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

Molecular Cloning: A Laboratory Manual

Sambrook, J., Fritsch, E., & Maniatis, T. (1989) · UCLA - Biblioteca de Ciencias de la Salud · Cited by 133,589

Molecular cloning: A laboratory manual

Deininger, P. L. (1990) · Analytical Biochemistry · doi:10.1016/0003-2697(90)90595-z · Cited by 84,684

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

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

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

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

p53: puzzle and paradigm.Preprint

Ko, L. J., & Prives, C. L. (1996) · Genes & Development · doi:10.1101/gad.10.9.1054 · Cited by 2,346

pEF-BOS, a powerful mammalian expression vector

Mizushima, S., & Nagata, S. (1990) · Nucleic Acids Research · doi:10.1093/nar/18.17.5322 · Cited by 1,594

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

[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 1,421

PKR inhibits the DNA damage response, and is associated with poor survival in AML and accelerated leukemia in NHD13 mice

Cheng, X., Byrne, M. T., Brown, K. D., Konopleva, M. Y., Kornblau, S. M., Bennett, R. L., & May, W. S. (2015) · Blood · doi:10.1182/blood-2015-03-635227 · Cited by 31

Enhanced Antiviral and Antiproliferative Properties of a STAT1 Mutant Unable to Interact with the Protein Kinase PKR

Wong, A. H., Durbin, J. E., Li, S., Dever, T. E., Decker, T., & Koromilas, A. E. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m011240200 · Cited by 32

Control of Oncogenesis by eIF2α Phosphorylation: Implications in PTEN and PI3K–Akt Signaling and Tumor Treatment

Koromilas, A. E., & Mounir, Z. (2013) · Future Oncology · doi:10.2217/fon.13.49 · Cited by 33

PKR, a cognitive decline biomarker, can regulate translation via two consecutive molecular targets p53 and Redd1 in lymphocytes of AD patients

Damjanac, M., Page, G., Ragot, S., Laborie, G., Gil, R., Hugon, J., & Paccalin, M. (2009) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2009.00688.x · Cited by 31

The Alzheimer's disease-associated TREM2 gene is regulated by p53 tumor suppressor protein

Zajkowicz, A., Gdowicz‐Kłosok, A., Krześniak, M., Janus, P., Łasut-Szyszka, B., & Rusin, M. (2018) · Neuroscience Letters · doi:10.1016/j.neulet.2018.05.037 · Cited by 29

The potential roles of p53 signaling reactivation in pancreatic cancer therapy

Ou, A., Zhao, X., & Lu, Z. (2021) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2021.188662 · Cited by 30

RAX is required for fly neuronal development and mouse embryogenesis

Bennett, R. L., Blalock, W. L., Choi, E.-J., Lee, Y. J., Zhang, Y., Zhou, L. J., Oh, S. P., & May, W. S. (2008) · Mechanisms of Development · doi:10.1016/j.mod.2008.06.009 · Cited by 29

Induction of E-Selectin Expression by Double-Stranded RNA and TNF-α Is Attenuated in Murine Aortic Endothelial Cells Derived from Double-Stranded RNA-Activated Kinase (PKR)-Null Mice

Bandyopadhyay, S. K., de la Motte, C. A., & Williams, B. R. G. (2000) · The Journal of Immunology · doi:10.4049/jimmunol.164.4.2077 · Cited by 29

Association of amino acid variations in the NS5A and E2‐PePHD region of hepatitis C virus 1b with hepatocellular carcinoma

Hung, C., Chen, C., Lee, C. ‐., Wu, C., Hu, T., Wang, J. ‐., Yen, Y., & Lu, S. (2007) · Journal of Viral Hepatitis · doi:10.1111/j.1365-2893.2007.00892.x · Cited by 28

Identification of the interferon-inducible double-stranded RNA-dependent protein kinase as a regulator of cellular response to bulky adducts.

