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 801–900 of 1,000
Emerging magic bullet: subcellular organelle-targeted cancer therapy
Yan, Y., Zhang, Y., Liu, J., Chen, B., & Wang, Y. (2024) · Medical Review · doi:10.1515/mr-2024-0044 · Cited by 14
Shi, J., Chen, L., Wang, X., & Ma, X. (2025) · Inflammation Research · doi:10.1007/s00011-025-01998-6 · Cited by 14
Yan, J.-J., Wang, Y., Shi, Z.-Y., Ding, Y.-Y., Wen, H.-Q., Wu, M., Sun, S., Cai, Y., & Zhang, Y. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.141488 · Cited by 14
Wei, Y., Zi, X., Zhai, J., Zhang, M., Li, J., Sun, Z., Ju, M., Zhang, X., & Shen, B. (2025) · Analytical Chemistry · doi:10.1021/acs.analchem.5c01131 · Cited by 14
Unfolded Protein Response: Cause or Consequence of Lipid and Lipoprotein Metabolism Disturbances?
Pinto, B., França, L. M., Laurindo, F. R. M., & Paes, A. M. D. A. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-11488-6_5 · Cited by 14
Pan, T. S., Zhang, L., Miao, K., & Wang, Y. (2020) · PubMed Central · Cited by 14
Cui, L., Li, C., Chen, B., Huang, H. H., Xia, Q., Li, X., Shen, Z., Ge, Z., & Wang, Y. (2020) · Microchimica Acta · doi:10.1007/s00604-020-04585-0 · Cited by 14
Tu, T., Li, B., Li, X., Zhang, B., Xiao, Y., Li, J., Qin, F., Liu, N., Sun, C., Liu, Q., et al. (2021) · Journal of Cardiology · doi:10.1016/j.jjcc.2021.08.012 · Cited by 14
Lipid Metabolism and Immune Checkpoints
Liao, Q., Zhou, Y., Xia, L., & Cao, D. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-981-33-6785-2_12 · Cited by 14
Agonal Factors Distort Gene-Expression Patterns in Human Postmortem Brains
Dai, R., Chen, Y., Dai, R., Jiang, Y. W., Tian, J., Liu, S., Xu, M. M., Li, M., Zhou, J., Liu, C., et al. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.614142 · Cited by 14
A Human Pan-Cancer System Analysis of Procollagen-Lysine, 2-Oxoglutarate 5-Dioxygenase 3 (PLOD3)
Gong, S., Duan, Y., Wu, C., Osterhoff, G., Schopow, N., & Kallendrusch, S. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22189903 · Cited by 14
Cardiac-specific CGI-58 deficiency activates the ER stress pathway to promote heart failure in mice
Xie, X., Tie, Y., Lai, S., Zhang, Y., Li, H., & Liu, Y. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-04282-7 · Cited by 14
Kuribara, T., & Totani, K. (2022) · Biology · doi:10.3390/biology11020199 · Cited by 14
Leyfman, Y., Emmanuel, N., Menon, G. P., Joshi, M., Wilkerson, W. B., Cappelli, J., Erick, T. K., Park, C. H., & Sharma, P. (2023) · Journal of Hematology & Oncology · doi:10.1186/s13045-023-01432-6 · Cited by 14
Subcellular localization and relevant mechanisms of human cancer‐related micropeptides
Deng, J., Xu, W., Jie, Y., & Chong, Y. (2023) · The FASEB Journal · doi:10.1096/fj.202301019rr · Cited by 14
Amyloid and immune homeostasis
Wang, Y., & Zhang, Y.-G. (2017) · Immunobiology · doi:10.1016/j.imbio.2017.10.038 · Cited by 14
Inositol-requiring enzyme 1α links palmitate-induced mTOR activation and lipotoxicity in hepatocytes
Chen, Y., Griffiths, A., Wang, J., Zhang, T., Song, Q., & Song, Z. (2020) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00165.2020 · Cited by 14
