Long-term high-fat feeding induces greater fat storage in mice lacking UCP3

Intramyocellular lipid concentrations are correlated with insulin sensitivity in humans: a 1 H NMR spectroscopy study

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

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Measurement of intracellular triglyceride stores by H spectroscopy: validation in vivo

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Mice overexpressing human uncoupling protein-3 in skeletal muscle are hyperphagic and lean

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

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Estimation of energy expenditure, net carbohydrate utilization, and net fat oxidation and synthesis by indirect calorimetry: evaluation of errors with special reference to the detailed composition of fuels

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Prediabetes in obese youth: a syndrome of impaired glucose tolerance, severe insulin resistance, and altered myocellular and abdominal fat partitioning.

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The basal proton conductance of mitochondria depends on adenine nucleotide translocase content

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Intramuscular triglyceride and muscle insulin sensitivity: Evidence for a relationship in nondiabetic subjects

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

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Increased uncoupling protein-2 and -3 mRNA expression during fasting in obese and lean humans.

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Physiological Role of UCP3 May Be Export of Fatty Acids from Mitochondria When Fatty Acid Oxidation Predominates: An Hypothesis

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Elevated Free Fatty Acids Induce Uncoupling Protein 3 Expression in Muscle: A Potential Explanation for the Effect of Fasting

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Role of UCP homologues in skeletal muscles and brown adipose tissue: mediators of thermogenesis or regulators of lipids as fuel substrate?

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Uncoupling Protein-3 Expression in Rodent Skeletal Muscle Is Modulated by Food Intake but Not by Changes in Environmental Temperature

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UCP2 and UCP3 rise in starved rat skeletal muscle but mitochondrial proton conductance is unchanged

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Tissue‐dependent upregulation of rat uncoupling protein‐2 expression in response to fasting or cold

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Physiological Increases in Uncoupling Protein 3 Augment Fatty Acid Oxidation and Decrease Reactive Oxygen Species Production Without Uncoupling Respiration in Muscle Cells

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

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Overexpression of uncoupling protein 3 in skeletal muscle protects against fat-induced insulin resistance

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An alternative function for human uncoupling protein 3: protection of mitochondria against accumulation of nonesterified fatty acids inside the mitochondrial matrix

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Skeletal muscle triglyceride: marker or mediator of obesity-induced insulin resistance in type 2 diabetes mellitus?

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Interorgan signaling between adipose tissue metabolism and skeletal muscle uncoupling protein homologs: is there a role for circulating free fatty acids?

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Constitutive UCP3 overexpression at physiological levels increases mouse skeletal muscle capacity for fatty acid transport and oxidation

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Up-Regulation of Uncoupling Protein 3 (UCP3) mRNA by Exercise Training and Down-Regulation of UCP3 by Denervation in Skeletal Muscles

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Uncoupling protein 3 content is decreased in skeletal muscle of patients with type 2 diabetes

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

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Post-starvation gene expression of skeletal muscle uncoupling protein 2 and uncoupling protein 3 in response to dietary fat levels and fatty acid composition: a link with insulin resistance.

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Physiological Levels of Mammalian Uncoupling Protein 2 Do Not Uncouple Yeast Mitochondria

Stuart, J. A., Harper, J. A., Brindle, K. M., Jekabsons, M. B., & Brand, M. D. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m011566200 · Cited by 99 · see citing works

Effect of acute exercise on uncoupling protein 3 is a fat metabolism-mediated effect

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Effects of fasting on muscle mitochondrial energetics and fatty acid metabolism in Ucp3(-/-) and wild-type mice.

Bézaire, V., Hofmann, W. E., Kramer, J. K. G., Kozak, L. P., & Harper, M.-E. (2001) · American Journal of Physiology. Endocrinology and Metabolism · doi:10.1152/ajpendo.2001.281.5.e975 · Cited by 90 · see citing works

Artifactual uncoupling by uncoupling protein 3 in yeast mitochondria at the concentrations found in mouse and rat skeletal-muscle mitochondria

HARPER, J. A., STUART, J. A., JEKABSONS, M. B., ROUSSEL, D., BRINDLE, K. M., DICKINSON, K., JONES, R. B., & BRAND, M. D. (2002) · Biochemical Journal · doi:10.1042/bj3610049 · Cited by 87 · see citing works

Increased fatty acid oxidation in transgenic mice overexpressing UCP3 in skeletal muscle

Wang, S., Subramaniam, A., Cawthorne, M. A., & Clapham, J. C. (2003) · Diabetes Obesity and Metabolism · doi:10.1046/j.1463-1326.2003.00273.x · Cited by 74 · see citing works

Percent relative cumulative frequency analysis in indirect calorimetry: application to studies of transgenic mice

