Endoplasmic Reticulum Stress: Signaling the Unfolded Protein Response

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 4,039

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

Wei, M. C., Zong, W.-X., Cheng, E. H.-Y., Lindsten, T., Panoutsakopoulou, V., Ross, A. J., Roth, K. A., MacGregor, G. R., Thompson, C. B., & Korsmeyer, S. J. (2001) · Science · doi:10.1126/science.1059108 · Cited by 3,988

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., Sadri, N., Yun, C., Popko, B., Paules, R., et al. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00105-9 · Cited by 3,323

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

Regulated Translation Initiation Controls Stress-Induced Gene Expression in Mammalian Cells

Harding, H. P., Novoa, I., Zhang, Y., Zeng, H., Wek, R., Schapira, M., & Ron, D. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)00108-8 · Cited by 3,276

Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-β

Nakagawa, T., Zhu, H., Morishima, N., Li, E., Xu, J., Yankner, B. A., & Yuan, J. (2000) · Nature · doi:10.1038/47513 · Cited by 3,256

Coupling of Stress in the ER to Activation of JNK Protein Kinases by Transmembrane Protein Kinase IRE1

Urano, F., Wang, X., Bertolotti, A., Zhang, Y., Chung, P., Harding, H. P., & Ron, D. (2000) · Science · doi:10.1126/science.287.5453.664 · Cited by 2,988

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 2,860

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

Calfon, M., 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 2,820

The mitochondrial permeability transition pore and its role in cell death

CROMPTON, M. (1999) · Biochemical Journal · doi:10.1042/bj3410233 · Cited by 2,432

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 2,069

XBP-1 Regulates a Subset of Endoplasmic Reticulum Resident Chaperone Genes in the Unfolded Protein Response

Lee, A.-H., Iwakoshi, N. N., & Glimcher, L. H. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.21.7448-7459.2003 · Cited by 2,037

CHOP is implicated in programmed cell death in response to impaired function of the endoplasmic reticulum

Zinszner, H., Kuroda, M., Wang, X., Batchvarova, N., Lightfoot, R. T., Remotti, H., Stevens, J. L., & Ron, D. (1998) · Genes & Development · doi:10.1101/gad.12.7.982 · Cited by 2,014

CHOP induces death by promoting protein synthesis and oxidation in the stressed endoplasmic reticulum

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 2,001

Functional and Genomic Analyses Reveal an Essential Coordination between the Unfolded Protein Response and ER-Associated Degradation

Travers, K. J., Patil, C. K., Wodicka, L., Lockhart, D. J., Weissman, J. S., & Walter, P. (2000) · Cell · doi:10.1016/s0092-8674(00)80835-1 · Cited by 1,992

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.-O., Aw, T.-Y., & Holbrook, N. J. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.4.1249-1259.2001 · Cited by 1,889

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

BCL-2, BCL-XL Sequester BH3 Domain-Only Molecules Preventing BAX- and BAK-Mediated Mitochondrial Apoptosis

Cheng, E. H.-Y. A., Wei, M. C., Weiler, S., Flavell, R. A., Mak, T. W., Lindsten, T., & Korsmeyer, S. J. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00320-3 · Cited by 1,707

Rapid degradation of a large fraction of newly synthesized proteins by proteasomes

Schubert, U., Antón, L. C., Gibbs, J., Norbury, C. C., Yewdell, J. W., & Bennink, J. R. (2000) · Nature · doi:10.1038/35008096 · Cited by 1,536

ER Stress Regulation of ATF6 Localization by Dissociation of BiP/GRP78 Binding and Unmasking of Golgi Localization Signals

Shen, J., Chen, X., Hendershot, L., & Prywes, R. (2002) · Developmental Cell · doi:10.1016/s1534-5807(02)00203-4 · Cited by 1,456

