ER stress-induced cell death mechanisms

Autophagy in the Pathogenesis of Disease

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Autophagy: Renovation of Cells and Tissues

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Endoplasmic Reticulum Stress Links Obesity, Insulin Action, and Type 2 Diabetes

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Bcl-2 Antiapoptotic Proteins Inhibit Beclin 1-Dependent Autophagy

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Roles of CHOP/GADD153 in endoplasmic reticulum stress

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Close Contacts with the Endoplasmic Reticulum as Determinants of Mitochondrial Ca ²⁺ Responses

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Autophagosome formation: core machinery and adaptations

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Perk is essential for translational regulation and cell survival during the unfolded protein response

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Gadd153 Sensitizes Cells to Endoplasmic Reticulum Stress by Down-Regulating Bcl2 and Perturbing the Cellular Redox State

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Autophagy Is Activated for Cell Survival after Endoplasmic ReticulumStress

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BCL-2, BCL-XL Sequester BH3 Domain-Only Molecules Preventing BAX- and BAK-Mediated Mitochondrial Apoptosis

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ER Stress Triggers Apoptosis by Activating BH3-Only Protein Bim

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XBP1 Links ER Stress to Intestinal Inflammation and Confers Genetic Risk for Human Inflammatory Bowel Disease

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Feedback Inhibition of the Unfolded Protein Response by GADD34-Mediated Dephosphorylation of eIF2α

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BAX and BAK Regulation of Endoplasmic Reticulum Ca 2+ : A Control Point for Apoptosis

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Plasma cell differentiation requires the transcription factor XBP-1

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Dissection of Autophagosome Formation Using Apg5-Deficient Mouse Embryonic Stem Cells

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Oligomerization and phosphorylation of the Ire1p kinase during intracellular signaling from the endoplasmic reticulum to the nucleus.

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The calcium-sensing receptor regulates the NLRP3 inflammasome through Ca2+ and cAMP

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Control of Macroautophagy by Calcium, Calmodulin-Dependent Kinase Kinase-β, and Bcl-2

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JNK phosphorylation of Bim-related members of the Bcl2 family induces Bax-dependent apoptosis

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Regulated Ire1-dependent decay of messenger RNAs in mammalian cells

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Autophagy Counterbalances Endoplasmic Reticulum Expansion during the Unfolded Protein Response

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TLR activation of the transcription factor XBP1 regulates innate immune responses in macrophages

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ER stress (PERK/eIF2α phosphorylation) mediates the polyglutamine-induced LC3 conversion, an essential step for autophagy formation

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Stress-Induced Phosphorylation and Activation of the Transcription Factor CHOP (GADD153) by p38 MAP Kinase

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Endoplasmic Reticulum Stress Plays a Central Role in Development of Leptin Resistance

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IRE1α Induces Thioredoxin-Interacting Protein to Activate the NLRP3 Inflammasome and Promote Programmed Cell Death under Irremediable ER Stress

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CHOP Is Involved in Endoplasmic Reticulum Stress-induced Apoptosis by Enhancing DR5 Expression in Human Carcinoma Cells

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IRE1α Kinase Activation Modes Control Alternate Endoribonuclease Outputs to Determine Divergent Cell Fates

Han, D., Lerner, A. G., Walle, L. V., Upton, J.-P., Xu, W., Hagen, A., Backes, B. J., Oakes, S. A., & Papa, F. R. (2009) · Cell · doi:10.1016/j.cell.2009.07.017 · Cited by 816 · see citing works

Novel role of PKR in inflammasome activation and HMGB1 release

Lü, B., Nakamura, T., Inouye, K., Li, J., Tang, Y., Lundbäck, P., Valdés‐Ferrer, S. I., Olofsson, P. S., Kalb, T. H., Roth, J., et al. (2012) · Nature · doi:10.1038/nature11290 · Cited by 772 · see citing works

Connecting endoplasmic reticulum stress to autophagy by unfolded protein response and calcium

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Atg8 Controls Phagophore Expansion during Autophagosome Formation

