The multifaceted role of Nrf2 in mitochondrial function

Holmström, Kira M.; Kostov, Rumen V.; Dinkova-Kostova, Albena T.

doi:10.1016/j.cotox.2016.10.002

Cited by 368Genomics, phytochemicals, and oxidative stressMitochondrial Function and PathologyRedox biology and oxidative stress

The multifaceted role of Nrf2 in mitochondrial function

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Holmström, Kira M., Kostov, Rumen V., Dinkova-Kostova, Albena T.·2016·Current Opinion in Toxicology

DOI 10.1016/j.cotox.2016.10.002PMC PMC5193490

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Abstract

The transcription factor nuclear factor erythroid 2 p45-related factor 2 (Nrf2) is the master regulator of the cellular redox homeostasis. Nrf2 target genes comprise of a large network of antioxidant enzymes, proteins involved in xenobiotic detoxification, repair and removal of damaged proteins, inhibition of inflammation, as well as other transcription factors. In recent years it has emerged that as part of its role as a regulator of cytoprotective gene expression, Nrf2 impacts mitochondrial function. Increased Nrf2 activity defends against mitochondrial toxins. Reduced glutathione, the principal small molecule antioxidant in the mammalian cell and a product of several of the downstream target genes of Nrf2, counterbalances mitochondrial ROS production. The function of Nrf2 is suppressed in mitochondria-related disorders, such as Parkinson's disease and Friedrich's ataxia. Studies using isolated mitochondria and cultured cells have demonstrated that Nrf2 deficiency leads to impaired mitochondrial fatty acid oxidation, respiration and ATP production. Small molecule activators of Nrf2 support mitochondrial integrity by promoting mitophagy and conferring resistance to oxidative stress-mediated permeability transition. Excitingly, recent studies have shown that Nrf2 also affects mitochondrial function in stem cells with implications for stem cell self-renewal, cardiomyocyte regeneration, and neural stem/progenitor cell survival.

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These factors, including nuclear respiratory factor 1, nuclear factor erythroid-2-like 2, GA binding protein (nuclear respiratory factor 2), and Sp4, directly and indirectly control the expression of respiratory chain subunits encoded by nuclear and mitochondrial DNA.
“These factors, including nuclear respiratory factor 1, nuclear factor erythroid-2-like 2, GA binding protein (nuclear respiratory factor 2), and Sp4 [110–114] directly and indirectly control the expression of respiratory chain subunits encoded by nuclear and mitochondrial DNA [110, 115, 116].”
From Neuronal Apolipoprotein E4 Expression Results in Proteome-Wide Alterations and Compromises Bioenergetic Capacity by Disrupting Mitochondrial Function (2019) · cites this paper as [113]
The “Nrf2 and mitochondrial homeostasis” section reports that Nrf2 stimulates mitochondrial biogenesis through activation of nuclear respiratory factor 1. The stem-cell section also describes Nrf2 activating Pitx2, which then activates components of the electron transport chain. These passages support an indirect role for Nrf2, but do not establish the stated direct and indirect control of respiratory-chain subunit genes encoded by both nuclear and mitochondrial DNA, or address GA binding protein and Sp4. (LLM, conf=0.84)
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After exercise, ROS oxidize Cys residues in KEAP1 to facilitate the release and stabilization of NFE2L2, which translocates to the nucleus to drive the expression of >200 endogenous antioxidant and xenobiotic detoxifying enzymes.
“However, after exercise, ROS oxidize Cys residues in KEAP1 to facilitate the release and stabilization of NFE2L2, which translocates to the nucleus to drive the expression of >200 endogenous antioxidant and xenobiotic detoxifying enzymes (4).”
From Skeletal muscle NOX4 is required for adaptive responses that prevent insulin resistance (2021) · cites this paper as [4]
The KEAP1/Cullin-3 E3 ligase complex normally binds and targets NFE2L2 for degradation.
“The KEAP1/Cullin-3 E3 ligase complex normally binds and targets NFE2L2 for degradation (4).”
From Skeletal muscle NOX4 is required for adaptive responses that prevent insulin resistance (2021) · cites this paper as [4]
The NFE2L2 pathway serves to prevent the oxidative damage of macromolecules, including proteins and lipids.
“Fundamentally, the NFE2L2 pathway serves to prevent the oxidative damage of macromolecules, including proteins and lipids (4).”
From Skeletal muscle NOX4 is required for adaptive responses that prevent insulin resistance (2021) · cites this paper as [4]
Exercise induces Nfe2l2 gene expression, whereas ROS generated during exercise would be expected to increase NFE2L2 stability.
“Exercise induces Nfe2l2 gene expression (7), whereas ROS generated during exercise would be expected to increase NFE2L2 stability (4, 30).”
From Skeletal muscle NOX4 is required for adaptive responses that prevent insulin resistance (2021) · cites this paper as [4]

