The DOI matches its Crossref record; 50 of the 51 references it cites were found in a registry or an index.
Sigma-1 receptor chaperone at the ER-mitochondrion interface mediates the mitochondrion-ER-nucleus signaling for cellular survival.
Open accessAbstract
The membrane of the endoplasmic reticulum (ER) of a cell forms contacts directly with mitochondria whereby the contact is referred to as the mitochondrion-associated ER membrane or the MAM. Here we found that the MAM regulates cellular survival via an MAM-residing ER chaperone the sigma-1 receptor (Sig-1R) in that the Sig-1R chaperones the ER stress sensor IRE1 to facilitate inter-organelle signaling for survival. IRE1 is found in this study to be enriched at the MAM in CHO cells. We found that IRE1 is stabilized at the MAM by Sig-1Rs when cells are under ER stress. Sig-1Rs stabilize IRE1 and thus allow for conformationally correct IRE1 to dimerize into the long-lasting, activated endonuclease. The IRE1 at the MAM also responds to reactive oxygen species derived from mitochondria. Therefore, the ER-mitochondrion interface serves as an important subcellular entity in the regulation of cellular survival by enhancing the stress-responding signaling between mitochondria, ER, and nucleus.
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
“Inside the cell Sig-1R is located mainly at the ER–mitochondrion interface—referred to as the MAM—and regulates cellular bioenergetics, particularly under stressful conditions (Su et al., 2010; Mori et al., 2013; Hayashi, 2015).”
From The therapeutic potentials of Ayahuasca: possible effects against various diseases of civilization (2016) · cites this paper as Mori et al., 2013
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
Yoshida, H., Matsui, T., Yamamoto, A., Okada, T., & Mori, K. (2001) · Cell · doi:10.1016/s0092-8674(01)00611-0 · Cited by 4,054
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
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
IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA
Calfon, M. A., Zeng, H., Urano, F., Till, J. H., Hubbard, S. R., Harding, H. P., Clark, S. G., & Ron, D. (2002) · Nature · doi:10.1038/415092a · Cited by 2,907
Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response
Bertolotti, A., Zhang, Y., Hendershot, L. M., Harding, H. P., & Ron, D. (2000) · Nature Cell Biology · doi:10.1038/35014014 · Cited by 2,871
Mitofusin 2 tethers endoplasmic reticulum to mitochondria
de Brito, O. M., & Scorrano, L. (2008) · Nature · doi:10.1038/nature07534 · Cited by 2,442
Close Contacts with the Endoplasmic Reticulum as Determinants of Mitochondrial Ca 2+ Responses
Rizzuto, R., Pinton, P., Carrington, W., Fay, F. S., Fogarty, K. E., Lifshitz, L. M., Tuft, R. A., & Pozzan, T. (1998) · Science · doi:10.1126/science.280.5370.1763 · Cited by 2,257
Flagged first, then by citations
1 of the 51 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Items 101–200 of 320
Zhemkov, V., Geva, M., Hayden, M. R., & Борисович, Б. И. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22084082 · Cited by 50
Ivanova, A., East, M. P., Yi, S. L., & Kahn, R. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.548529 · Cited by 50
Cellular stress responses in hepatitis C virus infection: Mastering a two-edged sword
Vasallo, C., & Gastaminza, P. (2015) · Virus Research · doi:10.1016/j.virusres.2015.03.013 · Cited by 47
