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ER-stress-induced transcriptional regulation increases protein synthesis leading to cell death
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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.
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“Prolonged or extreme ER stress, leading to an overload of the repair and degradation machineries, triggers cellular apoptosis (Han et al, 2013; Sano & Reed, 2013).”
From Differential dynamics of the mammalian mRNA and protein expression response to misfolding stress (2016) · cites this paper as Han et al, 2013
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Cites
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
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
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
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
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Dong, R., Qin, C., Yin, Y., Han, L., Xiao, C., Wang, K., Wei, R., Xia, Y., & Kong, L. (2023) · British Journal of Pharmacology · doi:10.1111/bph.16165 · Cited by 37
Zhang, W., Liu, Y., Li, T.-T., Piao, C., Liu, O., Liu, J., Qi, Y., Jia, L., & Du, J. (2016) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2016.08.008 · Cited by 37
Unfolded Protein Response of the Endoplasmic Reticulum in Tumor Progression and Immunogenicity
Yoo, Y.-S., Han, H. G., & Jeon, Y. J. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/2969271 · Cited by 37
Xie, Q., Gao, S., Lei, M., & Li, Z. (2022) · Aging · doi:10.18632/aging.203817 · Cited by 36
The PPP1R15 Family of eIF2-alpha Phosphatase Targeting Subunits (GADD34 and CReP)
Hicks, D., Giresh, K., Wrischnik, L. A., & Weiser, D. C. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242417321 · Cited by 41
Transcriptional regulation of secretory capacity by bZip transcription factors
Fox, R. M., & Andrew, D. J. (2014) · Frontiers in Biology · doi:10.1007/s11515-014-1338-7 · Cited by 36
Zhang, L., Hapon, M. B., Goyeneche, A. A., Srinivasan, R., Gamarra-Luques, C. D., Callegari, E. A., Drappeau, D. D., Terpstra, E. J. M., Pan, B., Knapp, J. R., et al. (2016) · Molecular Oncology · doi:10.1016/j.molonc.2016.05.001 · Cited by 36
Combined chemical–genetic approach identifies cytosolic HSP70 dependence in rhabdomyosarcoma
Sabnis, A. J., Guerriero, C. J., Olivas, V. R., Sayana, A., Shue, J., Flanagan, J., Asthana, S., Paton, A. W., Paton, J. C., Gestwicki, J. E., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1603883113 · Cited by 36
Bergmann, T. J., & Molinari, M. (2018) · Biology of the Cell · doi:10.1111/boc.201800029 · Cited by 36
Kim, C.-S., Joe, Y., Choi, H., Back, S. H., Park, J. W., Chung, H., Roh, E., Kim, M., Ha, T. Y., & Yu, R. (2019) · Journal of Inflammation · doi:10.1186/s12950-019-0221-3 · Cited by 36
Self-citationGonen, N., Meller, A., Sabath, N., & Shalgi, R. (2019) · iScience · doi:10.1016/j.isci.2019.07.022 · Cited by 36
Johnston, B. P., Pringle, E. S., & McCormick, C. (2019) · PLoS Pathogens · doi:10.1371/journal.ppat.1008185 · Cited by 36
Lebeaupin, C., Yong, J., & Kaufman, R. J. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-40204-4_8 · Cited by 38
Self-citationUnfolded Protein Response in Leukemia: From Basic Understanding to Therapeutic Opportunities
Khateb, A., & Ronai, Z. A. (2020) · Trends in cancer · doi:10.1016/j.trecan.2020.05.012 · Cited by 38
