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The PKR Activator PACT Is Induced by Aβ: Involvement in Alzheimer's Disease

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TDP-43 knockdown causes innate immune activation via protein kinase R in astrocytes

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PERK as a hub of multiple pathogenic pathways leading to memory deficits and neurodegeneration in Alzheimer’s disease

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Synaptic Loss, ER Stress and Neuro-Inflammation Emerge Late in the Lateral Temporal Cortex and Associate with Progressive Tau Pathology in Alzheimer’s Disease

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Inhibition of the ISR abrogates mGluR5-dependent long-term depression and spatial memory deficits in a rat model of Alzheimer’s disease

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eIF2α phosphorylation controls thermal nociception

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KDEL receptor 1 regulates T-cell homeostasis via PP1 that is a key phosphatase for ISR

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Alzheimer’s therapy targeting the β-secretase enzyme BACE1: Benefits and potential limitations from the perspective of animal model studies

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Acteoside Attenuates Oxidative Stress and Neuronal Apoptosis in Rats with Focal Cerebral Ischemia–Reperfusion Injury

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PKR knockout in the 5xFAD model of Alzheimer's disease reveals beneficial effects on spatial memory and brain lesions

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Differential Activation of the ER Stress Factor XBP1 by Oligomeric Assemblies

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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

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Perspectives on ROCK2 as a Therapeutic Target for Alzheimer’s Disease

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The PKR/P38/RIPK1 Signaling Pathway as a Therapeutic Target in Alzheimer’s Disease

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Quercetin Regulates the Integrated Stress Response to Improve Memory

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eIF2-dependent translation initiation: Memory consolidation and disruption in Alzheimer’s disease

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Inflammation kinase PKR phosphorylates α-synuclein and causes α-synuclein-dependent cell death

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Double stranded RNA activated EIF2 α kinase (EIF2AK2; PKR) is associated with Alzheimer's disease

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PKR kinase directly regulates tau expression and Alzheimer's disease‐related tau phosphorylation

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Dysregulated mTORC1-Dependent Translational Control: From Brain Disorders to Psychoactive Drugs

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

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Age-dependent shift in the de novo proteome accompanies pathogenesis in an Alzheimer’s disease mouse model

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Lymphocytes from Young Healthy Persons Carrying the ApoE4 Allele Overexpress Stress-Related Proteins Involved in the Pathophysiology of Alzheimer's Disease

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Urokinase-Type Plasminogen Activator Protects Cerebral Cortical Neurons from Soluble Aβ-Induced Synaptic Damage

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Echinacoside Suppresses Amyloidogenesis and Modulates F-actin Remodeling by Targeting the ER Stress Sensor PERK in a Mouse Model of Alzheimer’s Disease

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Pathogenesis and promising therapeutics of Alzheimer disease through eIF2α pathway and correspondent kinases

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Nitric Oxide Influences HSV-1-Induced Neuroinflammation

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The Amyloid Cascade Hypothesis 2.0 for Alzheimer’s Disease and Aging-Associated Cognitive Decline: From Molecular Basis to Effective Therapy

Volloch, V., & Rits‐Volloch, S. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241512246 · Cited by 29

Inhibition of Double-Stranded RNA-Dependent Protein Kinase Strongly Decreases Cytokine Production and Release in Peripheral Blood Mononuclear Cells from Patients with Alzheimer's Disease

Couturier, J., Page, G., Morel, M., Gontier, C., Lecron, J., Pontcharraud, R., Fauconneau, B., & Paccalin, M. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100258 · Cited by 26

Satratoxin G–Induced Apoptosis in PC-12 Neuronal Cells is Mediated by PKR and Caspase Independent

Islam, Z., Hegg, C. C., Bae, H. K., & Pestka, J. J. (2008) · Toxicological Sciences · doi:10.1093/toxsci/kfn110 · Cited by 25

Senile plaques in Alzheimer’s diseased brains: Possible association of β-amyloid with herpes simplex virus type 1 (HSV-1) L-particles

Kammerman, E. M., Neumann, D. M., Ball, M. J., Lukiw, W. J., & Hill, J. M. (2005) · Medical Hypotheses · doi:10.1016/j.mehy.2005.07.033 · Cited by 24

Significance of Molecular Signaling for Protein Translation Control in Neurodegenerative Diseases

Chang, R. C., Yu, M.-S., & Lai, C. S.-W. (2006) · Neurosignals · doi:10.1159/000102599 · Cited by 22

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

Could PKR inhibition modulate human neurodegeneration?

