Protein misfolding in the endoplasmic reticulum as a conduit to human disease

Control 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

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

Endoplasmic Reticulum Stress Links Obesity, Insulin Action, and Type 2 Diabetes

Özcan, U., Cao, Q., Yilmaz, E., Lee, A.-H., Iwakoshi, N. N., Özdelen, E., Tuncman, G., Görgün, C., Glimcher, L. H., & Hotamisligil, G. S. (2004) · Science · doi:10.1126/science.1103160 · Cited by 3,844

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

CHOP induces death by promoting protein synthesis and oxidation in the stressed endoplasmic reticulumPreprint

Marciniak, S. J., Yun, C. Y., Oyadomari, S., Novoa, I., Zhang, Y., Jungreis, R., Nagata, K., Harding, H. P., & Ron, D. (2004) · Genes & Development · doi:10.1101/gad.1250704 · Cited by 2,066

CHOP is implicated in programmed cell death in response to impaired function of the endoplasmic reticulumPreprint

Zinszner, H., Kuroda, M., Wang, X., Batchvarova, N., Lightfoot, R. T., Remotti, H. E., Stevens, J. L., & Ron, D. (1998) · Genes & Development · doi:10.1101/gad.12.7.982 · Cited by 2,039

From endoplasmic-reticulum stress to the inflammatory response

Zhang, K., & Kaufman, R. J. (2008) · Nature · doi:10.1038/nature07203 · Cited by 2,010

Reactive Oxygen Species Promote TNFα-Induced Death and Sustained JNK Activation by Inhibiting MAP Kinase Phosphatases

Kamata, H., Honda, S.-I., Maeda, S., Chang, L., Hirata, H., & Karin, M. (2005) · Cell · doi:10.1016/j.cell.2004.12.041 · Cited by 1,792

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

Han, J., Back, S. H., Hur, J., Lin, Y.-H., Gildersleeve, R., Shan, J., Yuan, C. L., Krokowski, D., Wang, S., Hatzoglou, M., et al. (2013) · Nature Cell Biology · doi:10.1038/ncb2738 · Cited by 1,691

XBP1 Links ER Stress to Intestinal Inflammation and Confers Genetic Risk for Human Inflammatory Bowel Disease

Kaser, A., Lee, A., Franke, A., Glickman, J. N., Zeißig, S., Tilg, H., Nieuwenhuis, E. E. S., Higgins, D. E., Schreiber, S., Glimcher, L. H., et al. (2008) · Cell · doi:10.1016/j.cell.2008.07.021 · Cited by 1,465

Defective Mitochondrial tRNA Taurine Modification Activates Global Proteostress and Leads to Mitochondrial Disease

Fakruddin, M., Wei, F., Suzuki, T., Asano, K., Kaieda, T., Omori, A., Izumi, R., Fujimura, A., Kaitsuka, T., Miyata, K., et al. (2018) · Cell Reports · doi:10.1016/j.celrep.2017.12.051 · Cited by 124

The Hydroxyquinoline Analogue YUM70 Inhibits GRP78 to Induce ER Stress–Mediated Apoptosis in Pancreatic Cancer

Samanta, S., Yang, S., Debnath, B., Xue, D., Kuang, Y., Ramkumar, K., Lee, A. S., Ljungman, M. E., & Neamati, N. (2021) · Cancer Research · doi:10.1158/0008-5472.can-20-1540 · Cited by 120

Astragaloside IV alleviates septic myocardial injury through DUSP1-Prohibitin 2 mediated mitochondrial quality control and ER-autophagy

Wang, J., Pu, X., Zhuang, H., Guo, Z., Wang, M., Yang, H., Li, C., & Chang, X. (2024) · Journal of Advanced Research · doi:10.1016/j.jare.2024.10.030 · Cited by 119

Physiological/pathological ramifications of transcription factors in the unfolded protein responsePreprint

Han, J., & Kaufman, R. J. (2017) · Genes & Development · doi:10.1101/gad.297374.117 · Cited by 120

The unfolded protein response as a target for anticancer therapeutics

Wang, M., Law, M. E., Castellano, R. K., & Law, B. K. (2018) · Critical Reviews in Oncology/Hematology · doi:10.1016/j.critrevonc.2018.05.003 · Cited by 121

Emerging Principles of Selective ER Autophagy

Wilkinson, S. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.05.012 · Cited by 117

