal of Virology · doi:10.1128/jvi.00957-06 · Cited by 112 · see citing works
13 The Double-stranded RNA-activated Protein Kinase PKRPreprint
Kaufman, R. J. (2000) · Cold Spring Harbor Monograph Archive · doi:10.1101/087969618.39.503 · Cited by 111 · see citing works
Activation of the cell stress kinase PKR in Alzheimer's disease and human amyloid precursor protein transgenic mice
Peel, A. (2003) · Neurobiology of Disease · doi:10.1016/s0969-9961(03)00086-x · Cited by 125 · see citing works
Cdk5 phosphorylates p53 and regulates its activity
Zhang, J., Krishnamurthy, P., & Johnson, G. V. W. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.00824.x · Cited by 108 · see citing works
Interferon, a growing cytokine family: 50 years of interferon research
Chelbi‐Alix, M. K., & Wietzerbin, J. (2007) · Biochimie · doi:10.1016/j.biochi.2007.05.001 · Cited by 108 · see citing works
Temporal Gene Regulation During HIV-1 Infection of Human CD4+ T CellsPreprint
Corbeil, J., Sheeter, D. A., Genini, D., Rought, S. E., Leoni, L. M., Du, P., Ferguson, M., Masys, D. R., Welsh, J. B., Fink, J. L., et al. (2001) · Genome Research · doi:10.1101/gr.180201 · Cited by 106 · see citing works
The impact of PKR activation: from neurodegeneration to cancer
Marchal, J. A., López, G., Perán, M., Comino, A., Delgado, J. R., Garcı́a-Garcı́a, J., Conde, V., Aranda, F. M., Rivas, C., Estéban, M., et al. (2014) · The FASEB Journal · doi:10.1096/fj.13-248294 · Cited by 104 · see citing works
Protein Kinase R (PKR) Interacts with and Activates Mitogen-activated Protein Kinase Kinase 6 (MKK6) in Response to Double-stranded RNA Stimulation
Silva, A. M., Whitmore, M., Xu, Z., Jiang, Z., Li, X., & Williams, B. R. G. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406554200 · Cited by 103 · see citing works
The B56α Regulatory Subunit of Protein Phosphatase 2A Is a Target for Regulation by Double-Stranded RNA-Dependent Protein Kinase PKR
Xu, Z., & Williams, B. R. G. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.14.5285-5299.2000 · Cited by 113 · see citing works
Serine 392 phosphorylation modulates p53 mitochondrial translocation and transcription-independent apoptosis
Castrogiovanni, C., Waterschoot, B., Backer, O. D., & Dumont, P. (2017) · Cell Death and Differentiation · doi:10.1038/cdd.2017.143 · Cited by 100 · see citing works
Presenilin-1 Mutations Sensitize Neurons to DNA Damage-Induced Death by a Mechanism Involving Perturbed Calcium Homeostasis and Activation of Calpains and Caspase-12
Chan, S. L., Culmsee, C., Haughey, N. J., Klapper, W., & Mattson, M. P. (2002) · Neurobiology of Disease · doi:10.1006/nbdi.2002.0542 · Cited by 98 · see citing works
Interferons and Apoptosis
Clemens, M. J. (2003) · Journal of Interferon & Cytokine Research · doi:10.1089/107999003766628124 · Cited by 96 · see citing works
Phosphorylation of serine 392 in p53 is a common and integral event during p53 induction by diverse stimuli
Cox, M. L., & Meek, D. W. (2009) · Cellular Signalling · doi:10.1016/j.cellsig.2009.11.014 · Cited by 95 · see citing works
Interferons α and γ induce p53-dependent and p53-independent apoptosis, respectively
Porta, C., Hadj-Slimane, R., Nejmeddine, M., Pampin, M., Tovey, M. G., Espert, L., Alvarez, S., & Chelbi‐Alix, M. K. (2004) · Oncogene · doi:10.1038/sj.onc.1208204 · Cited by 94 · see citing works
Protein serine/threonine phosphatase-1 dephosphorylates p53 at Ser-15 and Ser-37 to modulate its transcriptional and apoptotic activities
Li, D. W.-C., Liu, J.-P., Schmid, P. C., Schlosser, R., Feng, H., Liu, W.-B., Yan, Q., Gong, L., Sun, S.-M., Deng, M., et al. (2006) · Oncogene · doi:10.1038/sj.onc.1209334 · Cited by 94 · see citing works
p53 activation results in rapid dephosphorylation of the eIF4E-binding protein 4E-BP1, inhibition of ribosomal protein S6 kinase and inhibition of translation initiation
Horton, L. E., Bushell, M., Baus, D., Tilleray, V. J., Clemens, M. J., & Hensold, J. O. (2002) · Oncogene · doi:10.1038/sj.onc.1205662 · Cited by 92 · see citing works
Inhibition of PKR by Viruses
