The DOI matches its Crossref record; 44 of the 45 references it cites were found in a registry or an index.
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.
Overview
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
Verification
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?
In the citing paper
“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.
Citations
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 688
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 5,131
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
Yoshida, H., Matsui, T., Yamamoto, A., Okada, T., & Mori, K. (2001) · Cell · doi:10.1016/s0092-8674(01)00611-0 · Cited by 4,054
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
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
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
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 3,292
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 3,099
Urano, F., Wang, X.-Z., Bertolotti, A., Zhang, Y.-H., Chung, P., Harding, H., & Ron, D. (2000) · Science · doi:10.1126/science.287.5453.664 · Cited by 3,081
Flagged first, then by citations
1 of the 45 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Items 601–700 of 1,004
Barrero, C. A., Pérez, Ó. C., Aksoy, M. O., Moncada, C., Ji, R., López, Y., Mallilankaraman, K. B., Madesh, M., Criner, G. J., Kelsen, S. G., et al. (2013) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.201302-0342oc · Cited by 54
Moghadam, M. H., Aghaei, M., Fallahian, F., Jafari, S. M., Dolati, M., Abdolmohammadi, M. H., Hajiahmadi, S., & Esmaeili, S. (2014) · Tumor Biology · doi:10.1007/s13277-014-2744-9 · Cited by 52
Vellanki, R. N., Zhang, L., Guney, M. A., Rocheleau, J. V., GANNON, M. A., & Volchuk, A. (2010) · Endocrinology · doi:10.1210/en.2010-0137 · Cited by 54
Hübener‐Schmid, J., Vauti, F., Funke, C., Wolburg, H., Ye, Y., Schmidt, T., Wolburg‐Buchholz, K., Schmitt, I., Gardyan, A., Drießen, S., et al. (2011) · Brain · doi:10.1093/brain/awr118 · Cited by 56
Chen, H., Zhou, B., Yang, J., Ma, X., Deng, S., Huang, Y., Wen, Y., Yuan, J.-Q., & Yang, X.-Z. (2018) · Frontiers in Pharmacology · doi:10.3389/fphar.2018.00483 · Cited by 48
Krupkova, O., Sadowska, A., Kameda, T., Hitzl, W., Hausmann, O. N., Klasen, J., & Wuertz‐Kozak, K. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.01706 · Cited by 54
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
Lung alveolar epithelium and interstitial lung disease
Corvol, H., Flamein, F., Epaud, R., Clément, A., & Guillot, L. (2009) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2009.02.009 · Cited by 56
Hamamura, K., Goldring, M. B., & Yokota, H. (2008) · Archives of Oral Biology · doi:10.1016/j.archoralbio.2008.11.003 · Cited by 54
Etiology of type 2 diabetes and Alzheimer’s disease: Exploring the mitochondria
Silzer, T. K., & Phillips, N. R. (2018) · Mitochondrion · doi:10.1016/j.mito.2018.04.004 · Cited by 53
Sansone, C., Bruno, A., Piscitelli, C., Baci, D., Fontana, A., Brunet, C., Noonan, D. M., & Albini, A. (2021) · Cells · doi:10.3390/cells10020231 · Cited by 55
