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Protein misfolding in the endoplasmic reticulum as a conduit to human disease
Abstract
In eukaryotic cells, the endoplasmic reticulum is essential for the folding and trafficking of proteins that enter the secretory pathway. Environmental insults or increased protein synthesis often lead to protein misfolding in the organelle, the accumulation of misfolded or unfolded proteins - known as endoplasmic reticulum stress - and the activation of the adaptive unfolded protein response to restore homeostasis. If protein misfolding is not resolved, cells die. Endoplasmic reticulum stress and activation of the unfolded protein response help to determine cell fate and function. Furthermore, endoplasmic reticulum stress contributes to the aetiology of many human diseases.
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“However, if the ER stress due to infection is sustained and misfolded protein cannot be refolded or degraded, the cells can also directly increase Aβ production and associated neuroinflammation80.”
From Chlamydia pneumoniae can infect the central nervous system via the olfactory and trigeminal nerves and contributes to Alzheimer’s disease risk (2022) · cites this paper as [80]
Citations
Cites
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
Self-citationMarciniak, S. J., Yun, C. Y., Oyadomari, S., Novoa, I., Zhang, Y., Jungreis, R., Nagata, K., Harding, H. P., & Ron, D. (2004) · Genes & Development · doi:10.1101/gad.1250704 · Cited by 2,066
Zinszner, H., Kuroda, M., Wang, X., Batchvarova, N., Lightfoot, R. T., Remotti, H. E., Stevens, J. L., & Ron, D. (1998) · Genes & Development · doi:10.1101/gad.12.7.982 · Cited by 2,039
From endoplasmic-reticulum stress to the inflammatory response
Zhang, K., & Kaufman, R. J. (2008) · Nature · doi:10.1038/nature07203 · Cited by 2,010
Self-citationKamata, 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
Self-citationKaser, 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
Cited by
Sorted by citations
Items 501–600 of 1,000
Mukherjee, S., Mishra, A. K., Peer, G. D. G., Bagabir, S. A., Haque, S., Pandey, R. P., Raj, V. S., Jain, N. K., Pandey, A., & Kar, S. K. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.767493 · Cited by 30
Kim, S. H., Seo, H., Kwon, D., Yuk, D. Y., & Jung, Y. (2022) · Life · doi:10.3390/life12030354 · Cited by 30
Role of Caspase Family in Intervertebral Disc Degeneration and Its Therapeutic Prospects
Li, L., He, J., Zhang, G., Chen, H., Luo, Z., Deng, B., Zhou, Y., & Kang, X. (2022) · Biomolecules · doi:10.3390/biom12081074 · Cited by 30
Su, J., Peng, J., Wang, L., Xie, H., Zhou, Y., Chen, H., Shi, Y., Guo, Y. H., Zheng, Y., Guo, Y., et al. (2023) · Frontiers in Endocrinology · doi:10.3389/fendo.2023.1206154 · Cited by 30
Xia, J., Li, B., Yin, L., Zhao, N., Yan, Q., & Xu, B. (2019) · Neuroscience Letters · doi:10.1016/j.neulet.2019.03.035 · Cited by 31
Liu, Y., Cui, F., Xu, A., Wang, B., Ma, Y., Zhang, Q., Sun, Q., Zheng, Y., Xue, Y., Sun, Y., et al. (2024) · International Journal of Biological Sciences · doi:10.7150/ijbs.93787 · Cited by 29
Two pools of IRE1α in cardiac and skeletal muscle cells
