The DOI matches its Crossref record; 47 of the 47 references it cites were found in a registry or an index.
Respiration-dependent H2O2 Removal in Brain Mitochondria via the Thioredoxin/Peroxiredoxin System
Open accessAbstract
Mitochondrial reactive oxygen species (ROS) play an important role in both physiological cell signaling processes and numerous pathological states, including neurodegenerative disorders such as Parkinson disease. While mitochondria are considered the major cellular source of ROS, their role in ROS removal remains largely unknown. Using polarographic methods for real-time detection of steady-state H(2)O(2) levels, we were able to quantitatively measure the contributions of potential systems toward H(2)O(2) removal by brain mitochondria. Isolated rat brain mitochondria showed significant rates of exogenous H(2)O(2) removal (9-12 nmol/min/mg of protein) in the presence of substrates, indicating a respiration-dependent process. Glutathione systems showed only minimal contributions: 25% decrease with glutathione reductase inhibition and no effect by glutathione peroxidase inhibition. In contrast, inhibitors of thioredoxin reductase, including auranofin and 1-chloro-2,4-dinitrobenzene, attenuated H(2)O(2) removal rates in mitochondria by 80%. Furthermore, a 50% decrease in H(2)O(2) removal was observed following oxidation of peroxiredoxin. Differential oxidation of glutathione or thioredoxin proteins by copper (II) or arsenite, respectively, provided further support for the thioredoxin/peroxiredoxin system as the major contributor to mitochondrial H(2)O(2) removal. Inhibition of the thioredoxin system exacerbated mitochondrial H(2)O(2) production by the redox cycling agent, paraquat. Additionally, decreases in H(2)O(2) removal were observed in intact dopaminergic neurons with thioredoxin reductase inhibition, implicating this mechanism in whole cell systems. Therefore, in addition to their recognized role in ROS production, mitochondria also remove ROS. These findings implicate respiration- and thioredoxin-dependent ROS removal as a potentially important mitochondrial function that may contribute to physiological and pathological processes in the brain.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
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
“In this context, it is important to note that the H 2 O 2 scavenger activities of isolated mitochondria are lower with succinate as the sole substrate than with NADH-generating substrates like malate/glutamate or malate/pyruvate [111,112].”
From Differential effects of complex II on mitochondrial ROS production and their relation to cardioprotective pre- and postconditioning (2013) · cites this paper as [112]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
How mitochondria produce reactive oxygen species
Murphy, M. P. (2009) · Biochemical Journal · doi:10.1042/bj20081386 · Cited by 8,207
Wendel, A. (1981) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(81)77046-0 · Cited by 3,032
H 2 O 2 , a Necessary Evil for Cell Signaling
Rhee, S. G. (2006) · Science · doi:10.1126/science.1130481 · Cited by 2,160
Oxidative stress in neurodegeneration: Cause or consequence?
