Mediators of endoplasmic reticulum stress-induced apoptosis
Open accessAbstract
The efficient functioning of the endoplasmic reticulum (ER) is essential for most cellular activities and survival. Conditions that interfere with ER function lead to the accumulation and aggregation of unfolded proteins. ER transmembrane receptors detect the onset of ER stress and initiate the unfolded protein response (UPR) to restore normal ER function. If the stress is prolonged, or the adaptive response fails, apoptotic cell death ensues. Many studies have focused on how this failure initiates apoptosis, as ER stress-induced apoptosis is implicated in the pathophysiology of several neurodegenerative and cardiovascular diseases. In this review, we examine the role of the molecules that are activated during the UPR in order to identify the molecular switch from the adaptive phase to apoptosis. We discuss how the activation of these molecules leads to the commitment of death and the mechanisms that are responsible for the final demise of the cell.
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
Cites
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?
Alterations of ER redox state may influence the cell death machinery by inducing caspase-dependent apoptosis through the down-regulation of Bcl-2 protein, which physiologically blocks apoptotic cell death.
“Alterations of ER redox state may also influence the cell death machinery by inducing caspase-dependent apoptosis through the down-regulation of Bcl-2 protein, which physiologically blocks the apoptotic cell death [52]”
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
1 retracted
Proapoptotic BAX and BAK Modulate the Unfolded Protein Response by a Direct Interaction with IRE1α
Hetz, C. A., Bernasconi, P., Fisher, J. K., Lee, A., Bassik, M. C., Antonsson, B. E., Brandt, G. S., Iwakoshi, N. N., Schinzel, A. C., Glimcher, L. H., et al. (2006) · Science · doi:10.1126/science.1123480 · Cited by 666 · see citing works
RetractedControl of inositol 1,4,5-trisphosphate-induced Ca2+ release by cytosolic Ca2+
Bootman, M. D., Missiaen, L., Parys, J. B., SMEDT, H. D., & Casteels, R. (1995) · Biochemical Journal · doi:10.1042/bj3060445 · Cited by 5,120 · see citing works
Signal transduction by the JNK group of MAP kinases
Davis, R. J. (2000) · Cell · doi:10.1016/s0092-8674(00)00116-1 · Cited by 4,237 · see citing works
Yoshida, H., Matsui, T., Yamamoto, A., Okada, T., & Mori, K. (2001) · Cell · doi:10.1016/s0092-8674(01)00611-0 · Cited by 4,054 · see citing works
Proapoptotic BAX and BAK: A Requisite Gateway to Mitochondrial Dysfunction and Death
Wei, M. C., Zong, W.-X., Cheng, E. H.-Y., Lindsten, T., Panoutsakopoulou, V., Ross, A. J., Roth, K. A., MacGregor, G. R., Thompson, C. B., & Korsmeyer, S. J. (2001) · Science · doi:10.1126/science.1059108 · Cited by 3,988 · see citing works
Mutation of the mouse klotho gene leads to a syndrome resembling ageing
Kuro-o, M., Matsumura, Y., Aizawa, H., Kawaguchi, H., Suga, T., Utsugi, T., Ohyama, Y., Kurabayashi, M., Kaname, T., Kume, E., et al. (1997) · Nature · doi:10.1038/36285 · Cited by 3,837 · see citing works
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 · see citing works
Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-β
Nakagawa, T., Zhu, H., Morishima, N., Li, E., Xu, J., Yankner, B. A., & Yuan, J. (2000) · Nature · doi:10.1038/47513 · Cited by 3,262 · see citing works
THE MAMMALIAN UNFOLDED PROTEIN RESPONSE
Schröder, M., & Kaufman, R. J. (2005) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.011303.074134 · Cited by 3,035 · see citing works
Urano, F., Wang, X.-Z., Bertolotti, A., Zhang, Y., Chung, P., Harding, H. P., & Ron, D. (2000) · Science · doi:10.1126/science.287.5453.664 · Cited by 2,997 · see citing works
Lee, A., Iwakoshi, N. N., & Glimcher, L. H. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.21.7448-7459.2003 · Cited by 2,041 · see citing works
Harding, H. P., Zhang, Y., Bertolotti, A., Zeng, H., & Ron, D. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)80330-5 · Cited by 2,021 · see citing works
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 2,004 · see citing works