Cesaro, T., & Michiels, T. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.757238 · Cited by 93 · see citing works
Stoichiometric Phosphorylation of Human p53 at Ser315Stimulates p53-dependent Transcription
Blaydes, J. P., Luciani, M. G., Pospı́šilová, Š., Ball, H. M.-L., Vojtesek, B., & Hupp, T. R. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m003485200 · Cited by 90 · see citing works
Endogenous Double-Stranded RNA
Sadeq, S., Al-Hashimi, S., Cusack, C. M., & Werner, A. (2021) · Non-Coding RNA · doi:10.3390/ncrna7010015 · Cited by 81 · see citing works
Controlling activation of the RNA-dependent protein kinase by siRNAs using site-specific chemical modification
Puthenveetil, S., Whitby, L. R., Ren, J., Kelnar, K., Krebs, J., & Beal, P. A. (2006) · Nucleic Acids Research · doi:10.1093/nar/gkl464 · Cited by 80 · see citing works
Fanconi anemia type C and p53 cooperate in apoptosis and tumorigenesis
Freie, B. W., Li, X., Ciccone, S. L. M., Nawa, K., Cooper, S. H., Vogelweid, C. M., Schantz, L. D., Haneline, L. S., Orazi, A., Broxmeyer, H. E., et al. (2003) · Blood · doi:10.1182/blood-2003-03-0971 · Cited by 76 · see citing works
Malignant transformation of B lymphoma cell line BJAB by Epstein–Barr virus‐encoded small RNAs
Yamamoto, N., Takizawa, T., Iwanaga, Y., Shimizu, N., & Yamamoto, N. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)02145-1 · Cited by 76 · see citing works
The Atlantic salmon Z‐DNA binding protein kinase phosphorylates translation initiation factor 2 alpha and constitutes a unique orthologue to the mammalian dsRNA‐activated protein kinase R
Bergan, V., Jagus, R., Lauksund, S., Kileng, Ø., & Robertsen, B. (2007) · FEBS Journal · doi:10.1111/j.1742-4658.2007.06188.x · Cited by 72 · see citing works
Modulation of the Eukaryotic Initiation Factor 2 α-Subunit Kinase PERK by Tyrosine Phosphorylation
Su, Q., Wang, S., Gao, H. Q., Kazemi, S., Harding, H. P., Ron, D., & Koromilas, A. E. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704612200 · Cited by 71 · see citing works
Self-citation
Increased p53 phosphorylation after microtubule disruption is mediated in a microtubule inhibitor- and cell-specific manner
Stewart, Z. A., Tang, L. J., & Pietenpol, J. A. (2001) · Oncogene · doi:10.1038/sj.onc.1204060 · Cited by 66 · see citing works
PKR in Innate Immunity, Cancer, and Viral Oncolysis
Balachandran, S., & Barber, G. N. (2007) · Cancer Genomics and Proteomics · doi:10.1007/978-1-59745-335-6_18 · Cited by 65 · see citing works
Activation of the IκBα kinase (IKK) complex by double-stranded RNA-binding defective and catalytic inactive mutants of the interferon-inducible protein kinase PKR
Ishii, T. M., Kwon, H., Hiscott, J. B., Mosialos, G., & Koromilas, A. E. (2001) · Oncogene · doi:10.1038/sj.onc.1204267 · Cited by 65 · see citing works
Self-citation
Activation of the PKR/eIF2α signaling cascade inhibits replication of Newcastle disease virus
Zhang, S., Sun, Y., Chen, H., Dai, Y., Zhan, Y., Yu, S., Qiu, X., Tan, L., Song, C., & Ding, C. (2014) · Virology Journal · doi:10.1186/1743-422x-11-62 · Cited by 63 · see citing works
Role for p53 in Gene Induction by Double-Stranded RNA
Hummer, B. T., Li, X.-L., & Hassel, B. A. (2001) · Journal of Virology · doi:10.1128/jvi.75.16.7774-7777.2001 · Cited by 62 · 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
Human papillomaviruses target the double-stranded RNA protein kinase pathway
Hebner, C. M., Wilson, R., Rader, J. S., Bidder, M., & Laimins, L. A. (2006) · Journal of General Virology · doi:10.1099/vir.0.82098-0 · Cited by 60 · see citing works
Chicken interferons, their receptors and interferon-stimulated genes
Goossens, K. E., Ward, A. C., Lowenthal, J. W., & Bean, A. G. D. (2013) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2013.05.020 · Cited by 59 · see citing works
Down-Regulation of p53 by Double-Stranded RNA Modulates the Antiviral Response
Marques, J. T., Rebouillat, D., Ramana, C. V., Murakami, J., Hill, J. E., Gudkov, A. V., Silverman, R. H., Stark, G. R., & Williams, B. R. G. (2005) · Journal of Virology · doi:10.1128/jvi.79.17.11105-11114.2005 · Cited by 59 · see citing works
