Endoplasmic Reticulum Stress and Diabetes Mellitus.

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

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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

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 · see citing works

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

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Aggresomes, inclusion bodies and protein aggregation

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

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

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

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

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

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

Coupling endoplasmic reticulum stress to the cell death program

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

Cross-Talk between Two Cysteine Protease Families

Nakagawa, T., & Yuan, J. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.150.4.887 · Cited by 1,164 · see citing works

CHOP, a novel developmentally regulated nuclear protein that dimerizes with transcription factors C/EBP and LAP and functions as a dominant-negative inhibitor of gene transcription.Preprint

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

Heat shock, stress proteins, chaperones, and proteotoxicity

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

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 · 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

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

β-Cell death during progression to diabetes

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

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 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

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

Oyadomari, S., Koizumi, A., Takeda, K., Gotoh, T., Akira, S., Araki, E., & Mori, M. (2002) · Journal of Clinical Investigation · doi:10.1172/jci14550 · Cited by 858 · see citing works

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 819 · 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

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

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

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

Nitric oxide-induced apoptosis in pancreatic β cells is mediated by the endoplasmic reticulum stress pathway

Oyadomari, S., Takeda, K., Takiguchi, M., Gotoh, T., Matsumoto, M., Wada, I., Akira, S., Araki, E., & Mori, M. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.191207498 · Cited by 599 · see citing works

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 · 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

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 · see citing works

Endoplasmic reticulum stress-mediated apoptosis in pancreatic β-cells

Oyadomari, S., Araki, E., & Mori, M. (2002) · APOPTOSIS · doi:10.1023/a:1016175429877 · Cited by 517 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 294 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 84 · see citing works

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

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

Gebre-Medhin, S., Olofsson, C., & Mulder, H. (2000) · Diabetologia · doi:10.1007/s001250051364 · Cited by 67 · see citing works

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 64 · see citing works

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 · see citing works

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 · see citing works

Roles of CHOP/GADD153 in endoplasmic reticulum stress

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

Endoplasmic reticulum stress: cell life and death decisions

Xu, C. (2005) · Journal of Clinical Investigation · doi:10.1172/jci26373 · Cited by 2,260 · see citing works

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 1,816 · see citing works

ER stress and diseases

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

Decreased beta-cell mass in diabetes: significance, mechanisms and therapeutic implications

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A review of the mammalian unfolded protein response

Chakrabarti, A., Chen, A. W., & Varner, J. D. (2011) · Biotechnology and Bioengineering · doi:10.1002/bit.23282 · Cited by 408 · see citing works

Mechanisms of β-Cell Death in Type 2 Diabetes

Donath, M. Y., Ehses, J. A., Maedler, K., Schumann, D. M., Ellingsgaard, H., Eppler, E., & Reinecke, M. (2005) · Diabetes · doi:10.2337/diabetes.54.suppl_2.s108 · Cited by 444 · see citing works

Biology of Endoplasmic Reticulum Stress in the Heart

Groenendyk, J., Sreenivasaiah, P. K., Kim, D. H., Agellon, L. B., & Michalak, M. (2010) · Circulation Research · doi:10.1161/circresaha.110.227033 · Cited by 314 · see citing works

Arabidopsis Ubiquitin Conjugase UBC32 Is an ERAD Component That Functions in Brassinosteroid-Mediated Salt Stress Tolerance

Cui, F., Liu, L., Zhao, Q., Zhang, Z., Li, Q., Lin, B., Wu, Y., Tang, S., & Xie, Q. (2012) · The Plant Cell · doi:10.1105/tpc.111.093062 · Cited by 269 · see citing works

Endoplasmic Reticulum Stress Stimulates the Expression of Cyclooxygenase-2 through Activation of NF-κB and pp38 Mitogen-activated Protein Kinase

Hung, J., Su, I., Lei, H.-Y., Wang, H.-C., Lin, W.-C., Chang, W., Huang, W., Chang, W., Chang, Y.-S., Chen, C., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m403568200 · Cited by 257 · see citing works

Endoplasmic Reticulum Stress in the Heart

Glembotski, C. C. (2007) · Circulation Research · doi:10.1161/circresaha.107.161273 · Cited by 229 · see citing works

The integrated stress response prevents demyelination by protecting oligodendrocytes against immune-mediated damage

Lin, W., Bailey, S. L., Ho, H., Harding, H. P., Ron, D., Miller, S. D., & Popko, B. (2007) · Journal of Clinical Investigation · doi:10.1172/jci29571 · Cited by 200 · see citing works

Evaluation of the effects of anthocyanins in type 2 diabetes

Sancho, R. A. S., & Pastore, G. M. (2011) · Food Research International · doi:10.1016/j.foodres.2011.11.021 · Cited by 193 · see citing works

Stress and the inflammatory process: a major cause of pancreatic cell death in type 2 diabetes