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 1,996 · see citing works
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 1,895 · see citing works
A Selective Inhibitor of eIF2α Dephosphorylation Protects Cells from ER Stress
Boyce, M., Bryant, K. F., Jousse, C., Long, K., Harding, H. P., Scheuner, D. L., Kaufman, R. J., Ma, D., Coen, D. M., Ron, D., et al. (2005) · Science · doi:10.1126/science.1101902 · Cited by 1,403 · see citing works
Nishitoh, H., Matsuzawa, A., Tobiume, K., Saegusa, K., Takeda, K., Inoue, K., Hori, S., Kakizuka, A., & Ichijo, H. (2002) · Genes & Development · doi:10.1101/gad.992302 · Cited by 1,331 · see citing works
JNK phosphorylation of Bim-related members of the Bcl2 family induces Bax-dependent apoptosis
Lei, K., & Davis, R. J. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0438011100 · Cited by 1,068 · see citing works
Orchestrating the unfolded protein response in health and disease
Kaufman, R. J. (2002) · Journal of Clinical Investigation · doi:10.1172/jci0216886 · Cited by 1,015 · see citing works
Ohoka, N., Yoshii, S., Hattori, T., Onozaki, K., & Hayashi, H. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600596 · Cited by 1,004 · see citing works
Yoneda, T., Imaizumi, K., Oono, K., Yui, D., Gomi, F., Katayama, T., & Tohyama, M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010677200 · Cited by 866 · see citing works
TRB3: A <i>tribbles</i> Homolog That Inhibits Akt/PKB Activation by Insulin in Liver
Du, K., Herzig, S., Kulkarni, R. N., & Montminy, M. (2003) · Science · doi:10.1126/science.1079817 · Cited by 842 · see citing works
Cloning of mammalian Ire1 reveals diversity in the ER stress responses
Wang, X., Harding, H. P., Zhang, Y., Jolicoeur, E. M., Kuroda, M., & Ron, D. (1998) · The EMBO Journal · doi:10.1093/emboj/17.19.5708 · Cited by 787 · see citing works
ASK1 Is Essential for JNK/SAPK Activation by TRAF2
Nishitoh, H., Saitoh, M., Mochida, Y., Takeda, K., Nakano, H., Rothe, M., Miyazono, K., & Ichijo, H. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80283-x · Cited by 647 · see citing works
Bax and Bak can localize to the endoplasmic reticulum to initiate apoptosis
Zong, W., Li, C., Hatzivassiliou, G., Lindsten, T., Yu, Q., Yuan, J., & Thompson, C. B. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200302084 · Cited by 595 · see citing works
Caspase‐12 and ER‐Stress‐Mediated Apoptosis
Szegezdi, É., FitzGerald, U., & Samali, A. (2003) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1299.032 · Cited by 513 · see citing works
Self-citationEndoplasmic Reticulum Stress-induced Apoptosis
Li, J., Lee, B. A., & Lee, A. S. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m509868200 · Cited by 500 · see citing works
Brush, M., Weiser, D. C., & Shenolikar, S. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.4.1292-1303.2003 · Cited by 387 · see citing works
Yan, W., Frank, C. L., Korth, M. J., Sopher, B. L., Novoa, I., Ron, D., & Katze, M. G. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.252341799 · Cited by 385 · see citing works
Gene expression during ER stress–induced apoptosis in neurons
Reimertz, C., Kögel, D., Rami, A., Chittenden, T., & Prehn, J. H. M. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200305149 · Cited by 367 · see citing works
Hatai, T., Matsuzawa, A., Inoshita, S., Mochida, Y., Kuroda, T., Sakamaki, K., Kuida, K., Yonehara, S., Ichijo, H., & Takeda, K. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003412200 · Cited by 332 · see citing works
Enhanced bacterial clearance and sepsis resistance in caspase-12-deficient mice
Saleh, M., Mathison, J. C., Wolinski, M. K., Bensinger, S. J., Fitzgerald, P., Droin, N. M., Ulevitch, R. J., Green, D. R., & Nicholson, D. W. (2006) · Nature · doi:10.1038/nature04656 · Cited by 323 · see citing works
Ectopic expression of CHOP (GADD153) induces apoptosis in M1 myeloblastic leukemia cells
Matsumoto, M., Minami, M., Takeda, K., Sakao, Y., & Akira, S. (1996) · FEBS Letters · doi:10.1016/0014-5793(96)01016-2 · Cited by 321 · see citing works
Hu, P., Han, Z., Couvillon, A. D., & Exton, J. H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m407700200 · Cited by 318 · see citing works