Do, P. T., Wu, C.-C., Chiang, Y. H., Hu, C., & Chen, K. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms221810045 · Cited by 57
Yamasaki, S., Yagishita, N., Nishioka, K., & Nakajima, T. (2007) · Cell Cycle · doi:10.4161/cc.6.11.4277 · Cited by 53
Yin, Q., Dong, C., Dong, S., Dong, X.-L., Yan, H., Hou, X., Luo, D., Pei, J.-J., & Liu, X. (2012) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-012-9856-9 · Cited by 53
Fu, M., Li, L., Albrecht, T., Johnson, J. D., Kojic, L. D., & Nabi, I. R. (2011) · Cell Death and Differentiation · doi:10.1038/cdd.2010.181 · Cited by 53
Li, J., Cai, X., Xia, Q., Yao, K., Chen, J., Zhang, Y., Naranmandura, H., Liu, X., & Wu, Y. (2014) · Toxicological Sciences · doi:10.1093/toxsci/kfu223 · Cited by 53
Ding, L., Feng, H.-J., Macdonald, R. L., Botzolakis, E. J., Hu, N., & Gallagher, M. J. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.142299 · Cited by 53
Sequential Cytoprotective Responses to Sigma1 Ligand–Induced Endoplasmic Reticulum Stress
Schrock, J. M., Spino, C. M., Longen, C. G., Stabler, S. M., Marino, J. C., Pasternak, G. W., & Kim, F. J. (2013) · Molecular Pharmacology · doi:10.1124/mol.113.087809 · Cited by 53
Endotoxin causes functional endoplasmic reticulum failure, possibly mediated by mitochondria
Kozlov, A. V., Duvigneau, J. C., Miller, I., Nürnberger, S., Gesslbauer, B., Kungl, A. J., Öhlinger, W., Hartl, R. T., Gille, L., Staniek, K., et al. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.03.004 · Cited by 54
Alam, M. M., Kariya, R., Kawaguchi, A., Matsuda, K., Kudo, E., & Okada, S. (2016) · APOPTOSIS · doi:10.1007/s10495-016-1277-7 · Cited by 53
Kengne, F. G., Couturier, B. S., Soupart, A., Brion, J., & Decaux, G. (2017) · Journal of the American Society of Nephrology · doi:10.1681/asn.2016050509 · Cited by 55
Zecchini, S., Giovarelli, M., Perrotta, C., Morisi, F., Touvier, T., Renzo, I. D., Moscheni, C., Bassi, M. T., Cervia, D., Sandri, M., et al. (2018) · Autophagy · doi:10.1080/15548627.2018.1507439 · Cited by 54
Proteasome inhibition drastically but reversibly impairs murine lymphocyte development
Maseda, D., Meister, S., Neubert, K., i, M. H., & Voll, R. E. (2008) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4402297 · Cited by 53
Gao, H., Wang, Y., Wegierski, T., Skouloudaki, K., Pütz, M., Fu, X., Engel, C., Boehlke, C., Peng, H., Kuehn, E. W., et al. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddp463 · Cited by 52
Guo, F., Lin, E. A., Liu, P., Lin, J., & Liu, C.-J. (2010) · Cellular Signalling · doi:10.1016/j.cellsig.2010.07.006 · Cited by 53
Endoplasmic reticulum stress in murine liver and kidney exposed to microcystin-LR
Qin, W., Xu, L., Zhang, X., Wang, Y., Meng, X., Miao, A., & Yang, L. (2010) · Toxicon · doi:10.1016/j.toxicon.2010.07.017 · Cited by 52
Chen, B., Liu, G., Zou, P., Li, X., Hao, Q., Jiang, B., Yang, X., & Hu, Z. (2015) · Experimental Biology and Medicine · doi:10.1177/1535370215573394 · Cited by 52
Mitochondria mediated cell death in diabetes
Szabadkai, G., & Duchen, M. R. (2009) · APOPTOSIS · doi:10.1007/s10495-009-0363-5 · Cited by 54
Kim, H. S., Lim, J. M., Kim, J. Y., Kim, Y.-J., Park, S. I., & Sohn, J. (2015) · International Journal of Cancer · doi:10.1002/ijc.29879 · Cited by 52