LOXL2 drives epithelial-mesenchymal transition via activation of IRE1-XBP1 signalling pathway

Cuevas, E. P., Eraso, P., Mazón, M. J., Santos, V., Moreno‐Bueno, G., Cano, A., & Portillo, F. (2017) · Scientific Reports · doi:10.1038/srep44988 · Cited by 116

IRE1α prevents hepatic steatosis by processing and promoting the degradation of select microRNAs

Wang, J., Qiu, Y., Yang, Z., Kim, H., Qian, Q., Sun, Q., Zhang, C., Yin, L., Fang, D., Back, S. H., et al. (2018) · Science Signaling · doi:10.1126/scisignal.aao4617 · Cited by 116

Mitochondria-Associated Membranes and ER Stress

van Vliet, A. R., & Agostinis, P. (2017) · Current topics in microbiology and immunology · doi:10.1007/82_2017_2 · Cited by 116

Anti-inflammatory and antioxidant properties of leaf extracts of eleven South African medicinal plants used traditionally to treat inflammation

Ondua, M., Njoya, E. M., Abdalla, M. A., & McGaw, L. J. (2018) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2018.12.030 · Cited by 113

Rescue of α-synuclein aggregation in Parkinson’s patient neurons by synergistic enhancement of ER proteostasis and protein trafficking

Stojkovska, I., Wani, W. Y., Zunke, F., Belur, N. R., Pavlenko, E. A., Mwenda, N., Sharma, K., Francelle, L., & Mazzulli, J. R. (2021) · Neuron · doi:10.1016/j.neuron.2021.10.032 · Cited by 116

p62/ SQSTM 1—Dr. Jekyll and Mr. Hyde that prevents oxidative stress but promotes liver cancer

Taniguchi, K., Yamachika, S., He, F., & Karin, M. (2016) · FEBS Letters · doi:10.1002/1873-3468.12301 · Cited by 117

Lactobacillus rhamnosus GG supplementation modulates the gut microbiota to promote butyrate production, protecting against deoxynivalenol exposure in nude mice

Lin, R., Sun, Y., Mu, P., Zheng, T., Mu, H., Deng, F., Deng, Y., & Wen, J. (2020) · Biochemical Pharmacology · doi:10.1016/j.bcp.2020.113868 · Cited by 115

ATF4 in cellular stress, ferroptosis, and cancer

Tang, H., Kang, R., Liu, J., & Tang, D. (2024) · Archives of Toxicology · doi:10.1007/s00204-024-03681-x · Cited by 117

Disruption of IRE1α through its kinase domain attenuates multiple myeloma

Harnoss, J. M., Le Thomas, A., Shemorry, A., Marsters, S. A., Lawrence, D. A., Lu, M., Chen, Y.-C. A., Qing, J., Totpal, K., Kan, D., et al. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1906999116 · Cited by 109

Genetic risk in chronic pancreatitis: the misfolding-dependent pathway

Sahin‐Tóth, M. (2017) · Current Opinion in Gastroenterology · doi:10.1097/mog.0000000000000380 · Cited by 109

Phosphorylation switches protein disulfide isomerase activity to maintain proteostasis and attenuate ER stress

Yu, J., Li, T., Liu, Y., Wang, X., Zhang, J., Xie, W., Shi, G., Lou, J., Wang, L., Wang, C., et al. (2020) · The EMBO Journal · doi:10.15252/embj.2019103841 · Cited by 108

ATF6 aggravates acinar cell apoptosis and injury by regulating p53/AIFM2 transcription in Severe Acute Pancreatitis

Tan, J., Cao, R.-C., Zhou, L., Zhou, Z., Chen, H., Xu, J. M., Chen, X., Jin, Y.-C., Lin, J., Zeng, J.-L., et al. (2020) · Theranostics · doi:10.7150/thno.46934 · Cited by 107

Adiponectin reduces ER stress-induced apoptosis through PPARα transcriptional regulation of ATF2 in mouse adipose

Liu, Z., Gan, L., Wu, T., Feng, F., Luo, D., Gu, H., Liu, S., & Sun, C. (2016) · Cell Death and Disease · doi:10.1038/cddis.2016.388 · Cited by 106

Endoplasmic reticulum chaperones tweak the mitochondrial calcium rheostat to control metabolism and cell death

Gutiérrez, T., & Simmen, T. (2018) · Cell Calcium · doi:10.1016/j.ceca.2017.05.015 · Cited by 104

FICD acts bifunctionally to AMPylate and de-AMPylate the endoplasmic reticulum chaperone BiP

Preißler, S., Rato, C., Perera, L. A., Saudek, V., & Ron, D. (2016) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3337 · Cited by 104

ER Stress: A Therapeutic Target in Rheumatoid Arthritis?