Apoptotic crosstalk between the endoplasmic reticulum and mitochondria controlled by Bcl-2
Häcki, J., Egger, L., Monney, L., Conus, S., Rossé, T., Fellay, I., & Borner, C. (2000) · Oncogene · doi:10.1038/sj.onc.1203592 · Cited by 300 · see citing works
Phosphorylation of BCL‐2 regulates ER Ca2+ homeostasis and apoptosis
Bassik, M. C., Scorrano, L., Oakes, S. A., Pozzan, T., & Korsmeyer, S. J. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600104 · Cited by 278 · see citing works
van Huizen, R., Martindale, J. L., Gorospe, M., & Holbrook, N. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212074200 · Cited by 256 · see citing works
Ladiges, W., Knoblaugh, S. E., Morton, J., Korth, M. J., Sopher, B. L., Baskin, C. R., MacAuley, A., Goodman, A. G., LeBoeuf, R. C., & Katze, M. G. (2005) · Diabetes · doi:10.2337/diabetes.54.4.1074 · Cited by 211 · see citing works
Morishima, N., Nakanishi, K., Tsuchiya, K., Shibata, T., & Seiwa, E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408493200 · Cited by 184 · see citing works
The modification and assembly of proteins in the endoplasmic reticulum
Gaut, J. R., & Hendershot, L. M. (1993) · Current Opinion in Cell Biology · doi:10.1016/0955-0674(93)90127-c · Cited by 160 · see citing works
Adler, H. T., Chinery, R., Wu, D. Y., Kussick, S. J., Payne, J., Fornace, A. J., & Tkachuk, D. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.10.7050 · Cited by 156 · see citing works
Endoplasmic reticulum stress-induced cell death requires mitochondrial membrane permeabilization
Boya, P., COHEN, I. R., Zamzami, N., Vieira, H. L. A., & Kroemer, G. (2002) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401006 · Cited by 139 · see citing works
JAB1 participates in unfolded protein responses by association and dissociation with IRE1
Oono, K., Yoneda, T., Manabe, T., Yamagishi, S., Matsuda, S., Hitomi, J., Miyata, S., Mizuno, T., Imaizumi, K., Katayama, T., et al. (2004) · Neurochemistry International · doi:10.1016/j.neuint.2004.01.003 · Cited by 79 · see citing works
Distelhorst, C., & McCormick, T. S. (1996) · Cell Calcium · doi:10.1016/s0143-4160(96)90056-1 · Cited by 58 · see citing works
Flagged first, then by citations
1 of the 45 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
The integrated stress response
Pakos‐Zebrucka, K., Koryga, I., Mnich, K., Ljujic, M., Samali, A., & Gorman, A. M. (2016) · The EMBO Reports · doi:10.15252/embr.201642195 · Cited by 2,659 · see citing works
Self-citationIntegrating 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 2,603 · see citing works
Role of ROS and RNS Sources in Physiological and Pathological Conditions
Meo, S. D., Reed, T. T., Venditti, P., & Víctor, V. M. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/1245049 · Cited by 1,638 · see citing works
Cellular Stress Responses: Cell Survival and Cell Death
Fulda, S., Gorman, A. M., Hori, O., & Samali, A. (2010) · International Journal of Cell Biology · doi:10.1155/2010/214074 · Cited by 1,508 · see citing works
Self-citationEndoplasmic reticulum stress signals in the tumour and its microenvironment
Chen, X., & Cubillos-Ruiz, J. R. (2021) · Nature Reviews Cancer · doi:10.1038/s41568-020-00312-2 · Cited by 1,356 · see citing works
The impact of the endoplasmic reticulum protein-folding environment on cancer development
Wang, M., & Kaufman, R. J. (2014) · Nature reviews. Cancer · doi:10.1038/nrc3800 · Cited by 1,114 · see citing works
Rozpędek‐Kamińska, W., Pytel, D., Mucha, B., Leszczynska, H., Diehl, J. A., & Majsterek, I. (2016) · Current Molecular Medicine · doi:10.2174/1566524016666160523143937 · Cited by 871 · see citing works
Lipotoxicity and the gut-liver axis in NASH pathogenesis
Marra, F., & Svegliati-Baroni, G. (2018) · Journal of Hepatology · doi:10.1016/j.jhep.2017.11.014 · Cited by 847 · see citing works
The eIF2α kinases: their structures and functions
Donnelly, N., Gorman, A. M., Gupta, S., & Afshin Samali, A. (2013) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-1252-6 · Cited by 860 · see citing works
Self-citationXBP1 Controls Diverse Cell Type- and Condition-Specific Transcriptional Regulatory Networks
