K. Pakos-zebrucka, The integrated stress response, EMBO reports, vol.17, issue.10, pp.1374-1395201642195, 2016.
DOI : 10.15252/embr.201642195

M. C. Bonnet, C. Daurat, C. Ottone, and E. F. Meurs, The N-terminus of PKR is responsible for the activation of the NF-??B signaling pathway by interacting with the IKK complex, Cellular Signalling, vol.18, issue.11, pp.1865-1875, 2006.
DOI : 10.1016/j.cellsig.2006.02.010

J. Gil, TRAF Family Proteins Link PKR with NF-??B Activation, Molecular and Cellular Biology, vol.24, issue.10, pp.4502-4512, 2004.
DOI : 10.1128/MCB.24.10.4502-4512.2004

URL : http://mcb.asm.org/content/24/10/4502.full.pdf

B. Lu, Novel role of PKR in inflammasome activation and HMGB1 release, Nature, vol.187, issue.7413, pp.670-674, 2012.
DOI : 10.4049/jimmunol.1100613

H. C. Yim, The kinase activity of PKR represses inflammasome activity, Cell Research, vol.9, issue.3, pp.367-37911, 2016.
DOI : 10.1038/gene.2008.66

E. C. Hett, Chemical genetics reveals a kinase-independent role for protein kinase R in pyroptosis, Nature Chemical Biology, vol.586, issue.6, pp.398-405, 2013.
DOI : 10.1016/j.febslet.2012.02.045

H. C. Yim and B. Williams, Protein Kinase R and the Inflammasome, Journal of Interferon & Cytokine Research, vol.34, issue.6, pp.447-4540008, 2014.
DOI : 10.1089/jir.2014.0008

Y. He, L. Franchi, and G. Nunez, The protein kinase PKR is critical for LPS-induced iNOS production but dispensable for inflammasome activation in macrophages, European Journal of Immunology, vol.13, issue.5, pp.1147-1152201243187, 2013.
DOI : 10.1038/ni.2215

M. Costa-mattioli, eIF2?? Phosphorylation Bidirectionally Regulates the Switch from Short- to Long-Term Synaptic Plasticity and Memory, Cell, vol.129, issue.1, pp.195-206, 2007.
DOI : 10.1016/j.cell.2007.01.050

URL : https://doi.org/10.1016/j.cell.2007.01.050

P. J. Zhu, Suppression of PKR Promotes Network Excitability and Enhanced Cognition by Interferon-??-Mediated Disinhibition, Cell, vol.147, issue.6, pp.1384-1396, 2011.
DOI : 10.1016/j.cell.2011.11.029

T. Ito, M. Yang, and W. S. May, RAX, a Cellular Activator for Double-stranded RNA-dependent Protein Kinase during Stress Signaling, Journal of Biological Chemistry, vol.18, issue.22, pp.15427-15459, 1999.
DOI : 10.1128/MCB.18.12.7499

URL : http://www.jbc.org/content/274/22/15427.full.pdf

C. V. Patel, I. Handy, T. Goldsmith, and R. C. Patel, PACT, a Stress-modulated Cellular Activator of Interferon-induced Double-stranded RNA-activated Protein Kinase, PKR, Journal of Biological Chemistry, vol.1014, issue.48, pp.37993-37998, 2000.
DOI : 10.1073/pnas.88.17.7729

G. A. Peters, R. Hartmann, J. Qin, and G. C. Sen, Modular Structure of PACT: Distinct Domains for Binding and Activating PKR, Molecular and Cellular Biology, vol.21, issue.6, pp.1908-1920, 2001.
DOI : 10.1128/MCB.21.6.1908-1920.2001

M. Singh, D. Castillo, C. V. Patel, and R. C. Patel, Stress-Induced Phosphorylation of PACT Reduces Its Interaction with TRBP and Leads to PKR Activation, Biochemistry, vol.50, issue.21, pp.4550-4560, 2011.
DOI : 10.1021/bi200104h

M. Singh and R. Patel, Increased interaction between PACT molecules in response to stress signals is required for PKR activation, Journal of Cellular Biochemistry, vol.276, issue.8, pp.2754-2764, 2012.
DOI : 10.1074/jbc.M102108200

R. C. Patel and G. C. Sen, Requirement of PKR Dimerization Mediated by Specific Hydrophobic Residues for Its Activation by Double-Stranded RNA and Its Antigrowth Effects in Yeast, Molecular and Cellular Biology, vol.18, issue.12, pp.7009-7019, 1998.
DOI : 10.1128/MCB.18.12.7009

A. Daher, TRBP Control of PACT-Induced Phosphorylation of Protein Kinase R Is Reversed by Stress, Molecular and Cellular Biology, vol.29, issue.1, pp.254-26501030, 2009.
DOI : 10.1128/MCB.01030-08

