Uncoupling protein-2 negatively regulates insulin secretion and is a major link between obesity, β-cell dysfunction, and type 2 diabetes.

Cellular mechanisms of insulin resistance

Shulman, G. I. (2000) · Journal of Clinical Investigation · doi:10.1172/jci10583 · Cited by 2,714 · see citing works

The Triumvirate: β-Cell, Muscle, Liver: A Collusion Responsible for NIDDM

DeFronzo, R. A. (1988) · Diabetes · doi:10.2337/diab.37.6.667 · Cited by 2,456 · see citing works

THE MITOCHONDRIAL ELECTRON TRANSPORT AND OXIDATIVE PHOSPHORYLATION SYSTEM

Hatefi, Y. (1985) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.54.070185.005055 · Cited by 1,650 · see citing works

Uncoupling protein-2: a novel gene linked to obesity and hyperinsulinemia

Fleury, C., Neverova, M., Collins, S., Raimbault, S., Champigny, O., Lévi-Meyrueis, C., Bouillaud, F., Seldin, M. F., Surwit, R. S., Ricquier, D., et al. (1997) · Nature Genetics · doi:10.1038/ng0397-269 · Cited by 1,630 · see citing works

Mice lacking mitochondrial uncoupling protein are cold-sensitive but not obese

Enerbäck, S., Jacobsson, A., Simpson, E. M., Guerra, C., Yamashita, H., Harper, M.-E., & Kozak, L. P. (1997) · Nature · doi:10.1038/387090a0 · Cited by 1,379 · see citing works

Lipotoxicity in the Pathogenesis of Obesity-Dependent NIDDM: Genetic and Clinical Implications

Unger, R. H. (1995) · Diabetes · doi:10.2337/diab.44.8.863 · Cited by 1,100 · see citing works

Disruption of the uncoupling protein-2 gene in mice reveals a role in immunity and reactive oxygen species production

Arsenijevic, D., Onuma, H., Pecqueur, C., Raimbault, S., Manning, B. S., Miroux, B., Couplan, E., Alves‐Guerra, M., Goubern, M., Surwit, R. S., et al. (2000) · Nature Genetics · doi:10.1038/82565 · Cited by 1,079 · see citing works

Uncoupling protein‐3: a new member of the mitochondrial carrier family with tissue‐specific expression

Boss, O., Samec, S., Paoloni‐Giacobino, A., Rossier, C., Dulloo, A. G., Seydoux, J., Muzzin, P., & Giacobino, J. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00384-0 · Cited by 1,041 · see citing works

Uncoupling: new approaches to an old problem of bioenergetics

Skulachev, V. P. (1998) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(97)00091-1 · Cited by 893 · see citing works

Uncoupling Protein-3 Is a Mediator of Thermogenesis Regulated by Thyroid Hormone, β3-Adrenergic Agonists, and Leptin

Gong, D., He, Y., Karas, M., & Reitman, M. L. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.39.24129 · Cited by 740 · see citing works

UCP3: An Uncoupling Protein Homologue Expressed Preferentially and Abundantly in Skeletal Muscle and Brown Adipose Tissue

Vidal‐Puig, A., Solanes, G., Grujić, D., Flier, J. S., & Lowell, B. B. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.6740 · Cited by 711 · see citing works

Energy metabolism in uncoupling protein 3 gene knockout mice

Vidal-Puig, A. J., Grujic, D., Zhang, C.-Y., Hagen, T., Boss, O., Ido, Y., Szczepanik, A., Wade, J., Mootha, V., Cortright, R., et al. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m910179199 · Cited by 677 · see citing works

Role of apoptosis in failure of beta-cell mass compensation for insulin resistance and beta-cell defects in the male Zucker diabetic fatty rat

Pick, A., Clark, J., Kubstrup, C., Levisetti, M., Pugh, W., Bonner-Weir, S., & Polonsky, K. S. (1998) · Diabetes · doi:10.2337/diabetes.47.3.358 · Cited by 551 · see citing works

Defective insulin secretion and enhanced insulin action in KATP channel-deficient mice.

Miki, T., Nagashima, K., Tashiro, F., Kotake, K., Yoshitomi, H., Tamamoto, A., Gonoi, T., Iwanaga, T., Miyazaki, J., & Seino, S. (1998) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.95.18.10402 · Cited by 541 · see citing works

Effects of fat on insulin-stimulated carbohydrate metabolism in normal men.

