Mechanisms, regulation and functions of the unfolded protein response

Signal integration in the endoplasmic reticulum unfolded protein response

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The Unfolded Protein Response: From Stress Pathway to Homeostatic Regulation

Walter, P., & Ron, D. (2011) · Science · doi:10.1126/science.1209038 · Cited by 5,893 · see citing works

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 5,120 · see citing works

XBP1 mRNA Is Induced by ATF6 and Spliced by IRE1 in Response to ER Stress to Produce a Highly Active Transcription Factor

Yoshida, H., Matsui, T., Yamamoto, A., Okada, T., & Mori, K. (2001) · Cell · doi:10.1016/s0092-8674(01)00611-0 · Cited by 4,054 · see citing works

Proapoptotic BAX and BAK: A Requisite Gateway to Mitochondrial Dysfunction and Death

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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 · see citing works

Mutation of the mouse klotho gene leads to a syndrome resembling ageing

Kuro-o, M., Matsumura, Y., Aizawa, H., Kawaguchi, H., Suga, T., Utsugi, T., Ohyama, Y., Kurabayashi, M., Kaname, T., Kume, E., et al. (1997) · Nature · doi:10.1038/36285 · Cited by 3,837 · see citing works

An Integrated Stress Response Regulates Amino Acid Metabolism and Resistance to Oxidative Stress

Harding, H. P., Zhang, Y., Zeng, H., Novoa, I., Lu, P. D., Calfon, M. A., Sadri, N., Yun, C., Popko, B., Paules, R. S., et al. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00105-9 · Cited by 3,336 · see citing works

Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase

Harding, H. P., Zhang, Y., & Ron, D. (1999) · Nature · doi:10.1038/16729 · Cited by 3,310 · see citing works

Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response

Bertolotti, A., Zhang, Y., Hendershot, L. M., Harding, H. P., & Ron, D. (2000) · Nature Cell Biology · doi:10.1038/35014014 · Cited by 2,871 · see citing works

IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA

Calfon, M. A., Zeng, H., Urano, F., Till, J. H., Hubbard, S. R., Harding, H. P., Clark, S. G., & Ron, D. (2002) · Nature · doi:10.1038/415092a · Cited by 2,826 · see citing works

Adapting Proteostasis for Disease Intervention

Balch, W. E., Morimoto, R. I., Dillin, A., & Kelly, J. W. (2008) · Science · doi:10.1126/science.1141448 · Cited by 2,495 · see citing works

Regulation of apoptosis in health and disease: the balancing act of BCL-2 family proteins

Singh, R., Letai, A., & Sarosiek, K. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0089-8 · Cited by 2,111 · see citing works

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 2,073 · see citing works

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 2,004 · see citing works

Gadd153 Sensitizes Cells to Endoplasmic Reticulum Stress by Down-Regulating Bcl2 and Perturbing the Cellular Redox State

McCullough, K. D., Martindale, J. L., Klotz, L., Aw, T. Y., & Holbrook, N. J. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.4.1249-1259.2001 · Cited by 1,895 · see citing works

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 · see citing works

Reinitiation involving upstream ORFs regulates <i>ATF4</i> mRNA translation in mammalian cells

Vattem, K. M., & Wek, R. C. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0400541101 · Cited by 1,696 · see citing works

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 · see citing works

Signals from the lysosome: a control centre for cellular clearance and energy metabolism

Settembre, C., Fraldi, A., Medina, D. L., & Ballabio, A. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3565 · Cited by 1,689 · see citing works

The Unfolded Protein Response and Cell Fate Control

Hetz, C. A., & Papa, F. R. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.06.017 · Cited by 1,567 · see citing works

IRE1 Signaling Affects Cell Fate During the Unfolded Protein Response

Lin, J. H., Li, H., Yasumura, D., Cohen, H., Zhang, C., Panning, B., Shokat, K., Lavail, M., & Walter, P. (2007) · Science · doi:10.1126/science.1146361 · Cited by 1,435 · see citing works

