The DOI matches its Crossref record; 207 of the 210 references it cites were found in a registry or an index.
The dsRNA protein kinase PKR: Virus and cell control
Abstract
The IFN-induced double-stranded RNA-dependent protein kinase (PKR) is one of the four mammalian serine-threonine kinases (the three others being HRI, GCN2 and PERK) that phosphorylate the eIF2 alpha translation initiation factor, in response to stress signals, mainly as a result of viral infections. eIF2 alpha phosphorylation results in arrest of translation of both cellular and viral mRNAs, an efficient way to inhibit virus replication. The particularity of PKR is to activate by binding to dsRNA through two N terminal dsRNA binding motifs (dsRBM). PKR activation during a viral infection represents a threat for several viruses, which have therefore evolved to express PKR inhibitors, such as the Vaccinia E3L and K3L proteins. The function of PKR can also be regulated by cellular proteins, either positively (RAX/PACT; Mda7) or negatively (p58IPK, TRBP, nucleophosmin, Hsp90/70). PKR can provoke apoptosis, in part through its ability to control protein translation, but the situation appears to be more complex, as NF-kappaB, ATF-3 and p53 have also been implicated. PKR-induced apoptosis involves mainly the FADD/caspase 8 pathway, while the mitochondrial APAF/caspase 9 pathway is also engaged. As a consequence of the effects of PKR on translation, transcription and apoptosis, PKR can function to control cell growth and cell differentiation, and its activity can be controlled by the action of several oncogenes.
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“A study demonstrating that influenza virus infection was lethal in mice lacking the NK cell-activating receptor NCR1 suggests that NK cells are indeed crucial for protection against respiratory virus infections (78).”
From The airway epithelium: soldier in the fight against respiratory viruses (2011) · cites this paper as [78]
Citations
Cites
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
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
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
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
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 1,845
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
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
TRANSLATIONAL CONTROL IN MAMMALIAN CELLS
Hershey, J. W. B. (1991) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.60.070191.003441 · Cited by 1,029
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
Self-citationEnomoto, 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
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Qiao, P., Yu, J., Li, C., Chen, B., & Wang, Y. (2026) · Journal of Controlled Release · doi:10.1016/j.jconrel.2026.114820 · Cited by 3
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Templeton, E. M., Lassé, M., Kleffmann, T., Ellmers, L. J., Palmer, S. C., Davidson, T., Scott, N. J. A., Pickering, J. W., Charles, C. J., Endre, Z. H., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23021009 · Cited by 3
Harnessing dendritic cells as immunological bridges to potentiate mRNA cancer vaccines
Wu, R., Li, H., Li, Z., Hao, K., & Tian, H. (2025) · Journal of Materials Chemistry B · doi:10.1039/d5tb00995b · Cited by 3
Lavender, A. A., Solanke, O., Tang, H., Peck, H. E., Vanover, D. A., Santangelo, P. J., & Brinton, M. A. (2025) · Journal of Virology · doi:10.1128/jvi.00794-25 · Cited by 3
Lostalé‐Seijo, I., Martı́nez-Costas, J., & Benavente, J. (2016) · Journal of Virology · doi:10.1128/jvi.01175-16 · Cited by 3
Riad, S., Xiang, Y., AlDaif, B. A., Mercer, A. A., & Fleming, S. B. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.01797 · Cited by 3
Antiviral Effect of Hyunggaeyungyo-Tang on A549 Cells Infected with Human Coronavirus
Won, S.-Y., Seol, I.-C., Yoo, H.-R., & Kim, Y.-S. (2021) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2021/4494389 · Cited by 3
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Cryo-EM structure of Influenza A virus NS1 and antiviral protein kinase PKR complex
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Eldahshan, D. H., Bahy, D., Wahid, A. M., Ahmed, A. E., & Hanora, A. (2018) · Arab Journal of Gastroenterology · doi:10.1016/j.ajg.2018.06.002 · Cited by 3
Is There an Infectious Agent Behind Prostate Cancer?
