Involvement of the IRE1α-XBP1 pathway and XBP1s-dependent transcriptional reprogramming in metabolic diseases

Osf2/Cbfa1: A Transcriptional Activator of Osteoblast Differentiation

Ducy, P., Zhang, R., Geoffroy, V., Ridall, A. L., & Karsenty, G. (1997) · Cell · doi:10.1016/s0092-8674(00)80257-3 · Cited by 4,246 · see citing works

Targeted Disruption of Results in a Complete Lack of Bone Formation owing to Maturational Arrest of Osteoblasts

Komori, T., Yagi, H., Nomura, S., Yamaguchi, A., Sasaki, K., Deguchi, K., Shimizu, Y., Bronson, R. T., Gao, Y.-H., Inada, M., et al. (1997) · Cell · doi:10.1016/s0092-8674(00)80258-5 · Cited by 4,244 · 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

A central role for JNK in obesity and insulin resistance

Hirosumi, J., Tuncman, G., Chang, L., Görgün, C. Z., Uysal, K. T., Maeda, K., Karin, M., & Hotamisligil, G. S. (2002) · Nature · doi:10.1038/nature01137 · Cited by 3,359 · 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

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

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

From endoplasmic-reticulum stress to the inflammatory response

Zhang, K., & Kaufman, R. J. (2008) · Nature · doi:10.1038/nature07203 · Cited by 2,010 · see citing works

SREBP activity is regulated by mTORC1 and contributes to Akt-dependent cell growth

Porstmann, T., Santos, C. R., Griffiths, B., Cully, M., Wu, M., Leevers, S., Griffiths, J. R., Chung, Y.-L., & Schulze, A. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.07.007 · Cited by 1,413 · see citing works

XBP1 Links ER Stress to Intestinal Inflammation and Confers Genetic Risk for Human Inflammatory Bowel Disease

Kaser, A., Lee, A., Franke, A., Glickman, J. N., Zeißig, S., Tilg, H., Nieuwenhuis, E. E. S., Higgins, D. E., Schreiber, S., Glimcher, L. H., et al. (2008) · Cell · doi:10.1016/j.cell.2008.07.021 · Cited by 1,411 · see citing works

Plasma cell differentiation requires the transcription factor XBP-1

Reimold, A., Iwakoshi, N., Manis, J., Vallabhajosyula, P., Szomolanyi-Tsuda, E., Gravallese, E., Friend, D., Grusby, M., Alt, F., & Glimcher, L. (2001) · Nature · doi:10.1038/35085509 · Cited by 1,371 · 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

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

IRE1-mediated unconventional mRNA splicing and S2P-mediated ATF6 cleavage merge to regulate XBP1 in signaling the unfolded protein responsePreprint

Lee, K., Tirasophon, W., Shen, X., Michalak, M., Prywes, R., Okada, T., Yoshida, H., Mori, K., & Kaufman, R. J. (2002) · Genes & Development · doi:10.1101/gad.964702 · Cited by 1,055 · 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

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 · cited 2× · see citing works

Regulation of Hepatic Lipogenesis by the Transcription Factor XBP1

Lee, A.-H., Scapa, E., Cohen, D. E., & Glimcher, L. (2008) · Science · doi:10.1126/science.1158042 · Cited by 983 · see citing works

XBP1 Controls Diverse Cell Type- and Condition-Specific Transcriptional Regulatory Networks

Acosta‐Alvear, D., Zhou, Y., Blais, A., Tsikitis, M., Lents, N. H., Arias, C., Lennon, C. J., Kluger, Y., & Dynlacht, B. D. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.06.011 · Cited by 853 · 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

GRP78 expression inhibits insulin and ER stress–induced SREBP-1c activation and reduces hepatic steatosis in mice

Kammoun, H. L., Chabanon, H., Hainault, I., Luquet, S., Magnan, C., Koike, T., Ferré, P., & Foufelle, F. (2009) · Journal of Clinical Investigation · doi:10.1172/jci37007 · Cited by 732 · 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

A circadian rhythm orchestrated by histone deacetylase 3 controls hepatic lipid metabolism

Feng, D., Liu, T., Sun, Z., Bugge, A., Mullican, S. E., Alenghat, T., Liu, X. S., & Lazar, M. A. (2011) · Science · doi:10.1126/science.1198125 · Cited by 701 · 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