Rahmati, M., Moosavi, M. A., & McDermott, M. (2018) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2018.03.010 · Cited by 103

The Cross-Links of Endoplasmic Reticulum Stress, Autophagy, and Neurodegeneration in Parkinson’s Disease

Ren, H., Zhai, W., Lu, X., & Wang, G. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.691881 · Cited by 106

Protective effects of Astragaloside IV on endoplasmic reticulum stress-induced renal tubular epithelial cells apoptosis in type 2 diabetic nephropathy rats

Ju, Y., Su, Y., Chen, Q., Ma, K., Ji, T., Wang, Z., Li, W., & Li, W. (2018) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2018.10.041 · Cited by 97

Cellular stress in the pathogenesis of nonalcoholic steatohepatitis and liver fibrosis

Sharma, S. K., Guillou, D. L., & Chen, J. Y. (2023) · Nature Reviews Gastroenterology & Hepatology · doi:10.1038/s41575-023-00832-w · Cited by 100

Lipotoxicity-driven metabolic dysfunction-associated steatotic liver disease (MASLD)

Iturbe-Rey, S., Maccali, C., Arrese, M. A., Aspichueta, P., de Oliveira, C. P. M. S., Castro, R. E., Lapitz, A., Izquierdo‐Sánchez, L., Bujanda, L., Perugorria, M. J., et al. (2024) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2024.119053 · Cited by 102

ER Stress Inhibits Liver Fatty Acid Oxidation while Unmitigated Stress Leads to Anorexia-Induced Lipolysis and Both Liver and Kidney Steatosis

DeZwaan-McCabe, D., Sheldon, R. D., Gorecki, M. C., Guo, D., Gansemer, E. R., Kaufman, R. J., Rahmouni, K., Gillum, M. P., Taylor, E. B., Teesch, L. M., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.05.020 · Cited by 97

Significance of prohibitin domain family in tumorigenesis and its implication in cancer diagnosis and treatment

Yang, J., Li, B., & He, Q. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-0661-3 · Cited by 98

Unfolded protein response IRE1/XBP1 signaling is required for healthy mammalian brain aging

Cabral‐Miranda, F., Tamburini, G., Martínez, G., Ardiles, Á. O., Medinas, D. B., Gerakis, Y., Hung, M.-L. D., Vidal, R. L., Fuentealba, M., Miedema, T., et al. (2022) · The EMBO Journal · doi:10.15252/embj.2022111952 · Cited by 99

Sephin1, which prolongs the integrated stress response, is a promising therapeutic for multiple sclerosis

Chen, Y., Podojil, J. R., Kunjamma, R. B., Jones, J. S., Weiner, M., Lin, W., Miller, S. D., & Popko, B. (2018) · Brain · doi:10.1093/brain/awy322 · Cited by 99

PDIA1/P4HB is required for efficient proinsulin maturation and ß cell health in response to diet induced obesity

Jang, I., Pottekat, A., Poothong, J., Yong, J., Lagunas-Acosta, J., Charbono, A., Chen, Z., Scheuner, D., Liu, M. R., Itkin‐Ansari, P., et al. (2019) · eLife · doi:10.7554/elife.44528 · Cited by 96

Roles of sleep deprivation in cardiovascular dysfunctions

Liu, H., & Chen, A. (2019) · Life Sciences · doi:10.1016/j.lfs.2019.01.006 · Cited by 93

Toxicogenomic module associations with pathogenesis: a network-based approach to understanding drug toxicity

Sutherland, J. J., Webster, Y., Willy, J. A., Searfoss, G. H., Goldstein, K. M., Irizarry, A. R., Hall, D. G., & Stevens, J. L. (2017) · The Pharmacogenomics Journal · doi:10.1038/tpj.2017.17 · Cited by 95

Effects of white light‐emitting diode ( LED ) exposure on retinal pigment epithelium in vivo