Rovigatti, U. (2013) · InTech eBooks · doi:10.5772/54054 · Cited by 2
Biochemical and Radiological Markers of Alzheimer’s Disease Progression
Dziedzic, T., Pera, J., Klimkowicz‐Mrowiec, A., Mroczko, B., & Słowik, A. (2016) · Journal of Alzheimer s Disease · doi:10.3233/ifs-150578 · Cited by 3
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Brocard, M., Iadevaia, V., Klein, P., Hall, B. S., Lewis, G., Lu, J. Q., Burke, J. M., Parker, R., Ruggieri, A., Goodfellow, I., et al. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/490318 · Cited by 3
Tsai, R.-S., Tsai, J.-Y., Chung, Y.-T., Tseng, C., Liao, G., Albrecht, R. A., Kuan, C.-Y., Kuo, R., Ou, S.-C., & Hsu, W. (2025) · Emerging Microbes & Infections · doi:10.1080/22221751.2025.2556731 · Cited by 2
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Park, C., Brennan, G., Peng, C., Zhang, C., Cao, J., Tazi, L., & Rothenburg, S. (2025) · Viruses · doi:10.3390/v17121550 · Cited by 2
Jhelum, H., Schäfer, R., Kaufer, B. B., & Denner, J. (2025) · Viruses · doi:10.3390/v18010021 · Cited by 2
Zhou, H., Wang, M., Xin, Z., Li, Z., Wang, Q., Li, Y., & Liu, F. (2025) · Virulence · doi:10.1080/21505594.2025.2609570 · Cited by 2
Herpes simplex viruses and induction of interferon responses
Ma, Y., Verpooten, D., & He, B. (2008) · Virologica Sinica · doi:10.1007/s12250-008-2999-7 · Cited by 2
Shum, D., Bhinder, B., Mahida, J. P., Radu, C., Calder, P. A., & Djaballah, H. (2023) · GEN Biotechnology · doi:10.1089/genbio.2023.0001 · Cited by 2
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Ceraolo, M. G., Romero-Medina, M. C., Gobbato, S., Melita, G., Krynska, H., Sirand, C., Gupta, P., Viarisio, D., Robitaille, A., Marvel, J., et al. (2023) · mSphere · doi:10.1128/msphere.00450-23 · Cited by 2
Volloch, V., & Rits‐Volloch, S. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25189913 · Cited by 3
Feinstein, A. G., Cole, J. L., & May, E. R. (2024) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.4c02460 · Cited by 1
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Das, P. P., Sengupta, S., Balram, D., Lian, K., Azizov, S., Neogi, U., Pandey, S., & Kumar, D. (2024) · Advances in Natural Sciences Nanoscience and Nanotechnology · doi:10.1088/2043-6262/ad6b7d · Cited by 4
Volloch, V., & Rits‐Volloch, S. (2025) · Genes · doi:10.3390/genes16010046 · Cited by 3
Innate Immune Responses Elicited by Reovirus and Rotavirus
Sherry, B., Patton, J. T., & Dermody, T. S. (2014) · ASM Press eBooks · doi:10.1128/9781555815561.ch25 · Cited by 2
Cellular Stress and eIF-2α Kinase
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An Overview of Innate Immune Response to Human Rhinovirus Infection
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Mongelli, V. C. (2010) · Repositorio Digital Institucional de la Universidad de Buenos Aires (Universidad de Buenos Aires) · Cited by 2
Blanco-Melo, D., Nilsson-Payant, B. E., Uhl, S. A., Escudero-Pérez, B., Olschewski, S., Thibault, P. A., Panis, M., Rosenthal, M., Muñoz‐Fontela, C., Lee, B., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.03.12.989319 · Cited by 2
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Lewis, S. A., Forstrom, J., Tavani, J. R., Schafer, R., Tiede, Z., Padilla-Lopez, S. R., & Kruer, M. C. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.05.14.594240 · Cited by 2
Burnett, S. B., Culver, A. M., Simon, T. A., Rowson, T., Frederick, K., Palmer, K. J., Murray, S. A., Davis, S. W., & Patel, R. C. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.06.04.597421 · Cited by 2
Fendereski, M., Ming, H., Jiang, Z., & Guo, Y. (2023) · The Journal of Immunology · doi:10.4049/jimmunol.2300210 · Cited by 1
Volloch, V., & Rits‐Volloch, S. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26094252 · Cited by 3
Sweetman, E., & Tate, W. P. (2025) · Methods in molecular biology · doi:10.1007/978-1-0716-4498-0_2 · Cited by 1
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Pachymeningitis in intracranial liquor hypotension syndrome.