Andersen, J. K. (2004) · Nature Medicine · doi:10.1038/nrn1434 · Cited by 1,869
Extension of murine life span by overexpression of catalase targeted to mitochondria
Schriner, S. E., Linford, N. J., Martin, G. M., Treuting, P., Ogburn, C. E., Emond, M., Coskun, P. E., Ladiges, W., Wolf, N., Van Remmen, H., et al. (2005) · Science · doi:10.1126/science.1106653 · Cited by 1,724
Mitochondrial metabolism of reactive oxygen species
Andreyev, A. Y., Kushnareva, Y. E., & Starkov, A. A. (2005) · Biochemistry (Moscow) · doi:10.1007/s10541-005-0102-7 · Cited by 1,336
Generation of reactive oxygen species by the mitochondrial electron transport chain
Liu, Y., Fiskum, G., & Schubert, D. (2002) · Journal of Neurochemistry · doi:10.1046/j.0022-3042.2002.00744.x · Cited by 1,260
Glutathione, oxidative stress and neurodegeneration
Schulz, J. B., Lindenau, J. H., Seyfried, J., & DICHGANS, J. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2000.01595.x · Cited by 1,225
Lebovitz, R. M., Zhang, H., Vogel, H., Cartwright, J., Dionne, L., Lu, N., Huang, S., & Matzuk, M. M. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.18.9782 · Cited by 1,023
Environmental risk factors and Parkinson's disease
Liou, H., Tsai, M.-C., Chen, C., Jeng, J., Chang, Y. C., Chen, S. Y., & Chen, R.-T. (1997) · Neurology · doi:10.1212/wnl.48.6.1583 · Cited by 616
Flagged first, then by citations
Research works printed but not linked: 3
- Rogers, 2005, Proc. Am. Assoc. Cancer Res., 46, 454
- Kim, 2001, J. Neural Transm. Suppl., 223
- Andreyev, 2005, Biochemistry, 70, 200
Cited by
Sorted by citations
Items 101–199 of 199
Role of Mitochondria and Other ROS Sources in Hyperthyroidism-Linked Oxidative Stress
Venditti, P., Napolitano, G., & Meo, S. D. (2015) · Immunology Endocrine & Metabolic Agents - Medicinal Chemistry · doi:10.2174/187152221501150710124951 · Cited by 25
Silva-Rodrigues, T., de‐Souza‐Ferreira, E., Machado, C. M., Braga, B. C., Rodrigues-Ferreira, C., & Galina, A. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.09.017 · Cited by 25
Ohshima, Y., Kitami, A., Kawano, A., Tsukimoto, M., & Kojima, S. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.06.014 · Cited by 24
Shi, G. F., Yu, Q., Shi, L., & Zhang, Z. (2012) · Insect Molecular Biology · doi:10.1111/j.1365-2583.2012.01161.x · Cited by 23
Short time exposure to hydrogen peroxide induces sustained glutathione export from cultured neurons
Hohnholt, M. C., & Dringen, R. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.02.005 · Cited by 23
Yao, X., Li, M., He, J. N., Zhang, G., Wang, M., Ma, J., Sun, Y., Zhang, W., & Li, L. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.02.002 · Cited by 23
Increase in Trx2/Prx3 redox system immunoreactivity in the spinal cord and hippocampus of aged dogs.
Ahn, J., Choi, J.-H., Song, J.-M., Lee, C.-H., Yoo, K., Hwang, I., Kim, J. S., Shin, H., & Won, M. (2011) · Experimental Gerontology · doi:10.1016/j.exger.2011.08.004 · Cited by 24
López-Royuela, N., Rathore, M. G., Allende-Vega, N., Annicotte, J., Lluis Fajas, A., Ramachandran, B., Gulick, T., & Villalba, M. (2014) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2014.05.026 · Cited by 22
Eaton, L., Wang, T., Roy, M., & Pamenter, M. E. (2022) · Current Neuropharmacology · doi:10.2174/1570159x20666220327220929 · Cited by 21