Jaadane, I., Rodriguez, G. E. V., Boulenguez, P., Chahory, S., Carré, S., Savoldelli, M., Jonet, L., Béhar‐Cohen, F., Martinsons, C., & Torriglia, A. (2017) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.13255 · Cited by 92

Silver nanoparticles induce SH-SY5Y cell apoptosis via endoplasmic reticulum- and mitochondrial pathways that lengthen endoplasmic reticulum-mitochondria contact sites and alter inositol-3-phosphate receptor function

Li, L., Cui, J., Liu, Z., Zhou, X., Li, Z., Yu, Y., Jia, Y., Zuo, D., & Wu, Y. (2018) · Toxicology Letters · doi:10.1016/j.toxlet.2018.01.004 · Cited by 93

IRE1α Disruption in Triple-Negative Breast Cancer Cooperates with Antiangiogenic Therapy by Reversing ER Stress Adaptation and Remodeling the Tumor Microenvironment

Harnoss, J. M., Thomas, A. L., Reichelt, M., Guttman, O., Wu, T. D., Marsters, S. A., Shemorry, A., Lawrence, D. A., Kan, D., Segal, E., et al. (2020) · Cancer Research · doi:10.1158/0008-5472.can-19-3108 · Cited by 94

Genotoxic stress triggers the activation of IRE1α-dependent RNA decay to modulate the DNA damage response

Dufey, E., Pedro, J. M. B., Eggers, C., González-Quiroz, M., Urra, H., Sagredo, A. I., Sepúlveda, D., Pihán, P., Carreras‐Sureda, A., Hazari, Y., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-15694-y · Cited by 92

Therapeutic role of sirtuins in neurodegenerative disease and their modulation by polyphenols

Ajami, M., Pazoki–Toroudi, H., Amani, H., Nabavi, S. F., Braidy, N., Vacca, R. A., Atanasov, A. G., MOCAN, A., & Nabavi, S. M. (2016) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2016.11.022 · Cited by 94

Increased mitochondrial respiration promotes survival from endoplasmic reticulum stress

Knupp, J., Arvan, P., & Chang, A. (2018) · Cell Death and Differentiation · doi:10.1038/s41418-018-0133-4 · Cited by 94

Berberine ameliorates oxidative stress-induced apoptosis by modulating ER stress and autophagy in human nucleus pulposus cells

Luo, R., Liao, Z., Song, Y., Yin, H., Zhan, S., Li, G., Ma, L., Lu, S., Wang, K., Li, S., et al. (2019) · Life Sciences · doi:10.1016/j.lfs.2019.04.064 · Cited by 91

Chemical chaperone, TUDCA unlike PBA, mitigates protein aggregation efficiently and resists ER and non-ER stress induced HepG2 cell death

Uppala, J. K., Gani, A. R., & Ramaiah, K. V. A. (2017) · Scientific Reports · doi:10.1038/s41598-017-03940-1 · Cited by 90

Sex differences in particulate air pollution-related cardiovascular diseases: A review of human and animal evidence

Liao, M., Braunstein, Z., & Rao, X. (2023) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2023.163803 · Cited by 90

Tauopathies: Deciphering Disease Mechanisms to Develop Effective Therapies

Silva, M. C., & Haggarty, S. J. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21238948 · Cited by 89

Mild endoplasmic reticulum stress ameliorates lipopolysaccharide-induced neuroinflammation and cognitive impairment via regulation of microglial polarization

Wang, Y., Zhou, Q., Zhang, X., Qian, Q.-Q., Xu, J., Ni, P., & Qian, Y. (2017) · Journal of Neuroinflammation · doi:10.1186/s12974-017-1002-7 · Cited by 86

CDNF Protein Therapy in Parkinson’s Disease

Huttunen, H. J., & Saarma, M. (2019) · Cell Transplantation · doi:10.1177/0963689719840290 · Cited by 88

Endoplasmic reticulum stress in nonalcoholic (metabolic associated) fatty liver disease (NAFLD/MAFLD)

Flessa, C., Kyrou, I., Ansari, N. N., Kaltsas, G., Kassi, E. N., & Randeva, H. S. (2022) · Journal of Cellular Biochemistry · doi:10.1002/jcb.30247 · Cited by 87

Estrogens Promote Misfolded Proinsulin Degradation to Protect Insulin Production and Delay Diabetes