Boden, G., Jadali, F., White, J. V., Liang, Y. T., Mozzoli, M. A., Chen, X., Coleman, E., & Smith, C. R. (1991) · Journal of Clinical Investigation · doi:10.1172/jci115399 · Cited by 500 · see citing works

Cloning and Characterization of an Uncoupling Protein Homolog: A Potential Molecular Mediator of Human Thermogenesis

Gimeno, R. E., Dembski, M., Weng, X., Deng, N., Shyjan, A. W., Gimeno, C. J., Iris, F., Ellis, S. J., Woolf, E. A., & Tartaglia, L. A. (1997) · Diabetes · doi:10.2337/diab.46.5.900 · Cited by 496 · see citing works

ATP-sensitive K+ channels and insulin secretion: their role in health and disease

Ashcroft, F., & Gribble, F. (1999) · Diabetologia · doi:10.1007/s001250051247 · Cited by 435 · see citing works

Lack of Obesity and Normal Response to Fasting and Thyroid Hormone in Mice Lacking Uncoupling Protein-3

Gong, D., Monemdjou, S., Gavrilova, O., Leon, L. R., Marcus‐Samuels, B., Chou, C. J., Everett, C. A., Kozak, L. P., Li, C., Deng, C., et al. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m910177199 · Cited by 385 · see citing works

A 48-hour Lipid Infusion in the Rat Time-Dependently Inhibits Glucose-Induced Insulin Secretion and B Cell Oxidation Through a Process Likely Coupled to Fatty Acid Oxidation*

Sako, Y., & Grill, V. (1990) · Endocrinology · doi:10.1210/endo-127-4-1580 · Cited by 373 · see citing works

Sur1 Knockout Mice

Seghers, V. J., Nakazaki, M., DeMayo, F. J., Aguilar‐Bryan, L., & Bryan, J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.13.9270 · Cited by 366 · see citing works

Structure and function of the uncoupling protein from brown adipose tissue

Klingenberg, M., & Huang, S. (1999) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/s0005-2736(98)00232-6 · Cited by 359 · see citing works

Adipose tissue is required for the antidiabetic, but not for the hypolipidemic, effect of thiazolidinediones

Chao, L. C., Marcus‐Samuels, B., Mason, M. M., Moitra, J., Vinson, C., Arioǧlu, E., Gavrilova, O., & Reitman, M. L. (2000) · Journal of Clinical Investigation · doi:10.1172/jci11245 · Cited by 356 · see citing works

Diabetes-Obesity Syndromes in Mice

Coleman, D. L. (1982) · Diabetes · doi:10.2337/diab.31.1.s1 · Cited by 354 · see citing works

Cloning and expression of the mouse pgk-1 gene and the nucleotide sequence of its promoter

Adra, C. N., Boer, P. H., & McBurney, M. W. (1987) · Gene · doi:10.1016/0378-1119(87)90214-9 · Cited by 337 · see citing works

Pancreatic beta-cell glucokinase: closing the gap between theoretical concepts and experimental realities.

Matschinsky, F. M., Gläser, B., & Magnuson, M. A. (1998) · Diabetes · doi:10.2337/diabetes.47.3.307 · Cited by 334 · see citing works

Redistribution of substrates to adipose tissue promotes obesity in mice with selective insulin resistance in muscle

Kim, J. K., Michael, M. D., Previs, S. F., Peroni, O. D., Mauvais-Jarvis, F., Neschen, S., Kahn, B. B., Kahn, C. R., & Shulman, G. I. (2000) · Journal of Clinical Investigation · doi:10.1172/jci8305 · Cited by 331 · see citing works

Lilly Lecture: Molecular Mechanisms of Insulin Resistance: Lessons From Patients With Mutations in the Insulin-Receptor Gene

Taylor, S. I. (1992) · Diabetes · doi:10.2337/diab.41.11.1473 · Cited by 325 · see citing works

Brown adipose tissue thermogenesis and obesity

Himms‐Hagen, J. (1989) · Progress in Lipid Research · doi:10.1016/0163-7827(89)90009-x · Cited by 324 · see citing works

Transport function and regulation of mitochondrial uncoupling proteins 2 and 3

Jabůrek, M., Vařecha, M., Gimeno, R. E., Dembski, M., Ježek, P., Zhang, M., Burn, P., Tartaglia, L. A., & Garlid, K. D. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.37.26003 · Cited by 321 · see citing works

Uncoupling proteins 2 and 3 are highly active H ⁺ transporters and highly nucleotide sensitive when activated by coenzyme Q (ubiquinone)

Echtay, K. S., Winkler, E., Frischmuth, K., & Klingenberg, M. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.98.4.1416 · Cited by 313 · see citing works

Mechanisms by which glucose can control insulin release independently from its action on adenosine triphosphate-sensitive K+ channels in mouse B cells.

Gembal, M., Detimary, P., Gilon, P., Gao, Z. Y., & Henquin, J. C. (1993) · Journal of Clinical Investigation · doi:10.1172/jci116308 · Cited by 260 · see citing works

Long term exposure to fatty acids and ketones inhibits B-cell functions in human pancreatic islets of Langerhans

Zhou, Y. P. (1995) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.80.5.1584 · Cited by 243 · see citing works

The importance of the β-cell in the pathogenesis of type 2 diabetes mellitus

Kahn, S. E. (2000) · The American Journal of Medicine · doi:10.1016/s0002-9343(00)00336-3 · Cited by 242 · see citing works

Overexpression of uncoupling protein 2 inhibits glucose-stimulated insulin secretion from rat islets.

