Signal integration in the endoplasmic reticulum unfolded protein response

Perk is essential for translational regulation and cell survival during the unfolded protein response

Harding, H. P., Zhang, Y., Bertolotti, A., Zeng, H., & Ron, D. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)80330-5 · Cited by 2,021

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

Ye, J., Rawson, R. B., Komuro, R., Chen, X., Davé, U. P., Prywes, R., Brown, M. S., & Goldstein, J. L. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)00133-7 · Cited by 1,871

Targeted disruption of the chop gene delays endoplasmic reticulum stress-mediated diabetes

Oyadomari, S., Koizumi, A., Takeda, K., Gotoh, T., Akira, S., Araki, E., & Mori, M. (2002) · Journal of Clinical Investigation · doi:10.1172/jci0214550 · Cited by 752

XBP1

Sriburi, R., Jackowski, S., Mori, K., & Brewer, J. W. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200406136 · Cited by 653

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

Two phases of disulfide bond formation have differing requirements for oxygen

Koritzinsky, M., Levitin, F., van den Beucken, T., Rumantir, R. A., Harding, N. J., Chu, K. C., Boutros, P. C., Braakman, I., & Wouters, B. G. (2013) · Journal of Cell Biology · doi:10.1083/jcb.201307185 · Cited by 136

Adaptation of endoplasmic reticulum exit sites to acute and chronic increases in cargo load

Farhan, H., Weiss, M., Tani, K., Kaufman, R. J., & Hauri, H. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.136 · Cited by 138

Increased fidelity of protein synthesis extends lifespan

Martinez-Miguel, V. E., Lujan, C., Espie--Caullet, T., Martinez-Martinez, D., Moore, S., Backes, C., Gonzalez, S., Galimov, E. R., Brown, A. E. X., Halic, M., et al. (2021) · Cell Metabolism · doi:10.1016/j.cmet.2021.08.017 · Cited by 137

Inflammation meets metabolic disease: Gut feeling mediated by GLP-1

Zietek, T., & Rath, E. (2016) · Frontiers in Immunology · doi:10.3389/fimmu.2016.00154 · Cited by 131

A three-dimensional engineered tumour for spatial snapshot analysis of cell metabolism and phenotype in hypoxic gradients

Rodenhizer, D., Gaude, E., Cojocari, D., Mahadevan, R., Frezza, C., Wouters, B. G., & McGuigan, A. P. (2016) · Nature Materials · doi:10.1038/nmat4482 · Cited by 132

Genetic Defects in Severe Congenital Neutropenia: Emerging Insights into Life and Death of Human Neutrophil Granulocytes

Klein, C. (2011) · Annual Review of Immunology · doi:10.1146/annurev-immunol-030409-101259 · Cited by 132

Death Protein 5 and p53-Upregulated Modulator of Apoptosis Mediate the Endoplasmic Reticulum Stress–Mitochondrial Dialog Triggering Lipotoxic Rodent and Human β-Cell Apoptosis

Cunha, D. A., Igoillo-Esteve, M., Gurzov, E. N., Germano, C. M., Naamane, N., Marhfour, I., Fukaya, M., Vanderwinden, J.-M., Gysemans, C., Mathieu, C., et al. (2012) · Diabetes · doi:10.2337/db12-0123 · Cited by 130

A Comprehensive Review About SARS-CoV-2

Haque, S. M., Ashwaq, O., Sarief, A., & Azad John Mohamed, A. K. (2020) · Future Virology · doi:10.2217/fvl-2020-0124 · Cited by 121

Resveratrol treatment in patients with polycystic ovary syndrome decreased pro-inflammatory and endoplasmic reticulum stress markers

Brenjian, S., Moini, A., Yamini, N., Kashani, L., Faridmojtahedi, M., Bahramrezaie, M., Khodarahmian, M., & Amidi, F. (2020) · American Journal of Reproductive Immunology · doi:10.1111/aji.13186 · Cited by 128

Is fat so bad? Modulation of endoplasmic reticulum stress by lipid droplet formation

Hapala, I., Marza, E., & Ferreira, T. (2011) · Biology of the Cell · doi:10.1042/bc20100144 · Cited by 125

