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

ER homeostasis and autophagy

Smith, M., & Wilkinson, S. (2017) · Essays in Biochemistry · doi:10.1042/ebc20170092 · Cited by 214

Exposure to copper oxide nanoparticles triggers oxidative stress and endoplasmic reticulum (ER)-stress induced toxicology and apoptosis in male rat liver and BRL-3A cell

Liu, H., Lai, W., Liu, X., Yang, H., Fang, Y., Tian, L., Li, K., Nie, H., Zhang, W., Shi, Y., et al. (2020) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2020.123349 · Cited by 212

The Ubiquitin–Proteasome System in Immune Cells

Çetin, G., Klafack, S., Studencka‐Turski, M., Krüger, E., & Ebstein, F. (2021) · Biomolecules · doi:10.3390/biom11010060 · Cited by 218

ER stress, autophagy, and RNA viruses

Jheng, J.-R., Ho, J., & Horng, J. (2014) · Frontiers in Microbiology · doi:10.3389/fmicb.2014.00388 · Cited by 215

Effect on Tumor Cells of Blocking Survival Response to Glucose Deprivation

Park, H., Tomida, A., Sato, S., Tsukumo, Y., Yun, J., Yamori, T., Hayakawa, Y., TSURUO, T., & Shin‐ya, K. (2004) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/djh243 · Cited by 210

West Nile Virus Differentially Modulates the Unfolded Protein Response To Facilitate Replication and Immune Evasion

Ambrose, R. L., & Mackenzie, J. M. (2010) · Journal of Virology · doi:10.1128/jvi.02050-10 · Cited by 209

Protein kinase RNA- like endoplasmic reticulum kinase (PERK) signaling pathway plays a major role in reactive oxygen species (ROS)- mediated endoplasmic reticulum stress- induced apoptosis in diabetic cardiomyopathy

Liu, Z., Zhu, H., Chen, K., Dong, X., Wei, J., Qiu, C., & Xue, J. (2013) · Cardiovascular Diabetology · doi:10.1186/1475-2840-12-158 · Cited by 209

Endoplasmic reticulum stress in the pathogenesis of fibrotic disease

Kropski, J. A., & Blackwell, T. S. (2018) · Journal of Clinical Investigation · doi:10.1172/jci93560 · Cited by 218

A survival pathway forCaenorhabditis eleganswith a blocked unfolded protein response

Urano, F., Calfon, M. A., Yoneda, T., Yun, C., Kiraly, M., Clark, S. G., & Ron, D. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200203086 · Cited by 207

Intramembrane-cleaving proteases: controlled liberation of proteins and bioactive peptides

Weihofen, A., & Martoglio, B. (2003) · Trends in Cell Biology · doi:10.1016/s0962-8924(02)00041-7 · Cited by 208

Protein-tyrosine Phosphatase 1B Potentiates IRE1 Signaling during Endoplasmic Reticulum Stress

Gu, F., Nguyên, D. T., Stuible, M., Dubé, N., Tremblay, M. L., & Chevet, É. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.c400261200 · Cited by 204

Druggable sensors of the unfolded protein response

Maly, D. J., & Papa, F. R. (2014) · Nature Chemical Biology · doi:10.1038/nchembio.1664 · Cited by 206

BMP2 Protein Regulates Osteocalcin Expression via Runx2-mediated Atf6 Gene Transcription

Jang, W.-G., Kim, E., Kim, D., Ryoo, H., Lee, K., Kim, S.-H., Choi, H., & Koh, J. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.253187 · Cited by 202

Proprotein Convertases in Tumor Progression and Malignancy

Khatib, A., Siegfried, G., Chrétien, M., Metrakos, P. P., & Seidah, N. G. (2002) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)61140-6 · Cited by 201

SPPL2a and SPPL2b promote intramembrane proteolysis of TNFα in activated dendritic cells to trigger IL-12 production

Friedmann, E., Hauben, E., Maylandt, K., Schleeger, S., Vreugde, S., Lichtenthaler, S. F., Kuhn, P., Stauffer, D., Rovelli, G., & Martoglio, B. (2006) · Nature Cell Biology · doi:10.1038/ncb1440 · Cited by 201

Mesencephalic Astrocyte-derived Neurotrophic Factor Protects the Heart from Ischemic Damage and Is Selectively Secreted upon Sarco/endoplasmic Reticulum Calcium Depletion