Acosta‐Alvear, D., Zhou, Y., Blais, A., Tsikitis, M., Lents, N. H., Arias, C., Lennon, C. J., Kluger, Y., & Dynlacht, B. D. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.06.011 · Cited by 853 · see citing works
ER stress: Autophagy induction, inhibition and selection
Rashid, H.-O., Yadav, R. K., Kim, H., & Chae, H. (2015) · Autophagy · doi:10.1080/15548627.2015.1091141 · Cited by 796 · see citing works
Molecular effectors of multiple cell death pathways initiated by photodynamic therapy
Buytaert, E., Dewaele, M., & Agostinis, P. (2007) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2007.07.001 · Cited by 749 · see citing works
Song, B., Scheuner, D. L., Ron, D., Pennathur, S., & Kaufman, R. J. (2008) · Journal of Clinical Investigation · doi:10.1172/jci34587 · Cited by 693 · see citing works
Protein quality control in the early secretory pathway
Anelli, T., & Sitia, R. (2008) · The EMBO Journal · doi:10.1038/sj.emboj.7601974 · Cited by 623 · see citing works
Surviving Stress: Modulation of ATF4-Mediated Stress Responses in Normal and Malignant Cells
Wortel, I. M. N., van der Meer, L. T., Kilberg, M. S., & van Leeuwen, F. N. (2017) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2017.07.003 · Cited by 613 · see citing works
A Molecular Web: Endoplasmic Reticulum Stress, Inflammation, and Oxidative Stress
Chaudhari, N., Talwar, P., Parimisetty, A., Lefebvre d’Hellencourt, C., & Ravanan, P. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00213 · Cited by 600 · see citing works
Molecular Mechanisms of Apoptosis and Roles in Cancer Development and Treatment
Goldar, S., Khaniani, M. S., Derakhshan, S. M., & Baradaran, B. (2015) · Asian Pacific Journal of Cancer Prevention · doi:10.7314/apjcp.2015.16.6.2129 · Cited by 611 · see citing works
HSPA5 Regulates Ferroptotic Cell Death in Cancer Cells
Zhu, S., Zhang, Q., Sun, X., Zeh, H. J., Lotze, M. T., Kang, R., & Tang, D. (2017) · Cancer Research · doi:10.1158/0008-5472.can-16-1979 · Cited by 576 · see citing works
Mustafa, M., Ahmad, R., Tantry, I. Q., Ahmad, W., Siddiqui, S., Alam, M., Abbas, K., Moinuddin, Hassan, M. I., Habib, S., et al. (2024) · Cells · doi:10.3390/cells13221838 · Cited by 595 · see citing works
Human Coronaviruses: A Review of Virus–Host Interactions
Lim, Y. X., Ng, Y. W., Tam, J. P., & Liu, D. X. (2016) · Diseases · doi:10.3390/diseases4030026 · Cited by 585 · see citing works
Molecular mechanisms of lipotoxicity and glucotoxicity in nonalcoholic fatty liver disease
Mota, M., Banini, B. A., Cazanave, S. C., & Sanyal, A. J. (2016) · Metabolism · doi:10.1016/j.metabol.2016.02.014 · Cited by 570 · see citing works
Environmental toxicity, oxidative stress and apoptosis: Ménage à Trois
Franco, R., Sánchez-Olea, R., Reyes-Reyes, E. M., & Panayiotidis, M. I. (2009) · Mutation Research/Genetic Toxicology and Environmental Mutagenesis · doi:10.1016/j.mrgentox.2008.11.012 · Cited by 541 · see citing works
The Unfolded Protein Response: A Pathway That Links Insulin Demand with β-Cell Failure and Diabetes
Scheuner, D., & Kaufman, R. J. (2008) · Endocrine Reviews · doi:10.1210/er.2007-0039 · Cited by 525 · see citing works
Roles and regulation of the mucus barrier in the gut
Cornick, S., Tawiah, A., & Chadee, K. (2015) · Tissue Barriers · doi:10.4161/21688370.2014.982426 · Cited by 527 · see citing works
Cell Signaling and Stress ResponsesPreprint
Hotamışlıgil, G. S., & Davis, R. J. (2016) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a006072 · Cited by 496 · see citing works
Pathophysiological mechanisms and therapeutic approaches in obstructive sleep apnea syndrome
Lv, R., Liu, X., Zhang, Y., Dong, N., Wang, X., He, Y., Yue, H., & Yin, Q. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01496-3 · Cited by 521 · see citing works
Timmins, J. M., Özcan, L., Seimon, T. A., Li, G., Malagelada, C., Backs, J., Backs, T., Bassel‐Duby, R., Olson, E. N., Anderson, M. E., et al. (2009) · Journal of Clinical Investigation · doi:10.1172/jci38857 · Cited by 422 · see citing works
Endoplasmic reticulum stress in liver diseases
Ajoolabady, A., Kaplowitz, N., Lebeaupin, C., Kroemer, G., Kaufman, R. J., Malhi, H., & Ren, J. T. (2022) · Hepatology · doi:10.1002/hep.32562 · Cited by 410 · see citing works
