Cited by 1,630Endoplasmic Reticulum Stress and DiseaseHeat shock proteins researchCellular transport and secretion

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

Wang, Miao, Kaufman, Randal J.·2016·Nature

Open this paper in CoChat — free account

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.

Integrity signals

Registry

Crossref · 10.1038/nature17041

Cites

126 of 126 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

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?

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-citation
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
Self-citation
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
Self-citation
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

Show all 126 references

Sorted by citations

Items 301–400 of 1,000

Molecular regulation of hematopoietic stem cell quiescence
Chen, Z., Guo, Q., Song, G., & Hou, Y. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04200-w · Cited by 56
Apoptosis and its role in postmortem meat tenderness: A comprehensive review
Zhao, Y., Xiang, C., Roy, B. C., Bruce, H. L., Blecker, C. S., Zhang, Y., Liu, C., Zhang, D., Li, C., & Huang, C. (2024) · Meat Science · doi:10.1016/j.meatsci.2024.109652 · Cited by 51
Impaired calcium homeostasis via advanced glycation end products promotes apoptosis through endoplasmic reticulum stress in human nucleus pulposus cells and exacerbates intervertebral disc degeneration in rats
Luo, R., Song, Y., Liao, Z., Yin, H., Zhan, S., Wang, K., Li, S., Li, G., Ma, L., Lu, S., et al. (2019) · FEBS Journal · doi:10.1111/febs.14972 · Cited by 48
ER-Mitochondria Calcium Transfer, Organelle Contacts and Neurodegenerative Diseases
Vallese, F., Barazzuol, L., Maso, L., Brini, M., & Calí, T. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-12457-1_29 · Cited by 48
Unification of Opposites between Two Antioxidant Transcription Factors Nrf1 and Nrf2 in Mediating Distinct Cellular Responses to the Endoplasmic Reticulum Stressor Tunicamycin
Zhu, Y., Hu, S., Hu, S., Zheng, Z., Fan, Z., Qiu, L., & Zhang, Y. (2019) · Antioxidants · doi:10.3390/antiox9010004 · Cited by 48
Neuroprotective Effects of Thymoquinone by the Modulation of ER Stress and Apoptotic Pathway in In Vitro Model of Excitotoxicity
Landucci, E., Mazzantini, C., Buonvicino, D., Pellegrini-Giampietro, D. E., & Bergonzi, M. C. (2021) · Molecules · doi:10.3390/molecules26061592 · Cited by 48
Changes of Gut-Microbiota-Liver Axis in Hepatitis C Virus Infection
El‐Mowafy, M., Elgaml, A., El‐Mesery, M., Sultan, S., Ahmed, T. A., Gomaa, A. I., Aly, M., & Mottawea, W. (2021) · Biology · doi:10.3390/biology10010055 · Cited by 48
Advances in Enantiomer-Dependent Nanotherapeutics
Wang, Y., & Tay, A. K. P. (2023) · ACS Nano · doi:10.1021/acsnano.3c02798 · Cited by 47
Decoding the Tumor Microenvironment: Exosome-Mediated Macrophage Polarization and Therapeutic Frontiers
Li, Y., You, J., Zou, Z., Sun, G., Shi, Y., Sun, Y., Xu, S., & Zhang, X. (2025) · International Journal of Biological Sciences · doi:10.7150/ijbs.114222 · Cited by 48
Codelivery of GRP78 siRNA and docetaxel via RGD-PEG-DSPE/DOPA/CaP nanoparticles for the treatment of castration-resistant prostate cancer
Zhang, X., He, Z., Xiang, L., Li, L., Zhang, H., Lin, F., & Cao, H. (2019) · Drug Design Development and Therapy · doi:10.2147/dddt.s198400 · Cited by 48