Chan, C. B., MacDonald, P. E., Saleh, M. C., Johns, D. C., Marbàn, E., & Wheeler, M. B. (1999) · Diabetes · doi:10.2337/diabetes.48.7.1482 · Cited by 242 · see citing works

Uncoupling Protein 2: A Possible Link Between Fatty Acid Excess and Impaired Glucose-Induced Insulin Secretion?

Davis‐Lameloise, N., Muzzin, P., Prentki, M., & Assimacopoulos‐Jeannet, F. (2001) · Diabetes · doi:10.2337/diabetes.50.4.803 · Cited by 226 · see citing works

Retinoids activate proton transport by the uncoupling proteins UCP1 and UCP2

Rial, E., González‐Barroso, M., Fleury, C., Iturrizaga, S., Sanchı́s, D., Jiménez‐Jiménez, J., Ricquier, D., Goubern, M., & Bouillaud, F. (1999) · The EMBO Journal · doi:10.1093/emboj/18.21.5827 · Cited by 195 · see citing works

Normal development and growth of mice carrying a targeted disruption of the alpha 1 retinoic acid receptor gene.

Li, E., Sucov, H. M., Lee, K., Evans, R. M., & Jaenisch, R. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.4.1590 · Cited by 188 · see citing works

Pancreatic Islets in Mice with the Obese-hyperglycemic Syndrome: Lack of Effect of Carbutamide

Gepts, W., Christophe, B. J., & Mayer, J. (1960) · Diabetes · doi:10.2337/diab.9.1.63 · Cited by 175 · see citing works

Lipids up-regulate uncoupling protein 2 expression in rat hepatocytes

Cortez‐Pinto, H., Lin, H. Z., Yang, S. Q., Odwin-DaCosta, S., & Diehl, A. M. (1999) · Gastroenterology · doi:10.1016/s0016-5085(99)70022-3 · Cited by 154 · see citing works

Effects of Lipid on Basal Carbohydrate Metabolism in Normal Men

Boden, G. H., & Jadali, F. (1991) · Diabetes · doi:10.2337/diab.40.6.686 · Cited by 126 · see citing works

THE DISTRIBUTION PATTERN OF THE PANCREATIC ISLET VOLUME IN NORMAL AND HYPERGLYCAEMIC MICE

Hellman, B., Brolin, S. E., Hellerström, C., et al. (1961) · European Journal of Endocrinology · doi:10.1530/acta.0.0360609 · Cited by 124 · see citing works

Marked Improvement of Glucose Homeostasis in Diabetic ob/ob Mice Given Oral Vanadate

Brichard, S. M., Bailey, C. J., & Henquin, J. (1990) · Diabetes · doi:10.2337/diab.39.11.1326 · Cited by 113 · see citing works

Assessment of uncoupling activity of uncoupling protein 3 using a yeast heterologous expression system

Zhang, C.-Y., Hagen, T., Mootha, V. K., Slieker, L. J., & Lowell, B. B. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00441-x · Cited by 109 · see citing works

Effects of Adenoviral Overexpression of Uncoupling Protein-2 and -3 on Mitochondrial Respiration in Insulinoma Cells**This work was supported by V.A. Medical Research Funds and NIH Grants DK-25295 and HD-29569.

Hong, Y., Fink, B. D., Dillon, J. S., & Sivitz, W. I. (2001) · Endocrinology · doi:10.1210/endo.142.1.7889 · Cited by 107 · see citing works

Long-Chain Fatty Acids Inhibit Acetyl-CoA Carboxylase Gene Expression in the Pancreatic β-Cell Line INS-1

Brun, T. A., Assimacopoulos-Jeannet, F., Corkey, B. E., et al. (1997) · Diabetes · doi:10.2337/diab.46.3.393 · Cited by 100 · see citing works

Lipid rather than glucose metabolism is implicated in altered insulin secretion caused by oleate in INS-1 cells

Segall, L., Davis‐Lameloise, N., Assimacopoulos‐Jeannet, F., Roche, E., Corkey, P., Thumelin, S., Corkey, B. E., & Prentki, M. (1999) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.1999.277.3.e521 · Cited by 90 · see citing works

Renal Metabolism of C-Peptide in Man*

Zavaroni, I., Deferrari, G., Lugari, R., et al. (1987) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jcem-65-3-494 · Cited by 84 · see citing works

Adenovirus-mediated overexpression of uncoupling protein-2 in pancreatic islets of Zucker diabetic rats increases oxidative activity and improves beta-cell function.

