Protein Folding in the Endoplasmic Reticulum and the Unfolded Protein Response

Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism

Kitada, T., Asakawa, S., Hattori, N., Matsumine, H., Yamamura, Y., Minoshima, S., Yokochi, M., Mizuno, Y., & Shimizu, N. (1998) · Nature · doi:10.1038/33416 · Cited by 5,227 · see citing works

Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease

Goate, A., Chartier-Harlin, M.-C., Mullan, M., Brown, J., Crawford, F., Fidani, L., Giuffra, L., Haynes, A., Irving, N., James, L., et al. (1991) · Nature · doi:10.1038/349704a0 · Cited by 4,659 · see citing works

Protein folding in the cell

Gething, M.-J. H., & Sambrook, J. (1992) · Nature · doi:10.1038/355033a0 · Cited by 4,137 · 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

Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease

Sherrington, R., Rogaev, E. I., Liang, Y., Rogaeva, E. A., Levesque, G., Ikeda, M., Chi, H., Lin, C., Li, G., Holman, K., et al. (1995) · Nature · doi:10.1038/375754a0 · Cited by 4,051 · 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

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

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

Stress signaling from the lumen of the endoplasmic reticulum: coordination of gene transcriptional and translational controlsPreprint

Kaufman, R. J. (1999) · Genes & Development · doi:10.1101/gad.13.10.1211 · Cited by 2,247 · 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

Familial Alzheimer's disease in kindreds with missense mutations in a gene on chromosome 1 related to the Alzheimer's disease type 3 gene

Rogaev, E. I., Sherrington, R., Rogaeva, E. A., Levesque, G., Ikeda, M., Liang, Y., Chi, H., Lin, C., Holman, K., Tsuda, T., et al. (1995) · Nature · doi:10.1038/376775a0 · Cited by 2,052 · 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

Perk is essential for translational regulation and cell survival during the unfolded protein response

Harding, H. P., Zhang, Y., Bertolotti, A., Zeng, H., & Ron, D. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)80330-5 · Cited by 2,021 · 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

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. M., Lockhart, D. J., Weissman, J. S., & Walter, P. (2000) · Cell · doi:10.1016/s0092-8674(00)80835-1 · Cited by 1,994 · 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 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

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

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 1,258 · see citing works

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

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

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

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

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

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

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

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

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

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

Orchestrating the unfolded protein response in health and disease

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

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

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 904 · 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

Stress-Induced Phosphorylation and Activation of the Transcription Factor CHOP (GADD153) by p38 MAP Kinase

Wang, X., & Ron, D. (1996) · Science · doi:10.1126/science.272.5266.1347 · Cited by 885 · see citing works

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

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

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

Immunoglobulin heavy chain binding protein

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

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

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

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

A Familial Alzheimer's Disease Locus on Chromosome 1

Levy‐Lahad, E., Wijsman, E. M., Nemens, E. J., Anderson, L., Goddard, K. A. B., Weber, J. L., Bird, T. D., & Schellenberg, G. D. (1995) · Science · doi:10.1126/science.7638621 · Cited by 811 · 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

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

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

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

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

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

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. J., Kreibich, G., Hendershot, L. M., & Ron, D. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.8.4273 · Cited by 669 · 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

Retro-translocation of proteins from the endoplasmic reticulum into the cytosol

Tsai, B., Ye, Y., & Rapoport, T. A. (2002) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm780 · Cited by 647 · see citing works

How N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum.

Helenius, A. (1994) · Molecular Biology of the Cell · doi:10.1091/mbc.5.3.253 · Cited by 624 · 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

Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48

Jarosch, E., Taxis, C., Volkwein, C., Bordallo, J., Finley, D. J., Wolf, D. H., & Sommer, T. (2002) · Nature Cell Biology · doi:10.1038/ncb746 · Cited by 532 · see citing works

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 · see citing works

Diverse functions of JNK signaling and c-Jun in stress response and apoptosis

Leppä, S., & Bohmann, D. (1999) · Oncogene · doi:10.1038/sj.onc.1203173 · 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

A regulatory link between ER-associated protein degradation and the unfolded-protein response

Friedlander, R., Jarosch, E., Urban, J., Volkwein, C., & Sommer, T. (2000) · Nature Cell Biology · doi:10.1038/35017001 · Cited by 474 · see citing works

CHIP Is Associated with Parkin, a Gene Responsible for Familial Parkinson's Disease, and Enhances Its Ubiquitin Ligase Activity

Imai, Y., Soda, M., Hatakeyama, S., Akagi, T., Hashikawa, T., Nakayama, K. I., & Takahashi, R. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00583-x · Cited by 473 · see citing works

Role of EDEM in the Release of Misfolded Glycoproteins from the Calnexin Cycle

Molinari, M., Calanca, V., Galli, C., Lucca, P., & Paganetti, P. (2003) · Science · doi:10.1126/science.1079474 · Cited by 470 · see citing works

A novel ER α‐mannosidase‐like protein accelerates ER‐associated degradation

Hosokawa, N., Wada, I., Hasegawa, K., Yorihuzi, T., Tremblay, L. O., Herscovics, A. A., & Nagata, K. (2001) · EMBO Reports · doi:10.1093/embo-reports/kve084 · Cited by 467 · see citing works

Hrd1p/Der3p is a membrane-anchored ubiquitin ligase required for ER-associated degradation

Bays, N. W., Gardner, R. G., Seelig, L. P., Joazeiro, C. A. P., & Hampton, R. Y. (2000) · Nature Cell Biology · doi:10.1038/35050524 · Cited by 465 · see citing works

Proteasome-dependent endoplasmic reticulum-associated protein degradation: An unconventional route to a familiar fate

Werner, E. D., Brodsky, J. L., & McCracken, A. A. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.24.13797 · Cited by 463 · see citing works

EDEM As an Acceptor of Terminally Misfolded Glycoproteins Released from Calnexin

Oda, Y., Hosokawa, N., Wada, I., & Nagata, K. (2003) · Science · doi:10.1126/science.1079181 · Cited by 453 · see citing works

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 445 · see citing works

Coordinated regulation of a set of genes by glucose and calcium ionophores in mammalian cells

Lee, A. S. (1987) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(87)90011-9 · Cited by 438 · see citing works

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 · see citing works

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. H., & Sambrook, J. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05323.x · Cited by 374 · see citing works

ATF6 as a Transcription Activator of the Endoplasmic Reticulum Stress Element: Thapsigargin Stress-Induced Changes and Synergistic Interactions with NF-Y and YY1

Li, M., Baumeister, P., Roy, B., Phan, T., Foti, D. M., Luo, S. D., & Lee, A. S. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.14.5096-5106.2000 · Cited by 368 · see citing works

The relationship of N-linked glycosylation and heavy chain-binding protein association with the secretion of glycoproteins.