Wang, Q., Groenendyk, J., Paškevičius, T., Qin, W., Kor, K. C., Liu, Y., Hiess, F., Knollmann, B. C., Chen, S. R. W., Tang, J., et al. (2019) · The FASEB Journal · doi:10.1096/fj.201802626r · Cited by 29
Identification of biomarkers in macrophages of atherosclerosis by microarray analysis
Huang, H., Jiang, X. M., Hao, M.-L., Shan, M., Qiu, Y., Hu, G.-F., Wang, Q., Yu, Z.-Q., Meng, L., & Zou, Y. (2019) · Lipids in Health and Disease · doi:10.1186/s12944-019-1056-x · Cited by 29
Zou, Y., & Qi, Z. (2020) · Mediators of Inflammation · doi:10.1155/2020/6412916 · Cited by 29
Yan, Y., Wang, G., Luo, X., Zhang, P., Peng, S., Cheng, X., Wang, M., & Yang, X. (2021) · Environment International · doi:10.1016/j.envint.2021.106495 · Cited by 29
Self-citationGuo, Y., Hao, D., & Hu, H. (2021) · Molecular Biology Reports · doi:10.1007/s11033-021-06806-y · Cited by 29
Cui, F., Pan, Q., Wang, S., Zhao, F., Wang, R., Zhang, T., Song, Y., He, J., Zhang, H., Weng, Q., et al. (2021) · Advanced Science · doi:10.1002/advs.202102686 · Cited by 29
Roles of Protein Disulfide Isomerase in Breast Cancer
Yang, S., Jackson, C., Karapetyan, E., Dutta, P., Kermah, D., Wu, Y., Wu, Y., Schloss, J. V., & Vadgama, J. V. (2022) · Cancers · doi:10.3390/cancers14030745 · Cited by 31
Exosomes Immunity Strategy: A Novel Approach for Ameliorating Intervertebral Disc Degeneration
Li, W., Zhang, S., Wang, D., Zhang, H., Shi, Q., Zhang, Y., Wang, M., Ding, Z., Xu, S., Gao, B., et al. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.822149 · Cited by 29
Self-citationLivezey, M. R., Kim, J. E., & Shapiro, D. J. (2018) · Frontiers in Endocrinology · doi:10.3389/fendo.2018.00325 · Cited by 32
Systemic hypoxia led to little retinal neuronal loss and dramatic optic nerve glial response
Mesentier-Louro, L. A., Shariati, A., Dalal, R., Camargo, A., Kumar, V., Shamskhou, E. A., Pérez, V. D. J., & Liao, Y. J. (2020) · Experimental Eye Research · doi:10.1016/j.exer.2020.107957 · Cited by 30
Longitudinal dynamics of the tumor hypoxia response: From enzyme activity to biological phenotype
Lee, S. C.-E. S., Pyo, A. H. A., & Koritzinsky, M. (2023) · Science Advances · doi:10.1126/sciadv.adj6409 · Cited by 28
Li, D., Li, X., Zhang, X., Chen, J., Wang, Z., Yu, Z., Wu, M., & Liu, L. (2024) · Chinese Medicine · doi:10.1186/s13020-024-00981-3 · Cited by 28
Artemisinin and its derivatives throughout the therapeutic mechanisms and clinical potential
Addissouky, T. A. (2025) · Discover Chemistry. · doi:10.1007/s44371-025-00084-4 · Cited by 30
Zhao, J., Zhang, W., Zeng, Y., Lu, D., Ma, C., Zhang, M., Cai, X., Huang, Z., Yang, H., Li, J., et al. (2025) · Cancer Research · doi:10.1158/0008-5472.can-24-2558 · Cited by 28
Na, Y. J., Lee, D.-H., Kim, J. L., Kim, B. R., Park, S. H., Jo, M. J., Jeong, S., Kim, H. J., Lee, S., Jeong, Y. A., et al. (2017) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2017.06.010 · Cited by 28
Hijazi, I., Knupp, J., & Chang, A. (2020) · Journal of Cell Science · doi:10.1242/jcs.241539 · Cited by 28
Larburu, N., Adams, C. J., Chen, C.-S., Nowak, P. R., & Ali, M. M. U. (2020) · Open Biology · doi:10.1098/rsob.200089 · Cited by 29
Minchenko, D. O., Khita, O. O., Tsymbal, D. O., Danilovskyi, S. V., Rudnytska, O. V., Halkin, O. V., Kryvdiuk, I. V., Smeshkova, M. V., Yakymchuk, M. M., Безродный, Б. Г., et al. (2020) · Endocrine Regulations · doi:10.2478/enr-2020-0021 · Cited by 28
PROTACs in gastrointestinal cancers
Chen, Y., Yang, Q., Xu, J., Tang, L., Zhang, Y., Du, F., Zhao, Y., Wu, X., Li, M., Shen, J., et al. (2022) · Molecular Therapy — Oncolytics · doi:10.1016/j.omto.2022.10.012 · Cited by 28
Yuan, Z., Lu, L., Lian, Y., Zhao, Y., Tang, T., Xu, S., Yao, Z., & Yu, Z. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.1028002 · Cited by 28
Endoplasmic reticulum stress and quality control in relation to cisplatin resistance in tumor cells
Mu, W., Zhi, Y., Zhou, J., Wang, C., Chai, K., Fan, Z., & Lv, G. (2024) · Frontiers in Pharmacology · doi:10.3389/fphar.2024.1419468 · Cited by 28
Maganti, A. V., Tersey, S. A., Syed, F., Nelson, J. B., Colvin, S. C., Maier, B., & Mirmira, R. G. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.741694 · Cited by 28
New Insights into the Role of Endoplasmic Reticulum Stress in Breast Cancer Metastasis
Han, C.-C., & Wan, F. (2018) · Journal of Breast Cancer · doi:10.4048/jbc.2018.21.e51 · Cited by 28
Sekhar, A. R., Mallik, B., Kumar, V., & Sankar, J. (2019) · Organic & Biomolecular Chemistry · doi:10.1039/c9ob00408d · Cited by 28
Yarapureddy, S., Abril, J., Foote, J. A., Kumar, S., Asad, O., Sharath, V., Faraj, J., Daniel, D., Dickman, P. S., White‐Collins, A., et al. (2019) · Neoplasia · doi:10.1016/j.neo.2019.02.004 · Cited by 28
FNDC3B is associated with ER stress and poor prognosis in cervical cancer
Han, B., Wang, H., Zhang, J., & Tian, J. (2019) · Oncology Letters · doi:10.3892/ol.2019.11098 · Cited by 28
Díaz-Hung, M.-L., Martínez, G., & Hetz, C. A. (2020) · International review of cytology · doi:10.1016/bs.ircmb.2020.01.004 · Cited by 28
Stimulator of Interferon Genes Deficiency in Acute Exacerbation of Idiopathic Pulmonary Fibrosis
Qiu, H., Weng, D., Chen, T., Shen, L., Chen, S.-S., Wei, Y., Wu, Q., Zhao, M., Li, Q., Hu, Y., et al. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.01756 · Cited by 28
Endoplasmic Reticulum Membrane Homeostasis and the Unfolded Protein ResponsePreprint
Ernst, R., Renne, M. F., Jain, A., & von der Malsburg, A. (2024) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a041400 · Cited by 31
Vitamin D receptor attenuate ischemia-reperfusion kidney injury via inhibiting ATF4
Tang, S., Wu, X., Dai, Q., Li, Z., Yang, S., Liu, Y., Yi, B., Wang, J., Liao, Q., Zhang, W., et al. (2023) · Cell Death Discovery · doi:10.1038/s41420-023-01456-4 · Cited by 27
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Das, R., Das, U., Roy, N., Mukherjee, C., Sreelekha, U., & Paira, P. (2024) · Dyes and Pigments · doi:10.1016/j.dyepig.2024.112134 · Cited by 28
Luo, J., Xia, Y., Yin, Y., Luo, J., Liu, M., Zhang, H., Zhang, C., Zhao, Y., Yang, L., & Kong, L. (2019) · Theranostics · doi:10.7150/thno.36818 · Cited by 27
Paraneoplastic β Cell Dedifferentiation in Nondiabetic Patients with Pancreatic Cancer
Wang, Y., Ni, Q., Sun, J., Xu, M., Xie, J., Zhang, J., Fang, Y., Ning, G., & Wang, Q. (2019) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/clinem/dgz224 · Cited by 29
Cao, X., Lilla, S., Cao, Z., Pringle, M. A., Oka, O., Robinson, P. J., Szmaja, T., van Lith, M., Zanivan, S. R., & Bulleid, N. J. (2020) · Journal of Cell Science · doi:10.1242/jcs.241976 · Cited by 27
Wang, H., Dou, S., Zhu, J., Shao, Z., Wang, C., & Cheng, B. (2020) · Neuropeptides · doi:10.1016/j.npep.2020.102112 · Cited by 27
Li, J., Ullah, M. A., Jin, H., Liang, Y., Lin, L., Wang, J., Peng, X., Liao, H., Li, Y., Ge, Y., et al. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.604974 · Cited by 27
Zeng, Q., Liu, Y., Ling, M., Ma, R., Li, J., Chen, H., & Pan, L. (2021) · International Immunopharmacology · doi:10.1016/j.intimp.2021.107774 · Cited by 27
Schnegelberger, R. D., Lang, A. L., Arteel, G. E., & Beier, J. I. (2021) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2021.09.002 · Cited by 27
Emerging roles of endoplasmic reticulum proteostasis in brain development
Vásquez, G. E., Medinas, D. B., Urra, H., & Hetz, C. A. (2022) · Cells and Development · doi:10.1016/j.cdev.2022.203781 · Cited by 29
Shedding Light on NF-κB Functions in Cellular Organelles
Carrà, G., Avalle, L., Seclì, L., Brancaccio, M., & Morotti, A. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.841646 · Cited by 27
Wei, W., Li, Y., Wang, C., Gao, S., Zhao, Y., Yang, Z., Wang, H., Gao, Z., Jiang, Y., He, Y., et al. (2022) · Pharmacological Research · doi:10.1016/j.phrs.2022.106285 · Cited by 27
Han, H., He, Y., Hu, J., Lau, R., Lee, H., & Ji, C. (2017) · Hepatology Communications · doi:10.1002/hep4.1030 · Cited by 27
Fine-Tuning ER Stress Signal Transducers to Treat Amyotrophic Lateral Sclerosis
Medinas, D. B., González, J. V., Falcón, P., & Hetz, C. A. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00216 · Cited by 27
Oliveira, A. N., & Hood, D. A. (2018) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00275.2017 · Cited by 28
Wang, J., Li, H., Ren, Y., Yao, Y., Hu, J., Zheng, M., Ding, Y., Chen, Y., Shen, Y., Wang, L., et al. (2018) · Cellular Physiology and Biochemistry · doi:10.1159/000492996 · Cited by 27
Rellmann, Y., & Dreier, R. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/8421394 · Cited by 28
CRELD2, endoplasmic reticulum stress, and human diseases
Tang, Q., Liu, Q., Li, Y., Mo, L., & He, J. (2023) · Frontiers in Endocrinology · doi:10.3389/fendo.2023.1117414 · Cited by 26
Endoplasmic Reticulum Stress: A Key Regulator of Cardiovascular Disease
Zhao, C., & Zhang, S. (2023) · DNA and Cell Biology · doi:10.1089/dna.2022.0532 · Cited by 26
Bai, X., Wang, Y., Luo, X., Bao, X., Weng, X., Chen, Y., Zhang, S., Lv, Y., Dai, X., Zeng, M. Y., et al. (2024) · Cell Communication and Signaling · doi:10.1186/s12964-024-01480-6 · Cited by 27
Xie, Q., Wang, J., Li, R., Liu, H., Zhong, Y., Xu, Q., Ge, Y., Li, C., Sun, L., & Zhu, J. (2024) · International Journal of Biological Sciences · doi:10.7150/ijbs.99511 · Cited by 26
Alotaibi, G., & Alkhammash, A. (2025) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2025.177509 · Cited by 26
Fang, H., Lın, L., Chen, J., Wu, J., Tian, H., & Chen, X. (2019) · Biomaterials Science · doi:10.1039/c9bm00039a · Cited by 27
Wu, J., Wu, D., Zhang, L., Lin, C., Liao, J., Xie, R., Li, Z., Wu, S., Liu, A., Hu, W., et al. (2019) · Journal of Leukocyte Biology · doi:10.1002/jlb.3ma1119-173r · Cited by 26
Update on the role of endoplasmic reticulum stress in asthma.
Miao, K., Zhang, L., Pan, T. S., & Wang, Y. (2020) · PubMed Central · Cited by 26
The potential of artemisinins as anti-obesity agents via modulating the immune system
Shen, S., Liao, Q., Lyu, M., Wong, Y., Zhang, X., Zhou, J., Ma, N., & Wang, J. (2020) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2020.107696 · Cited by 26
Fu, X., Zhao, W., Li, K., Zhou, J., & Chen, X. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.653232 · Cited by 26
Zhou, Y., Bai, L., Li, T. X., Yang, L., Zhang, H., Zhang, Y., Hao, J., Gu, Y., & Liu, Y. (2021) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2021.111550 · Cited by 26
Ischemic brain injury in diabetes and endoplasmic reticulum stress
Rehni, A. K., Cho, S., & Dave, K. R. (2021) · Neurochemistry International · doi:10.1016/j.neuint.2021.105219 · Cited by 26
Zhang, L., Li, C., Fu, L., Yu, Z., Xu, G., Zhou, J., Shen, M., Feng, Z., Zhu, H., Xie, T., et al. (2022) · PeerJ · doi:10.7717/peerj.12759 · Cited by 26
Ma, X., Li, Y., & Zhao, B. Q. (2022) · Bioengineered · doi:10.1080/21655979.2022.2052672 · Cited by 26
iRhom pseudoproteases regulate ER stress-induced cell death through IP3 receptors and BCL-2
Dulloo, I., Atakpa‐Adaji, P., Yeh, Y.-C., Levet, C., Muliyil, S., Lu, F., Taylor, C. W., & Freeman, M. (2022) · Nature Communications · doi:10.1038/s41467-022-28930-4 · Cited by 26
MiR-142-5p/FAM134B Axis Manipulates ER-Phagy to Control PRRSV Replication
Guan, K., Su, Q., Kuang, K., Meng, X., Zhou, X. D., & Liu, B. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.842077 · Cited by 26
Ahmad, S., Zaki, A., Manda, K., Mohan, A., & Syed, M. A. (2022) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2022.109130 · Cited by 26
Nie, X., Ma, B., Liu, L., Yuan, X., Li, M., Liu, Y., Hou, Y., Yang, Y., Xu, J., & Wang, Y. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241411692 · Cited by 26
Guo, W., Wang, M., Yang, Z., Liu, D., Ma, B., Zhao, Y., Chen, Y., & Hu, Y. (2023) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2023.115792 · Cited by 26
Self-citationInjury to the nervous system: A look into the ER
Valenzuela, V., Oñate, M., Hetz, C. A., & Court, F. A. (2016) · Brain Research · doi:10.1016/j.brainres.2016.04.053 · Cited by 26
Al-Baghdadi, R. J. T., Nikonorova, I. A., Mirek, E. T., Wang, Y., Park, J., Belden, W. J., Wek, R. C., & Anthony, T. G. (2017) · Scientific Reports · doi:10.1038/s41598-017-01041-7 · Cited by 27
Baba, Y., Shigemi, Z., Hara, N., Moriguchi, M., Ikeda, M., Watanabe, T., & Fujimuro, M. (2017) · International Journal of Oncology · doi:10.3892/ijo.2017.4215 · Cited by 26
Imam, S., Prathibha, R., Dar, P., Almotah, K., Al-Khudhair, A., Hasan, S. A., Salim, N., Jilani, T. N., Mirmira, R. G., & Jaume, J. C. (2019) · Scientific Reports · doi:10.1038/s41598-018-38341-5 · Cited by 26
Tang, G., Chen, X., Ding, J., Du, J., Lin, X., Xia, L., Lian, J., Feng, Y., Xiu-sheng, H., & Liu, W. (2020) · Frontiers in Genetics · doi:10.3389/fgene.2019.01409 · Cited by 26
Protein Stability Buffers the Cost of Translation Attenuation following eIF2α Phosphorylation
Schneider, K., Nelson, G. M., Watson, J. L., Morf, J., Dalglish, M. M., Luh, L. M., Weber, A., & Bertolotti, A. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.108154 · Cited by 29
Adipokines regulate the development and progression of MASLD through organellar oxidative stress
Zhao, K., Zhang, H., Ding, W., Yu, X., Hou, Y., Liu, X., Li, X., & Wang, X. (2025) · Hepatology Communications · doi:10.1097/hc9.0000000000000639 · Cited by 25
Hao, B., Liu, Y., Wang, B., Wu, H., Chen, Y., & Zhang, L. (2025) · Experimental Hematology and Oncology · doi:10.1186/s40164-025-00642-7 · Cited by 26
Chien, C., Hung, Y., Shieh, Y., Hsieh, C., Lu, C., Lin, F., Su, S., & Lee, C.-H. (2017) · PLoS ONE · doi:10.1371/journal.pone.0179963 · Cited by 25
Key, J., Maletzko, A., Kohli, A., Gispert, S., Torres-Odio, S., Wittig, I., Heidler, J., Bárcena, C., López-Otı́n, C., Lei, Y., et al. (2020) · Neurogenetics · doi:10.1007/s10048-020-00609-2 · Cited by 25
Li, Z., Teng, M., Wang, Y., Wang, Q., Feng, Y., Xiao, Z., Li, C., & Zeng, K. (2021) · Photodermatology Photoimmunology & Photomedicine · doi:10.1111/phpp.12663 · Cited by 25
Wen, T., Xue, P., Ying, J., Cheng, S., Liu, Y., & Ruan, D. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/6492879 · Cited by 25
Amin, K. N., Rajagru, P., Sarkar, K., Munuswamy‐Ramanujam, G., Suzuki, T., Ali, D., & Ramkumar, K. M. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/2732435 · Cited by 25
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Cui, X., Wang, J., Zhang, Y., Wei, J.-L., & Wang, Y. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/2122856 · Cited by 25
Zhou, L., Shen, H., Li, X., & Wang, H. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.951406 · Cited by 27
Xie, H., Wang, Y., Liu, X., Gao, J. L., Yang, C., Huang, T., Zhang, L., Luo, X., Gao, Z., Wang, T., et al. (2022) · Metabolism · doi:10.1016/j.metabol.2022.155351 · Cited by 25
Chen, Y., Liu, X., Li, L., He, X., Fanghui, Z., Zhang, Y., Gao, H. L., Jin, Z., Wu, D., Wang, Q., et al. (2023) · Molecular Medicine · doi:10.1186/s10020-023-00604-x · Cited by 25
A new role for HERPUD1 and ERAD activation in osteoblast differentiation and mineralization
Américo-Da-Silva, L., Diaz, J., Bustamante, M., Mancilla, G., Oyarzún, I., Verdejo, H., & Quiroga, C. (2018) · The FASEB Journal · doi:10.1096/fj.201701229rr · Cited by 25
The lipid side of unfolded protein response
Białek, W., Hryniewicz‐Jankowska, A., Czechowicz, P., Sławski, J., Collawn, J. F., Czogalla, A., & Bartoszewski, R. (2024) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2024.159515 · Cited by 24
Implications of endoplasmic reticulum stress and autophagy in aging and cardiovascular diseases
Ma, C., Liu, Y., & Fu, Z. (2024) · Frontiers in Pharmacology · doi:10.3389/fphar.2024.1413853 · Cited by 26
The role of ER-associated degradation and ER-phagy in health and disease
Jeon, Y. J., & Ronai, Z. A. (2026) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02501-7 · Cited by 28
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Metadata
- Authors
- Wang, M., & Kaufman, R. J.
- Affiliations
- Sanford Burnham Prebys Medical Discovery Institute (US)
- Corresponding author
- Kaufman, Randal J.
- Venue
- Nature
- Published
- 2016-01
- Volume
- 529
- Issue
- 7586
- Pages
- 326-335
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2263498456
- Cited by
- 1,630
- References
- 126
- Citations by year
- 2026: 127 · 2025: 166 · 2024: 177 · 2023: 180 · 2022: 200 · 2021: 179 · 2020: 185 · 2019: 137 · 2018: 120 · 2017: 113 · 2016: 44
- FWCI
- 14.97
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Funders
- National Institutes of Health
- National Cancer Institute (P01CA128814, CA-128814)
- National Institute of Diabetes and Digestive and Kidney Diseases (R01 DK103183)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Keywords
- protein misfolding, endoplasmic reticulum stress, unfolded protein response, secretory pathway, protein folding, protein trafficking, cell fate, human disease, ER-associated degradation
- MeSH terms
- Animals, Disease, Endoplasmic Reticulum, Humans, Proteins, Protein Folding, Unfolded Protein Response, Molecular Targeted Therapy, Endoplasmic Reticulum Stress
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