Wang, M. Y., Shimabukuro, M., Lee, Y., Trinh, K. Y., Chen, J., Newgard, C. B., & Unger, R. H. (1999) · Diabetes · doi:10.2337/diabetes.48.5.1020 · Cited by 72 · see citing works

Luminometric Assays of ATP, Phosphocreatine, and Creatine for Estimation of Free ADP and Free AMP

Ronner, P., Friel, E., Czerniawski, K., & Fränkle, S. (1999) · Analytical Biochemistry · doi:10.1006/abio.1999.4317 · Cited by 70 · see citing works

Recombinant human uncoupling protein‐3 increases thermogenesis in yeast cells

Hinz, W., Faller, B., Grueninger, S., Gazzotti, P., & Chiesi, M. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00331-2 · Cited by 68 · see citing works

The uncoupling proteins.

Muzzin, P. (2002) · PubMed · Cited by 63 · see citing works

AN INTEGRATED VIEW OF β-CELL DYSFUNCTION IN TYPE-II DIABETES

Poitout, D., & Robertson, M. D. (1996) · Annual Review of Medicine · doi:10.1146/annurev.med.47.1.69 · Cited by 62 · see citing works

Dietary Fatty Acids Up-Regulate the Expression of UCP2 in 3T3-L1 Preadipocytes

Reilly, J. M., & Thompson, M. P. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.3705 · Cited by 41 · see citing works

Mitochondrial Electron Transport and Oxidative Phosphorylation

(1999) · Mitochondria · doi:10.1002/0471223891.ch5 · Cited by 21 · see citing works

Blood Glucose and Serum Insulin Levels in Lean and Genetically Obese Mice

Beloff-Chain, A., Freund, N., & Rookledge, K. A. (1975) · Hormone and Metabolic Research · doi:10.1055/s-0028-1093730 · Cited by 18 · see citing works

Effect of pertussis toxin on islet insulin secretion in obese (fa/fa) Zucker rats

Cawthorn, E. G., & Chan, C. B. (1991) · Molecular and Cellular Endocrinology · doi:10.1016/0303-7207(91)90161-k · Cited by 17 · see citing works

Polymerase Chain Reaction‐Restriction Fragment Length Polymorphisms (PCR‐RFLP) and Electrophoretic Assays for the Mouse Obese (Lepob) Mutation

Chung, W. K., Chua, S. C., Lee, G., et al. (1997) · Obesity Research · doi:10.1002/j.1550-8528.1997.tb00291.x · Cited by 16 · see citing works

Peroxisome Proliferator-Activated Receptor-γ Coactivator 1α (PGC-1α): Transcriptional Coactivator and Metabolic Regulator

Puigserver, P., & Spiegelman, B. M. (2003) · Endocrine Reviews · doi:10.1210/er.2002-0012 · Cited by 2,076 · see citing works

Mitochondrial dysfunction and type 2 diabetes

Lowell, B. B., & Shulman, G. I. (2005) · Science · doi:10.1126/science.1104343 · Cited by 2,070 · see citing works

Superoxide activates mitochondrial uncoupling proteins

Echtay, K. S., Roussel, D., St-Pierre, J., Jekabsons, M. B., Cadenas, S., Stuart, J. A., Harper, J. A., Roebuck, S. J., Morrison, A., Pickering, S., et al. (2002) · Nature · doi:10.1038/415096a · Cited by 1,382 · see citing works

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 · see citing works

Glucolipotoxicity: fuel excess and β-cell dysfunction

Poitout, V., & Robertson, R. P. (2008) · Endocrine Reviews · doi:10.1210/er.2007-0023 · Cited by 1,092 · see citing works

Mitochondrial superoxide: production, biological effects, and activation of uncoupling proteins

Brand, M. D., Affourtit, C., Esteves, T. C., Green, K., Lambert, A. J., Miwa, S., Pakay, J. L., & Parker, N. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.05.034 · Cited by 1,032 · see citing works

Molecular mechanisms of ROS production and oxidative stress in diabetes

Newsholme, P., Cruzat, V. F., Keane, K. N., Carlessi, R., & de Bittencourt, P. I. H. (2016) · Biochemical Journal · doi:10.1042/bcj20160503c · Cited by 878 · see citing works

Mitochondrial proton and electron leaks

Jastroch, M., Divakaruni, A. S., Mookerjee, S., Treberg, J. R., & Brand, M. D. (2010) · Essays in Biochemistry · doi:10.1042/bse0470053 · Cited by 829 · see citing works

Reactive oxygen species in health and disease

Alfadda, A. A., & Sallam, R. M. (2012) · Journal of Biomedicine and Biotechnology · doi:10.1155/2012/936486 · Cited by 824 · see citing works

Physiological functions of the mitochondrial uncoupling proteins UCP2 and UCP3

Brand, M. D., & Esteves, T. C. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.06.002 · Cited by 785 · see citing works

Mitochondrial Dysfunction in Diabetes: From Molecular Mechanisms to Functional Significance and Therapeutic Opportunities

Sivitz, W. I., & Yorek, M. A. (2010) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.2531 · Cited by 742 · see citing works