Bergeron, J., Benlimame, N., Nie, Z.-R., Xiao, D., Scrivens, P. J., Koromilas, A. E., & Alaoui‐Jamali, M. A. (2000) · PubMed · Cited by 28

Double-Stranded RNA-Dependent Protein Kinase-Dependent Apoptosis Induction by a Novel Small Compound

Hu, W., Hofstetter, W. L., Wei, X., Guo, W., Zhou, Y., Pataer, A., Li, H., Fang, B., & Swisher, S. G. (2008) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.108.141754 · Cited by 27

Genetically Targeted Cancer Therapy

Vorburger, S. A., Pataer, A., Swisher, S. G., & Hunt, K. K. (2004) · American Journal of PharmacoGenomics · doi:10.2165/00129785-200404030-00006 · Cited by 27

The Double-Stranded RNA-Activated Protein Kinase Mediates Radiation Resistance in Mouse Embryo Fibroblasts through Nuclear Factor κB and Akt Activation

von Holzen, U. W., Pataer, A., Raju, U., Bocangel, D., Vorburger, S. A., Liu, Y., Lu, X., Roth, J. A., Aggarwal, B. B., Barber, G. N., et al. (2007) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-06-2932 · Cited by 26

Ascochlorin activates p53 in a manner distinct from DNA damaging agents

Jeong, J.-H., Nakajima, H., Magae, J., Furukawa, C., Taki, K., Otsuka, K., Tomita, M., Lee, I., Kim, C., Chang, H., et al. (2009) · International Journal of Cancer · doi:10.1002/ijc.24259 · Cited by 25

Double-stranded RNA-dependent protein kinase, PKR, down-regulates CDC2/cyclin B1 and induces apoptosis in non-transformed but not in v-mos transformed cells

Dagon, Y., Dovrat, S., Vilchik, S., Hacohen, D., Shlomo, G., Sredni, B., Salzberg, S., & Nir, U. (2001) · Oncogene · doi:10.1038/sj.onc.1204945 · Cited by 25

Induction and activation of the p53 pathway: a role for the protein kinase CK2?

Meek, D. W., & Cox, M. L. (2011) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-011-0966-3 · Cited by 26

Blockade of the LRP16-PKR-NF-κB signaling axis sensitizes colorectal carcinoma cells to DNA-damaging cytotoxic therapy

Li, X., Wu, Z., Xiao-jing, A., Mei, Q., Bai, M., Hanski, L. L., Li, X., Ahola, T., & Han, W. (2017) · eLife · doi:10.7554/elife.27301 · Cited by 24

The double-stranded RNA-activated protein kinase mediates viral-induced encephalitis

Scheuner, D. L., Gromeier, M., Davies, M. V., Dorner, A. J., Song, B., Patel, R., Wimmer, E., McLendon, R. E., & Kaufman, R. J. (2003) · Virology · doi:10.1016/j.virol.2003.08.010 · Cited by 23

The caspase-generated fragments of PKR cooperate to activate full-length PKR and inhibit translation

Kalai, M., Suin, V., Festjens, N., Meeus, A., Bernis, A., Wang, X.-M., Saelens, X., & Vandenabeele, P. (2007) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4402110 · Cited by 22

Activated PKR inhibits pancreatic β-cell proliferation through sumoylation-dependent stabilization of P53

Song, Y., Wan, X., Gao, L., Pan, Y., Xie, W., Wang, H., & Guo, J. (2015) · Molecular Immunology · doi:10.1016/j.molimm.2015.09.007 · Cited by 22

A role for PKR in hematologic malignancies

Blalock, W. L., Bavelloni, A., Piazzi, M., Faenza, I., & Cocco, L. (2010) · Journal of Cellular Physiology · doi:10.1002/jcp.22092 · Cited by 22

Diversity in Viral Anti-PKR Mechanisms: A Remarkable Case of Evolutionary Convergence

Domingo-Gil, E., Toribio, R., Nájera, J. L., Estéban, M., & Ventoso, I. (2011) · PLoS ONE · doi:10.1371/journal.pone.0016711 · Cited by 21

Role of STING in the treatment of non-small cell lung cancer

Tang, W., Zhou, W., Ji, M., & Yang, X. (2024) · Cell Communication and Signaling · doi:10.1186/s12964-024-01586-x · Cited by 21

Human herpesvirus 6B induces phosphorylation of p53 in its regulatory domain by a CK2- and p38-independent pathway