How neurons cope with oxidative stress
Ebding, J., Mazzone, F., Kins, S., Pielage, J., & Maritzen, T. (2025) · Biological Chemistry · doi:10.1515/hsz-2024-0146 · Cited by 21
Carneiro, P., Duarte, M., & Videira, A. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.10.492 · Cited by 19
Folbergrová, J., Ješina, P., Nůsková, H., & Houštěk, J. (2012) · International Journal of Developmental Neuroscience · doi:10.1016/j.ijdevneu.2012.11.011 · Cited by 20
Schmitz, A. E., de Souza, L. F., dos Santos, B., Maher, P. A., Lopes, F. M., Londero, G. F., Klamt, F., & Dafré, A. L. (2017) · Neurotoxicity Research · doi:10.1007/s12640-017-9738-5 · Cited by 19
The specific features of free-radical processes and the antioxidant defense in the adult brain
Галкина, О. В. (2013) · Neurochemical Journal · doi:10.1134/s1819712413020025 · Cited by 19
Francisco, A., Engel, D. F., Figueira, T. R., Rogério, F., Bem, A. F. D., & Castilho, R. F. (2020) · Neuroscience · doi:10.1016/j.neuroscience.2020.05.042 · Cited by 19
Wiesen, T., & Atlas, D. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-04667-2 · Cited by 17
Sadri, S., Tomar, N., Yang, C., Audi, S. H., Cowley, A. W., & Dash, R. K. (2023) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2023.109690 · Cited by 19
Nunn, A. V. W., Guy, G. W., Botchway, S. W., & Bell, J. D. (2020) · Phytotherapy Research · doi:10.1002/ptr.6654 · Cited by 17
Mitochondrial mechanisms of redox cycling agents implicated in Parkinson’s disease
Lopert, P., & Patel, M. (2015) · Journal of Neural Transmission · doi:10.1007/s00702-015-1386-4 · Cited by 17
Self-citationYan, B., Park, J., Ahn, J., Lee, Y. J., Lee, T. H., Lee, C.-H., Cho, J., Kim, M., Kim, T. Y., Kang, I., et al. (2012) · Neurochemical Research · doi:10.1007/s11064-012-0702-8 · Cited by 14
Comparing Electron Leak in Vertebrate Muscle Mitochondria
Treberg, J. R., Munro, D., Jastroch, M., Quijada‐Rodriguez, A. R., Kutschke, M., & Wiens, L. M. (2018) · Integrative and Comparative Biology · doi:10.1093/icb/icy095 · Cited by 16
The acaricidal activity and mechanism of eugenol on Psoroptes cuniculi
Ma, W., Fan, Y., Liu, Z., Hao, Y., Mou, Y., Liu, Y., Zhang, W., & Song, X. (2019) · Veterinary Parasitology · doi:10.1016/j.vetpar.2018.12.012 · Cited by 15
Isei, M. O., Stevens, D., & Kamunde, C. (2021) · Comparative Biochemistry and Physiology Part C Toxicology & Pharmacology · doi:10.1016/j.cbpc.2021.108999 · Cited by 16
Selivanov, V. A., Zagubnaya, O. A., Nartsissov, Y. R., & Cascante, M. (2021) · PLoS ONE · doi:10.1371/journal.pone.0255164 · Cited by 15
Janus, or the Inevitable Battle Between Too Much and Too Little Oxygen
Mancardi, D., Ottolenghi, S., Attanasio, U., Tocchetti, C. G., Paroni, R. C., Pagliaro, P., & Samaja, M. (2022) · Antioxidants and Redox Signaling · doi:10.1089/ars.2021.0232 · Cited by 15
Low-dose Estrogen Is as Effective as High-dose Treatment in Rats With Postmenopausal Hypertension
Carraro, C. C., Sartório, C. L., Casali, K. R., Fernandes, R. O., Llesuy, S., Araújo, A. S. D. R., Belló‐Klein, A., & Rigatto, K. (2013) · Journal of Cardiovascular Pharmacology · doi:10.1097/fjc.0000000000000034 · Cited by 15
de Souza, L. F., Schmitz, A. E., da Silva, L. C. S., de Oliveira, K. A., Nedel, C. B., Tasca, C. I., Bem, A. F. D., Farina, M., & Dafré, A. L. (2017) · Toxicology in Vitro · doi:10.1016/j.tiv.2017.04.028 · Cited by 15
