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
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
Succinate, an intermediate in metabolism, signal transduction, ROS, hypoxia, and tumorigenesis
Tretter, L., Patócs, A., & Chinopoulos, C. (2016) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2016.03.012 · Cited by 550
Molecular Mechanisms of Superoxide Production by the Mitochondrial Respiratory Chain
Dröse, S., & Brandt, U. (2012) · Advances in experimental medicine and biology · doi:10.1007/978-1-4614-3573-0_6 · Cited by 536
Energy metabolism and inflammation in brain aging and Alzheimer’s disease
Yin, F., Sancheti, H., Patil, I., & Cadenas, E. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.04.200 · Cited by 538
Superoxide generation by complex III: From mechanistic rationales to functional consequences
Bleier, L., & Dröse, S. (2013) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2012.12.002 · Cited by 369
Redox Signaling Mediated by Thioredoxin and Glutathione Systems in the Central Nervous System
Ren, X., Zou, L., Zhang, X., Branco, V., Wang, J., Carvalho, C. M. L., Holmgren, A., & Lu, J. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2016.6925 · Cited by 376
Mitochondrial metabolism of reactive oxygen species
Venditti, P., Stefano, L. D., & Meo, S. D. (2013) · Mitochondrion · doi:10.1016/j.mito.2013.01.008 · Cited by 359
Targeting Oxidative Stress in Central Nervous System Disorders
Patel, M. (2016) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2016.06.007 · Cited by 312
Self-citationRedox Control of Microglial Function: Molecular Mechanisms and Functional Significance
Rojo, A. I., McBean, G. J., Cindrić, M., Egea, J., López, M. G., Rada, P., Žarković, N., & Cuadrado, A. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5745 · Cited by 321
Mitochondrial Management of Reactive Oxygen Species
Napolitano, G., Fasciolo, G., & Venditti, P. (2021) · Antioxidants · doi:10.3390/antiox10111824 · Cited by 305
Ronchi, J. A., Figueira, T. R., Ravagnani, F. G., Oliveira, H. C. F., Vercesi, A. E., & Castilho, R. F. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.05.049 · Cited by 283
Metabolic Dysfunction and Oxidative Stress in Epilepsy
Pearson-Smith, J. N., & Patel, M. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18112365 · Cited by 280
Self-citationBrown, G. C., & Borutaitė, V. (2011) · Mitochondrion · doi:10.1016/j.mito.2011.02.001 · Cited by 295
Mitochondrial Energy Metabolism and Redox Signaling in Brain Aging and Neurodegeneration
Yin, F., Boveris, A., & Cadenas, E. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4774 · Cited by 251
Du, Y., Zhang, H., Lu, J., & Holmgren, A. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.392225 · Cited by 230
A radical shift in perspective: mitochondria as regulators of reactive oxygen species
Munro, D., & Treberg, J. R. (2017) · Journal of Experimental Biology · doi:10.1242/jeb.132142 · Cited by 220
Dröse, S. (2013) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2013.01.004 · Cited by 201
Aon, M. A., Stanley, B. A., Sivakumaran, V., Kembro, J. M., O'Rourke, B., Paolocci, N., & Cortassa, S. (2012) · Journal of General Physiology · doi:10.1085/jgp.201210772 · Cited by 200
Stanley, B. A., Sivakumaran, V., Shi, S., McDonald, I., Lloyd, D., Watson, W. H., Aon, M. A., & Paolocci, N. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.284612 · Cited by 203
Mitochondrial ROS metabolism: 10 Years later
Andreyev, A. Y., Kushnareva, Y. E., Murphy, A. N., & Starkov, A. A. (2015) · Biochemistry (Moscow) · doi:10.1134/s0006297915050028 · Cited by 196
The Glutathione System: A New Drug Target in Neuroimmune Disorders
Morris, G., Anderson, G., Dean, O. M., Berk, M., Gałecki, P., Martín-Subero, M., & Maes, M. H. J. (2014) · Molecular Neurobiology · doi:10.1007/s12035-014-8705-x · Cited by 194
Cytoplasmic and Mitochondrial NADPH-Coupled Redox Systems in the Regulation of Aging