The UPR in atherosclerosis

Zhou, A. X., & Tabas, I. (2013) · Seminars in Immunopathology · doi:10.1007/s00281-013-0372-x · Cited by 121

The hyaluronidase, TMEM2, promotes ER homeostasis and longevity independent of the UPRER

Schinzel, R. T., Higuchi-Sanabria, R., Shalem, O., Moehle, E. A., Webster, B. M., Joe, L., Bar-Ziv, R., Frankino, P. A., Durieux, J., Pender, C., et al. (2019) · Cell · doi:10.1016/j.cell.2019.10.018 · Cited by 117

Adaptation to chronic ER stress enforces pancreatic β-cell plasticity

Chen, C.-W., Guan, B.-J., Alzahrani, M. R., Gao, Z., Gao, L., Bracey, S., Wu, J., Mbow, C. A., Jobava, R., Haataja, L., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-32425-7 · Cited by 116

Endoplasmic Reticulum Stress and Unfolded Protein Response in Cartilage Pathophysiology; Contributing Factors to Apoptosis and Osteoarthritis

Hughes, A., Oxford, A., Tawara, K., Jorcyk, C., & Oxford, J. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18030665 · Cited by 113

Pharmaceutical integrated stress response enhancement protects oligodendrocytes and provides a potential multiple sclerosis therapeutic

Way, S. W., Podojil, J. R., Clayton, B. L., Zaremba, A., Collins, T. L., Kunjamma, R. B., Robinson, A. P., Brugarolas, P., Miller, R. H., Miller, S. D., et al. (2015) · Nature Communications · doi:10.1038/ncomms7532 · Cited by 108

The pathophysiology of defective proteostasis in the hypothalamus — from obesity to ageing

Cavadas, C., Aveleira, C. A., Souza, G. F. P., & Velloso, L. A. (2016) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2016.107 · Cited by 105

Cholesterol biosynthesis and ER stress in peroxisome deficiency

Faust, P. L., & Kovacs, W. J. (2014) · Biochimie · doi:10.1016/j.biochi.2013.10.019 · Cited by 107

Expression of an activating mutation in the gene encoding the KATP channel subunit Kir6.2 in mouse pancreatic β cells recapitulates neonatal diabetes

Girard, C. A., Wunderlich, F. T., Shimomura, K., Collins, S., Kaizik, S., Proks, P., Abdulkader, F., Clark, A., Ball, V., Zubcevic, L., et al. (2008) · Journal of Clinical Investigation · doi:10.1172/jci35772 · Cited by 105

Thrombospondin 1 and Its Diverse Roles as a Regulator of Extracellular Matrix in Fibrotic Disease

Murphy-Ullrich, J. E. (2019) · Journal of Histochemistry & Cytochemistry · doi:10.1369/0022155419851103 · Cited by 104

BAP1 inhibits the ER stress gene regulatory network and modulates metabolic stress response

Dai, F., Lee, H., Zhang, Y., Zhuang, L., Yao, H., Xi, Y., Xiao, Z.-D., You, M. J., Li, W., Su, X., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1619588114 · Cited by 94

Endoplasmic reticulum stress in human skeletal muscle: any contribution to sarcopenia?

Deldicque, L. (2013) · Frontiers in Physiology · doi:10.3389/fphys.2013.00236 · Cited by 91

A multi-omics analysis reveals the unfolded protein response regulon and stress-induced resistance to folate-based antimetabolites

Reich, S., Nguyen, C. D. L., Has, C., Steltgens, S., Soni, H., Coman, C., Freyberg, M., Bichler, A., Seifert, N., Conrad, D., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-16747-y · Cited by 90

Type I interferons and endoplasmic reticulum stress in health and disease

(2020) · International Review of Cell and Molecular Biology · doi:10.1016/bs.ircmb.2019.10.004 · Cited by 83

Stress Signaling Pathways for the Pathogenicity of Cryptococcus

Bahn, Y.-S., & Jung, K.-W. (2013) · Eukaryotic Cell · doi:10.1128/ec.00218-13 · Cited by 84

Together JUN and DDIT3 (CHOP) control retinal ganglion cell death after axonal injury

Syc-Mazurek, S. B., Fernandes, K. A., Wilson, M. P., Shrager, P., & Libby, R. T. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0214-8 · Cited by 74

