Control of mRNA translation preserves endoplasmic reticulum function in beta cells and maintains glucose homeostasis

Global and societal implications of the diabetes epidemic

Zimmet, P., Alberti, K. G. M. M., & Shaw, J. (2001) · Nature · doi:10.1038/414782a · Cited by 5,883

Two defects contribute to hypothalamic leptin resistance in mice with diet-induced obesity

El-Haschimi, K., Pierroz, D. D., Hileman, S. M., Bjørbæk, C., & Flier, J. S. (2000) · Journal of Clinical Investigation · doi:10.1172/jci9842 · Cited by 887

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

Phosphorylation of initiation factor 2α by protein kinase GCN2 mediates gene-specific translational control of GCN4 in yeast

Dever, T. E., Feng, L., Wek, R. C., Cigan, A. M., Donahue, T. F., & Hinnebusch, A. G. (1992) · Cell · doi:10.1016/0092-8674(92)90193-g · Cited by 776

Mitochondrial function in normal and diabetic β-cells

Maechler, P., & Wollheim, C. B. (2001) · Nature · doi:10.1038/414807a · Cited by 519

Glucose stimulates proinsulin biosynthesis by a dose-dependent recruitment of pancreatic beta cells

Schuit, F. C., In't Veld, P. A., & Pipeleers, D. G. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.11.3865 · Cited by 308

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

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

Molecular and metabolic mechanisms of insulin resistance and β-cell failure in type 2 diabetes

Muoio, D. M., & Newgard, C. B. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2327 · Cited by 1,177

ER stress and diseases

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

Adipose tissue and insulin resistance in obese

Ahmed, B., Sultana, R., & Greene, M. W. (2021) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2021.111315 · Cited by 1,047

Autophagy—a key player in cellular and body metabolism

Kim, K. H., & Lee, M.-S. (2014) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2014.35 · Cited by 963

Endoplasmic Reticulum Stress Plays a Central Role in Development of Leptin Resistance

Ozcan, L., Ergin, A. S., Lu, A., Chung, J., Sarkar, S., Nie, D., Myers, M. G., & Ozcan, U. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2008.12.004 · Cited by 875

From acute ER stress to physiological roles of the Unfolded Protein Response

Wu, J., & Kaufman, R. J. (2006) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4401840 · Cited by 868

Endoplasmic reticulum stress contributes to beta cell apoptosis in type 2 diabetes

Laybutt, D. R., Preston, A. M., Åkerfeldt, M. C., Kench, J. G., Busch, A. K., Biankin, A. V., & Biden, T. J. (2007) · Diabetologia · doi:10.1007/s00125-006-0590-z · Cited by 830

Chronic Palmitate But Not Oleate Exposure Induces Endoplasmic Reticulum Stress, Which May Contribute to INS-1 Pancreatic β-Cell Apoptosis

Karaskov, E., Scott, C., Zhang, L., Teodoro, T., Ravazzola, M., & Volchuk, A. (2006) · Endocrinology · doi:10.1210/en.2005-1494 · Cited by 573

Reshaping endoplasmic reticulum quality control through the unfolded protein response

Wiseman, R. L., Mesgarzadeh, J. S., & Hendershot, L. M. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.03.025 · Cited by 441

The endoplasmic reticulum in pancreatic beta cells of type 2 diabetes patients

Marchetti, P., Bugliani, M., Lupi, R., Marselli, L., Masini, M., Boggi, U., Filipponi, F., Weir, G. C., Eizirik, D. L., & Cnop, M. (2007) · Diabetologia · doi:10.1007/s00125-007-0816-8 · Cited by 413

That which does not kill me makes me stronger: adapting to chronic ER stress

Rutkowski, D. T., & Kaufman, R. J. (2007) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2007.09.003 · Cited by 398

Endoplasmic reticulum stress and pancreatic β-cell death

Fonseca, S. G., Gromada, J., & Urano, F. (2011) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2011.02.008 · Cited by 384

Molecular Events Linking Oxidative Stress and Inflammation to Insulin Resistance and β-Cell Dysfunction

Keane, K. N., Cruzat, V. F., Carlessi, R., de Bittencourt, P. I. H., & Newsholme, P. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2015/181643 · Cited by 383

Translation Attenuation through eIF2α Phosphorylation Prevents Oxidative Stress and Maintains the Differentiated State in β Cells

Back, S. H., Scheuner, D., Han, J., Song, B., Ribick, M., Wang, J., Gildersleeve, R. D., Pennathur, S., & Kaufman, R. J. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2009.06.002 · Cited by 366

Endoplasmic Reticulum Stress: Its Role in Disease and Novel Prospects for Therapy

Schönthal, A. H. (2012) · Scientifica · doi:10.6064/2012/857516 · Cited by 353

Insulin crystallization depends on zinc transporter ZnT8 expression, but is not required for normal glucose homeostasis in mice

Lemaire, K., Ravier, M. A., Schraenen, A., Creemers, J. W. M., Van de Plas, R., Granvik, M., Van Lommel, L., Waelkens, E., Chimienti, F., Rutter, G. A., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0906587106 · Cited by 330

Pleiotropic Effects of GLP-1 and Analogs on Cell Signaling, Metabolism, and Function

Rowlands, J., Heng, J., Newsholme, P., & Carlessi, R. (2018) · Frontiers in Endocrinology · doi:10.3389/fendo.2018.00672 · Cited by 302

HSPA5 Gene encoding Hsp70 chaperone BiP in the endoplasmic reticulum

Wang, J., Lee, J., Liem, D., & Ping, P. (2017) · Gene · doi:10.1016/j.gene.2017.03.005 · Cited by 308

Selective Inhibition of Eukaryotic Translation Initiation Factor 2α Dephosphorylation Potentiates Fatty Acid-induced Endoplasmic Reticulum Stress and Causes Pancreatic β-Cell Dysfunction and Apoptosis

Cnop, M., Ladriere, L., Hekerman, P., Ortis, F., Cardozo, A. K., Dogusan, Z., Flamez, D., Boyce, M., Yuan, J., & Eizirik, D. L. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m607627200 · Cited by 289

Autophagy deficiency in beta cells leads to compromised unfolded protein response and progression from obesity to diabetes in mice

Quan, W., Hur, K. Y., Lim, Y., Oh, S. H., Lee, J.-C., Kim, K. H., Kim, G. H., Kim, S.-W., Kim, H. L., Lee, M.-K., et al. (2012) · Diabetologia · doi:10.1007/s00125-011-2350-y · Cited by 184

Intrinsic Regulators of Pancreatic β-Cell Proliferation

Heit, J. J., Karnik, S. K., & Kim, S. K. (2006) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.22.010305.104425 · Cited by 165

New mechanisms of metformin action: Focusing on mitochondria and the gut

Hur, K. Y., & Lee, M. (2015) · Journal of Diabetes Investigation · doi:10.1111/jdi.12328 · Cited by 161

Inside the β Cell: Molecular Stress Response Pathways in Diabetes Pathogenesis

Kulkarni, A., Muralidharan, C., May, S. C., Tersey, S. A., & Mirmira, R. G. (2022) · Endocrinology · doi:10.1210/endocr/bqac184 · Cited by 95

CPT1A Over-Expression Increases Reactive Oxygen Species in the Mitochondria and Promotes Antioxidant Defenses in Prostate Cancer

Joshi, M., Kim, J., D’Alessandro, A., Monk, E., Bruce, K., Elajaili, H., Nozik-Grayck, E., Goodspeed, A., Costello, J. C., & Schlaepfer, I. R. (2020) · Cancers · doi:10.3390/cancers12113431 · Cited by 54