Hepatitis B Surface Antigen Activates Unfolded Protein Response in Forming Ground Glass Hepatocytes of Chronic Hepatitis B
Li, Y., Xia, Y., Cheng, X., Kleiner, D. E., Hewitt, S. M., Sproch, J., Li, T., Zhuang, H., & Liang, T. J. (2019) · Viruses · doi:10.3390/v11040386 · Cited by 47
Lipid Nanoparticle-Mediated Induction of Endoplasmic Reticulum Stress in Cancer Cells
Ghosh, C., Nandi, A., & Basu, S. (2019) · ACS Applied Bio Materials · doi:10.1021/acsabm.9b00532 · Cited by 47
Light-induced modulation of the mitochondrial respiratory chain activity: possibilities and limitations
Lunová, M., Smolková, B., Uzhytchak, M., Janoušková, K. Ž., Jirsa, M., Egorova, D., Kulikov, A. V., Kubinová, Š., Dejneka, A., & Lunov, O. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03321-z · Cited by 47
Hypoxia: Turning vessels into vassals of cancer immunotolerance
Schito, L., & Rey, S. (2020) · Cancer Letters · doi:10.1016/j.canlet.2020.05.015 · Cited by 49
Pathological Aspects of COVID-19 as a Conformational Disease and the Use of Pharmacological Chaperones as a Potential Therapeutic Strategy
Aoe, T. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.01095 · Cited by 47
Acute Intermittent Porphyria: An Overview of Therapy Developments and Future Perspectives Focusing on Stabilisation of HMBS and Proteostasis Regulators
Bustad, H. J., Kallio, J. P., Vorland, M., Fiorentino, V., Sandberg, S., Schmitt, C., Aarsand, A. K., & Martı́nez, A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22020675 · Cited by 49
Kaempferol Alleviates Steatosis and Inflammation During Early Non-Alcoholic Steatohepatitis Associated With Liver X Receptor α-Lysophosphatidylcholine Acyltransferase 3 Signaling Pathway
Xiang, H., Shao, M., Lu, Y., Wang, J., Wu, T., & Ji, G. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.690736 · Cited by 46
Integrated traditional Chinese and Western medicine in the prevention and treatment of non-alcoholic fatty liver disease: future directions and strategies
Ding, X., He, X., Tang, B., & Lan, T. (2024) · Chinese Medicine · doi:10.1186/s13020-024-00894-1 · Cited by 49
XBP1s activates METTL3/METTL14 for ER-phagy and paclitaxel sensitivity regulation in breast cancer
Wang, J., Fan, P., Shen, P., Fan, C., Zhao, P., Shen, Y., Dong, K., Ling, R., Chen, S., & Zhang, J. (2024) · Cancer Letters · doi:10.1016/j.canlet.2024.216846 · Cited by 46
Inhibition of Endoplasmic Reticulum Stress Cooperates with SLC7A11 to Promote Disulfidptosis and Suppress Tumor Growth upon Glucose Limitation
Wang, J., Chen, J., Fan, K., Wang, M., Gao, M., Ren, Y., Wu, S., He, Q., Tu, K., Xu, Q., et al. (2024) · Advanced Science · doi:10.1002/advs.202408789 · Cited by 46
Self-citation
Specification of Physiologic and Disease States by Distinct Proteins and Protein Conformations
Jarosz, D. F., & Khurana, V. (2017) · Cell · doi:10.1016/j.cell.2017.10.047 · Cited by 46
Gene Therapy Strategies to Restore ER Proteostasis in Disease
Valenzuela, V., Jackson, K. L., Sardi, S. P., & Hetz, C. A. (2018) · Molecular Therapy · doi:10.1016/j.ymthe.2018.04.004 · Cited by 50
Knockdown of IRE1ɑ suppresses metastatic potential of colon cancer cells through inhibiting FN1-Src/FAK-GTPases signaling
Xie, Y., Liu, C., Qin, Y., Chen, J., & Fang, J. S. (2019) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2019.105572 · Cited by 46