ER Stress Triggers Apoptosis by Activating BH3-Only Protein Bim

Puthalakath, H., O’Reilly, L. A., Gunn, P. A., Lee, L., Kelly, P. N., Huntington, N. D., Hughes, P., Michalak, E. M., McKimm‐Breschkin, J. L., Motoyama, N., et al. (2007) · Cell · doi:10.1016/j.cell.2007.04.027 · Cited by 1,428 · see citing works

Feedback Inhibition of the Unfolded Protein Response by GADD34-Mediated Dephosphorylation of eIF2α

Novoa, I., Zeng, H., Harding, H. P., & Ron, D. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.153.5.1011 · Cited by 1,392 · see citing works

An Hsp70-like protein in the ER: identity with the 78 kd glucose-regulated protein and immunoglobulin heavy chain binding protein.

Munro, S., & Pelham, H. (1986) · Cell · doi:10.1016/0092-8674(86)90746-4 · Cited by 1,378 · see citing works

The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins

Kozutsumi, Y., Segal, M. S., Normington, K., Gething, M.-J. H., & Sambrook, J. (1988) · Nature · doi:10.1038/332462a0 · Cited by 1,322 · see citing works

Decay of Endoplasmic Reticulum-Localized mRNAs During the Unfolded Protein Response

Hollien, J., & Weissman, J. S. (2006) · Science · doi:10.1126/science.1129631 · Cited by 1,319 · see citing works

Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase

Cox, J. S., Shamu, C. E., & Walter, P. (1993) · Cell · doi:10.1016/0092-8674(93)90648-a · Cited by 1,240 · see citing works

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 · see citing works

Diabetes Mellitus and Exocrine Pancreatic Dysfunction in Perk−/− Mice Reveals a Role for Translational Control in Secretory Cell Survival

Harding, H. P., Zeng, H., Zhang, Y., Jungries, R., Chung, P., Plesken, H., Sabatini, D. D., & Ron, D. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00264-7 · Cited by 1,217 · see citing works

XBP1, Downstream of Blimp-1, Expands the Secretory Apparatus and Other Organelles, and Increases Protein Synthesis in Plasma Cell Differentiation

Shaffer, A. L., Shelef, M. A., Iwakoshi, N. N., Lee, A., Qian, S., Zhao, H., Yu, X., Yang, L., Tan, B. K., Rosenwald, A., et al. (2004) · Immunity · doi:10.1016/j.immuni.2004.06.010 · Cited by 1,060 · see citing works

Fatty Acid Trafficking in Starved Cells: Regulation by Lipid Droplet Lipolysis, Autophagy, and Mitochondrial Fusion Dynamics

Rambold, A. S., Cohen, S., & Lippincott-Schwartz, J. (2015) · Developmental Cell · doi:10.1016/j.devcel.2015.01.029 · Cited by 1,038 · see citing works

A Novel Mechanism for Regulating Activity of a Transcription Factor That Controls the Unfolded Protein Response

Cox, J. S., & Walter, P. (1996) · Cell · doi:10.1016/s0092-8674(00)81360-4 · Cited by 1,034 · see citing works

Aberrant lipid metabolism disrupts calcium homeostasis causing liver endoplasmic reticulum stress in obesity

Fu, S., Yang, L., Li, P., Hofmann, O., Dicker, L. H., Hide, W. A., Lin, X., Watkins, S. M., Ivanov, A. R., & Hotamışlıgil, G. S. (2011) · Nature · doi:10.1038/nature09968 · Cited by 1,024 · see citing works

Regulated Ire1-dependent decay of messenger RNAs in mammalian cells

Hollien, J., Lin, J. H., Li, H., Stevens, N. S., Walter, P., & Weissman, J. S. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200903014 · Cited by 1,021 · see citing works

Orchestrating the unfolded protein response in health and disease

Kaufman, R. J. (2002) · Journal of Clinical Investigation · doi:10.1172/jci0216886 · Cited by 1,015 · see citing works