Sirt1 Regulates Insulin Secretion by Repressing UCP2 in Pancreatic β Cells

Bordone, L., Motta, M. C., Picard, F., Robinson, A., Jhala, U. S., Apfeld, J., McDonagh, T., Lemieux, M., McBurney, M., Szilvasi, A., et al. (2005) · PLoS Biology · doi:10.1371/journal.pbio.0040031 · Cited by 715 · see citing works

UCP2 mediates ghrelin’s action on NPY/AgRP neurons by lowering free radicals

Andrews, Z. B., Liu, Z.-W., Walllingford, N., Erion, D. M., Borok, E., Friedman, J. M., Tschöp, M. H., Shanabrough, M., Cline, G., Shulman, G. I., et al. (2008) · Nature · doi:10.1038/nature07181 · Cited by 710 · see citing works

Glucose sensing by POMC neurons regulates glucose homeostasis and is impaired in obesity

Parton, L. E., Ye, C. P., Coppari, R., Enriori, P. J., Choi, B., Zhang, C.-Y., Xu, C., Vianna, C. R., Balthasar, N., Lee, C. E., et al. (2007) · Nature · doi:10.1038/nature06098 · Cited by 700 · see citing works

Thermogenic Mechanisms and Their Hormonal Regulation

Silva, J. E. (2006) · Physiological Reviews · doi:10.1152/physrev.00009.2005 · Cited by 687 · see citing works

The Role of Oxidative Stress and Hypoxia in Pancreatic Beta-Cell Dysfunction in Diabetes Mellitus

Gerber, P. A., & Rutter, G. A. (2017) · Antioxidants & Redox Signaling · doi:10.1089/ars.2016.6755 · Cited by 654 · see citing works

Redox regulation of mitochondrial function

Handy, D. E., & Loscalzo, J. (2012) · Antioxidants & Redox Signaling · doi:10.1089/ars.2011.4123 · Cited by 588 · see citing works

A signalling role for 4‐hydroxy‐2‐nonenal in regulation of mitochondrial uncoupling

Echtay, K. S., Esteves, T. C., Pakay, J. L., Jekabsons, M. B., Lambert, A. J., Portero‐Otín, M., Pamplona, R., Vidal‐Puig, A. J., Wang, S., Roebuck, S. J., et al. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg412 · Cited by 597 · see citing works

Mitochondrial uncoupling, ROS generation and cardioprotection

Cadenas, S. (2018) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2018.05.019 · Cited by 591 · see citing works

The role of mitochondria in the pathogenesis of type 2 diabetes

Patti, M.-E., & Corvera, S. (2010) · Endocrine Reviews · doi:10.1210/er.2009-0027 · Cited by 551 · see citing works

Hyperinsulinemia Drives Diet-Induced Obesity Independently of Brain Insulin Production

Mehran, A. E., Templeman, N. M., Brigidi, G. S., Lim, G. E., Chu, K.-Y., Hu, X., Botezelli, J. D., Asadi, A., Hoffman, B. G., Kieffer, T. J., et al. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.10.019 · Cited by 498 · see citing works

Prevention of mitochondrial oxidative damage as a therapeutic strategy in diabetes

Green, K., Brand, M. D., & Murphy, M. P. (2004) · Diabetes · doi:10.2337/diabetes.53.2007.s110 · Cited by 490 · see citing works

Diabetes mellitus and genetically programmed defects in β-cell function

Bell, G. I., & Polonsky, K. S. (2001) · Nature · doi:10.1038/414788a · Cited by 475 · see citing works

Targeting Sirtuin 1 to Improve Metabolism: All You Need Is NAD+?

Cantó, C., & Auwerx, J. (2012) · Pharmacological Reviews · doi:10.1124/pr.110.003905 · Cited by 433 · see citing works

The efficiency and plasticity of mitochondrial energy transduction.

Brand, M. D. (2005) · Biochemical Society Transactions · doi:10.1042/bst0330897 · Cited by 406 · see citing works

Sirtuins: The ‘ <i>magnificent seven</i> ’, function, metabolism and longevity

Dali‐Youcef, N., Lagouge, M., Froelich, S., Koehl, C., Schoonjans, K., & Auwerx, J. (2007) · Annals of Medicine · doi:10.1080/07853890701408194 · Cited by 402 · see citing works

Acquisition of Dynamic Function in Human Stem Cell-Derived β Cells

Velazco-Cruz, L., Song, J., Maxwell, K. G., Goedegebuure, M. M., Augsornworawat, P., Hogrebe, N. J., & Millman, J. R. (2019) · Stem Cell Reports · doi:10.1016/j.stemcr.2018.12.012 · Cited by 399 · see citing works

Superoxide Activates Mitochondrial Uncoupling Protein 2 from the Matrix Side

Echtay, K. S., Murphy, M. P., Smith, R. A. J., Talbot, D. A., & Brand, M. D. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m208262200 · Cited by 388 · see citing works