Xu, B., Allard, C., Álvarez‐Mercado, A. I., Fuselier, T. T., Kim, J. H., Coons, L. A., Hewitt, S. C., Urano, F., Korach, K. S., Levin, E. R., et al. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.06.019 · Cited by 85

Advanced nanomaterials as sample technique for bio-analysis

Sun, N., Yu, H., Wu, H., Shen, X., & Deng, C. (2021) · TrAC Trends in Analytical Chemistry · doi:10.1016/j.trac.2020.116168 · Cited by 85

Glucose Metabolism: A Sweet Relief of Alzheimer’s Disease

Duran-Aniotz, C. A., & Hetz, C. A. (2016) · Current Biology · doi:10.1016/j.cub.2016.07.060 · Cited by 85

Irisin attenuates myocardial ischemia/reperfusion‐induced cardiac dysfunction by regulating ER‐mitochondria interaction through a mitochondrial ubiquitin ligase‐dependent mechanism

Lu, L., Ma, J., Tang, J., Yang, L., Zheng, Q., Chen, S., Gao, E., Ren, J. T., Yang, L., & Yang, J. Z. (2020) · Clinical and Translational Medicine · doi:10.1002/ctm2.166 · Cited by 84

Misfolded proinsulin in the endoplasmic reticulum during development of beta cell failure in diabetes

Arunagiri, A., Haataja, L., Cunningham, C. N., Shrestha, N., Tsai, B., Qi, L., Liu, M., & Arvan, P. (2018) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.13531 · Cited by 89

Protein Quality Control in the Endoplasmic Reticulum and Cancer

Moon, H. W., Han, H. G., & Jeon, Y. J. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19103020 · Cited by 86

Circadian- and UPR-dependent control of CPEB4 mediates a translational response to counteract hepatic steatosis under ER stress

Maillo, C., Martín, J., Sebastián, D., Hernández-Alvarez, M., García-Rocha, M., Reina, O., Zorzano, A., Fernandez, M., & Méndez, R. (2017) · Nature Cell Biology · doi:10.1038/ncb3461 · Cited by 82

ER Stress in Cardiometabolic Diseases: From Molecular Mechanisms to Therapeutics

Ajoolabady, A., Wang, S., Kroemer, G., Klionsky, D. J., Uversky, V. N., Sowers, J. R., Aslkhodapasandhokmabad, H., Bi, Y., Ge, J., & Ren, J. T. (2021) · Endocrine Reviews · doi:10.1210/endrev/bnab006 · Cited by 85

Endoplasmic Reticulum Stress-Associated Neuronal Death and Innate Immune Response in Neurological Diseases

Shi, M., Chai, Y., Zhang, J., & Chen, X. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2021.794580 · Cited by 86

Significance of Programmed Cell Death Pathways in Neurodegenerative Diseases

Guo, D., Liu, Z., Zhou, J., Ke, C., & Li, D. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25189947 · Cited by 83

Inhibiting Mitochondrial Damage for Efficient Treatment of Cerebral Ischemia‐Reperfusion Injury Through Sequential Targeting Nanomedicine of Neuronal Mitochondria in Affected Brain Tissue

Wang, S., Shi, X., Xiong, T., Chen, Q., Yang, Y., Chen, W., Zhang, K., Nan, Y., Huang, Q., & Ai, K. (2024) · Advanced Materials · doi:10.1002/adma.202409529 · Cited by 82

Prostate cancer and the unfolded protein response

Storm, M. L., Sheng, X., Arnoldussen, Y. J., & Saatcioglu, F. (2016) · Oncotarget · doi:10.18632/oncotarget.9912 · Cited by 81

Endoplasmic Reticulum Stress Responses in Intratumoral Immune Cells: Implications for Cancer Immunotherapy

Song, M., & Cubillos‐Ruiz, J. R. (2019) · Trends in Immunology · doi:10.1016/j.it.2018.12.001 · Cited by 82

SPHK1 deficiency protects mice from acetaminophen-induced ER stress and mitochondrial permeability transition

Li, L., Wang, H., Zhang, J., Sha, Y., Wu, F., Wen, S., He, L., Sheng, L., You, Q., Shi, M., et al. (2020) · Cell Death & Differentiation · doi:10.1038/s41418-019-0471-x · Cited by 80

The heat shock protein 47 as a potential biomarker and a therapeutic agent in cancer research