A review of the mammalian unfolded protein response
Chakrabarti, A., Chen, A. W., & Varner, J. D. (2011) · Biotechnology and Bioengineering · doi:10.1002/bit.23282 · Cited by 408 · see citing works
Stress management at the ER: Regulators of ER stress-induced apoptosis
Gorman, A. M., Healy, S., Jäger, R., & Afshin Samali, A. (2012) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2012.02.003 · Cited by 404 · see citing works
Self-citationLiao, Z., Luo, R., Li, G., Song, Y., Zhan, S., Zhao, K., Hua, W., Zhang, Y., Wu, X., & Cao, Y. (2019) · Theranostics · doi:10.7150/thno.33638 · Cited by 403 · see citing works
Targeting ER stress induced apoptosis and inflammation in cancer
Verfaillie, T., Garg, A. D., & Agostinis, P. (2010) · Cancer Letters · doi:10.1016/j.canlet.2010.07.016 · Cited by 392 · see citing works
Endoplasmic Reticulum Stress and Cancer
Yadav, R. K., Chae, S., Kim, H., & Chae, H. (2014) · Journal of Cancer Prevention · doi:10.15430/jcp.2014.19.2.75 · Cited by 396 · see citing works
Keane, K. N., Cruzat, V. F., Carlessi, R., de Bittencourt, P. I. H., & Newsholme, P. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2015/181643 · Cited by 385 · see citing works
Endoplasmic reticulum stress and pancreatic β-cell death
Fonseca, S. G., Gromada, J., & Urano, F. (2011) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2011.02.008 · Cited by 384 · see citing works
The endoplasmic reticulum stress response in aging and age-related diseases
Brown, M. K., & Naidoo, N. N. (2012) · Frontiers in Physiology · doi:10.3389/fphys.2012.00263 · Cited by 372 · see citing works
Neuronal cell death in neurodegenerative diseases: recurring themes around protein handling
Gorman, A. M. (2008) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2008.00402.x · Cited by 362 · see citing works
Self-citationThe role of the unfolded protein response in cancer progression: From oncogenesis to chemoresistance
Madden, E. C., Logue, S. E., Healy, S., Manié, S. N., & Samali, A. (2018) · Biology of the Cell · doi:10.1111/boc.201800050 · Cited by 354 · see citing works
Self-citationCutting Edge: Activation of STING in T Cells Induces Type I IFN Responses and Cell Death
Larkin, B., Ilyukha, V., Sorokin, M., Buzdin, A., Vannier, E., & Poltorak, A. (2017) · The Journal of Immunology · doi:10.4049/jimmunol.1601999 · Cited by 361 · see citing works
Endoplasmic Reticulum Stress: Its Role in Disease and Novel Prospects for Therapy
Schönthal, A. H. (2012) · Scientifica · doi:10.6064/2012/857516 · Cited by 350 · see citing works
Linking ER Stress to Autophagy: Potential Implications for Cancer Therapy
Verfaillie, T., Salazar‐Roa, M., Velasco, G., & Agostinis, P. (2010) · International Journal of Cell Biology · doi:10.1155/2010/930509 · Cited by 344 · see citing works
Role of apoptosis in cardiovascular disease
Lee, Y., & Gustafsson, Å. B. (2009) · Apoptosis · doi:10.1007/s10495-008-0302-x · Cited by 333 · see citing works
Petsophonsakul, P., Furmanik, M., Forsythe, R. O., Dweck, M. R., Schurink, G. W. H., Natour, E., Reutelingsperger, C. P. M., Jacobs, M. J. H. M., Mees, B., & Schurgers, L. J. (2019) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.119.312787 · Cited by 344 · see citing works
Wende, A. R., & Abel, E. D. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2009.09.023 · Cited by 344 · see citing works
Jovaisaite, V., Mouchiroud, L., & Auwerx, J. (2014) · Journal of Experimental Biology · doi:10.1242/jeb.090738 · Cited by 335 · see citing works
Molecular mechanism involved in cyclophosphamide-induced cardiotoxicity: Old drug with a new vision
Iqubal, A., Iqubal, M. K., Sharma, S., Ansari, M. A., Najmi, A. K., Ali, S. M., Ali, J., & Haque, S. E. (2018) · Life Sciences · doi:10.1016/j.lfs.2018.12.018 · Cited by 330 · see citing works
Cell Death Pathways in Ischemic Stroke and Targeted Pharmacotherapy
Datta, A., Sarmah, D., Mounica, L., Kaur, H., Kesharwani, R., Verma, G., Veeresh, P., Kotian, V., Kalia, K., Borah, A., et al. (2020) · Translational Stroke Research · doi:10.1007/s12975-020-00806-z · Cited by 328 · see citing works
