Endoplasmic Reticulum Stress: Its Role in Disease and Novel Prospects for Therapy

Localization of GRP78 to mitochondria under the unfolded protein response

Sun, F.-C., Wei, S., Li, C.-W., Chang, Y.-S., Chao, C.-C., & Lai, Y.-K. (2006) · Biochemical Journal · doi:10.1042/bj20051916 · Cited by 178

Polyglutamine aggregates stimulate ER stress signals and caspase-12 activation

Kouroku, Y. (2002) · Human Molecular Genetics · doi:10.1093/hmg/11.13.1505 · Cited by 177

Treatment of Diabetes Using Traditional Chinese Medicine: Past, Present and Future

Tong, X.-L., Dong, L., Chen, L., & Zhen, Z. (2012) · The American Journal of Chinese Medicine · doi:10.1142/s0192415x12500656 · Cited by 177

HIV Protease Inhibitors Block Akt Signaling and Radiosensitize Tumor Cells Both In vitro and In vivo

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Progressive loss of β-cell function leads to worsening glucose tolerance in first-degree relatives of subjects with type 2 diabetes

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Gadd45 and Gadd153 messenger RNA levels are increased during hypoxia and after exposure of cells to agents which elevate the levels of the glucose-regulated proteins.

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Cripto Regulates Hematopoietic Stem Cells as a Hypoxic-Niche-Related Factor through Cell Surface Receptor GRP78

Miharada, K., Karlsson, G., Rehn, M., Rörby, E., Siva, K., Cammenga, J., & Karlsson, S. (2011) · Cell Stem Cell · doi:10.1016/j.stem.2011.07.016 · Cited by 170

Factorial phase III randomised trial of rofecoxib and prolonged constant infusion of gemcitabine in advanced non-small-cell lung cancer: the GEmcitabine-COxib in NSCLC (GECO) study

Gridelli, C., Gallo, C., Ceribelli, A., Gebbia, V., Gamucci, T., Ciardiello, F., Carozza, F., Favaretto, A. G., Daniele, B., Galetta, D., et al. (2007) · The Lancet Oncology · doi:10.1016/s1470-2045(07)70146-8 · Cited by 169

Regulation of PERK Signaling and Leukemic Cell Survival by a Novel Cytosolic Isoform of the UPR Regulator GRP78/BiP

Ni, M., Zhou, H., Wey, S., Baumeister, P., & Lee, A. S. (2009) · PLoS ONE · doi:10.1371/journal.pone.0006868 · Cited by 166

Using Cyclooxygenase-2 Inhibitors as Molecular Platforms to Develop a New Class of Apoptosis-Inducing Agents

Zhu, J. (2002) · CancerSpectrum Knowledge Environment · doi:10.1093/jnci/94.23.1745 · Cited by 166

Rrs1 Is Involved in Endoplasmic Reticulum Stress Response in Huntington Disease

Carnemolla, A., Fossale, E., Agostoni, E., Michelazzi, S., Calligaris, R., De Maso, L., Del Sal, G., MacDonald, M. E., & Persichetti, F. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.018325 · Cited by 164

Chemical Genomics Identifies the Unfolded Protein Response as a Target for Selective Cancer Cell Killing during Glucose Deprivation

Saito, S., Furuno, A., Sakurai, J., Sakamoto, A., Park, H.-R., Shin-ya, K., Tsuruo, T., & Tomida, A. (2009) · Cancer Research · doi:10.1158/0008-5472.can-08-2689 · Cited by 160

IRE1 plays an essential role in ER stress-mediated aggregation of mutant huntingtin via the inhibition of autophagy flux

Lee, H., Noh, J.-Y., Oh, Y., Kim, Y., Chang, J.-W., Chung, C.-W., Lee, S.-T., Kim, M., Ryu, H., & Jung, Y.-K. (2012) · Human Molecular Genetics · doi:10.1093/hmg/ddr445 · Cited by 157

Stress Chaperone GRP78/BiP Confers Chemoresistance to Tumor-Associated Endothelial Cells

Virrey, J. J., Dong, D., Stiles, C., Patterson, J. B., Pen, L., Ni, M., Schönthal, A. H., Chen, T. C., Hofman, F. M., & Lee, A. S. (2008) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-08-0060 · Cited by 157

Acute nutrient regulation of the unfolded protein response and integrated stress response in cultured rat pancreatic islets