Translation reinitiation at alternative open reading frames regulates gene expression in an integrated stress response

Lu, P. D., Harding, H. P., & Ron, D. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200408003 · Cited by 1,006 · see citing works

ER stress and the unfolded protein response in neurodegeneration

Hetz, C. A., & Saxena, S. (2017) · Nature Reviews Neurology · doi:10.1038/nrneurol.2017.99 · Cited by 1,006 · see citing works

TLR activation of the transcription factor XBP1 regulates innate immune responses in macrophages

Martinon, F., Chen, X., Lee, A.-H., & Glimcher, L. H. (2010) · Nature Immunology · doi:10.1038/ni.1857 · Cited by 996 · see citing works

Structure and function of ER membrane contact sites with other organelles

Phillips, M. J., & Voeltz, G. K. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2015.8 · Cited by 933 · see citing works

A stress response pathway from the endoplasmic reticulum to the nucleus requires a novel bifunctional protein kinase/endoribonuclease (Ire1p) in mammalian cellsPreprint

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Plasma cell differentiation and the unfolded protein response intersect at the transcription factor XBP-1

Iwakoshi, N. N., Lee, A.-H., Vallabhajosyula, P., Otipoby, K. L., Rajewsky, K., & Glimcher, L. H. (2003) · Nature Immunology · doi:10.1038/ni907 · Cited by 880 · see citing works

Mutations in filamin 1 Prevent Migration of Cerebral Cortical Neurons in Human Periventricular Heterotopia

Fox, J. W., Lamperti, E. D., Ekşioğlu, Y. Z., Hong, S. E., Feng, Y., Graham, D. A., Scheffer, I. E., Dobyns, W. B., Hirsch, B. A., Radtke, R. A., et al. (1998) · Neuron · doi:10.1016/s0896-6273(00)80651-0 · Cited by 877 · see citing works

GRP78 Induction in Cancer: Therapeutic and Prognostic Implications

Lee, A. S. (2007) · Cancer Research · doi:10.1158/0008-5472.can-07-0325 · Cited by 856 · see citing works

Immunoglobulin heavy chain binding protein

Haas, I. G., & Wabl, M. R. (1983) · Nature · doi:10.1038/306387a0 · Cited by 854 · see citing works

PERK is required at the ER-mitochondrial contact sites to convey apoptosis after ROS-based ER stress

Verfaillie, T., Rubio, N., Garg, A. D., Bultynck, G., Rizzuto, R., Decuypere, J.-P., Piette, J. G., Linehan, C., Gupta, S., Afshin Samali, A., et al. (2012) · Cell Death and Differentiation · doi:10.1038/cdd.2012.74 · Cited by 851 · see citing works

IRE1α Induces Thioredoxin-Interacting Protein to Activate the NLRP3 Inflammasome and Promote Programmed Cell Death under Irremediable ER Stress

Lerner, A. G., Upton, J.-P., Praveen, P. V. K., Ghosh, R., Nakagawa, Y., Igbaria, A., Shen, S., Nguyen, V. Q., Backes, B. J., Heiman, M., et al. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.07.007 · Cited by 841 · see citing works

Endoplasmic reticulum stress activates cleavage of CREBH to induce a systemic inflammatory response.

Zhang, K.-Z., Shen, X., Wu, J., Sakaki, K., Saunders, T., Rutkowski, D., Back, S., & Kaufman, R. J. (2006) · Cell · doi:10.1016/j.cell.2005.11.040 · Cited by 840 · see citing works

A transmembrane protein with a cdc2+CDC28-related kinase activity is required for signaling from the ER to the nucleus

Morl, K., Ma, W., Gething, M.-J. H., & Sambrook, J. (1993) · Cell · doi:10.1016/0092-8674(93)90521-q · Cited by 821 · see citing works

