Orchestrating the unfolded protein response in health and disease

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

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

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

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

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

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

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

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

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

The glucose-regulated proteins: stress induction and clinical applications

Lee, A. S. (2001) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(01)01908-9 · Cited by 1,033 · 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

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

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

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

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

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

Translational control in the endoplasmic reticulum stress response

Ron, D. (2002) · Journal of Clinical Investigation · doi:10.1172/jci0216784 · Cited by 728 · 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

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

Folic Acid Deficiency and Homocysteine Impair DNA Repair in Hippocampal Neurons and Sensitize Them to Amyloid Toxicity in Experimental Models of Alzheimer's Disease

Kruman, I. I., Kumaravel, T. S., Lohani, A., Pedersen, W. A., Cutler, R. G., Kruman, Y., Haughey, N. J., Lee, J., Evans, M. K., & Mattson, M. P. (2002) · Journal of Neuroscience · doi:10.1523/jneurosci.22-05-01752.2002 · Cited by 640 · see citing works

Activation of ATF6 and an ATF6 DNA Binding Site by the Endoplasmic Reticulum Stress Response

Wang, Y., Shen, J., Arenzana, N., Tirasophon, W., Kaufman, R. J., & Prywes, R. (2000) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)61473-0 · Cited by 617 · see citing works

The unfolded protein response in nutrient sensing and differentiation

Kaufman, R. J., Scheuner, D. L., Schröder, M., Shen, X., Lee, K., Liu, C. Y., & Arnold, S. M. (2002) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm829 · Cited by 607 · 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

The Ca2+ concentration of the endoplasmic reticulum is a key determinant of ceramide‐induced apoptosis: significance for the molecular mechanism of Bcl‐2 action

Pinton, P., Ferrari, D., Rapizzi, E., Virgilio, F. D., Pozzan, T., & Rizzuto, R. (2001) · The EMBO Journal · doi:10.1093/emboj/20.11.2690 · Cited by 599 · 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

Hyperhomocysteinemia enhances vascular inflammation and accelerates atherosclerosis in a murine model

Hofmann, M. A., Lalla, E., Lu, Y., Gleason, M. R., Wolf, B. M., Tanji, N., Ferran, L. J., Kohl, B., Rao, V., Kisiel, W., et al. (2001) · Journal of Clinical Investigation · doi:10.1172/jci10588 · Cited by 529 · 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

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

Reimold, A. M., Etkin, A., CLAUSS, I. M., Perkins, A. C., Friend, D. S., Zhang, J. H., Horton, H. F., Scott, A., Orkin, S. H., Byrne, M. C., et al. (2000) · Genes & Development · doi:10.1101/gad.14.2.152 · Cited by 517 · 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

Coupling Endoplasmic Reticulum Stress to the Cell Death Program

Rao, R. V., Castro‐Obregón, S., Frankowski, H., Schüler, M., Stoka, V., del Rio, G., Bredesen, D. E., & Ellerby, H. M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202726200 · Cited by 472 · see citing works

Mammalian stress response: induction of the glucose-regulated protein family

Lee, A. S. (1992) · Current Opinion in Cell Biology · doi:10.1016/0955-0674(92)90042-b · Cited by 442 · 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

Increased sensitivity to dextran sodium sulfate colitis in IRE1β-deficient mice

Bertolotti, A., Wang, X.-Z., Novoa, I., Jungreis, R., Schlessinger, K., Cho, J. H., West, A. B., & Ron, D. (2001) · Journal of Clinical Investigation · doi:10.1172/jci11476 · Cited by 412 · see citing works

ER quality control: towards an understanding at the molecular level

Ellgaard, L., & Helenius, A. (2001) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(00)00233-7 · Cited by 388 · 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

Homocysteine-Induced Endoplasmic Reticulum Stress and Growth Arrest Leads to Specific Changes in Gene Expression in Human Vascular Endothelial Cells

Outinen, P. A., Sood, S. K., Pfeifer, S. I., Pamidi, S., Podor, T. J., Li, J., Weitz, J. I., & Austin, R. C. (1999) · Blood · doi:10.1182/blood.v94.3.959.415k20_959_967 · Cited by 349 · see citing works

Regulated Step in Cholesterol Feedback Localized to Budding of SCAP from ER Membranes