Zhang, P., Su, C., Jiang, Z., & Zheng, C. (2016) · Journal of Virology · doi:10.1128/jvi.02056-16 · Cited by 52
Yang, F., Yu, X., Li, T., Wu, J., Zhao, Y., Liu, J., Sun, A., Dong, S., Wu, J., Zhong, X., et al. (2016) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00196.2016 · Cited by 52
Wang, G., Liu, S., Wang, L., Meng, L., Cui, C.-J., Zhang, H., Hu, S., Ma, N., & Wei, Y. (2017) · International Journal of Biological Sciences · doi:10.7150/ijbs.17758 · Cited by 52
Diphlorethohydroxycarmalol Attenuates Fine Particulate Matter-Induced Subcellular Skin Dysfunction
Zhen, A. X., Piao, M. J., Hyun, Y. J., Kang, K. A., Fernando, P. D. S. M., Cho, S. J., Ahn, M. J., & Hyun, J. W. (2019) · Marine Drugs · doi:10.3390/md17020095 · Cited by 54
Drug discovery and treatment paradigms in nonalcoholic steatohepatitis
Noureddin, M., Muthiah, M. D., & Sanyal, A. J. (2019) · Endocrinology Diabetes & Metabolism · doi:10.1002/edm2.105 · Cited by 52
Icariin improves the cognitive function of APP/PS1 mice via suppressing endoplasmic reticulum stress
Li, F., Zhang, Y., Lu, X., Shi, J., & Gong, Q. (2019) · Life Sciences · doi:10.1016/j.lfs.2019.116739 · Cited by 51
Xu, L., Su, L., & Liu, X. (2012) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-12-0602 · Cited by 51
IRE1α-XBP1 signaling pathway, a potential therapeutic target in multiple myeloma
Chen, L., Li, Q., She, T., Li, H., Yue, Y., Gao, S., Yan, T., Liu, S., Ma, J., & Wang, Y. (2016) · Leukemia Research · doi:10.1016/j.leukres.2016.07.006 · Cited by 51
A Role for Endoplasmic Reticulum Stress in Intracerebral Hemorrhage
Thangameeran, S. I. M., Tsai, S., Hung, H., Hu, W.-F., Pang, C., Chen, S.-Y., & Liew, H. (2020) · Cells · doi:10.3390/cells9030750 · Cited by 53
Biguanides drugs: Past success stories and promising future for drug discovery
Grytsai, O., Myrgorodska, I., Rocchi, S., Ronco, C., & Benhida, R. (2021) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2021.113726 · Cited by 51
Sakitani, K., Hirata, Y., Hikiba, Y., Hayakawa, Y., Ihara, S., Suzuki, H., Suzuki, N., Serizawa, T., Kinoshita, H., Sakamoto, K., et al. (2015) · BMC Cancer · doi:10.1186/s12885-015-1789-5 · Cited by 53
Qi, Y., & Xia, P. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.362160 · Cited by 51
Hsiao, P., Hsieh, Y., Chow, J., Yang, S., Hsiao, M., Hua, K., Lin, C., Chen, H., & Chien, M. (2013) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf402956m · Cited by 51
Why is autophagy important for melanoma? Molecular mechanisms and therapeutic implications
Corazzari, M., Fimia, G. M., Lovat, P. E., & Piacentini, M. (2013) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2013.07.001 · Cited by 56
Idebenone and Resveratrol Extend Lifespan and Improve Motor Function of HtrA2 Knockout Mice
Gerhardt, E., Gräber, S., Szegő, É. M., Moisoi, N., Martins, L. M., Outeiro, T. F., & Kermer, P. (2011) · PLoS ONE · doi:10.1371/journal.pone.0028855 · Cited by 52
Novel Benzo[a]quinolizidine Analogs Induce Cancer Cell Death through Paraptosis and Apoptosis
Zheng, H., Dong, Y., Li, L., Sun, B., Liu, L., Yuan, H., & Lou, H. (2016) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b00484 · Cited by 52
