ER Stress Induces Cleavage of Membrane-Bound ATF6 by the Same Proteases that Process SREBPs

The SREBP pathway: regulation of cholesterol metabolism by proteolysis of a membrane-bound transcription factor

Brown, M. S., & Goldstein, J. L. (1997) · Cell · doi:10.1016/s0092-8674(00)80213-5 · Cited by 3,834

Mammalian Transcription Factor ATF6 Is Synthesized as a Transmembrane Protein and Activated by Proteolysis in Response to Endoplasmic Reticulum Stress

Haze, K., Yoshida, H., Yanagi, H., Yura, T., & Mori, K. (1999) · Molecular Biology of the Cell · doi:10.1091/mbc.10.11.3787 · Cited by 2,100

[19] Receptor-mediated endocytosis of low-density lipoprotein in cultured cells

Goldstein, J. L., Basu, S. K., & Brown, M. S. (1983) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(83)98152-1 · Cited by 1,629

Amino Acid Preferences for Specific Locations at the Ends of α Helices

Richardson, J. S., & Richardson, D. C. (1988) · Science · doi:10.1126/science.3381086 · Cited by 1,364

Regulated Intramembrane Proteolysis

Brown, M. S., Ye, J., Rawson, R. B., & Goldstein, J. L. (2000) · Cell · doi:10.1016/s0092-8674(00)80675-3 · Cited by 1,329

Identification of the cis-Acting Endoplasmic Reticulum Stress Response Element Responsible for Transcriptional Induction of Mammalian Glucose-regulated Proteins

Yoshida, H., Haze, K., Yanagi, H., Yura, T., & Mori, K. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.50.33741 · Cited by 1,229

SREBP-1, a membrane-bound transcription factor released by sterol-regulated proteolysis

Wang, X., Sato, R., Brown, M. S., Hua, X., & Goldstein, J. L. (1994) · Cell · doi:10.1016/0092-8674(94)90234-8 · Cited by 1,003

Activation of ATF6 and an ATF6 DNA Binding Site by the Endoplasmic Reticulum Stress Response

Wang, Y., Shen, J., Arenzana, N., Tirasophon, W., Kaufman, R. J., & Prywes, R. (2000) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)61473-0 · Cited by 622

Activation of ATF6 and an ATF6 DNA binding site by the endoplasmic reticulum stress response.

Wang, Y., Shen, J., Arenzana, N., et al. (2000) · PubMed · doi:10.1074/jbc.m003322200 · Cited by 539

Sterol-Regulated Release of SREBP-2 from Cell Membranes Requires Two Sequential Cleavages, One Within a Transmembrane Segment

Sakai, J., Duncan, E. A., Rawson, R. B., Hua, X., Brown, M. S., & Goldstein, J. L. (1996) · Cell · doi:10.1016/s0092-8674(00)81304-5 · Cited by 486

Endoplasmic reticulum association and N‐linked glycosylation of the human Nrf3 transcription factor

Nouhi, Z., Chevillard, G., Derjuga, A., & Blank, V. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.10.041 · Cited by 44

Insights into the underlying pathogenesis and therapeutic potential of endoplasmic reticulum stress in degenerative musculoskeletal diseases

Wen, Z., Lin, J., Xie, W., Shan, Y., Zhen, G., & Li, Y. (2023) · Military Medical Research · doi:10.1186/s40779-023-00485-5 · Cited by 45

Class I histone deacetylases localize to the endoplasmic reticulum and modulate the unfolded protein response

Kahali, S., Sarcar, B., Prabhu, A. H., Seto, E., & Chinnaiyan, P. (2012) · The FASEB Journal · doi:10.1096/fj.11-193706 · Cited by 42

Enhanced cellular cholesterol efflux by naringenin is mediated through inhibiting endoplasmic reticulum stress - ATF6 activity in macrophages

Xu, X., Lei, T., Li, W., & Ou, H. (2019) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2019.06.005 · Cited by 42

Atf6α impacts cell number by influencing survival, death and proliferation

Sharma, R. B., Snyder, J. T., & Alonso, L. C. (2019) · Molecular Metabolism · doi:10.1016/j.molmet.2019.06.005 · Cited by 44

