Uncoupling protein 2 in the glial response to stress: Implications for neuroprotection

Molecular dissection of reactive astrogliosis and glial scar formation

Sofroniew, M. V. (2009) · Trends in Neurosciences · doi:10.1016/j.tins.2009.08.002 · Cited by 2,594 · see citing works

Differential Roles of M1 and M2 Microglia in Neurodegenerative Diseases

Tang, Y., & Le, W. (2016) · Molecular Neurobiology · doi:10.1007/s12035-014-9070-5 · Cited by 2,190 · see citing works

High protonic potential actuates a mechanism of production of reactive oxygen species in mitochondria

Korshunov, S. S., Skulachev, V. P., & Starkov, A. A. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)01159-9 · Cited by 1,727 · 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

The mitochondrial uncoupling-protein homologues

Krauss, S., Zhang, C., & Lowell, B. B. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1592 · Cited by 663 · see citing works

Uncoupling protein-2 prevents neuronal death and diminishes brain dysfunction after stroke and brain trauma

Mattiasson, G., Shamloo, M., Gido, G., Mathi, K., Tomasevic, G., Yi, S., Warden, C. H., Castilho, R. F., Melcher, T., Gonzalez-Zulueta, M., et al. (2003) · Nature Medicine · doi:10.1038/nm903 · Cited by 515 · see citing works

UCP2 transports C4 metabolites out of mitochondria, regulating glucose and glutamine oxidation

Vozza, A., Parisi, G., De Leonardis, F., Lasorsa, F. M., Castegna, A., Amorese, D., Marmo, R., Calcagnile, V. M., Palmieri, L., Ricquier, D., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1317400111 · Cited by 407 · see citing works

Inhibition of NADPH oxidase promotes alternative and anti‐inflammatory microglial activation during neuroinflammation

Choi, S., Aïd, S., Kim, H., Jackson, S. H., & Bosetti, F. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07572.x · Cited by 222 · see citing works

UCP2, a mitochondrial protein regulated at multiple levels

Donadelli, M., Dando, I., Fiorini, C., & Palmieri, M. (2013) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-013-1407-0 · Cited by 176 · see citing works

Uncoupling protein 2 deficiency aggravates astrocytic endoplasmic reticulum stress and nod-like receptor protein 3 inflammasome activation

Lu, M., Sun, X., Qiao, C., Liu, Y., Ding, J., & Hu, G. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2013.08.015 · Cited by 91 · see citing works

The mitochondrial uncoupling protein‐2 is a master regulator of both M1 and M2 microglial responses

Simone, R. D., Ajmone‐Cat, M. A., Pandolfi, M., Bernardo, A., Nuccio, C. D., Minghetti, L., & Visentin, S. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.13244 · Cited by 72 · see citing works

Stat3 mediates LIF‐induced protection of astrocytes against toxic ROS by upregulating the UPC2 mRNA pool

Lapp, D. W., Zhang, S. S.-M., & Barnstable, C. J. (2013) · Glia · doi:10.1002/glia.22594 · Cited by 38 · see citing works

Control of Mitochondrial pH by Uncoupling Protein 4 in Astrocytes Promotes Neuronal Survival

Perreten, H., Zenger, M., Azarias, G., Chatton, J., Magistretti, P. J., & Lengacher, S. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.570879 · Cited by 29 · see citing works

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 · see citing works

Mitochondrial Uncoupling: A Key Controller of Biological Processes in Physiology and Diseases

Demine, S., Renard, P., & Arnould, T. (2019) · Cells · doi:10.3390/cells8080795 · Cited by 476 · see citing works

Lipopolysaccharide‐induced alteration of mitochondrial morphology induces a metabolic shift in microglia modulating the inflammatory response in vitro and in vivo

Nair, S., Sobotka, K. S., Joshi, P., Gressèns, P., Fleiss, B., Thornton, C., Mallard, C. E., & Hagberg, H. (2019) · Glia · doi:10.1002/glia.23587 · Cited by 274 · see citing works

Mitochondrial Uncoupling Proteins: Subtle Regulators of Cellular Redox Signaling

Ježek, P., Holendová, B., Garlid, K., & Jabůrek, M. (2018) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7225 · Cited by 138 · see citing works