Dorner, A. J., Bole, D. G., & Kaufman, R. J. (1987) · The Journal of Cell Biology · doi:10.1083/jcb.105.6.2665 · Cited by 365 · see citing works

Immunoglobulin Binding Protein (BiP) Function Is Required to Protect Cells from Endoplasmic Reticulum Stress but Is Not Required for the Secretion of Selective Proteins

Morris, J. A., Dorner, A. J., Edwards, C. A., Hendershot, L. M., & Kaufman, R. J. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.7.4327 · Cited by 352 · see citing works

Sequential Waves of Functionally Related Proteins Are Expressed When B Cells Prepare for Antibody Secretion

van Anken, E., Romijn, E. P., Maggioni, C., Mezghrani, A., Sitia, R., Braakman, I., & Heck, A. J. R. (2003) · Immunity · doi:10.1016/s1074-7613(03)00024-4 · Cited by 352 · see citing works

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. L., & Kaufman, R. J. (2005) · Journal of Clinical Investigation · doi:10.1172/jci21848 · Cited by 348 · see citing works

<b>Molecular mechanisms and regulation of insulin exocytosis as a paradigm of endocrine secretion</b>

Lang, J. (1999) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1999.00043.x · Cited by 347 · see citing works

Overexpression of GRP78 mitigates stress induction of glucose regulated proteins and blocks secretion of selective proteins in Chinese hamster ovary cells.

Dorner, A. J., Wasley, L. C., & Kaufman, R. J. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05201.x · Cited by 342 · see citing works

Endoplasmic Reticulum Degradation Requires Lumen to Cytosol Signaling

Gardner, R. G., Swarbrick, G. M., Bays, N. W., Cronin, S. R., Wilhovsky, S., Seelig, L. P., Kim, C. G., & Hampton, R. Y. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.151.1.69 · Cited by 317 · see citing works

Translational control of proinsulin synthesis by glucose

Itoh, N., & Okamoto, H. (1980) · Nature · doi:10.1038/283100a0 · Cited by 315 · see citing works

Activation of an Unfolded Protein Response during Differentiation of Antibody-secreting B Cells

Gass, J. N., Gifford, N. M., & Brewer, J. W. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m205011200 · Cited by 306 · see citing works

Role of ATP and disulphide bonds during protein folding in the endoplasmic reticulum

Braakman, I., Helenius, J. H., & Helenius, A. (1992) · Nature · doi:10.1038/356260a0 · Cited by 287 · see citing works

Induction of neuronal death by ER stress in Alzheimer’s disease

Katayama, T., Imaizumi, K., Manabe, T., Hitomi, J., Kudo, T., & Tohyama, M. (2004) · Journal of Chemical Neuroanatomy · doi:10.1016/j.jchemneu.2003.12.004 · Cited by 287 · see citing works

Induction of two transformation-sensitive membrane polypeptides in normal fibroblasts by a block in glycoprotein synthesis or glucose deprivation

Pouysségur, J., Shiu, R. P. C., & Pastan, I. H. (1977) · Cell · doi:10.1016/0092-8674(77)90305-1 · Cited by 274 · see citing works

5 Mechanism and Regulation of Initiator Methionyl-tRNA Binding to RibosomesPreprint

Hinnebusch, A. G. (2000) · Cold Spring Harbor Monograph Archive · doi:10.1101/087969618.39.185 · Cited by 247 · see citing works

Membrane biogenesis during B cell differentiation: most endoplasmic reticulum proteins are expressed coordinately.

Wiest, D. L., Burkhardt, J. K., Hester, S., Hortsch, M., Meyer, D. I., & Argon, Y. (1990) · The Journal of Cell Biology · doi:10.1083/jcb.110.5.1501 · Cited by 230 · see citing works

Brain ischemia and reperfusion activates the eukaryotic initiation factor 2α kinase, PERK

Kumar, R., Azam, S. M., Sullivan, J. M., Owen, C. R., Cavener, D. R., Zhang, P., Ron, D., Harding, H. P., Chen, J.-J., Han, A., et al. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00387.x · Cited by 212 · see citing works

Increased Vulnerability of Hippocampal Neurons from Presenilin‐1 Mutant Knock‐In Mice to Amyloid β‐Peptide Tox: Central Roles of Superoxide Production and Caspase Activation

Guo, Q., Sebastian, L., Sopher, B. L., Miller, M. W., Ware, C. B., Martin, G. M., & Mattson, M. P. (1999) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1999.0721019.x · Cited by 197 · see citing works

Disturbed Activation of Endoplasmic Reticulum Stress Transducers by Familial Alzheimer's Disease-linked Presenilin-1 Mutations

Katayama, T., Imaizumi, K., Honda, A., Yoneda, T., Kudo, T., Takeda, M., Mori, K., Rozmahel, R. F., Fraser, P., George‐Hyslop, P. S., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104096200 · Cited by 181 · see citing works

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 178 · see citing works

Reduction of Endogenous GRP78 Levels Improves Secretion of a Heterologous Protein in CHO Cells

Dorner, A. J., Krane, M. G., & Kaufman, R. J. (1988) · Molecular and Cellular Biology · doi:10.1128/mcb.8.10.4063-4070.1988 · Cited by 162 · see citing works

Regulation of mRNA translation by protein folding in the endoplasmic reticulum

Kaufman, R. J. (2004) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2004.01.004 · Cited by 162 · see citing works

Biochemical characterization of the 94- and 78-kilodalton glucose-regulated proteins in hamster fibroblasts.

