The DOI matches its Crossref record; 102 of the 102 references it cites were found in a registry or an index.
Physiological functions of the mitochondrial uncoupling proteins UCP2 and UCP3
Open accessAbstract
Evidence for the physiological functions of UCP2 and UCP3 is critically reviewed. They do not mediate adaptive thermogenesis, but they may be significantly thermogenic under specific pharmacological conditions. There is strong evidence that the mild regulated uncoupling they cause attenuates mitochondrial ROS production, protects against cellular damage, and diminishes insulin secretion. Evidence that they export fatty acids physiologically is weak. UCP2 and UCP3 are important potential targets for treatment of aging, degenerative diseases, diabetes, and perhaps obesity.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“UCP1 plays a role in adaptive thermogenesis in mammalian brown adipose tissue to produce heat (314), whereas the actions of UCP2 and 3 are upregulated in response to oxidant stress caused by nutrient deprivation, glucose sensing, fatty acid metabolism, or other metabolic changes in order to lessen mitochondrial ROS production (49).”
From Redox regulation of mitochondrial function (2012) · cites this paper as [49]
Citations
Cites
Free radicals in biology and medicine
Gutteridge, J. M. C. (1991) · General Pharmacology The Vascular System · doi:10.1016/0306-3623(91)90478-o · Cited by 17,178
Brown Adipose Tissue: Function and Physiological Significance
CANNON, B., & NEDERGAARD, J. (2004) · Physiological Reviews · doi:10.1152/physrev.00015.2003 · Cited by 6,433
Free radicals in biology and medicine
Halliwell, B. B., & Gutteridge, J. M. C. (1985) · Journal of Free Radicals in Biology & Medicine · doi:10.1016/0748-5514(85)90140-0 · Cited by 2,938
Korshunov, S. S., Skulachev, V. P., & Starkov, A. A. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)01159-9 · Cited by 1,727
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
Topology of superoxide production from different sites in the mitochondrial electron transport chain
St-Pierre, J., Buckingham, J. A., Roebuck, S. J., & Brand, M. D. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207217200 · Cited by 1,545
Self-citationSuperoxide 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
Self-citationMitochondria and neuronal survival
Nicholls, D. G., & Budd, S. L. (2000) · Physiological Reviews · doi:10.1152/physrev.2000.80.1.315 · Cited by 1,243
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 1,100
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
Cited by
Sorted by citations
Items 401–500 of 781
Uncoupling protein-2 modulates the lipid metabolic response to fasting in mice
Sheets, A. R., Fülöp, P., Derdák, Z., Kassai, A., Sabo, E., Mark, N. M., Paragh, G., Wands, J. R., & Baffy, G. (2008) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00016.2008 · Cited by 31
Pinelli, M., Giacchetti, M., Acquaviva, F., Cocozza, S., Donnarumma, G., Lapice, E., Riccardi, G., Romano, G., Vaccaro, O., & Monticelli, A. (2006) · BMC Medical Genetics · doi:10.1186/1471-2350-7-85 · Cited by 29
Wojewoda, M., Duszyński, J., & Szczepanowska, J. (2011) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2011.04.011 · Cited by 28
Stanzione, R., Forte, M., Cotugno, M., Bianchi, F., Marchitti, S., Busceti, C. L., Fornai, F., & Rubattu, S. (2021) · Current Neuropharmacology · doi:10.2174/1570159x19666210421094204 · Cited by 30
Sung, Y.-Y., Kim, S., Yoo, B. W., & Kim, H. K. (2015) · BMC Complementary and Alternative Medicine · doi:10.1186/s12906-015-0875-1 · Cited by 28
Mitochondrial uncoupling protein 2 in pancreatic β ‐cells