XBP1 promotes triple-negative breast cancer by controlling the HIF1α pathway

Chen, X., Iliopoulos, D., Zhang, Q. H., Tang, Q., Greenblatt, M. B., Hatziapostolou, M., Lim, E., Tam, W. L., Ni, M., Chen, Y., et al. (2014) · Nature · doi:10.1038/nature13119 · Cited by 817 · see citing works

IRE1α Kinase Activation Modes Control Alternate Endoribonuclease Outputs to Determine Divergent Cell Fates

Han, D., Lerner, A. G., Walle, L. V., Upton, J.-P., Xu, W., Hagen, A., Backes, B. J., Oakes, S. A., & Papa, F. R. (2009) · Cell · doi:10.1016/j.cell.2009.07.017 · Cited by 816 · see citing works

EIF2AK3, encoding translation initiation factor 2-α kinase 3, is mutated in patients with Wolcott-Rallison syndrome

Delépine, M., Nicolino, M., Barrett, T., Golamaully, M., Mark Lathrop, G., & Julier, C. (2000) · Nature Genetics · doi:10.1038/78085 · Cited by 813 · see citing works

Adaptation to ER Stress Is Mediated by Differential Stabilities of Pro-Survival and Pro-Apoptotic mRNAs and Proteins

Rutkowski, D. T., Arnold, S. M., Miller, C. N., Wu, J., Li, J., Gunnison, K. M., Mori, K., Akha, A. A. S., Raden, D. L., & Kaufman, R. J. (2006) · PLoS Biology · doi:10.1371/journal.pbio.0040374 · Cited by 804 · see citing works

Noise Propagation in Gene Networks

Pedraza, J. M., & van Oudenaarden, A. (2005) · Science · doi:10.1126/science.1109090 · Cited by 796 · see citing works

Cloning of mammalian Ire1 reveals diversity in the ER stress responses

Wang, X., Harding, H. P., Zhang, Y., Jolicoeur, E. M., Kuroda, M., & Ron, D. (1998) · The EMBO Journal · doi:10.1093/emboj/17.19.5708 · Cited by 787 · see citing works

Phosphorylation of initiation factor 2α by protein kinase GCN2 mediates gene-specific translational control of GCN4 in yeast

Dever, T. E., Feng, L., Wek, R. C., Cigan, A. M., Donahue, T. F., & Hinnebusch, A. G. (1992) · Cell · doi:10.1016/0092-8674(92)90193-g · Cited by 776 · see citing works

Identification and Characterization of Pancreatic Eukaryotic Initiation Factor 2 α-Subunit Kinase, PEK, Involved in Translational Control

Shi, Y., Vattem, K. M., Sood, R., An, J., Liang, J., Stramm, L. E., & Wek, R. C. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.12.7499 · Cited by 776 · see citing works

Pharmacological brake-release of mRNA translation enhances cognitive memory

Sidrauski, C., Acosta‐Alvear, D., Khoutorsky, A., Vedantham, P., Hearn, B. R., Li, H., Gamache, K., Gallagher, C. M., Ang, K. K. H., Wilson, C. G. M., et al. (2013) · eLife · doi:10.7554/elife.00498 · Cited by 732 · see citing works

ER stress‐regulated translation increases tolerance to extreme hypoxia and promotes tumor growth

Bi, M., Naczki, C., Koritzinsky, M., Fels, D. R., Blais, J. D., Hu, N., Harding, H. P., Novoa, I., Varia, M. A., Raleigh, J. A., et al. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600777 · Cited by 732 · see citing works

Mammalian Genes Coordinately Regulated by Growth Arrest Signals and DNA-Damaging Agents

Fornace, A. J., Nebert, D. W., Hollander, M. C., Luethy, J. D., Papathanasiou, M., Fargnoli, J., & Holbrook, N. J. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.10.4196 · Cited by 705 · see citing works

Complementary Signaling Pathways Regulate the Unfolded Protein Response and Are Required for C. elegans Development