ATF6 as a Nodal Regulator of Proteostasis in the Heart
Glembotski, C. C., Arrieta, A., Blackwood, E. A., & Stauffer, W. T. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.00267 · Cited by 46
Salidroside alleviated hypoxia-induced liver injury by inhibiting endoplasmic reticulum stress-mediated apoptosis via IRE1α/JNK pathway
Xiong, Y., Wang, Y., Xiong, Y., Gao, W., & Teng, L. (2020) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2020.06.036 · Cited by 46
Overview of biological effects of melatonin on testis: A review
Heidarizadi, S., Rashidi, Z., Jalili, C., & Gholami, M. (2022) · Andrologia · doi:10.1111/and.14597 · Cited by 45
Ire1α in Pomc Neurons Is Required for Thermogenesis and Glycemia
Yao, T. S., Deng, Z., Gao, Y., Sun, J. M., Kong, X., Huang, Y., He, Z., Xu, Y., Chang, Y., Yu, K.-J., et al. (2016) · Diabetes · doi:10.2337/db16-0533 · Cited by 46
Self-citation
ER stress and cancer: The FOXO forkhead transcription factor link
Alasiri, G. A., Fan, L. Y.-N., Zona, S., Goldsbrough, I., Ke, H., Auner, H. W., & Lam, E. W. ‐. (2017) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2017.05.027 · Cited by 45
Glucose-regulated protein 78 is essential for cardiac myocyte survival
Wang, X., Bi, X., Zhang, G., Deng, Y., Luo, X., Xu, L., Scherer, P. E., Ferdous, A., Fu, G., Gillette, T. G., et al. (2018) · Cell Death and Differentiation · doi:10.1038/s41418-018-0109-4 · Cited by 45
Perfluoroalkyl acid exposure induces protective mitochondrial and endoplasmic reticulum autophagy in lung cells
Yan, X., Wan, B., Yang, Y., Cui, X., Xie, Y., & Guo, L. (2018) · Archives of Toxicology · doi:10.1007/s00204-018-2266-0 · Cited by 45
A Maleimide‐functionalized Tetraphenylethene for Measuring and Imaging Unfolded Proteins in Cells
Zhang, S., Liu, M., Tan, L. Y. F., Hong, Q., Pow, Z. L., Owyong, T. C., Ding, S., Wong, W. W. H., & Hong, Y. (2019) · Chemistry - An Asian Journal · doi:10.1002/asia.201900150 · Cited by 46
Targeting of the unfolded protein response (UPR) as therapy for Parkinson's disease
Martinez, A. N., López, N., González, C., & Hetz, C. A. (2019) · Biology of the Cell · doi:10.1111/boc.201800068 · Cited by 45
BDE-209 induces autophagy and apoptosis via IRE1α/Akt/mTOR signaling pathway in human umbilical vein endothelial cells
Hou, Y., Fu, J., Sun, S., Jin, Y., Wang, X., & Zhang, L. (2019) · Environmental Pollution · doi:10.1016/j.envpol.2019.07.030 · Cited by 45
The UPRosome – decoding novel biological outputs of IRE1α function
Urra, H., Pihán, P., & Hetz, C. A. (2020) · Journal of Cell Science · doi:10.1242/jcs.218107 · Cited by 45
FGF, Mechanism of Action, Role in Parkinson’s Disease, and Therapeutics
Liu, Y., Deng, J., Liu, Y., Li, W., & Nie, X. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.675725 · Cited by 46
A comprehensive analysis of prefoldins and their implication in cancer
Herranz-Montoya, I., Park, S., & Djouder, N. (2021) · iScience · doi:10.1016/j.isci.2021.103273 · Cited by 45
Targeting translation: a promising strategy for anticancer metallodrugs
Ortega, E., Vigueras, G., Ballester, F. J., & Ruiz, J. (2021) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2021.214129 · Cited by 44
Chemical Chaperones to Inhibit Endoplasmic Reticulum Stress: Implications in Diseases