Brand, M. D., Parker, N., Affourtit, C., Mookerjee, S. A., & Azzu, V. (2010) · Diabetes Obesity and Metabolism · doi:10.1111/j.1463-1326.2010.01264.x · Cited by 29
Self-citationMontez, P., Vázquez‐Medina, J. P., Rodríguez, R., Thorwald, M. A., Viscarra, J. A., Lam, L., Peti‐Peterdi, J., Nakano, D., Nishiyama, A., & Ortiz, R. M. (2012) · Endocrinology · doi:10.1210/en.2012-1390 · Cited by 31
Lombardi, A., Lanni, A., de Lange, P., Silvestri, E., Grasso, P., Senese, R., Goglia, F., & Moreno, M. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.11.073 · Cited by 28
Jack, B. U., Malherbe, C. J., Huisamen, B., Gabuza, K., Mazibuko-Mbeje, S. E., Schulze, A. E., Joubert, E., Muller, C. J. F., Louw, J., & Pheiffer, C. (2016) · South African Journal of Botany · doi:10.1016/j.sajb.2016.08.007 · Cited by 29
Cell type–specific efferocytosis determines functional plasticity of alveolar macrophages
Better, J., Estiri, M., Wetstein, M., Pervizaj-Oruqaj, L., Malainou, C., Ogungbemi-Alt, V. K., Ferrero, M. R., Langelage, M., Kuznetsova, I., Vazquez‐Armendariz, A. I., et al. (2025) · Science Immunology · doi:10.1126/sciimmunol.adl3852 · Cited by 32
D-galactose-induced mitochondrial DNA oxidative damage in the auditory cortex of rats
Du, Z., Yang, Q., Zhou, T., Liu, L., LI, S., Chen, S., & Gao, C. (2014) · Molecular Medicine Reports · doi:10.3892/mmr.2014.2653 · Cited by 27
Kim, D. H., Choi, J., Joo, J. I., Wang, X., Choi, D. K., Oh, T. S., & Yun, J. W. (2010) · Journal of Proteome Research · doi:10.1021/pr101048q · Cited by 25
Uddin, S. J., Afroz, M., Zihad, S. M. N. K., Rahman, M. S., Akter, S., Khan, I. N., Al-Rabbi, S. M. S., Rouf, R., Islam, M. T., Shilpi, J. A., et al. (2020) · Food Reviews International · doi:10.1080/87559129.2020.1734609 · Cited by 27
Bevilacqua, L., Seifert, E. L., Estey, C., Gerrits, M. F., & Harper, M. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.02.018 · Cited by 27
Mitochondrial Energy Metabolism and Redox State in Dyslipidemias
Vercesi, A. E., Castilho, R. F., Kowaltowski, A. J., & Oliveira, H. C. F. (2007) · IUBMB Life · doi:10.1080/15216540601178091 · Cited by 28
Zhou, M., Xu, A., Lam, K. S. L., Tam, P. K. H., Che, C., Chan, L., Lee, I., Wu, D., & Wang, Y. (2010) · Journal of Hepatology · doi:10.1016/j.jhep.2010.05.034 · Cited by 29
Effects of UCP2 and UCP3 Variants on the Manifestation of Overweight in Korean Children
Jun, H. S., Kim, I. K., Lee, H. J., Lee, H. J., Kang, J., Kim, J. R., Shin, H. D., & Song, J. (2008) · Obesity · doi:10.1038/oby.2008.531 · Cited by 27
Seshadri, N., Jonasson, M. E., Hunt, K. L., Xiang, B., Cooper, S., Wheeler, M. B., Dolinsky, V. W., & Doucette, C. A. (2017) · Molecular Metabolism · doi:10.1016/j.molmet.2017.04.008 · Cited by 26
Molecular evolution of uncoupling proteins and implications for brain function
Gaudry, M. J., & Jastroch, M. (2018) · Neuroscience Letters · doi:10.1016/j.neulet.2018.12.027 · Cited by 28
Sepsis Impairs Thyroid Hormone Signaling and Mitochondrial Function in the Mouse Diaphragm
Bloise, F. F., Santos, A. T., Brito, J., de Andrade, C. B. V., Oliveira, T. S., Souza, A. F. P., Fontes, K. N., Silva, J. D., Blanco, N. G., Silva, P. L., et al. (2020) · Thyroid · doi:10.1089/thy.2019.0124 · Cited by 27
Duan, W.-L., Wang, X.-J., Ma, Y., Sheng, Z.-M., Dong, H., Zhang, L., Zhang, B., & He, M. (2024) · Molecular Medicine Reports · doi:10.3892/mmr.2024.13170 · Cited by 33
Mitochondrial uncoupling as a target in the treatment of obesity
Costford, S. R., Gowing, A., & Harper, M. (2007) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/mco.0b013e3282f0dbe4 · Cited by 26
Mitochondrial protein phosphorylation: instigator or target of lipotoxicity?