NUPR1 protects liver from lipotoxic injury by improving the endoplasmic reticulum stress response
Borrello, M. T., Emma, M. R., Listì, A., Rubis, M., Coslet, S., Augello, G., Cusimano, A., Cabibi, D., Porcasi, R., Giannitrapani, L., et al. (2021) · The FASEB Journal · doi:10.1096/fj.202002413rr · Cited by 14
Wang, X., Yuan, J., Wang, H., Gan, N., Zhang, Q., Liu, B., Wang, J., Shu, Z., Rao, L., Gou, X., et al. (2019) · The Journal of Immunology · doi:10.4049/jimmunol.1900248 · Cited by 14
Sensing molecular carbon dioxide: a translational focus for respiratory disease
Vadász, I., Cummins, E. P., Brotherton, D. H., Casalino-Matsuda, S. M., Dada, L. A., Green, O., King, D. T., Kryvenko, V., Shigemura, M., Sporn, P. H. S., et al. (2025) · Physiological Reviews · doi:10.1152/physrev.00022.2024 · Cited by 13
CD147/Basigin: From Integrative Molecular Hub to Translational Therapeutic Target
Yang, X., Huijie, B., & Chen, Z. (2025) · Advanced Science · doi:10.1002/advs.202518884 · Cited by 13
Li, Y., Lu, L., Zhang, G., Ji, G., & Xu, H. (2022) · PubMed Central · Cited by 13
Yazdi, M. D., Nassan, F. L., Кошелева, А., Wang, C., Xu, Z., Di, Q., Réquia, W. J., Comfort, N. T., Wu, H., Laurent, L. C., et al. (2023) · Environment International · doi:10.1016/j.envint.2023.107735 · Cited by 13
Tamayo-Molina, Y. S., Velilla, P. A., Hernández-Sarmiento, L. J., & Inchima, S. U. (2023) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2023.130397 · Cited by 13
Fujiwara, M., Ferdousi, F., & Isoda, H. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241813867 · Cited by 13
Rahmati, M., Kwesiga, M. P., Lou, J., Tan, A. L., & McDermott, M. (2024) · Frontiers in Bioscience-Landmark · doi:10.31083/j.fbl2901042 · Cited by 13
Braun, M., Ashkenazi, A., Beveridge, R. E., Castanedo, G. M., Wallweber, H. A., Beresini, M. H., Clark, K., Bruyn, T. D., Fu, L., Gibbons, P., et al. (2024) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.3c02425 · Cited by 13
Recent progress on the organelle targeted AlEgens for bioimaging and treatment of diseases
Ding, Q., Luo, Y., Hu, J. P., Zhang, S., Zhang, W., Feng, Y., Qian, K., Li, X., Cheng, Z., & Gu, M. (2024) · Chemical Engineering Journal · doi:10.1016/j.cej.2024.153395 · Cited by 13
Zhan, Z., Huang, R., Chai, L., Yang, H., Dai, Y.-C., Chen, M., Gu, G., & Lv, Y. (2024) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2024.136699 · Cited by 13
Ji, F., Zhang, J., Mao, L., Tan, Y., Ye, M., He, X., Zhao, Y., Liu, J., Zhang, Y., Zhang, N., et al. (2025) · Nature Communications · doi:10.1038/s41467-024-55745-2 · Cited by 13
When Proteins Go Berserk: The Unfolded Protein Response and ER Stress
Meiseles, D., Arbeli, N., & Dvela‐Levitt, M. (2025) · The Nephron journals/Nephron journals · doi:10.1159/000544971 · Cited by 14
Li, J., Zi, X., Fang, J., Liang, M., Ju, M., Sun, Z., Shen, B., & Zhang, X. (2025) · ACS Sensors · doi:10.1021/acssensors.5c00807 · Cited by 13
Zhang, H., Zhou, F., Zhenyu, P., Bu, X., Wang, Y., & Chen, F. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2017.07.046 · Cited by 13
