ER stress and diseases

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

Endoplasmic Reticulum Stress Links Obesity, Insulin Action, and Type 2 Diabetes

Özcan, U., Cao, Q., Yilmaz, E., Lee, A.-H., Iwakoshi, N. N., Özdelen, E., Tuncman, G., Görgün, C., Glimcher, L. H., & Hotamisligil, G. S. (2004) · Science · doi:10.1126/science.1103160 · Cited by 3,844 · see citing works

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

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

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

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

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

Harding, H. P., Novoa, I., Zhang, Y., Zeng, H., Wek, R. C., Schapira, M., & Ron, D. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)00108-8 · Cited by 3,281 · see citing works

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 3,262 · see citing works

Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1.

Urano, F., Wang, X.-Z., Bertolotti, A., Zhang, Y.-H., Chung, P., Harding, H., & Ron, D. (2000) · Science · doi:10.1126/science.287.5453.664 · Cited by 3,081 · see citing works

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

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

Roles of CHOP/GADD153 in endoplasmic reticulum stress

Oyadomari, S., & Mori, M. (2003) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401373 · Cited by 2,833 · 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

Impairment of the Ubiquitin-Proteasome System by Protein Aggregation

Bence, N., Sampat, R. M., & Kopito, R. R. (2001) · Science · doi:10.1126/science.292.5521.1552 · Cited by 2,192 · 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

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

Lee, A., Iwakoshi, N. N., & Glimcher, L. H. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.21.7448-7459.2003 · Cited by 2,041 · see citing works

Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase

Shimura, H., Hattori, N., Kubo, S.-I., Mizuno, Y., Asakawa, S., Minoshima, S., Shimizu, N., Iwai, K., Chiba, T., Tanaka, K., et al. (2000) · Nature Genetics · doi:10.1038/77060 · Cited by 2,024 · see citing works

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

Marciniak, S. J., Yun, C. Y., Oyadomari, S., Novoa, I., Zhang, Y., Jungreis, R., Nagata, K., Harding, H. P., & Ron, D. (2004) · Genes & Development · doi:10.1101/gad.1250704 · Cited by 2,004 · see citing works

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

Zinszner, H., Kuroda, M., Wang, X., Batchvarova, N., Lightfoot, R. T., Remotti, H. E., Stevens, J. L., & Ron, D. (1998) · Genes & Development · doi:10.1101/gad.12.7.982 · Cited by 1,996 · see citing works

Aggresomes, inclusion bodies and protein aggregation

Kopito, R. R. (2000) · Trends in Cell Biology · doi:10.1016/s0962-8924(00)01852-3 · Cited by 1,906 · see citing works

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

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

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

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

ER stress and the unfolded protein response

Schröder, M., & Kaufman, R. J. (2004) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2004.06.056 · Cited by 1,750 · see citing works

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

Shen, J., Chen, X., Hendershot, L. M., & Prywes, R. (2002) · Developmental Cell · doi:10.1016/s1534-5807(02)00203-4 · Cited by 1,461 · see citing works

Organelle-specific initiation of cell death pathways

Ferri, K. F., & Kroemer, G. (2001) · Nature Cell Biology · doi:10.1038/ncb1101-e255 · Cited by 1,455 · see citing works

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. L., Kaufman, R. J., Ma, D., Coen, D. M., Ron, D., et al. (2005) · Science · doi:10.1126/science.1101902 · Cited by 1,403 · see citing works

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

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

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. Y., Sorcinelli, M. D., Pozzan, T., & Korsmeyer, S. J. (2003) · Science · doi:10.1126/science.1081208 · Cited by 1,387 · 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

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

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

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

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 1,331 · see citing works

Nrf2 Is a Direct PERK Substrate and Effector of PERK-Dependent Cell Survival

Cullinan, S. B., Zhang, D. D., Hannink, M., Arvisais, E. W., Kaufman, R. J., & Diehl, J. A. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.20.7198-7209.2003 · Cited by 1,233 · see citing works