Mughees, M., Wajid, S., & Samim, M. (2020) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2020.119583 · Cited by 36
Li, Y., Zhang, J., Zhou, K., Xie, L., Xiang, G., Fang, M., Han, W., Wang, X., & Xiao, J. (2020) · Cell Biology and Toxicology · doi:10.1007/s10565-020-09550-4 · Cited by 36
Peeri, H., Shalev, N., Vinayaka, A. C., Nizar, R., Kazimirsky, G., Namdar, D., Anil, S. M., Belausov, E., Brodie, C., & Koltai, H. (2021) · Cancers · doi:10.3390/cancers13071720 · Cited by 36
Qiao, L., Shao, X., Gao, S.-J., Ming, Z., Fu, X., & Wei, Q. (2021) · Colloids and Surfaces B Biointerfaces · doi:10.1016/j.colsurfb.2021.112046 · Cited by 37
Rodrigues, B. L., Dotti, I., Pascoal, L. B., Morari, J., Esteller, M., Coope, A., Ayrizono, M. D. L. S., Salas, A., & Leal, R. F. (2022) · Mediators of Inflammation · doi:10.1155/2022/6049500 · Cited by 36
Márton, M., Bánhegyi, G., Gyöngyösi, N., Kálmán, E. É., Pettkó‐Szandtner, A., Káldi, K., & Kapuy, O. (2022) · FEBS Open Bio · doi:10.1002/2211-5463.13484 · Cited by 36
Enhancement of the Acrolein-Induced Production of Reactive Oxygen Species and Lung Injury by GADD34
Sun, Y., Ito, S., Nishio, N., Tanaka, Y., Chen, N., Liu, L., & Isobe, K. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2015/170309 · Cited by 36
Induction of miR-3648 Upon ER Stress and Its Regulatory Role in Cell Proliferation
Rashid, F., Awan, H. M., Shah, A., Chen, L., & Shan, G. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18071375 · Cited by 36
Evstafieva, A. G., Kovaleva, I. E., Shoshinova, M. S., Budanov, A. V., & Chumakov, P. M. (2018) · PLoS ONE · doi:10.1371/journal.pone.0191107 · Cited by 36
Couasnay, G., Bon, N., Devignes, C.-S., Sourice, S., Bianchi, A., Véziers, J., Weiss, P., Elefteriou, F., Provot, S., Guicheux, J., et al. (2018) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.3609 · Cited by 36
Vetters, J., van Helden, M. J. G., Wahlen, S., Tavernier, S. J., Martens, A., Fayazpour, F., Vergote, K., Vanheerswynghels, M., Deswarte, K., Moorleghem, J. V., et al. (2019) · The Journal of Experimental Medicine · doi:10.1084/jem.20182164 · Cited by 38
Fan, H., Xu, Z., Yao, K., Zheng, B., Zhang, Y., Wang, X., Zhang, T., Li, X., Hu, H., Yue, B., et al. (2023) · Cancer Research · doi:10.1158/0008-5472.can-23-1443 · Cited by 40
Exploring paraptosis as a therapeutic approach in cancer treatment
Chang, L., Chiang, S.-K., Chen, S., & Hung, M. (2024) · Journal of Biomedical Science · doi:10.1186/s12929-024-01089-4 · Cited by 36
Unfolded Protein Response Pathways in Neurodegenerative Diseases
Shah, S. Z. A., Zhao, D., Khan, S. H., & Yang, L. (2015) · Journal of Molecular Neuroscience · doi:10.1007/s12031-015-0633-3 · Cited by 35
Gene therapy to target ER stress in brain diseases
Valenzuela, V., Martínez, G., Duran-Aniotz, C. A., & Hetz, C. A. (2016) · Brain Research · doi:10.1016/j.brainres.2016.04.064 · Cited by 36
Eigner, K., Filik, Y., Mark, F., Schütz, B., Klambauer, G., Moriggl, R., Hengstschläger, M., Stangl, H., Mikula, M., & Röhrl, C. (2017) · Scientific Reports · doi:10.1038/s41598-017-17888-9 · Cited by 35
D’Abrosca, B., Ciaramella, V., Graziani, V., Papaccio, F., Corte, C. M. D., Potenza, N., Fiorentino, A., Ciardiello, F., & Morgillo, F. (2019) · Scientific Reports · doi:10.1038/s41598-019-41372-1 · Cited by 35
Dash, S., Aydın, Y., & Wu, T. (2019) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2019.07.015 · Cited by 36
