Cited by 1,691Endoplasmic Reticulum Stress and DiseaseHeat shock proteins researchIon Channels and Receptors

The DOI matches its Crossref record; 66 of the 66 references it cites were found in a registry or an index.

ER-stress-induced transcriptional regulation increases protein synthesis leading to cell death

Open access

Han, Jaeseok, Back, Sung Hoon, Hur, Junguk, Lin, Yu-Hsuan, Gildersleeve, Robert, Shan, Jixiu, Yuan, Celvie L., Krokowski, Dawid, Wang, Shiyu, Hatzoglou, Maria, Kilberg, Michael S., Sartor, Maureen A., Kaufman, Randal J.·2013·Nature Cell Biology

DOI 10.1038/ncb2738PMC PMC3692270

Open this paper in CoChat — free account

Abstract

Protein misfolding in the endoplasmic reticulum (ER) leads to cell death through PERK-mediated phosphorylation of eIF2α, although the mechanism is not understood. ChIP-seq and mRNA-seq of activating transcription factor 4 (ATF4) and C/EBP homologous protein (CHOP), key transcription factors downstream of p-eIF2α, demonstrated that they interact to directly induce genes encoding protein synthesis and the unfolded protein response, but not apoptosis. Forced expression of ATF4 and CHOP increased protein synthesis and caused ATP depletion, oxidative stress and cell death. The increased protein synthesis and oxidative stress were necessary signals for cell death. We show that eIF2α-phosphorylation-attenuated protein synthesis, and not Atf4 mRNA translation, promotes cell survival. These results show that transcriptional induction through ATF4 and CHOP increases protein synthesis leading to oxidative stress and cell death. The findings suggest that limiting protein synthesis will be therapeutic for diseases caused by protein misfolding in the ER.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1038/ncb2738

Cites

66 of 66 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources
Huang, D. W., Sherman, B. T., & Lempicki, R. A. (2009) · Nature Protocols · doi:10.1038/nprot.2008.211 · Cited by 35,890
The Unfolded Protein Response: From Stress Pathway to Homeostatic Regulation
Walter, P., & Ron, D. (2011) · Science · doi:10.1126/science.1209038 · Cited by 5,897
The unfolded protein response: controlling cell fate decisions under ER stress and beyond
Hetz, C. A. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3270 · Cited by 4,223
Regulated Translation Initiation Controls Stress-Induced Gene Expression in Mammalian Cells
Harding, H. P., Novoa, I., Zhang, Y., Zeng, H., Wek, R. C., Schapira, M., & Ron, D. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)00108-8 · Cited by 3,344
An Integrated Stress Response Regulates Amino Acid Metabolism and Resistance to Oxidative Stress
Harding, H. P., Zhang, Y., Zeng, H., Novoa, I., Lu, P. D., Calfon, M. A., Sadri, N., Yun, C., Popko, B., Paules, R. S., et al. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00105-9 · Cited by 3,336
Genome-Wide Mapping of in Vivo Protein-DNA Interactions
Johnson, D. S., Mortazavi, A., Myers, R. M., & Wold, B. (2007) · Science · doi:10.1126/science.1141319 · Cited by 2,927
Integrating the mechanisms of apoptosis induced by endoplasmic reticulum stress
Tabas, I. A., & Ron, D. (2011) · Nature Cell Biology · doi:10.1038/ncb0311-184 · Cited by 2,655
CHOP induces death by promoting protein synthesis and oxidation in the stressed endoplasmic reticulumPreprint
Marciniak, S. J., Yun, C. Y., Oyadomari, S., Novoa, I., Zhang, Y., Jungreis, R., Nagata, K., Harding, H. P., & Ron, D. (2004) · Genes & Development · doi:10.1101/gad.1250704 · Cited by 2,066
CHOP is implicated in programmed cell death in response to impaired function of the endoplasmic reticulumPreprint
Zinszner, H., Kuroda, M., Wang, X., Batchvarova, N., Lightfoot, R. T., Remotti, H. E., Stevens, J. L., & Ron, D. (1998) · Genes & Development · doi:10.1101/gad.12.7.982 · Cited by 2,039
Gadd153 Sensitizes Cells to Endoplasmic Reticulum Stress by Down-Regulating Bcl2 and Perturbing the Cellular Redox State
McCullough, K. D., Martindale, J. L., Klotz, L., Aw, T. Y., & Holbrook, N. J. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.4.1249-1259.2001 · Cited by 1,945