Aging and the UPR(ER)

Taylor, R. C. (2016) · Brain Research · doi:10.1016/j.brainres.2016.04.017 · Cited by 83

Dissection of Ire1 Functions Reveals Stress Response Mechanisms Uniquely Evolved in Candida glabrata

Miyazaki, T., Nakayama, H., Nagayoshi, Y., Kakeya, H., & Kohno, S. (2013) · PLoS Pathogens · doi:10.1371/journal.ppat.1003160 · Cited by 78

Inactivation of VCP/ter94 Suppresses Retinal Pathology Caused by Misfolded Rhodopsin in Drosophila

Griciuc, A., Aron, L., Roux, M. J., Klein, R., Giangrande, A., & Ueffing, M. (2010) · PLoS Genetics · doi:10.1371/journal.pgen.1001075 · Cited by 78

Macrophage proliferation and apoptosis in atherosclerosis

Andrés, V., Pello, O. M., & Silvestre-Roig, C. (2012) · Current Opinion in Lipidology · doi:10.1097/mol.0b013e328357a379 · Cited by 74

The role of MRH domain-containing lectins in ERAD

Hosokawa, N., Kamiya, Y., & Kato, K. (2010) · Glycobiology · doi:10.1093/glycob/cwq013 · Cited by 71

Endoplasmic reticulum is at the crossroads of autophagy, inflammation, and apoptosis signaling pathways and participates in the pathogenesis of diabetes mellitus

Su, J., Zhou, L., Kong, X., Yang, X., Xiang, X., Zhang, Y., Li, X., & Sun, L. (2013) · Journal of Diabetes Research · doi:10.1155/2013/193461 · Cited by 70

Eating the dead to keep atherosclerosis at bay

Brophy, M. L., Dong, Y., Wu, H., Rahman, H. N. A., Song, K., & Chen, H. (2017) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2017.00002 · Cited by 68

PERK regulates skeletal muscle mass and contractile function in adult mice

Gallot, Y. S., Bohnert, K. R., Straughn, A. R., Xiong, G., Hindi, S. M., & Kumar, A. (2019) · The FASEB Journal · doi:10.1096/fj.201800683rr · Cited by 67

Potential for cellular stress response to hepatic factor VIII expression from AAV vector

Zolotukhin, I., Markusic, D. M., Palaschak, B., Hoffman, B. E., Srikanthan, M. A., & Herzog, R. W. (2016) · Molecular Therapy - Methods & Clinical Development · doi:10.1038/mtm.2016.63 · Cited by 65

Triglyceride-Rich Lipoprotein Modulates Endothelial Vascular Cell Adhesion Molecule (VCAM)-1 Expression via Differential Regulation of Endoplasmic Reticulum Stress

Wang, Y. I., Bettaieb, A., Sun, C., DeVerse, J. S., Radecke, C. E., Mathew, S., Edwards, C. M., Haj, F. G., Passerini, A. G., & Simon, S. I. (2013) · PLoS ONE · doi:10.1371/journal.pone.0078322 · Cited by 65

The ATF6α arm of the Unfolded Protein Response mediates replicative senescence in human fibroblasts through a COX2/prostaglandin E 2 intracrine pathway

Cormenier, J., Martin, N., Deslé, J., Salazar-Cardozo, C., Pourtier, A., Abbadie, C., & Pluquet, O. (2018) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2017.08.003 · Cited by 64

A Systematic Search for Endoplasmic Reticulum (ER) Membrane-associated RING Finger Proteins Identifies Nixin/ZNRF4 as a Regulator of Calnexin Stability and ER Homeostasis

Neutzner, A., Neutzner, M., Benischke, A.-S., Ryu, S.-W., Frank, S., Youle, R. J., & Karbowski, M. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.197459 · Cited by 62

Transcription of the NKG2D ligand MICA is suppressed by the IRE1/XBP1 pathway of the unfolded protein response through the regulation of E2F1

Obiedat, A., Seidel, E., Mahameed, M., Bernani, O., Tsukerman, P., Voutetakis, K., Chatziioannou, A., Mcmahon, M., Avril, T., Chevet, E., et al. (2019) · The FASEB Journal · doi:10.1096/fj.201801350rr · Cited by 51