Shen, X., Ellis, R. E., Lee, K., Liu, C.-Y., Yang, K., Solomon, A., Yoshida, H., Morimoto, R., Kurnit, D. M., Mori, K., et al. (2001) · Cell · doi:10.1016/s0092-8674(01)00612-2 · Cited by 703 · see citing works

Chop deletion reduces oxidative stress, improves β cell function, and promotes cell survival in multiple mouse models of diabetes

Song, B., Scheuner, D. L., Ron, D., Pennathur, S., & Kaufman, R. J. (2008) · Journal of Clinical Investigation · doi:10.1172/jci34587 · Cited by 693 · see citing works

Unfolded Proteins Are Ire1-Activating Ligands That Directly Induce the Unfolded Protein Response

Gardner, B. M., & Walter, P. (2011) · Science · doi:10.1126/science.1209126 · Cited by 689 · see citing works

Here, there, and everywhere: The importance of ER membrane contact sites

Wu, H., Carvalho, P., & Voeltz, G. K. (2018) · Science · doi:10.1126/science.aan5835 · Cited by 688 · see citing works

ATF6α Optimizes Long-Term Endoplasmic Reticulum Function to Protect Cells from Chronic Stress

Wu, J., Rutkowski, D. T., Dubois, M., Swathirajan, J., Saunders, T. L., Wang, J., Song, B., Yau, G. D.-Y., & Kaufman, R. J. (2007) · Developmental Cell · doi:10.1016/j.devcel.2007.07.005 · Cited by 680 · see citing works

Thioredoxin-Interacting Protein Mediates ER Stress-Induced β Cell Death through Initiation of the Inflammasome

Oslowski, C. M., Hara, T., O’Sullivan-Murphy, B., Kanekura, K., Lu, S., Hara, M., Ishigaki, S., Zhu, L. J., Hayashi, E., Hui, S. T. Y., et al. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.07.005 · Cited by 678 · see citing works

In and Out of the ER: Protein Folding, Quality Control, Degradation, and Related Human Diseases

Hebert, D. N., & Molinari, M. (2007) · Physiological Reviews · doi:10.1152/physrev.00050.2006 · Cited by 671 · see citing works

The unfolded protein response signals through high-order assembly of Ire1

Korennykh, A. V., Egea, P. F., Korostelev, A. A., Finer-Moore, J., Zhang, C., Shokat, K. M., Stroud, R. M., & Walter, P. (2009) · Nature · doi:10.1038/nature07661 · Cited by 656 · see citing works

Membrane lipid saturation activates endoplasmic reticulum unfolded protein response transducers through their transmembrane domains

Volmer, R., van der Ploeg, K., & Ron, D. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1217611110 · Cited by 655 · see citing works

XBP1

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

Translational Repression Mediates Activation of Nuclear Factor Kappa B by Phosphorylated Translation Initiation Factor 2

Deng, J., Lu, P. D., Zhang, Y., Scheuner, D. L., Kaufman, R. J., Sonenberg, N., Harding, H. P., & Ron, D. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.23.10161-10168.2004 · Cited by 645 · see citing works

IRE1α Cleaves Select microRNAs During ER Stress to Derepress Translation of Proapoptotic Caspase-2

Upton, J.-P., Wang, L., Han, D., Wang, E. S., Huskey, N. E., Lim, L., Truitt, M., McManus, M. T., Ruggero, D., Goga, A., et al. (2012) · Science · doi:10.1126/science.1226191 · Cited by 640 · see citing works

Sustained translational repression by eIF2α-P mediates prion neurodegeneration

Moreno, J. A., Radford, H. E., Peretti, D., Steinert, J. R., Verity, N., Martin, M. G., Halliday, M., Morgan, J., Dinsdale, D. D., Ortori, C. A., et al. (2012) · Nature · doi:10.1038/nature11058 · Cited by 616 · see citing works