Elouil, H., Bensellam, M., Guiot, Y., Mierde, D. V., Pascal, S. M. A., Schuit, F. C., & Jonas, J. (2007) · Diabetologia · doi:10.1007/s00125-007-0674-4 · Cited by 156

Endoplasmic Reticulum Stress and Liver Injury

Kaplowitz, N., Than, T. A., Shinohara, M., & Ji, C. (2007) · Seminars in Liver Disease · doi:10.1055/s-2007-991513 · Cited by 154

Central Administration of an Endoplasmic Reticulum Stress Inducer Inhibits the Anorexigenic Effects of Leptin and Insulin

Won, J. C., Jang, P., Namkoong, C., Koh, E. H., Kim, S. K., Park, J., Lee, K., & Kim, M. (2009) · Obesity · doi:10.1038/oby.2009.194 · Cited by 153 · cited 9×

(-)-Epigallocatechin gallate sensitizes breast cancer cells to paclitaxel in a murine model of breast carcinoma

Luo, T. L., Wang, J., Yin, Y., Hua, H., Jing, J., Sun, X., Li, M., Zhang, Y., & Jiang, Y. (2010) · Breast Cancer Research · doi:10.1186/bcr2473 · Cited by 152

Vascular Targeting and Antiangiogenesis Agents Induce Drug Resistance Effector GRP78 within the Tumor Microenvironment

Dong, D., Ko, B., Baumeister, P., Swenson, S., Costa, F. K., Markland, F. S., Stiles, C., Patterson, J. B., Bates, S. E., & Lee, A. S. (2005) · Cancer Research · doi:10.1158/0008-5472.can-05-0754 · Cited by 149

The cyclo-oxygenase-2 inhibitor celecoxib perturbs intracellular calcium by inhibiting endoplasmic reticulum Ca2+-ATPases: a plausible link with its anti-tumour effect and cardiovascular risks

JOHNSON, A. J., Hsu, A., Lin, H.-P., Song, X., & Chen, C. (2002) · Biochemical Journal · doi:10.1042/bj20020279 · Cited by 148

De‐regulation of GRP stress protein expression in human breast cancer cell lines

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The 78 kDa Glucose-Regulated Protein (GRP78/BIP) Is Expressed on the Cell Membrane, Is Released into Cell Culture Medium and Is Also Present in Human Peripheral Circulation

Delpino, A., & Castelli, M. (2002) · Bioscience Reports · doi:10.1023/a:1020966008615 · Cited by 146

The role of the unfolded protein response in the heart

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

Mechanism for the Suppression of the Mammalian Stress Response by Genistein, an Anticancer Phytoestrogen From Soy

Zhou, Y., & Lee, A. S. (1998) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/90.5.381 · Cited by 143

HIV-1 Protease Inhibitors Nelfinavir and Atazanavir Induce Malignant Glioma Death by Triggering Endoplasmic Reticulum Stress

Pyrko, P., Kardosh, A., Wang, W., Xiong, W., Schönthal, A. H., & Chen, T. C. (2007) · Cancer Research · doi:10.1158/0008-5472.can-07-0796 · Cited by 140

Chemical Biology Investigation of Cell Death Pathways Activated by Endoplasmic Reticulum Stress Reveals Cytoprotective Modulators of ASK1

Kim, I., Shu, C., Xu, W., Shiau, C., Grant, D., Vasile, S., Cosford, N. D. P., & Reed, J. C. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m807308200 · Cited by 139

Aggravated Endoplasmic Reticulum Stress as a Basis for Enhanced Glioblastoma Cell Killing by Bortezomib in Combination with Celecoxib or Its Non-Coxib Analogue, 2,5-Dimethyl-Celecoxib

Kardosh, A., Golden, E. B., Pyrko, P., Uddin, J., Hofman, F. M., Chen, T. C., Louie, S. G., Petasis, N. A., & Schönthal, A. H. (2008) · Cancer Research · doi:10.1158/0008-5472.can-07-5555 · Cited by 136

Thapsigargin, a histamine secretagogue, is a non-12-O-tetradecanolphorbol-13-acetate (TPA) type tumor promoter in two-stage mouse skin carcinogenesis

Hakii, H., Fujiki, H., Suganuma, M., Nakayasu, M., Tahira, T., Sügimura, T., Scheuer, P. J., & Christensen, S. B. (1986) · Journal of Cancer Research and Clinical Oncology · doi:10.1007/bf00389230 · Cited by 136

PROTEASOME INHIBITION IN MULTIPLE MYELOMA: Therapeutic Implication

Chauhan, D., Hideshima, T., & Anderson, K. C. (2005) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.45.120403.100037 · Cited by 135

Traditional Chinese Medicines in Treatment of Patients with Type 2 Diabetes Mellitus

Xie, W., Zhao, Y., & Zhang, Y. (2011) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2011/726723 · Cited by 132

Misfolded major histocompatibility complex class I molecules accumulate in an expanded ER-Golgi intermediate compartment.