Vankan, Y., Lambrechts, I., & Janssen, L. (2005) · PubMed · Cited by 1
Lee, H., Chao, H.-T., Lee, S. Y.-H., Lin, C., & Tsai, H. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242417393 · Cited by 1
Hidalgo, P., & González, R. A. (2024) · Elsevier eBooks · doi:10.1016/b978-0-12-818619-0.00130-1 · Cited by 1
Mohamed, A. A., Amin, M. A., Ragab, M. M., Ismail, S., & Baki, A. A. (2013) · Journal of Advanced Research · doi:10.1016/j.jare.2013.01.002 · Cited by 1
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Wilson, H. L., Napper, S., Mutwiri, G., den Hurk, S. V. D. L., Townsend, H. G. G., Babiuk, L. A., Potter, A. A., & Gerdts, V. (2012) · Wiley eBooks · doi:10.1002/9781118345313.ch2 · Cited by 1
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Venkatesh, P. H., Kumar, S., Kumar, N., Chaitanya, K., Turtle, L. C. W., & Satchidanandam, V. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.01.14.426643 · Cited by 1
Barbosa, N. S., Concha, J. O., & daSilva, L. L. P. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-818731-9.00037-9 · Cited by 1
洪, 涛., 张, 丽., & 代, 新. (2010) · Scientia Sinica Vitae · doi:10.1360/zc2010-40-11-993
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Developing Crosslinking Constructs of Protein Kinase R
Lopez, P. (2014) · OpenCommons - UConn (University of Connecticut)
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Welnowska, E. (2012) · Biblos-e Archivo (Universidad Autónoma de Madrid)
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Zhang, C. (2010) · University Library - University of Saskatchewan (University of Saskatchewan)
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Ruuska, M. (2014) · UTUPub (University of Turku)
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Vaughn, L. S. (2015) · Scholar Commons (University of South Carolina)
Yoboua, F. (2012) · Papyrus : Institutional Repository (Université de Montréal) · doi:10.71781/29597
Rice, A. D. (2008) · University of Florida Digital Collections (University of Florida)
Mathematisch-naturwissenschaftlichen Fakultät, I. (2009)
Glia Specific Innate Responses and Their Influence on Murine Coronavirus Inducedencephalomyelitis
Kapil, P. (2011) · OhioLink ETD Center (Ohio Library and Information Network)
Hopfner, K., Cui, S., Kirchhofer, A., & Pippig, D. A. (2010) · Royal Society of Chemistry eBooks · doi:10.1039/9781849732215-00121
Dalmay, T., Saalbach, G., Powell, P. P., Jefferson, M. A., Donaszi-Ivanov, A., & Pollen, S. (2014)
Poulsen, L. C. (2008) · NORA - Norwegian Open Research Archives
Paramyxovirus and Rig-Like Helicases: A Complex Molecular Interplay Driving Innate Immunity
Gerlier, D. (2011) · WORLD SCIENTIFIC eBooks · doi:10.1142/9789814317238_0012
HERPES SIMPLEX VIRUSES AND INTERFERON RESPONSES
Ma, Y., & He, B. (2012) · WORLD SCIENTIFIC eBooks · doi:10.1142/9789814338998_0023
Novel targets of eiF2 kinases determine cell fate during the integrated stress response
Baird, T. (2014) · IUScholarWorks (Indiana University) · doi:10.7912/c2/1883
Characterisation of the Vaccinia Virus Protein, C16, and its Role in Infection
Fahy, A. S. (2008) · Spiral (Imperial College London) · doi:10.25560/4656