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

Adiponectin: mechanistic insights and clinical implications

Turer, A. T., & Scherer, P. E. (2012) · Diabetologia · doi:10.1007/s00125-012-2598-x · Cited by 636 · see citing works

A Stress Signaling Pathway in Adipose Tissue Regulates Hepatic Insulin Resistance

Sabio, G., Das, M., Mora, A., Zhang, Z., Jun, J. Y., Ko, H. J., Barrett, T., Kim, J. K., & Davis, R. J. (2008) · Science · doi:10.1126/science.1160794 · Cited by 604 · see citing works

The unfolded protein response: integrating stress signals through the stress sensor IRE1α.

Hetz, C., Martinon, F., Rodríguez, D., & Glimcher, L. (2011) · Physiological Reviews · doi:10.1152/physrev.00001.2011 · Cited by 571 · see citing works

XBP1 Is Essential for Survival under Hypoxic Conditions and Is Required for Tumor Growth

Romero‐Ramírez, L., Cao, H., Nelson, D. W., Hammond, E. M., Lee, A., Yoshida, H., Mori, K., Glimcher, L. H., Denko, N. C., Giaccia, A. J., et al. (2004) · Cancer Research · doi:10.1158/0008-5472.can-04-1606 · Cited by 570 · see citing works

Prolonged Endoplasmic Reticulum Stress in Hypertrophic and Failing Heart After Aortic Constriction

Okada, K.-I., Minamino, T., Tsukamoto, Y., Liao, Y., Tsukamoto, O., Takashima, S., Hirata, A., Fujita, M., Nagamachi, Y., Nakatani, T., et al. (2004) · Circulation · doi:10.1161/01.cir.0000137836.95625.d4 · Cited by 522 · see citing works

JNK1 in Hematopoietically Derived Cells Contributes to Diet-Induced Inflammation and Insulin Resistance without Affecting Obesity

Solinas, G., Vilcu, C., Neels, J. G., Bandyopadhyay, G. K., Luo, J.-L., Naugler, W., Grivennikov, S., Wynshaw-Boris, A., Scadeng, M., Olefsky, J. M., et al. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.09.011 · Cited by 513 · see citing works

Regulation of the brown and white fat gene programs through a PRDM16/CtBP transcriptional complex

Kajimura, S., Seale, P., Tomaru, T., Erdjument-Bromage, H., Cooper, M. P., Ruas, J. L., Chin, S., Tempst, P., Lazar, M. A., & Spiegelman, B. M. (2008) · Genes & Development · doi:10.1101/gad.1666108 · Cited by 468 · 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

pXBP1(U) encoded in XBP1 pre-mRNA negatively regulates unfolded protein response activator pXBP1(S) in mammalian ER stress response

Yoshida, H., Oku, M., Suzuki, M., & Mori, K. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200508145 · Cited by 417 · see citing works

Translational Pausing Ensures Membrane Targeting and Cytoplasmic Splicing of <i>XBP1u</i> mRNA

Yanagitani, K., Kimata, Y., Kadokura, H., & Kohno, K. (2011) · Science · doi:10.1126/science.1197142 · Cited by 362 · see citing works

The Unfolded Protein Response Is an Important Regulator of Inflammatory Genes in Endothelial Cells

Gargalovic, P. S., Gharavi, N. M., Clark, M. J., Pagnon, J. C., Yang, W.-P., He, A., Truong, A. B., Baruch-Oren, T., Berliner, J. A., Kirchgessner, T. G., et al. (2006) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000242903.41158.a1 · Cited by 338 · see citing works

Activation of the Unfolded Protein Response in Infarcted Mouse Heart and Hypoxic Cultured Cardiac Myocytes

Thuerauf, D. J., Marcinko, M. C., Gude, N. A., Rubio, M., Sussman, M. A., & Glembotski, C. C. (2006) · Circulation Research · doi:10.1161/01.res.0000233317.70421.03 · Cited by 307 · see citing works

Unfolded Protein Response Signaling and Metabolic Diseases

Lee, J., & Özcan, U. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.r113.534743 · Cited by 306 · see citing works

Targeting the UPR transcription factor XBP1 protects against Huntington's disease through the regulation of FoxO1 and autophagy.