Glembotski, C. C., Thuerauf, D. J., Huang, C., Vekich, J. A., Gottlieb, R. A., & Doroudgar, S. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.356345 · Cited by 199

Gene expression in response to endoplasmic reticulum stress in Arabidopsis thaliana

Kamauchi, S., Nakatani, H., Nakano, C., & Urade, R. (2005) · FEBS Journal · doi:10.1111/j.1742-4658.2005.04770.x · Cited by 197

Structures of membrane proteins

Vinothkumar, K. R., & Henderson, R. A. (2010) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583510000041 · Cited by 205

Nitric Oxide and Endoplasmic Reticulum Stress

Gotoh, T., & Mori, M. (2006) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000223900.67024.15 · Cited by 200

Regulation of Hepatic Gluconeogenesis by an ER-Bound Transcription Factor, CREBH

Lee, M., Chanda, D., Yang, J., Oh, H., Kim, S. S., Yoon, Y.-S., Hong, S., Park, K., Lee, I., Choi, C. S., et al. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.02.016 · Cited by 198

Kaposi's sarcoma-associated herpesvirus-infected primary effusion lymphoma has a plasma cell gene expression profile

Jenner, R. G., Maillard, K. I., Cattini, N., Weiss, R. A., Boshoff, C., Wooster, R., & Kellam, P. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1630810100 · Cited by 193

Cancer Drug Discovery and Development

Humphrey, J. S., Price, K., Gupta, E., Baxter, A. R. W., Bird, J., Sonnichsen, D. S., & Naglich, J. G. (2003) · Humana Press eBooks · doi:10.1007/978-1-59259-325-5_21 · Cited by 195

Secretory Pathway Quality Control Operating in Golgi, Plasmalemmal, and Endosomal Systems

Arvan, P. R., Zhao, X., Ramos‐Castañeda, J., & Chang, A. (2002) · Traffic · doi:10.1034/j.1600-0854.2002.31102.x · Cited by 192

Underglycosylation of ATF6 as a Novel Sensing Mechanism for Activation of the Unfolded Protein Response

Hong, M. Y., Luo, S. D., Baumeister, P., Huang, J.-M., Gogia, R. K., Li, M., & Lee, A. S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m309804200 · Cited by 195

Hepatic steatosis in response to acute alcohol exposure in zebrafish requires sterol regulatory element binding protein activation #

Passeri, M. J., Cinaroglu, A., Gao, C., & Sadler, K. C. (2008) · Hepatology · doi:10.1002/hep.22667 · Cited by 190

Endoplasmic Reticulum Stress Activates Unfolded Protein Response Signaling and Mediates Inflammation, Obesity, and Cardiac Dysfunction: Therapeutic and Molecular Approach

Amen, O. M., Sarker, S. D., Ghildyal, R., & Arya, A. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.00977 · Cited by 190

Regulation of lipid metabolism by the unfolded protein response

Moncan, M., Mnich, K., Blomme, A., Almanza, A., Samali, A., & Gorman, A. M. (2021) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.16255 · Cited by 191

Identification of Toyocamycin, an agent cytotoxic for multiple myeloma cells, as a potent inhibitor of ER stress-induced XBP1 mRNA splicing

Ri, M., Tashiro, E., Oikawa, D., Shinjo, S., Tokuda, M., Yokouchi, Y., Narita, T., Masaki, A., Ito, A., Ding, J., et al. (2012) · Blood Cancer Journal · doi:10.1038/bcj.2012.26 · Cited by 187

Unfolded protein response in cancer: the Physician's perspective

Li, X., Zhang, K., & Li, Z. (2011) · Journal of Hematology & Oncology · doi:10.1186/1756-8722-4-8 · Cited by 193

Proteolytic Activation of Sterol Regulatory Element-binding Protein Induced by Cellular Stress through Depletion of Insig-1

Lee, J. N., & Ye, J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408235200 · Cited by 195

Reconstitution of intramembrane proteolysis in vitro reveals that pure rhomboid is sufficient for catalysis and specificity

Urban, S., & Wolfe, M. S. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0408306102 · Cited by 185

Nitric oxide induces coupling of mitochondrial signalling with the endoplasmic reticulum stress response

Xu, W., Liu, L., Charles, I. G., & Moncada, S. (2004) · Nature Cell Biology · doi:10.1038/ncb1188 · Cited by 182