Wu, Y., Li, Z., Zhang, X., & Liu, H. (2019) · World Journal of Gastroenterology · doi:10.3748/wjg.v25.i41.6205 · Cited by 35
Lorenz, N. I., Sittig, A. C. M., Urban, H., Luger, A., Engel, A. L., Münch, C., Steinbach, J. P., & Ronellenfitsch, M. W. (2021) · Scientific Reports · doi:10.1038/s41598-021-93663-1 · Cited by 35
GCN2 adapts protein synthesis to scavenging-dependent growth
Nofal, M., Wang, T., Yang, L., Jankowski, C. S. R., Li, H., Han, S., Parsons, L. R., Frese, A. N., Gitai, Z., Anthony, T. G., et al. (2021) · Cell Systems · doi:10.1016/j.cels.2021.09.014 · Cited by 38
Protein Aggregation in the ER: Calm behind the Storm
Li, H., & Sun, S. (2021) · Cells · doi:10.3390/cells10123337 · Cited by 36
Nutrient Regulation of Pancreatic Islet β-Cell Secretory Capacity and Insulin Production
Rohli, K. E., Boyer, C. K., Blom, S. E., & Stephens, S. B. (2022) · Biomolecules · doi:10.3390/biom12020335 · Cited by 36
Protein quality control and aggregation in the endoplasmic reticulum: From basic to bedside
Chen, G., Wei, T., Ju, F., & Li, H. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1156152 · Cited by 36
Hinton, A. O., Jr., Katti, P., Mungai, M., Hall, D. D., Koval, O. M., Shao, J., Vue, Z., Lopez, E. G., Rostami, R., Neikirk, K., et al. (2024) · Journal of Cellular Physiology · doi:10.1002/jcp.31204 · Cited by 38
Borrelidin Induces the Unfolded Protein Response in Oral Cancer Cells and Chop-Dependent Apoptosis
Sidhu, A., Miller, J. R., Tripathi, A., Garshott, D. M., Brownell, A. L., Chiego, D. J., Arewång, C.-J., Zeng, Q., Jackson, L. C., Bechler, S. A., et al. (2015) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.5b00133 · Cited by 34
Self-citationSieber, J., Hauer, C., Bhuvanagiri, M., Leicht, S., Krijgsveld, J., Neu‐Yilik, G., Hentze, M. W., & Kulozik, A. E. (2016) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m115.054056 · Cited by 36
To, M., Peterson, C. W. H., Roberts, M. A., Counihan, J. L., Wu, T., Forster, M. S., Nomura, D. K., & Olzmann, J. A. (2016) · Molecular Biology of the Cell · doi:10.1091/mbc.e16-07-0483 · Cited by 34
Wu, X., Luo, J., Liu, H., Cui, W., Guo, W., Zhao, L., Guo, H., Bai, H., Guo, K., Feng, D., et al. (2020) · Cell Proliferation · doi:10.1111/cpr.12759 · Cited by 34
Effects of fatty acids on inducing endoplasmic reticulum stress in bovine mammary epithelial cells
Sharmin, M. M., Mizusawa, M., Hayashi, S., Arai, W., Sakata, S., & Yonekura, S. (2020) · Journal of Dairy Science · doi:10.3168/jds.2019-18080 · Cited by 34
Kim, T. J., Pyun, D. H., Kim, M. J., Jeong, J. H., El‐Aty, A. M. A., & Jung, T. W. (2021) · Journal of Ginseng Research · doi:10.1016/j.jgr.2021.09.002 · Cited by 34
Hijacking Cellular Stress Responses to Promote Lifespan
Dutta, N., Garcia, G., & Higuchi‐Sanabria, R. (2022) · Frontiers in Aging · doi:10.3389/fragi.2022.860404 · Cited by 35
Endoplasmic reticulum stress in melanoma pathogenesis and resistance
Kong, Y., Jiang, J. L., Huang, Y., Li, L., Liu, X., Jin, Z., Wei, F., Liu, X., Zhang, S., Duan, X., et al. (2022) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.113741 · Cited by 35
Wu, Y. H., Fan, X., Chen, S., Deng, L., Jiang, L., Yang, S., & Dong, Z. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms24010544 · Cited by 34
ER stress in temozolomide-treated glioblastomas interferes with DNA repair and induces apoptosis