Nohturfft, A., Yabe, D., Goldstein, J. L., Brown, M. S., & Espenshade, P. J. (2000) · Cell · doi:10.1016/s0092-8674(00)00037-4 · Cited by 347 · 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

Herp, a New Ubiquitin-like Membrane Protein Induced by Endoplasmic Reticulum Stress

Kokame, K., Agarwala, K. L., Kato, H., & Miyata, T. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m002063200 · Cited by 332 · 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

Endoplasmic Reticulum Stress-Induced Formation of Transcription Factor Complex ERSF Including NF-Y (CBF) and Activating Transcription Factors 6α and 6β That Activates the Mammalian Unfolded Protein Response

Yoshida, H., Okada, T., Haze, K., Yanagi, H., Yura, T., Negishi, M., & Mori, K. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.4.1239-1248.2001 · Cited by 294 · see citing works

A lag in intracellular degradation of mutant alpha 1-antitrypsin correlates with the liver disease phenotype in homozygous PiZZ alpha 1-antitrypsin deficiency.

Wu, Y., Whitman, I. P., Molmenti, E. P., Moore, K., Hippenmeyer, P. J., & Perlmutter, D. H. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.19.9014 · Cited by 289 · see citing works

Homocysteine Induces Programmed Cell Death in Human Vascular Endothelial Cells through Activation of the Unfolded Protein Response

Zhang, C., Cai, Y., Adachi, M. T., Oshiro, S., Aso, T., Kaufman, R. J., & Kitajima, S. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100747200 · Cited by 288 · see citing works

A Role for Presenilin-1 in Nuclear Accumulation of Ire1 Fragments and Induction of the Mammalian Unfolded Protein Response

Niwa, M., Sidrauski, C., Kaufman, R. J., & Walter, P. (1999) · Cell · doi:10.1016/s0092-8674(00)81667-0 · Cited by 276 · see citing works

IRE1 and efferent signaling from the endoplasmic reticulum

Urano, F., Bertolotti, A., & Ron, D. (2000) · Journal of Cell Science · doi:10.1242/jcs.113.21.3697 · Cited by 270 · see citing works

The endoribonuclease activity of mammalian IRE1 autoregulates its mRNA and is required for the unfolded protein responsePreprint

Tirasophon, W., Lee, K., Callaghan, B. C., Welihinda, A. A., & Kaufman, R. J. (2000) · Genes & Development · doi:10.1101/gad.839400 · Cited by 267 · see citing works

Molecular Pathways of Protein Synthesis Inhibition during Brain Reperfusion: Implications for Neuronal Survival or Death

DeGracia, D. J., Kumar, R., Owen, C. R., Krause, G. S., & White, B. C. (2002) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1097/00004647-200202000-00001 · Cited by 233 · see citing works

Overexpression of Pex15p, a phosphorylated peroxisomal integral membrane protein required for peroxisome assembly in S.cerevisiae, causes proliferation of the endoplasmic reticulum membrane

Elgersma, Y., Kwast, L., van den Berg, M., et al. (1997) · The EMBO Journal · doi:10.1093/emboj/16.24.7326 · Cited by 221 · see citing works

Dietary Supplementation With Methionine and Homocysteine Promotes Early Atherosclerosis but Not Plaque Rupture in ApoE-Deficient Mice

Zhou, J., Møller, J., Danielsen, C. C., Bentzon, J. F., Ravn, H. B., Austin, R. C., & Falk, E. (2001) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/hq0901.096582 · Cited by 216 · 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

Procollagen folding and assembly: The role of endoplasmic reticulum enzymes and molecular chaperones

Lamandé, S. R., & Bateman, J. F. (1999) · Seminars in Cell and Developmental Biology · doi:10.1006/scdb.1999.0317 · Cited by 207 · see citing works

Involvement of Endoplasmic Reticulum Chaperones in the Folding of Hepatitis C Virus Glycoproteins

Choukhi, A., Ung, S., Wychowski, C., & Dubuisson, J. (1998) · Journal of Virology · doi:10.1128/jvi.72.5.3851-3858.1998 · Cited by 188 · see citing works

Protein aggregation in disease: a role for folding intermediates forming specific multimeric interactions

Horwich, A. L. (2002) · Journal of Clinical Investigation · doi:10.1172/jci0216781 · Cited by 185 · see citing works

mRNA splicing-mediated C-terminal replacement of transcription factor Hac1p is required for efficient activation of the unfolded protein response