An Emerging Role for the Unfolded Protein Response in Pancreatic Cancer

Robinson, C. M., Talty, A., Logue, S. E., Mnich, K., Gorman, A. M., & Samali, A. (2021) · Cancers · doi:10.3390/cancers13020261 · Cited by 43

The interaction of S100A16 and GRP78 actives endoplasmic reticulum stress-mediated through the IRE1α/XBP1 pathway in renal tubulointerstitial fibrosis

Jin, R., Zhao, A., Han, S., Zhang, D., Sun, H., Li, M., Su, D., & Liang, X. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-04249-8 · Cited by 42

GCAF(TMEM251) regulates lysosome biogenesis by activating the mannose-6-phosphate pathway

Zhang, W., Yang, X., Li, Y., Yu, L., Zhang, B., Zhang, J., Cho, W. J., Venkatarangan, V., Chen, L., Burugula, B. B., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-33025-1 · Cited by 41

Dual Functions of Yeast tRNA Ligase in the Unfolded Protein Response: Unconventional Cytoplasmic Splicing ofHAC1Pre-mRNA Is Not Sufficient to Release Translational Attenuation

Mori, T., Ogasawara, C., Inada, T., Englert, M., Beier, H., Takezawa, M., Endo, T., & Yoshihisa, T. (2010) · Molecular Biology of the Cell · doi:10.1091/mbc.e10-08-0693 · Cited by 42

KLF15 Is a Molecular Link between Endoplasmic Reticulum Stress and Insulin Resistance

Jung, D. Y., Chalasani, U., Pan, N., Friedline, R. H., Prosdocimo, D. A., Nam, M., Azuma, Y., Maganti, R. J., Yu, K. M., Velagapudi, A., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0077851 · Cited by 43

Lipid-induced ER stress in yeast and β cells: parallel trails to a common fate

Pineau, L., & Ferreira, T. (2010) · FEMS Yeast Research · doi:10.1111/j.1567-1364.2010.00674.x · Cited by 42

Dickkopf Homolog 3 Induces Stem Cell Differentiation into Smooth Muscle Lineage via ATF6 Signalling

Wang, X., Karamariti, E., Simpson, R., Wang, W., & Xu, Q. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.641415 · Cited by 41

Prolyl hydroxylase inhibition attenuates post-ischemic cardiac injury via induction of endoplasmic reticulum stress genes

Natarajan, R., Salloum, F. N., Fisher, B. J., Smithson, L. A., Almenara, J. A., & Fowler, A. A. (2009) · Vascular Pharmacology · doi:10.1016/j.vph.2009.05.007 · Cited by 41

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

A Functional Unfolded Protein Response Is Required for Normal Vegetative Development

Bao, Y., Bassham, D. C., & Howell, S. H. (2019) · PLANT PHYSIOLOGY · doi:10.1104/pp.18.01261 · Cited by 41

ORMDL3 and Asthma: Linking Sphingolipid Regulation to Altered T Cell Function

Luthers, C. R., Dunn, T. M., & Snow, A. L. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.597945 · Cited by 41

Site-1 Protease-Derived Soluble (Pro)Renin Receptor Contributes to Angiotensin II–Induced Hypertension in Mice

Ye, F., Peng, K., Luo, R., Wang, F., & Yang, T. (2020) · Hypertension · doi:10.1161/hypertensionaha.120.15100 · Cited by 41

How Do Enveloped Viruses Exploit the Secretory Proprotein Convertases to Regulate Infectivity and Spread?