Bradshaw, P. C. (2019) · Nutrients · doi:10.3390/nu11030504 · Cited by 178
Thiol redox homeostasis in neurodegenerative disease
McBean, G. J., Aslan, M., Griffiths, H. R., & Torrão, R. C. (2015) · Redox Biology · doi:10.1016/j.redox.2015.04.004 · Cited by 182
Kast, R. E., Boockvar, J. A., Brüning, A., Cappello, F., Chang, W., Cvek, B., Dou, Q. P., Dueñas‐González, A., Efferth, T., Focosi, D., et al. (2013) · Oncotarget · doi:10.18632/oncotarget.969 · Cited by 168
Nasoohi, S., Ismael, S., & Ishrat, T. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-0917-z · Cited by 162
Yoshioka, J., Chutkow, W. A., Lee, S., Kim, J. B., Yan, J., Tian, R., Lindsey, M. L., Feener, E. P., Seidman, C. E., Seidman, J. G., et al. (2011) · Journal of Clinical Investigation · doi:10.1172/jci44927 · Cited by 159
Mitochondrial respiratory chain complexes as sources and targets of thiol-based redox-regulation
Dröse, S., Brandt, U., & Wittig, I. (2014) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2014.02.006 · Cited by 155
Hyperbaric Oxygen Treatment: Effects on Mitochondrial Function and Oxidative Stress
Schottlender, N., Gottfried, I., & Ashery, U. (2021) · Biomolecules · doi:10.3390/biom11121827 · Cited by 148
Ruszkiewicz, J. A., & Albrecht, J. (2015) · Neurochemistry International · doi:10.1016/j.neuint.2014.12.012 · Cited by 125
Banh, S., Wiens, L. M., Sotiri, E., & Treberg, J. R. (2015) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/j.cbpb.2015.10.001 · Cited by 119
Goemaere, J., & Knoops, B. (2011) · The Journal of Comparative Neurology · doi:10.1002/cne.22689 · Cited by 112
Lopert, P., Day, B. J., & Patel, M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0050683 · Cited by 100
Self-citationMunro, D., Baldy, C., Pamenter, M. E., & Treberg, J. R. (2019) · Aging Cell · doi:10.1111/acel.12916 · Cited by 104
Mou, W., Li, D., Luo, Z., Mao, L., & Ying, T. (2015) · PLoS ONE · doi:10.1371/journal.pone.0129598 · Cited by 99
Lopert, P., & Patel, M. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.533653 · Cited by 96
Self-citationAl-Yafee, Y. A., AL-Ayadhi, L. Y., Haq, S. H., & El-Ansary, A. K. (2011) · BMC Neurology · doi:10.1186/1471-2377-11-139 · Cited by 93
Mitochondrial Properties in Skeletal Muscle Fiber
Dong, H., & Tsai, S. (2023) · Cells · doi:10.3390/cells12172183 · Cited by 102
Aging: A mitochondrial DNA perspective, critical analysis and an update
Shokolenko, I. N. (2014) · World Journal of Experimental Medicine · doi:10.5493/wjem.v4.i4.46 · Cited by 101
Thioredoxin (Trx): A redox target and modulator of cellular senescence and aging-related diseases
Yang, B., Lin, Y., Huang, Y., Shen, Y.-Q., & Chen, Q. (2024) · Redox Biology · doi:10.1016/j.redox.2024.103032 · Cited by 94
Munro, D., Banh, S., Sotiri, E., Tamanna, N., & Treberg, J. R. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.04.014 · Cited by 82
Scavenging of H2O2 by mouse brain mitochondria
Starkov, A. A., Andreyev, A. Y., Zhang, S. F., Starkova, N. N., Korneeva, M., Syromyatnikov, M., & Popov, V. N. (2014) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-014-9581-9 · Cited by 80
Sahdeo, S., Scott, B. D., McMackin, M. Z., Jasoliya, M., Brown, B. M., Wulff, H., Perlman, S., Pook, M. A., & Cortopassi, G. A. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu408 · Cited by 81
Kuksal, N., Chalker, J., & Mailloux, R. J. (2017) · Biological Chemistry · doi:10.1515/hsz-2017-0160 · Cited by 74
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
Understanding Long COVID; Mitochondrial Health and Adaptation—Old Pathways, New Problems
Nunn, A. V. W., Guy, G. W., Brysch, W., & Bell, J. D. (2022) · Biomedicines · doi:10.3390/biomedicines10123113 · Cited by 74
Rossetti, A. C., Paladini, M. S., Riva, M. A., & Molteni, R. (2020) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2020.107520 · Cited by 73