Vidal, R. L., Figueroa, A., Court, F., Thielen, P., Molina, C., Wirth, C., Caballero, B., Kiffin, R., Segura-Aguilar, J., Cuervo, A., et al. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds040 · Cited by 300 · see citing works

Regulation of glucose homeostasis through a XBP-1–FoxO1 interaction

Zhou, Y., Lee, J., Reno, C. M., Sun, C., Park, S. W., Chung, J., Lee, J., Fisher, S. J., White, M. F., Biddinger, S. B., et al. (2011) · Nature Medicine · doi:10.1038/nm.2293 · Cited by 295 · see citing works

The IRE1α-XBP1 Pathway of the Unfolded Protein Response is Required for Adipogenesis

Sha, H.-B., He, Y., Chen, H., Wang, C., Zenno, A., Shi, H., Yang, X.-Y., Zhang, X.-M., & Qi, L. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2009.04.009 · Cited by 294 · see citing works

A New Member of the Leucine Zipper Class of Proteins that Binds to the HLA DRα Promoter

Liou, H., Boothby, M. R., Finn, P. W., et al. (1990) · Science · doi:10.1126/science.2321018 · Cited by 293 · see citing works

Endoplasmic Reticulum Stress Plays Critical Role in Brain Damage After Cerebral Ischemia/Reperfusion in Rats

Nakka, V. P., Gusain, A., & Raghubir, R. (2010) · Neurotoxicity research · doi:10.1007/s12640-009-9110-5 · Cited by 287 · see citing works

XBP1 mRNA Splicing Triggers an Autophagic Response in Endothelial Cells through BECLIN-1 Transcriptional Activation

Margariti, A., Li, H., Chen, T., Martin, D., Vizcay‐Barrena, G., Alam, S., Karamariti, E., Xiao, Q., Zampetaki, A., Zhang, Z., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.412783 · Cited by 284 · see citing works

The regulatory subunits of PI3K, p85α and p85β, interact with XBP-1 and increase its nuclear translocation

Park, S. W., Zhou, Y., Lee, J., Lu, A., Sun, C., Chung, J., Ueki, K., & Özcan, U. (2010) · Nature Medicine · doi:10.1038/nm.2099 · Cited by 282 · see citing works

Silencing of Lipid Metabolism Genes through IRE1α-Mediated mRNA Decay Lowers Plasma Lipids in Mice

So, J., Hur, K. Y., Tarrio, M. L., Ruda, V. M., Frank-Kamenetsky, M. D., Fitzgerald, K. J., Koteliansky, V., Lichtman, A. H., Iwawaki, T., Glimcher, L. H., et al. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.09.004 · Cited by 280 · see citing works

Dual and opposing roles of the unfolded protein response regulated by IRE1α and XBP1 in proinsulin processing and insulin secretion

Lee, A., Heidtman, K. J., Hotamışlıgil, G. S., & Glimcher, L. H. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1105564108 · Cited by 277 · see citing works

IRE1α-XBP1s Induces PDI Expression to Increase MTP Activity for Hepatic VLDL Assembly and Lipid Homeostasis

Wang, S., Chen, Z., Lam, V., Han, J., Hassler, J. R., Finck, B. N., Davidson, N. O., & Kaufman, R. J. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.09.003 · Cited by 233 · see citing works

Sustained activation of XBP1 splicing leads to endothelial apoptosis and atherosclerosis development in response to disturbed flow

Zeng, L., Zampetaki, A., Margariti, A., Pepe, A. E., Alam, S., Martin, D., Xiao, Q., Wang, W., Jin, Z., COCKERILL, G. W., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0903197106 · Cited by 229 · see citing works

The chemical chaperone 4-phenylbutyrate inhibits adipogenesis by modulating the unfolded protein response

Basseri, S., Lhoták, Š., Sharma, A. M., & Austin, R. C. (2009) · Journal of Lipid Research · doi:10.1194/jlr.m900216-jlr200 · Cited by 223 · see citing works

P38 MAPK REGULATED XBP1s NUCLEAR TRANSLOCATION AND mRNA STABILITY ARE CRUCIAL FOR MAINTENANCE OF GLUCOSE HOMEOSTASIS IN OBESITY