Glucolipotoxicity of the pancreatic beta cell

Poitout, V., Amyot, J., Semache, M., Zarrouki, B., Hagman, D., & Fontés, G. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2009.08.006 · Cited by 382 · see citing works

Functional and morphological alterations of mitochondria in pancreatic beta cells from type 2 diabetic patients

Anello, M., Lupi, R., Spampinato, D., Piro, S., Masini, M., Boggi, U., Del Prato, S., Rabuazzo, A. M., Purrello, F., & Marchetti, P. (2005) · Diabetologia · doi:10.1007/s00125-004-1627-9 · Cited by 385 · see citing works

Obesity-related derangements in metabolic regulation

Muoio, D. M., & Newgard, C. B. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.103004.142512 · Cited by 345 · see citing works

Uncoupling Protein-2 Overexpression Inhibits Mitochondrial Death Pathway in Cardiomyocytes

Teshima, Y., Akao, M., Jones, S. P., & Marbán, E. (2003) · Circulation Research · doi:10.1161/01.res.0000085581.60197.4d · Cited by 318 · see citing works

Superoxide-mediated activation of uncoupling protein 2 causes pancreatic β cell dysfunction

Krauss, S., Zhang, C.-Y., Scorrano, L., Dalgaard, L. T., St-Pierre, J., Grey, S. T., & Lowell, B. B. (2003) · Journal of Clinical Investigation · doi:10.1172/jci200319774 · Cited by 401 · see citing works

A central thermogenic-like mechanism in feeding regulation: an interplay between arcuate nucleus T3 and UCP2

Coppola, A., Liu, Z.-W., Andrews, Z. B., Paradis, E., Roy, M.-C., Friedman, J. M., Ricquier, D., Richard, D., Horvath, T. L., Gao, X.-B., et al. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2006.12.002 · Cited by 295 · see citing works

Uncoupling Protein 2 Knockout Mice Have Enhanced Insulin Secretory Capacity After a High-Fat Diet

Joseph, J. W., Koshkin, V., Zhang, C.-Y., Wang, J., Lowell, B. B., Chan, C. B., & Wheeler, M. B. (2002) · Diabetes · doi:10.2337/diabetes.51.11.3211 · Cited by 220 · see citing works

Uncoupling protein-2 controls proliferation by promoting fatty acid oxidation and limiting glycolysis-derived pyruvate utilization

Pecqueur, C., Bui, T., Gelly, C., Hauchard, J., Barbot, C., Bouillaud, F., Ricquier, D., Miroux, B., & Thompson, C. B. (2008) · The FASEB Journal · doi:10.1096/fj.07-8945com · Cited by 209 · see citing works

Free Fatty Acid-induced β-Cell Defects Are Dependent on Uncoupling Protein 2 Expression

Joseph, J. W., Koshkin, V., Saleh, M. C., Sivitz, W. I., Zhang, C.-Y., Lowell, B. B., Chan, C. B., & Wheeler, M. B. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409189200 · Cited by 206 · see citing works

The basal proton conductance of skeletal muscle mitochondria from transgenic mice overexpressing or lacking uncoupling protein-3

Cadenas, S., Echtay, K. S., Harper, J. A., Jekabsons, M. B., Buckingham, J. A., Grau, E., Abuin, A., Chapman, H., Clapham, J. C., & Brand, M. D. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109736200 · Cited by 199 · see citing works

Uncoupling Protein-2 Is Critical for Nigral Dopamine Cell Survival in a Mouse Model of Parkinson's Disease

Andrews, Z. B., Horvath, B., Barnstable, C. J., Elseworth, J., Yang, L., Beal, M. F., Roth, R. H., Matthews, R. T., & Horvath, T. L. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.4269-04.2005 · Cited by 199 · see citing works

Mitochondrial uncoupling and lifespan

Mookerjee, S. A., Divakaruni, A. S., Jastroch, M., & Brand, M. D. (2010) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2010.03.010 · Cited by 169 · see citing works

Persistent oxidative stress due to absence of uncoupling protein 2 associated with impaired pancreatic β-cell function.

Pi, J., Bai, Y., Daniel, K. W., Liu, D., Lyght, O., Edelstein, D., Brownlee, M., Corkey, B. E., & Collins, S. (2009) · Endocrinology · doi:10.1210/en.2008-1642 · Cited by 163 · see citing works

No Evidence for a Basal, Retinoic, or Superoxide-induced Uncoupling Activity of the Uncoupling Protein 2 Present in Spleen or Lung Mitochondria

Couplan, E., del Mar Gonzalez-Barroso, M., Alves-Guerra, M. C., Ricquier, D., Goubern, M., & Bouillaud, F. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202535200 · Cited by 161 · see citing works

Suppression of β Cell Energy Metabolism and Insulin Release by PGC-1α

Yoon, J. C., Xu, G., Deeney, J. T., Yang, S.-N., Rhee, J., Puigserver, P., Levens, A. R., Yang, R., Zhang, C.-Y., Lowell, B. B., et al. (2003) · Developmental Cell · doi:10.1016/s1534-5807(03)00170-9 · Cited by 143 · see citing works