Øster, B., Bundgaard, B. B., Hupp, T. R., & Höllsberg, P. (2007) · Journal of General Virology · doi:10.1099/vir.0.83136-0 · Cited by 20

Protein kinase RNA-activated controls mitotic progression and determines paclitaxel chemosensitivity through B-cell lymphoma 2 in ovarian cancer

Yin, L., Zeng, Y., Zeng, R., Chen, Y., Wang, T., Rodabaugh, K. J., Yu, F., Natarajan, A., Karpf, A. R., & Dong, J. (2021) · Oncogene · doi:10.1038/s41388-021-02117-5 · Cited by 19

Identification of Kinases and Interactors of p53 Using Kinase-Catalyzed Cross-Linking and Immunoprecipitation

Garre, S., Gamage, A. K., Faner, T. R., Arachchige, P. D., & Pflum, M. K. H. (2018) · Journal of the American Chemical Society · doi:10.1021/jacs.8b10160 · Cited by 20

Double-Stranded RNA-Dependent Protein Kinase Is Involved in 2-Methoxyestradiol—Mediated Cell Death of Osteosarcoma Cells

Shogren, K. L., Turner, R. T., Yaszemski, M. J., & Maran, A. (2006) · Journal of Bone and Mineral Research · doi:10.1359/jbmr.060914 · Cited by 19

Protein kinase inhibitor 2-aminopurine overrides multiple genotoxic stress-induced cellular pathways to promote cell survival

Huang, S. H., Qu, L., Cuddihy, A. R., Ragheb, R., Taya, Y., & Koromilas, A. E. (2003) · Oncogene · doi:10.1038/sj.onc.1206490 · Cited by 19

Increased Expression of the dsRNA-Activated Protein Kinase PKR in Breast Cancer Promotes Sensitivity to Doxorubicin

Bennett, R. L., Carruthers, A. L., Hui, T., Kerney, K. R., Liu, X., & May, W. S. (2012) · PLoS ONE · doi:10.1371/journal.pone.0046040 · Cited by 18

RNAi in primary human chondrocytes: Efficiencies, kinetics, and non-specific effects of siRNA-mediated gene suppression

Klatt, A. R., Klinger, G., Zech, D., Paul‐Klausch, B., Renno, J. H., Schmidt, J., Malchau, G., & Wielckens, K. (2007) · Biologicals · doi:10.1016/j.biologicals.2006.12.003 · Cited by 18

Prevalence of wild-type in NS5A-PKR protein kinase binding domain in HCV-related hepatocellular carcinoma

Mitri, M. S. D., Morsica, G., Cassini, R., Bagaglio, S., Zoli, M., Alberti, A., & Bernardi, M. (2002) · Journal of Hepatology · doi:10.1016/s0168-8278(01)00235-5 · Cited by 18

Accumulation of an inactive form of p53 protein in cells treated with TNFα

Drané, P., Leblanc, V., Miró‐Mur, F., Saffroy, R., Debuire, B., & May, E. (2002) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4400983 · Cited by 20

Novel modulators of p53-signaling encoded by unknown genes of emerging viruses

Alzhanova, D. V., Corcoran, K., Bailey, A., Long, K. M., Taft-Benz, S., Graham, R. L., Broussard, G. S., Heise, M. T., Neumann, G., Halfmann, P., et al. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009033 · Cited by 17

Homogeneous time-resolved fluorescence assay for identifying p53 interactions with its protein partners, directly in a cellular extract

Leblanc, V., Delaunay, V., Lelong, J., Gas, F., Mathis, G., Grassi, J. J., & May, E. (2002) · Analytical Biochemistry · doi:10.1016/s0003-2697(02)00229-4 · Cited by 17

STING-mediated degradation of IFI16 negatively regulates apoptosis by inhibiting p53 phosphorylation at serine 392

Li, D., Xie, L., Qiao, Z., Mai, S., Zhu, J., Zhang, F., Chen, S., Li, L., Shen, F., Qin, Y., et al. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100930 · Cited by 16

Transcriptional activation of p21WAF1/CIP1 is mediated by increased DNA binding activity and increased interaction between p53 and Sp1 via phosphorylation during replicative senescence of human embryonic fibroblasts