Mitochondria, Oxytocin, and Vasopressin: Unfolding the Inflammatory Protein Response

Bordt, E. A., Smith, C. J., Demarest, T. G., Bilbo, S. D., & Kingsbury, M. A. (2019) · Neurotoxicity Research · doi:10.1007/s12640-018-9962-7 · Cited by 58

The IRE1α-XBP1 pathway regulates metabolic stress-induced compensatory proliferation of pancreatic β-cells

Xu, T., Yang, L., Yan, C., Wang, X., Huang, P., Zhao, F., Zhao, L., Zhang, M., Jia, W., Wang, X., et al. (2014) · Cell Research · doi:10.1038/cr.2014.55 · Cited by 60

Amyotrophic lateral sclerosis pathogenesis: a journey through the secretory pathway

Nassif, M., Matus, S., Castillo, K., & Hetz, C. (2010) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.2991 · Cited by 60

Impaired neurotransmission in ether lipid-deficient nerve terminals

Brodde, A., Teigler, A., Brugger, B., Lehmann, W. D., Wieland, F., Berger, J., & Just, W. W. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds097 · Cited by 57

Overexpression of GADD34 enhances production of recombinant human antithrombin III in Chinese hamster ovary cells

Omasa, T., Takami, T., Ohya, T., Kiyama, E., Hayashi, T., Nishii, H., Miki, H., Kobayashi, K., Honda, K., & Ohtake, H. (2008) · Journal of Bioscience and Bioengineering · doi:10.1263/jbb.106.568 · Cited by 57

Control of HIF-1α Expression by eIF2α Phosphorylation–Mediated Translational Repression

Zhu, K., Chan, W., Heymach, J., Wilkinson, M., & McConkey, D. J. (2009) · Cancer Research · doi:10.1158/0008-5472.can-08-4103 · Cited by 55

Photosensitized methyl paraben induces apoptosis via caspase dependent pathway under ambient UVB exposure in human skin cells

Dubey, D., Chopra, D., Singh, J., Srivastav, A. K., Kumari, S., Verma, A., & Ray, R. S. (2017) · Food and Chemical Toxicology · doi:10.1016/j.fct.2017.07.056 · Cited by 53

Icariin improves the cognitive function of APP/PS1 mice via suppressing endoplasmic reticulum stress

Li, F., Zhang, Y., Lu, X., Shi, J., & Gong, Q. (2019) · Life Sciences · doi:10.1016/j.lfs.2019.116739 · Cited by 51

ER Stress-Induced Secretion of Proteins and Their Extracellular Functions in the Heart

Meyer, B. A., & Doroudgar, S. (2020) · Cells · doi:10.3390/cells9092066 · Cited by 51

ER Stress Induces Anabolic Resistance in Muscle Cells through PKB-Induced Blockade of mTORC1

Deldicque, L., Bertrand, L., Patton, A., Francaux, M., & Baar, K. (2011) · PLoS ONE · doi:10.1371/journal.pone.0020993 · Cited by 50

The Endoplasmic Reticulum Stress Sensor Inositol-Requiring Enzyme 1α Augments Bacterial Killing through Sustained Oxidant Production

Abuaita, B. H., Burkholder, K. M., Boles, B. R., & O’Riordan, M. X. (2015) · mBio · doi:10.1128/mbio.00705-15 · Cited by 48

Inhibition of acyl-coenzyme A: cholesterol acyl transferase modulates amyloid precursor protein trafficking in the early secretory pathway

Huttunen, H. J., Peach, C., Bhattacharyya, R., Barren, C., Pettingell, W., Hutter-Paier, B., Windisch, M., Berezovska, O., & Kovacs, D. M. (2009) · The FASEB Journal · doi:10.1096/fj.09-134999 · Cited by 48

Endoplasmic Reticulum Stress and Tumor Microenvironment in Bladder Cancer: The Missing Link

Nie, Z., Chen, M., Wen, X., Gao, Y., Huang, D., Cao, H., Peng, Y., Guo, N., Ni, J., & Zhang, S. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.683940 · Cited by 43

Asbestos-induced Disruption of Calcium Homeostasis Induces Endoplasmic Reticulum Stress in Macrophages

Ryan, A. J., Larson-Casey, J. L., He, C., Murthy, S., & Carter, A. B. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.579870 · Cited by 43