Flagged first, then by citations

Show all 66 references

Sorted by citations

Items 401–500 of 1,000

The eukaryotic initiation factor 2 kinase GCN2 protects against hepatotoxicity during asparaginase treatment
Wilson, G. J., Bunpo, P., Cundiff, J. K., Wek, R. C., & Anthony, T. G. (2013) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00080.2013 · Cited by 57
Transcriptional Regulation of Cystathionine-γ-Lyase in Endothelial Cells by NADPH Oxidase 4-Dependent Signaling
Mistry, R. K., Murray, T. V., Prysyazhna, O. D., Martin, D., Burgoyne, J. R., Santos, C. X. C., Eaton, P., Shah, A. M., & Brewer, A. C. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.685578 · Cited by 60
Nutritional Stress Induced by Tryptophan-Degrading Enzymes Results in ATF4-Dependent Reprogramming of the Amino Acid Transporter Profile in Tumor Cells
Timosenko, E., Ghadbane, H., Silk, J. D., Shepherd, D., Gileadi, U., Howson, L. J., Laynes, R., Zhao, Q., Strausberg, R. L., Olsen, L. R., et al. (2016) · Cancer Research · doi:10.1158/0008-5472.can-15-3502 · Cited by 60
Activating transcription factor-4 promotes mineralization in vascular smooth muscle cells
Masuda, M., Miyazaki‐Anzai, S., Keenan, A. L., Shiozaki, Y., Okamura, K., Chick, W. S. H., Williams, K., Zhao, X., Rahman, S. M., Tintut, Y., et al. (2016) · JCI Insight · doi:10.1172/jci.insight.88646 · Cited by 57
GCN2 deficiency ameliorates cardiac dysfunction in diabetic mice by reducing lipotoxicity and oxidative stress
Feng, W. H., Lei, T., Wang, Y., Feng, R. M., Yuan, J.-T., Shen, X., Wu, Y., Gao, J., Ding, W., & Lu, Z. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.10.445 · Cited by 57
Caspase-mediated cleavage of IRE1 controls apoptotic cell commitment during endoplasmic reticulum stress
Shemorry, A., Harnoss, J. M., Guttman, O., Marsters, S. A., Kömüves, L. G., Lawrence, D. A., & Ashkenazi, A. (2019) · eLife · doi:10.7554/elife.47084 · Cited by 57
Selenoprotein T: An Essential Oxidoreductase Serving as a Guardian of Endoplasmic Reticulum Homeostasis
Pothion, H., Jehan, C., Tostivint, H., Cartier, D., Bucharles, C., Falluel‐Morel, A., Boukhzar, L., Anouar, Y., & Lihrmann, I. (2020) · Antioxidants and Redox Signaling · doi:10.1089/ars.2019.7931 · Cited by 57
The transcription factor CHOP, a central component of the transcriptional regulatory network induced upon CCl4 intoxication in mouse liver, is not a critical mediator of hepatotoxicity
Campos, G., Schmidt‐Heck, W., Ghallab, A., Rochlitz, K., Pütter, L., Medinas, D. B., Hetz, C. A., Widera, A., Cadenas, C., Begher‐Tibbe, B., et al. (2014) · Archives of Toxicology · doi:10.1007/s00204-014-1240-8 · Cited by 56
Neuronal endoplasmic reticulum stress in axon injury and neurodegeneration
Li, S., Liu, Y., Selzer, M. E., & Hu, Y. (2013) · Annals of Neurology · doi:10.1002/ana.24005 · Cited by 56
ER proteostasis addiction in cancer biology: Novel concepts
Dufey, E., Urra, H., & Hetz, C. A. (2015) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2015.04.003 · Cited by 58
The PERK pathway independently triggers apoptosis and a Rac1/Slpr/JNK/Dilp8 signaling favoring tissue homeostasis in a chronic ER stress Drosophila model
Demay, Y., Perochon, J., Szuplewski, S., Mignotte, B., & Gaumer, S. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.403 · Cited by 62
Testosterone production by a Leydig tumor cell line is suppressed by hyperthermia-induced endoplasmic reticulum stress in mice
Kim, J., Park, S.-J., Kim, T., Kim, J., & Lee, D. (2015) · Life Sciences · doi:10.1016/j.lfs.2015.12.042 · Cited by 56
Targeting p97 to Disrupt Protein Homeostasis in Cancer
Vekaria, P., Home, T., Weir, S. J., Schoenen, F. J., & Rao, R. (2016) · Frontiers in Oncology · doi:10.3389/fonc.2016.00181 · Cited by 61
Neuroprotective effect of He-Ying-Qing-Re formula on retinal ganglion cell in diabetic retinopathy
Zhang, C., Xu, Y., Tan, H., Li, S., Wang, N., Zhang, Y., & Feng, Y. (2017) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2017.12.018 · Cited by 58
Effects of Antioxidants in Reducing Accumulation of Fat in Hepatocyte
Yang, J., Shin, J., Seo, S., Kim, S., Lee, S. H., & Shin, E. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19092563 · Cited by 56
Mevalonate Pathway Enzyme HMGCS1 Contributes to Gastric Cancer Progression
Wang, I.-H., Huang, T., Chen, J., Chu, L.-W., Ping, Y., Hsu, K., Huang, K., Fang, W., Lee, H., Chen, C., et al. (2020) · Cancers · doi:10.3390/cancers12051088 · Cited by 57