Prezzavento, O., Arena, E., Sánchez–Fernández, C., Turnaturi, R., Parenti, C., Marrazzo, A., Catalano, R., Amata, E., Pasquinucci, L., & Cobos, E. J. (2016) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2016.09.077 · Cited by 47
Hampel, H. J., Lista, S., Néri, C., & Vergallo, A. (2019) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2019.101662 · Cited by 47
Better to keep in touch: investigating inter‐organelle cross‐talk
Rossini, M., Pizzo, P., & Filadi, R. (2020) · FEBS Journal · doi:10.1111/febs.15451 · Cited by 49
Kuo, C., Lin, C., & Hsu, T. (2017) · Cancer Research · doi:10.1158/0008-5472.can-16-3196 · Cited by 46
The UPRosome – decoding novel biological outputs of IRE1α function
Urra, H., Pihán, P., & Hetz, C. A. (2020) · Journal of Cell Science · doi:10.1242/jcs.218107 · Cited by 45
Fernandes, T., Domingues, M. R., Moreira, P. I., & Pereira, C. (2023) · Biology · doi:10.3390/biology12030414 · Cited by 45
Knocking Out Sigma-1 Receptors Reveals Diverse Health Problems
Couly, S., Goguadze, N., Yasui, Y., Kimura, Y., Wang, S., Sharikadze, N., Wu, H.-E., & Su, T. (2020) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-020-00983-3 · Cited by 44
Self-citationQu, J., Li, M., Li, D., Xin, Y., Li, J., Song, L., Wu, W., & Liu, X. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/8836818 · Cited by 44
Overview of Sigma-1R Subcellular Specific Biological Functions and Role in Neuroprotection
Lachance, V., Bélanger, S.-M., Hay, C., Corvec, V. L., Banouvong, V., Lapalme, M., Tarmoun, K., Beaucaire, G., Lussier, M. P., & Kourrich, S. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24031971 · Cited by 46
IP 3 R at ER-Mitochondrial Contact Sites: Beyond the IP 3 R-GRP75-VDAC1 Ca 2+ Funnel
Atakpa‐Adaji, P., & Ivanova, A. (2023) · Contact · doi:10.1177/25152564231181020 · Cited by 44
Yasui, Y., & Su, T. (2016) · Journal of Drug and Alcohol Research · doi:10.4303/jdar/235970 · Cited by 42
Self-citationAlterations in Ca2+ Signalling via ER-Mitochondria Contact Site Remodelling in Cancer
Kerkhofs, M., Giorgi, C., Marchi, S., Seitaj, B., Parys, J. B., Pinton, P., Bultynck, G., & Bittremieux, M. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-981-10-4567-7_17 · Cited by 46
Sánchez‐Álvarez, M., del Pozo, M. Á., & Bakal, C. (2017) · Scientific Reports · doi:10.1038/s41598-017-16662-1 · Cited by 47
The Unfolded Protein Response in Immune Cells as an Emerging Regulator of Neuroinflammation
Fernández, D., Geisse, A., Bernales, J. I., Lira, A., & Osorio, F. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.682633 · Cited by 44
Mitochondria‐Associated Endoplasmic Reticulum Membranes in Human Health and Diseases
Liu, Y., Mao, Z., Huang, J., Wang, H., Zhang, X., Zhou, X., Xu, Y., Pan, S., Liu, D., Liu, Z., et al. (2025) · MedComm · doi:10.1002/mco2.70259 · Cited by 42
Happy, M., Dejoie, J., Zajac, C. K., Cortez, B., Chakraborty, K., Aderemi, J., & Sauane, M. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.12.029 · Cited by 41
Sigma receptors as potential therapeutic targets for neuroprotection
Nguyen, L., Kaushal, N., Robson, M. J., & Matsumoto, R. R. (2014) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2014.09.022 · Cited by 41
Chaperone Sigma1R and Antidepressant Effect
Воронин, М. В., Vakhitova, Y. V., & Середенин, С. Б. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21197088 · Cited by 41
