CNS Peroxiredoxins and Their Regulation in Health and Disease
Abstract
Oxidative stress is thought to be a contributing factor in many chronic neurodegenerative pathologies, as well as acute cerebrovascular disorders such as stroke. Peroxiredoxins are a family of antioxidant enzymes that reduce peroxides directly through the use of a redox active cysteine within their active site, which in the process becomes oxidized. In order to cycle back to the reduced state, many peroxiredoxins rely on thiol-dependent reduction by the ubiquitous antioxidant enzyme thioredoxin. Peroxiredoxins, together with thioredoxin and thioredoxin's own ‘recycling enzyme’, thioredoxin reductase, represent an antioxidant enzymic system of growing significance in the context of neuronal physiology and pathology. Overexpression, knockdown, and knockout approaches have demonstrated an important role for peroxiredoxins in protecting neurons from oxidative insults. It is also becoming clear that neuronal peroxiredoxins are subjected to post-translational modifications that impair function as part of disease pathology. Conversely, components of this pathway are also subject to dynamic upregulation such as via endogenous synaptic activity-dependent signaling and induction of the Nrf2-dependent Phase II response. As such, the thioredoxin-peroxiredoxin system represents a potential therapeutic target for central nervous system disorders associated with oxidative stress. Antioxid. Redox Signal. 14, 1467–1477.
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The GSH deficit induced by NMDAR blockade in the developing mouse is associated with transcriptional downregulation of Gclc and reduced GCL activity, which contributes to the deleterious effects observed in vivo.
“Of note, the GSH deficit induced by NMDAR blockade in the developing mouse is associated with transcriptional downregulation of Gclc and reduced GCL activity, which contributes to the deleterious effects observed in vivo 77 .”
From Linking early-life NMDAR hypofunction and oxidative stress in schizophrenia pathogenesis (2016) · cites this paper as [77]
Synaptic NMDAR activity enhances the capacity of both the glutathione system and the thioredoxin/peroxiredoxin system through the transcriptional control of several key antioxidant genes.
“At the cellular level, synaptic NMDAR activity enhances the capacity of both the glutathione system and thioredoxin/peroxiredoxin system (another important antioxidant pathway in the brain 75 ) through the transcriptional control of several key antioxidant genes 73,76,77 (Figure.4).”
From Linking early-life NMDAR hypofunction and oxidative stress in schizophrenia pathogenesis (2016) · cites this paper as [77]
By increasing the supply of GSH precursors to neurons, the action of astrocytic NFE2L2 is additive and complementary to the effects of synaptic NMDA receptor activity in boosting GSH biosynthetic capacity.
“By increasing the supply of GSH precursors to neurons, the action of astrocytic NFE2L2 is additive and complementary to the effects of synaptic NMDA receptor activity in boosting GSH biosynthetic capacity 77 (see Figure.3).”
From Linking early-life NMDAR hypofunction and oxidative stress in schizophrenia pathogenesis (2016) · cites this paper as [77]
Cites
Aging: a theory based on free radical and radiation chemistry
Harman, D. (1956) · Journal of Gerontology · doi:10.1093/geronj/11.3.298 · Cited by 8,567 · see citing works
Cell Survival Responses to Environmental Stresses Via the Keap1-Nrf2-ARE Pathway
Kensler, T. W., Wakabayashi, N., & Biswal, S. (2007) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.46.120604.141046 · Cited by 3,630 · see citing works
Oxidative stress and neurodegeneration: where are we now?
Halliwell, B. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.03907.x · Cited by 2,614 · see citing works
Structure, mechanism and regulation of peroxiredoxins
Wood, Z. A., Schröder, E., Harris, J. R., & Poole, L. B. (2003) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(02)00003-8 · Cited by 2,546 · see citing works
Blockade of NMDA Receptors and Apoptotic Neurodegeneration in the Developing Brain
Ikonomidou, C., Bosch, F., Miksa, M., Bittigau, P., Vöckler, J., Dikranian, K., Tenkova, T. I., Stefovska, V., Turski, L., & Olney, J. W. (1999) · Science · doi:10.1126/science.283.5398.70 · Cited by 2,055 · see citing works
Gene regulation and DNA damage in the ageing human brain