Kim, H.-S., Heo, J., Park, S., Shin, J.-Y., Kang, H., Kim, M.-J., Kim, S. C., Kim, J., Park, J., & Lee, J. (2014) · Molecular Biology Reports · doi:10.1007/s11033-014-3094-9 · Cited by 16

The Cytotoxic Effect of Curcumin in Rhabdomyosarcoma Is Associated with the Modulation of AMPK, AKT/mTOR, STAT, and p53 Signaling

Salucci, S., Bavelloni, A., Stella, A. B., Fabbri, F., Vannini, I., Piazzi, M., Volkava, K., Scotlandi, K., Martinelli, G., Faenza, I., et al. (2023) · Nutrients · doi:10.3390/nu15030740 · Cited by 16

Maintaining Genome Integrity: Protein Kinases and Phosphatases Orchestrate the Balancing Act of DNA Double-Strand Breaks Repair in Cancer

Qin, S., Kitty, I., Hao, Y., Zhao, F., & Kim, W. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241210212 · Cited by 14

Downregulation of PERK activity and eIF2α serine 51 phosphorylation by mTOR complex 1 elicits pro-oxidant and pro-death effects in tuberous sclerosis-deficient cells

Krishnamoorthy, J., Tenkerian, C., Gupta, J., Ghaddar, N., Wang, S., Darini, C., Staschke, K. A., Ghosh, A., Gandin, V., Topisirović, I., et al. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-0326-2 · Cited by 15

Camptothecin-induced downregulation of MLL5 contributes to the activation of tumor suppressor p53

Cheng, F., Liu, J., Teh, C., Chong, S.-W., Korzh, V. P., Jiang, Y.-J., & Deng, L.-W. (2011) · Oncogene · doi:10.1038/onc.2011.71 · Cited by 15

Inhibition of protein phosphatase-1 is linked to phosphorylation of p53 and apoptosis

Long, X., Wu, G., Gaa, S. T., & Rogers, T. B. (2002) · APOPTOSIS · doi:10.1023/a:1013508811252 · Cited by 15

E3 ligase HECTD3 promotes RNA virus replication and virus-induced inflammation via K33-linked polyubiquitination of PKR

Huang, J., Zhou, Y., Li, X., Yang, M., Fang, Q., Li, Z., Wang, C., Chen, T., & Cao, X. (2023) · Cell Death and Disease · doi:10.1038/s41419-023-05923-9 · Cited by 14

Glycogen synthase kinase (GSK)-3 and the double-strand RNA-dependent kinase, PKR: When two kinases for the common good turn bad

Piazzi, M., Bavelloni, A., Faenza, I., & Blalock, W. L. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2020.118769 · Cited by 13

Delayed expression of apoptotic and cell-cycle control genes in carcinogen-exposed bladders of mice lacking p53.S389 phosphorylation

Bruins, W., Jonker, M. J., Bruning, O., Pennings, J. L. A., Schaap, M. M., Hoogervorst, E. M., STEEG, H. V., Breit, T. M., & de Vries, A. (2007) · Carcinogenesis · doi:10.1093/carcin/bgm041 · Cited by 13

Real-time surface plasmon resonance monitoring of site-specific phosphorylation of p53 protein and its interaction with MDM2 protein

Wu, L., He, Y., Hu, Y., Lu, H., Cao, Z. Y., Yi, X., & Wang, J. (2019) · The Analyst · doi:10.1039/c9an01121h · Cited by 13

Role for the double-stranded RNA-activated protein kinase PKR in Ad-TNF-α gene therapy in esophageal cancer

von Holzen, U. W., Bocangel, D., Pataer, A., Vorburger, S. A., Liu, Y., Lu, X., Hunt, K. K., & Swisher, S. G. (2005) · Surgery · doi:10.1016/j.surg.2005.04.011 · Cited by 13

Integrin alpha 11 is a novel type I interferon stimulated gene

LEOMILCOELHO, L., Mota, B. E. F., Sales, P. C. M., Marques, J. T., DEOLIVEIRA, J., Bonjardim, C. A., PEREGRINOFERREIRA, P., & Kroon, E. G. (2006) · Cytokine · doi:10.1016/j.cyto.2006.03.007 · Cited by 13