A Selective Inhibitor of eIF2α Dephosphorylation Protects Cells from ER Stress

Boyce, M., Bryant, K. F., Jousse, C., Long, K., Harding, H. P., Scheuner, D., Kaufman, R. J., Ma, D., Coen, D. M., Ron, D., et al. (2005) · Science · doi:10.1126/science.1101902 · Cited by 1,403

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 1,386

BAX and BAK Regulation of Endoplasmic Reticulum Ca 2+ : A Control Point for Apoptosis

Scorrano, L., Oakes, S. A., Opferman, J. T., Cheng, E. H., Sorcinelli, M. D., Pozzan, T., & Korsmeyer, S. J. (2003) · Science · doi:10.1126/science.1081208 · Cited by 1,385

Translational Control Is Required for the Unfolded Protein Response and In Vivo Glucose Homeostasis

Scheuner, D., Song, B., McEwen, E., Liu, C., Laybutt, R., Gillespie, P., Saunders, T., Bonner-Weir, S., & Kaufman, R. J. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00265-9 · Cited by 1,355

ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats

Nishitoh, H., Matsuzawa, A., Tobiume, K., Saegusa, K., Takeda, K., Inoue, K., Hori, S., Kakizuka, A., & Ichijo, H. (2002) · Genes & Development · doi:10.1101/gad.992302 · Cited by 1,338

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 1,317

Plasma cell differentiation requires the transcription factor XBP-1

Reimold, A. M., Iwakoshi, N. N., Manis, J., Vallabhajosyula, P., Szomolanyi-Tsuda, E., Gravallese, E. M., Friend, D., Grusby, M. J., Alt, F., & Glimcher, L. H. (2001) · Nature · doi:10.1038/35085509 · Cited by 1,305

Oligomerization and phosphorylation of the Ire1p kinase during intracellular signaling from the endoplasmic reticulum to the nucleus.

Shamu, C. E., & Walter, P. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00666.x · Cited by 1,264

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 1,231

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 1,228

ERAD: the long road to destruction

Meusser, B., Hirsch, C., Jarosch, E., & Sommer, T. (2005) · Nature Cell Biology · doi:10.1038/ncb0805-766 · Cited by 1,220

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

Cross-Talk between Two Cysteine Protease Families

Nakagawa, T., & Yuan, J. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.150.4.887 · Cited by 1,168

CHOP, a novel developmentally regulated nuclear protein that dimerizes with transcription factors C/EBP and LAP and functions as a dominant-negative inhibitor of gene transcription.

Ron, D., & Habener, J. F. (1992) · Genes & Development · doi:10.1101/gad.6.3.439 · Cited by 1,168

JNK phosphorylation of Bim-related members of the Bcl2 family induces Bax-dependent apoptosis

Lei, K., & Davis, R. J. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0438011100 · Cited by 1,068

The Proapoptotic Activity of the Bcl-2 Family Member Bim Is Regulated by Interaction with the Dynein Motor Complex

Puthalakath, H., Huang, D. C. S., O’Reilly, L. A., King, S. M., & Strasser, A. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80456-6 · Cited by 1,054

Investigation of the subcellular distribution of the bcl-2 oncoprotein: residence in the nuclear envelope, endoplasmic reticulum, and outer mitochondrial membranes.

Krajewski, S., Tanaka, S., Takayama, S., Schibler, M. J., Fenton, W. A., & Reed, J. C. (1993) · PubMed · Cited by 1,030

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 1,028

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

BCL-2 Is Phosphorylated and Inactivated by an ASK1/Jun N-Terminal Protein Kinase Pathway Normally Activated at G2/M

Yamamoto, K., Ichijo, H., & Korsmeyer, S. J. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.12.8469 · Cited by 1,003

Endoplasmic Reticulum Stress Signaling in Disease

Marciniak, S. J., & Ron, D. (2006) · Physiological Reviews · doi:10.1152/physrev.00015.2006 · Cited by 945