Jeon, J.-H., Im, S., Kim, H. S., Lee, D., Jeong, K., Ku, J., & Nam, T. (2022) · Drug Design Development and Therapy · doi:10.2147/dddt.s393816 · Cited by 44
Single Molecule Protein Segments Sequencing by a Plasmonic Nanopore
Zhou, J., Lan, Q., Li, W., Ji, L., Wang, K., & Xia, X. (2023) · Nano Letters · doi:10.1021/acs.nanolett.3c00086 · Cited by 44
Adaptive preconditioning in neurological diseases – therapeutic insights from proteostatic perturbations
Mollereau, B., Rzechorzek, N. M., Roussel, B. D., Sedru, M., van den Brink, D. M., Bailly‐Maitre, B., Palladino, F., Medinas, D. B., Domingos, P. M., Hunot, S., et al. (2016) · Brain Research · doi:10.1016/j.brainres.2016.02.033 · Cited by 46
Self-citation
N-acetylcysteine alleviates cadmium-induced placental endoplasmic reticulum stress and fetal growth restriction in mice
Guo, M.-Y., Wang, H., Chen, Y., Xia, M., Zhang, C., & Xu, D. (2018) · PLoS ONE · doi:10.1371/journal.pone.0191667 · Cited by 44
Confirming a critical role for death receptor 5 and caspase-8 in apoptosis induction by endoplasmic reticulum stress
Lam, M., Lawrence, D. A., Ashkenazi, A., & Walter, P. (2018) · Cell Death and Differentiation · doi:10.1038/s41418-018-0155-y · Cited by 44
Metabolic perturbations and cellular stress underpin susceptibility to symptomatic live-attenuated yellow fever infection
Chan, K. R., Gan, E. S., Chan, C. Y. Y., Liang, C., Low, J. Z. H., Zhang, S. L.-X., Ong, E. Z., Bhatta, A., Wijaya, L., Lee, Y. H., et al. (2019) · Nature Medicine · doi:10.1038/s41591-019-0510-7 · Cited by 44
Mitochondrial Peptide Humanin Protects Silver Nanoparticles-Induced Neurotoxicity in Human Neuroblastoma Cancer Cells (SH-SY5Y)
Gurunathan, S., Jeyaraj, M., Kang, M.-H., & Kim, J. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20184439 · Cited by 44
Sestrin2 protects dendritic cells against endoplasmic reticulum stress-related apoptosis induced by high mobility group box-1 protein
Wang, L., Zhu, X., Luo, Y., Wu, Y., Dong, N., Tong, Y., & Yao, Y.-M. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-2324-4 · Cited by 44
Activation of the IRE1 RNase through remodeling of the kinase front pocket by ATP-competitive ligands
Ferri, E., Thomas, A. L., Wallweber, H. A., Day, E. S., Walters, B. T., Kaufman, S. E., Braun, M., Clark, K., Beresini, M. H., Mortara, K. D., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-19974-5 · Cited by 44
Endoplasmic Reticulum-Mitochondria Contacts: A Potential Therapy Target for Cardiovascular Remodeling-Associated Diseases
Wang, Y., Zhang, X., Wen, Y., Li, S., Lu, X., Xu, R., & Li, C. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.774989 · Cited by 46
Histone Acetyltransferases and Deacetylases Are Required for Virulence, Conidiation, DNA Damage Repair, and Multiple Stresses Resistance of Alternaria alternata
Ma, H., Li, L., Gai, Y., Zhang, X., Chen, Y., Zhuo, X., Cao, Y., Jiao, C., Gmitter, F. G., & Li, H. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.783633 · Cited by 45
Functional Materials for Subcellular Targeting Strategies in Cancer Therapy: Progress and Prospects
Cheng, Y., Qu, Z., Jiang, Q., Xu, T., Zheng, H., Ye, P., He, M., Tong, Y., Ma, Y., & Bao, A. (2023) · Advanced Materials · doi:10.1002/adma.202305095 · Cited by 43
Nanocarriers Targeting Circular RNA ADARB1 Boost Radiosensitivity of Nasopharyngeal Carcinoma through Synergically Promoting Ferroptosis