Disturbed Activation of Endoplasmic Reticulum Stress Transducers by Familial Alzheimer's Disease-linked Presenilin-1 Mutations

Katayama, T., Imaizumi, K., Honda, A., Yoneda, T., Kudo, T., Takeda, M., Mori, K., Rozmahel, R. F., Fraser, P., George‐Hyslop, P. S., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104096200 · Cited by 184

Characterization of Stanniocalcin 2, a Novel Target of the Mammalian Unfolded Protein Response with Cytoprotective Properties

Ito, D., Walker, J. R., Thompson, C. S., Moroz, I., Lin, W., Veselits, M., Hakim, A. M., Fienberg, A. A., & Thinakaran, G. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.21.9456-9469.2004 · Cited by 179

Multiple Mechanisms of Unfolded Protein Response–Induced Cell Death

Hiramatsu, N., Chiang, W.-C. J., Kurt, T. D., Sigurdson, C. J., & Lin, J. H. (2015) · American Journal Of Pathology · doi:10.1016/j.ajpath.2015.03.009 · Cited by 181

The UPR Activator ATF6 Responds to Proteotoxic and Lipotoxic Stress by Distinct Mechanisms

Tam, A. B., Roberts, L. S., Chandra, V. K., Rivera, I. G., Nomura, D. K., Forbes, D. J., & Niwa, M. (2018) · Developmental Cell · doi:10.1016/j.devcel.2018.04.023 · Cited by 180

Gcn4p and Novel Upstream Activating Sequences Regulate Targets of the Unfolded Protein Response

Patil, C. K., Li, H., & Walter, P. (2004) · PLoS Biology · doi:10.1371/journal.pbio.0020246 · Cited by 179

The Unfolded Protein Response in Secretory Cell Function

Moore, K. A., & Hollien, J. (2012) · Annual Review of Genetics · doi:10.1146/annurev-genet-110711-155644 · Cited by 178

ER Stress and Angiogenesis

Binet, F., & Sapieha, P. S. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.07.010 · Cited by 178

The Multifaceted Proprotein Convertases: Their Unique, Redundant, Complementary, and Opposite Functions

Seidah, N. G., Sadr, M. S., Chrétien, M., & Mbikay, M. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.r113.481549 · Cited by 182

Structural basis for intramembrane proteolysis by rhomboid serine proteases

Shem, A. B., Fass, D., & Bibi, E. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0609773104 · Cited by 176

The Structure, Activation and Signaling of IRE1 and Its Role in Determining Cell Fate

Siwecka, N., Rozpędek‐Kamińska, W., Wawrzynkiewicz, A., Pytel, D., Diehl, J. A., & Majsterek, I. (2021) · Biomedicines · doi:10.3390/biomedicines9020156 · Cited by 181

Endoplasmic reticulum stress and apoptosis

Faitová, J., Krekac, D., Hrstka, R., & Vojtěšek, B. (2006) · Cellular & Molecular Biology Letters · doi:10.2478/s11658-006-0040-4 · Cited by 175

SREBPs: sterol-regulated transcription factors

Espenshade, P. J. (2006) · Journal of Cell Science · doi:10.1242/jcs.02866 · Cited by 174

Endoplasmic reticulum stress inhibition protects steatotic and non-steatotic livers in partial hepatectomy under ischemia–reperfusion

Mosbah, I. B., Alfany-Fernández, I., Martel, C., Zaoualí, M. A., Bintanel-Morcillo, M., Rimola, A., Rodés, J., Brenner, C., Roselló‐Catafau, J., & Peralta, C. (2010) · Cell Death and Disease · doi:10.1038/cddis.2010.29 · Cited by 175

Redox signaling loops in the unfolded protein response

Higa, A., & Chevet, É. (2012) · Cellular Signalling · doi:10.1016/j.cellsig.2012.03.011 · Cited by 174

Regulation by destruction: design of the σE envelope stress response

Ades, S. E. (2008) · Current Opinion in Microbiology · doi:10.1016/j.mib.2008.10.004 · Cited by 173

BBF2H7, a Novel Transmembrane bZIP Transcription Factor, Is a New Type of Endoplasmic Reticulum Stress Transducer

Kondo, S., Saito, A., Hino, S., Murakami, T., Ogata, M., Kanemoto, S., Nara, S., Yamashita, A., Yoshinaga, K., Hara, H., et al. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.01552-06 · Cited by 177

Osteogenesis Imperfecta: Mechanisms and Signaling Pathways Connecting Classical and Rare OI Types

Jovanovic, M., Ram, G. G., & Marini, J. C. (2021) · Endocrine Reviews · doi:10.1210/endrev/bnab017 · Cited by 182

ER stress: Can the liver cope?