Novials, A., Montané, J., & Cadavez, L. (2014) · Diabetes Metabolic Syndrome and Obesity · doi:10.2147/dmso.s37649 · Cited by 160 · see citing works

The endoplasmic reticulum-associated degradation is necessary for plant salt tolerance

Liu, L., Cui, F., Li, Q., Yin, B., Zhang, H., Lin, B., Wu, Y., Xia, R., Tang, S., & Xie, Q. (2010) · Cell Research · doi:10.1038/cr.2010.181 · Cited by 154 · see citing works

RyR2 and Calpain-10 Delineate a Novel Apoptosis Pathway in Pancreatic Islets

Johnson, J. D., Han, Z., Otani, K., Ye, H., Zhang, Y., Wu, H., Horikawa, Y., Misler, S., Bell, G. I., & Polonsky, K. S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m401216200 · Cited by 145 · see citing works

PERK (EIF2AK3) Regulates Proinsulin Trafficking and Quality Control in the Secretory Pathway

Gupta, S., McGrath, B. C., & Cavener, D. R. (2010) · Diabetes · doi:10.2337/db09-1064 · Cited by 136 · see citing works

Type 2 diabetes mellitus as a conformational disease.

Hayden, M. R., Tyagi, S. C., Kerklo, M. M., & Nicolls, M. R. (2005) · PubMed · Cited by 122 · see citing works

O-GlcNAc signaling attenuates ER stress-induced cardiomyocyte death

Ngoh, G. A., Hamid, T., Prabhu, S. D., & Jones, S. P. (2009) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00553.2009 · Cited by 121 · see citing works

Imatinib Mesylate Reduces Endoplasmic Reticulum Stress and Induces Remission of Diabetes in db/db Mice

Han, M. S., Chung, K. W., Cheon, H. G., Rhee, S. D., Yoon, C., Lee, M., Kim, K., & Lee, M. (2009) · Diabetes · doi:10.2337/db08-0080 · Cited by 117 · see citing works

β cell ER stress and the implications for immunogenicity in type 1 diabetes

Marré, M. L., James, E. A., & Piganelli, J. D. (2015) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2015.00067 · Cited by 112 · see citing works

CHOP plays a pivotal role in the astrocyte death induced by oxygen and glucose deprivation

Benavides, A., Pastor, M. D., Santos, P., Tranque, P., & Calvo, S. (2005) · Glia · doi:10.1002/glia.20242 · Cited by 107 · see citing works

Reactive Oxygen Species Promote Caspase-12 Expression and Tubular Apoptosis in Diabetic Nephropathy

Brezniceanu, M.-L., Lau, C. J., Godin, N., Chénier, I., Duclos, A. J., Ethier, J. H., Filep, J. G., Ingelfinger, J. R., Zhang, S., & Chan, J. S. D. (2010) · Journal of the American Society of Nephrology · doi:10.1681/asn.2009030242 · Cited by 107 · see citing works

Astragalus polysaccharides decreased the expression of PTP1B through relieving ER stress induced activation of ATF6 in a rat model of type 2 diabetes

Wang, N., Deling, Z., Mao, X., Zou, F., Jin, H., & Ouyang, J. (2009) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2009.03.001 · Cited by 106 · see citing works

PERK-opathies: An Endoplasmic Reticulum Stress Mechanism Underlying Neurodegeneration

Bell, M. C., Meier, S. E., Ingram, A., & Abisambra, J. F. (2015) · Current Alzheimer Research · doi:10.2174/1567205013666151218145431 · Cited by 98 · see citing works

Modifying Enzymes Are Elicited by ER Stress, Generating Epitopes That Are Selectively Recognized by CD4+ T Cells in Patients With Type 1 Diabetes

Marré, M. L., McGinty, J. W., Chow, I., DeNicola, M., Beck, N. W., Kent, S. C., Powers, A. C., Bottino, R., Harlan, D. M., Greenbaum, C. J., et al. (2018) · Diabetes · doi:10.2337/db17-1166 · Cited by 92 · see citing works

Inherent ER stress in pancreatic islet β cells causes self-recognition by autoreactive T cells in type 1 diabetes

Marré, M. L., Profozich, J., Coneybeer, J., Geng, X., Bertera, S., Ford, M., Trucco, M., & Piganelli, J. D. (2016) · Journal of Autoimmunity · doi:10.1016/j.jaut.2016.04.009 · Cited by 84 · see citing works

Endoplasmic Reticulum Stress-activated C/EBP Homologous Protein Enhances Nuclear Factor-κB Signals via Repression of Peroxisome Proliferator-activated Receptor γ

Park, S., Choi, H. J., Yang, H. J., Do, K. H., Kim, J., Lee, D. W., & Moon, Y. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.136259 · Cited by 83 · see citing works