Identification of the cis-Acting Endoplasmic Reticulum Stress Response Element Responsible for Transcriptional Induction of Mammalian Glucose-regulated Proteins

Yoshida, H., Haze, K., Yanagi, H., Yura, T., & Mori, K. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.50.33741 · Cited by 1,229 · see citing works

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

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

Coupling endoplasmic reticulum stress to the cell death program

Rao, R. V., Ellerby, H. M., & Bredesen, D. E. (2004) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401378 · Cited by 1,208 · see citing works

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 1,164 · see citing works

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.Preprint

Ron, D., & Habener, J. F. (1992) · Genes & Development · doi:10.1101/gad.6.3.439 · Cited by 1,156 · see citing works

The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol

Ye, Y., Meyer, H. H., & Rapoport, T. A. (2001) · Nature · doi:10.1038/414652a · Cited by 1,099 · see citing works

An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of parkin

Imai, Y., Soda, M., Inoue, H., Hattori, N., Mizuno, Y., & Takahashi, R. (2001) · Cell · doi:10.1016/s0092-8674(01)00407-x · Cited by 1,050 · see citing works

TRB3, a novel ER stress‐inducible gene, is induced via ATF4–CHOP pathway and is involved in cell death

Ohoka, N., Yoshii, S., Hattori, T., Onozaki, K., & Hayashi, H. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600596 · Cited by 1,004 · see citing works

A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol

Ye, Y., Shibata, Y., Yun, C., Ron, D., & Rapoport, T. A. (2004) · Nature · doi:10.1038/nature02656 · Cited by 963 · see citing works

ATF6 Activated by Proteolysis Binds in the Presence of NF-Y (CBF) Directly to the <i>cis</i> -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 · see citing works

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

Tirasophon, W., Welihinda, A. A., & Kaufman, R. J. (1998) · Genes & Development · doi:10.1101/gad.12.12.1812 · Cited by 921 · see citing works

Tripartite Management of Unfolded Proteins in the Endoplasmic Reticulum

Mori, K. (2000) · Cell · doi:10.1016/s0092-8674(00)80855-7 · Cited by 918 · see citing works

Transcriptional and Translational Control in the Mammalian Unfolded Protein Response

Harding, H. P., Calfon, M. A., Urano, F., Novoa, I., & Ron, D. (2002) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.18.011402.160624 · Cited by 918 · see citing works

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 · see citing works

The endoplasmic reticulum is the site of cholesterol-induced cytotoxicity in macrophages

Feng, B., Yao, P. M., Li, Y., Devlin, C. M., Zhang, D., Harding, H. P., Sweeney, M., Rong, J. X., Kuriakose, G., Fisher, E. A. A., et al. (2003) · Nature Cell Biology · doi:10.1038/ncb1035 · Cited by 886 · see citing works

ER stress and neurodegenerative diseases

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

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 866 · see citing works

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 858 · see citing works

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

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

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., Bandô, Y., Imaizumi, K., et al. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200310015 · Cited by 831 · see citing works

CHOP Is Involved in Endoplasmic Reticulum Stress-induced Apoptosis by Enhancing DR5 Expression in Human Carcinoma Cells

Yamaguchi, H., & Wang, H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406933200 · Cited by 825 · see citing works

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

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

BH3-only proteins that bind pro-survival Bcl-2 family members fail to induce apoptosis in the absence of Bax and BakPreprint

Zong, W., Lindsten, T., Ross, A. J., MacGregor, G. R., & Thompson, C. B. (2001) · Genes & Development · doi:10.1101/gad.897601 · Cited by 809 · see citing works

Cloning of mammalian Ire1 reveals diversity in the ER stress responses

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

The UCH-L1 Gene Encodes Two Opposing Enzymatic Activities that Affect α-Synuclein Degradation and Parkinson's Disease Susceptibility