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Keap1, the Sensor for Electrophiles and Oxidants that Regulates the Phase 2 Response, Is a Zinc Metalloprotein
Dinkova‐Kostova, A. T., Holtzclaw, W. D., & Wakabayashi, N. (2005) · Biochemistry · doi:10.1021/bi047434h · Cited by 220 · see citing works
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Impaired Nuclear Nrf2 Translocation Undermines the Oxidative Stress Response in Friedreich Ataxia
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Lipid-mediated regulation of SKN-1/Nrf in response to germ cell absence
Steinbaugh, M. J., Narasimhan, S. D., Robida-Stubbs, S., Mazzeo, L. E. M., Dreyfuss, J. M., Hourihan, J. M., Raghavan, P., Operaña, T. N., Esmaillie, R., & Blackwell, T. K. (2015) · eLife · doi:10.7554/elife.07836 · Cited by 213 · see citing works
Mitochondrial Permeability Transition: New Findings and Persisting Uncertainties
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Regulation ofγ-glutamylcysteine synthetase subunit gene expression: Insights into transcriptional control of antioxidant defenses
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Disease-specific, neurosphere-derived cells as models for brain disorders
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Lithium Promotes Longevity through GSK3/NRF2-Dependent Hormesis
Castillo-Quan, J. I., Li, L., Kinghorn, K. J., Ivanov, D. K., Tain, L. S., Slack, C., Kerr, F., Nespital, T., Thornton, J. M., Hardy, J., et al. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.03.041 · Cited by 186 · see citing works
Astrocyte-Specific Overexpression of Nrf2 Delays Motor Pathology and Synuclein Aggregation throughout the CNS in the Alpha-Synuclein Mutant (A53T) Mouse Model
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Neuroprotective effect of sulforaphane in 6-hydroxydopamine-lesioned mouse model of Parkinson's disease
Morroni, F., Tarozzi, A., Sita, G., Bolondi, C., Moraga, J. M. Z., Cantelli‐Forti, G., & Hrelia, P. (2013) · NeuroToxicology · doi:10.1016/j.neuro.2013.03.004 · Cited by 179 · see citing works
Proteostasis of polyglutamine varies among neurons and predicts neurodegeneration
Tsvetkov, A. S., Arrasate, M., Barmada, S., Ando, D. M., Sharma, P., Shaby, B. A., & Finkbeiner, S. (2013) · Nature Chemical Biology · doi:10.1038/nchembio.1308 · Cited by 178 · see citing works
Sulforaphane protects against rotenone-induced neurotoxicity in vivo: Involvement of the mTOR, Nrf2 and autophagy pathways
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Sulforaphane enhances aquaporin-4 expression and decreases cerebral edema following traumatic brain injury
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Nrf2 activation in the treatment of neurodegenerative diseases: a focus on its role in mitochondrial bioenergetics and function
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SKN-1 and Nrf2 couples proline catabolism with lipid metabolism during nutrient deprivation
Pang, S., Lynn, D. A., Lo, J. Y., Paek, J., & Curran, S. P. (2014) · Nature Communications · doi:10.1038/ncomms6048 · Cited by 155 · see citing works
Role of Keap1-Nrf2 signaling in depression and dietary intake of glucoraphanin confers stress resilience in mice
Yao, W., Zhang, J.-C., Ishima, T., Dong, C., Yang, C., Ren, Q., Ma, M., Han, M., Wu, J., Suganuma, H., et al. (2016) · Scientific Reports · doi:10.1038/srep30659 · Cited by 154 · see citing works
PMI: A ΔΨm Independent Pharmacological Regulator of Mitophagy
East, D. A., Fagiani, F., Crosby, J., Georgakopoulos, N., Bertrand, H. C., Schaap, M., Fowkes, A., Wells, G., & Campanella, M. (2014) · Chemistry & Biology · doi:10.1016/j.chembiol.2014.09.019 · Cited by 153 · see citing works
Amelioration of Alzheimer’s disease by neuroprotective effect of sulforaphane in animal model
Kim, H. V., Kim, H. Y., Ehrlich, H. Y., Choi, S. Y., Kim, D. J., & Kim, Y. S. (2012) · Amyloid · doi:10.3109/13506129.2012.751367 · Cited by 153 · see citing works
NRF2 Orchestrates the Metabolic Shift during Induced Pluripotent Stem Cell Reprogramming