Weatherbee, J. L., Kraus, J., & Ross, A. H. (2016) · Oncotarget · doi:10.18632/oncotarget.9907 · Cited by 34
Polo, M., Alegre, F., Moragrega, Á. B., Gibellini, L., Martí-Rodrigo, A., Blas‐García, A., Esplugues, J. V., & Apostolova, N. (2017) · British Journal of Pharmacology · doi:10.1111/bph.14045 · Cited by 35
ATF5 is a regulator of exercise-induced mitochondrial quality control in skeletal muscle
Slavin, M. B., Kumari, R., & Hood, D. A. (2022) · Molecular Metabolism · doi:10.1016/j.molmet.2022.101623 · Cited by 33
Louisse, J., Fragki, S., Rijkers, D., Janssen, A. W. F., van Dijk, B., Leenders, L., Staats, M., Bokkers, B. G. H., Zeilmaker, M. J., Piersma, A. H., et al. (2023) · Archives of Toxicology · doi:10.1007/s00204-023-03450-2 · Cited by 33
Manuel, A. M., Walla, M. D., Faccenda, A., Martin, S. L., Tanis, R. M., Piroli, G. G., Adam, J., Kantor, B., Mutus, B., Townsend, D. M., et al. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2016.6853 · Cited by 33
Miller, M., Mellul, A., Braun, M., Sherill-Rofe, D., Cohen, E., Shpilt, Z., Unterman, I., Braitbard, O., Hochman, J., Tshuva, E. Y., et al. (2020) · iScience · doi:10.1016/j.isci.2020.101262 · Cited by 33
Translation Inhibitors Activate Autophagy Master Regulators TFEB and TFE3
Dang, T. T., & Back, S. H. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222112083 · Cited by 33
Self-citationDi, S., Fan, C., Yang, Y., Jiang, S., Liang, M., Wu, G., Wang, B., Xin, Z., Hu, W., Zhu, Y., et al. (2015) · APOPTOSIS · doi:10.1007/s10495-015-1142-0 · Cited by 33
Deivasigamani, S., Verma, H., Ueda, R., Ratnaparkhi, A., & Ratnaparkhi, G. S. (2014) · Biology Open · doi:10.1242/bio.201410066 · Cited by 33
Su, H., Waldron, R. T., Gong, R., Ramanujan, V. K., Pandol, S. J., & Lugea, A. (2016) · PLoS ONE · doi:10.1371/journal.pone.0148999 · Cited by 33
Yonekura, S., Tsuchiya, M., Tokutake, Y., Mizusawa, M., Nakano, M., Miyaji, M., Ishizaki, H., & Haga, S. (2018) · Journal of Dairy Science · doi:10.3168/jds.2017-13718 · Cited by 33
The mevalonate pathway is an actionable vulnerability of t(4;14)-positive multiple myeloma
Longo, J., Smirnov, P., Li, Z., Branchard, E., van Leeuwen, J. E., Licht, J. D., Haibe‐Kains, B., Andrews, D. W., Keats, J. J., Pugh, T. J., et al. (2020) · Leukemia · doi:10.1038/s41375-020-0962-2 · Cited by 33
Xing, Y., & Liu, C. (2025) · Cell Death Discovery · doi:10.1038/s41420-025-02683-7 · Cited by 32
Ulbrich, L., Favaloro, F. L., Trobiani, L., Marchetti, V., Patel, V., Pascucci, T., Comoletti, D., Marciniak, S. J., & Jaco, A. D. (2015) · Biochemical Journal · doi:10.1042/bj20150274 · Cited by 33
Mays, C. E., & Soto, C. A. (2016) · Brain Research · doi:10.1016/j.brainres.2016.04.009 · Cited by 32
Li, X., Yu, X., Zhou, D., Chen, B., Li, W., Zheng, X., Zeng, H., Long, L., & Zhou, W. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.00737 · Cited by 32
Song, Y., Liu, L., Liu, B., Liu, R., Chen, Y., Li, C., Liu, G., Song, Z., Lu, C. C., Lü, A., et al. (2021) · Pharmacological Research · doi:10.1016/j.phrs.2020.105371 · Cited by 32
Alsterda, A. J., Asha, K., Powrozek, O., Repak, M., Goswami, S., Dunn, A. M., Memmel, H. C., & Sharma-Walia, N. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.654940 · Cited by 32
SLFN5 Regulates LAT1-Mediated mTOR Activation in Castration-Resistant Prostate Cancer