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PERK-dependent Activation of Nrf2 Contributes to Redox Homeostasis and Cell Survival following Endoplasmic Reticulum Stress

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Unfolded Proteins Are Ire1-Activating Ligands That Directly Induce the Unfolded Protein Response

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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

Endoplasmic reticulum stress, obesity and diabetes

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Thioredoxin-Interacting Protein Mediates ER Stress-Induced β Cell Death through Initiation of the Inflammasome

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IRE1α Cleaves Select microRNAs During ER Stress to Derepress Translation of Proapoptotic Caspase-2

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Proteasome inhibitors disrupt the unfolded protein response in myeloma cells

Lee, A., Iwakoshi, N. N., Anderson, K. C., & Glimcher, L. H. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1334037100 · Cited by 600 · see citing works

Role of ERO1-α–mediated stimulation of inositol 1,4,5-triphosphate receptor activity in endoplasmic reticulum stress–induced apoptosis

Li, G., Mongillo, M., Chin, K., Harding, H. P., Ron, D., Marks, A. R., & Tabas, I. A. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200904060 · Cited by 597 · see citing works

Caspase cleavage product of BAP31 induces mitochondrial fission through endoplasmic reticulum calcium signals, enhancing cytochrome c release to the cytosol

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Double-Stranded RNA-Dependent Protein Kinase Links Pathogen Sensing with Stress and Metabolic Homeostasis

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Reducing endoplasmic reticulum stress through a macrophage lipid chaperone alleviates atherosclerosis

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JNK- and p38 kinase-mediated phosphorylation of Bax leads to its activation and mitochondrial translocation and to apoptosis of human hepatoma HepG2 cells

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BiP Binding to the ER-Stress Sensor Ire1 Tunes the Homeostatic Behavior of the Unfolded Protein Response

Pincus, D., Chevalier, M. W., Aragón, T., van Anken, E., Vidal, S. E., El‐Samad, H., & Walter, P. (2010) · PLoS Biology · doi:10.1371/journal.pbio.1000415 · Cited by 433 · see citing works

Viruses, endoplasmic reticulum stress, and interferon responses

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ER stress-induced inflammation: does it aid or impede disease progression?

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Obesity-induced endoplasmic reticulum stress causes chronic inflammation in adipose tissue

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The structure of Atg4B–LC3 complex reveals the mechanism of LC3 processing and delipidation during autophagy

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Translation Attenuation through eIF2α Phosphorylation Prevents Oxidative Stress and Maintains the Differentiated State in β Cells

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HsAtg4B/HsApg4B/Autophagin-1 Cleaves the Carboxyl Termini of Three Human Atg8 Homologues and Delipidates Microtubule-associated Protein Light Chain 3- and GABAA Receptor-associated Protein-Phospholipid Conjugates

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ER stress in Alzheimer's disease: a novel neuronal trigger for inflammation and Alzheimer's pathology

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BAX Inhibitor-1 Is a Negative Regulator of the ER Stress Sensor IRE1α

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The BAG proteins: a ubiquitous family of chaperone regulators

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The Autophagy Protein Atg12 Associates with Antiapoptotic Bcl-2 Family Members to Promote Mitochondrial Apoptosis

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The CREB coactivator CRTC2 links hepatic ER stress and fasting gluconeogenesis

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Novel Role for JNK as a Stress-activated Bcl2 Kinase

Deng, X., Xiao, L., Lang, W., Gao, F., Ruvolo, P. P., & May, W. S. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100279200 · Cited by 296 · see citing works

BI-1 Regulates an Apoptosis Pathway Linked to Endoplasmic Reticulum Stress

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CHOP/GADD153 is a mediator of apoptotic death in substantia nigra dopamine neurons in an in vivo neurotoxin model of parkinsonism

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XBP1 mRNA Splicing Triggers an Autophagic Response in Endothelial Cells through BECLIN-1 Transcriptional Activation

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Endoplasmic Reticulum Stress Response Mediated by the PERK-eIF2α-ATF4 Pathway Is Involved in Osteoblast Differentiation Induced by BMP2