Ji, C., & Kaplowitz, N. (2006) · Journal of Hepatology · doi:10.1016/j.jhep.2006.06.004 · Cited by 171

Endoplasmic reticulum stress: a novel mechanism and therapeutic target for cardiovascular diseases

Liu, M., Chen, Z., & Chen, L. (2016) · Acta Pharmacologica Sinica · doi:10.1038/aps.2015.145 · Cited by 176

Biogenesis and metabolism of Alzheimer’s disease Aβ amyloid peptides

Evin, G. M., & Weidemann, A. (2002) · Peptides · doi:10.1016/s0196-9781(02)00063-3 · Cited by 179

The Proprotein Convertases, 20 Years Later

Seidah, N. G. (2011) · Methods in molecular biology · doi:10.1007/978-1-61779-204-5_3 · Cited by 168

Molecular Mechanisms of ER Stress and UPR in the Pathogenesis of Alzheimer’s Disease

Uddin, M. S., Tewari, D., Sharma, G., Kabir, M. T., Barreto, G. E., Bin-Jumah, M. N., Perveen, A., Abdel‐Daim, M. M., & Ashraf, G. M. (2020) · Molecular Neurobiology · doi:10.1007/s12035-020-01929-y · Cited by 166

SREBP-1c and lipogenesis in the liver: an update

Ferré, P., Phan, F., & Foufelle, F. (2021) · Biochemical Journal · doi:10.1042/bcj20210071 · Cited by 183

Endoplasmic reticulum stress in disease: mechanisms and therapeutic opportunities

Hosoi, T., & Ozawa, K. (2009) · Clinical Science · doi:10.1042/cs20080680 · Cited by 169

Dengue virus serotype infection specifies the activation of the unfolded protein response

Umareddy, I., Pluquet, O., Wang, Q. Y., Vasudevan, S. G., Chevet, É., & Gu, F. (2007) · Virology Journal · doi:10.1186/1743-422x-4-91 · Cited by 166

VAPB interacts with and modulates the activity of ATF6

Gkogkas, C. G., Middleton, S., Kremer, A., Wardrope, C., Hannah, M. J., Gillingwater, T. H., & Skehel, P. (2008) · Human Molecular Genetics · doi:10.1093/hmg/ddn040 · Cited by 161

ER Stress and Unfolded Protein Response in Amyotrophic Lateral Sclerosis

Kanekura, K., Suzuki, H., Aiso, S., & Matsuoka, M. (2009) · Molecular Neurobiology · doi:10.1007/s12035-009-8054-3 · Cited by 162

Plant transducers of the endoplasmic reticulum unfolded protein response

Iwata, Y., & Koizumi, N. (2012) · Trends in Plant Science · doi:10.1016/j.tplants.2012.06.014 · Cited by 161

RseP (YaeL), an Escherichia coli RIP protease, cleaves transmembrane sequences

Akiyama, Y., Kanehara, K., & Ito, K. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600449 · Cited by 159

Endoplasmic reticulum stress in β-cells and development of diabetes

Fonseca, S. G., Burcin, M. M., Gromada, J., & Urano, F. (2009) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2009.07.003 · Cited by 162

Unconventional splicing ofXBP1mRNA occurs in the cytoplasm during the mammalian unfolded protein response

Uemura, A., Oku, M., Mori, K., & Yoshida, H. (2009) · Journal of Cell Science · doi:10.1242/jcs.040584 · Cited by 158

Effects of the Isoform-specific Characteristics of ATF6α and ATF6β on Endoplasmic Reticulum Stress Response Gene Expression and Cell Viability

Thuerauf, D. J., Marcinko, M. C., Belmont, P. J., & Glembotski, C. C. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m701213200 · Cited by 167

The proprotein convertases are potential targets in the treatment of dyslipidemia

Seidah, N. G., & Prat, A. (2007) · Journal of Molecular Medicine · doi:10.1007/s00109-007-0172-7 · Cited by 155

Functional and morphological impact of ER stress on mitochondria

Vannuvel, K., Renard, P., Raes, M. J., & Arnould, T. (2013) · Journal of Cellular Physiology · doi:10.1002/jcp.24360 · Cited by 161