Lee, P.-T., Liévens, J.-C., Wang, S., Chuang, J., Khalil, B., Wu, H.-E., Chang, W., Maurice, T., & Su, T. (2020) · Nature Communications · doi:10.1038/s41467-020-19396-3 · Cited by 41
Self-citationMunguía-Galaviz, F. J., Miranda‐Díaz, A. G., Cárdenas-Sosa, M. A., & Echavarría, R. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24031997 · Cited by 40
Cantonero, C., Camello, P. J., Abate, C., Berardi, F., Salido, G. M., Rosado, J. A., & Redondo, P. C. (2020) · Cancers · doi:10.3390/cancers12020257 · Cited by 38
Shi, M., Liu, L., Min, X., Mi, L., Chai, Y., Chen, F., Wang, J., Yue, S., Zhang, J., Deng, Q., et al. (2022) · Journal of Clinical Medicine · doi:10.3390/jcm11092348 · Cited by 37
Loss of Sigma‐1 Receptor Chaperone Promotes Astrocytosis and Enhances the Nrf2 Antioxidant Defense
Weng, T.-Y., Hung, D. T., Su, T., & Tsai, S. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/4582135 · Cited by 38
Self-citationRole of Sigma-1 Receptor in Calcium Modulation: Possible Involvement in Cancer
Pontisso, I., & Combettes, L. (2021) · Genes · doi:10.3390/genes12020139 · Cited by 37
Mind the Gap: Mitochondria and the Endoplasmic Reticulum in Neurodegenerative Diseases
Leal, N. S., & Martins, L. M. (2021) · Biomedicines · doi:10.3390/biomedicines9020227 · Cited by 40
Involvement of ion channels and transporters in carcinoma angiogenesis and metastasis
Martial, S. (2016) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00218.2015 · Cited by 36
Zhang, Q., Chen, W., Zhang, B., Zhang, Y., Xiao, Y., An, Y., Han, L., Deng, H., Yao, S., Wang, H., et al. (2022) · Food and Chemical Toxicology · doi:10.1016/j.fct.2022.113592 · Cited by 35
Borbély, E., Varga, V. É., Szögi, T., Schuster, I., Bozsó, Z., Penke, B., & Fülöp, L. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23052514 · Cited by 35
Amyloid toxicity is enhanced after pharmacological or genetic invalidation of the σ1 receptor
Maurice, T., Strehaïano, M., Duhr, F., & Chevallier, N. (2017) · Behavioural Brain Research · doi:10.1016/j.bbr.2017.11.010 · Cited by 34
Connection Lost, MAM: Errors in ER–Mitochondria Connections in Neurodegenerative Diseases
Johri, A., & Chandra, A. (2021) · Brain Sciences · doi:10.3390/brainsci11111437 · Cited by 34
Sigma 1 Receptor and Its Pivotal Role in Neurological Disorders
Shokr, M. M., Badawi, G. A., Elshazly, S. M., Zaki, H. F., & Mohamed, A. F. (2024) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.4c00564 · Cited by 33
Sigma-1 receptor is a key genetic modulator in amyotrophic lateral sclerosis
Couly, S., Khalil, B., Viguier, V., Roussel, J., Maurice, T., & Liévens, J.-C. (2019) · Human Molecular Genetics · doi:10.1093/hmg/ddz267 · Cited by 33
Morihara, R., Yamashita, T., Liu, X., Nakano, Y., Fukui, Y., Sato, K., Ohta, Y., Hishikawa, N., Shang, J., & Abe, K. (2018) · Journal of Neuroscience Research · doi:10.1002/jnr.24270 · Cited by 32
Sigma-1 (σ1) receptor activity is necessary for physiological brain plasticity in mice
Crouzier, L., Couly, S., Roques, C., Peter, C., Belkhiter, R., Jacquemin, M. A., Bonetto, A., Delprat, B., & Maurice, T. (2020) · European Neuropsychopharmacology · doi:10.1016/j.euroneuro.2020.08.010 · Cited by 31
Lasbleiz, C., Peyrel, A., Tarot, P., Sarniguet, J., Crouzier, L., Cubedo, N., Delprat, B., Rossel, M., Maurice, T., & Liévens, J.-C. (2022) · Redox Biology · doi:10.1016/j.redox.2022.102542 · Cited by 31