The human hepatocyte TXG-MAPr: gene co-expression network modules to support mechanism-based risk assessment

Callegaro, G., Kunnen, S. J., Trairatphisan, P., Grosdidier, S., Niemeijer, M., den Hollander, W., Guney, E., Piñero Gonzalez, J., Furlong, L., Webster, Y. W., et al. (2021) · Archives of Toxicology · doi:10.1007/s00204-021-03141-w · Cited by 43

Endurance training in mice increases the unfolded protein response induced by a high-fat diet

Deldicque, L., Cani, P. D., Delzenne, N. M., Baar, K., & Francaux, M. (2013) · Journal of Physiology and Biochemistry · doi:10.1007/s13105-012-0204-9 · Cited by 41

Reducing ER stress with chaperone therapy reverses sleep fragmentation and cognitive decline in aged mice

Hafycz, J. M., Strus, E., & Naidoo, N. (2022) · Aging Cell · doi:10.1111/acel.13598 · Cited by 34

Integrating ER and Mitochondrial Proteostasis in the Healthy and Diseased Heart

Arrieta, A., Blackwood, E. A., Stauffer, W. T., & Glembotski, C. C. (2020) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2019.00193 · Cited by 27

Absence of direct effect of low-power millimeter-wave radiation at 60.4 GHz on endoplasmic reticulum stress

Nicolas Nicolaz, C., Zhadobov, M., Desmots, F., Sauleau, R., Thouroude, D., Michel, D., & Le Drean, Y. (2009) · Cell Biology and Toxicology · doi:10.1007/s10565-008-9101-y · Cited by 24

Transcriptomic identification of TMIGD1 and its relationship with the ileal epithelial cell differentiation in Crohn’s disease

Zabana, Y., Lorén, V., Domènech, E., Aterido, A., Garcia-Jaraquemada, A., Julià, A., Vicario, M., Pedrosa, E., Ferreiro, M., Troya, J., et al. (2020) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00027.2020 · Cited by 24

Endoplasmic reticulum stress and pulmonary hypertension

Hu, Y., Yang, W., Xie, L., Liu, T., Liu, H., & Liu, B. (2020) · Pulmonary Circulation · doi:10.1177/2045894019900121 · Cited by 21

DIP2 is a unique regulator of diacylglycerol lipid homeostasis in eukaryotes

Mondal, S., Kinatukara, P., Singh, S., Shambhavi, S., Patil, G. S., Dubey, N., Singh, S. H., Pal, B., Shekar, P. C., Kamat, S. S., et al. (2022) · eLife · doi:10.7554/elife.77665 · Cited by 19

An ire1-phk1 chimera reveals a dispensable role of autokinase activity in endoplasmic reticulum stress response

Mannan, M. A.-U., Shadrick, W. R., Biener, G., Shin, B.-S., Anshu, A., Raicu, V., Frick, D. N., & Dey, M. (2013) · Journal of Molecular Biology · doi:10.1016/j.jmb.2013.02.036 · Cited by 18

Endoplasmic reticulum stress links psoriasis vulgaris with keratinocyte inflammation

Zhao, M., Luo, J., Xiao, B., Tang, H., Song, F., Ding, X., & Yang, G. (2020) · Advances in Dermatology and Allergology · doi:10.5114/ada.2020.93382 · Cited by 18

Kch1 Family Proteins Mediate Essential Responses to Endoplasmic Reticulum Stresses in the Yeasts Saccharomyces cerevisiae and Candida albicans

Stefan, C. P., & Cunningham, K. W. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.508705 · Cited by 15

Intestinal Immune Homeostasis and Inflammatory Bowel Disease: A Perspective on Intracellular Response Mechanisms

Ranjan, K. (2020) · Gastrointestinal Disorders · doi:10.3390/gidisord2030024 · Cited by 6

Combined effects of multiple endoplasmic reticulum stresses on cytokine secretion in macrophage

Kim, H.-M., Do, C.-H., & Lee, D.-H. (2012) · Biomolecules and Therapeutics · doi:10.4062/biomolther.2012.20.3.346 · Cited by 5

Nucleosome proteostasis and histone turnover

Arrieta, A., & Vondriska, T. M. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.990006 · Cited by 4