Synergistic activation of p53-dependent transcription by two cooperating damage recognition pathways
Blaydes, J. P., Craig, A. L., Wallace, M., Ball, H. M.-L., Traynor, N. J., Gibbs, N. K., & Hupp, T. R. (2000) · Oncogene · doi:10.1038/sj.onc.1203773 · Cited by 60 · see citing works
Oncolytic herpes simplex virus-1 lacking ICP34.5 induces p53-independent death and is efficacious against chemotherapy-resistant ovarian cancer.
Coukos, G., Makrigiannakis, A., Kang, E. H., Rubin, S. C., Albelda, S. Μ., & Molnar-Kimber, K. L. (2000) · PubMed · Cited by 59 · see citing works
Hepatitis C Virus Envelope Protein E2 Does Not Inhibit PKR by Simple Competition with Autophosphorylation Sites in the RNA-Binding Domain
Taylor, D. R., Tian, B., Romano, P. R., Hinnebusch, A. G., Lai, M. M. C., & Mathews, M. B. (2001) · Journal of Virology · doi:10.1128/jvi.75.3.1265-1273.2001 · Cited by 59 · see citing works
Doxorubicin bypasses the cytoprotective effects of eIF2α phosphorylation and promotes PKR-mediated cell death
Peidis, P., Papadakis, A. I., Muaddi, H., Richard, S., & Koromilas, A. E. (2010) · Cell Death and Differentiation · doi:10.1038/cdd.2010.76 · Cited by 57 · see citing works
Self-citation
Reticulon 3-mediated Chk2/p53 activation suppresses hepatocellular carcinogenesis and is blocked by hepatitis B virus
Song, S., Shi, Y., Wu, W., Wu, H., Chang, L., Peng, P., Zhang, L., Fan, J., Gu, J., & Ruan, Y. (2020) · Gut · doi:10.1136/gutjnl-2020-321386 · Cited by 53 · see citing works
Phosphorylation of Specific Serine Residues in the PKR Activation Domain of PACT Is Essential for Its Ability to Mediate Apoptosis
Peters, G. A., Li, S., & Sen, G. C. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m607714200 · Cited by 54 · see citing works
Self-citation
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
Post-translational modification of p53 protein in response to ionizing radiation analyzed by mass spectrometry
Abraham, J., Kelly, J. F., Thibault, P., & Benchimol, S. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3415 · Cited by 53 · see citing works
Modulation of p53 Cellular Function and Cell Death by African Swine Fever Virus
Granja, A. G., Nogal, M. L., Hurtado, C., Salas, J., Salas, M. L., Carrascosa, Á. L., & Revilla, Y. (2004) · Journal of Virology · doi:10.1128/jvi.78.13.7165-7174.2004 · Cited by 51 · see citing works
Role of p38 MAPK and RNA-dependent Protein Kinase (PKR) in Hepatitis C Virus Core-dependent Nuclear Delocalization of Cyclin B1
Spaziani, A., Alisi, A., Sanna, D., & Balsano, C. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m512536200 · Cited by 50 · see citing works
Tumor Suppressor p53 Mediates Apoptotic Cell Death Triggered by Cyclosporin A
Pyrzyńska, B., Serrano, M., Martínez‐A, C., & Kaminska, B. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m104443200 · Cited by 49 · see citing works
Modulation of p53 by mitogen-activated protein kinase pathways and protein kinase C δ during avian reovirus S1133-induced apoptosis
Lin, P., Lee, J., Liao, M., Hsu, H., Chiu, S.-J., Liu, H., & Shih, W. (2009) · Virology · doi:10.1016/j.virol.2008.12.028 · Cited by 48 · 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
Self-citation
7,12-Dimethylbenz[a]anthracene-Induced Bone Marrow Toxicity Is p53-Dependent
Page, T. J. (2003) · Toxicological Sciences · doi:10.1093/toxsci/kfg115 · Cited by 48 · see citing works
PKR, the double stranded RNA‐dependent protein kinase as a critical target in Alzheimer's disease
Morel, M., Couturier, J., Lafay‐Chebassier, C., Paccalin, M., & Page, G. (2009) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2009.00849.x · Cited by 47 · see citing works
Role of PKR and Type I IFNs in Viral Control during Primary and Secondary Infection
Nakayama, Y., Plisch, E. H., Sullivan, J. A., Thomas, C. B., Czuprynski, C. J., Williams, B. R. G., & Suresh, M. (2010) · PLoS Pathogens · doi:10.1371/journal.ppat.1000966 · Cited by 47 · see citing works
Vesicular Stomatitis Virus Expressing Tumor Suppressor p53 Is a Highly Attenuated, Potent Oncolytic Agent