Differential responses to genotoxic agents between induced pluripotent stem cells and tumor cell lines

Lu, Y., Xu, D., Zhou, J., Ma, Y., Jiang, Y., Zeng, W., & Dai, W. H. (2013) · Journal of Hematology & Oncology · doi:10.1186/1756-8722-6-71 · Cited by 13

Phylogenetics and Functions of the Double-Stranded RNA-Binding Motif: A Genomic Survey

Tian, B., & Mathews, M. B. (2003) · Progress in nucleic acid research and molecular biology · doi:10.1016/s0079-6603(03)01012-2 · Cited by 13

Pkr

Williams, B. R. G., & Sadler, A. J. (2006) · AfCS-Nature Molecule Pages · doi:10.1038/mp.a000792.01 · Cited by 12

Inhibition of activation of dsRNA-dependent protein kinase and tumour growth inhibition

Eley, H. L., McDonald, P. S., Russell, S. T., & Tisdale, M. J. (2008) · Cancer Chemotherapy and Pharmacology · doi:10.1007/s00280-008-0782-y · Cited by 12

Human papillomavirus type 38 alters wild-type p53 activity to promote cell proliferation via the downregulation of integrin alpha 1 expression

Romero-Medina, M. C., Venuti, A., Melita, G., Robitaille, A., Ceraolo, M. G., Pacini, L., Sirand, C., Viarisio, D., Taverniti, V., Gupta, P., et al. (2020) · PLoS Pathogens · doi:10.1371/journal.ppat.1008792 · Cited by 11

Vaccinia Virus Recombinants as a Model System to Analyze Interferon-Induced Pathways

Gil, J., & Estéban, M. (2004) · Journal of Interferon & Cytokine Research · doi:10.1089/1079990042475706 · Cited by 11

Inhibiting the pro-tumor and transcription factor FACT: Mechanisms

Maluchenko, N. V., Chang, H.-W., Kozinova, M., Valieva, M. E., Gerasimova, N. S., Kitashov, A. V., Kirpichnikov, M. P., Georgiev, P. G., & Studitsky, V. M. (2016) · Molecular Biology · doi:10.1134/s0026893316040087 · Cited by 10

Phosphorylated PKR contributes the induction of GRP94 under ER stress

Ito, M., Onuki, R., Bandô, Y., Tohyama, M., & Sugiyama, Y. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.06.087 · Cited by 10

Antiviral Effects of Avian Interferon-Stimulated Genes

He, X., Zhang, S., Zou, Z., Gao, P., Yang, L., & Xiang, B. (2024) · Animals · doi:10.3390/ani14213062 · Cited by 11

Uncovering the PKR Pathway’s Potential for Treatment of Tumors

Mounir, Z., & Koromilas, A. E. (2010) · Future Oncology · doi:10.2217/fon.10.45 · Cited by 9

Mechanism of herpesvirus protein kinase UL13 in immune escape and viral replication

Zhou, L., Cheng, A., Wang, M., Wu, Y., Yang, Q., Tian, B., Ou, X., Sun, D., Zhang, S., Mao, S., et al. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.1088690 · Cited by 9

RNA recognition by PKR during DNA virus infection

Zhang, R., & Karijolich, J. J. (2024) · Journal of Medical Virology · doi:10.1002/jmv.29424 · Cited by 9

Effective control of viral infections by the adaptive immune system requires assistance from innate immunity

Barra, N. G., Gillgrass, A. E., & Ashkar, A. A. (2010) · Expert Review of Vaccines · doi:10.1586/erv.10.119 · Cited by 9

Механизмы ингибирования проопухолевого и транскрипционного фактора FACT

Малюченко, Н. В., Chang, H.-W., Kozinova, M., Valieva, M. E., Gerasimova, N. S., Kitashov, A. V., Kirpichnikov, M. P., Georgiev, P. G., & Studitsky, V. M. (2016) · Molecular Biology · doi:10.7868/s002689841604008x · Cited by 9

p48 Overexpression enhances interferon-mediated expression and activity of double-stranded RNA-dependent protein kinase in human hepatoma cells