A stress-responsive enhancer induces dynamic drug resistance in acute myeloid leukemia
Williams, M. S., Amaral, F. M. R., Simeoni, F., & Somervaille, T. C. P. (2019) · Journal of Clinical Investigation · doi:10.1172/jci130809 · Cited by 59
ATF6 is essential for human cone photoreceptor development
Kroeger, H., Grandjean, J. M. D., Chiang, W.-C. J., Bindels, D. S., Mastey, R., Okáľová, J., Nguyen, A., Powers, E. T., Kelly, J. W., Grimsey, N. J., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2103196118 · Cited by 55
β- cell dynamics in type 2 diabetes and in dietary and exercise interventions
Lv, C.-A., Sun, Y., Zhang, Z. Y., Aboelela, Z., Qiu, X., & Meng, Z. (2022) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjac046 · Cited by 57
Endoplasmic reticulum stress in brain ischemia
Su, Y., & Li, F. (2015) · International Journal of Neuroscience · doi:10.3109/00207454.2015.1059836 · Cited by 55
How does protein misfolding in the endoplasmic reticulum affect lipid metabolism in the liver?
Wang, S., & Kaufman, R. J. (2014) · Current Opinion in Lipidology · doi:10.1097/mol.0000000000000056 · Cited by 56
Self-citation
Regulation of the unfolded protein response by microRNAs
Bartoszewska, S., Kochan, K., Madanecki, P., Piotrowski, A., Ochocka, J. R., Collawn, J. F., & Bartoszewski, R. (2013) · Cellular & Molecular Biology Letters · doi:10.2478/s11658-013-0106-z · Cited by 56
Noncanonical SQSTM1/p62-Nrf2 pathway activation mediates proteasome inhibitor resistance in multiple myeloma cells via redox, metabolic and translational reprogramming
Riz, I., Hawley, T. S., Marsal, J., & Hawley, R. G. (2016) · Oncotarget · doi:10.18632/oncotarget.11960 · Cited by 56
TED-Seq Identifies the Dynamics of Poly(A) Length during ER Stress
Woo, Y. M., Kwak, Y., Namkoong, S., Kristjánsdóttir, K., Lee, S. H., Lee, J. H., & Kwak, H. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.08.084 · Cited by 55
Current Status of Endoplasmic Reticulum Stress in Type II Diabetes
Mustapha, S., Mohammed, M., Azemi, A. K., Jatau, A. I., Shehu, A., Mustapha, L., Aliyu, I. M., Danraka, R. N., Amin, A., Bala, A. A., et al. (2021) · Molecules · doi:10.3390/molecules26144362 · Cited by 54
Understanding ER homeostasis and the UPR to enhance treatment efficacy of acute myeloid leukemia
Śniegocka, M., Liccardo, F., Fazi, F., & Masciarelli, S. (2022) · Drug Resistance Updates · doi:10.1016/j.drup.2022.100853 · Cited by 54
Endoplasmic reticulum stress: key promoter of rosacea pathogenesis
Melnik, B. C. (2014) · Experimental Dermatology · doi:10.1111/exd.12517 · Cited by 56
Amyloid beta receptors responsible for neurotoxicity and cellular defects in Alzheimer’s disease
Kam, T., Gwon, Y., & Jung, Y. (2014) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1706-0 · Cited by 59
Subverting ER-Stress towards Apoptosis by Nelfinavir and Curcumin Coexposure Augments Docetaxel Efficacy in Castration Resistant Prostate Cancer Cells
Mathur, A., Elmageed, Z. Y. A., Liu, X., Kostochka, M. L., Zhang, H., Abdel‐Mageed, A. B., & Mondal, D. (2014) · PLoS ONE · doi:10.1371/journal.pone.0103109 · Cited by 54
γ-Tocotrienol-induced endoplasmic reticulum stress and autophagy act concurrently to promote breast cancer cell death
Tiwari, R. V., Parajuli, P., & Sylvester, P. W. (2015) · Biochemistry and Cell Biology · doi:10.1139/bcb-2014-0123 · Cited by 54
Inhibition of autophagic flux by ROS promotes apoptosis during DTT-induced ER/oxidative stress in HeLa cells
Xiang, X., Yang, X., Su, J., KANG, J.-S., Wu, Y., Xue, Y., Dong, Y., & Sun, L. (2016) · Oncology Reports · doi:10.3892/or.2016.4725 · Cited by 54
Translation attenuation by minocycline enhances longevity and proteostasis in old post-stress-responsive organisms
Solis, G. M., Kardakaris, R., Valentine, E. R., Bar‐Peled, L., Chen, A. L., Blewett, M. M., McCormick, M. A., Williamson, J. R., Kennedy, B. K., Cravatt, B. F., et al. (2018) · eLife · doi:10.7554/elife.40314 · Cited by 56
The transcription factor Xrp1 is required for PERK-mediated antioxidant gene induction in Drosophila
Brown, B., Mitra, S., Roach, F. D., Vasudevan, D., & Ryoo, H. D. (2021) · eLife · doi:10.7554/elife.74047 · Cited by 53
Integrated stress response regulates GDF15 secretion from adipocytes, preferentially suppresses appetite for a high-fat diet and improves obesity
Miyake, M., Zhang, J., Yasue, A., Hisanaga, S., Tsugawa, K., Sakaue, H., Oyadomari, M., Kiyonari, H., & Oyadomari, S. (2021) · iScience · doi:10.1016/j.isci.2021.103448 · Cited by 55