Cytomegalovirus as an oncomodulatory agent in the progression of glioma
Joseph, G. P., McDermott, R., Baryshnikova, M. A., Cobbs, C., & Ulasov, I. V. (2016) · Cancer Letters · doi:10.1016/j.canlet.2016.10.022 · Cited by 51
Gyöngyösi, B., Cho, Y., Lowe, P., Calenda, C. D., Iracheta‐Vellve, A., Satishchandran, A., Ambade, A., & Szabó, G. (2019) · Mucosal Immunology · doi:10.1038/s41385-019-0170-4 · Cited by 53
Masciarelli, S., & Sitia, R. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2008.01.003 · Cited by 51
Essential Role of PACT-Mediated PKR Activation in Tunicamycin-Induced Apoptosis
Singh, M., Fowlkes, V., Handy, I., Patel, C. V., & Patel, R. C. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.10.068 · Cited by 52
Lizardo, M. M., Morrow, J. J., Miller, T. E., Hong, E. S., Ren, L., Mendoza, A., Halsey, C. H., Scacheri, P. C., Helman, L. J., & Khanna, C. (2016) · Neoplasia · doi:10.1016/j.neo.2016.09.001 · Cited by 50
The Autophagy-Lysosomal Pathways and Their Emerging Roles in Modulating Proteostasis in Tumors
Dong, Z., & Cui, H. (2018) · Cells · doi:10.3390/cells8010004 · Cited by 50
Pashootan, P., Saadati, F., Fahimi, H., Rahmati, M., Strippoli, R., Zarrabi, A., Cordani, M., & Moosavi, M. A. (2023) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2023.123622 · Cited by 53
Chen, Y., Su, J., Tsao, C.-Y., Hung, C.-T., Chao, H.-H., Lin, J., Liao, M., Yang, Z.-Y., Huang, H. H., Tsai, F., et al. (2013) · Molecules · doi:10.3390/molecules180910146 · Cited by 51
A kinase inhibitor activates the IRE1α RNase to confer cytoprotection against ER stress
Han, D., Upton, J.-P., Hagen, A., Callahan, J. A., Oakes, S. A., & Papa, F. R. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.11.040 · Cited by 53
Activation of the Cellular Unfolded Protein Response by Recombinant Adeno-Associated Virus Vectors
Balakrishnan, B., Sen, D., Hareendran, S., Roshini, V., David, S., Srivastava, A., & Jayandharan, G. R. (2013) · PLoS ONE · doi:10.1371/journal.pone.0053845 · Cited by 50
Kim, E. C., Meng, H., & Jun, A. S. (2014) · Experimental Eye Research · doi:10.1016/j.exer.2014.06.002 · Cited by 50
Rao, R., Nalluri, S., Fiskus, W. C., Savoie, A., Buckley, K. M., Ha, K., Balusu, R., Joshi, A., Coothankandaswamy, V., Tao, J., et al. (2010) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-10-0529 · Cited by 50
Wei, Z., Weng, S., Wang, L., & Mao, Z.-J. (2017) · Molecular Medicine Reports · doi:10.3892/mmr.2017.8084 · Cited by 50
Angiotensin II Increases Endoplasmic Reticulum Stress in Adipose Tissue and Adipocytes
Menikdiwela, K. R., Ramalingam, L., Allen, L., Scoggin, S., Kalupahana, N., & Moustaid-Moussa, N. (2019) · Scientific Reports · doi:10.1038/s41598-019-44834-8 · Cited by 50
Luo, D., Fan, N., Zhang, X., Ngo, F. Y., Zhao, J., Zhao, W., Huang, M., Ding, L., Wang, Y., & Rong, J. (2022) · eLife · doi:10.7554/elife.72182 · Cited by 50
Lin, Y., Chen, S., Yue, P., Zou, W., Benbrook, D. M., Liu, S., Le, T. C., Berlin, K. D., Khuri, F. R., & Sun, S. (2008) · Cancer Research · doi:10.1158/0008-5472.can-07-6209 · Cited by 50