Sigma-1 receptor activation alleviates blood-brain barrier dysfunction in vascular dementia mice
Liu, D., Chi, T., Ji, X., Liu, P., Qi, X., Zhu, L., Wang, Z., Li, L., Chen, L., & Zou, L. (2018) · Experimental Neurology · doi:10.1016/j.expneurol.2018.07.002 · Cited by 31
Targeting Sigma-1 Receptor: A Promising Strategy in the Treatment of Parkinson’s Disease
Siddiqui, T., & Bhatt, L. K. (2023) · Neurochemical Research · doi:10.1007/s11064-023-03960-6 · Cited by 30
Воронин, М. В., Андреевич, К. И., Воронков, Д. Н., & Середенин, С. Б. (2019) · Scientific Reports · doi:10.1038/s41598-019-53413-w · Cited by 31
SIGMAR1 Confers Innate Resilience against Neurodegeneration
Couly, S., Yasui, Y., & Su, T. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24097767 · Cited by 29
Self-citationAbatematteo, F. S., Niso, M., Contino, M., Leopoldo, M., & Abate, C. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22126359 · Cited by 31
Koshenov, Z., Oflaz, F. E., Hirtl, M., Pilic, J., Bachkoenig, O. A., Gottschalk, B., Madreiter‐Sokolowski, C. T., Rost, R., Malli, R., & Graier, W. F. (2021) · Metabolites · doi:10.3390/metabo11070422 · Cited by 29
Yao, X., Zhu, J., Li, L., Yang, B., Chen, B., Bao, E., & Zhang, X. (2023) · Biochemical Pharmacology · doi:10.1016/j.bcp.2023.115434 · Cited by 29
The Sigma Receptors in Alzheimer’s Disease: New Potential Targets for Diagnosis and Therapy
Wang, T., & Jia, H. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241512025 · Cited by 30
Guo, M., Liu, R., Zhang, F., Qu, J., Yang, Y., & Li, X. (2024) · Pharmacological Research · doi:10.1016/j.phrs.2024.107409 · Cited by 32
Hussain, Y., Khan, H. Z., Efferth, T., & Alam, W. (2022) · Phytomedicine · doi:10.1016/j.phymed.2022.153985 · Cited by 28
Fu, F., & Doroudgar, S. (2022) · Current Opinion in Physiology · doi:10.1016/j.cophys.2022.100552 · Cited by 31
Mancuso, R., del Valle, J., Morell, M., Pallàs, M., Osta, R., & Navarro, X. (2014) · Orphanet Journal of Rare Diseases · doi:10.1186/1750-1172-9-78 · Cited by 28
Ye, W., Jiang, Z., Lu, X., Ren, X., Deng, M., Lin, S., Xiao, Y., Lin, S., Wang, S., Li, B., et al. (2016) · Oncotarget · doi:10.18632/oncotarget.10881 · Cited by 29
Wang, J., SAUL, A. B., Cui, X., Roon, P., & Smith, S. B. (2017) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.17-21947 · Cited by 28
Chaperone-Dependent Mechanisms as a Pharmacological Target for Neuroprotection
Воронин, М. В., Абрамова, Е. В., Verbovaya, E. R., Vakhitova, Y. V., & Середенин, С. Б. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24010823 · Cited by 27
Sigma 1 receptor activation modifies intracellular calcium exchange in the G93AhSOD1 ALS model
Tadić, V., Malci, A., Goldhammer, N., Stubendorff, B., Sengupta, S., Prell, T., Keiner, S., Liu, J., Guenther, M., Frahm, C., et al. (2017) · Neuroscience · doi:10.1016/j.neuroscience.2017.07.012 · Cited by 27
Mitochondria Associated Membranes (MAMs): Emerging Drug Targets for Diabetes
Sasi, U. S. S., Ganapathy, S., Palayyan, S. R., & Gopalan, R. K. (2019) · Current Medicinal Chemistry · doi:10.2174/0929867326666190212121248 · Cited by 26
Proulx, J. M., Park, I.-W., & Borgmann, K. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.715945 · Cited by 25
Fujii, C., Zorumski, C. F., & Izumi, Y. (2023) · Neural Regeneration Research · doi:10.4103/1673-5374.391334 · Cited by 25
The Sigma-1 Receptor–A Therapeutic Target for the Treatment of ALS?