GSK2606414 attenuates PERK/p-eIF2α/ATF4/CHOP axis and augments mitochondrial function to mitigate high glucose induced neurotoxicity in N2A cells
Gundu, C., Arruri, V. K., Sherkhane, B., Khatri, D. K., & Singh, S. B. (2022) · Current Research in Pharmacology and Drug Discovery · doi:10.1016/j.crphar.2022.100087 · Cited by 54
Cis- and trans-resveratrol have opposite effects on histone serine-ADP-ribosylation and tyrosine induced neurodegeneration
Jhanji, M., Rao, C. N., Massey, J. C., Hope, M. C., Zhou, X., Keene, C. D., Ma, T., Wyatt, M. D., Stewart, J. A., & Sajish, M. (2022) · Nature Communications · doi:10.1038/s41467-022-30785-8 · Cited by 55
Endoplasmic Reticulum Stress, Oxidative Stress, and Rheumatic Diseases
Scavuzzi, B. M., & Holoshitz, J. (2022) · Antioxidants · doi:10.3390/antiox11071306 · Cited by 55
Oxidative Stress Mediates Microcystin-LR-Induced Endoplasmic Reticulum Stress and Autophagy in KK-1 Cells and C57BL/6 Mice Ovaries
Liu, H., Zhang, X., Zhang, S., Huang, H., Wu, J., Wang, Y., Yuan, L., Liu, C., Zeng, X., Cheng, X., et al. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.01058 · Cited by 53
Widespread PERK-dependent repression of ER targets in response to ER stress
Gonen, N., Sabath, N., Burge, C. B., & Shalgi, R. (2019) · Scientific Reports · doi:10.1038/s41598-019-38705-5 · Cited by 53
The drug adaptaquin blocks ATF4/CHOP-dependent pro-death Trib3 induction and protects in cellular and mouse models of Parkinson's disease
Aimé, P., Karuppagounder, S. S., Rao, A., Chen, Y., Burke, R. E., Ratan, R. R., & Greene, L. A. (2020) · Neurobiology of Disease · doi:10.1016/j.nbd.2019.104725 · Cited by 55
Endoplasmic reticulum stress: New insights into the pathogenesis and treatment of retinal degenerative diseases
Gorbatyuk, M. S., Starr, C. R., & Gorbatyuk, O. S. (2020) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2020.100860 · Cited by 53
Characterizing Cell Stress and GRP78 in Glioma to Enhance Tumor Treatment
Liu, K., Tsung, K., & Attenello, F. J. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.608911 · Cited by 54
RGS2-mediated translational control mediates cancer cell dormancy and tumor relapse
Cho, J., Min, H., Lee, H. J., Hyun, S. Y., Sim, J. Y., Noh, M., Hwang, S. J., Park, S., Boo, H., Lee, H., et al. (2021) · Journal of Clinical Investigation · doi:10.1172/jci136779 · Cited by 53
The complex interplay between endoplasmic reticulum stress and the NLRP3 inflammasome: a potential therapeutic target for inflammatory disorders
Chong, W. C., Shastri, M. D., Peterson, G. M., Patel, R. P., Pathinayake, P. S., Dua, K., Hansbro, N. G., Hsu, A., Wark, P. A. B., Shukla, S. D., et al. (2021) · Clinical & Translational Immunology · doi:10.1002/cti2.1247 · Cited by 54
Nutrient Sensing in Cancer
Torrence, M. E., & Manning, B. D. (2017) · Annual Review of Cancer Biology · doi:10.1146/annurev-cancerbio-030617-050329 · Cited by 55
Drosophila melanogasterActivating Transcription Factor 4 Regulates Glycolysis During Endoplasmic Reticulum Stress
Lee, J., Oney, M., Frizzell, K., Phadnis, N., & Hollien, J. (2015) · G3 Genes Genomes Genetics · doi:10.1534/g3.115.017269 · Cited by 52
A forward genetic screen reveals novel independent regulators of ULBP1, an activating ligand for natural killer cells
Gowen, B. G., Chim, B., Marceau, C. D., Greene, T. T., Burr, P., Gonzalez, J. R., Hesser, C. R., Dietzen, P. A., Russell, T. A., Iannello, A., et al. (2015) · eLife · doi:10.7554/elife.08474 · Cited by 52
A Drosophila Reporter for the Translational Activation of ATF4 Marks Stressed Cells during Development
Kang, K., Ryoo, H. D., Park, J., Yoon, J., & Kang, M. (2015) · PLoS ONE · doi:10.1371/journal.pone.0126795 · Cited by 52
Nutlin-3 enhances the bortezomib sensitivity of p53-defective cancer cells by inducing paraptosis
Lee, D. M., Kim, I. Y., Seo, M. J., Kwon, M. R., & Choi, K. S. (2017) · Experimental & Molecular Medicine · doi:10.1038/emm.2017.112 · Cited by 52
P2RX7-MAPK1/2-SP1 axis inhibits MTOR independent HSPB1-mediated astroglial autophagy
Kim, J.-E., Ko, A.-R., Hyun, H.-W., Min, S.-J., & Kang, T. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-0586-x · Cited by 54
Translational Regulations in Response to Endoplasmic Reticulum Stress in Cancers
Jaud, M., Philippe, C., Bella, D. D., Tang, W., Pyronnet, S., Laurell, H., Mazzolini, L., Rouault‐Pierre, K., & Touriol, C. (2020) · Cells · doi:10.3390/cells9030540 · Cited by 58