Lee, A. S., Bell, J. R., & Ting, J. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)43091-2 · Cited by 150 · see citing works

Recognition of local glycoprotein misfolding by the ER folding sensor UDP-glucose:glycoprotein glucosyltransferase.

Helenius, A., & Ritter, C. (2000) · Nature Structural Biology · doi:10.1038/74035 · Cited by 143 · see citing works

Protein dissociation from GRP78 and secretion are blocked by depletion of cellular ATP levels.

Dorner, A. J., Wasley, L. C., & Kaufman, R. J. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.19.7429 · Cited by 142 · see citing works

Orchestrating the unfolded protein response in health and disease

Kaufman, R. J. (2002) · Journal of Clinical Investigation · doi:10.1172/jci200216886 · Cited by 130 · see citing works

Increased Production of β-Amyloid and Vulnerability to Endoplasmic Reticulum Stress by an Aberrant Spliced Form of Presenilin 2

Sato, N., Imaizumi, K., Manabe, T., Taniguchi, M., Hitomi, J., Katayama, T., Yoneda, T., Morihara, T., Yasuda, Y., Takagi, T., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m006886200 · Cited by 121 · see citing works

Transcriptional regulation of two genes specifically induced by glucose starvation in a hamster mutant fibroblast cell line.

Lee, A. S., Delegeane, A. M., Baker, V., & Chow, P. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)33296-4 · Cited by 120 · see citing works

Structure and Intermolecular Interactions of the Luminal Dimerization Domain of Human IRE1α

Liu, C. Y., Xu, Z., & Kaufman, R. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300418200 · Cited by 118 · see citing works

In Vivo Action of the HRD Ubiquitin Ligase Complex: Mechanisms of Endoplasmic Reticulum Quality Control and Sterol Regulation

Gardner, R. G., Shearer, A. G., & Hampton, R. Y. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.13.4276-4291.2001 · Cited by 116 · see citing works

Transient Cerebral Ischemia Activates Processing of xbp1 Messenger RNA Indicative of Endoplasmic Reticulum Stress

Paschen, W., Aufenberg, C., Hotop, S., & Mengesdorf, T. (2003) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1097/01.wcb.0000054216.21675.ac · Cited by 106 · see citing works

Unconventional Splicing of HAC1/ERN4 mRNA Required for the Unfolded Protein Response

Kawahara, T., Yanagi, H., Yura, T., & Mori, K. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.3.1802 · Cited by 91 · see citing works

Effect of Glucose on Initiation and Elongation Rates in Isolated Rat Pancreatic Islets

Permutt, M. A. (1974) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)42691-4 · Cited by 58 · see citing works

A role for the unfolded protein response in optimizing antibody secretion

Gunn, K., Gifford, N. M., Mori, K., & Brewer, J. W. (2004) · Molecular Immunology · doi:10.1016/j.molimm.2004.04.023 · Cited by 46 · see citing works

The Role for Endoplasmic Reticulum Stress in Diabetes Mellitus

Eizirik, D. L., Cardozo, A. K., & Cnop, M. (2008) · Endocrine Reviews · doi:10.1210/er.2007-0015 · Cited by 1,173 · see citing works

Hypoxia signalling through mTOR and the unfolded protein response in cancer

Wouters, B. G., & Koritzinsky, M. (2008) · Nature Reviews Cancer · doi:10.1038/nrc2501 · Cited by 894 · see citing works

Cellular Stress Responses, The Hormesis Paradigm, and Vitagenes: Novel Targets for Therapeutic Intervention in Neurodegenerative Disorders

Calabrese, V., Cornelius, C., Dinkova‐Kostova, A. T., Calabrese, E. J., & Mattson, M. P. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.3074 · Cited by 803 · see citing works

Initiation and execution of lipotoxic ER stress in pancreatic β-cells

Cunha, D. A., Hekerman, P., Ladrière, L., Bazarra-Castro, A., Ortis, F., Wakeham, M. C., Moore, F., Rasschaert, J., Cardozo, A. K., Bellomo, E. A., et al. (2008) · Journal of Cell Science · doi:10.1242/jcs.026062 · Cited by 593 · see citing works

Exposing synonymous mutations

Hunt, R., Simhadri, V. L., Iandoli, M., Sauna, Z. E., & Kimchi‐Sarfaty, C. (2014) · Trends in Genetics · doi:10.1016/j.tig.2014.04.006 · Cited by 386 · see citing works

Targeted gene knockout in mammalian cells by using engineered zinc-finger nucleases

Santiago, Y., Chan, E. M., Liu, P., Orlando, S., Zhang, L., Urnov, F. D., Holmes, M. C., Guschin, D. Y., Waite, A. J., Miller, J. C., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0800940105 · Cited by 358 · see citing works

High-Fat Diet Causes Lipotoxicity Responses in Cumulus–Oocyte Complexes and Decreased Fertilization Rates

Wu, L., Dunning, K. R., Yang, X., Russell, D. L., Lane, M., Norman, R. J., & Robker, R. L. (2010) · Endocrinology · doi:10.1210/en.2010-0551 · Cited by 357 · see citing works

Cellular stress response pathways and ageing: intricate molecular relationships

Kourtis, N., & Tavernarakis, N. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.162 · Cited by 304 · see citing works

Cadmium and cellular signaling cascades: interactions between cell death and survival pathways

Thévenod, F., & Lee, W. (2013) · Archives of Toxicology · doi:10.1007/s00204-013-1110-9 · Cited by 248 · see citing works

Induction of the unfolded protein response by α-synuclein in experimental models of Parkinson’s disease

Bellucci, A., Navarria, L., Zaltieri, M., Falarti, E., Bodei, S., Sigala, S., Battistin, L., Spillantini, M. G., Missale, C., & Spano, P. (2010) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2010.07143.x · Cited by 225 · see citing works

The Pathogenesis of Alzheimers Disease—Is It a Lifelong “Calciumopathy”?

