Endoplasmic Reticulum Stress and Diabetes Mellitus.

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 3,344

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 3,292

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

Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases

Bucciantini, M., Giannoni, E., Chiti, F., Baroni, F., Formigli, L., Zurdo, J., Taddei, N., Ramponi, G., Dobson, C. M., & Stefani, M. (2002) · Nature · doi:10.1038/416507a · Cited by 2,434

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 2,039

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 1,945

Aggresomes, inclusion bodies and protein aggregation

Kopito, R. R. (2000) · Trends in Cell Biology · doi:10.1016/s0962-8924(00)01852-3 · Cited by 1,942

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 1,372

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

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

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 1,211

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 1,197

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

Heat shock, stress proteins, chaperones, and proteotoxicity

Hightower, L. E. (1991) · Cell · doi:10.1016/0092-8674(91)90611-2 · Cited by 1,063

Inhibition of Bax Channel-Forming Activity by Bcl-2

Antonsson, B. E., Conti, F., Ciavatta, A., Montessuit, S., Lewis, S., Martinou, I., Bernasconi, L., Bernard, A., Mermod, J., Mazzei, G. J., et al. (1997) · Science · doi:10.1126/science.277.5324.370 · Cited by 1,028

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

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

Tripartite Management of Unfolded Proteins in the Endoplasmic Reticulum

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

A choice of death - the signal-transduction of immune-mediated beta-cell apoptosis

Eizirik, D. L., & Mandrup-Poulsen, T. R. (2001) · Diabetologia · doi:10.1007/s001250100021 · Cited by 891

β-Cell death during progression to diabetes

Mathis, D. J., Vence, L., & Benoist, C. O. (2001) · Nature · doi:10.1038/414792a · Cited by 884

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 868

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

Yoneda, T., Imaizumi, K., Oono, K., Yui, D., Gomi, F., Katayama, T., & Tohyama, M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010677200 · Cited by 866

Pancreatic islet cell toxicity of amylin associated with type-2 diabetes mellitus

Lorenzo, A., Razzaboni, B. L., Weir, G. C., & Yankner, B. A. (1994) · Nature · doi:10.1038/368756a0 · Cited by 820

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

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

Cloning of mammalian Ire1 reveals diversity in the ER stress responses

Wang, X., 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 803

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

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

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

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

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 601

A mutation in the insulin 2 gene induces diabetes with severe pancreatic β-cell dysfunction in the Mody mouse

Wang, J., Takeuchi, T., Tanaka, S., Kubo, S.-K., Kayo, T., Lu, D., Takata, K., Koizumi, A., & Izumi, T. (1999) · Journal of Clinical Investigation · doi:10.1172/jci4431 · Cited by 572

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

A Novel Locus, Mody4, Distal to D7Mit189 on Chromosome 7 Determines Early-Onset NIDDM in Nonobese C57BL/6 (Akita) Mutant Mice

Yoshioka, M., Kayo, T., Ikeda, T., & Koizuni, A. (1997) · Diabetes · doi:10.2337/diab.46.5.887 · Cited by 536

Endoplasmic reticulum stress-mediated apoptosis in pancreatic β-cells

Oyadomari, S., Araki, E., & Mori, M. (2002) · APOPTOSIS · doi:10.1023/a:1016175429877 · Cited by 519

Human caspase 12 has acquired deleterious mutations

Fischer, H., Koenig, U., Eckhart, L., & Tschachler, E. (2002) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)00289-9 · Cited by 346

Spontaneous diabetes mellitus in transgenic mice expressing human islet amyloid polypeptide.

Janson, J., Soeller, W. C., Roche, P. C., Nelson, R. T., Torchia, A. J., Kreutter, D. K., & Butler, P. C. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.14.7283 · Cited by 343

CHOP (GADD153) and its oncogenic variant, TLS-CHOP, have opposing effects on the induction of G1/S arrest.Preprint

Barone, M. V., Crozat, A., Tabaee, A., Philipson, L., & Ron, D. (1994) · Genes & Development · doi:10.1101/gad.8.4.453 · Cited by 336

Ectopic expression of CHOP (GADD153) induces apoptosis in M1 myeloblastic leukemia cells

Matsumoto, M., Minami, M., Takeda, K., Sakao, Y., & Akira, S. (1996) · FEBS Letters · doi:10.1016/0014-5793(96)01016-2 · Cited by 321

Islet amyloid and type 2 diabetes: from molecular misfolding to islet pathophysiology

Jaikaran, E. T. A. S., & Clark, A. (2001) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/s0925-4439(01)00078-3 · Cited by 298

Islet amyloid formation associated with hyperglycemia in transgenic mice with pancreatic beta cell expression of human islet amyloid polypeptide.

Verchere, C. B., D'Alessio, D. A., Palmiter, R. D., Weir, G. C., Bonner-Weir, S., Baskin, D. G., & Kahn, S. E. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.8.3492 · Cited by 278

Calcium, a signaling molecule in the endoplasmic reticulum?