Endoplasmic Reticulum Stress and the Hallmarks of Cancer

Urra, H., Dufey, E., Avril, T., Chevet, É., & Hetz, C. A. (2016) · Trends in cancer · doi:10.1016/j.trecan.2016.03.007 · Cited by 607 · see citing works

Proteasome inhibitors disrupt the unfolded protein response in myeloma cells

Lee, A., Iwakoshi, N. N., Anderson, K. C., & Glimcher, L. H. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1334037100 · Cited by 600 · see citing works

On the mechanism of sensing unfolded protein in the endoplasmic reticulum

Credle, J. J., Finer-Moore, J. S., Papa, F. R., Stroud, R. M., & Walter, P. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0509487102 · Cited by 589 · see citing works

UPR Pathways Combine to Prevent Hepatic Steatosis Caused by ER Stress-Mediated Suppression of Transcriptional Master Regulators

Rutkowski, D. T., Wu, J., Back, S.-H., Callaghan, M. U., Ferris, S. P., Iqbal, J., Clark, R. L., Miao, H. Z., Hassler, J. R., Fornek, J. L., et al. (2008) · Developmental Cell · doi:10.1016/j.devcel.2008.10.015 · Cited by 580 · see citing works

XBP-1 Is a Cell-Nonautonomous Regulator of Stress Resistance and Longevity

Taylor, R. C., & Dillin, A. G. (2013) · Cell · doi:10.1016/j.cell.2013.05.042 · Cited by 570 · see citing works

Opposing unfolded-protein-response signals converge on death receptor 5 to control apoptosis

Lu, M., Lawrence, D. A., Marsters, S. A., Acosta‐Alvear, D., Kimmig, P., Mendez, A. S., Paton, A. W., Paton, J. C., Walter, P., & Ashkenazi, A. (2014) · Science · doi:10.1126/science.1254312 · Cited by 569 · see citing works

Stress-Independent Activation of XBP1s and/or ATF6 Reveals Three Functionally Diverse ER Proteostasis Environments

Shoulders, M. D., Ryno, L. M., Genereux, J. C., Moresco, J. J., Tu, P. G., Wu, C., Yates, J. R., Su, A. I., Kelly, J. W., & Wiseman, R. L. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.03.024 · Cited by 558 · see citing works

XBP-1 deficiency in the nervous system protects against amyotrophic lateral sclerosis by increasing autophagy

Hetz, C., Thielen, P., Matus, S., Nassif, M., Court, F., Kiffin, R., Martinez, G., Cuervo, A. M., Brown, R. H., & Glimcher, L. H. (2009) · Genes &amp; Development · doi:10.1101/gad.1830709 · Cited by 530 · see citing works

Endoplasmic reticulum stress in immunity.

Bettigole, S., & Glimcher, L. (2015) · Annual Review of Immunology · doi:10.1146/annurev-immunol-032414-112116 · Cited by 491 · see citing works

XBP‐1 is required for biogenesis of cellular secretory machinery of exocrine glands

Lee, A., Chu, G. C., Iwakoshi, N. N., & Glimcher, L. H. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600903 · Cited by 452 · see citing works

Mfn2 modulates the UPR and mitochondrial function via repression of PERK

Muñoz, J. P., Ivanova, S., Sánchez‐Wandelmer, J., Martínez‐Cristóbal, P., Noguera, E., Sancho, A., Díaz‐Ramos, A., Hernández‐Alvarez, M. I., Sebastián, D., Mauvezin, C., et al. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.168 · Cited by 451 · see citing works

BiP Binding to the ER-Stress Sensor Ire1 Tunes the Homeostatic Behavior of the Unfolded Protein Response

Pincus, D., Chevalier, M. W., Aragón, T., van Anken, E., Vidal, S. E., El‐Samad, H., & Walter, P. (2010) · PLoS Biology · doi:10.1371/journal.pbio.1000415 · Cited by 433 · see citing works

Regulation of insulin biosynthesis in pancreatic beta cells by an endoplasmic reticulum-resident protein kinase IRE1

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