Sun, C., Lee, J., Zhou, Y.-J., Lee, J., Gokalp, D., Herrema, H., Park, S., Davis, R., & Ozcan, U. (2011) · Nature Medicine · doi:10.1038/nm.2449 · Cited by 192 · see citing works

A regulatory subunit of phosphoinositide 3-kinase increases the nuclear accumulation of X-box–binding protein-1 to modulate the unfolded protein response

Winnay, J. N., Boucher, J., Mori, M. A., Ueki, K., & Kahn, C. R. (2010) · Nature Medicine · doi:10.1038/nm.2121 · Cited by 191 · see citing works

Circadian Clock-Coordinated 12 Hr Period Rhythmic Activation of the IRE1α Pathway Controls Lipid Metabolism in Mouse Liver

Cretenet, G., Clech, M. L., & Gachon, F. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2009.11.002 · Cited by 187 · see citing works

Cotranslational Targeting of XBP1 Protein to the Membrane Promotes Cytoplasmic Splicing of Its Own mRNA

Yanagitani, K., Imagawa, Y., Iwawaki, T., Hosoda, A., Saito, M., Kimata, Y., & Kohno, K. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.02.033 · Cited by 166 · see citing works

Identification of a consensus element recognized and cleaved by IRE1α

Oikawa, D., Tokuda, M., Hosoda, A., et al. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq452 · Cited by 163 · see citing works

Hepatic IRE1α regulates fasting-induced metabolic adaptive programs through the XBP1s–PPARα axis signalling

Shao, M., Shan, B., Liu, Y., Deng, Y., Cheng, Y., Wu, Y., Mao, T., Qiu, Y., Zhou, Y., Jiang, S., et al. (2014) · Nature Communications · doi:10.1038/ncomms4528 · Cited by 157 · see citing works

Phosphoinositide 3-kinase regulatory subunit p85α suppresses insulin action via positive regulation of PTEN

Taniguchi, C. M., Tran, T. T., Kondo, T., Luo, J., Ueki, K., Cantley, L. C., & Kahn, C. R. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0604628103 · Cited by 152 · see citing works

Prevention of Steatosis by Hepatic JNK1

Sabio, G., Cavanagh, J., Ko, H. J., Jung, D. Y., Gray, S., Jun, J. Y., Barrett, T., Mora, A., Kim, J. K., & Davis, R. J. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2009.09.007 · Cited by 148 · see citing works

Murine Gcm1 gene is expressed in a subset of placental trophoblast cells

Basyuk, E. I., Cross, J. C., Corbin, J., Nakayama, H., Hunter, P., Nait‐Oumesmar, B., & Lazzarini, R. A. (1999) · Developmental Dynamics · doi:10.1002/(sici)1097-0177(199904)214:4 · Cited by 148 · see citing works

Endoplasmic Reticulum Stress Regulator XBP-1 Contributes to Effector CD8+ T Cell Differentiation during Acute Infection

Kamimura, D., & Bevan, M. J. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.181.8.5433 · Cited by 147 · see citing works

Activation of PPARα Ameliorates Hepatic Insulin Resistance and Steatosis in High Fructose–Fed Mice Despite Increased Endoplasmic Reticulum Stress

Chan, S. M. H., Sun, R., Zeng, X., Choong, Z.-H., Wang, H., Watt, M. J., & Ye, J. (2013) · Diabetes · doi:10.2337/db12-1397 · Cited by 145 · see citing works

Dissociation of Inositol-requiring Enzyme (IRE1α)-mediated c-Jun N-terminal Kinase Activation from Hepatic Insulin Resistance in Conditional X-box-binding Protein-1 (XBP1) Knock-out Mice

Jurczak, M. J., Lee, A., Jornayvaz, F. R., Lee, H., Birkenfeld, A. L., Guigni, B. A., Kahn, M., Samuel, V. T., Glimcher, L. H., & Shulman, G. I. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.316760 · Cited by 142 · see citing works

IRE1β Inhibits Chylomicron Production by Selectively Degrading MTP mRNA

Iqbal, J., Dai, K., Seimon, T. A., Jungreis, R., Oyadomari, M., Kuriakose, G., Ron, D., Tabas, I. A., & Hussain, M. M. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.03.005 · Cited by 140 · see citing works