Martinez, R. S., Salji, M. J., Rushworth, L. K., Ntala, C., Blanco, G. R., Hedley, A., Clark, W. A., Peixoto, P., Hervouet, É., Renaude, E., et al. (2021) · Cancer Research · doi:10.1158/0008-5472.can-20-3694 · Cited by 32
Karunakaran, U., Elumalai, S., Moon, J. S., & Won, K. C. (2021) · Redox Biology · doi:10.1016/j.redox.2021.102029 · Cited by 32
He, T., Wang, Q., Ao, J., Chen, K., Li, X., Zhang, J., & Duan, C. (2022) · Food and Chemical Toxicology · doi:10.1016/j.fct.2022.112986 · Cited by 32
Chen, M., Zhang, R., Chen, Y., Chen, X., Li, Y., Shen, J., Yuan, M., Chen, Y., Wu, J., & Sun, Q. (2023) · Phytomedicine · doi:10.1016/j.phymed.2023.154902 · Cited by 32
Immunomodulatory and Antioxidant Drugs in Glaucoma Treatment
Buonfiglio, F., Pfeiffer, N., & Gericke, A. (2023) · Pharmaceuticals · doi:10.3390/ph16091193 · Cited by 32
Lehman, S. L., Ryeom, S. W., & Koumenis, C. (2015) · Scientific Reports · doi:10.1038/srep11781 · Cited by 32
Rajesh, K., Krishnamoorthy, J., Gupta, J., Kazimierczak, U., Papadakis, A. I., Deng, Z., Wang, S., Kuninaka, S., & Koromilas, A. E. (2016) · Oncotarget · doi:10.18632/oncotarget.10480 · Cited by 33
Self-citationRahman, S., Ayyagari, A., Jan, A. T., & Minakshi, R. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00030 · Cited by 33
Masciarelli, S., Capuano, E., Ottone, T., Divona, M., Lavorgna, S., Liccardo, F., Śniegocka, M., Travaglini, S., Noguera, N. I., Picardi, A., et al. (2019) · Blood Advances · doi:10.1182/bloodadvances.2019000540 · Cited by 32
Chen, W., Liu, P., Liu, D., Huang, H., Feng, X., Fang, F., Li, L., Wu, J., Liu, L., Solow-Cordero, D. E., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-34682-y · Cited by 32
Wu, S., Wang, B., Li, H., Wang, H., Du, S., Huang, X., Fan, Y., Gao, Y., Gu, L., Huang, Q., et al. (2024) · Oncogene · doi:10.1038/s41388-024-03013-4 · Cited by 32
RetractedGani, A. R., Uppala, J. K., & Ramaiah, K. V. A. (2015) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2014.12.031 · Cited by 34
Wang, Y.-Z., Zhou, D., Phung, S., Warden, C., Rashid, R., Chan, N., & Chen, S. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1612991114 · Cited by 31
Anzmann, A. F., Pinto, S. M., Busa, V. F., Carlson, J., McRitchie, S., Sumner, S., Pandey, A., & Vernon, H. J. (2019) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2019.165538 · Cited by 31
Mo, C., Lu, L., Liu, D., & Wei, K. (2020) · Journal of Nanobiotechnology · doi:10.1186/s12951-020-00608-3 · Cited by 31
The Amino Acid Sensor Eif2ak4/GCN2 Is Required for Proliferation of Osteoblast Progenitors in Mice
Hu, G., Yu, Y., Tang, Y. J., Wu, C., Long, F., & Karner, C. M. (2020) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.4091 · Cited by 31
Mutations in COMP cause familial carpal tunnel syndrome
Li, C., Wang, N., Schäffer, A. A., Liu, X., Zhao, Z., Elliott, G., Garrett, L. J., Choi, N. T., Wang, Y., Wang, Y., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-17378-z · Cited by 31
Inhibition of ERAD synergizes with FTS to eradicate pancreatic cancer cells
Du, R., Sullivan, D. K., Azizian, N. G., Liu, Y., & Li, Y. (2021) · BMC Cancer · doi:10.1186/s12885-021-07967-6 · Cited by 31
The integrated stress response as a key pathway downstream of mitochondrial dysfunction
Bilen, M., Benhammouda, S., Slack, R. S., & Germain, M. (2022) · Current Opinion in Physiology · doi:10.1016/j.cophys.2022.100555 · Cited by 38