Raposo, G., van Santen, H. M., Leijendekker, R., Geuze, H. J., & Ploegh, H. L. (1995) · The Journal of Cell Biology · doi:10.1083/jcb.131.6.1403 · Cited by 132

Preferential Cytotoxicity of Bortezomib toward Hypoxic Tumor Cells via Overactivation of Endoplasmic Reticulum Stress Pathways

Fels, D. R., Ye, J., Segan, A. T., Kridel, S. J., Spiotto, M. T., Olson, M., Koong, A. C., & Koumenis, C. (2008) · Cancer Research · doi:10.1158/0008-5472.can-08-2873 · Cited by 132

Overexpression of the stress‐protein Grp94 reduces cardiomyocyte necrosis due to calcium overload and simulated ischemia

Vitadello, M., Penzo, D., Petronilli, V., Michieli, G., Gomirato, S., Menabò, R., Lisa, F. D., & Gorza, L. (2003) · The FASEB Journal · doi:10.1096/fj.02-0644fje · Cited by 131

Nelfinavir, a new anti-cancer drug with pleiotropic effects and many paths to autophagy

Gills, J. J., LoPiccolo, J., & Dennis, P. A. (2008) · Autophagy · doi:10.4161/auto.5224 · Cited by 131

Calcium-activated endoplasmic reticulum stress as a major component of tumor cell death induced by 2,5-dimethyl-celecoxib, a non-coxib analogue of celecoxib

Pyrko, P., Kardosh, A., Liu, Y.-T., Soriano, N., Xiong, W., Chow, R. H.-P., Uddin, J., Petasis, N. A., Mircheff, A. K., Farley, R. A., et al. (2007) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-06-0629 · Cited by 128

Glucosamine-Induced Endoplasmic Reticulum Dysfunction Is Associated With Accelerated Atherosclerosis in a Hyperglycemic Mouse Model

Werstuck, G. H., Khan, M. I., Femia, G., Kim, A. J., Tedesco, V. C., Trigatti, B. L., & Shi, Y. (2006) · Diabetes · doi:10.2337/diabetes.55.01.06.db05-0633 · Cited by 128

Endoplasmic reticulum (ER) stress: hepatitis C virus induces an ER-nucleus signal transduction pathway and activates NF-κB and STAT-3

Waris, G., Tardif, K. D., & Siddiqui, A. (2002) · Biochemical Pharmacology · doi:10.1016/s0006-2952(02)01300-x · Cited by 127

Celecoxib Versus Placebo for Men With Prostate Cancer and a Rising Serum Prostate-Specific Antigen After Radical Prostatectomy and/or Radiation Therapy

Smith, M. R., Manola, J. B., Kaufman, D. S., Oh, W. K., Bubley, G. J., & Kantoff, P. W. (2006) · Journal of Clinical Oncology · doi:10.1200/jco.2005.03.7804 · Cited by 127

The HIV Protease Inhibitor Nelfinavir Downregulates Akt Phosphorylation by Inhibiting Proteasomal Activity and Inducing the Unfolded Protein Response

Gupta, A., Li, B., Cerniglia, G. J., Ahmed, M. S., Hahn, S. M., & Maity, A. M. (2007) · Neoplasia · doi:10.1593/neo.07124 · Cited by 126

β-Cell Dysfunctional ERAD/Ubiquitin/Proteasome System in Type 2 Diabetes Mediated by Islet Amyloid Polypeptide–Induced UCH-L1 Deficiency

Costes, S., Huang, C.-J., Gurlo, T., Daval, M., Matveyenko, A. V., Rizza, R. A., Butler, A. E., & Butler, P. C. (2010) · Diabetes · doi:10.2337/db10-0522 · Cited by 126

Autophagy in tumorigenesis and cancer therapy: Dr. Jekyll or Mr. Hyde?