Wang, D., Tang, L. M., Chen, M., Gong, Z., Fan, C., Qu, H., Liu, Y., Shi, L., Mo, Y., Wang, Y., et al. (2024) · ACS Nano · doi:10.1021/acsnano.4c07676 · Cited by 44
Expression of a hepatitis B virus pre‐ S2 deletion mutant in the liver results in hepatomegaly and hepatocellular carcinoma in mice
Teng, Y., Neo, J. C., Wu, J., Chen, Y., Kao, C., & Tsai, T. (2016) · The Journal of Pathology · doi:10.1002/path.4850 · Cited by 43
When proteostasis goes bad: Protein aggregation in the cell
Radwan, M., Wood, R. J., Sui, X., & Hatters, D. M. (2017) · IUBMB Life · doi:10.1002/iub.1597 · Cited by 44
Oxidative stress promotes SIRT1 recruitment to the GADD34/PP1α complex to activate its deacetylase function
Lee, I. C. J., Ho, X. Y., George, S. E., Goh, C. W., Sundaram, J. R., Pang, K. K. L., Luo, W., Yusoff, P., Sze, N. S. K., & Shenolikar, S. (2017) · Cell Death and Differentiation · doi:10.1038/cdd.2017.152 · Cited by 43
Endoplasmic Reticulum Stress and Allergic Diseases
Jeong, J. S., Kim, S. R., Cho, S., & Lee, Y. C. (2017) · Current Allergy and Asthma Reports · doi:10.1007/s11882-017-0751-9 · Cited by 43
Chronic oxidative stress promotes GADD34-mediated phosphorylation of the TAR DNA-binding protein TDP-43, a modification linked to neurodegeneration
Goh, C. W., Lee, I. C. J., Sundaram, J. R., George, S. E., Yusoff, P., Brush, M., Sze, N. S. K., & Shenolikar, S. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.814111 · Cited by 49
Resveratrol synergizes with cisplatin in antineoplastic effects against AGS gastric cancer cells by inducing endoplasmic reticulum stress‑mediated apoptosis and G2/M phase arrest
Ren, M., Zhou, X., Gu, M., Jiao, W.-R., Yu, M., Wang, Y., Liu, S., Yang, J., & Ji, F. (2020) · Oncology Reports · doi:10.3892/or.2020.7708 · Cited by 43
Phosphorylation of EIF2S1 (eukaryotic translation initiation factor 2 subunit alpha) is indispensable for nuclear translocation of TFEB and TFE3 during ER stress
Dang, T. T., Kim, M., Lee, Y. Y., Le, H. T., Kim, K. H., Nam, S., Hyun, S. H., Kim, H. L., Chung, S. W., Chung, H., et al. (2023) · Autophagy · doi:10.1080/15548627.2023.2173900 · Cited by 42
ER Stress and Neurodegenerative Disease: A Cause or Effect Relationship?
Cabral‐Miranda, F., & Hetz, C. A. (2017) · Current topics in microbiology and immunology · doi:10.1007/82_2017_52 · Cited by 46
Shiga Toxin Therapeutics: Beyond Neutralization
Hall, G., Kurosawa, S., & Stearns-Kurosawa, D. J. (2017) · Toxins · doi:10.3390/toxins9090291 · Cited by 42
Proteostasis in the Endoplasmic Reticulum: Road to Cure
Nam, S. M., & Jeon, Y. J. (2019) · Cancers · doi:10.3390/cancers11111793 · Cited by 45
Cerebral dopamine neurotrophic factor–deficiency leads to degeneration of enteric neurons and altered brain dopamine neuronal function in mice
Lindahl, M., Chalazonitis, A., Palm, E., Pakarinen, E., Danilova, T., Pham, T. D., Setlik, W., Rao, M., Võikar, V., Huotari, J., et al. (2019) · Neurobiology of Disease · doi:10.1016/j.nbd.2019.104696 · Cited by 44
Enforced dimerization between XBP1s and ATF6f enhances the protective effects of the UPR in models of neurodegeneration
Vidal, R. L., Sepúlveda, D., Troncoso-Escudero, P., García-Huerta, P., González, C., Plate, L., Jerez, C., Cánovas, J., Rivera, C. A., Castillo, V., et al. (2021) · Molecular Therapy · doi:10.1016/j.ymthe.2021.01.033 · Cited by 44