Transcriptional and Post-Transcriptional Regulation of Proangiogenic Factors by the Unfolded Protein Response

Pereira, E. R., Liao, N., Neale, G. A. M., & Hendershot, L. M. (2010) · PLoS ONE · doi:10.1371/journal.pone.0012521 · Cited by 167

Regulated Intramembrane Proteolysis of Bri2 (Itm2b) by ADAM10 and SPPL2a/SPPL2b

Martin, L., Fluhrer, R., Reiß, K., Kremmer, E., Säftig, P., & Haass, C. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m706661200 · Cited by 155

IFAP Syndrome Is Caused by Deficiency in MBTPS2, an Intramembrane Zinc Metalloprotease Essential for Cholesterol Homeostasis and ER Stress Response

Oeffner, F., Fischer, G. O., Happle, R., König, A., Betz, R. C., Bornholdt, D., Neidel, U., Boente, M. D. C., Redler, S., Romero-Gomez, J., et al. (2009) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2009.03.014 · Cited by 154

A Futile Battle? Protein Quality Control and the Stress of Aging

Higuchi‐Sanabria, R., Frankino, P. A., Paul, J. W., Tronnes, S. U., & Dillin, A. G. (2018) · Developmental Cell · doi:10.1016/j.devcel.2017.12.020 · Cited by 153

Protein Quality Control in Plant Organelles: Current Progress and Future Perspectives

Sun, J., Li, J., Wang, M.-J., Song, Z., & Liu, J. (2020) · Molecular Plant · doi:10.1016/j.molp.2020.10.011 · Cited by 157

Herp Is Dually Regulated by Both the Endoplasmic Reticulum Stress-specific Branch of the Unfolded Protein Response and a Branch That Is Shared with Other Cellular Stress Pathways

Ma, Y., & Hendershot, L. M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313724200 · Cited by 154

Identification of Lassa virus glycoprotein signal peptide as a trans-acting maturation factor

Eichler, R., Lenz, O., Strecker, T., Eickmann, M., Klenk, H., & Garten, W. (2003) · EMBO Reports · doi:10.1038/sj.embor.7400002 · Cited by 154

Protective effect against Parkinson's disease-related insults through the activation of XBP1

Sado, M., Yamasaki, Y., Iwanaga, T., Onaka, Y., Ibuki, T., Nishihara, S., Mizuguchi, H., Momota, H., Kishibuchi, R., Hashimoto, T., et al. (2008) · Brain Research · doi:10.1016/j.brainres.2008.11.104 · Cited by 153

Protein Folding in the Endoplasmic Reticulum and the Unfolded Protein Response

Zhang, K., & Kaufman, R. J. (2005) · Handbook of Experimental Pharmacology · doi:10.1007/3-540-29717-0_3 · Cited by 152

Oxidative Folding: Cellular Strategies for Dealing with the Resultant Equimolar Production of Reactive Oxygen Species

Shimizu, Y., & Hendershot, L. M. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2501 · Cited by 150

Cleavage of the membrane‐bound transcription factor OASIS in response to endoplasmic reticulum stress

Murakami, T., Kondo, S., Ogata, M., Kanemoto, S., Saito, A., Wanaka, A., & Imaizumi, K. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03596.x · Cited by 149

Unfolded protein response (UPR) integrated signaling networks determine cell fate during hypoxia

Bartoszewska, S., & Collawn, J. F. (2020) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-020-00212-1 · Cited by 155

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

ATF6α downregulation of PPARα promotes lipotoxicity-induced tubulointerstitial fibrosis

Jao, T., Nangaku, M., Wu, C.-H., Sugahara, M., Saito, H., Maekawa, H., Ishimoto, Y., Aoe, M., Inoue, T., Tanaka, T., et al. (2019) · Kidney International · doi:10.1016/j.kint.2018.09.023 · Cited by 148

Membrane-bound transcription factors: regulated release by RIP or RUP

Hoppe, T., Rapé, M., & Jentsch, S. (2001) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(00)00218-0 · Cited by 148

Redox Balance in the Pathogenesis of Nonalcoholic Fatty Liver Disease: Mechanisms and Therapeutic Opportunities

Gambino, R., Musso, G., & Cassader, M. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.3058 · Cited by 147

Plasma cell differentiation initiates a limited ER stress response by specifically suppressing the PERK-dependent branch of the unfolded protein response