Graier, W. F., Malli, R., & Kostner, G. M. (2009) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2009.01.004 · Cited by 29
Ma, S., Wang, Q., Zhang, Y., Yang, D., Li, D., Tang, B., & Yang, Y. (2013) · American Journal of Hypertension · doi:10.1093/ajh/hpt225 · Cited by 26
Exercise Is Medicine for Nonalcoholic Fatty Liver Disease: Exploration of Putative Mechanisms
Heinle, J. W., DiJoseph, K., Sabag, A., Oh, S., Kimball, S. R., Keating, S., & Stine, J. G. (2023) · Nutrients · doi:10.3390/nu15112452 · Cited by 26
Giatromanolaki, A. N., Balaska, K., Kalamida, D., Kakouratos, C., Efthimios, S., & Michael, I. K. (2017) · Cancer Biology and Medicine · doi:10.20892/j.issn.2095-3941.2017.0089 · Cited by 25
Association of UCP2 and UCP3 polymorphisms with heart rate variability in Japanese men
Matsunaga, T., Gu, N., Yamazaki, H., Tsuda, M., Adachi, T., Yasuda, K., Moritani, T., Tsuda, K., Nonaka, M., & Nishiyama, T. (2009) · Journal of Hypertension · doi:10.1097/hjh.0b013e32831ac967 · Cited by 25
Sex-Dependent Effects of High-Fat-Diet Feeding on Rat Pancreas Oxidative Stress
Gómez‐Pérez, Y., Gianotti, M., Lladó, I., & Proenza, A. M. (2011) · Pancreas · doi:10.1097/mpa.0b013e31821f2645 · Cited by 25
The Role of Uncoupling Protein 2 During Myocardial Dysfunction in a Canine Model of Endotoxin Shock
Wang, X., Liu, D., Chai, W., Long, Y., Su, L., & Yang, R. (2015) · Shock · doi:10.1097/shk.0000000000000286 · Cited by 24
Ridge, E. A., Pachhain, S., Choudhury, S. R., Bodnar, S. R., Larsen, R. A., Phuntumart, V., & Sprague, J. E. (2019) · Scientific Reports · doi:10.1038/s41598-019-40803-3 · Cited by 25
Coccurello, R., & Volonté, C. (2020) · Frontiers in Endocrinology · doi:10.3389/fendo.2020.00199 · Cited by 25
Lyons, D. N., Zhang, L., Pandya, J. D., Danaher, R. J., Ma, F., Miller, C. S., Sullivan, P. G., Sirbu, C., & Westlund, K. N. (2017) · Clinical Journal of Pain · doi:10.1097/ajp.0000000000000515 · Cited by 24
Sánchez-Pérez, P., Mata, A., Torp, M., López-Bernardo, E., Heiestad, C. M., Aronsen, J. M., de Molina-Iracheta, A., Jiménez‐Borreguero, L. J., García-Rovés, P. M., Costa, A. S. H., et al. (2023) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2023.05.014 · Cited by 25
Maris, M., Waelkens, E., Cnop, M., D’Hertog, W., Cunha, D. A., Korf, H., Koike, T., Overbergh, L., & Mathieu, C. (2011) · Journal of Proteome Research · doi:10.1021/pr101290n · Cited by 25
Doerrier, C., García, J. A. G., Volt, H., Díaz-Casado, M. E., Lima‐Cabello, E., Ortiz, F., Luna‐Sánchez, M., Escames, G., López, L. C., & Acuña-Castroviejo, D. (2014) · Life Sciences · doi:10.1016/j.lfs.2014.11.031 · Cited by 24
Development of Chromanes as Novel Inhibitors of the Uncoupling Proteins
Rial, E., Rodríguez-Sánchez, L., Aller, P., Guisado, A., González‐Barroso, M. M., Gallardo‐Vara, E., Redondo‐Horcajo, M., Castellanos, E., de la Pradilla, R. F., & Viso, A. (2011) · Chemistry & Biology · doi:10.1016/j.chembiol.2010.12.012 · Cited by 24
Mitochondrial Uncoupling Protein 2 (UCP2) Regulates Retinal Ganglion Cell Number and Survival
Barnstable, C. J., Reddy, R., Li, H., & Horváth, T. L. (2016) · Journal of Molecular Neuroscience · doi:10.1007/s12031-016-0728-5 · Cited by 24
Kim, Y. H., & Lee, S. (2018) · Redox Biology · doi:10.1016/j.redox.2018.06.011 · Cited by 24