Tamada, Y., Nakao, K., Nagayama, Y., Nakata, K., Ichikawa, T., Kawamata, Y., Ishikawa, H., Hamasaki, K., Eguchi, K., & Ishii, N. (2002) · Journal of Hepatology · doi:10.1016/s0168-8278(02)00232-5 · Cited by 9

The Double-Stranded RNA-Activated Protein Kinase PKR

Kaufman, R. J. (2001) · CRC Press eBooks · doi:10.1201/9781420039122.ch2 · Cited by 9

Protection of eIF2B from inhibitory phosphorylated eIF2: A viral strategy to maintain mRNA translation during the PKR-triggered integrated stress response

Ito, T., Wuerth, J. D., & Weber, F. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.105287 · Cited by 9

Activation et modifications post-traductionnelles de p53 après dommage de l’ADN

Leblanc, V., & May, P. (2002) · médecine/sciences · doi:10.1051/medsci/2002185577 · Cited by 13

Expression of the double‐stranded RNA‐dependent kinase PKR influences osteosarcoma attachment independent growth, migration, and invasion

Piazzi, M., Bavelloni, A., Greco, S., Focaccia, E., Orsini, A., Benini, S., Gambarotti, M., Faenza, I., & Blalock, W. L. (2019) · Journal of Cellular Physiology · doi:10.1002/jcp.29024 · Cited by 8

PACT/PRKRA and p53 regulate transcriptional activity of DMRT1

Fujitani, K., Otomo, A., Nagayama, Y., Tachibana, T., Kato, R., Kawashima, Y., Kodera, Y., Kato, T., Takada, S., Tamura, K., et al. (2020) · Genetics and Molecular Biology · doi:10.1590/1678-4685-gmb-2019-0017 · Cited by 8

Therapeutic restoring p53 function with small molecule for oncogene-driven non-small cell lung cancer by targeting serine 392 phosphorylation

Li, L., Li, P., Ma, X., Zeng, S., Peng, Y., & Zhang, G. (2022) · Biochemical Pharmacology · doi:10.1016/j.bcp.2022.115188 · Cited by 8

2-Aminopurine Enhances the Oncolytic Activity of an E1b-Deleted Adenovirus in Hepatocellular Carcinoma Cells

Sharon, D. M., Schümann, M., MacLeod, S. H., McPherson, R., Chaurasiya, S., Shaw, A., & Hitt, M. (2013) · PLoS ONE · doi:10.1371/journal.pone.0065222 · Cited by 8

PKR: A NMR perspective

Lindhout, D. A., McKenna, S. A., Aitken, C. E., Liu, C. W., & Puglisi, J. D. (2007) · Progress in Nuclear Magnetic Resonance Spectroscopy · doi:10.1016/j.pnmrs.2007.07.001 · Cited by 7

HIV and Apoptosis: a Complex Interaction Between Cell Death and Virus Survival

Bermejo, M., Alcamı́, J., & Gil, J. (2004) · Progress in molecular and subcellular biology · doi:10.1007/978-3-540-74264-7_7 · Cited by 7

A Narrative Review of the TP53 and Its Product the p53 Protein

Foroutan, B. (2023) · OBM Genetics · doi:10.21926/obm.genet.2302185 · Cited by 8

A co-formulation of interferons alpha2b and gamma distinctively targets cell cycle in the glioblastoma-derived cell line U-87MG

Miranda, J., Vázquez‐Blomquist, D., Bringas, R., Fernández-de-Cossío, J., Palenzuela, D., Novoa, L. I., & Rivero, I. B. (2023) · BMC Cancer · doi:10.1186/s12885-023-11330-2 · Cited by 3

Molecular Mechanism of the Antiproliferative Activity of Short Immunostimulating dsRNA

Zharkov, M. I., Аркадьевна, З. М., Vlassov, V. V., & Chernolovskaya, E. L. (2019) · Frontiers in Oncology · doi:10.3389/fonc.2019.01454 · Cited by 3

The FANCC Gene and Its Products

Gordon, S. M., & Buchwald, M. (2007) · Springer eBooks · doi:10.1007/0-387-33776-8_4 · Cited by 2