Neuron‐specific translational control shift ensures proteostatic resilience during ER stress
Wolzak, K., Nölle, A., Farina, M., Abbink, T. E. M., van der Knaap, M. S., Verhage, M., & Scheper, W. (2022) · The EMBO Journal · doi:10.15252/embj.2021110501 · Cited by 31
Stress-Mediated Attenuation of Translation Undermines T-cell Activity in Cancer
Riesenberg, B., Hunt, E. G., Tennant, M. D., Hurst, K. E., Andrews, A. M., Leddy, L. R., Neskey, D. M., Hill, E. G., Rivera, G. O. R., Paulos, C. M., et al. (2022) · Cancer Research · doi:10.1158/0008-5472.can-22-1744 · Cited by 30
ER stress and calcium-dependent arrhythmias
Hamilton, S., & Terentyev, D. A. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.1041940 · Cited by 31
Andrysík, Z., Sullivan, K. D., Kieft, J. S., & Espinosa, J. M. (2022) · Nature Communications · doi:10.1038/s41467-022-35089-5 · Cited by 31
Parzych, K., Chinn, T. M., Chen, Z., Loaiza, S., Porsch, F., Valbuena, G. N., Kleijnen, M. F., Karadimitris, A., Gentleman, E., Keun, H. C., et al. (2015) · Cell Death and Disease · doi:10.1038/cddis.2015.373 · Cited by 31
Vandewynckel, Y., Laukens, D., Devisscher, L., Bogaerts, E., Paridaens, A., den Bussche, A. V., Raevens, S., Verhelst, X., Steenkiste, C. V., Jonckx, B., et al. (2016) · BMC Cancer · doi:10.1186/s12885-015-1990-6 · Cited by 31
Bashyal, B. P., Wijeratne, E. M. K., Tillotson, J., Arnold, A. E., Chapman, E., & Gunatilaka, A. A. L. (2017) · Journal of Natural Products · doi:10.1021/acs.jnatprod.6b00960 · Cited by 31
Danilova, T., & Lindahl, M. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.01457 · Cited by 32
Zhang, M., Gao, Y., Zhao, W., Yu, G., & Jin, F. (2018) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00163.2018 · Cited by 31
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Virgolini, M. J., Feliziani, C., Cambiasso, M. J., López, P. H. H., & Bollo, M. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2018.10.014 · Cited by 31
Nguyen, C., Malchow, S., Reich, S., Steltgens, S., Shuvaev, K. V., Loroch, S., Lorenz, C., Sickmann, A., Knobbe-Thomsen, C. B., Tews, B., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-45237-5 · Cited by 32
Matsumura, T., Nakamura‐Ishizu, A., Muddineni, S. S. N. A., Tan, D. Q., Wang, C. Q., Tokunaga, K., Tirado-Magallanes, R., Sian, S., Benoukraf, T., Okuda, T., et al. (2020) · Blood · doi:10.1182/blood.2019004292 · Cited by 31
Recent progress of endoplasmic reticulum stress in the mechanism of atherosclerosis
Ni, L., Yang, L., & Lin, Y. (2024) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2024.1413441 · Cited by 32
Self-citationCruz, P. G., Fribley, A. M., Miller, J. R., Larsen, M. J., Schultz, P. J., Jacob, R. T., Tamayo‐Castillo, G., Kaufman, R. J., & Sherman, D. H. (2015) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.5b00127 · Cited by 30
Self-citationSimultaneous activation and inhibition of autophagy sensitizes cancer cells to chemotherapy
Chi, K.-H., Wang, Y., Huang, Y.-C., Chiang, H.-C., Chi, M., Chi, C., Wang, H.-E., & Kao, S.-J. (2016) · Oncotarget · doi:10.18632/oncotarget.10873 · Cited by 30
Metadata
- 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
- Venue
- Nature Cell Biology
- Published
- 2013-04-28
- Volume
- 15
- Issue
- 5
- Pages
- 481-490
- ISSN
- 1465-7392 (ISSN-L)
- 1476-4679
- 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
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