Mastering organismal aging through the endoplasmic reticulum proteostasis network
Taylor, R. C., & Hetz, C. A. (2020) · Aging Cell · doi:10.1111/acel.13265 · Cited by 55
Endoplasmic reticulum stress is activated in acute pancreatitis
Wu, J. S., Li, W. M., Chen, Y. N., Zhao, Q., & Chen, Q. (2016) · Journal of Digestive Diseases · doi:10.1111/1751-2980.12347 · Cited by 51
Naringenin ameliorates hypoxia/reoxygenation-induced endoplasmic reticulum stress-mediated apoptosis in H9c2 myocardial cells: involvement in ATF6, IRE1α and PERK signaling activation
Tang, J., Jin, P., He, Q. P., Lu, L., Ma, J., Gao, W.-L., Bai, H., & Yang, J. Z. (2016) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-016-2848-1 · Cited by 51
TUDCA attenuates intestinal injury and inhibits endoplasmic reticulum stress-mediated intestinal cell apoptosis in necrotizing enterocolitis
Li, P., Fu, D., Sheng, Q., Yu, S., Bao, X., & Lv, Z. (2019) · International Immunopharmacology · doi:10.1016/j.intimp.2019.05.050 · Cited by 51
Pituitary cell translation and secretory capacities are enhanced cell autonomously by the transcription factor Creb3l2
Khetchoumian, K., Balsalobre, A., Mayran, A., Christian, H., Chénard, V., St‐Pierre, J., & Drouin, J. (2019) · Nature Communications · doi:10.1038/s41467-019-11894-3 · Cited by 53
The unfolded protein response links tumor aneuploidy to local immune dysregulation
Su, X., Dosset, M., Almanza, G., Searles, S. C., Sahani, P., Waller, T. C., Jepsen, K., Carter, H. K., & Zanetti, M. (2021) · EMBO Reports · doi:10.15252/embr.202152509 · Cited by 51
Regulation of cellular immunity by activating transcription factor 4
Mukherjee, D., Bercz, L. S., Torok, M. A., & Mace, T. A. (2020) · Immunology Letters · doi:10.1016/j.imlet.2020.09.006 · Cited by 51
Bone marrow plasma cells require P2RX4 to sense extracellular ATP
Ishikawa, M., Hasanali, Z. S., Zhao, Y., Das, A., Lavaert, M., Roman, C. J., Londregan, J., Allman, D., & Bhandoola, A. (2024) · Nature · doi:10.1038/s41586-024-07047-2 · Cited by 53
Dipeptidyl peptidase-4 inhibitor, vildagliptin, inhibits pancreatic beta cell apoptosis in association with its effects suppressing endoplasmic reticulum stress in db/db mice
Wu, Y., Guo, X., Li, C., Li, D., Zhang, J., Yang, Y., Kong, Y., Guo, H., Liu, D., & Chen, L. (2014) · Metabolism · doi:10.1016/j.metabol.2014.08.006 · Cited by 50
Antioxidants Complement the Requirement for Protein Chaperone Function to Maintain β-Cell Function and Glucose Homeostasis
Han, J., Song, B., Kim, J., Kodali, V. K., Pottekat, A., Wang, M., Hassler, J. R., Wang, S., Pennathur, S., Back, S. H., et al. (2015) · Diabetes · doi:10.2337/db14-1357 · Cited by 52
Self-citation
Madecassic Acid protects against hypoxia-induced oxidative stress in retinal microvascular endothelial cells via ROS-mediated endoplasmic reticulum stress
Yang, B., Xu, Y., Hu, Y., Luo, Y., Lü, X., Tsui, C., Lü, L., & Liang, X. (2016) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2016.10.015 · Cited by 50
Regulation of the unfolded protein response by noncoding RNA
McMahon, M., Samali, A., & Chevet, É. (2017) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00293.2016 · Cited by 50
Emerging Role of the Unfolded Protein Response in Tumor Immunosurveillance
Vanacker, H., Vetters, J., Moudombi, L., Caux, C., Janssens, S., & Michallet, M. (2017) · Trends in cancer · doi:10.1016/j.trecan.2017.05.005 · Cited by 50
DDX3 regulates endoplasmic reticulum stress-induced ATF4 expression
Adjibade, P., St-Sauveur, V. G., Bergeman, J., Huot, M., Khandjian, É. W., & Mazrouï, R. (2017) · Scientific Reports · doi:10.1038/s41598-017-14262-7 · Cited by 52
Preparation, characterization, and evaluation of azoxystrobin nanosuspension produced by wet media milling
Yao, J., Cui, B., Zhao, X., Wang, Y., Zeng, Z., Sun, C., Yang, D.-S., Liu, G., Gao, J., & Cui, H. (2018) · Applied Nanoscience · doi:10.1007/s13204-018-0745-5 · Cited by 50
Natural antioxidants’ effects on endoplasmic reticulum stress-related diseases
Reyes-Fermín, L. M., Aparicio-Trejo, O. E., Avila-Rojas, S. H., Gómez-Sierra, T., Martínez-Klimova, E., & Pedraza-Chaverri, J. (2020) · Food and Chemical Toxicology · doi:10.1016/j.fct.2020.111229 · Cited by 50
A beneficial adaptive role for CHOP in driving cell fate selection during ER stress