Heiber, J. F., & Barber, G. N. (2011) · Journal of Virology · doi:10.1128/jvi.05408-11 · Cited by 46 · see citing works
The Direct Binding of the Catalytic Subunit of Protein Phosphatase 1 to the PKR Protein Kinase Is Necessary but Not Sufficient for Inactivation and Disruption of Enzyme Dimer Formation
Tan, S., Tareen, S. U., Melville, M. W., Blakely, C. M., & Katze, M. G. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m205109200 · Cited by 47 · see citing works
The RAX/PACT-PKR stress response pathway promotes p53 sumoylation and activation, leading to G1arrest
Bennett, R. L., Pan, Y., Christian, J., Hui, T., & May, W. S. (2012) · Cell Cycle · doi:10.4161/cc.11.2.18999 · Cited by 45 · see citing works
Interferon-Inducible Protein IFIXα1 Functions as a Negative Regulator of HDM2
Ding, Y., Lee, J.-F., Lu, H., Lee, M., & Yan, D. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.5.1979-1996.2006 · Cited by 44 · see citing works
The Infectious Bursal Disease Virus RNA-Binding VP3 Polypeptide Inhibits PKR-Mediated Apoptosis
Busnadiego, I., Maestre, A. M., Rodrı́guez, D., & Rodrígúez, J. F. (2012) · PLoS ONE · doi:10.1371/journal.pone.0046768 · Cited by 44 · see citing works
Interaction of Double-stranded RNA-dependent Protein Kinase (PKR) with the Death Receptor Signaling Pathway in Amyloid β (Aβ)-treated Cells and in APPSLPS1 Knock-in Mice
Couturier, J., Morel, M., Pontcharraud, R., Gontier, V., Fauconneau, B., Paccalin, M., & Page, G. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.041954 · Cited by 44 · see citing works
Protein kinase R and its cellular regulators in cancer: An active player or a surveillant?
Lee, Y. S., Kunkeaw, N., & Lee, Y. (2019) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1558 · Cited by 44 · see citing works
Role for the double-stranded RNA activated protein kinase PKR in E2F-1-induced apoptosis
Vorburger, S. A., Pataer, A., Yoshida, K., Barber, G. N., Xia, W., Chiao, P. J., Ellis, L. M., Hung, M., Swisher, S. G., & Hunt, K. K. (2002) · Oncogene · doi:10.1038/sj.onc.1205761 · Cited by 40 · see citing works
Evidence of molecular links between PKR and mTOR signalling pathways in Aβ neurotoxicity: Role of p53, Redd1 and TSC2
Morel, M., Couturier, J., Pontcharraud, R., Gil, R., Fauconneau, B., Paccalin, M., & Page, G. (2009) · Neurobiology of Disease · doi:10.1016/j.nbd.2009.07.004 · Cited by 36 · see citing works
Activation of p53 Facilitates the Target Search in DNA by Enhancing the Target Recognition Probability
Itoh, Y., Murata, A., Sakamoto, S., Nanatani, K., Wada, T., Takahashi, S., & Kamagata, K. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.06.001 · Cited by 36 · see citing works
Clinical and therapeutic potential of protein kinase PKR in cancer and metabolism
García‐Ortega, M. B., Lopez, G., Jiménez, G., Garcia-Garcia, J., Conde, V., Boulaiz, H., Carrillo, E., Perán, M., Marchal, J. A., & Garcia, M. (2017) · Expert Reviews in Molecular Medicine · doi:10.1017/erm.2017.11 · Cited by 36 · see citing works
Proapoptotic effect of hepatitis C virus CORE protein in transiently transfected cells is enhanced by nuclear localization and is dependent on PKR activation
Realdon, S., Gerotto, M., Pero, F. D., Marin, O., Granato, A., Basso, G., Muraca, M., & Alberti, A. (2003) · Journal of Hepatology · doi:10.1016/j.jhep.2003.09.017 · Cited by 35 · see citing works
Lack of p53 Ser389 Phosphorylation Predisposes Mice to Develop 2-Acetylaminofluorene–Induced Bladder Tumors but not Ionizing Radiation–Induced Lymphomas
Hoogervorst, E. M., Bruins, W., Zwart, E., van Oostrom, C. T. M., van den Aardweg, G. J., Beems, R. B., van den Berg, J., Jacks, T., STEEG, H. V., & de Vries, A. (2005) · Cancer Research · doi:10.1158/0008-5472.can-04-4328 · Cited by 34 · see citing works
7–12 Dimethylbenz[a]anthracene-induced bone marrow hypocellularity is dependent on signaling through both the TNFR and PKR
Page, T. J., MacWilliams, P. S., Suresh, M., Jefcoate, C. R. E., & Czuprynski, C. J. (2004) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2004.02.014 · Cited by 34 · see citing works