Stutzmann, G. E. (2007) · The Neuroscientist · doi:10.1177/1073858407299730 · Cited by 195 · see citing works

Pathogenesis of MASLD and MASH – role of insulin resistance and lipotoxicity

Bansal, S., & Bansal, M. B. (2024) · Alimentary Pharmacology & Therapeutics · doi:10.1111/apt.17930 · Cited by 204 · see citing works

The Endoplasmic Reticulum Unfolded Protein Response in Neurodegenerative Disorders and Its Potential Therapeutic Significance

Remondelli, P., & Renna, M. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00187 · Cited by 167 · see citing works

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 · see citing works

Natural dietary anti-cancer chemopreventive compounds: redox-mediated differential signaling mechanisms in cytoprotection of normal cells versus cytotoxicity in tumor cells

Nair, S., Wenge, L. I., & Kong, A. T. (2007) · Acta Pharmacologica Sinica · doi:10.1111/j.1745-7254.2007.00549.x · Cited by 161 · see citing works

Molecular Mechanism of Lipotoxicity as an Interesting Aspect in the Development of Pathological States—Current View of Knowledge

Lipke, K., Kubis-Kubiak, A., & Piwowar, A. (2022) · Cells · doi:10.3390/cells11050844 · Cited by 145 · see citing works

Anticancer drugs and cardiotoxicity: Insights and perspectives in the era of targeted therapy

Raschi, E., Vasina, V. I., Ursino, M. G., Boriani, G., Martoni, A. A., & Ponti, F. D. (2009) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2009.10.002 · Cited by 151 · see citing works

Cell‐free protein expression based on extracts from CHO cells

Brödel, A. K., Sonnabend, A., & Kubick, S. (2013) · Biotechnology and Bioengineering · doi:10.1002/bit.25013 · Cited by 143 · see citing works

Integrated Proteomics and Genomics Strategies Bring New Insight into Candida albicans Response upon Macrophage Interaction

Fernández‐Arenas, E., Cabezón, V., Bermejo, C., Arroyo, J., Nombela, C., Diez‐Orejas, R., & Gil, C. (2006) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m600210-mcp200 · Cited by 131 · see citing works

Fatty acids and the endoplasmic reticulum in nonalcoholic fatty liver disease

Gentile, C. L., Frye, M. A., & Pagliassotti, M. J. (2010) · BioFactors · doi:10.1002/biof.135 · Cited by 130 · see citing works

Maintenance of muscle mass and load‐induced growth in Muscle <scp>RING</scp> Finger 1 null mice with age

Hwee, D. T., Baehr, L. M., Philp, A., Baar, K., & Bodine, S. C. (2014) · Aging Cell · doi:10.1111/acel.12150 · Cited by 121 · see citing works

Gap junctions in inherited human disorders of the central nervous system

Abrams, C. K., & Scherer, S. S. (2011) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2011.08.015 · Cited by 120 · see citing works

Using Molecular Biology to Maximize Concurrent Training

Baar, K. (2014) · Sports Medicine · doi:10.1007/s40279-014-0252-0 · Cited by 118 · see citing works

Treadmill exercise represses neuronal cell death and inflammation during Aβ-induced ER stress by regulating unfolded protein response in aged presenilin 2 mutant mice

Kang, E., Kwon, I., Koo, J., Kim, E.-J., Kim, C., Lee, J., Yang, C.-H., Lee, Y.-I., Cho, I., & Cho, J. (2013) · APOPTOSIS · doi:10.1007/s10495-013-0884-9 · Cited by 114 · see citing works

From α-synuclein to synaptic dysfunctions: New insights into the pathophysiology of Parkinson's disease

Bellucci, A., Zaltieri, M., Navarria, L., Grigoletto, J., Missale, C., & Spano, P. (2012) · Brain Research · doi:10.1016/j.brainres.2012.04.014 · Cited by 110 · see citing works

Exploiting alternative subcellular location for replication: Tombusvirus replication switches to the endoplasmic reticulum in the absence of peroxisomes

Jonczyk, M., Pathak, K. B., Sharma, M., & Nagy, P. D. (2007) · Virology · doi:10.1016/j.virol.2007.01.004 · Cited by 112 · see citing works

Unfolded Protein Response in Fuchs Endothelial Corneal Dystrophy: A Unifying Pathogenic Pathway?

Engler, C., Kelliher, C., Spitze, A. R., Speck, C. L., Eberhart, C. G., & Jun, A. S. (2010) · American Journal of Ophthalmology · doi:10.1016/j.ajo.2009.09.009 · Cited by 106 · see citing works

The central role of calcium in the effects of cytokines on beta-cell function: implications for type 1 and type 2 diabetes

Ramadan, J. W., Steiner, S. R., O'Neill, C. M., & Nunemaker, C. S. (2011) · Cell Calcium · doi:10.1016/j.ceca.2011.08.005 · Cited by 107 · see citing works

A versatile coupled cell‐free transcription–translation system based on tobacco BY‐2 cell lysates

Buntru, M., Vogel, S., Stoff, K., Spiegel, H., & Schillberg, S. (2014) · Biotechnology and Bioengineering · doi:10.1002/bit.25502 · Cited by 96 · see citing works

Bortezomib in the treatment of AL amyloidosis: targeted therapy?