Uncoupling proteins in the mitochondrial defense against oxidative stress

Hass, D. T., & Barnstable, C. J. (2021) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2021.100941 · Cited by 101 · see citing works

Uncoupling Protein 2: A Key Player and a Potential Therapeutic Target in Vascular Diseases

Pierelli, G., Stanzione, R., Forte, M., Migliarino, S., Perelli, M., Volpe, M., & Rubattu, S. D. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/7348372 · Cited by 87 · see citing works

Mitochondrial membrane potential and compartmentalized signaling: Calcium, ROS, and beyond

Selim, N. A., & Wojtovich, A. P. (2025) · Redox Biology · doi:10.1016/j.redox.2025.103859 · Cited by 92 · see citing works

LncRNA ANRIL acts as a modular scaffold of WDR5 and HDAC3 complexes and promotes alteration of the vascular smooth muscle cell phenotype

Zhang, C., Ge, S., Gong, W., Xu, J., Guo, Z., Liu, Z., Gao, X., Wei, X., & Ge, S. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-2645-3 · Cited by 86 · see citing works

The Role of MicroRNAs in Environmental Risk Factors, Noise-Induced Hearing Loss, and Mental Stress

Miguel, V., Cui, J. Y., Daimiel, L., Espinosa‐Díez, C., Fernandez-Hernando, C. F., Kavanagh, T. J., & Lamas, S. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7175 · Cited by 77 · see citing works

Uncoupling protein 2 reprograms the tumor microenvironment to support the anti-tumor immune cycle

Cheng, W.-C., Tsui, Y., Ragusa, S., Koelzer, V. H., Mina, M., Franco, F., Laubli, H. P., Tschumi, B., Speiser, D. E., Romero, P. J., et al. (2019) · Nature Immunology · doi:10.1038/s41590-018-0290-0 · Cited by 76 · see citing works

Increasing Nrf2 Activity as a Treatment Approach in Neuropsychiatry

Morris, G., Walker, A. J., Walder, K. R., Berk, M., Marx, W., Carvalho, A. F., Maes, M. H. J., & Puri, B. K. (2021) · Molecular Neurobiology · doi:10.1007/s12035-020-02212-w · Cited by 74 · see citing works

Neuronal autophagy aggravates microglial inflammatory injury by downregulating CX3CL1/fractalkine after ischemic stroke

Deng, Y., He, H., Ren, L., & Guo, T. (2018) · Neural Regeneration Research · doi:10.4103/1673-5374.244793 · Cited by 75 · see citing works

Developmental exposure to Pb2+ induces transgenerational changes to zebrafish brain transcriptome

Meyer, D. N., Crofts, E. J., Akemann, C., Gurdziel, K., Farr, R. L., Baker, B. B., Weber, D. N., & Baker, T. R. (2019) · Chemosphere · doi:10.1016/j.chemosphere.2019.125527 · Cited by 55 · see citing works

Diabetes–Alzheimer's Disease Link: Targeting Mitochondrial Dysfunction and Redox Imbalance

Carvalho, C., & Cardoso, S. (2020) · Antioxidants and Redox Signaling · doi:10.1089/ars.2020.8056 · Cited by 47 · see citing works

Signaling Pathways in Oxidative Stress-Induced Neurodegenerative Diseases: A Review of Phytochemical Therapeutic Interventions

Sebghatollahi, Z., Yogesh, R., Mahato, N., Kumar, V., Mohanta, Y. K., Baek, K.-H., & Mishra, A. K. (2025) · Antioxidants · doi:10.3390/antiox14040457 · Cited by 41 · see citing works

Melatonin decreases M1 polarization via attenuating mitochondrial oxidative damage depending on UCP2 pathway in prorenin-treated microglia

Hu, L., Zhang, S., Wen, H., Liu, T., Cai, J., Du, D., Zhu, D., Chen, F., & Xia, C. (2019) · PLoS ONE · doi:10.1371/journal.pone.0212138 · Cited by 39 · see citing works

Reduced brain UCP2 expression mediated by microRNA-503 contributes to increased stroke susceptibility in the high-salt fed stroke-prone spontaneously hypertensive rat