Tardito, S., Bassanetti, I., Bignardi, C., Elviri, L., Tegoni, M., Mucchino, C., Bussolati, O., Franchi‐Gazzola, R., & Marchiò, L. (2011) · Journal of the American Chemical Society · doi:10.1021/ja109413c · Cited by 325 · see citing works
Unfolded proteins and endoplasmic reticulum stress in neurodegenerative disorders
Doyle, K., Kennedy, D. C., Gorman, A. M., Gupta, S., Healy, S., & Samali, A. (2011) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2011.01374.x · Cited by 320 · see citing works
Self-citationPluquet, O., Pourtier, A., & Abbadie, C. (2015) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00334.2014 · Cited by 305 · see citing works
Targeting the endoplasmic reticulum-stress response as an anticancer strategy
Healy, S., Gorman, A. M., Mousavi-Shafaei, P., Gupta, S., & Afshin Samali, A. (2009) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2009.06.064 · Cited by 305 · see citing works
Self-citationKim, T. W., Lee, S. Y., Kim, M., Cheon, C., & Ko, S. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-0930-1 · Cited by 305 · see citing works
Cellular stress response pathways and ageing: intricate molecular relationships
Kourtis, N., & Tavernarakis, N. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.162 · Cited by 304 · see citing works
Metabolism, toxicity and anticancer activities of arsenic compounds
Khairul, I., Wang, Q. Q., Jiang, Y. H., Wang, C., & Naranmandura, H. (2017) · Oncotarget · doi:10.18632/oncotarget.14733 · Cited by 300 · see citing works
Obulesu, M., & Lakshmi, M. J. (2014) · Neurochemical Research · doi:10.1007/s11064-014-1454-4 · Cited by 290 · see citing works
Hombach‐Klonisch, S., Mehrpour, M., Shojaei, S., Harlos, C. H., Pitz, M. W., Hamaï, A., Siemianowicz, K., Likus, W., Wiecheć, E., Toyota, B. D., et al. (2017) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2017.10.017 · Cited by 290 · see citing works
Self-citationPhotoreceptor Cell Death Mechanisms in Inherited Retinal Degeneration
Sancho-Pellúz, J., Arango‐González, B., Kustermann, S., Romero, F. J., Veen, T. V., Zrenner, E., Ekström, P. A. R., & Paquet‐Durand, F. (2008) · Molecular Neurobiology · doi:10.1007/s12035-008-8045-9 · Cited by 287 · see citing works
Fuchs endothelial corneal dystrophy: The vicious cycle of Fuchs pathogenesis
Tone, S. O., Kocaba, V., Böhm, M., Wylęgała, A., White, T. L., & Jurkunas, U. V. (2020) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2020.100863 · Cited by 293 · see citing works
Logue, S. E., McGrath, E. P., Cleary, P., Greene, S., Mnich, K., Almanza, A., Chevet, É., Dwyer, R. M., Oommen, A. M., Legembre, P., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-05763-8 · Cited by 284 · see citing works
Self-citationAging Impairs the Unfolded Protein Response to Sleep Deprivation and Leads to Proapoptotic Signaling
Naidoo, N. N., Ferber, M., Master, M., Zhu, Y., & Pack, A. I. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.5685-07.2008 · Cited by 282 · see citing works
Chang, M., Shiau, A., Chen, Y., Chang, C., Chen, H. H., & Wu, C. (2008) · Cancer Science · doi:10.1111/j.1349-7006.2008.00827.x · Cited by 281 · see citing works
ER and aging—Protein folding and the ER stress response
Naidoo, N. N. (2009) · Ageing Research Reviews · doi:10.1016/j.arr.2009.03.001 · Cited by 280 · see citing works
Coronavirus infection, ER stress, apoptosis and innate immunity
Fung, T. S., & Liu, D. X. (2014) · Frontiers in Microbiology · doi:10.3389/fmicb.2014.00296 · Cited by 279 · see citing works
The mitochondrial death pathway: a promising therapeutic target in diseases
Gupta, S., Kass, G. E. N., Szegezdi, É., & Joseph, B. (2009) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2009.00697.x · Cited by 278 · see citing works
Stress-induced self-cannibalism: on the regulation of autophagy by endoplasmic reticulum stress
Deegan, S., Saveljeva, S., Gorman, A. M., & Samali, A. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-1173-4 · Cited by 273 · see citing works
Self-citationProteinuria and Hyperglycemia Induce Endoplasmic Reticulum Stress
Lindenmeyer, M. T., Rastaldi, M. P., Ikehata, M., Neusser, M. A., Kretzler, M., Cohen, C. D., & Diaeresis]ndorff, D. S. (2008) · Journal of the American Society of Nephrology · doi:10.1681/asn.2007121313 · Cited by 270 · see citing works