Sitia, R., Palladini, G. O., & Merlini, G. (2007) · Haematologica · doi:10.3324/haematol.12136 · Cited by 91 · see citing works

Glycoprotein Quality Control and Endoplasmic Reticulum Stress

Wang, Q., Groenendyk, J., & Michalak, M. (2015) · Molecules · doi:10.3390/molecules200813689 · Cited by 91 · see citing works

β-cell apoptosis in type 2 diabetes: quantitative and functional consequences

Lupi, R., & Prato, S. D. (2008) · Diabetes & Metabolism · doi:10.1016/s1262-3636(08)73396-2 · Cited by 87 · see citing works

Channelrhodopsin as a tool to investigate synaptic transmission and plasticity

Schoenenberger, P., Zhang, Y., & Oertner, T. G. (2010) · Experimental Physiology · doi:10.1113/expphysiol.2009.051219 · Cited by 84 · see citing works

β-cell failure in type 2 diabetes mellitus

Lencioni, C., Lupi, R., & Prato, S. D. (2008) · Current Diabetes Reports · doi:10.1007/s11892-008-0031-0 · Cited by 79 · see citing works

Why are some amyloidoses systemic? Does hepatic “chaperoning at a distance” prevent cardiac deposition in a transgenic model of human senile systemic (transthyretin) amyloidosis?

Buxbaum, J. N., Tagoe, C. E., Gallo, G., Walker, J. R., Kurian, S. M., & Salomon, D. R. (2012) · The FASEB Journal · doi:10.1096/fj.11-189571 · Cited by 79 · see citing works

Endoplasmic reticulum calcium release potentiates the ER stress and cell death caused by an oxidative stress in MCF-7 cells

Dejeans, N., Tajeddine, N., Beck, R., Verrax, J., Taper, H. S., Gailly, P. L., & Calderón, P. B. (2009) · Biochemical Pharmacology · doi:10.1016/j.bcp.2009.12.009 · Cited by 77 · see citing works

The ER and ageing II: Calcium homeostasis

Puzianowska-Kuznicka, M., & Kuznicki, J. (2009) · Ageing Research Reviews · doi:10.1016/j.arr.2009.05.002 · Cited by 73 · see citing works

Advanced Techniques for Detecting Protein Misfolding and Aggregation in Cellular Environments

Bai, Y., Zhang, S., Dong, H. Y., Liu, Y., Liu, C., & Zhang, X. (2023) · Chemical Reviews · doi:10.1021/acs.chemrev.3c00494 · Cited by 71 · see citing works

Fetal Growth Plate

Provot, S., & Schipani, E. (2007) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1402.076 · Cited by 71 · see citing works

Extracellular matrix genes as hypoxia-inducible targets

Myllyharju, J., & Schipani, E. (2009) · Cell and Tissue Research · doi:10.1007/s00441-009-0841-7 · Cited by 69 · see citing works

Inositol-Requiring Enzyme 1 Facilitates Diabetic Wound Healing Through Modulating MicroRNAs

Wang, J., Qiu, Y., Yang, Z.-Q., Li, L., & Zhang, K. (2016) · Diabetes · doi:10.2337/db16-0052 · Cited by 69 · see citing works

Identification of the Protein Targets of the Reactive Metabolite of Teucrin A in Vivo in the Rat

Drucková, A., Mernaugh, R. L., Ham, A. L., & Marnett, L. J. (2007) · Chemical Research in Toxicology · doi:10.1021/tx7001405 · Cited by 63 · see citing works

Endoplasmic reticulum stress (ER-stress) by 2-deoxy-D-glucose (2DG) reduces cyclooxygenase-2 (COX-2) expression and N-glycosylation and induces a loss of COX-2 activity via a Src kinase-dependent pathway in rabbit articular chondrocytes

Yu, S., & Kim, S. J. (2010) · Experimental & Molecular Medicine · doi:10.3858/emm.2010.42.11.079 · Cited by 62 · see citing works

Mechanism of Decision Making between Autophagy and Apoptosis Induction upon Endoplasmic Reticulum Stress

Kapuy, O. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25084368 · Cited by 61 · see citing works

Endoplasmic Reticulum Stress in Skeletal Muscle

Deldicque, L., Hespel, P., & Francaux, M. (2011) · Exercise and Sport Sciences Reviews · doi:10.1097/jes.0b013e3182355e8c · Cited by 61 · see citing works

Programming of Fetal Insulin Resistance in Pregnancies with Maternal Obesity by ER Stress and Inflammation

Westermeier, F., Sáez, P. J., Villalobos-Labra, R., Sobrevía, L., & Farías, M. (2014) · BioMed Research International · doi:10.1155/2014/917672 · Cited by 59 · see citing works

Toxicogenomics of endoplasmic reticulum stress inducer tunicamycin in the small intestine and liver of Nrf2 knockout and C57BL/6J mice

Nair, S., XU, C., Shen, G., Hebbar, V., Gopalakrishnan, A., Hu, R., JAIN, M., Liew, C. V., CHAN, J., & KONG, A. (2006) · Toxicology Letters · doi:10.1016/j.toxlet.2006.10.012 · Cited by 60 · see citing works

Confounding Roles of ER Stress and the Unfolded Protein Response in Skeletal Muscle Atrophy

Gallot, Y. S., & Bohnert, K. R. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22052567 · Cited by 59 · see citing works

Excessive eccentric exercise-induced overtraining model leads to endoplasmic reticulum stress in mice skeletal muscles

Pereira, B. C., da Rocha, A. L., Pinto, A. P., Pauli, J. R., de Souza, C. T., Cintra, D. E., Ropelle, E. R., de Freitas, E. C., Zagatto, A. M., & da Silva, A. S. R. (2015) · Life Sciences · doi:10.1016/j.lfs.2015.12.037 · Cited by 59 · see citing works

A chemical compound commonly used to inhibit PKR, {8‐(imidazol‐4‐ylmethylene)‐6H‐azolidino[5,4‐g] benzothiazol‐7‐one}, protects neurons by inhibiting cyclin‐dependent kinase

Chen, H., Wang, L., & D’Mello, S. R. (2008) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2008.06491.x · Cited by 57 · see citing works

Chemical enhancement of torsinA function in cell and animal models of torsion dystonia

Cao, S., Hewett, J. W., Yokoi, F., Lü, J., Buckley, A. C., Burdette, A. J., Chen, P., Nery, F. C., Li, Y., Breakefield, X. O., et al. (2010) · Disease Models & Mechanisms · doi:10.1242/dmm.003715 · Cited by 56 · see citing works