Rubattu, S. D., Stanzione, R., Bianchi, F., Cotugno, M., Forte, M., Ragione, F. D., Fioriniello, S., D’Esposito, M., Marchitti, S., Madonna, M., et al. (2017) · Cell Death and Disease · doi:10.1038/cddis.2017.278 · Cited by 34 · see citing works

Protective Role of UCP2 in Oxidative Stress and Apoptosis during the Silent Phase of an Experimental Model of Epilepsy Induced by Pilocarpine

Dutra, M. R. H., Feliciano, R. D. S., Jacinto, K. R., Gouveia, T. L. F., Brigidio, E., Serra, A. J., Morris, M., Naffah‐Mazzacoratti, M. D. G., & da Silva, J. A. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/6736721 · Cited by 33 · see citing works

A co-culture nanofibre scaffold model of neural cell degeneration in relevance to Parkinson’s disease

Chemmarappally, J. M., Pegram, H., Abeywickrama, N., Fornari, E., Hargreaves, A. J., Girolamo, L. A. D., & Stevens, B. (2020) · Scientific Reports · doi:10.1038/s41598-020-59310-x · Cited by 27 · see citing works

Deletion of Mitochondrial Uncoupling Protein 2 Exacerbates Mitochondrial Damage in Mice Subjected to Cerebral Ischemia and Reperfusion Injury under both Normo- and Hyperglycemic Conditions

He, M.-T., Ma, Y.-M., Wang, R., Zhang, J.-Z., Jing, L., & Li, P. A. (2020) · International Journal on Biological Sciences · doi:10.7150/ijbs.48204 · Cited by 24 · see citing works

Deletion of mitochondrial uncoupling protein 2 exacerbates mitophagy and cell apoptosis after cerebral ischemia and reperfusion injury in mice

He, M., Zhang, T., Fan, Y., Ma, Y., Zhang, J., Li, J., & Li, P. A. (2020) · International Journal of Medical Sciences · doi:10.7150/ijms.49849 · Cited by 24 · see citing works

Variability in oxidative stress-related genes (SOD2, CAT, GPX1, GSTP1, NOS3, NFE2L2, and UCP2) and susceptibility to migraine clinical phenotypes and features

Papasavva, M., Vikelis, M., Siokas, V., Katsarou, M., Dermitzakis, E. V., Raptis, A., Kalliantasi, A., Dardiotis, E., & Drakoulis, N. (2023) · Frontiers in Neurology · doi:10.3389/fneur.2022.1054333 · Cited by 23 · see citing works

Fatty Acid-Binding Protein 4 is Essential for the Inflammatory and Metabolic Response of Microglia to Lipopolysaccharide

Kagawa, Y., Low, Y. L., Pyun, J., Doglione, U., Short, J. L., Pan, Y., & Nicolazzo, J. A. (2023) · Journal of Neuroimmune Pharmacology · doi:10.1007/s11481-023-10079-6 · Cited by 24 · see citing works

Synthesis and Functionalisation of Superparamagnetic Nano-Rods towards the Treatment of Glioblastoma Brain Tumours

Habra, K., McArdle, S., Morris, R. H., & Cave, G. W. V. (2021) · Nanomaterials · doi:10.3390/nano11092157 · Cited by 21 · see citing works

CuATSM effectively ameliorates ALS patient astrocyte‐mediated motor neuron toxicity in human in vitro models of amyotrophic lateral sclerosis

Dennys, C. N., Roussel, F. S., Rodrigo, R., Zhang, X., Sierra-Delgado, J. A., Hartlaub, A. M., Saelim‐Ector, A., Ray, W., Heintzman, S., Fox, A., et al. (2022) · Glia · doi:10.1002/glia.24278 · Cited by 19 · see citing works

Targeted upregulation of uncoupling protein 2 within the basal ganglia output structure ameliorates dyskinesia after severe liver failure

Bai, Y., Bai, Y., Wang, S., Wu, F., Wang, D. H., Chen, J., Huang, J., Li, H., Li, Y.-Q., Wu, S., et al. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.05.005 · Cited by 17 · see citing works