Hawkins, K., Joy, S., Delhove, J. M. K. M., Kotiadis, V. N., Fernández, E., FitzPatrick, L. M., Whiteford, J. R., King, P., Bolaños, J. P., Duchen, M. R., et al. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.02.003 · Cited by 151 · see citing works
Peptide inhibitors of the Keap1–Nrf2 protein–protein interaction
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NRF2 Activation Restores Disease Related Metabolic Deficiencies in Olfactory Neurosphere-Derived Cells from Patients with Sporadic Parkinson's Disease
Cook, A. L., Vitale, A. M., Ravishankar, S., Matigian, N., Sutherland, G. T., Shan, J., Sutharsan, R., Perry, C., Silburn, P. A., Mellick, G. D., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0021907 · Cited by 143 · see citing works
Nrf2 participates in depressive disorders through an anti-inflammatory mechanism
Martín-de-Saavedra, M. D., Budni, J., Cunha, M. P., Gómez-Rangel, V., Lorrio, S., del Barrio, L., Lastres-Becker, I., Parada, E., Tordera, R. M., Rodrigues, A. L. S., et al. (2013) · Psychoneuroendocrinology · doi:10.1016/j.psyneuen.2013.03.020 · Cited by 143 · see citing works
Frugal chemoprevention: targeting Nrf2 with foods rich in sulforaphane
Yang, L., Palliyaguru, D. L., & Kensler, T. W. (2015) · Seminars in Oncology · doi:10.1053/j.seminoncol.2015.09.013 · Cited by 139 · see citing works
Expression of Concern: Role of the Nrf2‐ARE pathway in early brain injury after experimental subarachnoid hemorrhage
Chen, G., Fang, Q., Zhang, J., Zhou, D., & Wang, Z. (2011) · Journal of Neuroscience Research · doi:10.1002/jnr.22577 · Cited by 138 · see citing works
Different Susceptibility to the Parkinson's Toxin MPTP in Mice Lacking the Redox Master Regulator Nrf2 or Its Target Gene Heme Oxygenase-1
Innamorato, N. G., Jaźwa, A., Rojo, A. I., García, C., Fernández‐Ruíz, J., Grochot‐Przeczek, A., Stachurska, A., Józkowicz, A., Dulak, J., & Cuadrado, A. (2010) · PLoS ONE · doi:10.1371/journal.pone.0011838 · Cited by 138 · see citing works
Sulforaphane ameliorates the development of experimental autoimmune encephalomyelitis by antagonizing oxidative stress and Th17-related inflammation in mice
Li, B., Cui, W., Liu, J., Li, R., Liu, Q., Xie, X.-H., Ge, X., Zhang, J., Song, X., Wang, Y., et al. (2013) · Experimental Neurology · doi:10.1016/j.expneurol.2013.10.002 · Cited by 138 · see citing works
Emerging functional cross-talk between the Keap1-Nrf2 system and mitochondria
Itoh, K., Ye, P., Matsumiya, T., Tanji, K., & Ozaki, T. (2015) · Journal of Clinical Biochemistry and Nutrition · doi:10.3164/jcbn.14-134 · Cited by 138 · see citing works
Optimal ROS Signaling Is Critical for Nuclear Reprogramming
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The role of Nrf2 signaling in the regulation of antioxidants and detoxifying enzymes after traumatic brain injury in rats and mice
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Roles for ROS and hydrogen sulfide in the longevity response to germline loss in Caenorhabditis elegans
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Design, Synthesis, and Evaluation of Triazole Derivatives That Induce Nrf2 Dependent Gene Products and Inhibit the Keap1–Nrf2 Protein–Protein Interaction
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Activation of the Nrf2-ARE pathway by siRNA knockdown of Keap1 reduces oxidative stress and provides partial protection from MPTP-mediated neurotoxicity
Williamson, T. P., Johnson, D. A., & Johnson, J. A. (2012) · NeuroToxicology · doi:10.1016/j.neuro.2012.01.015 · Cited by 118 · see citing works
Deficits in bioenergetics and impaired immune response in granulocytes from children with autism
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Sulforaphane enhances progerin clearance in H utchinson– G ilford progeria fibroblasts
Gabriel, D., Roedl, D., Gordon, L. B., & Djabali, K. (2014) · Aging Cell · doi:10.1111/acel.12300 · Cited by 114 · see citing works
Proteasome dysfunction inDrosophilasignals to an Nrf2-dependent regulatory circuit aiming to restore proteostasis and prevent premature aging