Riachi, M., Himms‐Hagen, J., & Harper, M. (2004) · Canadian Journal of Physiology and Pharmacology · doi:10.1139/y04-117 · Cited by 68 · see citing works

Reduction of diet-induced obesity in transgenic mice overexpressing uncoupling protein 3 in skeletal muscle

Son, C., Hosoda, K., Ishihara, K., Bevilacqua, L., Masuzaki, H., Fushiki, T., Harper, M., & Nakao, K. (2004) · Diabetologia · doi:10.1007/s00125-003-1272-8 · Cited by 67 · see citing works

Effects of the presence, absence, and overexpression of uncoupling protein-3 on adiposity and fuel metabolism in congenic mice

Costford, S. R., Chaudhry, S. N., Salkhordeh, M., & Harper, M. (2006) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00401.2005 · Cited by 60 · see citing works

Resistance to high-fat-diet-induced obesity and sexual dimorphism in the metabolic responses of transgenic mice with moderate uncoupling protein 3 overexpression in glycolytic skeletal muscles

Tiraby, C., Tavernier, G., Capel, F., Mairal, A., Crampes, F., RAMI, J., Pujol, C., Boutin, J. A., & Langin, D. (2007) · Diabetologia · doi:10.1007/s00125-007-0765-2 · Cited by 56 · see citing works

Properties of the human long and short isoforms of the uncoupling protein‐3 expressed in yeast cells

Hinz, W., Grueninger, S., Pover, A. D., & Chiesi, M. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)01568-9 · Cited by 48 · see citing works

Mitochondrial uncoupling proteins and energy metabolism

Busiello, R. A., Savarese, S., & Lombardi, A. (2015) · Frontiers in Physiology · doi:10.3389/fphys.2015.00036 · Cited by 259 · see citing works

The on-off switches of the mitochondrial uncoupling proteins

Azzu, V., & Brand, M. D. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2009.11.001 · Cited by 239 · see citing works

Glutathionylation Acts as a Control Switch for Uncoupling Proteins UCP2 and UCP3

Mailloux, R. J., Seifert, E. L., Bouillaud, F., Aguer, C., Collins, S., & Harper, M.-E. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.240242 · Cited by 174 · see citing works

The Role of Mitochondria in the Pathophysiology of Skeletal Muscle Insulin Resistance

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Proinflammatory NFkB signalling promotes mitochondrial dysfunction in skeletal muscle in response to cellular fuel overloading

Nisr, R. B., Shah, D. S., Ganley, I. G., & Hundal, H. S. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03148-8 · Cited by 142 · see citing works

Mitochondrial proticity and ROS signaling: lessons from the uncoupling proteins

Mailloux, R. J., & Harper, M. (2012) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2012.04.004 · Cited by 122 · see citing works

Important Trends in UCP3 Investigation

Pohl, E. E., Rupprecht, A., Macher, G., & Hilse, K. E. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.00470 · Cited by 102 · see citing works

The DNA Repair Protein OGG1 Protects Against Obesity by Altering Mitochondrial Energetics in White Adipose Tissue

Komakula, S. S. B., Tůmová, J., Kumaraswamy, D., Burchat, N., Vartanian, V. L., Ye, H., Dobrzyń, A., Lloyd, R. S., & Sampath, H. (2018) · Scientific Reports · doi:10.1038/s41598-018-33151-1 · Cited by 80 · see citing works

Loss of Akt1 in Mice Increases Energy Expenditure and Protects against Diet-Induced Obesity

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Glutaredoxin-2 Is Required to Control Proton Leak through Uncoupling Protein-3

Mailloux, R. J., Xuan, J. Y., Beauchamp, B., Jui, L., Lou, M. F., & Harper, M. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.442905 · Cited by 64 · see citing works

The expression of UCP3 directly correlates to UCP1 abundance in brown adipose tissue

Hilse, K. E., Kalinovich, A., Rupprecht, A., Тихоновна, С. А., Zeitz, U., Staniek, K., Erben, R. G., & Pohl, E. E. (2015) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2015.10.011 · Cited by 64 · see citing works

Mitochondrial Actions of Thyroid Hormone

Lanni, A., Moreno, M., & Goglia, F. (2016) · Comprehensive physiology · doi:10.1002/cphy.c150019 · Cited by 64 · see citing works

Central Leptin Activates Mitochondrial Function and Increases Heat Production in Skeletal Muscle

Henry, B. A., Andrews, Z. B., Rao, A., & Clarke, I. J. (2011) · Endocrinology · doi:10.1210/en.2011-0143 · Cited by 54 · see citing works

Cell Death and Heart Failure in Obesity: Role of Uncoupling Proteins

Ruiz‐Ramírez, A., López-Acosta, O., Barrios-Maya, M. A., & El‐Hafidi, M. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/9340654 · Cited by 54 · see citing works