Zhou, S., Zhao, L., Kuang, M., Zhang, B., Liang, Z., Yi, T., Wei, Y., & Zhao, X. (2012) · Cancer Letters · doi:10.1016/j.canlet.2012.02.017 · Cited by 125

Mechanistic Studies of a Peptidic GRP78 Ligand for Cancer Cell-Specific Drug Delivery

Liu, Y. M., Steiniger, S. C. J., Kim, Y. S., Kaufmann, G. F., Felding‐Habermann, B., & Janda, K. D. (2007) · Molecular Pharmaceutics · doi:10.1021/mp060122j · Cited by 124

Progress in the unraveling of the endoplasmic reticulum stress/autophagy pathway and cancer: Implications for future therapeutic approaches

Schleicher, S. M., Moretti, L., Varki, V., & Lu, J. (2010) · Drug Resistance Updates · doi:10.1016/j.drup.2010.04.002 · Cited by 121

Transmembrane bZIP Transcription Factors in ER Stress Signaling and the Unfolded Protein Response

Bailey, D., & O’Hare, P. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1796 · Cited by 119

Baicalein protects HT22 murine hippocampal neuronal cells against endoplasmic reticulum stress-induced apoptosis through inhibition of reactive oxygen species production and CHOP induction

Choi, J. H., Choi, A. Y., Yoon, H., Choe, W., Yoon, K., Ha, J., Yeo, E., & Kang, I. (2010) · Experimental & Molecular Medicine · doi:10.3858/emm.2010.42.12.084 · Cited by 119

Selective Abrogation of BiP/GRP78 Blunts Activation of NF-κB through the ATF6 Branch of the UPR: Involvement of C/EBPβ and mTOR-Dependent Dephosphorylation of Akt

Nakajima, S., Hiramatsu, N., Hayakawa, K., Saito, Y., Kato, H., Huang, T., Yao, J. Q., Paton, A. W., Paton, J. C., & Kitamura, M. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.00939-10 · Cited by 119

Phase II trial of irinotecan plus celecoxib in adults with recurrent malignant glioma

Reardon, D. A., Quinn, J. A., Vredenburgh, J. J., Rich, J. N., Gururangan, S., Badruddoja, M., Herndon, J. E., Dowell, J. M., Friedman, A. H., & Friedman, H. S. (2004) · Cancer · doi:10.1002/cncr.20776 · Cited by 117

Free fatty acids stimulate autophagy in pancreatic β-cells via JNK pathway

Komiya, K., Uchida, T., Ueno, T., Koike, M., Abe, H., Hirose, T., Kawamori, R., Uchiyama, Y., Kominami, E., Fujitani, Y., et al. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.09.101 · Cited by 117

Endoplasmic reticulum stress and autophagy as targets for cancer therapy

Schönthal, A. H. (2008) · Cancer Letters · doi:10.1016/j.canlet.2008.07.005 · Cited by 116

Celecoxib upregulates endoplasmic reticulum chaperones that inhibit celecoxib-induced apoptosis in human gastric cells

Tsutsumi, S., Namba, T., Tanaka, K.-I., Arai, Y., Ishihara, T., Aburaya, M., Mima, S., Hoshino, T., & Mizushima, T. (2005) · Oncogene · doi:10.1038/sj.onc.1209139 · Cited by 114

Tauroursodeoxycholate (TUDCA), chemical chaperone, enhances function of islets by reducing ER stress

Lee, Y. Y., Hong, S. H., Lee, Y. J., Chung, S. S., Jung, H. S., Park, S. G., & Park, K. S. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.06.022 · Cited by 113

Protracted lithium treatment protects against the ER stress elicited by thapsigargin in rat PC12 cells: roles of intracellular calcium, GRP78 and Bcl-2

Hiroi, T., Wei, H., Hough, C. J., Leeds, P. R., & Chuang, D. M. (2005) · The Pharmacogenomics Journal · doi:10.1038/sj.tpj.6500296 · Cited by 105

The critical role of JNK in the ER‐mitochondrial crosstalk during apoptotic cell death

Verma, G., & Datta, M. (2011) · Journal of Cellular Physiology · doi:10.1002/jcp.22903 · Cited by 105

Stress-sensing mechanisms in the unfolded protein response: similarities and differences between yeast and mammals

Kohno, K. (2009) · The Journal of Biochemistry · doi:10.1093/jb/mvp196 · Cited by 105

Direct non-cyclooxygenase-2 targets of celecoxib and their potential relevance for cancer therapy