ATF6 Activated by Proteolysis Binds in the Presence of NF-Y (CBF) Directly to the cis -Acting Element Responsible for the Mammalian Unfolded Protein Response

Yoshida, H., Okada, T., Haze, K., Yanagi, H., Yura, T., Negishi, M., & Mori, K. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.18.6755-6767.2000 · Cited by 934

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

Tirasophon, W., Welihinda, A. A., & Kaufman, R. J. (1998) · Genes & Development · doi:10.1101/gad.12.12.1812 · Cited by 917

An Endoplasmic Reticulum Stress-specific Caspase Cascade in Apoptosis

Morishima, N., Nakanishi, K., Takenouchi, H., Shibata, T., & Yasuhiko, Y. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204973200 · Cited by 901

The Transmembrane Kinase Ire1p Is a Site-Specific Endonuclease That Initiates mRNA Splicing in the Unfolded Protein Response

Sidrauski, C., & Walter, P. (1997) · Cell · doi:10.1016/s0092-8674(00)80369-4 · Cited by 899

ER stress and neurodegenerative diseases

Lindholm, D., Wootz, H., & Korhonen, L. (2006) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4401778 · Cited by 882

From acute ER stress to physiological roles of the Unfolded Protein Response

Wu, J., & Kaufman, R. J. (2006) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4401840 · Cited by 868

Activation of Caspase-12, an Endoplastic Reticulum (ER) Resident Caspase, through Tumor Necrosis Factor Receptor-associated Factor 2-dependent Mechanism in Response to the ER Stress

Yoneda, T., Imaizumi, K., Oono, K., Yui, D., Gomi, F., Katayama, T., & Tohyama, M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010677200 · Cited by 865

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/jci14550 · Cited by 857

Involvement of caspase-4 in endoplasmic reticulum stress-induced apoptosis and Aβ-induced cell death

Hitomi, J., Katayama, T., Eguchi, Y., Kudo, T., Taniguchi, M., Koyama, Y., Manabe, T., Yamagishi, S., Bando, Y., Imaizumi, K., et al. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200310015 · Cited by 830

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., & Sambrook, J. (1993) · Cell · doi:10.1016/0092-8674(93)90521-q · Cited by 818

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

Cloning of mammalian Ire1 reveals diversity in the ER stress responses

Wang, X.-Z. (1998) · The EMBO Journal · doi:10.1093/emboj/17.19.5708 · Cited by 787

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., & Wek, R. C. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.12.7499 · Cited by 774

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

Translational control in the endoplasmic reticulum stress response

Ron, D. (2002) · Journal of Clinical Investigation · doi:10.1172/jci0216784 · Cited by 726

Endoplasmic Reticulum Stress Activates Cleavage of CREBH to Induce a Systemic Inflammatory Response

Zhang, K., Shen, X., Wu, J., Sakaki, K., Saunders, T., Rutkowski, D. T., Back, S. H., & Kaufman, R. J. (2006) · Cell · doi:10.1016/j.cell.2005.11.040 · Cited by 716

Two Distinct Stress Signaling Pathways Converge Upon the CHOP Promoter During the Mammalian Unfolded Protein Response

Ma, Y., Brewer, J. W., Alan Diehl, J., & Hendershot, L. M. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00234-6 · Cited by 688

Signals from the Stressed Endoplasmic Reticulum Induce C/EBP-Homologous Protein (CHOP/GADD153)

Wang, X.-Z., Lawson, B., Brewer, J. W., Zinszner, H., Sanjay, A., Mi, L.-J., Boorstein, R., Kreibich, G., Hendershot, L. M., & Ron, D. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.8.4273 · Cited by 669

ASK1 Is Essential for JNK/SAPK Activation by TRAF2

Nishitoh, H., Saitoh, M., Mochida, Y., Takeda, K., Nakano, H., Rothe, M., Miyazono, K., & Ichijo, H. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80283-x · Cited by 646

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

Deng, J., Lu, P. D., Zhang, Y., Scheuner, D., 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 643