Uncoupling protein 3 expression levels influence insulin sensitivity, fatty acid oxidation, and related signaling pathways

Senese, R., Valli, V., Moreno, M., Lombardi, A., Busiello, R. A., Cioffi, F., Silvestri, E., Goglia, F., Lanni, A., & de Lange, P. (2011) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-010-0892-3 · Cited by 52 · see citing works

Thyroid Hormone, Thyromimetics, and Metabolic Efficiency

Yehuda‐Shnaidman, E., Kalderon, B., & Bar‐Tana, J. (2013) · Endocrine Reviews · doi:10.1210/er.2013-1006 · Cited by 52 · see citing works

Protective Role of Mitochondrial Uncoupling Proteins against Age-Related Oxidative Stress in Type 2 Diabetes Mellitus

Čater, M., & Bombek, L. K. (2022) · Antioxidants · doi:10.3390/antiox11081473 · Cited by 51 · see citing works

Increased mitochondrial content rescues in vivo muscle oxidative capacity in long‐term high‐fat‐diet‐fed rats

van den Broek, N. M. A., Čiapaitė, J., Feyter, H. M. M. L. D., Houten, S. M., Wanders, R. J. A., Jeneson, J. A. L., Nicolay, K., & Prompers, J. J. (2009) · The FASEB Journal · doi:10.1096/fj.09-143842 · Cited by 50 · see citing works

Interactions between the consumption of a high-fat diet and fasting in the regulation of fatty acid oxidation enzyme gene expression: an evaluation of potential mechanisms

Frier, B. C., Jacobs, R. L., & Wright, D. C. (2010) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00367.2010 · Cited by 50 · see citing works

Mitochondrial uncoupling in skeletal muscle by UCP1 augments energy expenditure and glutathione content while mitigating ROS production

Adjeitey, C. N., Mailloux, R. J., deKemp, R. A., & Harper, M. (2013) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00057.2013 · Cited by 48 · see citing works

Uncoupling protein-2 decreases the lipogenic actions of ghrelin.

Andrews, Z., Erion, D., Beiler, R. J., Choi, C., Shulman, G., & Horvath, T. (2010) · Endocrinology · doi:10.1210/en.2009-0850 · Cited by 45 · see citing works

Mitochondrial Uncoupling Proteins (UCPs) as Key Modulators of ROS Homeostasis: A Crosstalk between Diabesity and Male Infertility?

Monteiro, B. S., Freire‐Brito, L., Carrageta, D. F., Oliveira, P. F., & Alves, M. G. (2021) · Antioxidants · doi:10.3390/antiox10111746 · Cited by 47 · see citing works

Vitamin D3/VDR resists diet-induced obesity by modulating UCP3 expression in muscles

Fan, Y., Futawaka, K., Koyama, R., Fukuda, Y., Hayashi, M., Imamoto, M., Miyawaki, T., Kasahara, M., Tagami, T., & Moriyama, K. (2016) · Journal of Biomedical Science · doi:10.1186/s12929-016-0271-2 · Cited by 44 · see citing works

Exercise, fasting, and mimetics: toward beneficial combinations?

Jaspers, R. T., Zillikens, M. C., Friesema, E. C. H., Paoli, G. D., Bloch, W., Uitterlinden, A. G., Goglia, F., Lanni, A., & de Lange, P. (2016) · The FASEB Journal · doi:10.1096/fj.201600652r · Cited by 43 · see citing works

Role of lipid-derived mediators in skeletal muscle insulin resistance

Taube, A., Eckardt, K., & Eckel, J. (2009) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00241.2009 · Cited by 40 · see citing works

Sex Differences in the Metabolic Effects of Testosterone in Sheep

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Hexokinase II acts through UCP3 to suppress mitochondrial reactive oxygen species production and maintain aerobic respiration

Mailloux, R. J., Dumouchel, T., Aguer, C., deKemp, R., Beanlands, R. S., & Harper, M. (2011) · Biochemical Journal · doi:10.1042/bj20110571 · Cited by 38 · see citing works

Implications of mitochondrial uncoupling in skeletal muscle in the development and treatment of obesity

Thrush, A. B., Dent, R., McPherson, R., & Harper, M. (2013) · FEBS Journal · doi:10.1111/febs.12399 · Cited by 33 · see citing works

Modified High-Sucrose Diet-Induced Abdominally Obese and Normal-Weight Rats Developed High Plasma Free Fatty Acid and Insulin Resistance

Cao, L., Liu, X., Cao, H., Lv, Q., & Tong, N. (2012) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2012/374346 · Cited by 33 · see citing works

Effects of Eicosapentaenoic Acid and Docosahexaenoic Acid on Uncoupling Protein 3 Gene Expression in C2C12 Muscle Cells