Schönthal, A. H. (2007) · British Journal of Cancer · doi:10.1038/sj.bjc.6604049 · Cited by 104

Unfolded Protein Response Is Required in nu/nu Mice Microvasculature for Treating Breast Tumor with Tunicamycin

Banerjee, A., Lang, J.-Y., Hung, M., Sengupta, K., Banerjee, S. K., Baksi, K., & Banerjee, D. K. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.169771 · Cited by 103

Sensing Endoplasmic Reticulum Stress

Parmar, V. M., & Schröder, M. (2012) · Advances in experimental medicine and biology · doi:10.1007/978-1-4614-1680-7_10 · Cited by 103

Targeting endoplasmic reticulum protein transport: a novel strategy to kill malignant B cells and overcome fludarabine resistance in CLL

Carew, J. S., Nawrocki, S. T., Krupnik, Y. V., Dunner, K., McConkey, D. J., Keating, M. J., & Huang, P. (2005) · Blood · doi:10.1182/blood-2005-05-1923 · Cited by 102

Non-COX-2 targets and cancer: Expanding the molecular target repertoire of chemoprevention

Kashfi, K., & Rigas, B. (2005) · Biochemical Pharmacology · doi:10.1016/j.bcp.2005.05.004 · Cited by 102

Geldanamycin, an hsp90/GRP94-binding drug, induces increased transcription of endoplasmic reticulum (ER) chaperones via the ER stress pathway

Lawson, B., Brewer, J. W., & Hendershot, L. M. (1998) · Journal of Cellular Physiology · doi:10.1002/(sici)1097-4652(199802)174:2<170::aid-jcp4>3.0.co;2-l · Cited by 101

Endoplasmic Reticulum Stress and the Unfolded Protein Response in Nonalcoholic Fatty Liver Disease

Gentile, C. L., Frye, M. A., & Pagliassotti, M. J. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3790 · Cited by 101

Valproate protects the retina from endoplasmic reticulum stress-induced apoptosis after ischemia–reperfusion injury

Zhang, Z., Tong, N., Gong, Y., Qiu, Q., Yin, L., Lv, X.-H., & Wu, X. (2011) · Neuroscience Letters · doi:10.1016/j.neulet.2011.09.003 · Cited by 100

Blockade of GRP78 sensitizes breast cancer cells to microtubules‐interfering agents that induce the unfolded protein response

Wang, J., Yin, Y., Hua, H., Li, M., Luo, T. L., Xu, L., Wang, R., Liu, D., Zhang, Y., & Jiang, Y. (2009) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2009.00873.x · Cited by 100

Pathogen–endoplasmic-reticulum interactions: in through the out door

Roy, C. R., Salcedo, S. P., & Gorvel, J. (2006) · Nature reviews. Immunology · doi:10.1038/nri1775 · Cited by 98

A Trojan Horse in Drug Development: Targeting of Thapsigargins Towards Prostate Cancer Cells

Christensen, S. B., Skytte, D. M., Denmeade, S. R., Dionne, C. A., MØLLER, J. V., Nissen, P., & Isaacs, J. T. (2009) · Anti-Cancer Agents in Medicinal Chemistry · doi:10.2174/1871520610909030276 · Cited by 97

Highly conserved glucose-regulated protein in hamster and chicken cells: preliminary characterization of its cDNA clone.

Lee, A. S., Delegeane, A. M., & Scharff, D. J. (1981) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.78.8.4922 · Cited by 96

(−)-Epigallocatechin-3-gallate Inhibits Hsp90 Function by Impairing Hsp90 Association with Cochaperones in Pancreatic Cancer Cell Line Mia Paca-2

Li, Y., Zhang, T., Jiang, Y., Lee, H.-F., Schwartz, S. J., & Sun, D. (2009) · Molecular Pharmaceutics · doi:10.1021/mp900037p · Cited by 94

Geldanamycin and its derivatives as Hsp90 inhibitors

Górska‐Ponikowska, M. (2012) · Frontiers in bioscience · doi:10.2741/4050 · Cited by 93

Critical Roles of Hydrophobicity and Orientation of Side Chains for Inactivation of Sarcoplasmic Reticulum Ca2+-ATPase with Thapsigargin and Thapsigargin Analogs

Winther, A.-M. L., Liu, H., Sonntag, Y., Olesen, C., le Maire, M., Søhoel, H., Olsen, C. E., Christensen, S. B., Nissen, P., & MØLLER, J. V. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.136242 · Cited by 92