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 616

The PERK Eukaryotic Initiation Factor 2α Kinase Is Required for the Development of the Skeletal System, Postnatal Growth, and the Function and Viability of the Pancreas

Zhang, P., McGrath, B., Li, S., Frank, A., Zambito, F., Reinert, J., Gannon, M., Ma, K., McNaughton, K., & Cavener, D. R. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.11.3864-3874.2002 · Cited by 604

Nitric oxide-induced apoptosis in pancreatic β cells is mediated by the endoplasmic reticulum stress pathway

Oyadomari, S., Takeda, K., Takiguchi, M., Gotoh, T., Matsumoto, M., Wada, I., Akira, S., Araki, E., & Mori, M. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.191207498 · Cited by 599

Bax and Bak can localize to the endoplasmic reticulum to initiate apoptosis

Zong, W.-X., Li, C., Hatzivassiliou, G., Lindsten, T., Yu, Q.-C., Yuan, J., & Thompson, C. B. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200302084 · Cited by 595

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 587

Coupling Endoplasmic Reticulum Stress to the Cell Death Program

Rao, R. V., Hermel, E., Castro-Obregon, S., del Rio, G., Ellerby, L. M., Ellerby, H. M., & Bredesen, D. E. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102225200 · Cited by 575

Distinct roles of activating transcription factor 6 (ATF6) and double-stranded RNA-activated protein kinase-like endoplasmic reticulum kinase (PERK) in transcription during the mammalian unfolded protein response

OKADA, T., YOSHIDA, H., AKAZAWA, R., NEGISHI, M., & MORI, K. (2002) · Biochemical Journal · doi:10.1042/bj20020391 · Cited by 522

An essential role in liver development for transcription factor XBP-1

Reimold, A. M., Etkin, A., Clauss, I., Perkins, A., Friend, D. S., Zhang, J., Horton, H. F., Scott, A., Orkin, S. H., Byrne, M. C., et al. (2000) · Genes & Development · doi:10.1101/gad.14.2.152 · Cited by 516

The Luminal Domain of ATF6 Senses Endoplasmic Reticulum (ER) Stress and Causes Translocation of ATF6 from the ER to the Golgi

Chen, X., Shen, J., & Prywes, R. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m110636200 · Cited by 488

PERK mediates cell-cycle exit during the mammalian unfolded protein response

Brewer, J. W., & Diehl, J. A. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.220247197 · Cited by 463

tRNA Ligase Is Required for Regulated mRNA Splicing in the Unfolded Protein Response

Sidrauski, C., Cox, J. S., & Walter, P. (1996) · Cell · doi:10.1016/s0092-8674(00)81361-6 · Cited by 443

Endoplasmic reticulum stress in health and disease

Zhao, L., & Ackerman, S. L. (2006) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2006.06.005 · Cited by 440

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

Lipson, K. L., Fonseca, S. G., Ishigaki, S., Nguyen, L. X., Foss, E., Bortell, R., Rossini, A. A., & Urano, F. (2006) · Cell Metabolism · doi:10.1016/j.cmet.2006.07.007 · Cited by 430

Phosphorylation of the α Subunit of Eukaryotic Initiation Factor 2 Is Required for Activation of NF-κB in Response to Diverse Cellular Stresses

Jiang, H.-Y., Wek, S. A., McGrath, B. C., Scheuner, D., Kaufman, R. J., Cavener, D. R., & Wek, R. C. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.16.5651-5663.2003 · Cited by 423

Ligand-independent Dimerization Activates the Stress Response Kinases IRE1 and PERK in the Lumen of the Endoplasmic Reticulum

Liu, C. Y., Schröder, M., & Kaufman, R. J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m004454200 · Cited by 421

A 22 bp cis-acting element is necessary and sufficient for the induction of the yeast KAR2 (BiP) gene by unfolded proteins.