Seidah, N. G., Pasquato, A., & Andréo, U. (2021) · Viruses · doi:10.3390/v13071229 · Cited by 41

Endoplasmic Reticulum Stress in Disease Pathogenesis

Lin, J. H., Walter, P., & Yen, T. S. B. (2007) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev.pathol.3.121806.151434 · Cited by 41

Activating transcription factor 6 protects against endothelial barrier dysfunction

Kubra, K., Akhter, M. S., Saini, Y., Kousoulas, K. G., & Barabutis, N. (2022) · Cellular Signalling · doi:10.1016/j.cellsig.2022.110432 · Cited by 41

Eukaryotic and prokaryotic stomatins: the proteolytic link

Green, J. B., Fricke, B., Chetty, M. C., von Düring, M., Preston, G. M., & Stewart, G. W. (2004) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2004.01.016 · Cited by 41

Exendin-4 inhibits glucolipotoxic ER stress in pancreatic β cells via regulation of SREBP1c and C/EBPβ transcription factors

Oh, Y. S., Lee, Y.-J., KANG, Y. Y., Han, J., Lim, O.-K., & Jun, H. (2012) · Journal of Endocrinology · doi:10.1530/joe-12-0311 · Cited by 41

The Membrane-Bound Transcriptional Regulator CadC Is Activated by Proteolytic Cleavage in Response to Acid Stress

Lee, Y. H., Kim, J. H., Bang, I. S., & Park, Y. (2008) · Journal of Bacteriology · doi:10.1128/jb.00012-08 · Cited by 41

St. John's wort and its constituent hyperforin concordantly regulate expression of genes encoding enzymes involved in basic cellular pathways

Krusekopf, S., & Roots, I. (2005) · Pharmacogenetics and Genomics · doi:10.1097/01.fpc.0000175597.60066.3d · Cited by 42

Targeting Phosphorylation of Eukaryotic Initiation Factor-2α to Treat Human Disease

Fullwood, M. J., Zhou, W., & Shenolikar, S. (2012) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-396456-4.00005-5 · Cited by 43

Involvement of androgen receptor and glucose-regulated protein 78 kDa in human hepatocarcinogenesis

Jiang, X., Kanda, T., Nakamoto, S., Miyamura, T., Wu, S., & Yokosuka, O. (2014) · Experimental Cell Research · doi:10.1016/j.yexcr.2014.02.017 · Cited by 40

Crosstalk between the Unfolded Protein Response and NF- κ B-Mediated Inflammation in the Progression of Chronic Kidney Disease

Mohammed‐Ali, Z., Cruz, G. L., & Dickhout, J. G. (2015) · Journal of Immunology Research · doi:10.1155/2015/428508 · Cited by 40

Three weeks voluntary running wheel exercise increases endoplasmic reticulum stress in the brain of mice

Kim, Y., Park, M., Boghossian, S., & York, D. A. (2010) · Brain Research · doi:10.1016/j.brainres.2009.12.062 · Cited by 41

Transcriptome Analysis of Newt Lens Regeneration Reveals Distinct Gradients in Gene Expression Patterns

Sousounis, K., Looso, M., Maki, N., Ivester, C. J., Braun, T. W., & Tsonis, P. A. (2013) · PLoS ONE · doi:10.1371/journal.pone.0061445 · Cited by 40

The role of CREB-H transcription factor in triglyceride metabolism

Lee, A. (2012) · Current Opinion in Lipidology · doi:10.1097/mol.0b013e3283508fed · Cited by 40

Acute infection of mice with C lostridium difficile leads to eIF2α phosphorylation and pro‐survival signalling as part of the mucosal inflammatory response

Akha, A. A. S., Theriot, C. M., Erb‐Downward, J. R., McDermott, A. J., Falkowski, N. R., Tyra, H. M., Rutkowski, D. T., Young, V. B., & Huffnagle, G. B. (2013) · Immunology · doi:10.1111/imm.12122 · Cited by 40

Why cells need intramembrane proteases – a mechanistic perspective

Střı́šovský, K. (2015) · FEBS Journal · doi:10.1111/febs.13638 · Cited by 40

Roles of Grp78 in Female Mammalian Reproduction

Zhang, C. (2017) · Advances in anatomy, embryology and cell biology · doi:10.1007/978-3-319-51409-3_7 · Cited by 40

Transcriptional regulation of the 26S proteasome by Nrf1

Koizumi, S., Hamazaki, J., & Murata, S. (2018) · Proceedings of the Japan Academy Series B · doi:10.2183/pjab.94.021 · Cited by 43