Beetch, M., Harandi‐Zadeh, S., Yang, T., Boycott, C., Chen, Y., Stefañska, B., & Mohammed, S. I. (2020) · Scientific Reports · doi:10.1038/s41598-020-59260-4 · Cited by 24
Influence of dietary fats on ecstasy‐induced hyperthermia
Mills, E., Weaver, K. L., Abramson, E. M., Pfeiffer, M. E., & Sprague, J. E. (2007) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0707312 · Cited by 23
McDonald, R. B., Walker, K. M., Warman, D. B., Griffey, S. M., Warden, C. H., Ramsey, J. J., & Horwitz, B. A. (2008) · Experimental Gerontology · doi:10.1016/j.exger.2008.09.011 · Cited by 25
Gaudry, M. J., Campbell, K. L., & Jastroch, M. (2018) · Handbook of Experimental Pharmacology · doi:10.1007/164_2018_116 · Cited by 24
Favorit, V., Hood, W. R., Kavazis, A. N., & Skibiel, A. L. (2021) · Journal of Dairy Science · doi:10.3168/jds.2021-20138 · Cited by 23
Ghosh, S. K., Banerjee, K. K., Vaidya, V. A., & Kolthur‐Seetharam, U. (2016) · Journal of Neuroendocrinology · doi:10.1111/jne.12397 · Cited by 23
Calpain-mediated protein targets in cardiac mitochondria following ischemia–reperfusion
Li, L., Thompson, J., Hu, Y., Lesnefsky, E. J., Willard, B. B., & Chen, Q. (2022) · Scientific Reports · doi:10.1038/s41598-021-03947-9 · Cited by 24
Humphrey, D. M., Toivonen, J. M., Giannakou, M. E., Partridge, L., & Brand, M. D. (2009) · Experimental Gerontology · doi:10.1016/j.exger.2009.02.001 · Cited by 23
Self-citationIn vitro ischemia decreases histone H4K16 acetylation in neural cells
Dmitriev, R. I., & Papkovsky, D. B. (2014) · FEBS Letters · doi:10.1016/j.febslet.2014.11.038 · Cited by 24
Impaired Mitochondrial Respiration in Large Cerebral Arteries of Rats with Type 2 Diabetes
Merdžo, I., Rutkai, I., Sure, V. N. L. R., McNulty, C. A., Katakam, P. V. G., & Busija, D. W. (2017) · Journal of Vascular Research · doi:10.1159/000454812 · Cited by 23
UCP2 Mitigates the Loss of Human Spermatozoa Motility by Promoting mROS Elimination
Wang, X., Qian, H., Huang, X., Li, J., Zhang, J., Zhu, N., Chen, H., Zhu, C., Wang, J., Zhang, P., et al. (2018) · Cellular Physiology and Biochemistry · doi:10.1159/000494479 · Cited by 23
Reptilian uncoupling protein: functionality and expression in sub-zero temperatures
Rey, B., Sibille, B., Romestaing, C., Belouze, M., Letexier, D., Servais, S., Barré, H., Duchamp, C., & Voituron, Y. (2008) · Journal of Experimental Biology · doi:10.1242/jeb.012328 · Cited by 25
Silvestri, E., de Lange, P., Moreno, M., Lombardi, A., Ragni, M., Feola, A., Schiavo, L., Goglia, F., & Lanni, A. (2006) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2006.02.016 · Cited by 24
Novel reptilian uncoupling proteins: molecular evolution and gene expression during cold acclimation
Schwartz, T. S., Murray, S. A., & Seebacher, F. (2008) · Proceedings of the Royal Society B Biological Sciences · doi:10.1098/rspb.2007.1761 · Cited by 25
Cui, X., Sun, Q., & Wang, H. (2025) · Frontiers in Pharmacology · doi:10.3389/fphar.2025.1510322 · Cited by 24
The 12-day thermoregulatory metamorphosis of Red-winged Blackbirds (Agelaius phoeniceus)
Sirsat, S. K. G., Sirsat, T. S., Crossley, J. L., Sotherland, P. R., & Dzialowski, E. M. (2016) · Journal of Comparative Physiology B · doi:10.1007/s00360-016-0978-0 · Cited by 22