Lu, T., Pan, Y., Kao, S.-Y., Li, C., Kohane, I., Chan, J., & Yankner, B. A. (2004) · Nature · doi:10.1038/nature02661 · Cited by 1,874 · see citing works
Calcium-mediated neurotoxicity: relationship to specific channel types and role in ischemic damage
Choi, D. W. (1988) · Trends in Neurosciences · doi:10.1016/0166-2236(88)90200-7 · Cited by 1,726 · see citing works
Extrasynaptic NMDARs oppose synaptic NMDARs by triggering CREB shut-off and cell death pathways
Hardingham, G. E., Fukunaga, Y., & Bading, H. (2002) · Nature Neuroscience · doi:10.1038/nn835 · Cited by 1,686 · see citing works
Self-citationGlutamate release in severe brain ischaemia is mainly by reversed uptake
Rossi, D. J., Oshima, T., & Attwell, D. (2000) · Nature · doi:10.1038/35002090 · Cited by 1,128 · see citing works
Mechanistic Studies of the Nrf2-Keap1 Signaling Pathway
Zhang, D. D. (2006) · Drug Metabolism Reviews · doi:10.1080/03602530600971974 · Cited by 1,091 · see citing works
ATP-dependent reduction of cysteine–sulphinic acid by S. cerevisiae sulphiredoxin
Biteau, B., Labarre, J., & Tolédano, M. B. (2003) · Nature · doi:10.1038/nature02075 · Cited by 970 · see citing works
Oxidative Stress and Its Role in the Pathogenesis of Ischaemic Stroke
Allen, C., & Bayraktutan, U. (2009) · International Journal of Stroke · doi:10.1111/j.1747-4949.2009.00387.x · Cited by 969 · see citing works
S-Nitrosylated protein-disulphide isomerase links protein misfolding to neurodegeneration
Uehara, T., Nakamura, T., Yao, D., Shi, Z., Gu, Z., Ma, Y., Masliah, E., Nomura, Y., & Lipton, S. A. (2006) · Nature · doi:10.1038/nature04782 · Cited by 908 · see citing works
Shih, A. Y., Johnson, D. A., Wong, G., Kraft, A. D., Jiang, L., Erb, H., Johnson, J. A., & Murphy, T. H. (2003) · Journal of Neuroscience · doi:10.1523/jneurosci.23-08-03394.2003 · Cited by 786 · see citing works
S -Nitrosylation of Parkin Regulates Ubiquitination and Compromises Parkin's Protective Function
Chung, K. K. K., Thomas, B., Li, X., Pletniková, O., Troncoso, J. C., Marsh, L., Dawson, V. L., & Dawson, T. M. (2004) · Science · doi:10.1126/science.1093891 · Cited by 765 · see citing works
Regeneration of peroxiredoxins by p53-regulated sestrins, homologs of bacterial AhpD
Budanov, A. V., Sablina, A. A., Feinstein, E., Koonin, E. V., & Chumakov, P. M. (2004) · Science · doi:10.1126/science.1095569 · Cited by 731 · see citing works
Enomoto, A. (2001) · Toxicological Sciences · doi:10.1093/toxsci/59.1.169 · Cited by 728 · see citing works
Oxidative stress in brain aging, neurodegenerative and vascular diseases: An overview
Mariani, E., Polidori, M. C., Cherubini, A., & Mecocci, P. (2005) · Journal of Chromatography B · doi:10.1016/j.jchromb.2005.04.023 · Cited by 682 · see citing works
Keap1/Nrf2 Signaling Regulates Oxidative Stress Tolerance and Lifespan in Drosophila
Sykiotis, G. P., & Bohmann, D. (2008) · Developmental Cell · doi:10.1016/j.devcel.2007.12.002 · Cited by 675 · see citing works
Role of NRF2 in Protection Against Hyperoxic Lung Injury in Mice
Cho, H., Jedlicka, A., Reddy, S. P., Kensler, T. W., Yamamoto, M. P., Zhang, L.-Y., & Kleeberger, S. R. (2002) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/ajrcmb.26.2.4501 · Cited by 660 · see citing works
NMDA-receptor-mediated, cell-specific integration of new neurons in adult dentate gyrus
Tashiro, A., Sandler, V. M., Toni, N., Zhao, C., & Gage, F. H. (2006) · Nature · doi:10.1038/nature05028 · Cited by 620 · see citing works
Distinct Roles of Thioredoxin in the Cytoplasm and in the Nucleus
Hirota, K., Murata, M., Sachi, Y., Nakamura, H., Takeuchi, J. S., Mori, K., & Yodoi, J. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.39.27891 · Cited by 610 · see citing works
FoxO transcription factors in the maintenance of cellular homeostasis during aging
Salih, D. A., & Brunet, A. (2008) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2008.02.005 · Cited by 604 · see citing works
Johnson, J. A., Johnson, D. A., Kraft, A. D., Calkins, M. J., Jakel, R. J., Vargas, M. R., & Chen, P. (2008) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1427.036 · Cited by 588 · see citing works
Liu, H., Nishitoh, H., Ichijo, H., & Kyriakis, J. M. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.6.2198-2208.2000 · Cited by 545 · see citing works
Kraft, A. D., Johnson, D. A., & Johnson, J. A. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.3817-03.2004 · Cited by 541 · see citing works
Nrf2, a multi‐organ protector?