Mori, K., Sant, A., Kohno, K., Normington, K., Gething, M. J., & Sambrook, J. F. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05323.x · Cited by 374

The crystal structure of human IRE1 luminal domain reveals a conserved dimerization interface required for activation of the unfolded protein response

Zhou, J., Liu, C. Y., Back, S. H., Clark, R. L., Peisach, D., Xu, Z., & Kaufman, R. J. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0606480103 · Cited by 374

The promoter region of the yeast KAR2 (BiP) gene contains a regulatory domain that responds to the presence of unfolded proteins in the endoplasmic reticulum.

Kohno, K., Normington, K., Sambrook, J., Gething, M. J., & Mori, K. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.2.877 · Cited by 358

Human caspase 12 has acquired deleterious mutations

Fischer, H., Koenig, U., Eckhart, L., & Tschachler, E. (2002) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)00289-9 · Cited by 347

The unfolded protein response sensor IRE1α is required at 2 distinct steps in B cell lymphopoiesis

Zhang, K., Wong, H. N., Song, B., Miller, C. N., Scheuner, D., & Kaufman, R. J. (2005) · Journal of Clinical Investigation · doi:10.1172/jci200521848 · Cited by 347

Enhanced bacterial clearance and sepsis resistance in caspase-12-deficient mice

Saleh, M., Mathison, J. C., Wolinski, M. K., Bensinger, S. J., Fitzgerald, P., Droin, N., Ulevitch, R. J., Green, D. R., & Nicholson, D. W. (2006) · Nature · doi:10.1038/nature04656 · Cited by 322

Block of HAC1 mRNA Translation by Long-Range Base Pairing Is Released by Cytoplasmic Splicing upon Induction of the Unfolded Protein Response

Rüegsegger, U., Leber, J. H., & Walter, P. (2001) · Cell · doi:10.1016/s0092-8674(01)00505-0 · Cited by 311

Translational control by the ER transmembrane kinase/ribonuclease IRE1 under ER stress

Iwawaki, T., Hosoda, A., Okuda, T., Kamigori, Y., Nomura-Furuwatari, C., Kimata, Y., Tsuru, A., & Kohno, K. (2001) · Nature Cell Biology · doi:10.1038/35055065 · Cited by 308

Apoptotic crosstalk between the endoplasmic reticulum and mitochondria controlled by Bcl-2

Häcki, J., Egger, L., Monney, L., Conus, S., Rossé, T., Fellay, I., & Borner, C. (2000) · Oncogene · doi:10.1038/sj.onc.1203592 · Cited by 301

OASIS, a CREB/ATF-family member, modulates UPR signalling in astrocytes

Kondo, S., Murakami, T., Tatsumi, K., Ogata, M., Kanemoto, S., Otori, K., Iseki, K., Wanaka, A., & Imaizumi, K. (2005) · Nature Cell Biology · doi:10.1038/ncb1213 · Cited by 292

Selective Inhibition of Eukaryotic Translation Initiation Factor 2α Dephosphorylation Potentiates Fatty Acid-induced Endoplasmic Reticulum Stress and Causes Pancreatic β-Cell Dysfunction and Apoptosis

Cnop, M., Ladriere, L., Hekerman, P., Ortis, F., Cardozo, A. K., Dogusan, Z., Flamez, D., Boyce, M., Yuan, J., & Eizirik, D. L. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m607627200 · Cited by 289

PERK EIF2AK3 control of pancreatic β cell differentiation and proliferation is required for postnatal glucose homeostasis

Zhang, W., Feng, D., Li, Y., Iida, K., McGrath, B., & Cavener, D. R. (2006) · Cell Metabolism · doi:10.1016/j.cmet.2006.11.002 · Cited by 285

Phosphorylation of BCL‐2 regulates ER Ca2+ homeostasis and apoptosis

Bassik, M. C., Scorrano, L., Oakes, S. A., Pozzan, T., & Korsmeyer, S. J. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600104 · Cited by 278