Hugon, J., Paquet, C., & Chang, R. C. (2009) · Expert Review of Neurotherapeutics · doi:10.1586/ern.09.92 · Cited by 23

The Amyloid Cascade Hypothesis 2.0: Generalization of the Concept

Volloch, V., & Rits‐Volloch, S. (2022) · Journal of Alzheimer s Disease Reports · doi:10.3233/adr-220079 · Cited by 22

Bioinformatics Identification of Modules of Transcription Factor Binding Sites in Alzheimer′s Disease‐Related Genes by In Silico Promoter Analysis and Microarrays

Augustin, R., Lichtenthaler, S. F., Greeff, M., Hansen, J., Wurst, W., & Trümbach, D. (2011) · International Journal of Alzheimer s Disease · doi:10.4061/2011/154325 · Cited by 23

Inhibition of the PERK-Dependent Unfolded Protein Response Signaling Pathway Involved in the Pathogenesis of Alzheimer’s Disease

Rozpędek‐Kamińska, W., Pytel, D., Popławski, T., Walczak, A., Gradzik, K., Wawrzynkiewicz, A., Wojtczak, R., Mucha, B., Diehl, J. A., & Majsterek, I. (2019) · Current Alzheimer Research · doi:10.2174/1567205016666190228121157 · Cited by 22

The proteomic effects of ketone bodies: implications for proteostasis and brain proteinopathies

García‐Velázquez, L., & Massieu, L. (2023) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2023.1214092 · Cited by 21

A Perspective on the Potential Involvement of Impaired Proteostasis in Neuropsychiatric Disorders

Hui, K. K., Endo, R., Sawa, A., & Tanaka, M. (2021) · Biological Psychiatry · doi:10.1016/j.biopsych.2021.09.001 · Cited by 18

Concurrence of High Fat Diet and APOE Gene Induces Allele Specific Metabolic and Mental Stress Changes in a Mouse Model of Alzheimer’s Disease

Segev, Y., Livne, A., Mints, M., & Rosenblum, K. (2016) · Frontiers in Behavioral Neuroscience · doi:10.3389/fnbeh.2016.00170 · Cited by 18

Bis(ethylmaltolato)oxidovanadium (IV) mitigates neuronal apoptosis resulted from amyloid-beta induced endoplasmic reticulum stress through activating peroxisome proliferator-activated receptor γ

He, Z., Wang, M.-H., Zhao, Q., Li, X., Liu, P., Ren, B., Wu, C., Du, X., Li, N., & Liu, Q. (2020) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2020.111073 · Cited by 18

A truncated PACT protein resulting from a frameshift mutation reported in movement disorder DYT16 triggers caspase activation and apoptosis

Burnett, S. B., Vaughn, L. S., Strom, J. M., Francois, A., & Patel, R. C. (2019) · Journal of Cellular Biochemistry · doi:10.1002/jcb.29223 · Cited by 18

Dual Kinase Inhibition Affords Extended in vitro Neuroprotection in Amyloid-β Toxicity

Gourmaud, S., Mouton‐Liger, F., Abadie, C., MEURS, E. F., Paquet, C., & Hugon, J. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-160509 · Cited by 17

Blood-Based Kinase Assessments in Alzheimer’s Disease

Hugon, J., Mouton‐Liger, F., Cognat, E., Dumurgier, J., & Paquet, C. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00338 · Cited by 16

Revealing brain mechanisms of mTOR-mediated translational regulation: Implications for chronic pain

Cho, C., Michailidis, V., & Martin, L. J. (2018) · Neurobiology of Pain · doi:10.1016/j.ynpai.2018.03.002 · Cited by 16

The integrated stress response in the brain: cell type-specific functions in health and neurological disorders

Ho-Tieng, D., Sharma, V. K., Sonenberg, N., Gkogkas, C. G., & Khoutorsky, A. (2025) · Trends in Neurosciences · doi:10.1016/j.tins.2025.08.002 · Cited by 14

Expression of phosphorylated eukaryotic initiation factor 2 alpha in neuronal apoptosis beta-amyloid toxicity

Chang, R. C., Suen, K., & Ma, E. (2001) · The HKU Scholars Hub (University of Hong Kong)

Involvement of double‐stranded RNA‐dependent protein kinase and phosphorylation of eukaryotic initiation factor‐2α in neuronal degeneration

Chang, R. C., Suen, K., Ma, C., Elyaman, W., Ng, H., & Hugon, J. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.01237.x · Cited by 180

Activation of eukaryotic initiation factor-2α-kinases in okadaic acid-treated neurons

Kim, S. M., Yoon, S., Choi, J. E., Park, J. S., Choi, J. M., Nguyen, T. T., & Kim, D. H. (2010) · Neuroscience · doi:10.1016/j.neuroscience.2010.06.016 · Cited by 26

Differential expression of phosphorylated translation initiation factor 2 alpha in Alzheimer’s disease and Creutzfeldt-Jakob’s disease

Ferrer, I. (2002) · Neuropathology and Applied Neurobiology · doi:10.1046/j.1365-2990.2002.t01-1-00410.x · Cited by 52

P3‐344: Activation of eIF2α‐kinases in okadaic acid‐treated neurons

Yoon, S., Kim, S., Choi, J., & Kim, D. (2010) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2010.05.1845