Duarte, B. D. P., & Bonatto, D. (2018) · Journal of Cancer Research and Clinical Oncology · doi:10.1007/s00432-018-2739-9 · Cited by 80

Endoplasmic Reticulum Stress and Autophagy in the Pathogenesis of Non-alcoholic Fatty Liver Disease (NAFLD): Current Evidence and Perspectives

Flessa, C., Kyrou, I., Ansari, N. N., Kaltsas, G., Papavassiliou, A. G., Kassi, E. N., & Randeva, H. S. (2021) · Current Obesity Reports · doi:10.1007/s13679-021-00431-3 · Cited by 81

Mouse γ-Synuclein Promoter-Mediated Gene Expression and Editing in Mammalian Retinal Ganglion Cells

Qizhao, W., Zhuang, P., Huang, H., Li, L., Liu, L., Webber, H. C., Dalal, R., Siew, L., Fligor, C. M., Chang, K., et al. (2020) · Journal of Neuroscience · doi:10.1523/jneurosci.0102-20.2020 · Cited by 82

MYC and the unfolded protein response in cancer: synthetic lethal partners in crime?

Zhang, T., Li, N., Sun, C., Jin, Y., & Sheng, X. (2020) · EMBO Molecular Medicine · doi:10.15252/emmm.201911845 · Cited by 79

IRE1 signaling regulates chondrocyte apoptosis and death fate in the osteoarthritis

Huang, R., Zhang, H., Sun, W., Duan, L., Li, W., Daping, W., & Alahdal, M. (2021) · Journal of Cellular Physiology · doi:10.1002/jcp.30537 · Cited by 79

Redox regulation of UPR signalling and mitochondrial ER contact sites

Casas-Martinez, J. C., Samali, A., & McDonagh, B. (2024) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-024-05286-0 · Cited by 85

Knockdown of IRE1α inhibits colonic tumorigenesis through decreasing β-catenin and IRE1α targeting suppresses colon cancer cells

Li, X.-X., Zhang, H.-S., Xu, Y.-M., Zhang, R.-J., Chen, Y., Fan, L., Qin, Y.-Q., Liu, Y., Li, M., & Fang, J. (2017) · Oncogene · doi:10.1038/onc.2017.284 · Cited by 83

The unfolded protein response in ischemic heart disease

Wang, X., Xu, L., Gillette, T. G., Jiang, X., & Wang, Z. V. (2018) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2018.02.013 · Cited by 79

Interaction of volatile organic compounds and underlying liver disease: a new paradigm for risk

Lang, A. L., & Beier, J. I. (2018) · Biological Chemistry · doi:10.1515/hsz-2017-0324 · Cited by 79

Dynamic changes in complexes of IRE1α, PERK, and ATF6α during endoplasmic reticulum stress

Sundaram, A., Appathurai, S., Plumb, R., & Mariappan, M. (2018) · Molecular Biology of the Cell · doi:10.1091/mbc.e17-10-0594 · Cited by 78

HRD1-mediated METTL14 degradation regulates m6A mRNA modification to suppress ER proteotoxic liver disease

Wei, J., Harada, B. T., Lü, D., Ma, R., Gao, B., Xu, Y., Montauti, E. I., Mani, N. L., Chaudhuri, S. M., Gregory, S., et al. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.10.028 · Cited by 78

Endoplasmic Reticulum Protein Quality Control Failure in Myelin Disorders

Volpi, V. G., Touvier, T., & D’Antonio, M. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2016.00162 · Cited by 78

At the crossway of ER‐stress and proinflammatory responses

Reverendo, M., Mendes, A., Argüello, R., Gatti, E., & Pierre, P. (2019) · The FEBS Journal · doi:10.1111/febs.14391 · Cited by 72

ATF4 Mediates Mitochondrial Unfolded Protein Response in Alveolar Epithelial Cells

Jiang, D., Cui, H., Xie, N., Banerjee, S., Liu, R.-M., Dai, H., Thannickal, V. J., & Liu, G. (2020) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2020-0107oc · Cited by 78

Small Molecules to Improve ER Proteostasis in Disease

Gonzalez‐Teuber, V., Albert‐Gascó, H., Auyeung, V. C., Papa, F. R., Mallucci, G. R., & Hetz, C. A. (2019) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2019.07.003 · Cited by 77