Mori, K., Ogawa, N., Kawahara, T., et al. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.050010197 · Cited by 181 · see citing works

Preclinical and clinical evaluation of proteasome inhibitor PS-341 for the treatment of cancer

Adams, J. (2002) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(02)00343-5 · Cited by 141 · see citing works

Targeting of the c-Abl Tyrosine Kinase to Mitochondria in Endoplasmic Reticulum Stress-Induced Apoptosis

Ito, Y., Pandey, P., Mishra, N. C., et al. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.18.6233-6242.2001 · Cited by 134 · see citing works

Homocysteine thiolactone induces apoptotic DNA damage mediated by increased intracellular hydrogen peroxide and caspase 3 activation in HL-60 cells

Huang, R.-F. S., Huang, S.-M., Lin, B.-S., et al. (2001) · Life Sciences · doi:10.1016/s0024-3205(01)01066-9 · Cited by 129 · see citing works

Endoplasmic Reticulum Stress-inducible Protein, Herp, Enhances Presenilin-mediated Generation of Amyloid β-Protein

Sai, X., Kawamura, Y., Kokame, K., Yamaguchi, H., Shiraishi, H., Suzuki, R., Suzuki, T., Kawaichi, M., Miyata, T., Kitamura, T., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m112372200 · Cited by 126 · see citing works

The Protein Kinase/Endoribonuclease IRE1α That Signals the Unfolded Protein Response Has a Luminal N-terminal Ligand-independent Dimerization Domain

Liu, C. Y., Wong, H. N., Schauerte, J. A., & Kaufman, R. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m112454200 · Cited by 122 · see citing works

The basic domain/leucine zipper protein hXBP-1 preferentially binds to and transactivates CRE-like sequences containing an ACGT core

CLAUSS, I. M. (1996) · Nucleic Acids Research · doi:10.1093/nar/24.10.1855 · Cited by 105 · see citing works

Genetic tailoring of N-linked oligosaccharides: The role of glucose residues in glycoprotein processing of Saccharomyces cerevisiae in vivo

Jakob, C. A., Burda, P., Heesen, S. T., Aebi, M., & Roth, J. (1998) · Glycobiology · doi:10.1093/glycob/8.2.155 · Cited by 86 · see citing works

Targeted Disruption of CRE-Binding Factor TREB5 Gene Leads to Cellular Necrosis in Cardiac Myocytes at the Embryonic Stage

Masaki, T., Yoshida, M., & Noguchi, S. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.0972 · Cited by 67 · see citing works

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

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Cellular Origin of Hexokinase in Pancreatic Islets

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Induction of glucose-regulated protein (glucose-regulated protein 78/B:P and glucose-regulated protein 94) and heat shock protein 70 transcripts in the immature rat brain following status epilepticus

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Induction of secretory pathway components in yeast is associated with increased stability of their mRNA

Hyde, M., Block-Alper, L., Felix, J., Webster, P. C., & Meyer, D. I. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200112008 · Cited by 42 · see citing works

Null Mutation in IRE1 Gene Inhibits Overproduction of Microsomal Cytochrome P450Alkl (CYP 52A3) and Proliferation of the Endoplasmic Reticulum in Saccharomyces cerevisiae

Takewaka, T., Zimmer, T., Hirata, A., et al. (1999) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a022314 · Cited by 26 · see citing works

Ultrastructural changes during the enhancement of cellular 3-hydroxy-3-methyl-glutaryl-coenzyme A reductase in a Chinese hamster cell mutant resistant to compactin (ML 236B).

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Characterization and Regulation of the Genes Encoding Ribosomal Proteins L39 and S7 of the Human PathogenCandida albicans

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Mechanisms, regulation and functions of the unfolded protein response

Hetz, C., Zhang, K., & Kaufman, R. J. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0250-z · Cited by 2,666 · see citing works

Mediators of endoplasmic reticulum stress-induced apoptosis

Szegezdi, E., Logue, S. E., Gorman, A. M., & Samali, A. (2006) · The EMBO Reports · doi:10.1038/sj.embor.7400779 · Cited by 2,345 · see citing works

From endoplasmic-reticulum stress to the inflammatory response

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Autophagy Is Activated for Cell Survival after Endoplasmic ReticulumStress

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