Review: Using isolated mitochondria to investigate mitochondrial hydrogen peroxide metabolism
Treberg, J. R. (2021) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/j.cbpb.2021.110614 · Cited by 13
Insights into the Multifaceted Roles of Thioredoxin-1 System: Exploring Knockout Murine Models
Shcholok, T., & Eftekharpour, E. (2024) · Biology · doi:10.3390/biology13030180 · Cited by 13
Rajput, C., Sarkar, A., & Singh, M. P. (2021) · Molecular Neurobiology · doi:10.1007/s12035-021-02456-0 · Cited by 13
Toxicity assessment of 2,4-D and MCPA herbicides in primary culture of fish hepatic cells
Salvo, L. M., Malucelli, M. I. C., da Silva, J. R. M. C., Alberton, G. C., & de Assis, H. C. S. (2015) · Journal of Environmental Science and Health Part B · doi:10.1080/03601234.2015.1018754 · Cited by 13
Aluf, Y., Vaya, J., Khatib, S., & Finberg, J. P. M. (2011) · Neuropharmacology · doi:10.1016/j.neuropharm.2011.03.006 · Cited by 13
Jiménez, A. G., Ruhs, E. C., Tobin, K. J., Anderson, K. N., Pogam, A. L., Régimbald, L., & Vézina, F. (2020) · Journal of Experimental Biology · doi:10.1242/jeb.218826 · Cited by 13
Michihara, A., Oda, A., & 見土, 万. (2016) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.b15-00663 · Cited by 13
Morris, G., Walder, K. R., Berk, M., Carvalho, A. F., Marx, W., Bortolasci, C. C., Yung, A. R., Puri, B. K., & Maes, M. H. J. (2021) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/j.pnpbp.2021.110481 · Cited by 13
Zhang, N., Wang, L., Duan, Q., Lin, L., Ahmed, M., Wang, T., & Yao, X. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2015/267027 · Cited by 12
Venditti, P., Napolitano, G., Barone, D., Coppola, I., & Meo, S. D. (2015) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2015.01.019 · Cited by 13
Role of enzymatic and non-enzymatic processes in H2O2 removal by rat liver and heart mitochondria
Venditti, P., Napolitano, G., & Meo, S. D. (2013) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-013-9534-8 · Cited by 12
de‐Souza‐Ferreira, E., Neto, I. M. R., Martins, E. L., & Galina, A. (2019) · Journal of Neurochemistry · doi:10.1111/jnc.14705 · Cited by 12
Kojima, S. M. S., Takai, E., & Tsukimoto, M. (2011) · Anti-aging Medicine · doi:10.3793/jaam.8.108 · Cited by 13
Reversible inhibition of hydrogen peroxide elimination by calcium in brain mitochondria
Tretter, L., Angeli, E. B., Ardestani, M. R., Goracci, G., & Ádám‐Vizi, V. (2011) · Journal of Neuroscience Research · doi:10.1002/jnr.22658 · Cited by 11
Ohmori, I., Ouchida, M., Imai, H., Ishida, S., Toyokuni, S., & Mashimo, T. (2022) · Neurobiology of Disease · doi:10.1016/j.nbd.2022.105921 · Cited by 18
Průchová, P., Gotvaldová, K., Smolková, K., Alán, L., Holendová, B., Tauber, J. A., Galkin, A. S., Ježek, P., & Jabůrek, M. (2022) · Antioxidants · doi:10.3390/antiox11020198 · Cited by 10
Moyse, E., Arseneault, M., Gaudreau, P., Ferland, G., & Ramassamy, C. (2015) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2015.04.002 · Cited by 10
Singer, E. M., Linehan, J., Babilonia, G., Imam, S. A., Smith, D. D., Loera, S., Wilson, T. G., & Smith, S. S. (2013) · PLoS ONE · doi:10.1371/journal.pone.0060562 · Cited by 9
Thyroid state affects H2O2 removal by rat heart mitochondria