Tsakiri, E. N., Sykiotis, G. P., Papassideri, I. S., Terpos, E., Dimopoulos, M. A., Gorgoulis, V. G., Bohmann, D., & Trougakos, I. P. (2013) · Aging Cell · doi:10.1111/acel.12111 · Cited by 113 · see citing works
Reduced Nrf2 expression mediates the decline in neural stem cell function during a critical middle‐age period
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Sulforaphane produces antidepressant- and anxiolytic-like effects in adult mice
Wu, S., Gao, Q., Zhao, P., Gao, Y., Xi, Y., Wang, X., Liang, Y., Shi, H., & Ma, Y. (2016) · Behavioural Brain Research · doi:10.1016/j.bbr.2015.12.030 · Cited by 97 · see citing works
Genetic Activation of Nrf2 Protects against Fasting-Induced Oxidative Stress in Livers of Mice
Zhang, Y.-K. J., Wu, K. C., & Klaassen, C. D. (2013) · PLoS ONE · doi:10.1371/journal.pone.0059122 · Cited by 94 · see citing works
Activation of the Nuclear Factor E2-Related Factor 2/Antioxidant Response Element Pathway Is Neuroprotective after Spinal Cord Injury
Wang, X., Vaccari, J. P. D. R., Wang, H., Diaz, P., German, R., Marcillo, A. E., & Keane, R. W. (2011) · Journal of Neurotrauma · doi:10.1089/neu.2011.1922 · Cited by 93 · see citing works
Neuroprotective Effects of Sulforaphane after Contusive Spinal Cord Injury
Benedict, A. L., Mountney, A., Hurtado, A., Bryan, K. E., Schnaar, R. L., Dinkova‐Kostova, A. T., & Talalay, P. (2012) · Journal of Neurotrauma · doi:10.1089/neu.2012.2474 · Cited by 91 · see citing works
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SIRT2- and NRF2-Targeting Thiazole-Containing Compound with Therapeutic Activity in Huntington's Disease Models
Quinti, L., Casale, M., Moniot, S., Pais, T. F., Kanegan, M. J. V., Kaltenbach, L. S., Pallos, J., Lim, R. G., Naidu, S. D., Runne, H., et al. (2016) · Cell chemical biology · doi:10.1016/j.chembiol.2016.05.015 · Cited by 89 · see citing works
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Natural thioallyl compounds increase oxidative stress resistance and lifespan in Caenorhabditis elegans by modulating SKN-1/Nrf
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An overview of the molecular mechanisms and novel roles of Nrf2 in neurodegenerative disorders
Yang, Y., Jiang, S., Yan, J., Li, Y., Xin, Z., Yan, L., & Qu, Y. (2014) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2014.09.002 · Cited by 86 · see citing works
The spatiotemporal regulation of the Keap1–Nrf2 pathway and its importance in cellular bioenergetics
Dinkova‐Kostova, A. T., Baird, L., Holmström, K. M., Meyer, C. J., & Abramov, A. Y. (2015) · Biochemical Society Transactions · doi:10.1042/bst20150003 · Cited by 86 · see citing works
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A diet rich in high-glucoraphanin broccoli interacts with genotype to reduce discordance in plasma metabolite profiles by modulating mitochondrial function
Armah, C. N., Τράκα, Μ., Dainty, J. R., Defernez, M., Janssens, A. I. W. A., Leung, W., Doleman, J. F., Potter, J. F., & Mithen, R. F. (2013) · American Journal of Clinical Nutrition · doi:10.3945/ajcn.113.065235 · Cited by 77 · see citing works
Targeting lipid peroxidation and mitochondrial imbalance in Friedreich's ataxia
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NRF2 and the Phase II Response in Acute Stress Resistance Induced by Dietary Restriction
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Brain mitochondria from rats treated with sulforaphane are resistant to redox-regulated permeability transition
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Transcription Factor Nrf2 Protects the Spinal Cord from Inflammation Produced by Spinal Cord Injury
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Sulforaphane prevents quinolinic acid‐induced mitochondrial dysfunction in rat striatum
Luis‐García, E. R., Limón-Pacheco, J. H., Serrano‐García, N., Hernández‐Pérez, A. D., Pedraza‐Chaverrí, J., & Orozco‐Ibarra, M. (2016) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/jbt.21837 · Cited by 44 · see citing works