Mavlyutov, T. A., Baker, E. M., Losenegger, T. M., Kim, J. R., Torres, B., Epstein, M. L., & Ruoho, A. E. (2017) · Advances in Experimental Medicine and Biology · doi:10.1007/978-3-319-50174-1_17 · Cited by 24
Implication of Endoplasmic Reticulum Stress in Autism Spectrum Disorder
Kawada, K., & Mimori, S. (2017) · Neurochemical Research · doi:10.1007/s11064-017-2370-1 · Cited by 25
Enkirch, T., Sauber, S., Anderson, D. E., Gan, E. S., Kenanov, D., Maurer‐Stroh, S., & von Messling, V. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.01097 · Cited by 24
Role of Sigma-1 Receptor in Cocaine Abuse and Neurodegenerative Disease
Cai, Y. C., Yang, L., Niu, F., Liao, K., & Buch, S. J. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-50174-1_12 · Cited by 24
Protein Localization at Mitochondria-ER Contact Sites in Basal and Stress Conditions
Ilacqua, N., Sánchez‐Álvarez, M., Bachmann, M., Costiniti, V., del Pozo, M. Á., & Giacomello, M. (2017) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2017.00107 · Cited by 23
An, Y., Qi, Y. A., Li, Y., Li, Z., Yang, C., & Dong, J. (2022) · Neuroscience Letters · doi:10.1016/j.neulet.2022.136528 · Cited by 23
Cardiac Sigma Receptors – An Update
Stračina, T., & Nováková, M. (2018) · Physiological Research · doi:10.33549/physiolres.934052 · Cited by 23
Involvement of Chaperone Sigma1R in the Anxiolytic Effect of Fabomotizole
Воронин, М. В., Vakhitova, Y. V., Tsypysheva, I. P., Tsypyshev, D. O., Rybina, I. V., Kurbanov, R. D., Абрамова, Е. В., & Середенин, С. Б. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22115455 · Cited by 22
Chaperones vs. oxidative stress in the pathobiology of ischemic stroke
Soldatov, V. O., Venediktov, A. A., Белых, А. Е., Piavchenko, G. A., Naimzada, M. D., Ogneva, N., Kartashkina, N. L., & Bushueva, O. Y. (2024) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2024.1513084 · Cited by 22
Zampieri, D., Laurini, E., Vio, L., Fermeglia, M., Pricl, S., Wünsch, B., Schepmann, D., & Mamolo, M. G. (2014) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2014.12.018 · Cited by 22
Inositol Requiring Enzyme (IRE), a multiplayer in sensing endoplasmic reticulum stress
Zhou, Z., Wang, Q., & Michalak, M. (2021) · Animal Cells and Systems · doi:10.1080/19768354.2021.2020901 · Cited by 22
Records of RNA locations in living yeast revealed through covalent marks
Medina-Muñoz, H. C., Lapointe, C. P., Porter, D. F., & Wickens, M. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1921408117 · Cited by 23
Central role of Sigma-1 receptor in ochratoxin A-induced ferroptosis
Chen, W., Han, L., Yang, R., Wang, H., Yao, S., Deng, H., Liu, S., Zhou, Y., & Shen, X. L. (2024) · Archives of Toxicology · doi:10.1007/s00204-024-03805-3 · Cited by 21
Sansbury, S. E., Serebrenik, Y. V., Lapidot, T., Smith, D. G., Burslem, G. M., & Shalem, O. (2023) · Molecular Cell · doi:10.1016/j.molcel.2025.04.002 · Cited by 22
Drug Screening Identifies Sigma-1-Receptor as a Target for the Therapy of VWM Leukodystrophy
Atzmon, A., Herrero, M., Sharet-Eshed, R., Gilad, Y., Senderowitz, H., & Elroy‐Stein, O. (2018) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2018.00336 · Cited by 21
Mitochondria–membranous organelle contacts at a glance
Diokmetzidou, A., & Scorrano, L. (2025) · Journal of Cell Science · doi:10.1242/jcs.263895 · Cited by 23