Transmissible Endoplasmic Reticulum Stress: A Novel Perspective on Tumor Immunity

Jiang, Z., Zhang, G., Huang, L., Yuan, Y., Wu, C., & Li, Y. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00846 · Cited by 39

Microplastics and di (2-ethylhexyl) phthalate synergistically induce apoptosis in mouse pancreas through the GRP78/CHOP/Bcl-2 pathway activated by oxidative stress

Wang, Y., Zhang, Y., Sun, X., Xu, S., & Xu, S. (2022) · Food and Chemical Toxicology · doi:10.1016/j.fct.2022.113315 · Cited by 40

Ricin and Ricin-Containing Immunotoxins: Insights into Intracellular Transport and Mechanism of action in Vitro

Słomińska-Wojewódzka, M., & Sandvig, K. (2013) · Antibodies · doi:10.3390/antib2020236 · Cited by 40

The effect of chronic ozone exposure on the activation of endoplasmic reticulum stress and apoptosis in rat hippocampus

Rodríguez-Martínez, E., Nava-Ruiz, C., Escamilla-Chimal, E., Borgonio-Perez, G., & Rivas-Arancibia, S. (2016) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2016.00245 · Cited by 39

Selenoproteins synergistically protect porcine skeletal muscle from oxidative damage via relieving mitochondrial dysfunction and endoplasmic reticulum stress

Jing, J., He, Y., Liu, Y., Tang, J., Wang, L., Jia, G., Liu, G., Chen, X., Tian, G., Cai, J., et al. (2023) · Journal of Animal Science and Biotechnology/Journal of animal science and biotechnology · doi:10.1186/s40104-023-00877-6 · Cited by 40

The role of endoplasmic reticulum stress, mitochondrial dysfunction and their crosstalk in intervertebral disc degeneration

Yao, D., Chen, E., Li, Y., Wang, K., Liao, Z., Li, M., & Huang, L. C. (2023) · Cellular Signalling · doi:10.1016/j.cellsig.2023.110986 · Cited by 39

Targeting proteostasis for cancer therapy: current advances, challenges, and future perspectives

Zhang, C., Li, J., Tang, Q., Li, L., & Cao, D. (2025) · Molecular Cancer · doi:10.1186/s12943-025-02472-x · Cited by 43

Site-1 protease cleavage site is important for the ER stress-induced activation of membrane-associated transcription factor bZIP28 in Arabidopsis

Sun, L., Zhang, S., Lu, S., & Liu, J. (2015) · Science China Life Sciences · doi:10.1007/s11427-015-4807-6 · Cited by 38

Conserved and plant-unique strategies for overcoming endoplasmic reticulum stress

Ruberti, C., & Brandizzí, F. (2014) · Frontiers in Plant Science · doi:10.3389/fpls.2014.00069 · Cited by 38

Structural and functional comparison of the non-structural protein 4B in flaviviridae

Welsch, C., Albrecht, M., Maydt, J., Herrmann, E. M., Welker, M. W., Sarrazin, C., Scheidig, A. J., Lengauer, T., & Zeuzem, S. (2007) · Journal of Molecular Graphics and Modelling · doi:10.1016/j.jmgm.2007.03.012 · Cited by 40

Secretory Defect and Cytotoxicity

Li, S., Yang, Z., Hu, J. G., Gordon, W. C., Bazan, N. G., Haas, A. L., Bok, D., & Jin, M. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.418251 · Cited by 39

ER Stress Activates the TOR Pathway through Atf6

Allen, D., & Seo, J. H. (2018) · Journal of Molecular Signaling · doi:10.5334/1750-2187-13-1 · Cited by 41

ER Protein Quality Control and the Unfolded Protein Response in the Heart

Arrieta, A., Blackwood, E. A., & Glembotski, C. C. (2017) · Current topics in microbiology and immunology · doi:10.1007/82_2017_54 · Cited by 39

Characterization of Proprotein Convertases and Their Involvement in Virus Propagation

Garten, W. (2018) · Springer eBooks · doi:10.1007/978-3-319-75474-1_9 · Cited by 39