Liu, K., Zhao, C., Adajar, R. C., DeZwaan-McCabe, D., & Rutkowski, D. T. (2024) · EMBO Reports · doi:10.1038/s44319-023-00026-0 · Cited by 51
Programming a Ferroptosis‐to‐Apoptosis Transition Landscape Revealed Ferroptosis Biomarkers and Repressors for Cancer Therapy
Vinik, Y., Maimon, A., Dubey, V., Raj, H., Abramovich, I., Malitsky, S., Itkin, M., Ma’ayan, A., Westermann, F., Gottlieb, E., et al. (2024) · Advanced Science · doi:10.1002/advs.202307263 · Cited by 49
Palmitate Induces mRNA Translation and Increases ER Protein Load in Islet β-Cells via Activation of the Mammalian Target of Rapamycin Pathway
Hatanaka, M., Maier, B., Sims, E. K., Templin, A. T., Kulkarni, R., Evans‐Molina, C., & Mirmira, R. G. (2014) · Diabetes · doi:10.2337/db14-0105 · Cited by 49
Activation of SK2 channels preserves ER Ca2+ homeostasis and protects against ER stress-induced cell death
Richter, M., Vidovic, N., Honrath, B., Mahavadi, P., Dodel, R. C., Dolga, A. M., & Culmsee, C. (2015) · Cell Death and Differentiation · doi:10.1038/cdd.2015.146 · Cited by 49
eIF2α phosphorylation controls thermal nociception
Khoutorsky, A., Sorge, R. E., Prager‐Khoutorsky, M., Pawlowski, S. A., Longo, G., Jafarnejad, S. M., Tahmasebi, S., Martin, L. J., Pitcher, M. H., Gkogkas, C. G., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1614047113 · Cited by 50
Can Co-Activation of Nrf2 and Neurotrophic Signaling Pathway Slow Alzheimer’s Disease?
Murphy, K. E., & Park, J. C. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18061168 · Cited by 49
Retinoic acid and arsenic trioxide sensitize acute promyelocytic leukemia cells to ER stress
Masciarelli, S., Capuano, E., Ottone, T., Divona, M., Panfilis, S. D., Banella, C., Noguera, N. I., Picardi, A., Fontemaggi, G., Blandino, G., et al. (2017) · Leukemia · doi:10.1038/leu.2017.231 · Cited by 49
Time-resolved analysis of amino acid stress identifies eIF2 phosphorylation as necessary to inhibit mTORC1 activity in liver
Nikonorova, I. A., Mirek, E. T., Signore, C. C., Goudie, M. P., Wek, R. C., & Anthony, T. G. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra117.001625 · Cited by 52
Chronic oxycodone induces axonal degeneration in rat brain
Fan, R., Schrott, L. M., Arnold, T., Snelling, S., Rao, M., Graham, D. D., Cornelius, A. P., & Korneeva, N. L. (2018) · BMC Neuroscience · doi:10.1186/s12868-018-0417-0 · Cited by 50
Comparison of base-line and chemical-induced transcriptomic responses in HepaRG and RPTEC/TERT1 cells using TempO-Seq
Limonciel, A., Ates, G., Carta, G., Wilmes, A., Watzele, M., Shepard, P. J., VanSteenhouse, H. C., Seligmann, B. E., Yeakley, J. M., van de Water, B., et al. (2018) · Archives of Toxicology · doi:10.1007/s00204-018-2256-2 · Cited by 49
NADPH oxidase activity is required for ER stress survival in plants
Angelos, E. R., & Brandizzí, F. (2018) · The Plant Journal · doi:10.1111/tpj.14091 · Cited by 49
Adaptive translational pausing is a hallmark of the cellular response to severe environmental stress
Jobava, R., Mao, Y., Guan, B., Hu, D., Krokowski, D., Chen, C.-W., Shu, X. E., Chukwurah, E., Wu, J., Gao, Z., et al. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.09.029 · Cited by 49
Self-citation
ATF 4 mediates necrosis induced by glucose deprivation and apoptosis induced by 2‐deoxyglucose in the same cells
León‐Annicchiarico, C. L., Ramírez‐Peinado, S., Domínguez‐Villanueva, D., Gonsberg, A., Lampidis, T. J., & Muñoz‐Pinedo, C. (2015) · FEBS Journal · doi:10.1111/febs.13369 · Cited by 51
Phosphorylation of eIF2α Is Dispensable for Differentiation but Required at a Posttranscriptional Level for Paneth Cell Function and Intestinal Homeostasis in Mice
Cao, S. S., Wang, M., Harrington, J. C., Chuang, B., Eckmann, L., & Kaufman, R. J. (2014) · Inflammatory Bowel Diseases · doi:10.1097/mib.0000000000000010 · Cited by 48
Self-citation
Tunicamycin-induced endoplasmic reticulum stress reduces in vitro subpopulation and invasion of CD44+/CD24- phenotype breast cancer stem cells
Nami, B., Dönmez, H., & Koçak, N. (2016) · Experimental and Toxicologic Pathology · doi:10.1016/j.etp.2016.06.004 · Cited by 48
Endoplasmic reticulum stress induces autophagy and apoptosis while inhibiting proliferation and drug resistance in multiple myeloma through the PI3K/Akt/mTOR signaling pathway
Fu, Y., Liu, X., Gao, M. Q., Zhang, Y., & Liu, J. (2017) · Oncotarget · doi:10.18632/oncotarget.17862 · Cited by 48
Bavachin Induces Apoptosis through Mitochondrial Regulated ER Stress Pathway in HepG2 Cells