Tesei, A., Cortesi, M., Pignatta, S., Arienti, C., Dondio, G. M., Bigogno, C., Malacrida, A., Miloso, M., Meregalli, C., Chiorazzi, A., et al. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.00490 · Cited by 20
Ververis, A., Dajani, R. B., Koutsou, P., Aloqaily, A., Nelson-Williams, C. J., Loring, E. C., Arafat, A., Mubaidin, A. F., Horany, K., Bader, M., et al. (2019) · Journal of Medical Genetics · doi:10.1136/jmedgenet-2019-106108 · Cited by 20
Role of IRE1α in podocyte proteostasis and mitochondrial health
Navarro‐Betancourt, J. R., Papillon, J., Guillemette, J., Iwawaki, T., Chung, C.-F., & Cybulsky, A. V. (2020) · Cell Death Discovery · doi:10.1038/s41420-020-00361-4 · Cited by 20
Parakh, S., & Atkin, J. D. (2021) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2021.02.002 · Cited by 20
Amodio, G., Pagliara, V., Moltedo, O., & Remondelli, P. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.641194 · Cited by 20
MAM-mediated mitophagy and endoplasmic reticulum stress: the hidden regulators of ischemic stroke
Jia, Z., Li, H., Xu, K., Li, R., Yang, S., Chen, L., Zhang, Q., Li, S., & Sun, X. (2024) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2024.1470144 · Cited by 19
Monaghan, R. M. (2025) · Open Biology · doi:10.1098/rsob.240287 · Cited by 19
Sereti, E., Tsimplouli, C., Kalaitsidou, E., Sakellaridis, N., & DIMAS, K. S. (2021) · Biomedicines · doi:10.3390/biomedicines9010038 · Cited by 22
Xie, W., Chen, M., Loor, J. J., Song, X., Ma, N., Zhou, S., Zhang, H., Chang, G., & Shen, X. (2023) · Journal of Dairy Science · doi:10.3168/jds.2022-22879 · Cited by 18
An Emerging Role for Sigma Receptor 1 in Personalized Treatment of Breast Cancer
Robinson, T. S., & Osman, M. A. (2023) · Cancers · doi:10.3390/cancers15133464 · Cited by 18
Abdullah, C. S., Aishwarya, R., Alam, S., Remex, N. S., Morshed, M., Nitu, S. S., Miriyala, S., Panchatcharam, M., Hartman, B., King, J., et al. (2021) · Mitochondrion · doi:10.1016/j.mito.2021.12.002 · Cited by 18
Martin, P., Maurice, T., Gammaitoni, A. R., Farfel, G. M., Boyd, B., & Galer, B. S. (2022) · Epilepsy & Behavior · doi:10.1016/j.yebeh.2021.108526 · Cited by 17
Are Sigma Receptor Modulators a Weapon Against Multiple Sclerosis Disease?
Collina, S., Rui, M., Stotani, S., Bignardi, E., Rossi, D., Curti, D., Giordanetto, F., Malacrida, A., Scuteri, A., & Cavaletti, G. (2017) · Future Medicinal Chemistry · doi:10.4155/fmc-2017-0122 · Cited by 17
Borde, P., Cosgrove, N. S., Charmsaz, S., Safrany, S. T., & Young, L. S. (2022) · Cancer Gene Therapy · doi:10.1038/s41417-022-00552-4 · Cited by 16
Kulkarni, P. G., Mohire, V. M., Waghmare, P. P., & Banerjee, T. (2024) · Mitochondrion · doi:10.1016/j.mito.2024.101874 · Cited by 16
Peeking into Sigma-1 Receptor Functions Through the Retina
Mavlyutov, T. A., & Guo, L. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-50174-1_19 · Cited by 16
Sigma-1 receptor and amyotrophic lateral sclerosis
Benarroch, E. E. (2018) · Neurology · doi:10.1212/wnl.0000000000006347 · Cited by 16
Erratum: Proteostasis control by the unfolded protein response
Hetz, C. A., Chevet, É., & Oakes, S. A. (2015) · Nature Cell Biology · doi:10.1038/ncb3221 · Cited by 19
Wang, Y., Zhang, Y., Jin, Q., Zhao, H., & Li, P. (2025) · Cell Death and Disease · doi:10.1038/s41419-025-08236-1 · Cited by 15
Yao, S., Chen, W., Wang, H., Yang, R., Zhou, Y., Liu, S., & Shen, X. L. (2024) · Food Science and Human Wellness · doi:10.26599/fshw.2024.9250372 · Cited by 15