Organelles coordinate milk production and secretion during lactation: Insights into mammary pathologies
Dai, W., White, R. R., Liu, J., & Liu, H. (2022) · Progress in Lipid Research · doi:10.1016/j.plipres.2022.101159 · Cited by 42
Dominant and recessive mutations in rhodopsin activate different cell death pathways
Comitato, A., Salvo, M. T. D., Turchiano, G., Montanari, M., Sakami, S., Palczewski, K., & Marigo, V. (2016) · Human Molecular Genetics · doi:10.1093/hmg/ddw137 · Cited by 44
Beta-elemene: A phytochemical with promise as a drug candidate for tumor therapy and adjuvant tumor therapy
Feng, Y., An, Q., Zhao, Z., Wu, M., Yang, C., Liang, W., Xu, X., Jiang, T., & Zhang, G. (2024) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2024.116266 · Cited by 42
Role of the unfolded protein response in tumor cell characteristics and cancer outcome
Galmiche, A., Sauzay, C., Chevet, É., & Pluquet, O. (2016) · Current Opinion in Oncology · doi:10.1097/cco.0000000000000339 · Cited by 41
Taurine ameliorated homocysteine-induced H9C2 cardiomyocyte apoptosis by modulating endoplasmic reticulum stress
Zhang, Z., Zhao, L., Zhou, Y., Lu, X., Wang, Z., Wang, J., & Li, W. (2017) · APOPTOSIS · doi:10.1007/s10495-017-1351-9 · Cited by 41
Ready player one? Autophagy shapes resistance to photodynamic therapy in cancers
Duan, X., Chen, B., Cui, Y., Zhou, L., Wu, C., Yang, Z., Wen, Y., Miao, X., Li, Q., Xiong, L., et al. (2018) · APOPTOSIS · doi:10.1007/s10495-018-1489-0 · Cited by 43
Endoplasmic reticulum stress mediates inflammatory response triggered by ultra-small superparamagnetic iron oxide nanoparticles in hepatocytes
He, C., Jiang, S., Yao, H., Zhang, L., Yang, C., Zhan, D.-L., Lin, G., Zeng, Y., Xia, Y., Lin, Z., et al. (2018) · Nanotoxicology · doi:10.1080/17435390.2018.1530388 · Cited by 41
Impact of chrysin on the molecular mechanisms underlying diabetic complications
Farkhondeh, T., Samarghandian, S., & Roshanravan, B. (2019) · Journal of Cellular Physiology · doi:10.1002/jcp.28488 · Cited by 41
4-Phenylbutyric Acid Reduces Endoplasmic Reticulum Stress in Chondrocytes That Is Caused by Loss of the Protein Disulfide Isomerase ERp57
Rellmann, Y., Gronau, I., Hansen, U. J., & Dreier, R. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/6404035 · Cited by 42
Catestatin improves insulin sensitivity by attenuating endoplasmic reticulum stress: In vivo and in silico validation
Dasgupta, A., Bandyopadhyay, G. K., Ray, I., Bandyopadhyay, K., Chowdhury, N., De, R. K., & Mahata, S. K. (2020) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2020.02.005 · Cited by 41
SESN2 protects against denervated muscle atrophy through unfolded protein response and mitophagy
Yang, X., Xue, P., Yuan, M., Xu, X., Wang, C., Li, W., Machens, H., & Chen, Z. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-04094-9 · Cited by 41
Current and prospective strategies for advancing the targeted delivery of CRISPR/Cas system via extracellular vesicles
Huang, X., Li, A., Xu, P., Yu, Y., Li, S., Hu, L., & Feng, S. (2023) · Journal of Nanobiotechnology · doi:10.1186/s12951-023-01952-w · Cited by 43
Dysregulated mast cell activation induced by diabetic milieu exacerbates the progression of diabetic peripheral neuropathy in mice