Yang, Y. C., Tang, X., Hao, F., Ma, Z.-C., Wang, Y., Wang, L., & Gao, Y. (2017) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.b17-00672 · Cited by 48
Targeting of cathepsin C induces autophagic dysregulation that directs ER stress mediated cellular cytotoxicity in colorectal cancer cells
Khaket, T. P., Singh, M. P., Khan, I., Bhardwaj, M., & Kang, S. C. (2018) · Cellular Signalling · doi:10.1016/j.cellsig.2018.02.017 · Cited by 48
Small molecule modulator of protein disulfide isomerase attenuates mutant huntingtin toxicity and inhibits endoplasmic reticulum stress in a mouse model of Huntington’s disease
Zhou, X., Li, G., Kaplan, A. R., Gaschler, M. M., Zhang, X., Hou, Z., Jiang, M., Piantedosi, R., Cremers, S., Stockwell, B. R., et al. (2018) · Human Molecular Genetics · doi:10.1093/hmg/ddy061 · Cited by 48
Discovery of a Redox Thiol Switch: Implications for Cellular Energy Metabolism
Gao, X., Li, L., Parisien, M., Mcleod, M., Wu, J., Bederman, I., Gao, Z., Krokowski, D., Abbott, D. W., Diatchenko, L., et al. (2020) · Molecular & Cellular Proteomics · doi:10.1074/mcp.ra119.001910 · Cited by 50
Self-citation
Recent advances and future directions in targeting the secretory apparatus in multiple myeloma
Auner, H. W., & Cenci, S. (2014) · British Journal of Haematology · doi:10.1111/bjh.13172 · Cited by 49
Mitochondrial Quality Control in Age-Related Pulmonary Fibrosis
Roque, W., Cuevas-Mora, K., & Romero, F. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21020643 · Cited by 47
PERK prevents hepatic lipotoxicity by activating the p62-ULK1 axis-mediated noncanonical KEAP1-Nrf2 pathway
Lee, D. H., Park, J. S., Lee, Y. S., & Bae, S. H. (2022) · Redox Biology · doi:10.1016/j.redox.2022.102235 · Cited by 47
Translational Upregulation of an Individual p21Cip1 Transcript Variant by GCN2 Regulates Cell Proliferation and Survival under Nutrient Stress
Lehman, S. L., Cerniglia, G. J., Johannes, G. J., Ye, J., Ryeom, S. W., & Koumenis, C. (2015) · PLoS Genetics · doi:10.1371/journal.pgen.1005212 · Cited by 50
LCZ696 Protects against Diabetic Cardiomyopathy-Induced Myocardial Inflammation, ER Stress, and Apoptosis through Inhibiting AGEs/NF-κB and PERK/CHOP Signaling Pathways
Belali, O. M., Ahmed, M. M., Mohany, M., Belali, T. M., Alotaibi, M. M., Alhoshani, A., & Al-Rejaie, S. S. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23031288 · Cited by 46
Harnessing Hyperthermia: Molecular, Cellular, and Immunological Insights for Enhanced Anticancer Therapies
Lukácsi, S., Munkácsy, G., & Győrffy, B. (2024) · Integrative Cancer Therapies · doi:10.1177/15347354241242094 · Cited by 48
Proline Biosynthesis Is Required for Endoplasmic Reticulum Stress Tolerance in Saccharomyces cerevisiae
Liang, X., Dickman, M. B., & Becker, D. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.562827 · Cited by 46
CCAAT/Enhancer-Binding Protein Homologous (CHOP) Protein Promotes Carcinogenesis in the DEN-Induced Hepatocellular Carcinoma Model
Scaiewicz, V., Nahmias, A., Chung, R. T., Mueller, T., Tirosh, B., & Shibolet, O. (2013) · PLoS ONE · doi:10.1371/journal.pone.0081065 · Cited by 46
Complementary Roles of GADD34- and CReP-Containing Eukaryotic Initiation Factor 2α Phosphatases during the Unfolded Protein Response
Reid, D. W., Tay, A. S. L., Sundaram, J. R., Lee, I. C. J., Chen, Q., George, S. E., Nicchitta, C. V., & Shenolikar, S. (2016) · Molecular and Cellular Biology · doi:10.1128/mcb.00190-16 · Cited by 52
Dysregulation of mRNA translation and energy metabolism in cancer
Leibovitch, M., & Topisirović, I. (2017) · Advances in Biological Regulation · doi:10.1016/j.jbior.2017.11.001 · Cited by 46
Translational Regulation of Cancer Metastasis
Micalizzi, D. S., Ebright, R. Y., Haber, D. A., & Maheswaran, S. (2021) · Cancer Research · doi:10.1158/0008-5472.can-20-2720 · Cited by 47
Lipid-induced endoplasmic reticulum stress in X-linked adrenoleukodystrophy
van de Beek, M.-C., Ofman, R., Dijkstra, I. M. E., Wijburg, F. A., Engelen, M., Wanders, R. J. A., & Kemp, S. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2017.06.003 · Cited by 48
Induction of early growth response gene 1 (EGR1) by endoplasmic reticulum stress is mediated by the extracellular regulated kinase (ERK) arm of the MAPK pathways
Shan, J., Dudenhausen, E. E., & Kilberg, M. S. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2018.09.009 · Cited by 45
Self-citation