Ma, Y., Shimizu, Y., Mann, M. J., Jin, Y., & Hendershot, L. M. (2009) · Cell Stress and Chaperones · doi:10.1007/s12192-009-0142-9 · Cited by 147

Glycosylation Is Important for Cell Surface Expression of the Water Channel Aquaporin-2 but Is Not Essential for Tetramerization in the Endoplasmic Reticulum

Hendriks, G., Koudijs, M. J., van Balkom, B. W. M., Oorschot, V. M. J., Klumperman, J., Deen, P. M. T., & van der Sluijs, P. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m310767200 · Cited by 147

MBTPS2 mutations cause defective regulated intramembrane proteolysis in X-linked osteogenesis imperfecta

Lindert, U., Cabral, W. A., Ausavarat, S., Tongkobpetch, S., Ludin, K., Barnes, A. M., Yeetong, P., Weis, M., Krabichler, B., Srichomthong, C., et al. (2016) · Nature Communications · doi:10.1038/ncomms11920 · Cited by 146

The expanding roles of endoplasmic reticulum stress in virus replication and pathogenesis

Li, S., Kong, L., & Yu, X. (2013) · Critical Reviews in Microbiology · doi:10.3109/1040841x.2013.813899 · Cited by 145

The unfolded protein response and Alzheimer’s disease

Imaizumi, K., Miyoshi, K., Katayama, T., Yoneda, T., Taniguchi, M., Kudo, T., & Tohyama, M. (2001) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/s0925-4439(01)00049-7 · Cited by 147

The unfolded protein response and its relevance to connective tissue diseases

Boot-Handford, R. P., & Briggs, M. D. (2010) · Cell and Tissue Research · doi:10.1007/s00441-009-0877-8 · Cited by 143

Endoplasmic reticulum stress and protein quality control in diabetic cardiomyopathy

Yang, L., Zhao, D., Ren, J. T., & Yang, J. Z. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2014.05.006 · Cited by 146

Endoplasmic reticulum stress as a pro-fibrotic stimulus

Tanjore, H., Lawson, W. E., & Blackwell, T. S. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2012.11.011 · Cited by 151

Intramembrane proteolysis controls diverse signalling pathways throughout evolution

Urban, S. (2002) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(02)00334-9 · Cited by 147

Activation mechanisms of the HACI‐mediated unfolded protein response in filamentous fungi

Saloheimo, M., Valkonen, M. J., & Penttilä, M. E. (2003) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03363.x · Cited by 144

The role of the unfolded protein response in the heart

Glembotski, C. C. (2007) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2007.10.017 · Cited by 143

The unfolded protein response is shaped by the NMD pathway

Karam, R., Lou, C., Kroeger, H., Huang, L., Lin, J. H., & Wilkinson, M. (2015) · EMBO Reports · doi:10.15252/embr.201439696 · Cited by 143

ER Stress and the UPR in Shaping Intestinal Tissue Homeostasis and Immunity

Coleman, O. I., & Haller, D. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.02825 · Cited by 147

An overview of transcriptional regulation in response to toxicological insult

Jennings, P., Limonciel, A., Felice, L., & Leonard, M. O. (2012) · Archives of Toxicology · doi:10.1007/s00204-012-0919-y · Cited by 147

ENDOPLASMIC RETICULUM STRESS IN SEPSIS

Khan, M. M., Yang, W.-L., & Wang, P. (2015) · Shock · doi:10.1097/shk.0000000000000425 · Cited by 147

eIF2α-CHOP-BCl-2/JNK and IRE1α-XBP1/JNK signaling promote apoptosis and inflammation and support the proliferation of Newcastle disease virus

Li, Y., Jiang, W., Niu, Q., Sun, Y., Meng, C., Tan, L., Song, C., Qiu, X., Liao, Y., & Ding, C. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-2128-6 · Cited by 142

The endoplasmic reticulum stress response and diabetic kidney disease

Cunard, R. A., & Sharma, K. (2011) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00021.2011 · Cited by 139

Luman/CREB3 Induces Transcription of the Endoplasmic Reticulum (ER) Stress Response Protein Herp through an ER Stress Response Element

Liang, G., Audas, T. E., Li, Y., Cockram, G. P., Dean, J. D., Martyn, A. C., Kokame, K., & Lu, R. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.01046-06 · Cited by 139

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