Yao, X., Wang, X., Zhang, R., Kong, L., Fan, C., & Qian, Y. (2025) · Nature Communications · doi:10.1038/s41467-025-59562-z · Cited by 40
Endoplasmic Reticulum Stress Signaling Pathways: Activation and Diseases
Zheng, Z. J., Shang, Y., Tao, J., Zhang, J., & Sha, B. (2019) · Current Protein and Peptide Science · doi:10.2174/1389203720666190621103145 · Cited by 40
SDF2-like protein 1 (SDF2L1) regulates the endoplasmic reticulum localization and chaperone activity of ERdj3 protein
Hanafusa, K., Wada, I., & Hosokawa, N. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.009603 · Cited by 40
Advances in the Development of Pharmacological Chaperones for the Mucopolysaccharidoses
Diaz, J. C., Castillo, J. C. D., Rodríguez‐López, A., & Alméciga-Díaz, C. J. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms21010232 · Cited by 42
Protective Properties of FOXO1 Inhibition in a Murine Model of Non-alcoholic Fatty Liver Disease Are Associated With Attenuation of ER Stress and Necroptosis
Ding, H., Tang, Z.-T., Tang, N., Zhu, Z., Liu, H., Pan, C.-Y., Hu, A., Lin, Y., Gou, P., Yuan, X., et al. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.00177 · Cited by 40
Caveolin-1 suppresses tumor formation through the inhibition of the unfolded protein response
Díaz, M. I., Díaz, P., Bennett, J. C., Urra, H., Ortiz, R. J., Contreras-Orellana, P., Hetz, C. A., & Quest, A. F. G. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-02792-4 · Cited by 40
Emerging Roles of Tripartite Motif-Containing Family Proteins (TRIMs) in Eliminating Misfolded Proteins
Zhang, L., Afolabi, L. O., Wan, X., Li, Y., & Chen, L. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00802 · Cited by 41
Exosomes of oral squamous cell carcinoma cells containing miR-181a-3p induce muscle cell atrophy and apoptosis by transmissible endoplasmic reticulum stress signaling
Qiu, L., Chen, W., Wu, C., Yuan, Y., & Li, Y. (2020) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2020.09.066 · Cited by 40
A review and analysis of the clinical literature on Charcot–Marie–Tooth disease caused by mutations in neurofilament protein L
Stone, E. J., Kolb, S. J., & Brown, A. (2021) · Cytoskeleton · doi:10.1002/cm.21676 · Cited by 40
The function of SUMOylation and its crucial roles in the development of neurological diseases
Chen, X., Zhang, Y., Wang, Q., Qin, Y., Yang, X., Xing, Z., Shen, Y., Wu, H., & Qi, Y. (2021) · The FASEB Journal · doi:10.1096/fj.202002702r · Cited by 39
Astaxanthin treatment ameliorates ER stress in polycystic ovary syndrome patients: a randomized clinical trial
Jabarpour, M., Aleyasin, A., Nashtaei, M. S., Lotfi, S., & Amidi, F. (2023) · Scientific Reports · doi:10.1038/s41598-023-28956-8 · Cited by 39
Mechanisms of Biological Effects of Ionic Liquids: From Single Cells to Multicellular Organisms
Egorova, K. S., Кибардин, А. В., Posvyatenko, A. V., & Ananikov, V. P. (2024) · Chemical Reviews · doi:10.1021/acs.chemrev.3c00420 · Cited by 40
Ferroptosis and endoplasmic reticulum stress in rheumatoid arthritis
Ao, Q., Hu, H., & Huang, Y. S. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1438803 · Cited by 39
NF-Y (CBF) regulation in specific cell types and mouse models
Maity, S. N. (2016) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2016.10.014 · Cited by 39
Uncertainty in an era of transformative therapy for haemophilia: Addressing the unknowns