URL : https://hal.archives-ouvertes.fr/pasteur-00460560

S. B. Singh, Human IRGM regulates autophagy and cell-autonomous immunity functions through mitochondria, Nature Cell Biology, vol.452, issue.12, pp.1154-1165, 2010.
DOI : 10.1038/ncb1730

URL : https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2996476/pdf

C. Paquet, The PKR Activator PACT Is Induced by A??: Involvement in Alzheimer's Disease, Brain Pathology, vol.25, issue.2, pp.219-229, 2012.
DOI : 10.1042/bst0250509

F. Mouton-liger, Oxidative stress increases BACE1 protein levels through activation of the PKR-eIF2?? pathway, Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease, vol.1822, issue.6, pp.885-896, 2012.
DOI : 10.1016/j.bbadis.2012.01.009

C. R. Stewart, CD36 ligands promote sterile inflammation through assembly of a Toll-like receptor 4 and 6 heterodimer, Nature Immunology, vol.17, issue.2, pp.155-1611836, 2010.
DOI : 10.1073/pnas.211445098

A. Jekabsone, P. K. Mander, A. Tickler, M. Sharpe, and G. C. Brown, Fibrillar beta-amyloid peptide Abeta1-40 activates microglial proliferation via stimulating TNF-alpha release and H2O2 derived from NADPH oxidase: a cell culture study, J Neuroinflammation, vol.3, issue.24, pp.1742-2094, 2006.

A. Halle, The NALP3 inflammasome is involved in the innate immune response to amyloid-??, Nature Immunology, vol.17, issue.8, pp.857-8651636, 2008.
DOI : 10.1126/science.1067081

N. V. Jammi, L. R. Whitby, and P. A. Beal, Small molecule inhibitors of the RNA-dependent protein kinase, Biochemical and Biophysical Research Communications, vol.308, issue.1, pp.50-57, 2003.
DOI : 10.1016/S0006-291X(03)01318-4

S. Nekhai, A. Kumar, D. P. Bottaro, and R. Petryshyn, Peptides Derived from the Interferon-Induced PKR Prevent Activation by HIV-1 TAR RNA, Virology, vol.222, issue.1, pp.193-200, 1996.
DOI : 10.1006/viro.1996.0410

URL : https://doi.org/10.1006/viro.1996.0410

Y. Lin, R. Shi, X. Wang, and H. M. Shen, Luteolin, a Flavonoid with Potential for Cancer Prevention and Therapy, Current Cancer Drug Targets, vol.8, issue.7, pp.634-646, 2008.
DOI : 10.2174/156800908786241050

P. Cassonnet, Benchmarking a luciferase complementation assay for detecting protein complexes, Nature Methods, vol.8, issue.12, pp.990-9921773, 2011.
DOI : 10.1093/bioinformatics/btq430

X. Mo, AKT1, LKB1, and YAP1 Revealed as MYC Interactors with NanoLuc-Based Protein-Fragment Complementation Assay, Molecular Pharmacology, vol.91, issue.4, pp.339-347, 2017.
DOI : 10.1124/mol.116.107623

G. Laraki, Interactions between the double-stranded RNA-binding proteins TRBP and PACT define the Medipal domain that mediates protein-protein interactions, RNA Biology, vol.5, issue.2, pp.92-103, 2008.
DOI : 10.4161/rna.5.2.6069

E. S. Lee, C. H. Yoon, Y. S. Kim, and Y. S. Bae, The double-strand RNA-dependent protein kinase PKR plays a significant role in a sustained ER stress-induced apoptosis, FEBS Letters, vol.18, issue.22, pp.4325-4332, 2007.
DOI : 10.1038/sj.onc.1203127

C. R. Raetz, , a defined endotoxin that activates macrophages via TLR-4, Journal of Lipid Research, vol.260, issue.5, pp.1097-1111, 2006.
DOI : 10.1093/emboj/19.19.5071

URL : http://www.jlr.org/content/47/5/1097.full.pdf

M. Macoch, Nrf2-dependent repression of interleukin-12 expression in human dendritic cells exposed to inorganic arsenic. Free radical biology & medicine 88, pp.381-390, 2015.
URL : https://hal.archives-ouvertes.fr/hal-01117679

S. B. Cullinan and J. A. Diehl, PERK-dependent Activation of Nrf2 Contributes to Redox Homeostasis and Cell Survival following Endoplasmic Reticulum Stress, Journal of Biological Chemistry, vol.23, issue.19, pp.20108-20117, 2004.
DOI : 10.1083/jcb.200302084