Marquez-Acevedo, A. S., Hood, W. R., Collier, R. J., & Skibiel, A. L. (2023) · Journal of Dairy Science · doi:10.3168/jds.2023-23340 · Cited by 32
Cellular heterogeneity and plasticity during NAFLD progression
Park, H., Choi, J., Kim, H.-M., Yang, D.-Y., An, T. H., Lee, E., Han, B., Lee, S. C., Kim, W. K., Bae, K., et al. (2023) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2023.1221669 · Cited by 22
Grayson, C., & Mailloux, R. J. (2023) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2023.08.015 · Cited by 23
Geetha, R., Chandrasekaran, S. P., & Anuradha, C. V. (2016) · Clinical and Experimental Pharmacology and Physiology · doi:10.1111/1440-1681.12671 · Cited by 22
Tissue-specific seasonal changes in mitochondrial function of a mammalian hibernator
Heim, A. B., Chung, D. J., Florant, G. L., & Chicco, A. J. (2017) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00427.2016 · Cited by 22
Uncoupling Protein 2 Inhibits Myointimal Hyperplasia in Preclinical Animal Models of Vascular Injury
Zhang, Y., Zhang, Y., Li, W., Wang, P., Gu, R., Feng, Y.-X., Wei, S., Peng, K., Zhang, Y., Su, L., et al. (2017) · Journal of the American Heart Association · doi:10.1161/jaha.117.006593 · Cited by 23
Milton‐Laskibar, I., Aguirre, L., Etxeberría, U., Milagro, F. I., Martínez, J. A., & Portillo, M. P. (2018) · Nutrients · doi:10.3390/nu10101446 · Cited by 21
Bandyopadhaya, A., Tzika, A. A., & Rahme, L. G. (2019) · mBio · doi:10.1128/mbio.02211-19 · Cited by 21
Cardoso, S., Santos, M. S., Moreno, A. J., & Moreira, P. I. (2013) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-013-9503-2 · Cited by 21
He, Y., Luan, Z., Fu, X.-A., & Xu, X. (2016) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2016.2478 · Cited by 21
Bryant, H. J., Chung, D. J., & Schulte, P. M. (2018) · Journal of Experimental Biology · doi:10.1242/jeb.186320 · Cited by 23
Disrupted mitochondrial genes and inflammation following stroke
Gibbs, W. S., Weber, R. A., Schnellmann, R. G., & Adkins, D. L. (2016) · Life Sciences · doi:10.1016/j.lfs.2016.09.021 · Cited by 21
Cholico, G. N., Fling, R. R., Zacharewski, N. A., Fader, K. A., Nault, R., & Zacharewski, T. R. (2021) · Scientific Reports · doi:10.1038/s41598-021-95214-0 · Cited by 20
Zhang, M.-X., Song, Y., Xu, W., Zhang, L.-X., Li, C., & Li, Y. (2022) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2022/8831750 · Cited by 20
Rothman, D. L., Behar, K. L., & Dienel, G. A. (2022) · Journal of Neurochemistry · doi:10.1111/jnc.15619 · Cited by 21
The Basics of Oxidative Biochemistry
Miwa, S., Müller, F. L., & Beckman, K. B. (2008) · Humana Press eBooks · doi:10.1007/978-1-59745-420-9_2 · Cited by 20
The UCP2-related mitochondrial pathway participates in rhein-induced apoptosis in HK-2 cells
Mao, Y., Zhang, M., Yang, J., Sun, H., Wang, D., Zhang, X., Yu, F., & Li, J. (2017) · Toxicology Research · doi:10.1039/c6tx00410e · Cited by 20
Gomathi, P., Samarth, A. P., Raj, N. B. A. J., Sasikumar, S., Murugan, P. S., Nallaperumal, S., & Selvam, G. S. (2019) · Gene · doi:10.1016/j.gene.2019.03.041 · Cited by 20
Franck, J. P. C., Slight-Simcoe, E., & Wegner, N. C. (2019) · Comparative Biochemistry and Physiology Part A Molecular & Integrative Physiology · doi:10.1016/j.cbpa.2019.03.024 · Cited by 20