The Group VIA Calcium-Independent Phospholipase A2 Participates in ER Stress-Induced INS-1 Insulinoma Cell Apoptosis by Promoting Ceramide Generation via Hydrolysis of Sphingomyelins by Neutral Sphingomyelinase

Lei, X., Zhang, S., Bohrer, A., Bao, S. S., Song, H., & Ramanadham, S. (2007) · Biochemistry · doi:10.1021/bi700017z · Cited by 83 · see citing works

Too much of a good thing: why it is bad to stimulate the beta cell to secrete insulin

Aston‐Mourney, K., Proietto, J., Morahan, G., & Andrikopoulos, S. (2008) · Diabetologia · doi:10.1007/s00125-008-0930-2 · Cited by 79 · see citing works

T Cell Epitopes and Post-Translationally Modified Epitopes in Type 1 Diabetes

McGinty, J. W., Marré, M. L., Bajzik, V., Piganelli, J. D., & James, E. A. (2015) · Current Diabetes Reports · doi:10.1007/s11892-015-0657-7 · Cited by 77 · see citing works

Immune recognition of citrullinated epitopes

Nguyen, H. Q. T., & James, E. A. (2016) · Immunology · doi:10.1111/imm.12640 · Cited by 73 · see citing works

Misfolded Proinsulin Affects Bystander Proinsulin in Neonatal Diabetes

Hodish, I., Liu, M. R., Rajpal, G., Larkin, D. D., Holz, R. W., Adams, A. M., Liu, L., & Arvan, P. R. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.038042 · Cited by 72 · see citing works

Apoptosis of pancreatic β-cells in Type 1 diabetes

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Insulin-Like Growth Factor (IGF)-I/IGF-Binding Protein-3 Complex: Therapeutic Efficacy and Mechanism of Protection against Type 1 Diabetes

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Endoplasmic Reticulum Stress-Mediated Apoptotic Pathway Is Involved in Corpus Luteum Regression in Rats

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Environmental Factors Contribute to β Cell Endoplasmic Reticulum Stress and Neo-Antigen Formation in Type 1 Diabetes

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Swimming Differentially Affects T2DM-Induced Skeletal Muscle ER Stress and Mitochondrial Dysfunction Related to MAM

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Considerations for Defining Cytokine Dose, Duration, and Milieu That Are Appropriate for Modeling Chronic Low-Grade Inflammation in Type 2 Diabetes

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High Glucose Exposure Promotes Activation of Protein Phosphatase 2A in Rodent Islets and INS-1 832/13 β-Cells by Increasing the Posttranslational Carboxylmethylation of Its Catalytic Subunit

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Oxidative stress induces unfolding protein response and inflammation in nasal polyposis

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Tracking cellular stress with labeled FMAU reflects changes in mitochondrial TK2

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Glucose regulated proteins 78 protects insulinoma cells (NIT-1) from death induced by streptozotocin, cytokines or cytotoxic T lymphocytes

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The Role of β‐Cell Dysfunction in the Cardiometabolic Syndrome

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Melatonin ameliorates myocardial apoptosis by suppressing endoplasmic reticulum stress in rats with long‑term diabetic cardiomyopathy

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Comparison of the effect of individual saturated and unsaturated fatty acids on cell growth and death induction in the human pancreatic β-cell line NES2Y

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Emerging Roles for Mesencephalic Astrocyte-Derived Neurotrophic Factor (MANF) in Pancreatic Beta Cells and Diabetes

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Is cystic fibrosis-related diabetes an apoptotic consequence of ER stress in pancreatic cells?

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Administration of mulberry leaves maintains pancreatic β-cell mass in obese/type 2 diabetes mellitus mouse model

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Ginkgolide B‑induced AMPK pathway activation protects astrocytes by regulating endoplasmic reticulum stress, oxidative stress and energy metabolism induced by Aβ1‑42

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Estradiol Prevents High Glucose-Induced β-cell Apoptosis by Decreased BTG2 Expression

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Hyperglycemia magnifies bupivacaine‐induced cell apoptosis triggered by mitochondria dysfunction and endoplasmic reticulum stress

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Bushen Zhuangjin decoction inhibits TM-induced chondrocyte apoptosis mediated by endoplasmic reticulum stress

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Soluble and insoluble protein aggregates, endoplasmic reticulum stress, and vascular dysfunction in Alzheimer’s disease and cardiovascular diseases

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The immunosuppressive and protective ability of glucose-regulated protein 78 for improvement of alloimmunity in β cell transplantation

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Baldspot/ELOVL6 is a conserved modifier of disease and the ER stress response

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GANAB and N-Glycans Substrates Are Relevant in Human Physiology, Polycystic Pathology and Multiple Sclerosis: A Review

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PERK in POMC neurons connects celastrol with metabolism

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Endoplasmic reticulum stress in β-cells and development of diabetes

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