Intranuclear Ion Fountains as Regulators of Genome Functioning: Fountain Hypothesis of Dominance and Some Epigenetic Effects

Olovnikov, A. M. (2001) · Molecular Biology · doi:10.1023/a:1004827523693 · Cited by 2

p53 protein biosignatures in acute myeloid leukemia

Ånensen, N. (2006) · NORA - Norwegian Open Research Archives · Cited by 2

Overcoming immunotherapy resistance in breast cancer: a novel strategy by targeting the integrated stress response

Yue, J., Pu, T., He, D., Luo, Y., Ruan, S., Li, H., Jianwei, Z., Su, G., Su, J., Chen, S., et al. (2026) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2026.1720480 · Cited by 1

p53 and Immunity

Narayan, V., Meek, S. E. M., & Ball, K. L. (2010) · Molecular biology intelligence unit · doi:10.1007/978-1-4419-8231-5_12 · Cited by 1

The p53 Pathway, Cancer and Aging

Braithwaite, A. W., & Edwards, S. J. (2003) · Springer eBooks · doi:10.1007/978-94-017-0669-8_8 · Cited by 1

HeberFERON distinctively targets Cell Cycle in the glioblastoma-derived cell line U-87MGPreprint

Miranda, J., Vázquez‐Blomquist, D., Bringas, R., Fernández-de-Cossío, J., Palenzuela, D., Novoa, L. I., & Rivero, I. B. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.09.22.508971 · Cited by 1

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Meek, D. W. (2013) · Wiley eBooks · doi:10.1002/9781118482490.ch6

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Debus, M. A. (2007)

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Vaz, T. H. (2008) · doi:10.47749/t/unicamp.2008.431193

by increased DNA binding activity and increased interaction between p53 and Sp1 via phosphorylation during replicative senescence of human embryonic fibroblasts

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Abu-Thuraia, A. (2011) · doi:10.82308/31818

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Faculty Opinions recommendation of Identification of Kinases and Interactors of p53 Using Kinase-Catalyzed Cross-Linking and Immunoprecipitation.

Stock, A. (2018) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.734257035.793553259

PKR

Sadler, A. J. (2017) · Springer eBooks · doi:10.1007/978-3-319-67199-4_51

PKR

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Additional file 3 of A co-formulation of interferons alpha2b and gamma distinctively targets cell cycle in the glioblastoma-derived cell line U-87MG

Miranda, J., Vázquez‐Blomquist, D., Bringas, R., Fernández-de-Cossío, J., Palenzuela, D., Novoa, L. I., & Rivero, I. B. (2023) · Figshare · doi:10.6084/m9.figshare.24054351

Additional file 2 of A co-formulation of interferons alpha2b and gamma distinctively targets cell cycle in the glioblastoma-derived cell line U-87MG

Miranda, J., Vázquez-Blomquist, D., Bringas, R., Fernández-de-Cossío, J., Palenzuela, D., Novoa, L. I., & Rivero, I. B. (2023) · Figshare · doi:10.6084/m9.figshare.24054348

Additional file 1 of A co-formulation of interferons alpha2b and gamma distinctively targets cell cycle in the glioblastoma-derived cell line U-87MG

Miranda, J., Vázquez-Blomquist, D., Bringas, R., Fernández-de-Cossío, J., Palenzuela, D., Novoa, L. I., & Rivero, I. B. (2023) · Figshare · doi:10.6084/m9.figshare.24054345

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Grass, V. (2018) · theses.fr (ABES) · doi:10.70675/3b10422cz9bf4z4f02z81dczcf237dc03a18

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Robitaille, A. (2019) · theses.fr (ABES) · doi:10.70675/847ed257zbae5z488dza042z7d95234c0ad7

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Chaumont, L. (2024) · theses.fr (ABES) · doi:10.70675/9cd855d8z917bz4381z9011z256c1ac71cba · Cited by 1

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Cuddihy, A. R. (1999) · Library and Archives Canada (Government of Canada) · doi:10.82308/11035

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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

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Clemens, M. J., & Elia, A. (1997) · Journal of Interferon & Cytokine Research · doi:10.1089/jir.1997.17.503 · Cited by 605

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