The Xbp1s/GalE axis links ER stress to postprandial hepatic metabolism

Deng, Y., Wang, Z. V., Tao, C., Gao, N., Holland, W. L., Ferdous, A., Repa, J. J., Liang, G., Ye, J., Lehrman, M. A., et al. (2012) · Journal of Clinical Investigation · doi:10.1172/jci62819 · Cited by 139 · see citing works

Vascular Endothelial Cell Growth–Activated XBP1 Splicing in Endothelial Cells Is Crucial for Angiogenesis

Zeng, L., Xiao, Q., Chen, M., et al. (2013) · Circulation · doi:10.1161/circulationaha.112.001337 · Cited by 136 · see citing works

Ligand-independent activation of estrogen receptor by XBP-1

Ding, L. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg731 · Cited by 127 · see citing works

XBP1 Controls Maturation of Gastric Zymogenic Cells by Induction of MIST1 and Expansion of the Rough Endoplasmic Reticulum

Huh, W. J., Esen, E., Geahlen, J. H., Bredemeyer, A. J., Lee, A., Shi, G., Konieczny, S. F., Glimcher, L. H., & Mills, J. C. (2010) · Gastroenterology · doi:10.1053/j.gastro.2010.08.050 · Cited by 125 · see citing works

Emerging roles for XBP1, a sUPeR transcription factor

He, Y., Sun, S.-Y., Sha, H.-B., Liu, Z., Yang, L., Xue, Z., Chen, H., & Qi, L. (2010) · Gene Expression · doi:10.3727/105221610x12819686555051 · Cited by 122 · see citing works

Bone morphogenetic protein-2 activates NADPH oxidase to increase endoplasmic reticulum stress and human coronary artery smooth muscle cell calcification

Liberman, M., Johnson, R. C., Handy, D. E., Loscalzo, J., & Leopold, J. A. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.08.114 · Cited by 122 · see citing works

Preconditioning with Endoplasmic Reticulum Stress Mitigates Retinal Endothelial Inflammation via Activation of X-box Binding Protein 1

Li, J., Wang, J. J., & Zhang, S. X. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.199729 · Cited by 115 · see citing works

pXBP1(U), a Negative Regulator of the Unfolded Protein Response Activator pXBP1(S), Targets ATF6 but not ATF4 in Proteasome-mediated Degradation

Yoshida, H., Uemura, A., & Mori, K. (2009) · Cell Structure and Function · doi:10.1247/csf.06028 · Cited by 114 · see citing works

ER stress signalling through eIF2α and CHOP, but not IRE1α, attenuates adipogenesis in mice

Han, J., Murthy, R., Wood, B., Song, B., Wang, S., Sun, B., Malhi, H., & Kaufman, R. J. (2013) · Diabetologia · doi:10.1007/s00125-012-2809-5 · Cited by 114 · see citing works

Endoplasmic reticulum stress leads to lipid accumulation through upregulation of SREBP-1c in normal hepatic and hepatoma cells

Fang, D., Wan, Y., Shen, W., Cao, J., Sun, Z.-X., Yu, H., Zhang, Q., Cheng, W., Chen, J., & Ning, B. (2013) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-013-1694-7 · Cited by 114 · see citing works

XBP-1u suppresses autophagy by promoting the degradation of FoxO1 in cancer cells

Zhao, Y., Li, X., Cai, M.-Y., Ma, K., Yang, J. H., Zhou, J., Fu, W., Wei, F.-Z., Wang, L., Xie, D., et al. (2013) · Cell Research · doi:10.1038/cr.2013.2 · Cited by 113 · see citing works

Constitutive Role for IRE1α-XBP1 Signaling Pathway in the Insulin-Mediated Hepatic Lipogenic Program

Ning, J., Hong, T., Ward, A. R., Pi, J., Liu, Z., Liu, H.-Y., & Cao, W. (2011) · Endocrinology · doi:10.1210/en.2010-1036 · Cited by 109 · see citing works

Endoplasmic Reticulum Stress Promotes Macrophage-derived Foam Cell Formation by Up-regulating Cluster of Differentiation 36 (CD36) Expression

Yao, S., Miao, C., Tian, H., Sang, H., Yang, N., Jiao, P., Han, J., Zong, C., & Qin, S. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.524512 · Cited by 104 · see citing works