Lee, J., Li, J., Johnson, D. A., Stein, T. D., Kraft, A. D., Calkins, M. J., Jakel, R. J., & Johnson, J. A. (2005) · The FASEB Journal · doi:10.1096/fj.04-2591hyp · Cited by 532 · see citing works
The complexity of neurobiological processes in acute ischemic stroke
Brouns, R., & Deyn, P. P. D. (2009) · Clinical Neurology and Neurosurgery · doi:10.1016/j.clineuro.2009.04.001 · Cited by 527 · see citing works
Synaptic NMDA receptor activity boosts intrinsic antioxidant defenses
Papadia, S., Soriano, F. X., Léveillé, F., Martel, M.-A., Dakin, K. A., Hansen, H. H., Kaindl, A., Sifringer, M., Fowler, J., Stefovska, V., et al. (2008) · Nature Neuroscience · doi:10.1038/nn2071 · Cited by 498 · see citing works
Self-citationThe pathways and molecular mechanisms regulating Nrf2 activation in response to chemical stress
Nguyen, T., Yang, C. S., & Pickett, C. B. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.04.033 · Cited by 463 · see citing works
Thioredoxin-dependent Redox Regulation of p53-mediated p21 Activation
Ueno, M., Masutani, H., Arai, R. J., Yamauchi, A., Hirota, K., Sakai, T., Inamoto, T., Yamaoka, Y., Yodoi, J., & Nikaido, T. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.50.35809 · Cited by 428 · see citing works
Shih, A. Y., Li, P., & Murphy, T. H. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.4014-05.2005 · Cited by 413 · see citing works
Peskin, A. V., Low, F. M., Paton, L. N., Maghzal, G. J., Hampton, M. B., & Winterbourn, C. C. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m700339200 · Cited by 394 · see citing works
Chang, T.-S., Jeong, W., Woo, H. A., Lee, S. M., Park, S., & Rhee, S. G. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409482200 · Cited by 388 · see citing works
Schulze, P. C., Yoshioka, J., Takahashi, T., He, Z., King, G. L., & Lee, R. T. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m400549200 · Cited by 369 · see citing works
Regulation of Neuronal Glutathione Synthesis
Aoyama, K., Watabe, M., & Nakaki, T. (2008) · Journal of Pharmacological Sciences · doi:10.1254/jphs.08r01cr · Cited by 356 · see citing works
Activation of the Keap1/Nrf2 pathway for neuroprotection by electrophillic phase II inducers
Satoh, T., Okamoto, S.-I., Cui, J., Watanabe, Y., Furuta, K., Suzuki, M., Tohyama, K., & Lipton, S. A. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0505723102 · Cited by 342 · see citing works
Overexpression of thioredoxin in transgenic mice attenuates focal ischemic brain damage
Takagi, Y., Mitsui, A., Nishiyama, A., Nozaki, K., Sono, H., Gon, Y., Hashimoto, N., & Yodoi, J. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.7.4131 · Cited by 337 · see citing works
Antioxidant Activities of Bile Pigments
Stocker, R. (2004) · Antioxidants and Redox Signaling · doi:10.1089/ars.2004.6.841 · Cited by 313 · see citing works
Hemin-induced Activation of the Thioredoxin Gene by Nrf2
Kim, Y. C., Masutani, H., Yamaguchi, Y., Itoh, K., Yamamoto, M. P., & Yodoi, J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100103200 · Cited by 313 · see citing works
Zhang, S., Zou, M., Lü, L., Lau, D., Ditzel, D. A. W., Delucinge-Vivier, C., Aso, Y., Descombes, P., & Bading, H. (2009) · PLoS Genetics · doi:10.1371/journal.pgen.1000604 · Cited by 311 · see citing works
Smith, P. D., Crocker, S. J., Jackson-Lewis, V. R., Jordan‐Sciutto, K. L., Hayley, S. P., Mount, M. P., O'Hare, M. J., Callaghan, S. M., Slack, R. S., Przedborski, S., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2232515100 · Cited by 310 · see citing works
Lee, J.-M., Shih, A. Y., Murphy, T. H., & Johnson, J. A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305204200 · Cited by 308 · see citing works
Glucose and NADPH oxidase drive neuronal superoxide formation in stroke
Suh, S. W., Shin, B. S., Ma, H., Hoecke, M. V., Brennan, A. M., Yenari, M. A., & Swanson, R. A. (2008) · Annals of Neurology · doi:10.1002/ana.21511 · Cited by 292 · see citing works
Aberrant expression of peroxiredoxin subtypes in neurodegenerative disorders
Krapfenbauer, K., Engidawork, E., Cairns, N. J., Fountoulakis, M., & Lübec, G. (2003) · Brain Research · doi:10.1016/s0006-8993(02)04243-9 · Cited by 288 · see citing works
Inhibition of NADPH Oxidase is Neuroprotective after Ischemia—Reperfusion
Chen, H., Song, Y. S., & Chan, P. H. (2009) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.2009.47 · Cited by 286 · see citing works
Synaptic and Extrasynaptic NMDA Receptor NR2 Subunits in Cultured Hippocampal Neurons