Marchi, U. D., Fernandez‐Martinez, S., de la Fuente, S., Wiederkehr, A., & Domingo, J. S. (2020) · British Journal of Pharmacology · doi:10.1111/bph.15018 · Cited by 22
A novel amino acid and metabolomics signature in mice overexpressing muscle uncoupling protein 3
Aguer, C., Piccolo, B. D., Fiehn, O., Adams, S. H., & Harper, M. (2016) · The FASEB Journal · doi:10.1096/fj.201600914r · Cited by 19
CD36/Sirtuin 1 Axis Impairment Contributes to Hepatic Steatosis in ACE2‐Deficient Mice
Nunes-Souza, V., Alenina, N. V., Qadri, F., Penninger, J. M., Santos, R. A. S., Bäder, M., & Rabelo, L. A. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/6487509 · Cited by 20
Palmer, B. R., Devereaux, C. L., Dhamrait, S. S., Mocatta, T. J., Pilbrow, A. P., Frampton, C. M., Skelton, L., Yandle, T. G., Winterbourn, C. C., Richards, M., et al. (2009) · Cardiovascular Diabetology · doi:10.1186/1475-2840-8-31 · Cited by 20
Zinc-α2-glycoprotein promotes browning of white adipose tissue in cold-exposed male mice
Fan, G., Dang, X., Li, Y., Chen, J., Zhao, R., & Yang, X. (2019) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2019.110669 · Cited by 19
Karimi, R., Cleven, A. J., Elbarbry, F., & Hoang, H. (2020) · European Journal of Drug Metabolism and Pharmacokinetics · doi:10.1007/s13318-020-00656-y · Cited by 22
β-Adrenergic stimulation does not activate p38 MAP kinase or induce PGC-1α in skeletal muscle
Kim, S. H., Asaka, M., Higashida, K., Takahashi, Y., Holloszy, J. O., & Han, D.-H. (2013) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00581.2012 · Cited by 22
Hu, M., Lin, H., Yang, L., Cheng, Y., & Zhang, H. (2017) · The Journal of Biochemistry · doi:10.1093/jb/mvw084 · Cited by 19
Isothermal Microcalorimetry of Tumor Cells: Enhanced Thermogenesis by Metastatic Cells
Lemos, D., Oliveira, T., Martins, L., de Azevedo, V. R., Rodrigues, M. F., Ketzer, L. A., & Rumjanek, F. D. (2019) · Frontiers in Oncology · doi:10.3389/fonc.2019.01430 · Cited by 19
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 18
Parker, N., Vidal‐Puig, A., Azzu, V., & Brand, M. D. (2009) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2009.06.005 · Cited by 19
Self-citationGilea, A. I., Berti, C. C., Magistrati, M., di Punzio, G., Goffrini, P., Baruffini, E., & Dallabona, C. (2021) · Genes · doi:10.3390/genes12121866 · Cited by 18
Jain, A., Kim, B. R., Yu, W., Moninger, T. O., Karp, P. H., Wagner, B. A., & Welsh, M. J. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2318771121 · Cited by 20
Fonseca, P. A. D. S., Suárez‐Vega, A., Arranz, J. J., & Gutiérrez‐Gil, B. (2024) · Genetics Selection Evolution · doi:10.1186/s12711-024-00910-w · Cited by 18
Compromised respiratory adaptation and thermoregulation in aging and age-related diseases
Chan, S. L., Wei, Z., Chigurupati, S., & Tu, W. (2009) · Ageing Research Reviews · doi:10.1016/j.arr.2009.09.006 · Cited by 18
Bracale, R., Petroni, M. L., Davinelli, S., Bracale, U. M., Scapagnini, G., Carruba, M. O., & Nisoli, E. (2014) · PLoS ONE · doi:10.1371/journal.pone.0098244 · Cited by 18
Cho, Y. S., Lee, J. H., Jung, K., Park, J.-W., Moon, S. H., Choe, Y. S., & Lee, K.-H. (2016) · Nuclear Medicine and Biology · doi:10.1016/j.nucmedbio.2016.06.001 · Cited by 20