Glial cells improve Parkinson’s disease by modulating neuronal function and regulating neuronal ferroptosis

Li, M., Chen, M., Li, H., Gao, D., Zhao, L., & Zhu, M. (2025) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2024.1510897 · Cited by 15 · see citing works

FACS-array–based cell purification yields a specific transcriptome of striatal medium spiny neurons in a murine Huntington disease model

Miyazaki, H., Yamanaka, T., Oyama, F., Kino, Y., Kurosawa, M., Yamada-Kurosawa, M., Yamano, R., Shimogori, T., Hattori, N., & Nukina, N. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.012983 · Cited by 12 · see citing works

Protective effect of Fructus corni polysaccharide on hippocampal tissues and its relevant mechanism in epileptic rats induced by lithium chloride‑pilocarpine

Sun, X., Kong, L., & Li, Z. (2018) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2018.6142 · Cited by 13 · see citing works

Bioenergetic-Related Gene Expression in the Hippocampus Predicts Internalizing vs. Externalizing Behavior in a F 2 Cross of Selectively-Bred RatsPreprint

Hebda‐Bauer, E. K., Hagenauer, M. H., Munro, D. B., Blandino, P., Meng, F., Arakawa, K., Chitre, A. S., Ozel, A. B., Mohammadi, P., Watson, S. J., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.07.14.500129 · Cited by 4 · see citing works

Expression of MAPK and inflammasomes in cells of the brain in experimental Alzheimer's disease

Gorina, Y. V., Lopatina, O. L., Komleva, Y. К., Игоревич, Ч. А., & Salmina, A. B. (2017) · Annals of Clinical and Experimental Neurology · doi:10.17816/acen.2017.4.5 · Cited by 2 · see citing works

Bioenergetic-related gene expression in the hippocampus predicts internalizing vs. externalizing behavior in an animal model of temperament

Hebda‐Bauer, E. K., Hagenauer, M. H., Munro, D. B., Blandino, P., Meng, F., Arakawa, K., Stead, J. D. H., Chitre, A. S., Ozel, A. B., Mohammadi, P., et al. (2025) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2025.1469467 · Cited by 2 · see citing works

Decreased Oxidative Stress Markers in Patients with Active and Generalized Vitiligo

Özcan, Y., Karagün, E., & Alpay, M. (2022) · Konuralp Tıp Dergisi · doi:10.18521/ktd.880577 · Cited by 1 · see citing works

Expression of MAPK and Inflammasomes in Brain Cells in Experimental Alzheimer’s Disease

Gorina, Y. V., Lopatina, O. L., Komleva, Y. K., Черных, А. И., & Salmina, A. B. (2018) · Human Physiology · doi:10.1134/s0362119718080042

Uncoupling protein 2: a novel player in neuroprotection

Paradis, É., Clavel, S., Bouillaud, F., Ricquier, D., & Richard, D. (2003) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2003.10.009 · Cited by 52 · see citing works

Uncoupling protein-2 prevents neuronal death and diminishes brain dysfunction after stroke and brain trauma

Mattiasson, G., Shamloo, M., Gido, G., Mathi, K., Tomasevic, G., Yi, S., Warden, C. H., Castilho, R. F., Melcher, T., Gonzalez-Zulueta, M., et al. (2003) · Nature Medicine · doi:10.1038/nm903 · Cited by 515 · see citing works

The mitochondrial uncoupling protein‐2 is a master regulator of both M1 and M2 microglial responses

Simone, R. D., Ajmone‐Cat, M. A., Pandolfi, M., Bernardo, A., Nuccio, C. D., Minghetti, L., & Visentin, S. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.13244 · Cited by 72 · see citing works

Neuroprotective Role of Mitochondrial Uncoupling Protein 2 in Cerebral Stroke

Mehta, S. L., & Li, P. A. (2009) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.2009.4 · Cited by 81 · see citing works

Uncoupling Protein 2 Inhibition Exacerbates Glucose Fluctuation-Mediated Neuronal Effects

Cardoso, S., Seiça, R. M. F., & Moreira, P. I. (2017) · Neurotoxicity Research · doi:10.1007/s12640-017-9805-y · Cited by 16 · see citing works