Cellular mechanisms of peroxynitrite-induced neuronal death

Ramdial, K., Franco, M. C., & Estévez, Á. G. (2017) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2017.05.008 · Cited by 77

ZnO Nanoparticles Induced Male Reproductive Toxicity Based on the Effects on the Endoplasmic Reticulum Stress Signaling Pathway

Tang, Y., Chen, B., Hong, W., Chen, L., Yao, L., Zhao, Y., Aguilar, Z. P., & Xu, H. (2019) · International Journal of Nanomedicine · doi:10.2147/ijn.s223318 · Cited by 76

Ferroptosis in ulcerative colitis: Potential mechanisms and promising therapeutic targets

Long, D., Mao, C., Huang, Y., Xu, Y., & Zhu, Y. (2024) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2024.116722 · Cited by 81

Zero-shot prediction of mutation effects with multimodal deep representation learning guides protein engineering

Cheng, P., Mao, C., Tang, J., Yang, S., Cheng, Y., Wang, W., Gu, Q., Han, W., Chen, H., Li, S., et al. (2024) · Cell Research · doi:10.1038/s41422-024-00989-2 · Cited by 76

The Role of IGF/IGF-1R Signaling in Hepatocellular Carcinomas: Stemness-Related Properties and Drug Resistance

Ngo, M.-H. T., Jeng, H.-Y., Kuo, Y., Nanda, J. D., Brahmadhi, A., Ling, T., Chang, T., & Huang, Y. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22041931 · Cited by 79

The hormesis principle of neuroplasticity and neuroprotection

Mattson, M. P., & Leak, R. K. (2024) · Cell Metabolism · doi:10.1016/j.cmet.2023.12.022 · Cited by 77

Emerging role of Unfolded Protein Response (UPR) mediated proteotoxic apoptosis in diabetes

Pandey, V. K., Mathur, A., & Kakkar, P. (2018) · Life Sciences · doi:10.1016/j.lfs.2018.11.041 · Cited by 76

Vitamin E δ-tocotrienol triggers endoplasmic reticulum stress-mediated apoptosis in human melanoma cells

Montagnani Marelli, M., Marzagalli, M., Moretti, R. M., Beretta, G., Casati, L., Comitato, R., Gravina, G. L., Festuccia, C., & Limonta, P. (2016) · Scientific Reports · doi:10.1038/srep30502 · Cited by 74

Together JUN and DDIT3 (CHOP) control retinal ganglion cell death after axonal injury

Syc-Mazurek, S. B., Fernandes, K. A., Wilson, M. P., Shrager, P., & Libby, R. T. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0214-8 · Cited by 74

Clinical spectrum, prognosis and estimated prevalence of DNAJB11-kidney disease

Huynh, V. T., Audrézet, M., Sayer, J. A., Ong, A. C. M., Lefèvre, S., Brun, V. L., Després, A., Senum, S. R., Chebib, F. T., Barroso‐Gil, M., et al. (2020) · Kidney International · doi:10.1016/j.kint.2020.02.022 · Cited by 73

In vitro FRET analysis of IRE1 and BiP association and dissociation upon endoplasmic reticulum stress

Kopp, M. C., Nowak, P. R., Larburu, N., Adams, C. J., & Ali, M. M. U. (2018) · eLife · doi:10.7554/elife.30257 · Cited by 73

Liver – master and servant of serum proteome

Kuscuoglu, D., Janciauskiene, S. M., Hamesch, K., Haybaeck, J., Trautwein, C., & Strnad, P. (2018) · Journal of Hepatology · doi:10.1016/j.jhep.2018.04.018 · Cited by 73

Deconvoluting Stress-Responsive Proteostasis Signaling Pathways for Pharmacologic Activation Using Targeted RNA Sequencing

Grandjean, J. M. D., Plate, L., Morimoto, R. I., Bollong, M. J., Powers, E. T., & Wiseman, R. L. (2019) · ACS Chemical Biology · doi:10.1021/acschembio.9b00134 · Cited by 72

AGE/RAGE signaling-mediated endoplasmic reticulum stress and future prospects in non-coding RNA therapeutics for diabetic nephropathy

Pathomthongtaweechai, N., & Chutipongtanate, S. (2020) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2020.110655 · Cited by 72

Zinc offers splenic protection through suppressing PERK/IRE1-driven apoptosis pathway in common carp (Cyprinus carpio) under arsenic stress