Roongta, U. V., Pabalan, J. G., Wang, X., Ryseck, R.-P., Fargnoli, J., Henley, B. J., Yang, W.-P., Zhu, J., Madireddi, M. T., Lawrence, R. M., et al. (2011) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-11-0126 · Cited by 266 · see citing works
Compounds Triggering ER Stress Exert Anti-Melanoma Effects and Overcome BRAF Inhibitor Resistance
Cerezo, M., Lehraiki, A., Millet, A., Rouaud, F., Plaisant, M., Jaune, E., Botton, T., Ronco, C., Abbe, P., Amdouni, H., et al. (2016) · Cancer Cell · doi:10.1016/j.ccell.2016.04.013 · Cited by 265 · see citing works
Roles of XBP1s in Transcriptional Regulation of Target Genes
Park, S.-M., Kang, T.-I., & So, J. (2021) · Biomedicines · doi:10.3390/biomedicines9070791 · Cited by 265 · see citing works
Bánhegyi, G., BAUMEISTER, P., Benedetti, A., Dong, D., Fu, Y., Lee, A. S., Li, J., Mao, C., Margittai, É., Ni, M., et al. (2007) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1391.007 · Cited by 262 · see citing works
Molecular mechanisms of pesticide-induced neurotoxicity: Relevance to Parkinson's disease
Franco, R., Li, S., Rodríguez‐Rocha, H., Burns, M., & Panayiotidis, M. I. (2010) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2010.06.003 · Cited by 262 · see citing works
ER Stress-Mediated Signaling: Action Potential and Ca2+ as Key Players
Bahar, E., Kim, H., & Yoon, H. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17091558 · Cited by 257 · see citing works
Senkal, C. E., Ponnusamy, S., Bielawski, J., Hannun, Y. A., & Öğretmen, B. (2009) · The FASEB Journal · doi:10.1096/fj.09-135087 · Cited by 254 · see citing works
Endoplasmic reticulum stress in disorders of myelinating cells
Lin, W., & Popko, B. (2009) · Nature Neuroscience · doi:10.1038/nn.2273 · Cited by 253 · see citing works
Hamid, T., Guo, S. Z., Kingery, J. R., Xiang, X., Dawn, B., & Prabhu, S. D. (2010) · Cardiovascular Research · doi:10.1093/cvr/cvq274 · Cited by 253 · see citing works
A lifetime of stress: ATF6 in development and homeostasis
Hillary, R. F., & FitzGerald, U. (2018) · Journal of Biomedical Science · doi:10.1186/s12929-018-0453-1 · Cited by 253 · see citing works
Cadmium and cellular signaling cascades: interactions between cell death and survival pathways
Thévenod, F., & Lee, W. (2013) · Archives of Toxicology · doi:10.1007/s00204-013-1110-9 · Cited by 248 · see citing works
Gupta, S., Deepti, A., Deegan, S., Lisbona, F., Hetz, C. A., & Afshin Samali, A. (2010) · PLoS Biology · doi:10.1371/journal.pbio.1000410 · Cited by 245 · see citing works
Nakka, V. P., Prakash-babu, P., & Vemuganti, R. (2014) · Molecular Neurobiology · doi:10.1007/s12035-014-9029-6 · Cited by 226 · see citing works
Bcl-2 family on guard at the ER
Szegezdi, É., Macdonald, D. C., Chonghaile, T. N., Gupta, S., & Afshin Samali, A. (2009) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00612.2008 · Cited by 241 · see citing works
Apoptosis: A review of pro‐apoptotic and anti‐apoptotic pathways and dysregulation in disease
O'Brien, M., & Kirby, R. (2008) · Journal of Veterinary Emergency and Critical Care · doi:10.1111/j.1476-4431.2008.00363.x · Cited by 246 · see citing works
Chami, M., Oulès, B., Szabadkai, G., Tacine, R., Rizzuto, R., & Paterlini-Bréchot, P. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.11.014 · Cited by 235 · see citing works
Discovery of a first-in-class EZH2 selective degrader
Ma, A., Στρατικόπουλος, Η., Park, K., Wei, J., Martin, T. C., Yang, X., Schwarz, M. C., Leshchenko, V. V., Rialdi, A., Dale, B., et al. (2019) · Nature Chemical Biology · doi:10.1038/s41589-019-0421-4 · Cited by 240 · see citing works
Davenport, E. L., Moore, H. E., Dunlop, A. S., Sharp, S. Y., Workman, P., Morgan, G. J., & Davies, F. E. (2007) · Blood · doi:10.1182/blood-2006-11-053728 · Cited by 238 · see citing works
Lipotoxicity in type 2 diabetic cardiomyopathy
van de Weijer, T., Schrauwen‐Hinderling, V. B., & Schrauwen, P. (2011) · Cardiovascular Research · doi:10.1093/cvr/cvr212 · Cited by 235 · see citing works
Medigeshi, G. R., Lancaster, A. M., Hirsch, A. J., Briese, T., Lipkin, W. I., DeFilippis, V. R., Früh, K., Mason, P. W., Nikolich‐Žugich, J., & Nelson, J. A. (2007) · Journal of Virology · doi:10.1128/jvi.01151-07 · Cited by 236 · see citing works