Removal of H2O2 and generation of superoxide radical: Role of cytochrome c and NADH
Velayutham, M., Hemann, C. F., & Zweier, J. L. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.04.007 · Cited by 70
Maneb and Paraquat-Mediated Neurotoxicity: Involvement of Peroxiredoxin/Thioredoxin System
Roede, J. R., Hansen, J. M., Go, Y., & Jones, D. P. (2011) · Toxicological Sciences · doi:10.1093/toxsci/kfr058 · Cited by 67
The Role of the Thioredoxin System in Brain Diseases
Bjørklund, G., Zou, L., Peana, M., Chasapis, C. T., Hangan, T., Lu, J., & Maes, M. H. J. (2022) · Antioxidants · doi:10.3390/antiox11112161 · Cited by 74
Neuroprotection of antioxidant enzymes against transient global cerebral ischemia in gerbils
Lee, J., & Won, M. (2014) · Anatomy & Cell Biology · doi:10.5115/acb.2014.47.3.149 · Cited by 65
Sultana, R., Baglioni, M., Cecchetti, R., Cai, J., Klein, J. B., Bastiani, P., Ruggiero, C., Mecocci, P., & Butterfield, D. A. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.08.001 · Cited by 64
Acetaminophen Reactive Intermediates Target Hepatic Thioredoxin Reductase
Jan, Y.-H., Heck, D. E., Dragomir, A.-C., Gardner, C. R., Laskin, D. L., & Laskin, J. D. (2014) · Chemical Research in Toxicology · doi:10.1021/tx5000443 · Cited by 63
Kameritsch, P., Singer, M. S., Nuernbergk, C., Ríos, N., Reyes, A. M., Schmidt, K., Kirsch, J., Schneider, H., Müller, S., Pogoda, K., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1921828118 · Cited by 60
Tretter, L., Horváth, G., Hölgyesi, Á., Essek, F., & Adam-Vizi, V. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.09.024 · Cited by 63
Singh, P., & Chowdhuri, D. K. (2016) · Molecular Neurobiology · doi:10.1007/s12035-016-9909-z · Cited by 62
Simoni, S. D., Linard, D., Hermans, E., Knoops, B., & Goemaere, J. (2012) · Journal of Neurochemistry · doi:10.1111/jnc.12117 · Cited by 60
Kirsch, J., Schneider, H., Pagel, J.-I., Rehberg, M., Singer, M. S., Hellfritsch, J., Chillo, O., Schubert, K., Qiu, J., Pogoda, K., et al. (2016) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.116.307843 · Cited by 60
Slade, L., Chalker, J., Kuksal, N., Young, A., Gardiner, D., & Mailloux, R. J. (2017) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2017.05.010 · Cited by 60
Wang, L., Duan, Q., Wang, T., Ahmed, M., Zhang, N., Li, Y., Li, L., & Yao, X. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2015/217670 · Cited by 65
Mitochondrial function and energy metabolism in neuronal HT22 cells resistant to oxidative stress
Pfeiffer, A., Jaeckel, M., Lewerenz, J., Noack, R., Pouya, A., Schacht, T., Hoffmann, C., Winter, J., Schweiger, S., Schäfer, M. K. E., et al. (2013) · British Journal of Pharmacology · doi:10.1111/bph.12549 · Cited by 59
Mitozo, P. A., de Souza, L. F., Loch-Neckel, G., Flesch, S., Maris, A. F., Figueiredo, C. P., Santos, A. R. S., Farina, M., & Dafré, A. L. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.03.017 · Cited by 58
Hellfritsch, J., Kirsch, J., Schneider, M., Fluege, T., Wortmann, M., Frijhoff, J., Dagnell, M., Fey, T., Esposito, I., Kölle, P., et al. (2015) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.5889 · Cited by 57
Munro, D., & Pamenter, M. E. (2019) · Aging Cell · doi:10.1111/acel.13009 · Cited by 55
Simplified qPCR method for detecting excessive mtDNA damage induced by exogenous factors
Gureev, A. P., Shaforostova, E. A., Starkov, A. A., & Popov, V. N. (2017) · Toxicology · doi:10.1016/j.tox.2017.03.010 · Cited by 58
Kudin, A. P., Augustynek, B., Lehmann, A. K., Kovács, R., & Kunz, W. S. (2012) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2012.02.023 · Cited by 54
Tang, S., Fuß, A., Fattahi, Z., & Culmsee, C. (2024) · Cell Death and Disease · doi:10.1038/s41419-024-07015-8 · Cited by 53
Lopert, P., & Patel, M. (2014) · Redox Biology · doi:10.1016/j.redox.2014.04.010 · Cited by 52
Self-citationBirds and longevity: Does flight driven aerobicity provide an oxidative sink?