Liu, Y., Fallon, L., Lashuel, H. A., Liu, Z., & Lansbury, P. T. (2002) · Cell · doi:10.1016/s0092-8674(02)01012-7 · Cited by 786 · see citing works

Intracellular signaling from the endoplasmic reticulum to the nucleus: the unfolded protein response in yeast and mammals

Patil, C., & Walter, P. (2001) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(00)00219-2 · Cited by 779 · see citing works

Autocrine Tumor Necrosis Factor Alpha Links Endoplasmic Reticulum Stress to the Membrane Death Receptor Pathway through IRE1α-Mediated NF-κB Activation and Down-Regulation of TRAF2 Expression

Hu, P., Han, Z., Couvillon, A., Kaufman, R., & Exton, J. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.8.3071-3084.2006 · Cited by 777 · see citing works

Parkin Suppresses Unfolded Protein Stress-induced Cell Death through Its E3 Ubiquitin-protein Ligase Activity

Imai, Y., Soda, M., & Takahashi, R. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.c000447200 · Cited by 766 · see citing works

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 · see citing works

Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1

Cummings, C. J., Mancini, M. A., Antalffy, B. A., DeFranco, D. B., Orr, H. T., & Zoghbi, H. Y. (1998) · Nature Genetics · doi:10.1038/502 · Cited by 744 · see citing works

Regulation of apoptosis by endoplasmic reticulum pathways

Breckenridge, D. G., Germain, M., Mathai, J. P., Nguyen, M., & Shore, G. C. (2003) · Oncogene · doi:10.1038/sj.onc.1207108 · Cited by 742 · see citing works

Distinct Ubiquitin-Ligase Complexes Define Convergent Pathways for the Degradation of ER Proteins

Carvalho, P., Goder, V., & Rapoport, T. A. (2006) · Cell · doi:10.1016/j.cell.2006.05.043 · Cited by 726 · see citing works

Homocysteine-induced endoplasmic reticulum stress causes dysregulation of the cholesterol and triglyceride biosynthetic pathways

Werstuck, G. H., Lentz, S. R., Dayal, S., Hossain, G. S., Sood, S. K., Shi, Y., Zhou, J., Maeda, N., Krisans, S. K., Malinow, M. R., et al. (2001) · Journal of Clinical Investigation · doi:10.1172/jci11596 · Cited by 702 · see citing works

Endoplasmic Reticulum Chaperone Protein GRP78 Protects Cells from Apoptosis Induced by Topoisomerase Inhibitors

Reddy, R. K., Mao, C., Baumeister, P., Austin, R. C., Kaufman, R. J., & Lee, A. S. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212328200 · Cited by 695 · see citing works

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

Ma, Y., Brewer, J. W., Diehl, J. A., & Hendershot, L. M. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00234-6 · Cited by 689 · see citing works

A Time-Dependent Phase Shift in the Mammalian Unfolded Protein Response

Yoshida, H., Matsui, T., Hosokawa, N., Kaufman, R. J., Nagata, K., & Mori, K. (2003) · Developmental Cell · doi:10.1016/s1534-5807(03)00022-4 · Cited by 675 · see citing works

Hsp70 and Hsp40 chaperones can inhibit self-assembly of polyglutamine proteins into amyloid-like fibrils

Muchowski, P. J., Schaffar, G., Sittler, A., Wanker, E. E., Hayer-Hartl, M. K., & Hartl, F. U. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.140202897 · Cited by 668 · see citing works

XBP1

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

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. C., Li, S., Frank, A. T., Zambito, F., Reinert, J., GANNON, M. A., Ma, K., McNaughton, K., & Cavener, D. R. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.11.3864-3874.2002 · Cited by 604 · see citing works

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 · see citing works

Function of the p97–Ufd1–Npl4 complex in retrotranslocation from the ER to the cytosol

Ye, Y., Meyer, H. H., & Rapoport, T. A. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200302169 · Cited by 598 · see citing works