Redox Control of Endoplasmic Reticulum Function

Csala, M., Margittai, É., & Bánhegyi, G. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2529 · Cited by 90

Effect of an Inducer of BiP, a Molecular Chaperone, on Endoplasmic Reticulum (ER) Stress-Induced Retinal Cell Death

Inokuchi, Y., Nakajima, Y., Shimazawa, M., et al. (2009) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.08-2123 · Cited by 90

BiP Binding Keeps ATF6 at Bay

Sommer, T., & Jarosch, E. (2002) · Developmental Cell · doi:10.1016/s1534-5807(02)00210-1 · Cited by 90

Downregulation of survivin expression and concomitant induction of apoptosis by celecoxib and its non-cyclooxygenase-2-inhibitory analog, dimethyl-celecoxib (DMC), in tumor cells in vitro and in vivo

Pyrko, P., Soriano, N., Kardosh, A., Liu, Y., Uddin, J., Petasis, N. A., Hofman, F. M., Chen, C., Chen, T. C., & Schönthal, A. H. (2006) · Molecular Cancer · doi:10.1186/1476-4598-5-19 · Cited by 90

Histone H3 and heat shock protein GRP78 are selectively cross-linked to DNA by photoactivated gilvocarcin V in human fibroblasts.

Matsumoto, A., & Hanawalt, P. C. (2000) · PubMed · Cited by 90

Inhibition of Endoplasmic Reticulum Stress Improves Mouse Embryo Development

Zhang, J. Y., Diao, Y. F., Kim, H. R., & Jin, D. I. (2012) · PLoS ONE · doi:10.1371/journal.pone.0040433 · Cited by 88

Regulation of ER stress proteins by valproate: therapeutic implications

Bown, C. D., Wang, J., Chen, B., & Young, L. T. (2002) · Bipolar Disorders · doi:10.1034/j.1399-5618.2002.t01-1-40201.x · Cited by 86

AAV-mediated delivery of the transcription factor XBP1s into the striatum reduces mutant Huntingtin aggregation in a mouse model of Huntington’s disease

Zuleta, A., Vidal, R. L., Armentano, D., Parsons, G., & Hetz, C. A. (2012) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2012.03.033 · Cited by 86

Ligation of cell surface GRP78 with antibody directed against the COOH-terminal domain of GRP78 suppresses Ras/MAPK and PI 3-kinase/AKT signaling while promoting caspase activation in human prostate cancer cells

Misra, U. K., & Pizzo, S. V. (2010) · Cancer Biology & Therapy · doi:10.4161/cbt.9.2.10422 · Cited by 86

A Phase I Clinical Trial of Thoracic Radiotherapy and Concurrent Celecoxib for Patients with Unfavorable Performance Status Inoperable/Unresectable Non–Small Cell Lung Cancer

Liao, Z. X., Komaki, R. U., Milas, L., Yuan, C., Kies, M. S., Chang, J. Y., Jeter, M. D., Guerrero, T. M., Blumenschien, G., Smith, C. M., et al. (2005) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-04-1741 · Cited by 86

OSU-03012 Promotes Caspase-Independent but PERK-, Cathepsin B-, BID-, and AIF-Dependent Killing of Transformed Cells

Yacoub, A., Park, M. A., Hanna, D. E., Hong, Y. K., Mitchell, C., Pandya, A. P., Harada, H., Powis, G., Chen, C., Koumenis, C., et al. (2006) · Molecular Pharmacology · doi:10.1124/mol.106.025007 · Cited by 85

Mood stabilizing drug lithium increases expression of endoplasmic reticulum stress proteins in primary cultured rat cerebral cortical cells

Shao, L., Sun, X., Xu, L., Young, L. T., & Wang, J. (2005) · Life Sciences · doi:10.1016/j.lfs.2005.07.007 · Cited by 85

The HIV Protease Inhibitors Nelfinavir and Saquinavir, but Not a Variety of HIV Reverse Transcriptase Inhibitors, Adversely Affect Human Proteasome Function

Piccinini, M., RINAUDO, M. T., Anselmino, A., Buccinnà, B., Ramondetti, C., Dematteis, A., Ricotti, E., Palmisano, L., Mostert, M., & Tovo, P. (2005) · Antiviral Therapy · doi:10.1177/135965350501000203 · Cited by 84