Hickey, A. J., Jüllig, M., Aitken, J. F., Loomes, K. M., Hauber, M. E., & Phillips, A. R. J. (2011) · Ageing Research Reviews · doi:10.1016/j.arr.2011.12.002 · Cited by 59
Fukui, M., Choi, H. J., & Zhu, B. T. (2012) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2012.04.030 · Cited by 54
Francisco, A., Ronchi, J. A., Navarro, C. D. C., Figueira, T. R., & Castilho, R. F. (2018) · Journal of Neurochemistry · doi:10.1111/jnc.14602 · Cited by 46
Molecular Targets in Alzheimer’s Disease
Bjørklund, G., Aaseth, J., Dadar, M., & Chirumbolo, S. (2019) · Molecular Neurobiology · doi:10.1007/s12035-019-1563-9 · Cited by 48
Cha, J., Kim, J. Y., Jung, I. J., Kim, M. R., Melencion, A., Alam, S. S., Yun, D., Lee, S. Y., Kim, M. G., & Kim, W. (2014) · Plant Physiology and Biochemistry · doi:10.1016/j.plaphy.2014.04.008 · Cited by 46
Yang, J., Hamid, S., Cai, J., Liu, Q., Xu, S., & Zhang, Z. (2017) · Cellular Signalling · doi:10.1016/j.cellsig.2017.07.012 · Cited by 44
Morris, G., Walder, K. R., Berk, M., Marx, W., Walker, A. J., Maes, M. H. J., & Puri, B. K. (2020) · Molecular Biology Reports · doi:10.1007/s11033-020-05590-5 · Cited by 47
Singh, M., Murthy, V., & Ramassamy, C. (2013) · Neurochemistry International · doi:10.1016/j.neuint.2013.01.030 · Cited by 43
Genetic Alterations in Oxidant and Anti-Oxidant Enzymes in the Vascular System
Awad, M. A., Aldosari, S., & Abid, M. R. (2018) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2018.00107 · Cited by 42
Chen, H., Denton, T. T., Xu, H., Calingasan, N. Y., Beal, M. F., & Gibson, G. E. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13836 · Cited by 42
Xia, N., Zhang, Q., Wang, S. T., Gu, L., Yang, H. M., Liu, L., Bakshi, R., Yang, H. M., & Zhang, H. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.09.017 · Cited by 41
Zhao, Y., Sun, Y., Ding, Y., Wang, X., Zhou, Y., Li, W., Huang, S., Li, Z., Kong, L., Guo, Q., et al. (2015) · Oncotarget · doi:10.18632/oncotarget.4657 · Cited by 42
Treberg, J. R., Munro, D., Banh, S., Zacharias, P., & Sotiri, E. (2015) · Redox Biology · doi:10.1016/j.redox.2015.05.001 · Cited by 42
Selenium Protects Neonates against Neurotoxicity from Prenatal Exposure to Manganese
Yang, X., Bao, Y., Fu, H., Li, L., Ren, T., & Yu, X. (2014) · PLoS ONE · doi:10.1371/journal.pone.0086611 · Cited by 39
Homozygous mutation in TXNRD1 is associated with genetic generalized epilepsy
Kudin, A. P., Baron, G., Zsurka, G., Hampel, K. G., Elger, C. E., Grote, A., Weber, Y. G., Lerche, H., Thiele, H., Nürnberg, P., et al. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.02.040 · Cited by 39
Zhou, J., Wang, C., Wu, J. S., Fukunaga, A., Cheng, Z., Wang, J., Yamauchi, A., Yodoi, J., & Tian, H. (2019) · Antioxidants and Redox Signaling · doi:10.1089/ars.2019.7807 · Cited by 39
Redox modification of proteins as essential mediators of CNS autophagy and mitophagy
Lizama, B. N., & McLaughlin, B. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.06.007 · Cited by 38
Li, C., Xia, W., Jiang, Y., Liu, W., Zhang, B., Xu, S., & Li, Y. (2020) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2020.139403 · Cited by 36