Garg, A. D., Ruysscher, D. D., & Agostinis, P. (2015) · OncoImmunology · doi:10.1080/2162402x.2015.1069938 · Cited by 229 · see citing works
Endoplasmic Reticulum Stress in the Heart
Glembotski, C. C. (2007) · Circulation Research · doi:10.1161/circresaha.107.161273 · Cited by 229 · see citing works
Unfolding the Interactions between Endoplasmic Reticulum Stress and Oxidative Stress
Ong, G., & Logue, S. E. (2023) · Antioxidants · doi:10.3390/antiox12050981 · Cited by 228 · see citing works
Self-citationCigarette Smoke Induces an Unfolded Protein Response in the Human Lung
Kelsen, S. G., Duan, X., Ji, R., Pérez, Ó. C., Liu, C., & Merali, S. (2007) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2007-0221oc · Cited by 223 · see citing works
Trailing TRAIL Resistance: Novel Targets for TRAIL Sensitization in Cancer Cells
Trivedi, R., & Mishra, D. P. (2015) · Frontiers in Oncology · doi:10.3389/fonc.2015.00069 · Cited by 223 · see citing works
GRP78 at the Centre of the Stage in Cancer and Neuroprotection
Casas, C. (2017) · Frontiers in Neuroscience · doi:10.3389/fnins.2017.00177 · Cited by 222 · see citing works
Paraptosis in the anti-cancer arsenal of natural products
Lee, D., Kim, I. Y., Saha, S., & Choi, K. S. (2016) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2016.01.003 · Cited by 215 · see citing works
Yang, X. F., Wang, Y., Li, Q., Zhong, Y., Chen, L., Du, Y., He, J., Liao, L., Xiong, K., Yi, C., et al. (2018) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2018.00186 · Cited by 214 · see citing works
ER stress, autophagy, and RNA viruses
Jheng, J.-R., Ho, J., & Horng, J. (2014) · Frontiers in Microbiology · doi:10.3389/fmicb.2014.00388 · Cited by 210 · see citing works
Effects of curcumin on mitochondria in neurodegenerative diseases
Bagheri, H., Ghasemi, F., Barreto, G. E., Rafiee, R., Sathyapalan, T., & Sahebkar, A. (2019) · BioFactors · doi:10.1002/biof.1566 · Cited by 211 · see citing works
Liu, Z., Zhu, H., Chen, K., Dong, X., Wei, J., Qiu, C., & Xue, J. (2013) · Cardiovascular Diabetology · doi:10.1186/1475-2840-12-158 · Cited by 209 · see citing works
Jäger, R., Bertrand, M. J. M., Gorman, A. M., Vandenabeele, P., & Afshin Samali, A. (2012) · Biology of the Cell · doi:10.1111/boc.201100055 · Cited by 208 · see citing works
Self-citation“Go upstream, young man”: lessons learned from the p38 saga
Hammaker, D. R., & Firestein, G. S. (2009) · Annals of the Rheumatic Diseases · doi:10.1136/ard.2009.119479 · Cited by 206 · see citing works
The ER–mitochondria interface: The social network of cell death
Grimm, S. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.11.018 · Cited by 200 · see citing works
- Authors
- Szegezdi, E., Logue, S. E., Gorman, A. M., & Samali, A.
- Affiliations
- National University of Ireland (IE)
- Venue
- The EMBO Reports
- Published
- 2006-09-01
- Volume
- 7
- Issue
- 9
- Pages
- 880-885
- ISSN
- 1469-221X (ISSN-L)
- 1469-3178
- PMC
- PMC1559676
- OpenAlex
- W2133644385
- Cited by
- 2,345
- References
- 45
- Citations by year
- 2026: 42 · 2025: 85 · 2024: 121 · 2023: 129 · 2022: 147 · 2021: 126 · 2020: 147 · 2019: 139 · 2018: 154 · 2017: 140 · 2016: 140 · 2015: 140 · 2014: 137 · 2013: 134 · 2012: 124
- FWCI
- 5.47
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- EMBO Reports (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Arrow@dit (Dublin Institute of Technology) (submittedVersion)
- ARAN (University of Galway Research Repository) (Ollscoil na Gaillimhe – University of Galway) (submittedVersion, cc-by-nc-nd)
- Funders
- Science Foundation Ireland
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Life Sciences › Neuroscience › Sensory Systems › Ion Channels and Receptors
- Keywords
- endoplasmic reticulum stress, apoptosis, unfolded protein response, ER stress-induced apoptosis, unfolded proteins, neurodegenerative diseases, cardiovascular disease, cell death mechanisms
- MeSH terms
- Animals, Endoplasmic Reticulum, Humans, Models, Biological, Signal Transduction, Apoptosis, Protein Folding, Oxidative Stress, Molecular Chaperones, Protein Transport, Mice
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