Protective Role of (RS)-glucoraphanin Bioactivated with Myrosinase in an Experimental Model of Multiple Sclerosis
Giacoppo, S., Galuppo, M., Iori, R., Nicola, G. R. D., Cassata, G., Bramanti, P., & Mazzon, E. (2013) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.12106 · Cited by 40 · see citing works
Nutrition, hormetic stress and health
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The ubiquitin-conjugating enzyme UBE2E3 and its import receptor importin-11 regulate the localization and activity of the antioxidant transcription factor NRF2
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Sulforaphane attenuates matrix metalloproteinase-9 expression following spinal cord injury in mice.
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Sulforaphane reduces the alterations induced by quinolinic acid: Modulation of glutathione levels
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The Effectiveness of Dimethyl Fumarate Monotherapy in the Treatment of Relapsing-Remitting Multiple Sclerosis: A Systematic Review and Meta-Analysis
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Targeting the KEAP1-NRF2 system to prevent kidney disease progression
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Mechanisms of mitophagy in cellular homeostasis, physiology and pathology
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Therapeutic targeting of the NRF2 and KEAP1 partnership in chronic diseases
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Regulation of Mitochondrial Biogenesis as a Way for Active Longevity: Interaction Between the Nrf2 and PGC-1α Signaling Pathways
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Regulation of Nrf2 by Mitochondrial Reactive Oxygen Species in Physiology and Pathology
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Reactive Oxygen Species and Mitochondrial Dynamics: The Yin and Yang of Mitochondrial Dysfunction and Cancer Progression
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Targeting Nrf2 to Suppress Ferroptosis and Mitochondrial Dysfunction in Neurodegeneration
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Mitochondrial Management of Reactive Oxygen Species
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Antioxidants: Positive or Negative Actors?
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PPARγ/PGC1α signaling as a potential therapeutic target for mitochondrial biogenesis in neurodegenerative disorders
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The Link between Oxidative Stress, Mitochondrial Dysfunction and Neuroinflammation in the Pathophysiology of Alzheimer’s Disease: Therapeutic Implications and Future Perspectives
Jurcău, M. C., Andronie-Cioara, F. L., Jurcău, A., Marcu, F., Ţiț, D. M., Pașcalău, N., & Nistor-Cseppentö, D. C. (2022) · Antioxidants · doi:10.3390/antiox11112167 · Cited by 226 · see citing works
Effects of curcumin on mitochondria in neurodegenerative diseases
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An Overview of the Nrf2/ARE Pathway and Its Role in Neurodegenerative Diseases
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Homocysteine and Mitochondria in Cardiovascular and Cerebrovascular Systems
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The Role of Reactive Oxygen Species in the Life Cycle of the Mitochondrion
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Antioxidant and Adaptative Response Mediated by Nrf2 during Physical Exercise
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Air pollution-derived PM2.5 impairs mitochondrial function in healthy and chronic obstructive pulmonary diseased human bronchial epithelial cells
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Mitohormesis and metabolic health: The interplay between ROS, cAMP and sirtuins
Palmeira, C. M., Teodoro, J. S., Amorim, J. A., Steegborn, C., Sinclair, D. A., & Rolo, A. P. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2019.07.017 · Cited by 159 · see citing works