A Comprehensive Systems Biological Study of Autophagy-Apoptosis Crosstalk during Endoplasmic Reticulum Stress

Holczer, M., Márton, M., Kurucz, A., Bánhegyi, G., & Kapuy, O. (2015) · BioMed Research International · doi:10.1155/2015/319589 · Cited by 55 · see citing works

Insulin Is a Key Modulator of Fetoplacental Endothelium Metabolic Disturbances in Gestational Diabetes Mellitus

Sobrevía, L., Salsoso, R., Fuenzalida, B., Barros, E., Toledo, L., Silva, L., Pizarro, C., Subiabre, M., Villalobos-Labra, R., Henríquez, J. A., et al. (2016) · Frontiers in Physiology · doi:10.3389/fphys.2016.00119 · Cited by 54 · see citing works

Glycosylation flux analysis reveals dynamic changes of intracellular glycosylation flux distribution in Chinese hamster ovary fed-batch cultures

Hutter, S., Villiger, T. K., Brühlmann, D., Stettler, M., Broly, H., Šoóš, M., & Gunawan, R. (2017) · Metabolic Engineering · doi:10.1016/j.ymben.2017.07.005 · Cited by 52 · see citing works

Endoplasmic reticulum stress in murine liver and kidney exposed to microcystin-LR

Qin, W., Xu, L., Zhang, X., Wang, Y., Meng, X., Miao, A., & Yang, L. (2010) · Toxicon · doi:10.1016/j.toxicon.2010.07.017 · Cited by 52 · see citing works

Panaxydol, a component of P anax ginseng, induces apoptosis in cancer cells through EGFR activation and ER stress and inhibits tumor growth in mouse models

Kim, H. S., Lim, J. M., Kim, J. Y., Kim, Y.-J., Park, S. I., & Sohn, J. (2015) · International Journal of Cancer · doi:10.1002/ijc.29879 · Cited by 52 · see citing works

Assessment of the AAV-mediated expression of channelrhodopsin-2 and halorhodopsin in brainstem neurons mediating auditory signaling

Shimano, T., Fyk‐Kolodziej, B. E., Mirza, N., Asako, M., Tomoda, K., Bledsoe, S. C., Pan, Z., Molitor, S. C., & Holt, A. G. (2012) · Brain Research · doi:10.1016/j.brainres.2012.10.030 · Cited by 51 · see citing works

Myelin under stress

D’Antonio, M., Feltri, M. L., & Wrabetz, L. G. (2009) · Journal of Neuroscience Research · doi:10.1002/jnr.22066 · Cited by 50 · see citing works

ER Stress Induces Anabolic Resistance in Muscle Cells through PKB-Induced Blockade of mTORC1

Deldicque, L., Bertrand, L., Patton, A., Francaux, M., & Baar, K. (2011) · PLoS ONE · doi:10.1371/journal.pone.0020993 · Cited by 50 · see citing works

Protein quality control: the who’s who, the where’s and therapeutic escapes

Roth, J., Yam, G. H., Fan, J., Hirano, K., Gaplovská-Kyselá, K., Fourn, V. L., Guhl, B., Santimaria, R., Torossi, T., Ziak, M., et al. (2007) · Histochemistry and Cell Biology · doi:10.1007/s00418-007-0366-7 · Cited by 49 · see citing works

Inflammation induced ER stress affects absorptive intestinal epithelial cells function and integrity

Chotikatum, S., Naim, H. Y., & El‐Najjar, N. (2018) · International Immunopharmacology · doi:10.1016/j.intimp.2017.12.016 · Cited by 48 · see citing works

Minocycline prevents paraquat-induced cell death through attenuating endoplasmic reticulum stress and mitochondrial dysfunction

Huang, C., Lee, Y., Yang, Y.-C., Kuo, T.-Y., & Huang, N. (2012) · Toxicology Letters · doi:10.1016/j.toxlet.2011.12.021 · Cited by 45 · see citing works

Endoplasmic Reticulum stress induces hepatic stellate cell apoptosis and contributes to fibrosis resolution

Minicis, S. D., Candelaresi, C., Agostinelli, L., Taffetani, S., Saccomanno, S., Rychlicki, C., Trozzi, L., Marzioni, M., Benedetti, A., & Svegliati‐Baroni, G. (2012) · Liver International · doi:10.1111/j.1478-3231.2012.02860.x · Cited by 45 · see citing works

AID−/−μs−/− Mice Are Agammaglobulinemic and Fail to Maintain B220−CD138+ Plasma Cells

Kumazaki, K., Tirosh, B., Maehr, R., Boes, M. L., Honjo, T., & Ploegh, H. L. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.178.4.2192 · Cited by 45 · see citing works

Production of lysophosphatidylcholine by cPLA2 in the brain of mice lacking PPT1 is a signal for phagocyte infiltration

Zhang, Z., Lee, Y., Kim, S. J., Choi, M. S., Tsai, P.-C., Saha, A., Wei, H., Xu, Y., Xiao, Y., Zhang, P., et al. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddm029 · Cited by 45 · see citing works

ER stress disturbs SR/ER-mitochondria Ca2+ transfer: Implications in Duchenne muscular dystrophy

Pauly, M., Angebault, C., Dridi, H., Notarnicola, C., Scheuermann, V., Lacampagne, A., Matecki, S., & Fauconnier, J. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2017.06.009 · Cited by 44 · see citing works

An efficient in vitro translation system from mammalian cells lacking the translational inhibition caused by eIF2 phosphorylation

Zeenko, V. V., Wang, C., Majumder, M., Komar, A. A., Snider, M. D., Merrick, W. C., Kaufman, R. J., & Hatzoglou, M. (2008) · RNA · doi:10.1261/rna.825008 · Cited by 44 · see citing works

Cucurbitacin I induces cancer cell death through the endoplasmic reticulum stress pathway