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

Nadanaka, S., Okada, T., Yoshida, H., & Mori, K. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00408-06 · Cited by 266

Identification of ERSE-II, a New cis-Acting Element Responsible for the ATF6-dependent Mammalian Unfolded Protein Response

Kokame, K., Kato, H., & Miyata, T. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010486200 · Cited by 262

Cotranslocational Degradation Protects the Stressed Endoplasmic Reticulum from Protein Overload

Oyadomari, S., Yun, C., Fisher, E. A., Kreglinger, N., Kreibich, G., Oyadomari, M., Harding, H. P., Goodman, A. G., Harant, H., Garrison, J. L., et al. (2006) · Cell · doi:10.1016/j.cell.2006.06.051 · Cited by 252

Identification of the G13 (cAMP-response-element-binding protein-related protein) gene product related to activating transcription factor 6 as a transcriptional activator of the mammalian unfolded protein response

Haze, K., Okada, T., Yoshida, H., Yanagi, H., Yura, T., Negishi, M., & Mori, K. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3550019 · Cited by 247

Ubiquitous Calpains Promote Caspase-12 and JNK Activation during Endoplasmic Reticulum Stress-induced Apoptosis

Tan, Y., Dourdin, N., Wu, C., De Veyra, T., Elce, J. S., & Greer, P. A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m601299200 · Cited by 237

The DRiP hypothesis decennial: support, controversy, refinement and extension

Yewdell, J. W., & Nicchitta, C. V. (2006) · Trends in Immunology · doi:10.1016/j.it.2006.06.008 · Cited by 218

The Unfolded Protein Response Pathway in

Welihinda, A. A., & Kaufman, R. J. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.30.18181 · Cited by 176

CREB-H: a novel mammalian transcription factor belonging to the CREB/ATF family and functioning via the box-B element with a liver-specific expression

Omori, Y. (2001) · Nucleic Acids Research · doi:10.1093/nar/29.10.2154 · Cited by 166

Palindrome with Spacer of One Nucleotide Is Characteristic of the cis-Acting Unfolded Protein Response Element inSaccharomyces cerevisiae

Mori, K., Ogawa, N., Kawahara, T., Yanagi, H., & Yura, T. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.16.9912 · Cited by 152

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 151

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

Bcl-2 and Bcl-X L Block Thapsigargin-Induced Nitric Oxide Generation, c-Jun NH 2 -Terminal Kinase Activity, and Apoptosis

Srivastava, R. K., Sollott, S. J., Khan, L., Hansford, R. G., Lakatta, E. G., & Longo, D. L. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.8.5659 · Cited by 148

Endoplasmic reticulum stress-induced cell death requires mitochondrial membrane permeabilization

Boya, P., COHEN, I. R., Zamzami, N., Vieira, H. L. A., & Kroemer, G. (2002) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401006 · Cited by 141

Cytoplasmic IRE1α-mediated XBP1 mRNA Splicing in the Absence of Nuclear Processing and Endoplasmic Reticulum Stress

Back, S. H., Lee, K., Vink, E. I., & Kaufman, R. J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602030200 · Cited by 135

Luman, the Cellular Counterpart of Herpes Simplex Virus VP16, Is Processed by Regulated Intramembrane Proteolysis

Raggo, C. M., Rapin, N., Stirling, J., Gobeil, P., Smith-Windsor, E., O’Hare, P., & Misra, V. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.16.5639-5649.2002 · Cited by 133

Ribosomal Stress Couples the Unfolded Protein Response to p53-dependent Cell Cycle Arrest

Zhang, F., Hamanaka, R. B., Bobrovnikova-Marjon, E. V., Gordan, J. D., Dai, M., Lu, H., Simon, M. C., & Diehl, J. A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m604674200 · Cited by 128

CREB4, a Transmembrane bZip Transcription Factor and Potential New Substrate for Regulation and Cleavage by S1P