Thomas, C. G., Miller, A., & Westbrook, G. L. (2005) · Journal of Neurophysiology · doi:10.1152/jn.00771.2005 · Cited by 286 · see citing works
Papadia, S., Stevenson, P., Hardingham, N. R., Bading, H., & Hardingham, G. E. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.5019-04.2005 · Cited by 262 · see citing works
Self-citationCoupling of the NMDA receptor to neuroprotective and neurodestructive events
Hardingham, G. E. (2009) · Biochemical Society Transactions · doi:10.1042/bst0371147 · Cited by 260 · see citing works
Self-citationFang, J., Nakamura, T., Cho, D., Gu, Z., & Lipton, S. A. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0705904104 · Cited by 256 · see citing works
Nrf2-mediated protection against 6-hydroxydopamine
Jakel, R. J., Townsend, J. A., Kraft, A. D., & Johnson, J. A. (2007) · Brain Research · doi:10.1016/j.brainres.2007.01.131 · Cited by 252 · see citing works
Role of Cdk5-Mediated Phosphorylation of Prx2 in MPTP Toxicity and Parkinson's Disease
Qu, D., Rashidian, J., Mount, M. P., Aleyasin, H., Parsanejad, M., Lira, A., Haque, E., Zhang, Y., Callaghan, S. M., Daigle, M., et al. (2007) · Neuron · doi:10.1016/j.neuron.2007.05.033 · Cited by 251 · see citing works
Thioredoxin, a Singlet Oxygen Quencher and Hydroxyl Radical Scavenger: Redox Independent Functions
Das, K. C., & Das, C. K. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.3689 · Cited by 250 · see citing works
Blockade of NMDA receptors increases cell death and birth in the developing rat dentate gyrus
Gould, E., Cameron, H. A., & McEwen, B. S. (1994) · The Journal of Comparative Neurology · doi:10.1002/cne.903400408 · Cited by 244 · see citing works
Pohl, D., Bittigau, P., Ishimaru, M. J., Stadthaus, D., Hübner, C., Olney, J. W., Turski, L., & Ikonomidou, C. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.5.2508 · Cited by 235 · see citing works
Activation of the Nrf2–ARE signaling pathway: a promising strategy in cancer prevention
Giudice, A., & Montella, M. (2006) · BioEssays · doi:10.1002/bies.20359 · Cited by 232 · see citing works
Camacho, A., & Massieu, L. (2006) · Archives of Medical Research · doi:10.1016/j.arcmed.2005.05.014 · Cited by 206 · see citing works
Ogusucu, R., Rettori, D., Munhoz, D. C., Netto, L. E. S., & Augusto, O. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2006.10.042 · Cited by 196 · see citing works
Cell death: protein misfolding and neurodegenerative diseases
Nakamura, T., & Lipton, S. A. (2009) · APOPTOSIS · doi:10.1007/s10495-008-0301-y · Cited by 191 · see citing works
Neuronal death enhanced by N -methyl- d -aspartate antagonists
Ikonomidou, C., Stefovska, V. G., & Turski, L. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.220412197 · Cited by 188 · see citing works
Yang, L., Calingasan, N. Y., Thomas, B., Chaturvedi, R. K., Kiaei, M., Wille, E. J., Liby, K. T., Williams, C. R., Royce, D. B., Risingsong, R., et al. (2009) · PLoS ONE · doi:10.1371/journal.pone.0005757 · Cited by 172 · see citing works
Nadeau, P. J., Charette, S. J., Tolédano, M. B., & Landry, J. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-05-0491 · Cited by 171 · see citing works
Rhee, S. G., Jeong, W., Chang, T. S., & Woo, H. A. (2007) · Kidney International · doi:10.1038/sj.ki.5002380 · Cited by 159 · see citing works
Martel, M., Wyllie, D. J. A., & Hardingham, G. E. (2008) · Neuroscience · doi:10.1016/j.neuroscience.2008.01.080 · Cited by 149 · see citing works
Self-citationSuppression of the Intrinsic Apoptosis Pathway by Synaptic Activity
Léveillé, F., Papadia, S., Fricker, M., Bell, K. F. S., Soriano, F. X., Martel, M., Puddifoot, C. A., Habel, M., Wyllie, D. J. A., Ikonomidou, C., et al. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.5115-09.2010 · Cited by 145 · see citing works
Self-citationSoriano, F. X., Léveillé, F., Papadia, S., Higgins, L. G., Varley, J. A., Baxter, P. S., Hayes, J. D., & Hardingham, G. E. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05648.x · Cited by 144 · see citing works
Self-citationTranscriptional Regulation of the AP-1 and Nrf2 Target Gene Sulfiredoxin
Soriano, F. X., Baxter, P. S., Murray, L. M., Sporn, M. B., Gillingwater, T. H., & Hardingham, G. E. (2009) · Molecules and Cells · doi:10.1007/s10059-009-0050-y · Cited by 142 · see citing works
Self-citationSurvival Signaling Pathways Activated by NMDA Receptors
Hetman, M., & Kharebava, G. (2006) · Current Topics in Medicinal Chemistry · doi:10.2174/156802606777057553 · Cited by 141 · see citing works