Li, H., Chen, H., Li, R., Xin, J., Wu, S., Lan, J., Xue, K., Li, X., Zuo, C., Jiang, W., et al. (2018) · Journal of Cellular Biochemistry · doi:10.1002/jcb.27570 · Cited by 42 · see citing works

Endurance training in mice increases the unfolded protein response induced by a high-fat diet

Deldicque, L., Cani, P. D., Delzenne, N. M., Baar, K., & Francaux, M. (2013) · Journal of Physiology and Biochemistry · doi:10.1007/s13105-012-0204-9 · Cited by 41 · see citing works

Plasma Membrane Ca2+-ATPase Overexpression Depletes Both Mitochondrial and Endoplasmic Reticulum Ca2+ Stores and Triggers Apoptosis in Insulin-secreting BRIN-BD11 Cells

Jiang, L., Allagnat, F., Nguidjoe, E., Kamagaté, A., Pachera, N., Vanderwinden, J., Brini, M., Carafoli, E., Eizirik, D. L., Cardozo, A. K., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.116681 · Cited by 39 · see citing works

Feedback mechanisms in the regulation of intracellular calcium ([Ca2+]i) in the peripheral nociceptive system: Role of TRPV-1 and pain related receptors

Hagenacker, T., Ledwig, D., & Büsselberg, D. (2007) · Cell Calcium · doi:10.1016/j.ceca.2007.05.019 · Cited by 39 · see citing works

Ageing and Low-Level Chronic Inflammation: The Role of the Biological Clock

Colombini, B., Dinu, M., Murgo, E., Lotti, S., Tarquini, R., Sofi, F., & Mazzoccoli, G. (2022) · Antioxidants · doi:10.3390/antiox11112228 · Cited by 37 · see citing works

Nutrient deprivation induces α-synuclein aggregation through endoplasmic reticulum stress response and SREBP2 pathway

Jiang, P., Gan, M., Lin, W.-L., & Yen, S.-H. C. (2014) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2014.00268 · Cited by 37 · see citing works

A systems biological analysis of the ATF4‐GADD34‐CHOP regulatory triangle upon endoplasmic reticulum stress

Márton, M., Bánhegyi, G., Gyöngyösi, N., Kálmán, E. É., Pettkó‐Szandtner, A., Káldi, K., & Kapuy, O. (2022) · FEBS Open Bio · doi:10.1002/2211-5463.13484 · Cited by 36 · see citing works

The unfolded protein response in human skeletal muscle is not involved in the onset of glucose tolerance impairment induced by a fat-rich diet

Deldicque, L., Proeyen, K. V., Francaux, M., & Hespel, P. (2010) · European Journal of Applied Physiology · doi:10.1007/s00421-010-1783-1 · Cited by 36 · see citing works

Defining cutaneous molecular pathobiology of arsenicals using phenylarsine oxide as a prototype

Srivastava, R. K., Li, C., Weng, Z., Agarwal, A., Elmets, C. A., Afaq, F., & Athar, M. (2016) · Scientific Reports · doi:10.1038/srep34865 · Cited by 36 · see citing works

Cross organelle stress response disruption promotes gentamicin-induced proteotoxicity

Igwebuike, C., Yaglom, J. A., Huiting, L. N., Feng, H., Campbell, J. D., Wang, Z., Havasi, A., Pimentel, D. R., Sherman, M. Y., & Borkan, S. C. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-2382-7 · Cited by 36 · see citing works

Gene expression profiling of erythroblasts from refractory anaemia with ring sideroblasts (RARS) and effects of G‐CSF

Nikpour, M., Pellagatti, A., Liu, A., Karimi, M., Malcovati, L., Gogvadze, V. G., Forsblom, A., Wainscoat, J. S., Cazzola, M., Zhivotovsky, B., et al. (2010) · British Journal of Haematology · doi:10.1111/j.1365-2141.2010.08174.x · Cited by 36 · see citing works

Retinoid x receptor modulation protects against ER stress response and rescues glaucoma phenotypes in adult mice

Dheer, Y., Chitranshi, N., Gupta, V. B., Sharma, S., Pushpitha, K., Abbasi, M., Mirzaei, M., You, Y., Graham, S. L., & Gupta, V. (2019) · Experimental Neurology · doi:10.1016/j.expneurol.2019.01.015 · Cited by 35 · see citing works

Increased sensitivity to glucose starvation correlates with downregulation of glycogen phosphorylase isoform PYGB in tumor cell lines resistant to 2-deoxy-d-glucose

Philips, K. B., Kurtoğlu, M., Leung, H. J., Liu, H., Gao, N., Lehrman, M. A., Murray, T. G., & Lampidis, T. J. (2013) · Cancer Chemotherapy and Pharmacology · doi:10.1007/s00280-013-2358-8 · Cited by 30 · see citing works

Sulfur mustard induces an endoplasmic reticulum stress response in the mouse ear vesicant model

Chang, Y., Wang, J. D., Svoboda, K. K. H., Casillas, R. P., Laskin, J. D., Gordon, M. K., & Gerecke, D. R. (2013) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2013.01.014 · Cited by 29 · see citing works

The MHC Class I Heavy Chain Structurally Conserved Cysteines 101 and 164 Participate in HLA-B27 Dimer Formation

Lenart, I., Guiliano, D. B., Burn, G. L., Campbell, E. C., Morley, K. D., Fussell, H., Powis, S. J., & Antoniou, A. N. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3693 · Cited by 28 · see citing works

Unfolded protein response to global ischemia following 48 h of reperfusion in the rat brain: the effect of age and meloxicam

Llorente, I. L., Burgin, T. C., Pérez‐Rodríguez, D., Martínez‐Villayandre, B., Pérez-García, C. C., & Fernández‐López, A. (2013) · Journal of Neurochemistry · doi:10.1111/jnc.12337 · Cited by 27 · see citing works

Astragalus Polysaccharide Extends Lifespan via Mitigating Endoplasmic Reticulum Stress in the Silkworm, Bombyx mori

Song, J., Chen, M., Li, Z., Zhang, J., Hu, H., Tong, X., & Dai, F. (2019) · Aging and Disease · doi:10.14336/ad.2019.0515 · Cited by 27 · see citing works