Genetic, physical and functional interactions between the double-stranded RNA-dependent protein kinase PKR and the tumor suppressor p53
Cuddihy, A. R. (1999) · Library and Archives Canada (Government of Canada) · doi:10.82308/11035
Self-citation
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
Self-citation
PKR , a p53 target gene, plays a crucial role in the tumor-suppressor function of p53
Yoon, C., Lee, E.-S., Lim, D.-S., & Bae, Y. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0812148106 · Cited by 124 · see citing works
The Double-Stranded RNA-Dependent Protein Kinase PKR: Structure and Function
Clemens, M. J., & Elia, A. (1997) · Journal of Interferon & Cytokine Research · doi:10.1089/jir.1997.17.503 · Cited by 605 · 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

Authors: Cuddihy, A. R., Hoi-Tao Wong, A., Wai Ning Tam, N., Li, S., & Koromilas, A. E.
Affiliations: McGill University (CA)
ORCID: Cuddihy, Andrew R
Koromilas, Antonis E
Venue: Oncogene
Publisher: Springer Science and Business Media LLC
Published: 1999-04-28
Volume: 18
Issue: 17
Pages: 2690-2702
ISSN: 0950-9232 (ISSN-L)
1476-5594
DOI: 10.1038/sj.onc.1202620
OpenAlex: W2010358674
Cited by: 203
References: 68
Citations by year: 2026: 2 · 2024: 4 · 2023: 10 · 2022: 4 · 2021: 6 · 2020: 5 · 2019: 6 · 2018: 5 · 2017: 4 · 2016: 5 · 2015: 2 · 2014: 5 · 2013: 7 · 2012: 5
FWCI: 6.76
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
www.springer.com/tdm (vor)
Locations: Oncogene (publishedVersion)
PubMed (publishedVersion)
Topics: Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
Life Sciences › Immunology and Microbiology › Immunology › interferon and immune responses
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
Keywords: PKR, p53, protein-protein interaction, double-stranded RNA-dependent protein kinase, interferon, tumor suppressor, N-terminal regulatory domain, eIF2α, protein synthesis inhibition, gene expression regulation
MeSH terms: Amino Acid Sequence, Animals, Cell Line, Humans, Molecular Sequence Data, Phosphorylation, Precipitin Tests, RNA, Double-Stranded, Serine, Tumor Suppressor Protein p53, Protein Structure, Tertiary, eIF-2 Kinase

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

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

Abstract

Integrity signals

Claims the paper makes

Claims other papers make about this one

Cites

Cited by

Related

Record

About these checks