Saito, A., Ochiai, K., Kondo, S., Tsumagari, K., Murakami, T., Cavener, D. R., & Imaizumi, K. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.152900 · Cited by 282 · see citing works

Reduction of ER stress via a chemical chaperone prevents disease phenotypes in a mouse model of primary open angle glaucoma

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Reduction of ER stress via a chemical chaperone prevents disease phenotypes in a mouse model of primary open angle glaucoma

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How IRE1 Reacts to ER Stress

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Targeted deletion of apoptosis signal-regulating kinase 1 attenuates left ventricular remodeling

Yamaguchi, O., Higuchi, Y., Hirotani, S., Kashiwase, K., Nakayama, H., Hikoso, S., Takeda, T., Watanabe, T., Asahi, M., Taniike, M., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2136717100 · Cited by 222 · see citing works

The transcription factor ATF4 regulates glucose metabolism in mice through its expression in osteoblasts

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The Endoplasmic Reticulum Stress-C/EBP Homologous Protein Pathway-Mediated Apoptosis in Macrophages Contributes to the Instability of Atherosclerotic Plaques

Tsukano, H., Gotoh, T., Endo, M., Miyata, K., Tazume, H., Kadomatsu, T., Yano, M., Iwawaki, T., Kohno, K., Araki, K., et al. (2010) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.110.206094 · Cited by 211 · see citing works

miR-211 Is a Prosurvival MicroRNA that Regulates chop Expression in a PERK-Dependent Manner

Chitnis, N., Pytel, D., Bobrovnikova-Marjon, E. V., Pant, D. K., Zheng, H. W., Maas, N. L., Frederick, B. T., Kushner, J. A., Chodosh, L. A., Koumenis, C., et al. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.08.025 · Cited by 205 · see citing works

Identification of Toyocamycin, an agent cytotoxic for multiple myeloma cells, as a potent inhibitor of ER stress-induced XBP1 mRNA splicing

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Unfolded protein response in cancer: the Physician's perspective

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Induction of the unfolded protein response and cell death pathway in Alzheimer's disease, but not in aged Tg2576 mice

Lee, J. H., Won, S. M., Suh, J., Son, S. J., Moon, G. J., Park, U. J., & Gwag, B. J. (2010) · Experimental & Molecular Medicine · doi:10.3858/emm.2010.42.5.040 · Cited by 184 · see citing works

Macrophage Apoptosis in Atherosclerosis: Consequences on Plaque Progression and the Role of Endoplasmic Reticulum Stress

Tabas, I. A. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2469 · Cited by 181 · see citing works

Herpes Simplex Virus 1 Infection Activates the Endoplasmic Reticulum Resident Kinase PERK and Mediates eIF-2α Dephosphorylation by the γ 1 34.5 Protein

Cheng, G., Feng, Z., & He, B. (2005) · Journal of Virology · doi:10.1128/jvi.79.3.1379-1388.2005 · Cited by 165 · see citing works

ER Stress and Unfolded Protein Response in Amyotrophic Lateral Sclerosis

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Serine 129 Phosphorylation of α-Synuclein Induces Unfolded Protein Response-mediated Cell Death

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Bax inhibitor-1: a highly conserved endoplasmic reticulum-resident cell death suppressor

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Toll-like receptor activation suppresses ER stress factor CHOP and translation inhibition through activation of eIF2B

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Involvement of the double-stranded-RNA-dependent kinase PKR in interferon expression and interferon-mediated antiviral activity.

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BAX inhibitor‐1 regulates autophagy by controlling the IRE1α branch of the unfolded protein response

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BI-1 Regulates Endoplasmic Reticulum Ca2+ Homeostasis Downstream of Bcl-2 Family Proteins

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MicroRNA-30c-2* limits expression of proadaptive factor XBP1 in the unfolded protein response

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Transmembrane bZIP Transcription Factors in ER Stress Signaling and the Unfolded Protein Response

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Hepatic Bax Inhibitor-1 Inhibits IRE1α and Protects from Obesity-associated Insulin Resistance and Glucose Intolerance

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