Mechanisms controlling the multistage post-translational processing of endogenous Nrf1α/TCF11 proteins to yield distinct isoforms within the coupled positive and negative feedback circuits

Xiang, Y., Wang, M., Hu, S., Qiu, L., Yang, F., Zhang, Z., Yu, S., Pi, J., & Zhang, Y. (2018) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2018.09.036 · Cited by 39

The Pancreatic ß-cell Response to Secretory Demands and Adaption to Stress

Kalwat, M. A., Scheuner, D., Rodrigues-dos-Santos, K., Eizirik, D. L., & Cobb, M. H. (2021) · Endocrinology · doi:10.1210/endocr/bqab173 · Cited by 40

Apoptosis induced by t10,c12-conjugated linoleic acid is mediated by an atypical endoplasmic reticulum stress response

Ou, L., Wu, Y., Ip, C. C. Y., Meng, X., Hsu, Y.-C., & Ip, M. M. (2008) · Journal of Lipid Research · doi:10.1194/jlr.m700465-jlr200 · Cited by 39

Transcription Factor CREB3L1 Regulates Endoplasmic Reticulum Stress Response Genes in the Osmotically Challenged Rat Hypothalamus

Greenwood, M., Greenwood, M. P., Paton, J. F. R., & Murphy, D. (2015) · PLoS ONE · doi:10.1371/journal.pone.0124956 · Cited by 39

Environment of the Active Site Region of RseP, an Escherichia coli Regulated Intramembrane Proteolysis Protease, Assessed by Site-directed Cysteine Alkylation

Koide, K., Maegawa, S., Ito, K., & Akiyama, Y. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m607339200 · Cited by 39

The cargo receptor ERGIC-53 is a target of the unfolded protein response

Nyfeler, B., Nufer, O., Matsui, T., Mori, K., & Hauri, H. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(03)00634-x · Cited by 39

MASH as an emerging cause of hepatocellular carcinoma: current knowledge and future perspectives

Karin, M., & Kim, J. Y. (2024) · Molecular Oncology · doi:10.1002/1878-0261.13685 · Cited by 45

The Role of Endoplasmic Reticulum Stress in Autoimmune-Mediated Beta-Cell Destruction in Type 1 Diabetes

Zhong, J., Rao, X., Xu, J.-F., Yang, P. C., & Wang, C. (2012) · Experimental Diabetes Research · doi:10.1155/2012/238980 · Cited by 38

Identification of an old antibiotic clofoctol as a novel activator of unfolded protein response pathways and an inhibitor of prostate cancer

Wang, M., Shim, J. S., Li, R., Dang, Y., He, Q., Das, M., & Liu, J. O. (2014) · British Journal of Pharmacology · doi:10.1111/bph.12800 · Cited by 42

The Human Cytomegalovirus Endoplasmic Reticulum-Resident Glycoprotein UL148 Activates the Unfolded Protein Response

Siddiquey, M. N. A., Zhang, H., Nguyen, C. C., Domma, A. J., & Kamil, J. P. (2018) · Journal of Virology · doi:10.1128/jvi.00896-18 · Cited by 38

The roles of ER stress in epilepsy: Molecular mechanisms and therapeutic implications

Fu, J., Tao, T., Li, Z., Chen, Y., Li, J., & Peng, L. (2020) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2020.110658 · Cited by 38

Hijacking Cellular Stress Responses to Promote Lifespan

Dutta, N., Garcia, G., & Higuchi‐Sanabria, R. (2022) · Frontiers in Aging · doi:10.3389/fragi.2022.860404 · Cited by 35

Brain trauma induces X‐box protein 1 processing indicative of activation of the endoplasmic reticulum unfolded protein response

Paschen, W., Yatsiv, I., Shoham, S., & Shohami, E. (2004) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.02218.x · Cited by 39

Heightened Induction of Proapoptotic Signals in Response to Endoplasmic Reticulum Stress in Primary Fibroblasts from a Mouse Model of Longevity

Akha, A. A. S., Harper, J. M., Salmon, A. B., Schroeder, B. A., Tyra, H. M., Rutkowski, D. T., & Miller, R. A. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.220541 · Cited by 38