Wang, Y., Zhao, H., Mu, M., Guo, M., & Xing, M. (2020) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2020.111473 · Cited by 72

Exosomes Derived from Human Urine-Derived Stem Cells Inhibit Intervertebral Disc Degeneration by Ameliorating Endoplasmic Reticulum Stress

Xiang, H., Su, W., Wu, X., Chen, W., Cong, W., Yang, S., Liu, C., Qiu, C., Yang, S., Wang, Y., et al. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/6697577 · Cited by 72

Recent advances in endoplasmic reticulum targeting metal complexes

Huang, C., Li, T., Liang, J., Huang, H., Zhang, P., & Banerjee, S. (2020) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2020.213178 · Cited by 72

HDAC6 Inhibition Promotes Transcription Factor EB Activation and Is Protective in Experimental Kidney Disease

Brijmohan, A. S., Batchu, S. N., Majumder, S., Alghamdi, T. A., Thieme, K., McGaugh, S., Liu, Y., Advani, S. L., Bowskill, B. B., Kabir, M. G., et al. (2018) · Frontiers in Pharmacology · doi:10.3389/fphar.2018.00034 · Cited by 71

Anticancer properties of tocotrienols: A review of cellular mechanisms and molecular targets

Marelli, M. M., Marzagalli, M., Fontana, F., Raimondi, M., Moretti, R. M., & Limonta, P. (2018) · Journal of Cellular Physiology · doi:10.1002/jcp.27075 · Cited by 71

Factor VIII exhibits chaperone-dependent and glucose-regulated reversible amyloid formation in the endoplasmic reticulum

Poothong, J., Pottekat, A., Siirin, M., Campos, A. R., Paton, A. W., Paton, J. C., Lagunas-Acosta, J., Chen, Z., Swift, M. F., Volkmann, N., et al. (2020) · Blood · doi:10.1182/blood.2019002867 · Cited by 70

Heat Shock Proteins and Their Role in Pregnancy: Redefining the Function of “Old Rum in a New Bottle”

Jee, B., Dhar, R., Singh, S. K., & Karmakar, S. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.648463 · Cited by 75

Obese mice weight loss role on nonalcoholic fatty liver disease and endoplasmic reticulum stress treated by a GLP-1 receptor agonist

Pontes-da-Silva, R. M., Marinho, T. D. S., Cardoso, L. E. M., Mandarim‐de‐Lacerda, C. A., & Águila, M. B. (2021) · International Journal of Obesity · doi:10.1038/s41366-021-00955-7 · Cited by 72

Endoplasmic reticulum stress and kidney dysfunction

Gallazzini, M., & Pallet, N. (2018) · Biology of the Cell · doi:10.1111/boc.201800019 · Cited by 71

The Sec61 translocon limits IRE1α signaling during the unfolded protein response

Sundaram, A., Plumb, R., Appathurai, S., & Mariappan, M. (2017) · eLife · doi:10.7554/elife.27187 · Cited by 69

Homocysteine Induces Apoptosis of Human Umbilical Vein Endothelial Cells via Mitochondrial Dysfunction and Endoplasmic Reticulum Stress

Zhang, Z., Wei, C., Zhou, Y., Yan, T., Wang, Z., Li, W., & Zhao, L. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/5736506 · Cited by 69

Endoplasmic Reticulum Stress in Disease

Kaufman, R. J., & Popolo, L. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-394447-4.20053-9 · Cited by 1

Endoplasmic Reticulum Stress in Disease Pathogenesis

Lin, J. H., Walter, P., & Yen, T. S. B. (2007) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev.pathmechdis.3.121806.151434 · Cited by 843

Cellular Mechanisms of Endoplasmic Reticulum Stress Signaling in Health and Disease

Dufey, E., Sepúlveda, D., Rivera, D. R., & Hetz, C. A. (2014) · Universidad de Chile · Cited by 29

Protein Folding in the Endoplasmic Reticulum and the Unfolded Protein Response

Zhang, K., & Kaufman, R. J. (2005) · Handbook of Experimental Pharmacology · doi:10.1007/3-540-29717-0_3 · Cited by 152

The endoplasmic reticulum and the unfolded protein response

Malhotra, J. D., & Kaufman, R. J. (2007) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2007.09.003 · Cited by 1,014