He, R., Kong, Y., Peng, F., Li, L., Shi, H., & Liu, Z. (2020) · Journal of Proteomics · doi:10.1016/j.jprot.2020.103924 · Cited by 13
Dai, Q., Han, S., Liu, T., Zheng, J., Liu, C., Li, J., & Li, S. (2020) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.00274 · Cited by 13
Periplocin and cardiac glycosides suppress the unfolded protein response
Tokugawa, M., Inoue, Y., Ishiuchi, K., Kujirai, C., Matsuno, M., Ri, M., Itoh, Y., Miyajima, C., Morishita, D., Ohoka, N., et al. (2021) · Scientific Reports · doi:10.1038/s41598-021-89074-x · Cited by 13
MicroRNA-494 Regulates Endoplasmic Reticulum Stress in Endothelial Cells
Chatterjee, N., Fraile‐Bethencourt, E., Baris, A. M., Espinosa‐Díez, C., & Anand, S. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.671461 · Cited by 13
Wang, Y., Zhang, J., & Zheng, S. (2021) · Cancer Cell International · doi:10.1186/s12935-021-02167-5 · Cited by 13
Chaudhary, P., Sharma, S., Singh, R., & Arya, R. (2021) · Journal of Cellular Biochemistry · doi:10.1002/jcb.30148 · Cited by 13
Liu, Y., Liu, W.-F., Chen, W.-C., Li, W., Lin, Y.-L., Xu, C., & He, H. (2021) · Neurological Research · doi:10.1080/01616412.2021.1979750 · Cited by 13
Cetinkaya-Un, B., Ün, B., Akpolat, M., Andiç, F., & Yazır, Y. (2021) · Reproductive Sciences · doi:10.1007/s43032-021-00753-6 · Cited by 13
Feng, Y., Lang, J., Sun, B., Yan, Z., Zhao, Z., & Sun, G. (2023) · Neurological Research · doi:10.1080/01616412.2023.2170905 · Cited by 13
Yu, X., Ding, H., Wang, D., Ren, Z., Chen, B., Wu, Q., Yuan, T., Liu, Y., Zhang, L., Zhao, J., et al. (2023) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2023.110686 · Cited by 13
Liang, Y., Luo, X., Schefczyk, S., Muungani, L. T., Deng, H., Wang, B., Baba, H. A., Lu, M., Wedemeyer, H. H., Schmidt, H., et al. (2024) · JHEP Reports · doi:10.1016/j.jhepr.2024.101012 · Cited by 13
Fohlen, B., Tavernier, Q., Huynh, T. M., Caradeuc, C., Corre, D. L., Bertho, G., Cholley, B., & Pallet, N. (2017) · EBioMedicine · doi:10.1016/j.ebiom.2017.12.023 · Cited by 14
Arasi, F. P., Shahrestanaki, M. K., & Aghaei, M. (2018) · Journal of Cellular Physiology · doi:10.1002/jcp.27719 · Cited by 13
Huang, L., Liu, Z., Jiang, H., Li, L., & Fu, R. (2019) · Journal of Investigative Medicine · doi:10.1136/jim-2018-000953 · Cited by 13
UPR modulation of host immunity by Pseudomonas aeruginosa in cystic fibrosis
Bedi, B., Lin, K.-C., Maurice, N., Yuan, Z.-H., Bijli, K. M., Koval, M., Hart, C., Goldberg, J., Stecenko, A., & Sadikot, R. (2020) · Clinical science · doi:10.1042/cs20200066 · Cited by 11
Chen, M., Li, S., Hao, M.-L., Chen, J., Zhao, Z., Hong, S., Min, J., Tang, J., Hu, M., & Li, H. (2020) · FEBS Open Bio · doi:10.1002/2211-5463.12965 · Cited by 13
Aging alters the metabolic flux signature of the ER‐unfolded protein response in vivo in mice
Ward, C., Peng, L., Yuen, S., Halstead, J., Palacios, H. H., Nyangau, E., Mohammed, H., Ziari, N., Dandan, M., Frakes, A. E., et al. (2022) · Aging Cell · doi:10.1111/acel.13558 · Cited by 13
Németh, B. C., Demcsák, A., Geisz, A., & Sahin‐Tóth, M. (2022) · Scientific Reports · doi:10.1038/s41598-022-09595-x · Cited by 14
Chen, H., Liu, D., Hua, J., Wu, M., Hua, Y., Feng, C., He, Z., Moffett, P., & Zhang, K. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.111040 · Cited by 13
Light‐Induced Chiral Iron Copper Selenide Nanoparticles Prevent β‐Amyloidopathy In Vivo
Zhang, H., Hao, C., Qu, A., Sun, M., Xu, L., Xu, C., & Kuang, H. (2020) · Angewandte Chemie · doi:10.1002/ange.202002028 · Cited by 12
Zhao, W., Li, G., Zhang, Q., Chen, M., He, L., Wu, Z., Zhang, Y., Fan, M., Liang, Y., Zhang, W., et al. (2023) · Biochemical Pharmacology · doi:10.1016/j.bcp.2023.115453 · Cited by 15
Tukacs, V., Mittli, D., Hunyadi‐Gulyás, É., Hlatky, D., Medzihradszky, K. F., Darula, Z., Nyitrai, G., Czurkó, A., Juhász, G., Kardos, J., et al. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03215-z · Cited by 13
Non-Genomic Hallmarks of Aging—The Review
Holmannová, D., Borský, P., Kovaříková, H., Štveráková, T., Vošmik, M., Hruška, L., Fiala, Z., & Borská, L. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242015468 · Cited by 13
Ma, Z., Horrocks, J., Mir, D. A., Cox, M., Ruzga, M. N., Rollins, J. A., & Rogers, A. N. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1263344 · Cited by 12
Endoplasmic Reticulum Stress and Unfolded Protein Response in Vernal Keratoconjunctivitis
Leonardi, A., Donato, A. C., Rosani, U., Stefano, A. D., Cavarzeran, F., & Brun, P. (2024) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.65.4.23 · Cited by 12
Upadhayay, S., Soni, D., Dhureja, M., Temgire, P., Kumar, V., Arthur, R., & Kumar, P. (2025) · Molecular Neurobiology · doi:10.1007/s12035-025-04962-x · Cited by 12
Park, S., Jeong, I., & Kim, O. (2025) · Nutrients · doi:10.3390/nu17101682 · Cited by 12
Sangüesa, G., Montañés, J. C., Baena, M., Sánchez, R. M., Roglans, N., Alegret, M., & Laguna, J. C. (2018) · European Journal of Nutrition · doi:10.1007/s00394-018-1654-9 · Cited by 13
Ji, S., Sun, J. H., Bian, C., Huang, X., Chang, Z., Yang, M., Lu, R., & Ji, H. (2020) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/j.cbpb.2020.110479 · Cited by 12
Expression liabilities in a four‐chain bispecific molecule
Guo, C., Chen, F., Xiao, Q. F., Catterall, H. B., Robinson, J. H., Wang, Z., Mock, M. L., & Hubert, R. (2021) · Biotechnology and Bioengineering · doi:10.1002/bit.27850 · Cited by 12
Ward, C., Peng, L., Yuen, S., Chang, M., Karapetyan, R., Nyangau, E., Mohammed, H., Palacios, H. H., Ziari, N., Joe, L. K., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23031073 · Cited by 12
Luo, R., Liang, H., Zhang, W., Li, G., Zhao, K., Hua, W., Song, Y., & Cao, Y. (2022) · Acta Biochimica et Biophysica Sinica · doi:10.3724/abbs.2022024 · Cited by 12
Wu, Y., Meng, W., Guan, M., Zhao, X., Zhang, C., Fang, Q., Zhang, Y., Sun, Z., Cai, M., Huang, D., et al. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.963083 · Cited by 12
Deng, Q., Ding, K., Li, Y., Jiao, Y., Hu, R., Zhang, T., Wang, Z., & Tang, B. Z. (2022) · Biomaterials · doi:10.1016/j.biomaterials.2022.121767 · Cited by 12
Ettorre, G. M. (2022) · Updates in surgery/Updates in surgery series · doi:10.1007/978-3-031-09371-5 · Cited by 12
Zhuang, H., Hudson, E., Han, S., Arja, R. D., Hui, W. W. Y., Lu, L., & Reeves, W. H. (2022) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00051.2022 · Cited by 12
Feng, X., Yang, G., Zhang, L., Tao, S., Shim, J. S., Chen, L., & Wu, Q. (2022) · Investigational New Drugs · doi:10.1007/s10637-022-01306-7 · Cited by 12
Ssu72 phosphatase is essential for thermogenic adaptation by regulating cytosolic translation
Park, E., Kim, H. S., Lee, D.-H., Kim, S., Yoon, J.-S., Lee, J.-M., Im, S. J., Lee, H., Lee, M.-W., & Lee, C. (2023) · Nature Communications · doi:10.1038/s41467-023-36836-y · Cited by 12
Chlorogenic acid alleviates oxidative damage in hepatocytes by regulating miR-199a-5p/GRP78 axis
Li, J., Ge, H., Xu, Y., Xie, J., Karim, N., Yan, F., Mo, J., & Chen, W. (2023) · Food Bioscience · doi:10.1016/j.fbio.2023.102595 · Cited by 12
Natural products modulate cell apoptosis: a promising way for treating endometrial cancer
Zhou, X., Zeng, Y., Zheng, R., Wang, Y., Li, T., Song, S., Zhang, S., Huang, J., & Ren, Y. (2023) · Frontiers in Pharmacology · doi:10.3389/fphar.2023.1209412 · Cited by 12
Zeng, X., Geng, W.-S., Zhang, Y., Yin, J., Xu, G., Yu, M., Li, L., & Jia, J. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.102000 · Cited by 12
Guo, H., Hongyan, W., Lou, W., Khan, R. U., You, J., Huang, B., Shu, H., Li, G., & Dai, S. (2024) · International Journal of Biometeorology · doi:10.1007/s00484-024-02674-w · Cited by 12
Aghaei, M., Ghanadian, M., Sajjadi, S. E., Saghafian, R., & Shahrestanaki, M. K. (2018) · Fitoterapia · doi:10.1016/j.fitote.2018.06.024 · Cited by 12
Morphology Remodeling and Selective Autophagy of Intracellular Organelles during Viral Infections
Ren, S., Ding, C., & Sun, Y. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21103689 · Cited by 13
Hernández, R. B., Carrascal, M., Abián, J., Michalke, B., Farina, M., González, Y. R., Iyirhiaro, G. O., Moteshareie, H., Burnside, D. J., Golshani, A., et al. (2020) · Metallomics · doi:10.1039/d0mt00085j · Cited by 13
Wang, M., Liu, C. X., Li, Y., Zhang, Q., Zhu, L., Fang, Z., & Jin, L. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.01781 · Cited by 12
Self-citationZhao, S., Li, X., Lu, P., Li, X., Ming-fei, S., & Wang, H. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.646723 · Cited by 12
Ooi, C., Smith, T., Gluenz, E., Wand, N. V., Vaughan, S., & Rudenko, G. (2018) · Traffic · doi:10.1111/tra.12561 · Cited by 13
ER stress-related molecules induced by Hantaan virus infection in differentiated THP-1 cells
Li, Z., Shen, Y., Song, Y. J., Zhang, Y., Zhang, C., Ma, Y., Zhang, F., & Chen, L. (2020) · Cell Stress and Chaperones · doi:10.1007/s12192-020-01150-9 · Cited by 12
Yang, Y., Zhao, J., Gao, H.-B., Li, J.-J., Li, X., Niu, X., Lei, Y., & Li, X. (2021) · Molecular Medicine Reports · doi:10.3892/mmr.2021.12174 · Cited by 12
The unfolded protein response and the biology of uveal melanoma
Zhang, S., Wang, K., Zhu, X., Cherepanoff, S., Conway, R. M., Madigan, M. C., Zhu, L., Murray, M. T., & Zhou, F. (2022) · Biochimie · doi:10.1016/j.biochi.2022.01.017 · Cited by 11
α-Hederin induces human colorectal cancer cells apoptosis through disturbing protein homeostasis
Wang, Q., Feng, H., Li, Z., Wu, Q., Li, L., Sun, D., Tan, J., Fan, M., Yu, C., Xu, C., et al. (2023) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2023.110785 · Cited by 11
Sun, Z., Wang, J., Ji, Z., Ma, J., Chen, Y., & Jiao, G. (2024) · Biological Trace Element Research · doi:10.1007/s12011-023-04048-6 · Cited by 11
Niella, R. V., Corrêa, J. M. X., dos Santos, J. F. R., Lima, L. F., Marques, C. S. D. C., Santos, L. C., Santana, L. R., Silva, Á. J. C., Farias, K. S., Pirovani, C. P., et al. (2024) · PLoS ONE · doi:10.1371/journal.pone.0287390 · Cited by 11
Xue, J., Ren, H., Zhang, Q., Gu, J., Xu, Q., Sun, J., Zhang, L., & Zhou, M.-S. (2024) · Frontiers in Pharmacology · doi:10.3389/fphar.2024.1442831 · Cited by 11
A stress paradox: the dual role of the unfolded protein response in the placenta
Chowdhury, D., Jang, C. E., Lajoie, P., & Renaud, S. J. (2024) · Frontiers in Endocrinology · doi:10.3389/fendo.2024.1525189 · Cited by 12
Kumar, P., Mishra, T., Sanyam, S., Mondal, A., & Basu, S. (2025) · ACS Applied Bio Materials · doi:10.1021/acsabm.4c01722 · Cited by 11
Functional analysis of the mammalian RNA ligase for IRE1 in the unfolded protein response
Poothong, J., Tirasophon, W., & Kaufman, R. J. (2017) · Bioscience Reports · doi:10.1042/bsr20160574 · Cited by 11
Self-citationHan, S., Mao, L., Liao, Y., Sun, S., Zhang, Z., Mo, Y., Liu, H., Zhi, X., Lin, S., Seo, H. S., et al. (2019) · The Journal of Immunology · doi:10.4049/jimmunol.1801546 · Cited by 11
Endoplasmic Reticulum Stress Induced Proliferation Remains Intact in Aging Mouse β-Cells
Snyder, J. T., Darko, C., Sharma, R. B., & Alonso, L. C. (2021) · Frontiers in Endocrinology · doi:10.3389/fendo.2021.734079 · Cited by 12
Tian, J., Shi, H., Wang, X., Wu, H., Wang, C., Liu, N., Wang, D., Shi, D., Zhang, H., & Zhang, Z. (2022) · Environmental Science and Pollution Research · doi:10.1007/s11356-022-19496-1 · Cited by 11
Illuminating Sub‐Cellular Organelles by Small Molecule AIEgens
Ingle, J., Sengupta, P., & Basu, S. (2022) · ChemBioChem · doi:10.1002/cbic.202200370 · Cited by 11
Zhang, J., Tang, Y., Xu, W., Hu, Z., Xu, S., & Niu, Q. (2022) · Biological Trace Element Research · doi:10.1007/s12011-022-03463-5 · Cited by 11
Ma, J., Liu, Y., Valladolid‐Acebes, I., Recio-López, P., Peng, G., Li, J., Berggren, P., Juntti‐Berggren, L., & Tong, N. (2022) · Cellular Signalling · doi:10.1016/j.cellsig.2022.110535 · Cited by 11
Non-alcoholic fatty liver disease and liver secretome
Khan, M. S., Lee, C.-H., & Kim, S. G. (2022) · Archives of Pharmacal Research · doi:10.1007/s12272-022-01419-w · Cited by 13
Cendron, L., Rothenberger, S., Cassari, L., Dettin, M., & Pasquato, A. (2022) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2022.10.001 · Cited by 12
Role of the endoplasmic reticulum in the search for early biomarkers of meat quality
González‐Blanco, L., Sierra, V., Diñeiro, Y., Coto‐Montes, A. M., & Oliván, M. (2023) · Meat Science · doi:10.1016/j.meatsci.2023.109224 · Cited by 11
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