Physical interaction between hepatitis C virus NS4B protein and CREB-RP/ATF6β

Tong, W.-Y., Nagano‐Fujii, M., Hidajat, R., Deng, L., Takigawa, Y., & Hotta, H. (2002) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)02638-4 · Cited by 38

Transcriptional cross talk between orphan nuclear receptor ERR and transmembrane transcription factor ATF6 coordinates endoplasmic reticulum stress response

Misra, J., Kim, D.-K., Choi, W., Koo, S., Lee, C.-H., Back, S.-H., Kaufman, R. J., & Choi, H.-S. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt429 · Cited by 39

Shiga Toxins: Intracellular Trafficking to the ER Leading to Activation of Host Cell Stress Responses

Lee, M., Cherla, R. P., & Tesh, V. L. (2010) · Toxins · doi:10.3390/toxins2061515 · Cited by 38

Computational prediction of membrane-tethered transcription factors

Zupicich, J., Brenner, S. E., & Skarnes, W. C. (2001) · Genome biology · doi:10.1186/gb-2001-2-12-research0050 · Cited by 38

Enhanced GRP78 protein expression via the IRE1α/ASK1/p38 MAPK pathway during As2O3-induced endoplasmic reticulum stress in BEAS-2B cells

Yuan, J., Yao, C., Tang, J., Liu, Y., Huang, C., Yu, S., Wei, H., Han, Y. K., & Chen, G. (2021) · Toxicology · doi:10.1016/j.tox.2021.152962 · Cited by 37

Mechanism of cell death pathways in status epilepticus and related therapeutic agents

Du, K., He, M., Zhao, D., Wang, Y., Ma, C., Liang, H., Wang, W., Min, D., Xue, L., & Guo, F. (2022) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.112875 · Cited by 37

Antioxidant System and Endoplasmic Reticulum Stress in Cataracts

Zhang, X., Liu, B., Lal, K., Liu, H., Tran, M., Zhou, M.-Y., Ezugwu, C., Gao, X., Dang, T., Au, M.-L., et al. (2023) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-023-01427-4 · Cited by 37

A switch from life to death in endoplasmic reticulum stressed β ‐cells

Oslowski, C. M., & Urano, F. (2010) · Diabetes Obesity and Metabolism · doi:10.1111/j.1463-1326.2010.01277.x · Cited by 38

Structural and mechanistic principles of intramembrane proteolysis – lessons from rhomboids

Střı́šovský, K. (2013) · FEBS Journal · doi:10.1111/febs.12199 · Cited by 39

IGL-1 solution reduces endoplasmic reticulum stress and apoptosis in rat liver transplantation

Mosbah, I. B., Zaoualí, M. A., Martel, C., Bjaoui, M., Abdennebi, H. B., Hotter, G., Brenner, C., & Roselló‐Catafau, J. (2012) · Cell Death and Disease · doi:10.1038/cddis.2012.12 · Cited by 37

Paradoxical roles of ATF6α and ATF6β in modulating disease severity caused by mutations in collagen X

Forouhan, M., Mori, K., & Boot-Handford, R. (2018) · Matrix Biology · doi:10.1016/j.matbio.2018.03.004 · Cited by 37

Systemic signaling contributes to the unfolded protein response of the plant endoplasmic reticulum

Lai, Y.-S., Stefano, G., Zemelis‐Durfee, S., Ruberti, C., Gibbons, L., & Brandizzí, F. (2018) · Nature Communications · doi:10.1038/s41467-018-06289-9 · Cited by 37

Interactions Between Autophagy and the Unfolded Protein Response: Implications for Inflammatory Bowel Disease

Hooper, K. M., Barlow, P. G., Henderson, P., & Stevens, C. (2018) · Inflammatory Bowel Diseases · doi:10.1093/ibd/izy380 · Cited by 39

Site-1 protease–derived soluble (pro)renin receptor targets vasopressin receptor 2 to enhance urine concentrating capability