Transcriptional Regulation of the Grp78 Promoter by Endoplasmic Reticulum Stress

Hong, M. Y., Lin, M.-Y., Huang, J.-M., Baumeister, P., Hakre, S., Roy, A. L., & Lee, A. S. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413753200 · Cited by 84

Free cholesterol overloading induced smooth muscle cells death and activated both ER- and mitochondrial-dependent death pathway

Ke-di, X. U., Ming, Y., Yongping, W., Yi, Y., & Xiao-xiang, Z. (2009) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2009.04.019 · Cited by 84

Dimethyl-Celecoxib (DMC), a derivative of celecoxib that lacks cyclooxygenase-2-Inhibitory function, potently mimics the anti-tumor effects of celecoxib on burkitt’s lymphoma in vitro and in vivo

Kardosh, A., Wang, W., Uddin, J., Petasis, N. A., Hofman, F. M., Chen, T. C., & Schönthal, A. H. (2005) · Cancer Biology & Therapy · doi:10.4161/cbt.4.5.1699 · Cited by 83

Reduction of GRP78 expression with siRNA activates unfolded protein response leading to apoptosis in HeLa cells

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Misfolded proinsulin accumulates in expanded pre‐Golgi intermediates and endoplasmic reticulum subdomains in pancreatic beta cells of Akita mice

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HIV Protease Inhibitor Nelfinavir Inhibits Growth of Human Melanoma Cells by Induction of Cell Cycle Arrest

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A chemical chaperone 4-PBA ameliorates palmitate-induced inhibition of glucose-stimulated insulin secretion (GSIS)

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2-Deoxy d -Glucose Prevents Cell Surface Expression of NKG2D Ligands through Inhibition of N-Linked Glycosylation

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Pyrvinium Targets the Unfolded Protein Response to Hypoglycemia and Its Anti-Tumor Activity Is Enhanced by Combination Therapy

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Targeted disruption of the Chop gene delays endoplasmic reticulum stress–mediated diabetes

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COX-2 inhibition is neither necessary nor sufficient for celecoxib to suppress tumor cell proliferation and focus formation in vitro

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A novel celecoxib derivative, OSU03012, induces cytotoxicity in primary CLL cells and transformed B-cell lymphoma cell line via a caspase- and Bcl-2–independent mechanism

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Involvement of Gadd153 in the pathogenic action of presenilin‐1 mutations

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Endoplasmic Reticulum Stress-Mediated Apoptosis of EBV-Transformed B Cells by Cross-Linking of CD70 Is Dependent upon Generation of Reactive Oxygen Species and Activation of p38 MAPK and JNK Pathway

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Protein Disulfide Isomerase Regulates Endoplasmic Reticulum Stress and the Apoptotic Process during Prion Infection and PrP Mutant-Induced Cytotoxicity

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A murine monoclonal antibody directed against the carboxyl-terminal domain of GRP78 suppresses melanoma growth in mice

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Preferential killing of triple-negative breast cancer cells in vitro and in vivo when pharmacological aggravators of endoplasmic reticulum stress are combined with autophagy inhibitors

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The role of autophagy in endoplasmic reticulum stress-induced pancreatic β cell death

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PLAB induction in fenretinide-induced apoptosis of ovarian cancer cells occurs via a ROS-dependent mechanism involving ER stress and JNK activation

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Dual neuroprotective pathways of a pro‐electrophilic compound via HSF‐1‐activated heat‐shock proteins and Nrf2‐activated phase 2 antioxidant response enzymes

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Nelfinavir induces the unfolded protein response in ovarian cancer cells, resulting in ER vacuolization, cell cycle retardation and apoptosis

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Modulation of CCAAT/Enhancer Binding Protein Homologous Protein (CHOP)-dependent DR5 Expression by Nelfinavir Sensitizes Glioblastoma Multiforme Cells to Tumor Necrosis Factor-related Apoptosis-inducing Ligand (TRAIL)

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Multitarget inhibition of drug-resistant multiple myeloma cell lines by dimethyl-celecoxib (DMC), a non–COX-2 inhibitory analog of celecoxib

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Glucose-regulated protein 78 as a novel effector of BRCA1 for inhibiting stress-induced apoptosis

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Enhanced killing of chemo-resistant breast cancer cells via controlled aggravation of ER stress

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SCAMP5 Links Endoplasmic Reticulum Stress to the Accumulation of Expanded Polyglutamine Protein Aggregates via Endocytosis Inhibition