Stirling, J., & O’Hare, P. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-06-0500 · Cited by 117

Reversible phosphorylation of eukaryotic initiation factor 2? in response to endoplasmic reticular signaling

Prostko, C. R., Brostrom, M. A., & Brostrom, C. O. (1993) · Molecular and Cellular Biochemistry · doi:10.1007/bf01076776 · Cited by 114

TcGPXII, a glutathione-dependent Trypanosoma cruzi peroxidase with substrate specificity restricted to fatty acid and phospholipid hydroperoxides, is localized to the endoplasmic reticulum

Wilkinson, S. R., Taylor, M. C., TOUITHA, S., Maurício, I. L., MEYER, D. J., & Kelly, J. M. (2002) · Biochemical Journal · doi:10.1042/bj20020038 · Cited by 112

Activation of Mammalian Unfolded Protein Response Is Compatible with the Quality Control System Operating in the Endoplasmic Reticulum

Nadanaka, S., Yoshida, H., Kano, F., Murata, M., & Mori, K. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e03-09-0693 · Cited by 109

Requirement of the p38 mitogen-activated protein kinase signalling pathway for the induction of the 78 kDa glucose-regulated protein/immunoglobulin heavy-chain binding protein by azetidine stress: activating transcription factor 6 as a target for stress-induced phosphorylation

Luo, S. D., & Lee, A. S. (2002) · Biochemical Journal · doi:10.1042/bj20011802 · Cited by 87

Cross-talk between two apoptotic pathways activated by endoplasmic reticulum stress: differential contribution of caspase-12 and AIF

Sanges, D., & Marigo, V. (2006) · APOPTOSIS · doi:10.1007/s10495-006-9006-2 · Cited by 84

OASIS is a transcriptional activator of CREB/ATF family with a transmembrane domain

Omori, Y., Imai, J., Suzuki, Y., Watanabe, S., Tanigami, A., & Sugano, S. (2002) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)00253-x · Cited by 84

A new pharmacology – drugging stressed folding pathways

Wiseman, R. L., & Balch, W. E. (2005) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2005.06.011 · Cited by 63

BH3‐only proteins: Integrated control point of apoptosis

Shibue, T., & Taniguchi, T. (2006) · International Journal of Cancer · doi:10.1002/ijc.21751 · Cited by 54

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

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Goffin, L., Vodala, S., Fraser, C., Ryan, J. L., Timms, M., Meusburger, S., Catimel, B., Nice, E. C., Silver, P. A., Xiao, C.-Y., et al. (2006) · Molecular Biology of the Cell · doi:10.1091/mbc.e06-04-0292 · Cited by 24

The Role of Hypoxia in Development of the Mammalian Embryo

Dunwoodie, S. L. (2009) · Developmental Cell · doi:10.1016/j.devcel.2009.11.008 · Cited by 651

Positive and Negative Regulation of Insulin Signaling by Reactive Oxygen and Nitrogen Species

Bashan, N., Kovsan, J., Kachko, I., Ovadia, H., & Rudich, A. (2009) · Physiological Reviews · doi:10.1152/physrev.00014.2008 · Cited by 542

The unfolded protein response is activated in skeletal muscle by high-fat feeding: potential role in the downregulation of protein synthesis

Deldicque, L., Cani, P. D., Philp, A., Raymackers, J.-M., Meakin, P. J., Ashford, M. L. J., Delzenne, N. M., Francaux, M., & Baar, K. (2010) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00038.2010 · Cited by 163

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Hicks, D., Farsani, G. T., Laval, S., Collins, J., Sarkozy, A., Martoni, E., Shah, A., Zou, Y., Koch, M., Bonnemann, C. G., et al. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddt637 · Cited by 111

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Zhou, X., Chen, Z., Zhong, W., Yu, R., & He, L. (2019) · Human & Experimental Toxicology · doi:10.1177/0960327119842273 · Cited by 18