Venditti, P., Napolitano, G., Fasciolo, G., & Meo, S. D. (2018) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2018.11.025 · Cited by 9
Mitochondrial Management of ROS in Physiological and Pathological Conditions
Venditti, P., & Napolitano, G. (2025) · Antioxidants · doi:10.3390/antiox14010043 · Cited by 9
Superoxide signals for the mitophagy of dysfunctional mitochondria to maintain quality control
Curtis, W. M., & Bradshaw, P. C. (2025) · Redox Biology · doi:10.1016/j.redox.2025.103979 · Cited by 8
Furukawa, A., Kakita, A., Chiba, Y., Kitaura, H., Fujii, Y., Fukuda, M., Kameyama, S., & Shimada, A. (2020) · Epilepsy Research · doi:10.1016/j.eplepsyres.2020.106502 · Cited by 8
Lee, C.-H., Park, J., Cho, J.-H., Ahn, J., Bae, E., & Won, M. (2015) · Molecular Medicine Reports · doi:10.3892/mmr.2015.3760 · Cited by 9
Mitochondrial Dysfunction in Parkinson’s Disease
Patel, M., & McElroy, P. B. (2017) · Royal Society of Chemistry eBooks · doi:10.1039/9781782622888-00061 · Cited by 9
Self-citationProspect of thioredoxin as a possibly effective tool to combat OSAHS
Pan, Y., You, L., Zhou, J., Wang, C., Wang, J., Fukunaga, A., Yodoi, J., & Tian, H. (2022) · Sleep And Breathing · doi:10.1007/s11325-022-02640-z · Cited by 7
The cell origin of reactive oxygen species and its implication for evolutionary trade-offs
Kervella, M., Bertile, F., Bouillaud, F., & Criscuolo, F. (2025) · Open Biology · doi:10.1098/rsob.240312 · Cited by 10
The association of plasma peroxiredoxin 3 with insulin in pregnant women
Wang, L., Hao, J., Yu, A.-Q., Li, T., Liu, R., Li, L., Li, J., & Li, X. (2018) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2018.12.021 · Cited by 8
The neuronal protection of a zinc-binding protein isolated from oyster
Hsu, W.-H., Lin, Y.-C., Chen, B.-R., Wu, S., & Lee, B.-H. (2018) · Food and Chemical Toxicology · doi:10.1016/j.fct.2018.02.009 · Cited by 6
Foley, T. D., Montovano, G., & Ayala, M. C. (2020) · Neurochemical Research · doi:10.1007/s11064-020-03046-7 · Cited by 6
Sodium nitroprusside as a priming agent induces drought stress tolerance in Citrus
Scialò, E., Sicilia, A., & Piero, A. R. L. (2025) · Current Plant Biology · doi:10.1016/j.cpb.2025.100508 · Cited by 5
Liu, S., Pi, J., & Zhang, Q. (2025) · Antioxidants · doi:10.3390/antiox14020235 · Cited by 5
H2O2 Signalling Pathway: A Possible Bridge between Insulin Receptor and Mitochondria
Анатольевич, П. И. (2012) · Current Neuropharmacology · doi:10.2174/1570159x11209040311 · Cited by 5
α-Haemoglobin regulates sympathoadrenal cell metabolism to maintain a catecholaminergic phenotype
Marcos-Almaraz, M. T., Rodríguez‐Gómez, J. A., López‐Barneo, J., & Pascual, A. (2011) · Biochemical Journal · doi:10.1042/bj20111640 · Cited by 5
Wang, M., Yang, X.-Y., Zhang, N., Zhang, D., & Zhu, X. (2016) · BioMed Research International · doi:10.1155/2016/3571962 · Cited by 5
The Hormesis of Thinking: A Deeper Quantum Thermodynamic Perspective?
Nunn, A. V. W., Guy, G. W., & Bell, J. D. (2017) · International Journal of Neurorehabilitation · doi:10.4172/2376-0281.1000272 · Cited by 5
Isei, M. O., Chinnappareddy, N., Stevens, D., & Kamunde, C. (2021) · Comparative Biochemistry and Physiology Part C Toxicology & Pharmacology · doi:10.1016/j.cbpc.2021.109111 · Cited by 5
What can naked mole‐rats teach us about ameliorating hypoxia‐related human diseases?