Lee, K., Iijima‐Ando, K., Iijima, K., Lee, W., Lee, J., Yu, K., & Lee, D. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.028027 · Cited by 139 · see citing works
Existing and emerging mechanisms for transport of iron and manganese to the brain
Malecki, E. A., Devenyi, A. G., Beard, J. L., & Connor, J. R. (1999) · Journal of Neuroscience Research · doi:10.1002/(sici)1097-4547(19990415)56:2 · Cited by 137 · see citing works
Reed, T. T., Pierce Jr., W. M., Turner, D. M., Markesbery, W. R., & Allan Butterfield, D. (2009) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2008.00478.x · Cited by 135 · see citing works
Mitochondrial peroxiredoxin‐3 protects hippocampal neurons from excitotoxic injury in vivo
Hattori, F., Murayama, N., Noshita, T., & Oikawa, S. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01918.x · Cited by 132 · see citing works
Forder, J. P., & Tymianski, M. (2008) · Neuroscience · doi:10.1016/j.neuroscience.2008.10.021 · Cited by 123 · see citing works
Deregulated Cdk5 promotes oxidative stress and mitochondrial dysfunction
Sun, K., de Pablo, Y., Vincent, F., & Shah, K. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05616.x · Cited by 123 · see citing works
Characterization of neural cell types expressing peroxiredoxins in mouse brain
Jin, M., Lee, Y., Kim, J., Sun, H., Moon, E., Shong, M., Kim, S.-U., Lee, S. H., Lee, T., Yu, D., et al. (2005) · Neuroscience Letters · doi:10.1016/j.neulet.2005.02.048 · Cited by 109 · see citing works
Yoshida, Y., Yoshikawa, A., Kinumi, T., Ogawa, Y., Saito, Y., Ohara, K., Yamamoto, H., Imai, Y., & Niki, E. (2007) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2007.06.012 · Cited by 105 · see citing works
Radyuk, S. N., Michalak, K., Klichko, V. I., Benes, J. J., Rebrin, I., Sohal, R. S., & Orr, W. C. (2009) · Biochemical Journal · doi:10.1042/bj20082003 · Cited by 102 · see citing works
Emerging roles of thioredoxin cycle enzymes in the central nervous system
Patenaude, A., Murthy, M. R., & Mirault, M. (2005) · Cellular and Molecular Life Sciences (CMLS) · doi:10.1007/s00018-005-4541-5 · Cited by 101 · see citing works
Pro-survival signalling from the NMDA receptor
Hardingham, G. E. (2006) · Biochemical Society Transactions · doi:10.1042/bst0340936 · Cited by 100 · see citing works
Self-citationActivation of Nrf2–ARE pathway in brain after traumatic brain injury
Yan, W. X., Wang, H., Hu, Z.-G., Wang, Q.-F., & Yin, H.-X. (2008) · Neuroscience Letters · doi:10.1016/j.neulet.2007.11.060 · Cited by 97 · see citing works
Sestrin 2 Is Not a Reductase for Cysteine Sulfinic Acid of Peroxiredoxins
Woo, H. A., Bae, S. H., Park, S., & Rhee, S. G. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2360 · Cited by 96 · see citing works
Monti, B., & Contestabile, A. (2000) · European Journal of Neuroscience · doi:10.1046/j.1460-9568.2000.00189.x · Cited by 92 · see citing works
Yoshida, T., Nakamura, H., Masutani, H., & Yodoi, J. (2005) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1323.002 · Cited by 92 · see citing works
Role of sestrin2 in peroxide signaling in macrophages
Essler, S., Dehne, N., & Brüne, B. (2009) · FEBS Letters · doi:10.1016/j.febslet.2009.10.017 · Cited by 90 · see citing works
Yao, J., Taylor, M., Davey, F. D., Ren, Y., Aiton, J., Coote, P. J., Fang, F., Chen, J. X., Yan, S. D., & Gunn‐Moore, F. J. (2007) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2007.03.013 · Cited by 84 · see citing works
Lau, D., & Bading, H. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.0802-09.2009 · Cited by 82 · see citing works
Mubarak, B. R. A., Soriano, F. X., & Hardingham, G. E. (2009) · Channels · doi:10.4161/chan.3.4.9381 · Cited by 82 · see citing works
Self-citationPronounced Cell Death in the Absence of NMDA Receptors in the Developing Somatosensory Thalamus
Adams, S. M., Vaccari, J. C. D. R., & Corriveau, R. A. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.3290-04.2004 · Cited by 80 · see citing works
Typical 2‐Cys peroxiredoxins – modulation by covalent transformations and noncovalent interactions
Arán, M., Ferrero, D. S., Pagano, E. A., & Wolosiuk, R. A. (2009) · FEBS Journal · doi:10.1111/j.1742-4658.2009.06984.x · Cited by 74 · see citing works
Essential Role of Cytoplasmic cdk5 and Prx2 in Multiple Ischemic Injury Models,In Vivo
Rashidian, J., Rousseaux, M. W. C., Venderová, K., Qu, D., Callaghan, S. M., Phillips, M., Bland, R. J., During, M. J., Mao, Z., Slack, R. S., et al. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.3892-09.2009 · Cited by 74 · see citing works