Contribution of Sigma‐1 receptor to cytoprotective effect of afobazole
Воронин, М. В., & Андреевич, К. И. (2016) · Pharmacology Research & Perspectives · doi:10.1002/prp2.273 · Cited by 15
Pereira, A. C., Madeira, N. G. G. F., Morais, S., Macedo, A., Cruz, M. T., & Pereira, C. (2022) · Cells · doi:10.3390/cells11030433 · Cited by 16
Cagalinec, M., Mohd, A., Borecká, S., Bultynck, G., Choubey, V., Yanovsky‐Dagan, S., Ezer, S., Gašperíková, D., Harel, T., Jurkovičová, D., et al. (2025) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2025.119954 · Cited by 15
Repurposing Sigma-1 Receptor-Targeting Drugs for Therapeutic Advances in Neurodegenerative Disorders
Eskandari, K., Bélanger, S.-M., Lachance, V., & Kourrich, S. (2025) · Pharmaceuticals · doi:10.3390/ph18050700 · Cited by 15
Sarkar, R., Rao, K. B. N., Jha, M. P., & Mapa, K. (2022) · Cell Stress and Chaperones · doi:10.1007/s12192-022-01264-2 · Cited by 14
The regulatory role of endoplasmic reticulum chaperone proteins in neurodevelopment
Sun, H., Wu, M., Wang, M., Zhang, X., & Zhu, J. Z. (2022) · Frontiers in Neuroscience · doi:10.3389/fnins.2022.1032607 · Cited by 14
Calmodulin regulates MGRN1‐GP78 interaction mediated ubiquitin proteasomal degradation system
Mukherjee, R., Bhattacharya, A., Sau, A., Basil, S., Chakrabarti, S., & Chakrabarti, O. (2018) · The FASEB Journal · doi:10.1096/fj.201701413rrr · Cited by 14
Metadata
- Authors
- Mori, T., Hayashi, T., Hayashi, E., & Su, T.-P.
- Affiliations
- United States Department of Health and Human Services (US)
- Corresponding author
- Su, Tsung-Ping
- Venue
- PLoS ONE
- Publisher
- Public Library of Science (PLoS)
- Published
- 2013-10-18
- Volume
- 8
- Issue
- 10
- Pages
- e76941
- ISSN
- 1932-6203 (ISSN-L)
- PMC
- PMC3799859
- OpenAlex
- W1994289493
- Cited by
- 317
- References
- 51
- Citations by year
- 2026: 22 · 2025: 24 · 2024: 20 · 2023: 29 · 2022: 26 · 2021: 38 · 2020: 33 · 2019: 34 · 2018: 18 · 2017: 29 · 2016: 16 · 2015: 10 · 2014: 17
- FWCI
- 8.51
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- PLoS ONE (publishedVersion, public-domain)
- Europe PMC (PubMed Central) (publishedVersion, public-domain)
- PubMed Central (publishedVersion, public-domain)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Figshare (submittedVersion, cc-by)
- Funders
- U.S. Department of Health and Human Services
- National Institutes of Health
- National Institute on Drug Abuse
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
- Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Pharmacology › Pharmacological Receptor Mechanisms and Effects
- Life Sciences › Neuroscience › Sensory Systems › Ion Channels and Receptors
- Keywords
- sigma-1 receptor, mitochondria-associated membranes, endoplasmic reticulum, IRE1, endoplasmic reticulum stress, mitochondrial reactive oxygen species, molecular chaperones, protein stabilization, endonuclease activation, cell survival
- MeSH terms
- Sigma-1 Receptor, Animals, Cell Nucleus, Cell Survival, Cricetulus, Endoplasmic Reticulum, Endoribonucleases, Cricetinae, HeLa Cells, Humans, Immunohistochemistry, Intracellular Membranes, Mitochondria, Mutation, Protein Binding, Blotting, Western, Signal Transduction, CHO Cells, Protein Serine-Threonine Kinases, Reactive Oxygen Species, Receptors, sigma, Microscopy, Confocal, Molecular Chaperones, RNA Interference, Cell Line, Tumor, 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