Regulated IRE1‐dependent decay participates in curtailing immunoglobulin secretion from plasma cells

Benhamron, S., Hadar, R., Iwawaki, T., So, J., Lee, A., & Tirosh, B. (2013) · European Journal of Immunology · doi:10.1002/eji.201343953 · Cited by 97 · see citing works

In situ hybridization studies suggest a role for the basic region‐leucine zipper protein hXBP‐1 in exocrine gland and skeletal development during mouse embryogenesis

CLAUSS, I. M., Gravallese, E. M., Darling, J. M., Shapiro, F. E., Glimcher, M. J., & Glimcher, L. H. (1993) · Developmental Dynamics · doi:10.1002/aja.1001970207 · Cited by 97 · see citing works

A new player in the orchestra of cell growth: SREBP activity is regulated by mTORC1 and contributes to the regulation of cell and organ size

Porstmann, T., Santos, C. R., Lewis, C. A., Griffiths, B. L., & Schulze, A. (2009) · Biochemical Society Transactions · doi:10.1042/bst0370278 · Cited by 92 · see citing works

Potential for therapeutic manipulation of the UPR in disease

Park, S. W., & Özcan, U. (2013) · Seminars in Immunopathology · doi:10.1007/s00281-013-0370-z · Cited by 90 · see citing works

Stressed out about obesity: IRE1α-XBP1 in metabolic disorders

Sha, H.-B., He, Y., Yang, L., & Qi, L. (2011) · Trends in endocrinology and metabolism · doi:10.1016/j.tem.2011.05.002 · Cited by 86 · see citing works

SLC33A1/AT-1 Protein Regulates the Induction of Autophagy Downstream of IRE1/XBP1 Pathway

Pehar, M., Jonas, M. C., Hare, T. M., & Puglielli, L. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.363911 · Cited by 85 · see citing works

Xbp1-Independent Ire1 Signaling Is Required for Photoreceptor Differentiation and Rhabdomere Morphogenesis in Drosophila

Coelho, D. S., Cairrão, F., Zeng, X., Pires, E., Coelho, A. V., Ron, D., Ryoo, H. D., & Domingos, P. M. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.09.046 · Cited by 84 · see citing works

The Role of Adipocyte XBP1 in Metabolic Regulation during Lactation

Gregor, M. F., Misch, E. S., Yang, L., Hummasti, S., Inouye, K., Lee, A., Bierie, B., & Hotamışlıgil, G. S. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.03.042 · Cited by 81 · see citing works

A Novel Feedback Loop Regulates the Response to Endoplasmic Reticulum Stress via the Cooperation of Cytoplasmic Splicing and mRNA Translation

Majumder, M., Huang, C. C., Snider, M., Komar, A., Tanaka, J., Kaufman, R., Krokowski, D., & Hatzoglou, M. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.06665-11 · Cited by 81 · see citing works

X-Box Binding Protein 1 Is Essential for Insulin Regulation of Pancreatic α-Cell Function

Akiyama, M., Liew, C. W., Lu, S., Hu, J. Y., Martinez, R., Hambro, B., Kennedy, R. T., & Kulkarni, R. (2013) · Diabetes · doi:10.2337/db12-1747 · Cited by 79 · see citing works

BRD7 Regulates XBP1s’ Activity and Glucose Homeostasis through Its Interaction with the Regulatory Subunits of PI3K

Park, S. W., Herrema, H., Salazar, M., Çakır, I., Cabi, S., Sahin, F. B., Chiu, Y., Cantley, L. C., & Özcan, U. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.04.006 · Cited by 76 · see citing works

The p85α Regulatory Subunit of Phosphoinositide 3-Kinase Potentiates c-Jun N-Terminal Kinase-Mediated Insulin Resistance

Taniguchi, C. M., Alemán, J. O., Ueki, K., Luo, J., Asano, T., Kaneto, H., Stephanopoulos, G. N., Cantley, L. C., & Kahn, C. R. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00079-07 · Cited by 75 · see citing works

Estrogen regulation of X-box binding protein-1 and its role in estrogen induced growth of breast and endometrial cancer cells