The Involvement of Endoplasmic Reticulum Stress in the Suppression of Colorectal Tumorigenesis by Tolfenamic Acid

Zhang, X., Lee, S., Min, K., McEntee, M. F., Jeong, J. B., Li, Q., & Baek, S. J. (2013) · Cancer Prevention Research · doi:10.1158/1940-6207.capr-13-0220 · Cited by 26 · see citing works

Regulatory proteins of eukaryotic initiation factor 2‐alpha subunit (eIF2α) phosphatase, under ischemic reperfusion and tolerance

García‐Bonilla, L., Cid, C., Alcázar, A., Bürda, J., Ayuso, M. I., & Salinas, M. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04844.x · Cited by 26 · see citing works

Altered redox state of luminal pyridine nucleotides facilitates the sensitivity towards oxidative injury and leads to endoplasmic reticulum stress dependent autophagy in HepG2 cells

Száraz, P., Bánhegyi, G., & Benedetti, A. (2009) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2009.10.004 · Cited by 25 · see citing works

Differences in Unfolded Protein Response Pathway Activation in the Lenses of Three Types of Cataracts

Yang, J., Zhou, S., Gu, J., Wang, Y., Guo, M., & Liu, Y. (2015) · PLoS ONE · doi:10.1371/journal.pone.0130705 · Cited by 25 · see citing works

Multiple system‐level feedback loops control life‐and‐death decisions in endoplasmic reticulum stress

Kapuy, O., Márton, M., Bánhegyi, G., & Vinod, P. K. U. (2019) · FEBS Letters · doi:10.1002/1873-3468.13689 · Cited by 24 · see citing works

Endoplasmic reticulum stress is a target for therapy in Waldenstrom macroglobulinemia

Leleu, X. P., Xu, L., Jia, X., Sacco, A., Farag, M., Hunter, Z. R., Moreau, A., Ngo, H. T., Hatjiharissi, E., Ho, A. W., et al. (2008) · Blood · doi:10.1182/blood-2007-10-116848 · Cited by 24 · see citing works

Experimental Colitis Is Associated with Ultrastructural Changes in Inflamed and Uninflamed Regions of the Gastrointestinal Tract

Bou-Fersen, A. M., Anim, J. T., & Khan, I. U. (2008) · Medical Principles and Practice · doi:10.1159/000117791 · Cited by 22 · see citing works

4-Methyl-2,4-bis(4-hydroxyphenyl)pent-1-ene, a Major Active Metabolite of Bisphenol A, Triggers Pancreatic β-Cell Death via a JNK/AMPKα Activation-Regulated Endoplasmic Reticulum Stress-Mediated Apoptotic Pathway

Huang, C.-C., Huang, C.-C., Su, C., Fang, K., Yen, C., Yen, C., Lin, C.-T., Lee, K.-I., Chen, Y.-W., Liu, S., et al. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094379 · Cited by 20 · see citing works

MPP+-induces PUMA- and p53-dependent, but ATF3-independent cell death

Bernstein, A. I., & O’Malley, K. L. (2013) · Toxicology Letters · doi:10.1016/j.toxlet.2013.03.003 · Cited by 21 · see citing works

Diseases of connexins expressed in myelinating glia

Abrams, C. K. (2017) · Neuroscience Letters · doi:10.1016/j.neulet.2017.05.037 · Cited by 21 · 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

Caffeine Inhibits Paclitaxel-Induced Apoptosis in Colorectal Cancer Cells through the Upregulation of Mcl-1 Levels

MHAIDAT, N. M., ALZOUBI, K. H., AL-AZZAM, S. I., & ALSAAD, A. A. (2014) · Molecular Medicine Reports · doi:10.3892/mmr.2013.1763 · Cited by 20 · see citing works

Cocoa Extract Provides Protection against 6-OHDA Toxicity in SH-SY5Y Dopaminergic Neurons by Targeting PERK

Vestuto, V., Amodio, G., Pepe, G., Basilicata, M. G., Belvedere, R., Napolitano, E., Guarnieri, D., Pagliara, V., Paladino, S., Rodriquez, M., et al. (2022) · Biomedicines · doi:10.3390/biomedicines10082009 · Cited by 18 · see citing works

The two N‐glycans present on bovine Pofut1 are differently involved in its solubility and activity

Loriol, C., Audfray, A., Dupuy, F., Germot, A., & Maftah, A. A. (2007) · FEBS Journal · doi:10.1111/j.1742-4658.2007.05663.x · Cited by 18 · see citing works

Enhanced ubiquitin-proteasome activity in calreticulin deficient cells: A compensatory mechanism for cell survival

Uvarov, A. V., & Mesaeli, N. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2008.03.004 · Cited by 18 · see citing works

Response of Rat Retinal Capillary Pericytes and Endothelial Cells to Glucose

Makita, J., Hosoya, K., Zhang, P., & Kador, P. F. (2010) · Journal of Ocular Pharmacology and Therapeutics · doi:10.1089/jop.2010.0051 · Cited by 17 · 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

The unfolded protein response—a stress signaling pathway of the endoplasmic reticulum

Shen, X., Zhang, K., & Kaufman, R. J. (2004) · Journal of Chemical Neuroanatomy · doi:10.1016/j.jchemneu.2004.02.006 · Cited by 290 · see citing works

The endoplasmic reticulum and the unfolded protein response

Malhotra, J. D., & Kaufman, R. J. (2007) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2007.09.003 · Cited by 984 · see citing works

Unfolded Protein Response: An Intracellular Signaling Pathway Activated by the Accumulation of Unfolded Proteins in the Lumen of the Endoplasmic Reticulum

Kaufman, R. J. (2003) · Elsevier eBooks · doi:10.1016/b978-012124546-7/50678-1

Unfolded protein response

Cao, S. S., & Kaufman, R. J. (2012) · Current Biology · doi:10.1016/j.cub.2012.07.004 · Cited by 365 · see citing works