Hu, J. R., Lu, X., Zhang, X., Shao, X., Wang, Y., Chen, J., Zhao, B., Li, S., Xu, C., & Wei, C. (2020) · Cell Biology International · doi:10.1002/cbin.11360 · Cited by 49
The Kidney in Obesity: Current Evidence, Perspectives and Controversies
Kounatidis, D. C., Vallianou, N. G., Stratigou, T., Voukali, M., Karampela, Ι., & Dalamaga, Μ. (2024) · Current Obesity Reports · doi:10.1007/s13679-024-00583-y · Cited by 54
Kim, J., Song, B., Lee, K., Kim, D., Kim, S., Choo, Y. ‐., Chang, K., & Koo, D. (2011) · Reproduction in Domestic Animals · doi:10.1111/j.1439-0531.2011.01969.x · Cited by 49
Seervi, M., Sobhan, P. K., Joseph, J., Mathew, K. A., & Santhoshkumar, T. R. (2013) · Cell Death and Disease · doi:10.1038/cddis.2013.502 · Cited by 49
Janssen, K., Horn, S., Niemann, M. T., Daniel, P. T., Schulze‐Osthoff, K., & Fischer, U. (2009) · Journal of Cell Science · doi:10.1242/jcs.055772 · Cited by 50
Lee, J. H., Kwon, J. H., Jeon, Y. H., Ko, K. Y., Lee, S.-R., & Kim, I. Y. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.534529 · Cited by 50
Lim, J. C., Lim, S. K., Park, M. J., Kim, G.-Y., Han, H. J., & Park, S. H. (2011) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00032.2010 · Cited by 49
Lenin, R. R., Sankaramoorthy, A., Mohan, V., & Balasubramanyam, M. (2015) · Journal of Leukocyte Biology · doi:10.1189/jlb.3a1214-609r · Cited by 53
Hussien, Y., Podojil, J. R., Robinson, A. P., Lee, A. S., Miller, S. D., & Popko, B. (2015) · Journal of Neuroscience · doi:10.1523/jneurosci.0693-15.2015 · Cited by 51
Li, K., Chen, Q., Wang, D., Duan, Q., Tian, S., He, J., Ou, Y., & Bai, D. (2016) · Cancer Medicine · doi:10.1002/cam4.895 · Cited by 49
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
Wang, C., & Xian-jin, F. (2018) · Journal of Cellular Physiology · doi:10.1002/jcp.27038 · Cited by 48
Zhao, Q., Zhong, J., Bi, Y., Liu, Y., Liu, Y., Guo, J., Pan, L., Tan, Y. L., & Yu, X. (2020) · Phytomedicine · doi:10.1016/j.phymed.2020.153306 · Cited by 49
Gurunathan, S., Jeyaraj, M., Kang, M.-H., & Kim, J. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21186792 · Cited by 49
Sestrin2 as a Potential Target for Regulating Metabolic-Related Diseases
Gong, L., Wang, Z., Wang, Z., & Zhang, Z. (2021) · Frontiers in Endocrinology · doi:10.3389/fendo.2021.751020 · Cited by 52
Kozlov, A. V., Duvigneau, J. C., Hyatt, T. C., Raju, R. P., Behling, T., Hartl, R. T., Staniek, K., Miller, I., Gregor, W., Redl, H. R., et al. (2010) · Molecular Medicine · doi:10.2119/molmed.2009.00184 · Cited by 49
Targeting Glucose Metabolism Sensitizes Pancreatic Cancer to MEK Inhibition
Yan, L., Tu, B., Yao, J., Gong, J., Carugo, A., Bristow, C. A., Wang, Q., Zhu, C., Dai, B., Kang, Y., et al. (2021) · Cancer Research · doi:10.1158/0008-5472.can-20-3792 · Cited by 48
Senescence and Apoptosis: Architects of Mammalian Development
Wanner, E., Thoppil, H., & Riabowol, K. T. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.620089 · Cited by 52
Kim, D. Y., Shin, J. Y., Lee, J. E., Kim, H., Chung, S. J., Yoo, H. S., Kim, S. J., Cho, H. J., Lee, E., Nam, S. J., et al. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2221929120 · Cited by 48
Assays for detecting the unfolded protein response.