Kadamani, K. L., Rahnamaie‐Tajadod, R., Eaton, L., Bengtsson, J., Ojaghi, M., Cheng, H., & Pamenter, M. E. (2024) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.15219 · Cited by 4
In vivo chemogenetic generation of intraneuronal H2O2
Maltsev, D. I., Solotenkov, M. A., Elesina, E. A., Dolbeneva, A. A., Fedotova, A., Morozova, K. I., Fedotov, I. V., Lanin, A. А., Fedotov, A. B., Korzhenevskii, D. A., et al. (2026) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2026.01.006 · Cited by 4
Tetteh, P. A., Kalvani, Z., Stevens, D., Sappal, R., & Kamunde, C. (2024) · Aquatic Toxicology · doi:10.1016/j.aquatox.2024.106986 · Cited by 4
Vitamin C and Its Role in Brain Development and Cognition
Hasselholt, S., Tveden‐Nyborg, P., & Lykkesfeldt, J. (2012) · doi:10.1007/978-1-137-00689-9_3 · Cited by 3
Abushikha, M. A. A., Karağaç, M. S., Yeşilkent, E. N., & Ceylan, H. (2025) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-025-04279-5 · Cited by 2
Mitochondrial redox biology: Reactive species production and antioxidant defenses
Napolitano, G., Fasciolo, G., Meo, S. D., & Venditti, P. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-821562-3.00053-8 · Cited by 3
Tetteh, P. A., Kalvani, Z., Stevens, D., Sappal, R., & Kamunde, C. (2025) · Comparative Biochemistry and Physiology Part C Toxicology & Pharmacology · doi:10.1016/j.cbpc.2025.110286 · Cited by 2
Reactive Oxygen Species and Antioxidant Enzymes in the Developing Brain
Galkina, O. (2015) · International Journal of Neurology Research · doi:10.17554/j.issn.2313-5611.2015.01.26 · Cited by 2
Contribution of Insulin Resistance in Pathogenesis of Alzheimer Disease
Erol, A. (2013) · Wiley eBooks · doi:10.1002/9781118395318.ch3 · Cited by 2
Making sense of subcellular H2O2 in mammals
Waldeck‐Weiermair, M., Covington, T. A., Pandey, A. K., & Michel, T. M. (2026) · Redox Biochemistry and Chemistry · doi:10.1016/j.rbc.2026.100080 · Cited by 1
Kolotyeva, N. A., Novikova, S. V., Namiot, E., Zembatov, G. M., Tregub, P. P., Rozanova, N. A., Makarov, V., Komleva, Y. K., & Салмина, А. (2026) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-026-02132-x · Cited by 2
Detoxification mechanisms in autism spectrum disorders
El-Ansary, A. K. (2013) · OA Autism · doi:10.13172/2052-7810-1-2-752 · Cited by 1
Glutathione and Thiol Redox Signalling in Parkinson’s Disease
Smeyne, M., & Smeyne, R. J. (2017) · Royal Society of Chemistry eBooks · doi:10.1039/9781782622888-00144 · Cited by 1
Sources of Reactive Oxygen Species in Normoxic and Hypoxic Naked Mole-Rat Brain
Eaton, L., Bengtsson, J., Welch, I., Halal, A. K., & Pamenter, M. E. (2024) · Medical Research Archives · doi:10.18103/mra.v12i1.4857 · Cited by 1
Wiggins, L. M. (2014) · Oxidants and Antioxidants in Medical Science · doi:10.5455/oams.310714.or.071
EFEITO DO TRATAMENTO COM ESTRADIOL SOBRE O CONTROLE DA PRESSÃO ARTERIAL E O ESTRESSE OXIDATIVO
Carraro, C. C. (2012) · Americanae (AECID Library)
CHANGES OF THIOL-DISULFIDE BALANCE IN PARKINSON’S DISEASE
Kanunnikava, N. P. (2018) · Proceedings of the National Academy of Sciences of Belarus Medical series · doi:10.29235/1814-6023-2018-15-1-108-118
Szereszewski, K. E. (2019) · Carleton University's Institutional Repository (MacOdrum Library, Carleton University) · doi:10.22215/etd/2019-13837
Txn1 mutation causes epilepsy associated with vacuolar degeneration in the midbrainPreprint
Ohmori, I., Ouchida, M., Imai, H., Ishida, S., Toyokuni, S., & Mashimo, T. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.10.07.463470
Leung, M. C. K. (2012) · DukeSpace (Duke University)
Tran, N. B. (2022) · Publication Server of Goethe University Frankfurt am Main (Goethe University Frankfurt) · doi:10.21248/gups.71335
Ca2+ Inhibits Reactive Oxygen Species Scavenging in Naked Mole-Rat Cortical Homogenates
Jaffer, B., Cheng, H., & Pamenter, M. E. (2025) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-025-01603-8
van Hameren, G. (2018) · theses.fr (ABES) · doi:10.70675/71c15a42zb6d9z4edazb7c1zd3f51e09c949
Same mitochondria, different longevities : what do ants tell us about metabolic ageing ?