Novel Nrf2-Inducer Prevents Mitochondrial Defects and Oxidative Stress in Friedreich’s Ataxia Models
Abeti, R., Baccaro, A., Esteras, N., & Giunti, P. (2018) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2018.00188 · Cited by 158 · see citing works
NRF2 activation induces NADH-reductive stress, providing a metabolic vulnerability in lung cancer
Weiss‐Sadan, T., Ge, M., Hayashi, M., Gohar, M., Yao, C.-H., de Groot, A., Harry, S. A., Carlin, A. D., Fischer, H., Shi, L., et al. (2023) · Cell Metabolism · doi:10.1016/j.cmet.2023.01.012 · Cited by 156 · see citing works
AMPK and NRF2: Interactive players in the same team for cellular homeostasis?
Petsouki, E., Cabrera, S. N. S., & Heiß, E. H. (2022) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2022.07.014 · Cited by 157 · see citing works
HIV-1 TAT-mediated microglial activation: role of mitochondrial dysfunction and defective mitophagy
Thangaraj, A., Periyasamy, P., Liao, K., Bendi, V. S., Callen, S. E., Pendyala, G., & Buch, S. J. (2018) · Autophagy · doi:10.1080/15548627.2018.1476810 · Cited by 147 · see citing works
Mechanistic Connections between Endoplasmic Reticulum (ER) Redox Control and Mitochondrial Metabolism
Fan, Y., & Simmen, T. (2019) · Cells · doi:10.3390/cells8091071 · Cited by 141 · see citing works
Redox Mechanisms in Neurodegeneration: From Disease Outcomes to Therapeutic Opportunities
Sbodio, J. I., Snyder, S. H., & Paul, B. D. (2018) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7321 · Cited by 143 · see citing works
Role of Nrf2 and protective effects of Metformin against tobacco smoke-induced cerebrovascular toxicity
Prasad, S., Sajja, R. K., Kaisar, M. A., Park, J. H., Villalba, H., Liles, T., Abbruscato, T. J., & Cucullo, L. (2017) · Redox Biology · doi:10.1016/j.redox.2017.02.007 · Cited by 140 · see citing works
Transcription factor NRF2 as a promising therapeutic target for Alzheimer’s disease
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Nrf2 as a regulator of energy metabolism and mitochondrial function
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Authors: Holmström, K. M., Kostov, R. V., & Dinkova-Kostova, A. T.
Affiliations: University of Helsinki (FI)
University of Dundee (GB)
Corresponding author: Holmström, Kira M.
ORCID: Holmström, Kira M.
Venue: Current Opinion in Toxicology
Publisher: Elsevier BV
Published: 2016-12
Volume: 1
Pages: 80-91
ISSN: 2468-2020 (ISSN-L)
DOI: 10.1016/j.cotox.2016.10.002
PMC: PMC5193490
OpenAlex: W2530829140
Cited by: 368
References: 127
Citations by year: 2026: 20 · 2025: 34 · 2024: 31 · 2023: 37 · 2022: 41 · 2021: 61 · 2020: 48 · 2019: 37 · 2018: 42 · 2017: 15
FWCI: 2.84
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
creativecommons.org/licenses/by/4.0/ (vor)
Locations: Current Opinion in Toxicology (publishedVersion, cc-by)
PubMed Central (publishedVersion, cc-by)
PubMed (publishedVersion)
Discovery Research Portal (University of Dundee) (submittedVersion, cc-by)
Työväentutkimus Vuosikirja (submittedVersion)
Funders: Cancer Research UK (C20953, A18644)
Biotechnology and Biological Sciences Research Council (BB/J007498/1)
Reata Pharmaceuticals
Academy of Finland
European Research Council
Tampere University Hospital Medical Research Fund
Sigrid Juselius Foundation
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics, phytochemicals, and oxidative stress
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Keywords: Nrf2, mitochondrial function, redox homeostasis, antioxidant enzymes, xenobiotic detoxification, reduced glutathione, mitochondrial reactive oxygen species, mitochondrial toxins, Parkinson's disease, Friedreich's ataxia, mitochondrial fatty acid oxidation, mitochondrial respiration, ATP production, mitophagy, permeability transition, oxidative stress, Nrf2 activators, stem cells, cardiomyocyte regeneration, neural stem/progenitor cells

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The multifaceted role of Nrf2 in mitochondrial function

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