Cawley, K., Deegan, S., Samali, A., & Gupta, S. (2011) · Methods in Enzymology · doi:10.1016/b978-0-12-385114-7.00002-7 · Cited by 48
Lin, Y., Wu, M.-H., Wei, T.-T., Lin, Y.-C., Huang, W.-C., Huang, L., Lin, Y., & Chen, C.-C. (2014) · Oncotarget · doi:10.18632/oncotarget.1628 · Cited by 48
The evolving paradigm of cell-nonautonomous UPR-based regulation of immunity by cancer cells
Zanetti, M., Rodvold, J. J., & Mahadevan, N. R. (2015) · Oncogene · doi:10.1038/onc.2015.108 · Cited by 49
Liu, J., Liu, Y., Chen, L., Wang, Y., & Li, J. (2013) · Journal of Diabetes Research · doi:10.1155/2013/630537 · Cited by 47
Wang, C., Li, T., Tang, S., Zhao, D., Zhang, C., Zhang, S., Deng, S., Zhou, Y., & Xiao, X. (2015) · Environmental Toxicology and Pharmacology · doi:10.1016/j.etap.2015.11.020 · Cited by 51
Physiological Functions of the COPI Complex in Higher Plants
Ahn, H., Kang, Y. W., Lim, H. M., Hwang, I., & Pai, H. (2015) · Molecules and Cells · doi:10.14348/molcells.2015.0115 · Cited by 48
Merlot, A. M., Shafie, N. H., Yu, Y., Richardson, V., Jansson, P. J., Sahni, S., Lane, D. J. R., Kovačević, Ž., Kalinowski, D. S., & Richardson, D. R. (2016) · Biochemical Pharmacology · doi:10.1016/j.bcp.2016.04.001 · Cited by 49
Khan, I., Paul, S., Jakhar, R., Bhardwaj, M., Han, J., & Kang, S. C. (2016) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2016.09.094 · Cited by 48
Lin, T., Lee, J. E., Oqani, R. K., Kim, S. Y., Cho, E. S., Jeong, Y. D., Baek, J. J., & Jin, D. I. (2016) · Reproductive Biology · doi:10.1016/j.repbio.2016.10.003 · Cited by 48
Bose, K., Harini, L., Krishnakumar, V., Kannan, V. R., Sundar, K., & Kathiresan, T. (2016) · APOPTOSIS · doi:10.1007/s10495-016-1318-2 · Cited by 48
Utaipan, T., Athipornchai, A., Suksamrarn, A., Chunsrivirot, S., & Chunglok, W. (2017) · Oncology Reports · doi:10.3892/or.2017.5352 · Cited by 48
Fu, Y., Liu, X., Gao, M. Q., Zhang, Y., & Liu, J. (2017) · Oncotarget · doi:10.18632/oncotarget.17862 · Cited by 48
Control of Protein Homeostasis in the Early Secretory Pathway: Current Status and Challenges
Sicari, D., Igbaria, A., & Chevet, É. (2019) · Cells · doi:10.3390/cells8111347 · Cited by 50
Yap, K. N., Yamada, K. Y. H., Zikeli, S., Kiaris, H., & Hood, W. R. (2020) · Biological reviews/Biological reviews of the Cambridge Philosophical Society · doi:10.1111/brv.12667 · Cited by 47
Quercetin and its role in modulating endoplasmic reticulum stress: A review
Eisvand, F., Tajbakhsh, A., Seidel, V., Zirak, M. R., Tabeshpour, J., & Shakeri, A. (2021) · Phytotherapy Research · doi:10.1002/ptr.7283 · Cited by 50
Westhuizen, D., Bezuidenhout, D. I., & Munro, O. Q. (2021) · Dalton Transactions · doi:10.1039/d1dt02783b · Cited by 49
Homeostatic Functions of BCL-2 Proteins beyond Apoptosis
Danial, N. N., Giménez-Cassina, A., & Tondera, D. (2010) · Advances in experimental medicine and biology · doi:10.1007/978-1-4419-6706-0_1 · Cited by 48
Metabolic Regulation of Insulin Secretion
Keane, K. N., & Newsholme, P. (2014) · Vitamins and hormones · doi:10.1016/b978-0-12-800174-5.00001-6 · Cited by 52
Chiarelli, N., Carini, G., Zoppi, N., Ritelli, M., & Colombi, M. (2018) · PLOS ONE · doi:10.1371/journal.pone.0191220 · Cited by 45
Liu, Y.-Y., Huo, D., Zeng, L.-T., Fan, G.-Q., Shen, T., Zhang, T., Cai, J., & Cui, J. (2022) · Ageing Research Reviews · doi:10.1016/j.arr.2022.101763 · Cited by 48
Metadata
- 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