Škulj, S., Vazdar, K., Margetić, D., & Vazdar, M. (2018) · The Journal of Organic Chemistry · doi:10.1021/acs.joc.8b02231 · Cited by 18
UCP2 Overexpression Redirects Glucose into Anabolic Metabolic Pathways
Sreedhar, A., Cassel, T., Smith, P., Lu, D., Nam, H. W., Lane, A. N., & Zhao, Y. (2018) · PROTEOMICS · doi:10.1002/pmic.201800353 · Cited by 20
Real-Sandoval, S. A., Gutiérrez‐López, G. F., Domínguez‐López, A., Paniagua‐Castro, N., Michicotl-Meneses, M. M., & Jaramillo‐Flores, M. E. (2020) · Journal of Functional Foods · doi:10.1016/j.jff.2020.103781 · Cited by 19
Role of UCP2 in the Energy Metabolism of the Cancer Cell Line A549
Segalés, J., Sànchez‐Martìn, C., Pujol-Morcillo, A., Martín‐Ruíz, M., Santos, P. D. L., Lobato-Alonso, D., Oliver, E., & Rial, E. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24098123 · Cited by 17
Genetics of ischemic stroke functional outcome
Carnwath, T., Demel, S. L., & Prestigiacomo, C. J. (2024) · Journal of Neurology · doi:10.1007/s00415-024-12263-x · Cited by 20
Pathogenesis of Nonalcoholic Fatty Liver Disease
Machado, M. V., & Diehl, A. M. (2018) · Elsevier eBooks · doi:10.1016/b978-0-323-37591-7.00025-2 · Cited by 17
Silva, T. L. A., Braz, G. R. F., Silva, S. C. D. A., Pedroza, A. A. D. S., Freitas, C. D. M., Ferreira, D. J. S., da Silva, A. I., & Lagranha, C. J. (2018) · European Journal of Neuroscience · doi:10.1111/ejn.13971 · Cited by 17
Li, Q., Xu, Z., Liu, L., Yu, H., Hua, R., Tao, L., Zhang, X., Chen, X., Gu, D., Fan, Y., et al. (2013) · Molecular Biology Reports · doi:10.1007/s11033-012-2030-0 · Cited by 17
Du, Z., Hu, Y., Yang, Y., Sun, Y., Zhang, S., Zhou, T., Zeng, L., Zhang, W., Huang, X., Kong, W., et al. (2012) · Journal of Huazhong University of Science and Technology [Medical Sciences] · doi:10.1007/s11596-012-0081-z · Cited by 17
Boardman, N. T., Larsen, T. S., Severson, D. L., Essop, M. F., & Aasum, E. (2011) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.01190.2010 · Cited by 17
Metadata
- Authors
- Brand, M. D., & Esteves, T. C.
- Affiliations
- MRC Mitochondrial Biology Unit (GB)
- Corresponding author
- Brand, Martin D.
- Venue
- Cell Metabolism
- Publisher
- Elsevier BV
- Published
- 2005-08
- Volume
- 2
- Issue
- 2
- Pages
- 85-93
- ISSN
- 1550-4131 (ISSN-L)
- OpenAlex
- W1992678387
- Cited by
- 785
- References
- 101
- Citations by year
- 2026: 16 · 2025: 18 · 2024: 16 · 2023: 26 · 2022: 34 · 2021: 41 · 2020: 33 · 2019: 40 · 2018: 48 · 2017: 44 · 2016: 39 · 2015: 40 · 2014: 32 · 2013: 41 · 2012: 35
- FWCI
- 3.56
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell Metabolism (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Physiology (medical) › Adipose Tissue and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Keywords
- UCP2, UCP3, mitochondrial uncoupling proteins, thermogenesis, mitochondrial reactive oxygen species, insulin secretion, fatty acid export, aging, degenerative diseases, diabetes mellitus, obesity
- MeSH terms
- Uncoupling Protein 2, Uncoupling Protein 3, Insulin Secretion, Aging, Animals, Carrier Proteins, Fatty Acids, Insulin, Ion Channels, Mitochondria, Obesity, Oxidation-Reduction, Reactive Oxygen Species, Oxidative Stress, Protein Isoforms, Thermogenesis, Mitochondrial Proteins, Membrane Transport Proteins
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review