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

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

On the mechanism of sensing unfolded protein in the endoplasmic reticulum

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

The unfolded protein response

Zhang, K., & Kaufman, R. J. (2006) · Neurology · doi:10.1212/01.wnl.0000192306.98198.ec · Cited by 580 · see citing works

Endoplasmic Reticulum Stress and the Unfolded Protein Response in Cellular Models of Parkinson's Disease

Ryu, E. J., Harding, H. P., Angelastro, J. M., Vitolo, O. V., Ron, D., & Greene, L. A. (2002) · The Journal of Neuroscience · doi:10.1523/jneurosci.22-24-10690.2002 · Cited by 572 · see citing works

Coupling Endoplasmic Reticulum Stress to the Cell Death Program

Rao, R. V., Hermel, E., Castro‐Obregón, S., del Rio, G., Ellerby, L., Ellerby, H. M., & Bredesen, D. E. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102225200 · Cited by 570 · see citing works

Role of 26S proteasome and HRD genes in the degradation of 3-hydroxy-3-methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein.

Hampton, R. Y., Gardner, R. G., & Rine, J. (1996) · Molecular Biology of the Cell · doi:10.1091/mbc.7.12.2029 · Cited by 569 · see citing works

TUNICAMYCIN, A NEW ANTIBIOTIC. I

Takatsuki, A., Arima, Κ., & Tamura, G. (1971) · The Journal of Antibiotics · doi:10.7164/antibiotics.24.215 · Cited by 558 · see citing works

The unfolded protein response is activated in Alzheimer’s disease

Hoozemans, J. J. M., Veerhuis, R., van Haastert, E. S., Rozemüller, A. J. M., Baas, F., Eikelenboom, P., & Scheper, W. (2005) · Acta Neuropathologica · doi:10.1007/s00401-005-1038-0 · Cited by 549 · see citing works

AAA-ATPase p97/Cdc48p, a Cytosolic Chaperone Required for Endoplasmic Reticulum-Associated Protein Degradation

Rabinovich, E., Kerem, A., Fröhlich, K., Diamant, N., & Bar‐Nun, S. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.2.626-634.2002 · Cited by 546 · see citing works

Betaine decreases hyperhomocysteinemia, endoplasmic reticulum stress, and liver injury in alcohol-fed mice

Ji, C., & Kaplowitz, N. (2003) · Gastroenterology · doi:10.1016/s0016-5085(03)00276-2 · Cited by 539 · see citing works

Transcriptional abnormalities in Huntington disease

Sugars, K. L., & Rubinsztein, D. C. (2003) · Trends in Genetics · doi:10.1016/s0168-9525(03)00074-x · Cited by 529 · see citing works

A Series of Ubiquitin Binding Factors Connects CDC48/p97 to Substrate Multiubiquitylation and Proteasomal Targeting

Richly, H., Rapé, M., Braun, S. J., Rumpf, S., Hoege, C., & Jentsch, S. (2005) · Cell · doi:10.1016/j.cell.2004.11.013 · Cited by 523 · 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

Presenilin-1 mutations downregulate the signalling pathway of the unfolded-protein response

Katayama, T., Imaizumi, K., Sato, N., Miyoshi, K., Kudo, T., Hitomi, J., Morihara, T., Yoneda, T., Gomi, F., Mori, Y., et al. (1999) · Nature Cell Biology · doi:10.1038/70265 · Cited by 521 · see citing works

Activation of the atf6, xbp1 and grp78 genes in human hepatocellular carcinoma: A possible involvement of the er stress pathway in hepatocarcinogenesis

Shuda, M., Kondoh, N., Imazeki, N., Tanaka, K., Okada, T., Mori, K., Hada, A., Arai, M., Wakatsuki, T., Matsubara, O., et al. (2003) · Journal of Hepatology · doi:10.1016/s0168-8278(03)00029-1 · Cited by 520 · see citing works

Endoplasmic reticulum stress-mediated apoptosis in pancreatic β-cells

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

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