Sengupta, S., Sharma, C. G. N., & Jordan, V. C. (2010) · Hormone Molecular Biology and Clinical Investigation · doi:10.1515/hmbci.2010.025 · Cited by 74 · see citing works

XBP-1 specifically promotes IgM synthesis and secretion, but is dispensable for degradation of glycoproteins in primary B cells

Tirosh, B., Iwakoshi, N. N., Glimcher, L. H., & Ploegh, H. L. (2005) · The Journal of Experimental Medicine · doi:10.1084/jem.20050575 · Cited by 74 · see citing works

Compartmentalized expression of three novel sarco/endoplasmic reticulum Ca2+ATPase 3 isoforms including the switch to ER stress, SERCA3f, in non-failing and failing human heart

Dally, S., Monceau, V., Corvazier, E., Bredoux, R., Raies, A. M., Bobe, R., del Monte, F., & Enouf, J. (2008) · Cell Calcium · doi:10.1016/j.ceca.2008.08.002 · Cited by 70 · see citing works

X-box binding protein 1 regulates brain natriuretic peptide through a novel AP1/CRE-like element in cardiomyocytes

Sawada, T., Minamino, T., Fu, H. Y., et al. (2010) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2010.02.004 · Cited by 67 · see citing works

Rapamycin Inhibits Postprandial-Mediated X-Box-Binding Protein-1 Splicing in Rat Liver

Pfaffenbach, K. T., Nivala, A. M., Reese, L., Ellis, F., Wang, D., Wei, Y., & Pagliassotti, M. J. (2010) · Journal of Nutrition · doi:10.3945/jn.109.119883 · Cited by 60 · see citing works

ER stress does not cause upregulation and activation of caspase-2 to initiate apoptosis

Sandow, J. J., Dorstyn, L., O’Reilly, L. A., Tailler, M., Kumar, S., Strasser, A., & Ekert, P. G. (2013) · Cell Death and Differentiation · doi:10.1038/cdd.2013.168 · Cited by 56 · see citing works

The specialized unfolded protein response of B lymphocytes: ATF6α-independent development of antibody-secreting B cells

Aragon, I. V., Barrington, R. A., Jackowski, S., Mori, K., & Brewer, J. W. (2012) · Molecular Immunology · doi:10.1016/j.molimm.2012.04.001 · Cited by 54 · see citing works

Molecular Analysis of Endoplasmic Reticulum Stress Response After Global Forebrain Ischemia/Reperfusion in Rats: Effect of Neuroprotectant Simvastatin

Urban, P., Pavlíková, M., Sivoňová, M. K., et al. (2008) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-008-9309-7 · Cited by 53 · see citing works

Mild endoplasmic reticulum stress augments the proinflammatory effect of IL-1β in pancreatic rat β-cells via the IRE1α/XBP1s pathway.

Miani, M., Colli, M., Ladrière, L., Cnop, M., & Eizirik, D. (2012) · Endocrinology · doi:10.1210/en.2011-2090 · Cited by 48 · see citing works

Activating Transcription Factor 6 Mediates Oxidized LDL-Induced Cholesterol Accumulation and Apoptosis in Macrophages by Up-Regulating CHOP Expression

Yao, S., Zong, C., Zhang, Y., et al. (2012) · Journal of Atherosclerosis and Thrombosis · doi:10.5551/jat.13425 · Cited by 45 · see citing works

Sarcalumenin plays a critical role in age-related cardiac dysfunction due to decreases in SERCA2a expression and activity

Jiao, Q., Takeshima, H., Ishikawa, Y., & Minamisawa, S. (2011) · Cell Calcium · doi:10.1016/j.ceca.2011.10.003 · Cited by 38 · see citing works

Xbp1-mediated histone H4 deacetylation contributes to DNA double-strand break repair in yeast

Tao, R., Chen, H., Gao, C., et al. (2011) · Cell Research · doi:10.1038/cr.2011.58 · Cited by 38 · see citing works

Adipocyte Spliced Form of X-Box–Binding Protein 1 Promotes Adiponectin Multimerization and Systemic Glucose Homeostasis

Sha, H.-B., Yang, L., Liu, M., Xia, S., Liu, Y., Liu, F., Kersten, S., & Qi, L. (2014) · Diabetes · doi:10.2337/db13-1067 · Cited by 38 · see citing works