Hwang, I. K., Yoo, K., Kim, D. W., Lee, C. H., Choi, J. H., Kwon, Y., Kim, Y., Choi, S. Y., & Won, M. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.02.007 · Cited by 68 · see citing works
Compartmentalized NMDA receptor signalling to survival and death
Soriano, F. X., & Hardingham, G. E. (2007) · The Journal of Physiology · doi:10.1113/jphysiol.2007.138875 · Cited by 65 · see citing works
Self-citationCumming, R. C., Dargusch, R., Fischer, W. H., & Schubert, D. A. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m700869200 · Cited by 61 · see citing works
Samouilidou, E. C., & Grapsa, E. J. (2003) · Blood Purification · doi:10.1159/000070691 · Cited by 61 · see citing works
Accumulation of overoxidized Peroxiredoxin III in aged rat liver mitochondria
Musicco, C., Capelli, V., Pesce, V., Timperio, A. M., Calvani, M., Mosconi, L., Zolla, L., Cantatore, P., & Gadaleta, M. N. (2009) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2009.03.002 · Cited by 60 · see citing works
Peroxiredoxin II preserves cognitive function against age-linked hippocampal oxidative damage
Kim, S., Jin, M.-H., Kim, Y. S., Lee, S., Cho, Y. S., Cho, K.-J., Lee, K., Kim, Y. I., Kim, G. W., Kim, J., et al. (2009) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2009.05.017 · Cited by 56 · see citing works
Boulos, S., Meloni, B. P., Arthur, P. G., Bojarski, C., & Knuckey, N. W. (2007) · Journal of Neuroscience Research · doi:10.1002/jnr.21429 · Cited by 55 · see citing works
Lipton, S. A., Nakamura, T., Yao, D., Shi, Z., Uehara, T., & Gu, Z. (2005) · Science · doi:10.1126/science.1110135 · Cited by 52 · see citing works
NMDA receptor activity regulates transcription of antioxidant pathways
Lipton, S. A. (2008) · Nature Neuroscience · doi:10.1038/nn0408-381 · Cited by 45 · see citing works
Excitotoxic Hippocampal Injury is Attenuated in Thioredoxin Transgenic Mice
Takagi, Y., Hattori, I., Nozaki, K., Mitsui, A., Ishikawa, M., Hashimoto, N., & Yodoi, J. (2000) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1097/00004647-200005000-00009 · Cited by 33 · see citing works
Wang, Q., Zhao, X., He, S., Liu, Y., An, M., & Ji, J. (2009) · Neurochemical Research · doi:10.1007/s11064-009-0023-8 · Cited by 22 · see citing works
Yoo, K., Park, O. K., Yu, J., Yan, B., Li, H., Lee, C. H., Choi, J. H., Kim, D. W., Hwang, I. K., & Won, M. (2008) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-008-9333-7 · Cited by 9 · see citing works
Excitotoxic Insults Lead to Peroxiredoxin Hyperoxidation
Léveillé, F., Soriano, F. X., Papadia, S., & Hardingham, G. E. (2009) · Oxidative Medicine and Cellular Longevity · doi:10.4161/oxim.2.2.8300 · Cited by 9 · see citing works
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Functions and mechanisms of microglia/macrophages in neuroinflammation and neurogenesis after stroke
Xiong, X., Liu, L., & Yang, Q. (2016) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2016.05.001 · Cited by 703 · see citing works
Metabolism and functions of copper in brain
Scheiber, I. F., Mercer, J. F. B., & Dringen, R. (2014) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2014.01.002 · Cited by 511 · see citing works
The Thioredoxin System as a Therapeutic Target in Human Health and Disease
Mahmood, D. F. D., Abderrazak, A., Hadri, K. E., Simmet, T., & Rouis, M. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4757 · Cited by 305 · see citing works
Hasel, P., Dando, O., Jiwaji, Z., Baxter, P. S., Todd, A., Heron, S., Márkus, N. M., McQueen, J., Hampton, D. W., Torvell, M., et al. (2017) · Nature Communications · doi:10.1038/ncomms15132 · Cited by 305 · see citing works
Self-citationLinking early-life NMDAR hypofunction and oxidative stress in schizophrenia pathogenesis
Hardingham, G. E., & Do, K. Q. (2016) · Nature Reviews Neuroscience · doi:10.1038/nrn.2015.19 · Cited by 304 · see citing works
Self-citationOxidative Stress in Neurodegenerative Diseases: Mechanisms and Therapeutic Perspectives
Melo, A. D. S., Monteiro, L., Lima, R. M. F., de Oliveira, D. M., de Cerqueira, M. D., & El-Bachá, R. D. S. (2011) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2011/467180 · Cited by 252 · see citing works
Nrf2-dependent persistent oxidative stress results in stress-induced vulnerability to depression
Bouvier, E., Brouillard, F., Molet, J., Claverie, D., Cabungcal, J.-H., Cresto, N., Doligez, N., Rivat, C., Do, K. Q., Bernard, C., et al. (2017) · Molecular Psychiatry · doi:10.1038/mp.2016.144 · Cited by 248 · see citing works