Lee, M.-S., Kim, I.-H., & Kim, Y. (2013) · Nutrients · doi:10.3390/nu5051660 · Cited by 31 · see citing works

Hippocampal responsiveness to 17β-estradiol and equol after long-term ovariectomy: Implication for a therapeutic window of opportunity

Hamilton, R. T., Rettberg, J. R., Mao, Z., To, J., Zhao, L., Appt, S. E., Register, T. C., Kaplan, J. R., & Brinton, R. D. (2011) · Brain Research · doi:10.1016/j.brainres.2011.01.029 · Cited by 29 · see citing works

UCP3 Expression in Liver Modulates Gene Expression and Oxidative Metabolism in Response to Fatty Acids, and Sensitizes Mitochondria to Permeability Transition

Cámara, Y., Mampel, T., Armengol, J., Villarroya, F., & Dejean, L. M. (2009) · Cellular Physiology and Biochemistry · doi:10.1159/000233249 · Cited by 26 · see citing works

Significance of uncoupling protein 3 in mitochondrial function upon mid- and long-term dietary high-fat exposure

Nabben, M., Joris Hoeks, J., Moonen‐Kornips, E., van Beurden, D., Briedé, J. J., Hesselink, M. K. C., Glatz, J. F. C., & Schrauwen, P. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.11.012 · Cited by 23 · see citing works

Muscle-UCP3 in the regulation of energy metabolism

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A novel amino acid and metabolomics signature in mice overexpressing muscle uncoupling protein 3

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Uncoupling protein-3 as a molecular determinant of the action of 3,5,3′-triiodothyronine on energy metabolism

Flandin, P., Lehr, L., Asensio, C. S., Giacobino, J., Rohner‐Jeanrenaud, F., Muzzin, P., & Jimenez, M. (2009) · Endocrine · doi:10.1007/s12020-009-9217-8 · Cited by 19 · see citing works

Age-related sex differences in the expression of important disease-linked mitochondrial proteins in mice

Moschinger, M., Hilse, K. E., Rupprecht, A., Zeitz, U., Erben, R. G., Rülicke, T., & Pohl, E. E. (2019) · Biology of Sex Differences · doi:10.1186/s13293-019-0267-1 · Cited by 18 · see citing works

Genetic ablation of myelin protein zero-like 3 in mice increases energy expenditure, improves glycemic control, and reduces hepatic lipid synthesis

Czyzyk, T. A., Andrews, J. L., Coşkun, T., Wade, M. R., Hawkins, E. D., Lockwood, J. F., Varga, G., Sahr, A. E., Chen, Y., Brozinick, J. T., et al. (2013) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00228.2013 · Cited by 18 · see citing works

Targeting energy expenditure in muscle as a means of combating obesity

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Human mitochondrial uncoupling protein 3 functions as a metabolite transporter

Leonardis, F. D., Ahmed, A., Vozza, A., Capobianco, L., Riley, C. L., Barile, S. N., Molfetta, D. D., Tiziani, S., DiGiovanni, J., Palmieri, L., et al. (2023) · FEBS Letters · doi:10.1002/1873-3468.14784 · Cited by 14 · see citing works

Absence of Uncoupling Protein-3 at Thermoneutrality Impacts Lipid Handling and Energy Homeostasis in Mice

Lombardi, A., Busiello, R. A., Matteis, R. D., Lionetti, L., Savarese, S., Moreno, M., Gentile, A., Silvestri, E., Senese, R., de Lange, P., et al. (2019) · Cells · doi:10.3390/cells8080916 · Cited by 14 · see citing works

Adaptive gene expression of alternative splicing variants of PGC-1α regulates whole-body energy metabolism

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Calorie restriction in mice overexpressing UCP3: Evidence that prior mitochondrial uncoupling alters response

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Running Head:

Costford, S. R., Chaudhry, S. N., Salkhordeh, M., & Harper, M.-E. (2013)

Effects of the presence, absence, and overexpression of uncoupling protein-3 on adiposity and fuel metabolism in congenic mice

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The effect of high‐fat feeding on intramuscular lipid and lipid peroxidation levels in UCP3‐ablated mice

Joris Hoeks, J., Hesselink, M. K. C., Sluiter, W. J., Schaart, G., Willems, J., Morrisson, A., Clapham, J. C., Saris, W. H. M., & Schrauwen, P. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.01.059 · Cited by 26 · see citing works

Significance of uncoupling protein 3 in mitochondrial function upon mid- and long-term dietary high-fat exposure

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Constitutive UCP3 overexpression at physiological levels increases mouse skeletal muscle capacity for fatty acid transport and oxidation

Bézaire, V., Spriet, L. L., Campbell, S., Sabet, N., Gerrits, M. F., Bonen, A., & Harper, M. (2005) · The FASEB Journal · doi:10.1096/fj.04-2765fje · Cited by 132 · see citing works