Wang, F., Xu, C., Luo, R., Peng, K., Ramkumar, N., Xie, S., Lu, X., Zhao, L., Zuo, C.-J., Kohan, D. E., et al. (2019) · JCI Insight · doi:10.1172/jci.insight.124174 · Cited by 37

The PERK Inhibitor GSK2606414 Enhances Reovirus Infection in Head and Neck Squamous Cell Carcinoma via an ATF4-Dependent Mechanism

McLaughlin, M., Pedersen, M., Roulstone, V., Bergerhoff, K. F., Smith, H. G., Whittock, H., Kyula, J., Dillon, M. T., Pandha, H., Vile, R. G., et al. (2020) · Molecular Therapy — Oncolytics · doi:10.1016/j.omto.2020.01.001 · Cited by 37

The role of ATF6 in Cr(VI)-induced apoptosis in DF-1 cells

Zhang, S., Zhao, X., Hao, J., Zhu, Y., Wang, Y., Wang, L., Guo, S., Yi, H., Liu, Y., & Liu, J. (2020) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2020.124607 · Cited by 37

Golgi stress response: A regulatory mechanism of Golgi function

Gao, J., Gao, A., Liu, W., & Chen, L. (2021) · BioFactors · doi:10.1002/biof.1780 · Cited by 37

Protein Aggregation in the ER: Calm behind the Storm

Li, H., & Sun, S. (2021) · Cells · doi:10.3390/cells10123337 · Cited by 36

The Role of Endoplasmic Reticulum Stress in Differentiation of Cells of Mesenchymal Origin

Турищева, Е. П., Vildanova, M. S., Онищенко, Г. Е., & Смирнова, Е. А. (2022) · Biochemistry (Moscow) · doi:10.1134/s000629792209005x · Cited by 37

Trafficking of the bZIP Transmembrane Transcription Factor CREB‐H into Alternate Pathways of ERAD and Stress‐Regulated Intramembrane Proteolysis

Bailey, D., Barreca, C., & O’Hare, P. (2007) · Traffic · doi:10.1111/j.1600-0854.2007.00654.x · Cited by 37

Intramembrane Proteolysis of Mgm1 by the Mitochondrial Rhomboid Protease Is Highly Promiscuous Regarding the Sequence of the Cleaved Hydrophobic Segment

Schäfer, A., Zick, M., Kief, J. H., Steger, M., Heide, H., Duvezin‐Caubet, S., Neupert, W., & Reichert, A. S. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.06.014 · Cited by 37

Core principles of intramembrane proteolysis: comparison of rhomboid and site-2 family proteases

Urban, S., & Shi, Y. (2008) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2008.03.005 · Cited by 37

Effect of modulation of unfolded protein response pathway on dengue virus infection

Diwaker, D., Mishra, K. P., & Ganju, L. (2015) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmv108 · Cited by 37

Induction of miR-3648 Upon ER Stress and Its Regulatory Role in Cell Proliferation

Rashid, F., Awan, H. M., Shah, A., Chen, L., & Shan, G. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18071375 · Cited by 36

Proteolytic processing of secretory pathway kinase Fam20C by site-1 protease promotes biomineralization

Chen, X., Zhang, J., Liu, P., Wei, Y., Wang, X., Xiao, J., Wang, C., & Wang, L. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2100133118 · Cited by 36

Endoplasmic Reticulum Stress and Pathogenesis of Vascular Calcification

Rao, Z., Zheng, Y., Xu, L., Wang, Z., Zhou, Y., Chen, M., Dong, N., Cai, Z., & Li, F. (2022) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2022.918056 · Cited by 36

Regulation of protein homeostasis in neurodegenerative diseases: the role of coding and non-coding genes

Sin, O., & Nollen, E. A. A. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-1985-0 · Cited by 43

The Unfolded Protein Response in Lung Disease

Marciniak, S. J., & Ron, D. (2010) · Proceedings of the American Thoracic Society · doi:10.1513/pats.201001-015aw · Cited by 36

Intramembrane proteolytic cleavage of a membrane-tethered transcription factor by a metalloprotease depends on ATP

Zhou, R., Cusumano, C., Sui, D., Garavito, R. M., & Kroos, L. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0901455106 · Cited by 36