UCP2, not a physiologically relevant uncoupler but a glucose sparing switch impacting ROS production and glucose sensing

Bouillaud, F. (2009) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2009.01.003 · Cited by 146 · see citing works

The regulation and turnover of mitochondrial uncoupling proteins

Azzu, V., Jastroch, M., Divakaruni, A. S., & Brand, M. D. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.02.035 · Cited by 146 · see citing works

Upregulation of uncoupling proteins by oral administration of capsiate, a nonpungent capsaicin analog

Masuda, Y., Haramizu, S., Oki, K., Ohnuki, K., Watanabe, T., Yazawa, S., Kawada, T., Hashizume, S.-I., & Fushiki, T. (2003) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00828.2002 · Cited by 143 · see citing works

In beta-cells, mitochondria integrate and generate metabolic signals controlling insulin secretion

Maechler, P., Carobbio, S., & Rubi, B. (2006) · The International Journal of Biochemistry &amp; Cell Biology · doi:10.1016/j.biocel.2005.12.006 · Cited by 140 · see citing works

The polymorphisms of UCP2 and UCP3 genes associated with fat metabolism, obesity and diabetes

Jia, J. ‐., Zhang, X., Ge, C. ‐., & Jois, M. (2009) · Obesity Reviews · doi:10.1111/j.1467-789x.2009.00569.x · Cited by 137 · see citing works

β-Cell Uncoupling Protein 2 Regulates Reactive Oxygen Species Production, Which Influences Both Insulin and Glucagon Secretion

Robson-Doucette, C. A., Sultan, S., Allister, E. M., Wikstrom, J. D., Koshkin, V., Bhattacharjee, A., Prentice, K. J., Sereda, S. B., Shirihai, O. S., & Wheeler, M. B. (2011) · Diabetes · doi:10.2337/db11-0132 · Cited by 136 · see citing works

Decreased Mitochondrial Proton Leak and Reduced Expression of Uncoupling Protein 3 in Skeletal Muscle of Obese Diet-Resistant Women

Harper, M.-E., Dent, R., Monemdjou, S., Bézaire, V., Van Wyck, L., Wells, G., Kavaslar, G. N., Gauthier, A., Tesson, F., & McPherson, R. (2002) · Diabetes · doi:10.2337/diabetes.51.8.2459 · Cited by 129 · see citing works

The efficiency of cellular energy transduction and its implications for obesity

Harper, M.-E., Green, K., & Brand, M. D. (2008) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.28.061807.155357 · Cited by 121 · see citing works

Resistance to cerebral ischemic injury in UCP2 knockout mice: evidence for a role of UCP2 as a regulator of mitochondrial glutathione levels

De Bilbao, F., Arsenijevic, D., Vallet, P., Hjelle, O. P., Ottersen, O. P., Bouras, C., Raffin, Y., Abou, K., Langhans, W., Collins, S., et al. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02432.x · Cited by 108 · see citing works

Metformin induces oxidative stress in white adipocytes and raises uncoupling protein 2 levels

Anedda, A., Rial, E., & González-Barroso, M. M. (2008) · Journal of Endocrinology · doi:10.1677/joe-08-0278 · Cited by 98 · see citing works

Coenzyme Q10 Depletion in Medical and Neuropsychiatric Disorders: Potential Repercussions and Therapeutic Implications

Morris, G., Anderson, G., Berk, M., & Maes, M. (2013) · Molecular Neurobiology · doi:10.1007/s12035-013-8477-8 · Cited by 96 · see citing works

Reactive oxygen species and uncoupling protein 2 in pancreatic <i>β</i> ‐cell function

Pi, J., & Collins, S. (2010) · Diabetes, Obesity and Metabolism · doi:10.1111/j.1463-1326.2010.01269.x · Cited by 91 · see citing works

Mitochondrial recoupling: a novel therapeutic strategy for cancer

Baffy, G., Derdak, Z., & Robson, S. C. (2011) · British Journal of Cancer · doi:10.1038/bjc.2011.245 · Cited by 88 · see citing works

Uncoupling protein-2 contributes significantly to high mitochondrial proton leak in INS-1E insulinoma cells and attenuates glucose-stimulated insulin secretion

Affourtit, C., & Brand, M. D. (2008) · Biochemical Journal · doi:10.1042/bj20070954 · Cited by 85 · see citing works

Uncoupling protein-2 attenuates glucose-stimulated insulin secretion in INS-1E insulinoma cells by lowering mitochondrial reactive oxygen species

Affourtit, C., Jastroch, M., & Brand, M. D. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.12.020 · Cited by 83 · see citing works

On the role of uncoupling protein-2 in pancreatic beta cells

Affourtit, C., & Brand, M. D. (2008) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2008.03.022 · Cited by 78 · see citing works

Fatty Acid Flippase Activity of UCP2 Is Essential for Its Proton Transport in Mitochondria