Kervella, M. (2023) · theses.fr (ABES) · doi:10.70675/7b57ef70z057dz4435za749zb0c6dcd534e4
Metals exposure dissociates mitochondrial NAD(P)H redox state from H₂O₂ emission
Tetteh, P. A., Kalvani, Z., Stevens, D., Sappal, R., & Kamunde, C. (2026) · Comparative Biochemistry and Physiology Part C Toxicology & Pharmacology · doi:10.1016/j.cbpc.2026.110639
Park, H.-J., & Kim, H.-M. (2026) · Biology · doi:10.3390/biology15171519
Mitochondrial calcium and ROS: present understanding and future directions
Roth, C. I., Vadovsky, A. C., Steele, K. J., Raftu, A., Shaman, S., Roberts, J. G., & Bazil, J. N. (2026) · Mitochondrion · doi:10.1016/j.mito.2026.102222
Redox imbalance and epigenetic reprogramming underlie polysubstance-induced neuronal dysfunction
Chennakesavan, K., Hammond, H. R., Kalaisejiane, N., Devan, S., Karnati, A., Eans, S. O., Williams, A. K., McLaughlin, J. P., & Samikkannu, T. (2026) · Pharmacological Research · doi:10.1016/j.phrs.2026.109703
Metadata
- Authors
- Drechsel, D. A., & Patel, M.
- Affiliations
- University of Colorado Denver (US)
- Corresponding author
- Patel, Manisha
- ORCID
- Patel, Manisha
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2010-09
- Volume
- 285
- Issue
- 36
- Pages
- 27850-27858
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC2934652
- OpenAlex
- W2090005130
- Cited by
- 199
- References
- 46
- Citations by year
- 2026: 7 · 2025: 9 · 2024: 6 · 2023: 3 · 2022: 10 · 2021: 13 · 2020: 11 · 2019: 9 · 2018: 13 · 2017: 15 · 2016: 10 · 2015: 20 · 2014: 18 · 2013: 17 · 2012: 20
- FWCI
- 7.16
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- American Foundation for Pharmaceutical Education
- National Institutes of Health (RO1NS04748, 1f31ns061438-01a1, RO1NS039587)
- National Institute of Neurological Disorders and Stroke (1F31NS061438, R01NS039587, R01NS045748, R01NS04748, F31 NS061438, RO1NS039587)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Biochemistry (medical) › Antioxidant Activity and Oxidative Stress
- Keywords
- hydrogen peroxide removal, brain mitochondria, thioredoxin system, peroxiredoxin, thioredoxin reductase, mitochondrial reactive oxygen species, oxidative stress, Parkinson's disease, dopaminergic neurons, glutathione, paraquat, auranofin, arsenite, mitochondrial respiration
- MeSH terms
- Animals, Brain, Cell Line, Cell Membrane Permeability, Dopamine, Enzyme Inhibitors, Hydrogen Peroxide, Liver, Male, Metals, Mitochondria, Polarography, Thioredoxins, Thioredoxin-Disulfide Reductase, Rats, Sprague-Dawley, Cell Respiration, Rats, Peroxiredoxins
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