J. D. Wardyn, A. H. Ponsford, and C. M. Sanderson, Dissecting molecular cross-talk between Nrf2 and NF-??B response pathways, Biochemical Society Transactions, vol.43, issue.4, pp.621-626, 2015.
DOI : 10.1042/BST20150014

URL : http://europepmc.org/articles/pmc4613495?pdf=render

I. Novoa, Stress-induced gene expression requires programmed recovery from translational repression, The EMBO Journal, vol.22, issue.5, pp.1180-1187, 2003.
DOI : 10.1093/emboj/cdg112

URL : http://emboj.embopress.org/content/embojnl/22/5/1180.full.pdf

M. Boyce, A Selective Inhibitor of eIF2?? Dephosphorylation Protects Cells from ER Stress, Science, vol.307, issue.5711, pp.935-9391101902, 2005.
DOI : 10.1126/science.1101902

H. Wang, H. Wang, H. Cheng, and Z. Che, Ameliorating effect of luteolin on memory impairment in an Alzheimer's disease model. Molecular medicine reports 13, pp.4215-4220, 2016.

A. Taliou, E. Zintzaras, L. Lykouras, and K. Francis, An Open-Label Pilot Study of a Formulation Containing the Anti-Inflammatory Flavonoid Luteolin and Its Effects on Behavior in Children With Autism Spectrum Disorders, Clinical Therapeutics, vol.35, issue.5, pp.592-602006, 2013.
DOI : 10.1016/j.clinthera.2013.04.006

N. Abraham, Characterization of Transgenic Mice with Targeted Disruption of the Catalytic Domain of the Double-stranded RNA-dependent Protein Kinase, PKR, Journal of Biological Chemistry, vol.67, issue.9, pp.5953-5962, 1999.
DOI : 10.1074/jbc.273.3.1808

Y. L. Yang, Deficient signaling in mice devoid of double-stranded RNA-dependent protein kinase, Embo J, vol.14, pp.6095-6106, 1995.

M. Haneklaus and L. A. Neill, NLRP3 at the interface of metabolism and inflammation, Immunological Reviews, vol.99, issue.1, pp.53-6212285, 2015.
DOI : 10.1073/pnas.092324399

T. Nakamura, A. Arduini, B. Baccaro, M. Furuhashi, and G. S. Hotamisligil, Small-Molecule Inhibitors of PKR Improve Glucose Homeostasis in Obese Diabetic Mice, Diabetes, vol.63, issue.2, pp.526-534, 2014.
DOI : 10.2337/db13-1019

G. I. Lancaster, PKR is not obligatory for high-fat diet-induced obesity and its associated metabolic and inflammatory complications, Nature Communications, vol.274, issue.10626, 2016.
DOI : 10.1074/jbc.274.9.5953

URL : http://www.nature.com/articles/ncomms10626.pdf

S. Gourmaud, Dual Kinase Inhibition Affords Extended in vitro Neuroprotection in Amyloid-beta Toxicity, J Alzheimers Dis, vol.54103233, pp.1659-1670160509, 2016.
DOI : 10.3233/jad-160509

F. Mouton-liger, PKR downregulation prevents neurodegeneration and beta-amyloid production in a thiamine-deficient model, Cell death & disease, vol.6, p.552, 1594.
DOI : 10.1038/cddis.2014.552

URL : http://www.nature.com/cddis/journal/v6/n1/pdf/cddis2014552a.pdf

R. C. Coll, A small-molecule inhibitor of the NLRP3 inflammasome for the treatment of inflammatory diseases, Nature Medicine, vol.1040, issue.3, pp.248-2553806, 2015.
DOI : 10.1007/978-1-62703-523-1_2

D. Akazawa, CD81 Expression Is Important for the Permissiveness of Huh7 Cell Clones for Heterogeneous Hepatitis C Virus Infection, Journal of Virology, vol.81, issue.10, pp.5036-5045, 2007.
DOI : 10.1128/JVI.01573-06

A. G. Laurent, B. Krust, J. Galabru, J. Svab, and A. G. Hovanessian, Monoclonal antibodies to an interferon-induced Mr 68,000 protein and their use for the detection of double-stranded RNA-dependent protein kinase in human cells., Proc. Natl. Acad. Sci.USA, pp.4341-4345, 1985.
DOI : 10.1073/pnas.82.13.4341

M. F. Hibert and . French, European academic compound library initiative. Drug discovery today 14, pp.723-725012, 2009.
DOI : 10.1016/j.drudis.2009.05.012

J. H. Zhang, T. D. Chung, and K. R. Oldenburg, A Simple Statistical Parameter for Use in Evaluation and Validation of High Throughput Screening Assays, Journal of Biomolecular Screening, vol.4, issue.2, pp.67-73, 1999.
DOI : 10.1177/108705719900400206