Corbett, E. F., & Michalak, M. (2000) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)01588-7 · Cited by 265

Nitric Oxide-induced Apoptosis in RAW 264.7 Macrophages Is Mediated by Endoplasmic Reticulum Stress Pathway Involving ATF6 and CHOP

Gotoh, T., Oyadomari, S., Mori, K., & Mori, M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m107988200 · Cited by 240

Identification of Novel Cytokine-Induced Genes in Pancreatic β-Cells by High-Density Oligonucleotide Arrays

Cardozo, A. K., Kruhøffer, M., Leeman, R., Orntoft, T. F., & Eizirik, D. L. (2001) · Diabetes · doi:10.2337/diabetes.50.5.909 · Cited by 229

Missense Mutation of Amylin Gene (S20G) in Japanese NIDDM Patients

Sakagashira, S., Sanke, T., Hanabusa, T., Shimomura, H., Ohagi, S., Kumagaye, K. Y., Nakajima, K., & Nanjo, K. (1996) · Diabetes · doi:10.2337/diab.45.9.1279 · Cited by 162

Extensive islet amyloid formation is induced by development of Type II diabetes mellitus and contributes to its progression: pathogenesis of diabetes in a mouse model

Höppener, J. W. M., Oosterwijk, C., Nieuwenhuis, M. G., Posthuma, G., Thijssen, J. H. H., Vroom, T. M., Ahrén, B., & Lips, C. J. M. (1999) · Diabetologia · doi:10.1007/s001250051175 · Cited by 153

CHOP-Dependent Stress-Inducible Expression of a Novel Form of Carbonic Anhydrase VI

Sok, J. C., Wang, X.-Z., Batchvarova, N., Kuroda, M., Harding, H. P., & Ron, D. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.1.495 · Cited by 148

Compensatory responses in mice carrying a null mutation for Ins1 or Ins2.

Leroux, L., Desbois, P., Lamotte, L., Duvillié, B., Cordonnier, N., Jackerott, M., Jami, J., Bucchini, D., & Joshi, R. L. (2001) · Diabetes · doi:10.2337/diabetes.50.2007.s150 · Cited by 137

Mapping of murine diabetogenic gene mody on chromosome 7 at D7Mit258 and its involvement in pancreatic islet and beta cell development during the perinatal period.

Kayo, T., & Koizumi, A. (1998) · Journal of Clinical Investigation · doi:10.1172/jci1842 · Cited by 95

Induction of CHOP and apoptosis by nitric oxide in p53‐deficient microglial cells

Kawahara, K., Oyadomari, S., Gotoh, T., Kohsaka, S., Nakayama, H., & Mori, M. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)02898-8 · Cited by 95

Pancreatic Expression and Secretion of Human Islet Amyloid Polypeptide in a Transgenic Mouse

D’Alessio, D. A., Verchere, C. B., Kahn, S. E., Hoagland, V. D., Baskin, D. G., Palmiter, R. D., & Ensinck, J. W. (1994) · Diabetes · doi:10.2337/diab.43.12.1457 · Cited by 93

Chronic overproduction of islet amyloid polypeptide/amylin in transgenic mice: lysosomal localization of human islet amyloid polypeptide and lack of marked hyperglycaemia or hyperinsulinaemia

Höppener, J. W. M., Verbeek, J. S., de Koning, E. J. P., Oosterwijk, C., van Hulst, K. L., Visser-Vernooy, H. J., Hofhuis, F. M., van Gaalen, S., Berends, M. J. H., Hackeng, W. H. L., et al. (1993) · Diabetologia · doi:10.1007/bf00400803 · Cited by 81

Effect of nitric oxide on endoplasmic reticulum calcium homeostasis, protein synthesis and energy metabolism

Doutheil, J., Althausen, S., Treiman, M., & Paschen, W. (2000) · Cell Calcium · doi:10.1054/ceca.1999.0099 · Cited by 72

AUTOPSY FINDINGS IN THE WOLCOTT-RALLISON SYNDROME

Thornton, C., Carson, D. J., & Stewart, F. J. (1997) · Pediatric Pathology & Laboratory Medicine · doi:10.1080/15513819709168589 · Cited by 71

Islet amyloid polypeptide in the islets of Langerhans: friend or foe?

Gebré‐Medhin, S., Olofsson, C. S., & Mulder, H. (2000) · Diabetologia · doi:10.1007/s001250051364 · Cited by 60

Autopsy Findings in the Wolcott-Rallison Syndrome

Thornton, C. M., Carson, D. J., & Stewart, F. A. (1997) · Fetal and Pediatric Pathology · doi:10.3109/15513819709168589 · Cited by 9

Type 2 diabetes as an inflammatory disease

Donath, M. Y., & Shoelson, S. E. (2011) · Nature Reviews Immunology · doi:10.1038/nri2925 · Cited by 3,737

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 2,879

Endoplasmic reticulum stress: cell life and death decisions

Xu, C. (2005) · Journal of Clinical Investigation · doi:10.1172/jci26373 · Cited by 2,291

Cell death and endoplasmic reticulum stress: disease relevance and therapeutic opportunities

Kim, I., Xu, W., & Reed, J. C. (2008) · Nature Reviews Drug Discovery · doi:10.1038/nrd2755 · Cited by 1,840

ER stress and diseases

Yoshida, H. (2007) · The FEBS Journal · doi:10.1111/j.1742-4658.2007.05639.x · Cited by 1,086

Endoplasmic reticulum stress-mediated apoptosis in pancreatic β-cells

Oyadomari, S., Araki, E., & Mori, M. (2002) · APOPTOSIS · doi:10.1023/a:1016175429877 · Cited by 519

Identification and characterization of the endoplasmic reticulum (ER)-stress pathways in pancreatic beta-cells

Pirot, P., Cardozo, A. K., & Eizirik, D. L. (2007)

Endoplasmic reticulum stress in β-cells and development of diabetes

Fonseca, S. G., Burcin, M. M., Gromada, J., & Urano, F. (2009) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2009.07.003 · Cited by 162

Endoplasmic reticulum stress in beta-cells and development of diabetes

Fonseca, S. G., Burcin, M., Gromada, J., & Urano, F. (2009) · eScholarship@UMassChan · Cited by 2

Relationship between endoplasmic reticulum stress and apoptosis of pancreatic β-cells

Jin-han, Z. (2015)