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Zeldich, E., Chen, C.-D., Colvin, T. A., Bove‐Fenderson, E., Liang, J. J., Zhou, T. B. T., Harris, D. A., & Abraham, C. R. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.567321 · Cited by 225 · see citing works
Bell, K. F. S., Al-Mubarak, B., Martel, M.-A., McKay, S., Wheelan, N., Hasel, P., Márkus, N. M., Baxter, P., Deighton, R. F., Serio, A., et al. (2015) · Nature Communications · doi:10.1038/ncomms8066 · Cited by 191 · see citing works
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Nijland, P. G., Witte, M. E., van het Hof, B., van der Pol, S., Bauer, J., Lassmann, H., van der Valk, P., de Vries, H. E., & van Horssen, J. (2014) · Acta Neuropathologica Communications · doi:10.1186/s40478-014-0170-2 · Cited by 96 · see citing works
Gokhale, A., Larimore, J., Werner, E., So, L., Moreno-De-Luca, A., Lese-Martin, C., Lupashin, V. V., Smith, Y., & Faundez, V. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.5640-11.2012 · Cited by 85 · see citing works
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Jia, Q., & Sieburth, D. (2021) · Nature Communications · doi:10.1038/s41467-021-22561-x · Cited by 77 · see citing works
Ren, B., Yuan, T., Diao, Z., Zhang, C., Liu, Z., & Liu, X. (2018) · Food & Function · doi:10.1039/c8fo01436a · Cited by 74 · see citing works
Rossetti, A. C., Paladini, M. S., Riva, M. A., & Molteni, R. (2020) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2020.107520 · Cited by 70 · see citing works
Yang, Y., Cuevas, S., Yang, S., Villar, V. A. M., Escano, C. S., Asico, L. D., Yu, P., Jiang, X., Weinman, E. J., Armando, I., et al. (2014) · Hypertension · doi:10.1161/hypertensionaha.114.03840 · Cited by 67 · see citing works
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RetractedHardingham, G. E., & Lipton, S. A. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3573 · Cited by 64 · see citing works
Self-citationSun, J., Ren, X. S., & Simpkins, J. W. (2015) · Molecular Pharmacology · doi:10.1124/mol.115.098269 · Cited by 60 · see citing works
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Self-citationLee, D. G., Kam, M. K., Lee, S., Lee, H. J., & Lee, D. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-2402-7 · Cited by 51 · see citing works
Zeida, A., Reyes, A. M., Lebrero, M. C. G., Radí, R., Trujillo, M., & Estrin, D. A. (2014) · Chemical Communications · doi:10.1039/c4cc02899f · Cited by 49 · see citing works
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Li, L., Zhu, K., Liu, Y., Wu, X., Wu, J., Zhao, Y., & Zhao, J. (2014) · Neuroscience · doi:10.1016/j.neuroscience.2014.10.066 · Cited by 46 · see citing works
Lee, D. G., Kam, M. K., Kim, K., Kim, H. S., Kwon, O., Lee, H., & Lee, D.-S. (2018) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2018.06.005 · Cited by 45 · see citing works
Xu, Z., Zhang, L., Wang, Q., Marshall, C., Xiao, N., Gao, J., Wu, T., Ding, J., Hu, G., & Xiao, M. (2013) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.12139 · Cited by 44 · see citing works
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Self-citationChen, J., Li, X., Xu, S., Zhang, M., Wu, Z., Zhang, X., Xu, Y., & Chen, Y. (2020) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2020.00077 · Cited by 33 · see citing works
Gupta, K., Chandran, S., & Hardingham, G. (2012) · British Journal of Clinical Pharmacology · doi:10.1111/bcp.12022 · Cited by 38 · see citing works
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Zhao, J., Qu, Y., Gao, H., Zhong, M., Li, X., Zhang, F., Chen, Y., Gan, L., Hu, G., Zhang, H., et al. (2020) · Chemical Communications · doi:10.1039/d0cc05900e · Cited by 30 · see citing works
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Burnside, S. W., & Hardingham, G. E. (2017) · Biochemical Society Transactions · doi:10.1042/bst20170013 · Cited by 21 · see citing works
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Teng, F. Y. H., & Tang, B. L. (2013) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-013-1776-6 · Cited by 16 · see citing works
Khodaie, N., Tajuddin, N. F., Mitchell, R. M., Neafsey, E. J., & Collins, M. A. (2018) · Neurotoxicity Research · doi:10.1007/s12640-018-9886-2 · Cited by 15 · see citing works
Lee, D. G., Kim, K., Lee, H., Bae, Y. C., Huh, J., Lee, S., & Lee, D. (2019) · NeuroToxicology · doi:10.1016/j.neuro.2019.08.003 · Cited by 14 · see citing works