Authors: Han, J., Back, S. H., Hur, J., Lin, Y.-H., Gildersleeve, R., Shan, J., Yuan, C. L., Krokowski, D., Wang, S., Hatzoglou, M., Kilberg, M. S., Sartor, M. A., & Kaufman, R. J.
Affiliations: Sanford Burnham Prebys Medical Discovery Institute (US)
University of Michigan (US)
University of Florida (US)
Case Western Reserve University (US)
Corresponding author: Kaufman, Randal J.
ORCID: Han, Jaeseok
Back, Sung Hoon
Hur, Junguk
Lin, Yu-Hsuan
Shan, Jixiu
Krokowski, Dawid
Wang, Shiyu
Hatzoglou, Maria
Sartor, Maureen A.
Kaufman, Randal J.
Venue: Nature Cell Biology
Publisher: Springer Science and Business Media LLC
Published: 2013-04-28
Volume: 15
Issue: 5
Pages: 481-490
ISSN: 1465-7392 (ISSN-L)
1476-4679
DOI: 10.1038/ncb2738
PMC: PMC3692270
OpenAlex: W2074471441
Cited by: 1,691
References: 66
Citations by year: 2026: 102 · 2025: 136 · 2024: 140 · 2023: 136 · 2022: 153 · 2021: 136 · 2020: 153 · 2019: 123 · 2018: 127 · 2017: 118 · 2016: 117 · 2015: 112 · 2014: 102 · 2013: 30
FWCI: 70.01
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.springer.com/tdm (tdm)
Locations: Nature Cell Biology (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
Funders: University of Michigan
National Heart, Lung, and Blood Institute (R01HL052173, HL 057346, P01HL057346, HL052173)
National Institute of Diabetes and Digestive and Kidney Diseases (R01DK088227, R01DK042394, R24DK093074, DK-042394, R01DK094729, DK092062, DK53307, DK088227, DK-094729, R01DK053307, DK60596, DK093074, R37DK060596, R01DK092062, R37DK042394, R01DK060596)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
Life Sciences › Neuroscience › Sensory Systems › Ion Channels and Receptors
Keywords: endoplasmic reticulum stress, unfolded protein response, ATF4, CHOP, eIF2α phosphorylation, protein synthesis, oxidative stress, ATP depletion, cell death, transcriptional regulation, protein misfolding, apoptosis
MeSH terms: Adenosine Triphosphate, Animals, Binding Sites, Cell Survival, Gene Expression Regulation, Phosphorylation, Promoter Regions, Genetic, Protein Binding, RNA, Messenger, Transcription, Genetic, Protein Biosynthesis, Eukaryotic Initiation Factor-2, Cell Death, Reactive Oxygen Species, Protein Folding, Protein Interaction Mapping, Chromatin Immunoprecipitation, Mice, Activating Transcription Factor 4, Transcription Factor CHOP, Unfolded Protein Response, Endoplasmic Reticulum Stress

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

ER-stress-induced transcriptional regulation increases protein synthesis leading to cell death

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks