The DOI matches its Crossref record; 126 of the 126 references it cites were found in a registry or an index.
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.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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
“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 601–700 of 1,000
Lu, Y., Shimada, K., Tang, S., Zhang, J., Ogawa, Y., Noda, T., Shibuya, H., & Ikawa, M. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2207263120 · Cited by 24
Qiu, X., Li, L., Wei, J., An, X., Ampadu, J. A., Zheng, W., Yu, C., Peng, C., Li, X., & Cai, X. (2023) · International Immunopharmacology · doi:10.1016/j.intimp.2023.109813 · Cited by 24
The Dynamic Role of Endoplasmic Reticulum Stress in Chronic Liver Disease
Jackson, K. G., Way, G. W., Zeng, J., Lipp, M. K., & Zhou, H. (2023) · American Journal Of Pathology · doi:10.1016/j.ajpath.2023.03.009 · Cited by 24
Endoplasmic Reticulum Selective Autophagy Alleviates Anthracycline-Induced Cardiotoxicity
Nakagama, S., Maejima, Y., Fan, Q., Shiheido‐Watanabe, Y., Tamura, N., Ihara, K., & Sasano, T. (2023) · JACC CardioOncology · doi:10.1016/j.jaccao.2023.05.009 · Cited by 24
Naeem, M. S., Han, R., Ahmad, N., Zhao, W., & Zhao, L. (2023) · Plant Growth Regulation · doi:10.1007/s10725-023-01106-w · Cited by 24
Chen, T., Qiu, H., Zhao, M., Chen, S., Wu, Q., Zhou, N., Lu, L., Song, J., Tang, D., Weng, D., et al. (2018) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.13992 · Cited by 24
de Jong, F., Pokorny, J., Manshian, B. B., Daelemans, B., Vandaele, J., Startek, J. B., Soenen, S. J., der Auweraer, M. V., Dehaen, W., Rocha, S., et al. (2020) · Dyes and Pigments · doi:10.1016/j.dyepig.2020.108200 · Cited by 24
Neuroprotection Effect of Astragaloside IV from 2-DG-Induced Endoplasmic Reticulum Stress
Fu, Y., Cai, J., Xi, M., He, Y., Yang, Z., Zheng, Y., Zhang, Y., Xi, J., & He, Y. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/9782062 · Cited by 24
UFMylation of HRD1 regulates endoplasmic reticulum homeostasis
Luo, H., Jiao, Q., Shen, C., Gong, W., Yuan, J., Liu, Y., Chen, Z., Liu, J., Xu, X., Cong, Y., et al. (2023) · The FASEB Journal · doi:10.1096/fj.202300004rrrr · Cited by 23
Pan, C., Chen, Z., Li, C., Han, T., Liu, H., & Wang, X. (2021) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.16540 · Cited by 23
Shi, F., Wang, Z., Wu, Q., Zhong, X., Zhang, M., Li, B., Ren, W., Yuan, S., & Chen, Y. (2022) · Pharmacological Research · doi:10.1016/j.phrs.2022.106366 · Cited by 23
Bip-Yorkie interaction determines oncogenic and tumor-suppressive roles of Ire1/Xbp1s activation
Yang, S., Jiang, H., Bian, W., Xu, W., Guo, Y., Song, S., Zheng, J., Kuang, X., Wu, C., Ding, X., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2202133119 · Cited by 23
An ER-targeted “reserve-release” fluorogen for topological quantification of reticulophagy
Fang, H., Hu, L., Chen, Q., Geng, S., Qiu, K., Wang, C., Hao, M., Tian, Z., Chen, H., Liu, L., et al. (2022) · Biomaterials · doi:10.1016/j.biomaterials.2022.121929 · Cited by 23
Endoplasmic reticulum stress associates with the development of intervertebral disc degeneration
Huang, J., Zhou, Q., Ren, Q., Luo, L., Ji, G., & Zheng, T. (2023) · Frontiers in Endocrinology · doi:10.3389/fendo.2022.1094394 · Cited by 23
Hepatotoxic mechanism of cantharidin: insights and strategies for therapeutic intervention
Jin, D., Huang, N., & Wei, J.-X. (2023) · Frontiers in Pharmacology · doi:10.3389/fphar.2023.1201404 · Cited by 23
Liu, Y., You, S., Ding, L., Yuan, F., & Sun, Y. (2024) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2024.171447 · Cited by 23
Hsp90, a team player in protein quality control and the stress response in bacteria
Wickramaratne, A. C., Wickner, S., & Kravats, A. N. (2024) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00176-22 · Cited by 26
Nanotechnology‐Mediated Immunomodulation Strategy for Inflammation Resolution
Li, Y., Liu, W., Wang, Y., Liu, T., & Feng, Y. (2024) · Advanced Healthcare Materials · doi:10.1002/adhm.202401384 · Cited by 24
The Role of Reductive Stress in the Pathogenesis of Endocrine-Related Metabolic Diseases and Cancer
Mladenov, M. I., Sazdova, I., Hadzi‐Petrushev, N., Konakchieva, R., & Gagov, H. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26051910 · Cited by 23
Moriyama, K. (2025) · World Journal of Clinical Cases · doi:10.12998/wjcc.v13.i29.108380 · Cited by 26
Induction of blood-circulating bile acids supports recovery from myelosuppressive chemotherapy
Sigurðsson, V., Haga, Y., Takei, H., Mansell, E., Okamatsu-Haga, C., Suzuki, M., Radulović, V., van der Garde, M., Koide, S., Soboleva, S., et al. (2020) · Blood Advances · doi:10.1182/bloodadvances.2019000133 · Cited by 23
Guan, W., Nakata, K., Sagara, A., Iwamoto, C., Endo, S., Matsuda, R., Matsumoto, S., Ikenaga, N., Shindo, K., Moriyama, T., et al. (2021) · Pancreatology · doi:10.1016/j.pan.2021.09.012 · Cited by 22
Targeting UPR branches, a potential strategy for enhancing efficacy of cancer chemotherapy
Yu, M., Lun, J., Zhang, H., Wang, L., Zhang, G., Zhang, H., & Fang, J. S. (2021) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmab131 · Cited by 22
Asthma Susceptibility Gene ORMDL3 Promotes Autophagy in Human Bronchial Epithelium
Guo, F., Hao, Y. T., Zhang, L., Croteau‐Chonka, D. C., Thibault, D. M., Kothari, P. H., Li, L., Levy, B. D., Zhou, X., & Raby, B. A. (2022) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2021-0305oc · Cited by 22
Liu, C. X., Wang, B., Zhu, W. P., Xu, Y. F., Yang, Y. Y., & Qian, X. H. (2022) · Angewandte Chemie International Edition · doi:10.1002/anie.202205509 · Cited by 22
Ran, H., He, Q., Han, Y., Wang, J., Wang, H., Yue, B., Zhang, M., Chai, Z., Cai, X. M., Zhong, J., et al. (2022) · Epigenetics · doi:10.1080/15592294.2022.2135194 · Cited by 22
Song, N., Song, Y., Hu, B., Liu, X., Yu, X., Zhou, H., Long, J., & Yu, Z. (2022) · Advanced Healthcare Materials · doi:10.1002/adhm.202202039 · Cited by 22
Zhang, X., Huo, Z., Jia, X., Xiong, Y., Li, B., Zhang, L., Li, X., Li, X., Fang, Y., Dong, X., et al. (2024) · Food & Function · doi:10.1039/d3fo05400d · Cited by 22
Oxidative photocatalysis on membranes triggers non-canonical pyroptosis
Lee, C., Park, M., Wijesinghe, W. C. B., Na, S., Lee, C. G., Hwang, E., Yoon, G., Lee, J. K., Roh, D., Kwon, Y. H., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-47634-5 · Cited by 22
Phillipson‐Weiner, L., Mirek, E. T., Wang, Y.-P., McAuliffe, W. G., Wek, R. C., & Anthony, T. G. (2016) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00052.2016 · Cited by 22
Fine-tuning PERK signaling to control cell fate under stress
Urra, H., & Hetz, C. A. (2017) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3478 · Cited by 22
Roest, G., Hesemans, E., Welkenhuyzen, K., Luyten, T., Engedal, N., Bultynck, G., & Parys, J. B. (2018) · Cells · doi:10.3390/cells7120239 · Cited by 23
Omentin protects H9c2 cells against docetaxel cardiotoxicity
Lage, R., Cebro-Márquez, M., Rodríguez‐Mañero, M., González‐Juanatey, J. R., & Moscoso, I. (2019) · PLoS ONE · doi:10.1371/journal.pone.0212782 · Cited by 22
Dual Targeting of Endoplasmic Reticulum by Redox-Deubiquitination Regulation for Cancer Therapy
Cai, B., Hou, M., Zhang, S., Xin, Z., Huang, J., Yang, J., Wang, Y., Cai, X., Xie, S., Zhang, C., et al. (2021) · International Journal of Nanomedicine · doi:10.2147/ijn.s321612 · 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
He, M., Li, D., Fang, C., & Xu, Q. (2022) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2022.109464 · Cited by 22
Tirla, A., & Rivera‐Fuentes, P. (2016) · Angewandte Chemie International Edition · doi:10.1002/anie.201608779 · Cited by 22
He, Z., Liu, Q., Wang, Y., Zhao, B., Zhang, L., Yang, X. V., & Wang, Z. (2025) · PeerJ · doi:10.7717/peerj.19192 · Cited by 25
Li, Y., Liu, Y., Luo, S.-Z., Huang, X., Shen, Y., Wang, W.-S., & Lang, Z.-C. (2025) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2025.1585758 · Cited by 21
Fu, C., Zhan, J., Huai, J., Ma, S., Li, M., Chen, G., Chen, M., Cai, Y., & Ou, C. (2020) · Nanoscale · doi:10.1039/d0nr00151a · Cited by 21
Zhang, Q., Sun, Q., Tong, Y., Bi, X., Chen, L., Lü, J., & Ding, W. Q. (2022) · International Urology and Nephrology · doi:10.1007/s11255-021-03093-1 · Cited by 21
Vidak, S., Serebryannyy, L., Pegoraro, G., & Misteli, T. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112534 · Cited by 21
The in vivo drug delivery pattern of the organelle-targeting small molecules
Fang, Z., & Chen, H. (2023) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2023.115020 · Cited by 21
Targeting the organelle for radiosensitization in cancer radiotherapy
Sun, X., Wu, L., Du, L., Xu, W., & Han, M. Y. (2024) · Asian Journal of Pharmaceutical Sciences · doi:10.1016/j.ajps.2024.100903 · Cited by 22
Wei, Y., Li, Q., He, K., Liao, G., Cheng, L., Liao, G., & Cheng, L. (2024) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2024.08.036 · Cited by 21
Metabolic syndrome and dermatological diseases: association and treatment
Xia, J., Li, D., & Liu, G. (2025) · Nutrition & Metabolism · doi:10.1186/s12986-025-00924-1 · Cited by 21
Stress Coping Strategies in the Heart: An Integrated View
Michalak, M., & Agellon, L. B. (2018) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2018.00168 · Cited by 22
Defective endoplasmic reticulum export causes proinsulin misfolding in pancreatic β cells
Zhu, R., Li, X., Xu, J., Barrabi, C., Kekulandara, D. N., Woods, J., Chen, X., & Liu, M. R. (2019) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2019.110470 · Cited by 21
Yao, Z., Wang, W., Ning, J., Zhang, X., Zheng, W., Qian, Y., & Fan, C. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.00967 · Cited by 21
In a search for efficient treatment for amyotrophic lateral sclerosis: Old drugs for new approaches
Kukharsky, M. S., Skvortsova, V. I., Бачурин, С. О., & Buchman, V. L. (2020) · Medicinal Research Reviews · doi:10.1002/med.21725 · Cited by 21
Impact of knockdown LincRNA-Cox2 on apoptosis of macrophage infected with Bacillus Calmette-Guérin
Xu, Y., Yu, J., Ma, C., Gong, Z., Wu, X., & Deng, G. (2020) · Molecular Immunology · doi:10.1016/j.molimm.2020.11.008 · Cited by 21
Xie, P., Ren, Z., Lv, J., Hu, Y.-M., Guan, Z., & Yu, W. (2020) · Current Medical Science · doi:10.1007/s11596-020-2286-x · Cited by 21
Integrated signaling system under endoplasmic reticulum stress in eukaryotic microorganisms
Cao, T., Peng, B., Zhou, X., Cai, J., Tang, Y., Luo, J., Xie, H., Zhang, J., & Liu, S. (2021) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-021-11380-1 · Cited by 21
Wang, J., Yang, C., Hu, X., Yao, X., Han, L. S., Wu, X., Li, R., Wen, T., & Ming, L. (2022) · Journal of Fungi · doi:10.3390/jof8020153 · Cited by 21
Ciaglia, T., Miranda, M. R., Micco, S. D., Vietri, M., Smaldone, G., Musella, S., Sarno, V. D., Auriemma, G., Sardo, C., Moltedo, O., et al. (2024) · Antioxidants · doi:10.3390/antiox13121585 · Cited by 20
Zhao, D., Li, Y., Xiang, L., Saiding, Q., Lin, Z., Cai, Z., Wang, J., & Cui, W. (2025) · Research · doi:10.34133/research.0777 · Cited by 20
Zhang, Y., Li, Y., Wang, R., Wang, S., Sun, B., Cao, D., Sun, Z., Lv, W., Bo, M., & Zhang, Y. (2025) · Antioxidants · doi:10.3390/antiox14080926 · Cited by 20
Zhang, Y., Gao, J., & Luo, Y. (2019) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2019.109053 · Cited by 20
Wang, S., Xu, X., Ju, X., Wang, S., Li, J., Yan, P., Yu, Z., & Song, M. (2020) · Neuroreport · doi:10.1097/wnr.0000000000001554 · Cited by 20
Gopalakrishnan, S., & Ismail, A. (2021) · Phytotherapy Research · doi:10.1002/ptr.7236 · Cited by 21
Ma, N., Xu, N., Yin, D., Zheng, P., Liu, W., Wang, G., Hui, Y., Han, G., Yang, C., & Cheng, X. (2021) · Medicine · doi:10.1097/md.0000000000026879 · Cited by 21
The Entropy Perspective on Human Illness and Aging
Wang, Z. (2021) · Engineering · doi:10.1016/j.eng.2021.08.014 · Cited by 20
Li, Y., Huang, S., Wang, J., Dai, J., Cai, J., Yan, S., Huang, Z., He, S., Wang, P., Liu, J., et al. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.101997 · Cited by 24
iASPP suppression mediates terminal UPR and improves BRAF-inhibitor sensitivity of colon cancers
Zheng, S., Wang, X., Liu, H., Zhao, D. H., Lin, Q., Jiang, Q., Li, L., & Hu, Y. (2022) · Cell Death and Differentiation · doi:10.1038/s41418-022-01086-w · Cited by 20
Mitochondria and Endoplasmic Reticulum Stress in Retinal Organoids from Patients with Vision Loss
Lee, E.-J., Diaz‐Aguilar, M. S., Min, H., Choi, J., Duran, D. A. V., Grandjean, J. M. D., Wiseman, R. L., Kroeger, H., & Lin, J. H. (2022) · American Journal Of Pathology · doi:10.1016/j.ajpath.2022.12.002 · Cited by 21
Catalani, E., Quondam, S. D., Brunetti, K., Cherubini, A., Bongiorni, S., Taddei, A. R., Zecchini, S., Giovarelli, M., Palma, C. D., Perrotta, C., et al. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.115298 · Cited by 20
Xu, P., Zhong, S., Wei, Y., Duan, X., Zhang, M., Shen, W., Ma, Y., & Zhang, Y. (2024) · ACS Nano · doi:10.1021/acsnano.4c06138 · Cited by 20
Urinary Angiogenin Reflects the Magnitude of Kidney Injury at the Infrahistologic Level
Tavernier, Q., Mami, I., Rabant, M., Karras, A., Laurent‐Puig, P., Chevet, É., Thervet, É., Anglicheau, D., & Pallet, N. (2016) · Journal of the American Society of Nephrology · doi:10.1681/asn.2016020218 · Cited by 21
Kuribara, T., Hirano, M., Speciale, G., Williams, S. J., Ito, Y., & Totani, K. (2017) · ChemBioChem · doi:10.1002/cbic.201700081 · Cited by 20
Endoplasmic Reticulum: Target for Next‐Generation Cancer Therapy
Banerjee, S., & Zhang, W. (2018) · ChemBioChem · doi:10.1002/cbic.201800461 · Cited by 20
Minchenko, D. O., Tsymbal, D. O., Davydov, V. V., & Minchenko, О. H. (2019) · Endocrine Regulations · doi:10.2478/enr-2019-0005 · Cited by 20
Kumar, V., Mesentier-Louro, L. A., Oh, A. J., Heng, K., Shariati, A., Huang, H., Hu, Y., & Liao, Y. J. (2019) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.18-24890 · Cited by 20
Weng, J., Chen, M., Lin, Q., Chen, J., Wang, S., & Fang, D. (2019) · Gene · doi:10.1016/j.gene.2019.144095 · Cited by 20
Pathogenic Effects of Impaired Retrieval between the Endoplasmic Reticulum and Golgi Complex
Kokubun, H., Jin, H., & Aoe, T. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20225614 · Cited by 20
Liu, X., Zhang, E., Yin, S., Zhao, C., Fan, L., & Hu, H. (2020) · Toxins · doi:10.3390/toxins12010055 · Cited by 20
Walenna, N. F., Kurihara, Y., Chou, B., Ishii, K., Soejima, T., & Hiromatsu, K. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.010683 · Cited by 20
Chow‐Shi‐Yée, M., Grondin, M., Ouellet, F., & Averill‐Bates, D. A. (2020) · Cell Stress and Chaperones · doi:10.1007/s12192-020-01115-y · 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
Huang, C.-C., Huang, C.-C., Su, C., Fang, K., Yen, C., Yen, C., Lin, C.-T., Lee, K.-I., Chen, Y.-W., Liu, S., et al. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094379 · Cited by 20
Maturation of the Na,K-ATPase in the Endoplasmic Reticulum in Health and Disease
Kryvenko, V., Vagin, O., Dada, L. A., Sznajder, J. I., & Vadász, I. (2021) · The Journal of Membrane Biology · doi:10.1007/s00232-021-00184-z · Cited by 21
Ling, C., Nie, P., Yao, L., Tang, Y., Hong, W., Liu, W., Fu, F., & Xu, H. (2021) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2021.112814 · Cited by 20
De novo sphingolipid biosynthesis necessitates detoxification in cancer cells
Spears, M. E., Lee, N., Hwang, S., Park, S. J., Carlisle, A. E., Li, R., Doshi, M. B., Armando, A. M., Gao, J., Simin, K. J., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111415 · Cited by 20
Liu, J., Ge, P., Luo, Y., Sun, Z., Luo, X., Li, H., Pei, B., Xun, L., Zhang, X., Jiang, Y., et al. (2025) · Drug Design Development and Therapy · doi:10.2147/dddt.s512207 · Cited by 20
The unfolded protein response transducer IRE1α promotes reticulophagy in podocytes
Navarro‐Betancourt, J. R., Papillon, J., Guillemette, J., Chung, C.-F., Iwawaki, T., & Cybulsky, A. V. (2022) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2022.166391 · Cited by 19
Mohan, S., Nair, A., Poornima, M. S., & Raghu, K. G. (2023) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2023.110365 · Cited by 19
New tool for diseases mechanism studies: Endoplasmic reticulum-targeted fluorescent probes
Tang, Q., Li, H., Hu, H., & Chen, L. (2023) · Dyes and Pigments · doi:10.1016/j.dyepig.2023.111634 · Cited by 19
Sonsalla, G., Malpartida, A. B., Riedemann, T., Gušić, M., Rusha, E., Bulli, G., Najas, S., Janjic, A., Hersbach, B. A., Smialowski, P., et al. (2024) · Neuron · doi:10.1016/j.neuron.2023.12.020 · Cited by 19
Roles of β-Cell Hypoxia in the Progression of Type 2 Diabetes
Yamagata, K., Tsuyama, T., & Sato, Y. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25084186 · Cited by 20
Harmon, R. M., Ayers, J., McCarthy, E. F., Kowalczyk, A. P., Green, K. J., & Simpson, C. L. (2024) · Journal of Investigative Dermatology · doi:10.1016/j.jid.2024.06.1289 · Cited by 20
STK25 regulates oxidative capacity and metabolic efficiency in adipose tissue
Sütt, S., Cansby, E., Paul, A., Amrutkar, M., Nuñez‐Durán, E., Kulkarni, N. M., Ståhlman, M., Borén, J., Laurencikiene, J., Howell, B. W., et al. (2018) · Journal of Endocrinology · doi:10.1530/joe-18-0182 · Cited by 19
Exploring Seipin: From Biochemistry to Bioinformatics Predictions
Sarmento, A. S. C., Medeiros, L. B. D. A., Agnez‐Lima, L. F., Lima, J. G., & Campos, J. T. A. D. M. (2018) · International Journal of Cell Biology · doi:10.1155/2018/5207608 · Cited by 19
Iwahashi, N., Ikezaki, M., Matsuzaki, I., Yamamoto, M., Toujima, S., Murata, S., Ihara, Y., & Ino, K. (2018) · Endocrinology · doi:10.1210/en.2018-00868 · Cited by 19
From Young to Old: AMPylation Hits the Brain
Sieber, S. A., Cappello, S., & Kielkowski, P. (2020) · Cell chemical biology · doi:10.1016/j.chembiol.2020.05.009 · Cited by 19
Srinivasan, M. P., Bhopale, K. K., Caracheo, A. A., Amer, S. M., Khan, S., Kaphalia, L., Loganathan, G., Balamurugan, A. N., & Kaphalia, B. S. (2020) · Biochemical Pharmacology · doi:10.1016/j.bcp.2020.114174 · Cited by 19
PERK in POMC neurons connects celastrol with metabolism
He, Z., Lieu, L., Dong, Y., Afrin, S., Chau, D., Kabahizi, A., Wallace, B., Cao, J., Hwang, E., Yao, T. S., et al. (2021) · JCI Insight · doi:10.1172/jci.insight.145306 · Cited by 19
In situ monitoring of protein transfer into nanoscale channels
Pan, Y., Wang, X., Li, H., Ren, J., Zhang, Y., Jordahl, D., Schuster, I., Farmakes, J., Hong, H., Yang, Z., et al. (2021) · Cell Reports Physical Science · doi:10.1016/j.xcrp.2021.100576 · Cited by 19
Lin, Z., Ni, L., Teng, C., Zhang, Z., Wu, L. H., Yu, J. H., Lu, X., & Lin, Z. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.745621 · Cited by 19
Huang, Z., Gong, J., Lin, W.-L., Feng, Z., Ma, Y., Tu, Y., Cai, X., Liu, J., Lv, C., Lv, X., et al. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.860757 · Cited by 19
Zhang, L., Pavicic, P. G., Datta, S., Song, Q., Xu, X., Wei, W., Su, F., Rayman, P. A., Zhao, C., & Hamilton, T. A. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.01390 · Cited by 19
Zha, J., Bi, S., Deng, M., Chen, K., Shi, P., Feng, L., He, J., Pu, X., Guo, C., Zhao, H., et al. (2021) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2021.174107 · Cited by 18
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
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