Berardi, M. J., & Chou, J. J. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.07.004 · Cited by 76 · see citing works

Uncoupling Proteins: Role in Insulin Resistance and Insulin Insufficiency

B.Chan, C., & Harper, M.-E. (2006) · Current Diabetes Reviews · doi:10.2174/157339906777950660 · Cited by 71 · see citing works

Stronger control of ATP/ADP by proton leak in pancreatic β-cells than skeletal muscle mitochondria

Affourtit, C., & Brand, M. D. (2006) · Biochemical Journal · doi:10.1042/bj20051280 · Cited by 71 · see citing works

Insulin Signaling Regulates Mitochondrial Function in Pancreatic β-Cells

Liu, S., Okada, T., Assmann, A., Soto, J., Liew, C. W., Bugger, H., Shirihai, O. S., Abel, E. D., & Kulkarni, R. N. (2009) · PLoS ONE · doi:10.1371/journal.pone.0007983 · Cited by 58 · see citing works

Role of Peroxisome Proliferator-Activated Receptor-γ Coactivator-1α in the Transcriptional Regulation of the Human Uncoupling Protein 2 Gene in INS-1E Cells

Oberkofler, H., Klein, K., Felder, T. K., Krempler, F., & Patsch, W. (2006) · Endocrinology · doi:10.1210/en.2005-0817 · Cited by 59 · see citing works

Novel insights into pancreatic β-cell glucolipotoxicity from real-time functional analysis of mitochondrial energy metabolism in INS-1E insulinoma cells

Barlow, J., & Affourtit, C. (2013) · Biochemical Journal · doi:10.1042/bj20131002 · Cited by 53 · see citing works

Emerging roles of β-cell mitochondria in type-2-diabetes

Las, G., Oliveira, M. F., & Shirihai, O. S. (2020) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2019.100843 · Cited by 51 · see citing works

Free fatty acids increase PGC‐1α expression in isolated rat islets

Zhang, P., Liu, C., Zhang, C., Zhang, Y., Shen, P., Zhang, J., & Zhang, C.-Y. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.01.046 · Cited by 45 · see citing works

Reconstitution of novel mitochondrial uncoupling proteins UCP2 and UCP3

Žáčkova, M., & Ježek, P. (2002) · Bioscience Reports · doi:10.1023/a:1016009022186 · Cited by 25 · see citing works

Parameter adaptations during phenotype transitions in progressive diseases

Tiemann, C. A., Vanlier, J., Hilbers, P. A., & van Riel, N. A. (2011) · BMC Systems Biology · doi:10.1186/1752-0509-5-174 · Cited by 22 · see citing works

The UCP2-866G/A Polymorphism Could be Considered as a Genetic Marker of Different Functional Prognosis in Ischemic Stroke after Recanalization

Díaz-Maroto Cicuéndez, I., Fernández-Díaz, E., García-García, J., Jordán, J., Fernández-Cadenas, I., Montaner, J., Serrano-Heras, G., & Segura, T. (2017) · NeuroMolecular Medicine · doi:10.1007/s12017-017-8470-x · Cited by 12 · see citing works

Mitochondrial uncoupling protein-2 is not involved in palmitate-induced impairment of glucose-stimulated insulin secretion in INS-1E insulinoma cells and is not needed for the amplification of insulin release

Hirschberg Jensen, V., & Affourtit, C. (2015) · Biochemistry and Biophysics Reports · doi:10.1016/j.bbrep.2015.03.008 · Cited by 9 · see citing works

Downregulation of miR-140-3p is a Cause of Upregulation of Rhoa Protein in Bronchial Smooth Muscle of Murine Experimental Asthma

Chiba, Y., Ando, Y., Fujii, S., et al. (2021) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2020-0292le · Cited by 7 · see citing works

Comparative Transcriptomics of PKD1 Downregulation and PKA Upregulation or Downregulation

Li, X., Wang, X., Li, J., et al. (2022) · Journal of the American Society of Nephrology · doi:10.1681/asn.20223311s1395c · Cited by 1 · see citing works

THE CORRELATION BETWEEN DONOR CHARACTERISTICS AND THE SUCCESS OF HUMAN ISLET ISOLATION1,2

ZENG, Y., TORRE, M. A., Karrison, T. G., & Thistlethwaite, J. R. (1994) · Transplantation · doi:10.1097/00007890-199403270-00031 · Cited by 87 · see citing works

P.100: Impact of Islet Purity on Short- and Long-term Graft Function in Islet Allotransplantation

Balak, J. R. A., Doppenberg, J. B., Nijhoff, M. F., et al. (2021) · Transplantation · doi:10.1097/01.tp.0000804492.08932.fb

Characterization of Islet Health and Function Prior to Transplantation

Weber, C. S., Hart, N. J., Steyn, L. V., et al. (2020) · The FASEB Journal · doi:10.1096/fasebj.2020.34.s1.06703