Protective effects of XBP1 against oxygen and glucose deprivation/reoxygenation injury in rat primary hippocampal neurons

Ibuki, T., Yamasaki, Y., Mizuguchi, H., et al. (2012) · Neuroscience Letters · doi:10.1016/j.neulet.2012.04.053 · Cited by 34 · see citing works

XBP-1 increases ERα transcriptional activity through regulation of large-scale chromatin unfolding

Fang, Y., Yan, J., Ding, L., et al. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.08.100 · Cited by 29 · see citing works

Minimally modified low-density lipoprotein induces macrophage endoplasmic reticulum stress via toll-like receptor 4

Yao, S., Yang, N., Song, G., et al. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2012.03.003 · Cited by 26 · see citing works

Hepatic Nuclear Factor 1α (HNF1α) Dysfunction Down-regulates X-box-binding Protein 1 (XBP1) and Sensitizes β-Cells to Endoplasmic Reticulum Stress

Kirkpatrick, C. L., Wiederkehr, A., Baquié, M., Akhmedov, D., Wang, H., Gauthier, B. R., Akerman, İ., Ishihara, H., Ferrer, J. P., & Wollheim, C. B. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.247866 · Cited by 25 · see citing works

Reconstitution and characterization of the unconventional splicing of XBP1u mRNA in vitro

Shinya, S., Kadokura, H., Imagawa, Y., et al. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr132 · Cited by 23 · see citing works

Direct proteasome binding and subsequent degradation of unspliced XBP‐1 prevent its intracellular aggregation

Navon, A., Gatushkin, A., Zelcbuch, L., Shteingart, S., Farago, M., Hadar, R., & Tirosh, B. (2009) · FEBS Letters · doi:10.1016/j.febslet.2009.11.069 · Cited by 22 · see citing works

Nitric oxide selectively depletes macrophages in atherosclerotic plaques via induction of endoplasmic reticulum stress

Martinet, W., Croons, V., Timmermans, J., Herman, A. G., & Meyer, G. R. Y. D. (2007) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0707426 · Cited by 22 · see citing works

Inhibition of x-box binding protein 1 reduces tunicamycin-induced apoptosis in aged murine macrophages

Song, Y., Shen, H., Du, W., & Goldstein, D. R. (2013) · Aging Cell · doi:10.1111/acel.12105 · Cited by 21 · see citing works

[Oxidized low density lipoprotein induces macrophage endoplasmic reticulum stress via CD36.].

Yao, S., Sang, H., Yang, N., et al. (2010) · PubMed · Cited by 7 · see citing works

GANAB and N-Glycans Substrates Are Relevant in Human Physiology, Polycystic Pathology and Multiple Sclerosis: A Review

De Masi, R., & Orlando, S. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23137373 · Cited by 20 · see citing works

Induction of the unfolded protein response (UPR) during pseudorabies virus infection

Yang, S., Zhu, J., Zhou, X., et al. (2019) · Veterinary Microbiology · doi:10.1016/j.vetmic.2019.108485 · Cited by 27 · see citing works

Endoplasmic Reticulum Stress and Inflammation

Adolph, T.-E., Niederreiter, L., Blumberg, R. S., & Kaser, A. (2012) · Digestive Diseases · doi:10.1159/000338121 · Cited by 67 · see citing works

The balance between adaptive and apoptotic unfolded protein responses regulates β-cell death under ER stress conditions through XBP1, CHOP and JNK

Chan, J. Y., Luzuriaga, J., Maxwell, E. L., West, P. K., Bensellam, M., & Laybutt, D. R. (2015) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2015.06.025 · Cited by 126 · see citing works

LCN2 null mice are sensitive to endoplasmic reticulum stress and unfolded protein responses

Borkham‐Kamphorst, E., de Leur, E. V., Haas, U., et al. (2019) · Zeitschrift für Gastroenterologie · doi:10.1055/s-0038-1677061

Adaptive Unfolded Protein Response Attenuates Alcohol-Induced Pancreatic Damage

Lugea, A., Tischler, D., Nguyen, J., Gong, J., Gukovsky, I., French, S. W., Gorelick, F. S., & Pandol, S. J. (2010) · Gastroenterology · doi:10.1053/j.gastro.2010.11.038 · Cited by 159 · see citing works