Ángel, M. A., & Chaves, G. (2016) · Anales de la Real Academia Nacional de Farmacia
Evasion and Resistance of Host Antiviral Defense pathways by Alphaviruses
Bhalla, N. (2016) · D-Scholarship@Pitt (University of Pittsburgh)
Heparin Activates PKR by Inducing Dimerization
Anderson, E., Pierre-Louis, W., Wong, C. J., Lary, J. W., & Cole, J. L. (2011) · Biophysical Journal · doi:10.1016/j.bpj.2010.12.501
Factors affecting the non-structural functions of Rubella virus capsid
Willows, S. D. (2015) · ERA: Education and Research Archive (University of Alberta) · doi:10.7939/r3pk0767w
Dey, S. (2012) · IUScholarWorks (Indiana University) · doi:10.7912/c2/1864
Ng, K. (2018) · ERA: Education and Research Archive (University of Alberta) · doi:10.7939/r30863n33
Análise transcritômica de amostras humanas naturalmente infectadas por virus Chikungunya
Cruz, N. B. (2019) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/d.95.2019.tde-10092019-160208
Lamichhane, R. (2019) · Biological and medical physics, biomedical engineering · doi:10.1007/978-1-4939-9726-8_1
Designed synthesis of silica based nanocarriers for mRNA delivery
Wang, Y. (2020) · The University of Queensland · doi:10.14264/b28d1e7
Pitcheshwar, P., Shen, H., Han, J., & Tang, S. J. (2021) · Springer eBooks · doi:10.1007/978-3-030-76571-2_7
Guo, J., Lin, A. E., Aditya, C., Ploß, A., & Harris, M. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.09.29.462334
Sønstevold, T. (2021) · NORA - Norwegian Open Research Archives
[How and when is topical treatment applied into the ear?].
Hopsu, E., Närkiö‐Mäkelä, M., & Silvola, J. T. (2011) · PubMed
The impact of the integrated stress response on DNA replication
Choo, J. A. M. Y. (2020) · doi:10.53846/goediss-7917
Metadata
- Authors
- García, M. A., Meurs, E. F., & Esteban, M.
- Affiliations
- Institut Pasteur (FR)
- ORCID
- Meurs, E.F.
- Venue
- Biochimie
- Publisher
- Elsevier BV
- Published
- 2007-06
- Volume
- 89
- Issue
- 6-7
- Pages
- 799-811
- ISSN
- 0037-9042 (ISSN-L)
- 0300-9084
- OpenAlex
- W2085487477
- Cited by
- 644
- References
- 210
- Citations by year
- 2026: 16 · 2025: 30 · 2024: 32 · 2023: 38 · 2022: 33 · 2021: 44 · 2020: 49 · 2019: 20 · 2018: 24 · 2017: 25 · 2016: 25 · 2015: 30 · 2014: 34 · 2013: 38 · 2012: 58
- FWCI
- 2.91
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochimie (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › interferon and immune responses
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Keywords
- PKR, double-stranded RNA-dependent protein kinase, eIF2α phosphorylation, translational arrest, antiviral innate immunity, interferon signaling, PKR inhibitor, p58IPK, TRBP, nucleophosmin, apoptosis, NF-κB, ATF3, p53, oncogenes, cell growth and differentiation, viral replication inhibition
- MeSH terms
- Animals, Antiviral Agents, Gene Expression Regulation, Humans, Models, Biological, RNA, Messenger, Protein Biosynthesis, Signal Transduction, Gene Expression Regulation, Viral, NF-kappa B, Apoptosis, Protein Structure, Tertiary, eIF-2 Kinase, Amino Acid Motifs, Cell Proliferation
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