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Genistein demethylates the promoter of CHD5 and inhibits neuroblastoma growth in vivo

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Chaperone-Targeting Cytotoxin and Endoplasmic Reticulum Stress-Inducing Drug Synergize to Kill Cancer Cells

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OSU-03012 suppresses GRP78/BiP expression that causes PERK-dependent increases in tumor cell killing

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Hepatitis C virus NS2 protein triggers endoplasmic reticulum stress and suppresses its own viral replication

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CCAAT/Enhancer Binding Protein Homologous Protein-Dependent Death Receptor 5 Induction and Ubiquitin/Proteasome-Mediated Cellular FLICE-Inhibitory Protein Down-Regulation Contribute to Enhancement of Tumor Necrosis Factor-Related Apoptosis-Inducing Ligand-Induced Apoptosis by Dimethyl-Celecoxib in Human Non–Small-Cell Lung Cancer Cells

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Combination Therapy With Gefitinib and Rofecoxib in Patients With Platinum-Pretreated Relapsed Non–Small-Cell Lung Cancer

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Tamoxifen enhances the cytotoxic effects of nelfinavir in breast cancer cells

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Redox-Dependent Protein Quality Control in the Endoplasmic Reticulum: Folding to Degradation

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Impaired ATF6α processing, decreased Rheb and neuronal cell cycle re-entry in Huntington's disease

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Effects of the Natural Isoflavonoid Genistein on Growth, Signaling Pathways and Gene Expression of Matrix Macromolecules by Breast Cancer Cells

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Selective Cytotoxic Activity of Valinomycin against HT-29 Human Colon Carcinoma Cells via Down-Regulation of GRP78

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Etoposide‐resistant HT‐29 human colon carcinoma cells during glucose deprivation are sensitive to piericidin A, a GRP78 down‐regulator

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The Cyclooxygenase-2 Inhibitor Celecoxib Is a Potent Inhibitor of Human Carbonic Anhydrase II

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Nerve growth factor attenuates 2-deoxy-d-glucose-triggered endoplasmic reticulum stress-mediated apoptosis via enhanced expression of GRP78

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Initial Experience Combining Cyclooxygenase-2 Inhibition with Chemoradiation for Locally Advanced Pancreatic Cancer

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Autoantibodies against cell surface GRP78 promote tumor growth in a murine model of melanoma

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Phase I/II study of selective cyclooxygenase-2 inhibitor celecoxib as a radiation sensitizer in patients with unresectable brain metastases

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Efrapeptin J, a New Down-regulator of the Molecular Chaperone GRP78 from a Marine Tolypocladium sp.

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Arctigenin Suppresses Unfolded Protein Response and Sensitizes Glucose Deprivation-Mediated Cytotoxicity of Cancer Cells

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Amelioration of Glucolipotoxicity-Induced Endoplasmic Reticulum Stress by a “Chemical Chaperone” in Human THP-1 Monocytes

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Identification of ERdj3 and OBF-1/BOB-1/OCA-B as Direct Targets of XBP-1 during Plasma Cell Differentiation

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The Apoptosis Inhibitor ARC Alleviates the ER Stress Response to Promote β-Cell Survival

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A novel inhibitor of advanced glycation and endoplasmic reticulum stress reduces infarct volume in rat focal cerebral ischemia

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Identification of Subtilase Cytotoxin (SubAB) Receptors Whose Signaling, in Association with SubAB-Induced BiP Cleavage, Is Responsible for Apoptosis in HeLa Cells

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Cyclooxygenase-2 independent effects of cyclooxygenase-2 inhibitors on oxidative stress and intracellular glutathione content in normal and malignant human B-cells

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The Escherichia coli Subtilase Cytotoxin A Subunit Specifically Cleaves Cell-surface GRP78 Protein and Abolishes COOH-terminal-dependent Signaling

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Fluvoxamine Attenuated Endoplasmic Reticulum Stress-Induced Leptin Resistance

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A Correction to the Research Article Titled: “Engineering a Prostate-Specific Membrane Antigen–Activated Tumor Endothelial Cell Prodrug for Cancer Therapy” by S. R. Denmeade, A. M. Mhaka, D. Marc Rosen, W. N. Brennen, S. Dalrymple, I. Dach, C. Olesen, B. Gurel, A. M. De Marzo, G. Wilding, M. A. Carducci, C. A. Dionne, J. V. Møller, P. Nissen, S. B. Christensen, J. T. Isaacs

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