H2O2 Signalling Pathway: A Possible Bridge between Insulin Receptor and Mitochondria
Анатольевич, П. И. (2012) · Current Neuropharmacology · doi:10.2174/157015912804143559 · Cited by 36
Kamunde, C., Sharaf, M. S., & MacDonald, N. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.05.064 · Cited by 35
Induction of apoptosis in indole-3-carbinol-treated lung cancer H1299 cells via ROS level elevation
Lim, H. M., Park, S., & Nam, M. J. (2020) · Human & Experimental Toxicology · doi:10.1177/0960327120969968 · Cited by 33
Li, L., & Yu, A.-Q. (2015) · Journal of Cancer Research and Clinical Oncology · doi:10.1007/s00432-015-1916-3 · Cited by 34
Hippocampal antioxidative system in mesial temporal lobe epilepsy
Ristić, A. J., Savić, D. Z., Sokić, D. V., Pristov, J. B., Brkljačić, J. M., Baščarević, V., Raičević, S., Savić, S., & Spasojević, I. (2015) · Epilepsia · doi:10.1111/epi.12981 · Cited by 31
The compensatory antioxidant response system with a focus on neuroprogressive disorders
Morris, G., Puri, B. K., Walker, A. J., Berk, M., Walder, K. R., Bortolasci, C. C., Marx, W., Carvalho, A. F., & Maes, M. H. J. (2019) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/j.pnpbp.2019.109708 · Cited by 33
Brain Mitochondrial Drug Delivery: Influence of Drug Physicochemical Properties
Durazo, S. A., Kadam, R. S., Drechsel, D. A., Patel, M., & Kompella, U. B. (2011) · Pharmaceutical Research · doi:10.1007/s11095-011-0532-4 · Cited by 29
Self-citationTargeting mitochondria in the regulation of neurodegenerative diseases: A comprehensive review
Maurya, S. K., Gupta, S., Bakshi, A., Kaur, H., Jain, A., Senapati, S., & Baghel, M. S. (2022) · Journal of Neuroscience Research · doi:10.1002/jnr.25110 · Cited by 31
Knuuti, J., Belevich, G., Sharma, V., Bloch, D. A., & Verkhovskaya, M. L. (2013) · Molecular Microbiology · doi:10.1111/mmi.12424 · Cited by 29
The pH sensitivity of H2O2 metabolism in skeletal muscle mitochondria
Banh, S., & Treberg, J. R. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.04.035 · Cited by 29
Mitochondria can act as energy-sensing regulators of hydrogen peroxide availability
Treberg, J. R., Braun, K., & Selseleh, P. (2018) · Redox Biology · doi:10.1016/j.redox.2018.11.002 · Cited by 29
Embryonic oxidative stress results in reproductive impairment for adult zebrafish
Newman, T. A. C., Carleton, C., Leeke, B. J., Hampton, M. B., & Horsfield, J. A. (2015) · Redox Biology · doi:10.1016/j.redox.2015.10.010 · Cited by 28
Mechanism Underlying the Effectiveness of Deferiprone in Alleviating Parkinson’s Disease Symptoms
Sun, Y., Pham, A. N., & Waite, T. D. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.7b00478 · Cited by 28
Measurement of ROS Homeostasis in Isolated Mitochondria
Tretter, L., & Ambrus, A. (2014) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/b978-0-12-801415-8.00012-6 · Cited by 27
Veniamin, S., Sawatzky, L. G., Banting, G. S., & Glerum, D. M. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.06.024 · Cited by 27
Yang, J., Hamid, S., Liu, Q., Cai, J., Xu, S., & Zhang, Z. (2017) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2017.08.027 · Cited by 25
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