Liang, X., Li, Y., Chu, P., Wang, Q., Wang, H., Liao, L., Yang, C., Zhu, Z., Wang, Y., & He, L. (2022) · Antioxidants · doi:10.3390/antiox11101952 · Cited by 13 · see citing works
Paladini, M. S., Spero, V., Begni, V., Marchisella, F., Guidi, A., Gruca, P., Łasoń, M., Litwa, E., Papp, M., Riva, M. A., et al. (2020) · Pharmacological Research · doi:10.1016/j.phrs.2020.105330 · Cited by 11 · see citing works
Bettegazzi, B., Pelizzoni, I., Scarzella, F. S., Restelli, L. M., Zacchetti, D., Maltecca, F., Casari, G., Grohovaz, F., & Codazzi, F. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/4721950 · Cited by 10 · see citing works
Markus, T., Ley, D., Hansson, S. R., Wieloch, T. W., & Ruscher, K. (2018) · BMC Neuroscience · doi:10.1186/s12868-018-0415-2 · Cited by 7 · see citing works
Ge, M.-M., Zhang, X., Xu, C., Miao, C., & Liao, Q.-W. (2025) · Redox Biology · doi:10.1016/j.redox.2025.103898 · Cited by 6 · see citing works
Sulfenic Acids and Peroxiredoxins in Oxidant Defense and Signaling
Poole, L. B., Nelson, K. J., & Karplus, P. A. (2013) · Springer eBooks · doi:10.1007/978-94-007-5787-5_4 · Cited by 6 · see citing works
Bessières, B., Cruz, E., & Alberini, C. M. (2021) · eLife · doi:10.7554/elife.68590 · Cited by 5 · see citing works
Protein misfolding and its dual role in neurodegeneration and cancer progression
Jamwal, R. S., Sharma, B., Minerva, Gupta, A., Misri, S., Shankaryan, R., Shah, R., & Kumar, R. (2025) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2025.10.001 · Cited by 4 · see citing works
Long-term plasticity of astrocytic phenotypes and their control by neurons in health and disease
Wardlaw, K. S., & Hardingham, G. E. (2023) · Essays in Biochemistry · doi:10.1042/ebc20220090 · Cited by 4 · see citing works
Self-citationLinville, R. M., James, B. T., Galani, K., Ho, L., Shin, J. H., Oliver, E., Fass, S. B., Cameron, J. C., Fitzwalter, B. E., Bock, R., et al. (2026) · Cell · doi:10.1016/j.cell.2026.08.006 · Cited by 4 · see citing works
Neurochemical Aspects of Oxidative and Nitrosative Stress
Farooqui, A. A. (2014) · Springer eBooks · doi:10.1007/978-3-319-04111-7_6 · Cited by 3 · see citing works
Therapeutic effect of erythropoietin and its derivatives in the treatment of acute ischemic stroke
Rama, R., & Torrella, J. R. (2025) · Exploration of Neuroprotective Therapy · doi:10.37349/ent.2025.1004101 · Cited by 1 · see citing works
Differential expression patterns of peroxiredoxins in olfactory neurons
Kolesnikova, A. S., Khokhlov, A. A., Romanov, R. A., & Bystrova, M. F. (2014) · Biochemistry (Moscow) Supplement Series A Membrane and Cell Biology · doi:10.1134/s1990747814040047 · Cited by 1 · see citing works
Waters, D. J., & Chiang, E. C. (2019) · Acta Scientifci Nutritional Health · doi:10.31080/asnh.2019.03.0450 · Cited by 1 · see citing works
Robbins, D. F., & Zhao, Y. (2014) · Springer eBooks · doi:10.1007/978-3-642-30018-9_107
Traynelis, S. F. (2019) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.734278718.793567057
- Authors
- Bell, K. F. S., & Hardingham, G. E.
- Affiliations
- University of Edinburgh (GB)
- ORCID
- Hardingham, Giles E.
- Venue
- Antioxidants & Redox Signaling
- Publisher
- SAGE Publications
- Published
- 2011-04
- Volume
- 14
- Issue
- 8
- Pages
- 1467-1477
- ISSN
- 1523-0864 (ISSN-L)
- 1557-7716
- OpenAlex
- W2020509501
- Cited by
- 71
- References
- 103
- Citations by year
- 2026: 1 · 2025: 4 · 2023: 1 · 2022: 2 · 2021: 3 · 2020: 8 · 2019: 5 · 2018: 8 · 2017: 4 · 2016: 7 · 2015: 6 · 2014: 10 · 2013: 5 · 2012: 3
- FWCI
- 0.34
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Antioxidants and Redox Signaling (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Wellcome Trust
- Canadian Institutes of Health Research
- Biotechnology and Biological Sciences Research Council
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Health Sciences › Medicine › Biochemistry › Antioxidant Activity and Oxidative Stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics, phytochemicals, and oxidative stress
- Keywords
- peroxiredoxin, thioredoxin, thioredoxin reductase, oxidative stress, antioxidant enzymes, neurodegenerative diseases, stroke, post-translational modification, Nrf2, synaptic activity, neuroprotection, therapeutic target
- MeSH terms
- Animals, Central Nervous System, Central Nervous System Diseases, Health, Humans, Oxidation-Reduction, Oxidative Stress, Peroxiredoxins
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