Curcumin downregulates H19 gene transcription in tumor cells

Kujundžić, R. N., Grbeša, I., Ivkić, M., Katdare, M., & Gall‐Tros̆elj, K. (2008) · Journal of Cellular Biochemistry · doi:10.1002/jcb.21742 · Cited by 36

Three branches to rule them all? UPR signalling in response to chemically versus misfolded proteins‐induced ER stress

Bergmann, T. J., & Molinari, M. (2018) · Biology of the Cell · doi:10.1111/boc.201800029 · Cited by 36

Increased expression of endoplasmic reticulum stress-related caspase-12 and CHOP in the hippocampus of EAE mice

Kamarehei, M., Ardestani, S. K., Firouzi, M., Zahednasab, H., Keyvani, H., & Harirchian, M. H. (2019) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2019.01.020 · Cited by 36

KSHV activates unfolded protein response sensors but suppresses downstream transcriptional responses to support lytic replication

Johnston, B. P., Pringle, E. S., & McCormick, C. (2019) · PLoS Pathogens · doi:10.1371/journal.ppat.1008185 · Cited by 36

Functional Peroxisomes Are Essential for Efficient Cholesterol Sensing and Synthesis

Charles, K. N., Shackelford, J. E., Faust, P. L., Fliesler, S. J., Stangl, H., & Kovacs, W. J. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.560266 · Cited by 36

PIDDosome-SCAP crosstalk controls high-fructose-diet-dependent transition from simple steatosis to steatohepatitis

Kim, J. Y., Wang, L. Q., Sladky, V. C., Oh, T. G., Liu, J., Trinh, K., Eichin, F., Downes, M., Hosseini, M., Jacotot, E. D., et al. (2022) · Cell Metabolism · doi:10.1016/j.cmet.2022.08.005 · Cited by 37

Nutritional related liver disease: targeting the endoplasmic reticulum stress

Kammoun, H. L., Hainault, I., Ferré, P., & Foufelle, F. (2009) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/mco.0b013e32833189db · Cited by 40

Non‐invasive UPR monitoring system and its applications in CHO production cultures

Du, Z., Treiber, D., McCoy, R. E., Miller, A. K., Han, M., He, F., Domnitz, S. B., Heath, C. A., & Reddy, P. (2013) · Biotechnology and Bioengineering · doi:10.1002/bit.24877 · Cited by 36

Activation of the Unfolded Protein Response Is Necessary and Sufficient for Reducing Topoisomerase IIα Protein Levels and Decreasing Sensitivity to Topoisomerase-Targeted Drugs

Gray, M. D., Mann, M. J., Nitiss, J. L., & Hendershot, L. M. (2005) · Molecular Pharmacology · doi:10.1124/mol.105.014753 · Cited by 36

A Serine Protease Inhibitor Prevents Endoplasmic Reticulum Stress-induced Cleavage but Not Transport of the Membrane-bound Transcription Factor ATF6

Okada, T., Haze, K., Nadanaka, S., Yoshida, H., Seidah, N. G., Hirano, Y., Sato, R., Negishi, M., & Mori, K. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300923200 · Cited by 213

Dependence of Site-2 Protease Cleavage of ATF6 on Prior Site-1 Protease Digestion Is Determined by the Size of the Luminal Domain of ATF6

Shen, J., & Prywes, R. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408466200 · Cited by 149

ER stress signaling by regulated proteolysis of ATF6

Shen, J., & Prywes, R. (2005) · Methods · doi:10.1016/j.ymeth.2004.10.011 · Cited by 120

Role of Disulfide Bridges Formed in the Luminal Domain of ATF6 in Sensing Endoplasmic Reticulum Stress

Nadanaka, S., Okada, T., Yoshida, H., & Mori, K. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00408-06 · Cited by 268

Analysis of ATF6 Activation in Site-2 Protease-deficient Chinese Hamster Ovary Cells

Nadanaka, S., Yoshida, H., Sato, R., & Mori, K. (2006) · Cell Structure and Function · doi:10.1247/csf.06015 · Cited by 30