Pierce, G. F. (2020) · Haemophilia · doi:10.1111/hae.14023 · Cited by 39
Restoring the epigenetically silenced PCK2 suppresses renal cell carcinoma progression and increases sensitivity to sunitinib by promoting endoplasmic reticulum stress
Xiong, Z., Yuan, C., Shi, J., Xiong, W., Huang, Y., Xiao, W., Yang, H., Chen, K., & Zhang, X. (2020) · Theranostics · doi:10.7150/thno.48469 · Cited by 39
Phosphorylation of SNX27 by MAPK11/14 links cellular stress–signaling pathways with endocytic recycling
Mao, L., Liao, C., Qin, J., Gong, Y., Zhou, Y., Li, S., Liu, Z., Deng, H., Deng, W., Sun, Q., et al. (2021) · The Journal of Cell Biology · doi:10.1083/jcb.202010048 · Cited by 40
In vivo screen identifies a SIK inhibitor that induces β cell proliferation through a transient UPR
Charbord, J., Ren, L., Sharma, R. B., Johansson, A., Ågren, R., Chu, L., Tworus, D., Schulz, N., Charbord, P., Stewart, A. F., et al. (2021) · Nature Metabolism · doi:10.1038/s42255-021-00391-x · Cited by 39
Emerging roles of ER-resident selenoproteins in brain physiology and physiopathology
Jehan, C., Cartier, D., Bucharles, C., Anouar, Y., & Lihrmann, I. (2022) · Redox Biology · doi:10.1016/j.redox.2022.102412 · Cited by 41
Activation of UPR Signaling Pathway is Associated With the Malignant Progression and Poor Prognosis in Prostate Cancer
Liu, J., Xiao, M., Li, J., Wang, D., He, Y., He, J., Gao, F., Mai, L., Li, Y., Liang, Y., et al. (2016) · The Prostate · doi:10.1002/pros.23264 · Cited by 39
Up‐regulation of golgi α‐mannosidase IA and down‐regulation of golgi α‐mannosidase IC activates unfolded protein response during hepatocarcinogenesis
Tu, H., Hsiao, Y., Yang, W., Tsai, S., Lin, H., Liao, C., Lu, J., Chou, Y., Wang, H., & Yuh, C. (2017) · Hepatology Communications · doi:10.1002/hep4.1032 · Cited by 39
Systematic Review of Calcium Channels and Intracellular Calcium Signaling: Relevance to Pesticide Neurotoxicity
Costas‐Ferreira, C., & Faro, L. R. F. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222413376 · Cited by 39
Update of treatment for Gaucher disease
Kong, W., Lu, C., Ding, Y., & Meng, Y. (2022) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2022.175023 · Cited by 38
Reduced Endoplasmic Reticulum Stress-Mediated Autophagy Is Required for Leptin Alleviating Inflammation in Adipose Tissue
Gan, L., Liu, Z., Luo, D., Ren, Q., Wu, H., Li, C., & Sun, C. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.01507 · Cited by 38
CTRP3 attenuates high-fat diet-induced male reproductive dysfunction in mice
Yang, M., Yin, T., Yin, L., Hu, X., & Yang, J. (2018) · Clinical Science · doi:10.1042/cs20180179 · Cited by 38
Role of amino acid metabolism in angiogenesis
Oberkersch, R. E., & Santoro, M. M. (2018) · Vascular Pharmacology · doi:10.1016/j.vph.2018.11.001 · Cited by 38

Authors: Wang, M., & Kaufman, R. J.
Affiliations: Sanford Burnham Prebys Medical Discovery Institute (US)
Corresponding author: Kaufman, Randal J.
ORCID: Wang, Miao
Kaufman, Randal J.
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 2016-01
Volume: 529
Issue: 7586
Pages: 326-335
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/nature17041
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

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

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks