Glutathione/thioredoxin systems modulate mitochondrial H2O2 emission: An experimental-computational study
Open accessAbstract
The net emission of hydrogen peroxide (H2O2) from mitochondria results from the balance between reactive oxygen species (ROS) continuously generated in the respiratory chain and ROS scavenging. The relative contribution of the two major antioxidant systems in the mitochondrial matrix, glutathione (GSH) and thioredoxin (Trx), has not been assessed. In this paper, we examine this key question via combined experimental and theoretical approaches, using isolated heart mitochondria from mouse, rat, and guinea pig. As compared with untreated control mitochondria, selective inhibition of Trx reductase with auranofin along with depletion of GSH with 2,4-dinitrochlorobenzene led to a species-dependent increase in H2O2 emission flux of 17, 11, and 6 fold in state 4 and 15, 7, and 8 fold in state 3 for mouse, rat, and guinea pig mitochondria, respectively. The maximal H2O2 emission as a percentage of the total O2 consumption flux was 11%/2.3% for mouse in states 4 and 3 followed by 2%/0.25% and 0.74%/0.29% in the rat and guinea pig, respectively. A minimal computational model accounting for the kinetics of GSH/Trx systems was developed and was able to simulate increase in H2O2 emission fluxes when both scavenging systems were inhibited separately or together. Model simulations suggest that GSH/Trx systems act in concert. When the scavenging capacity of either one of them saturates during H2O2 overload, they relieve each other until complete saturation, when maximal ROS emission occurs. Quantitatively, these results converge on the idea that GSH/Trx scavenging systems in mitochondria are both essential for keeping minimal levels of H2O2 emission, especially during state 3 respiration, when the energetic output is maximal. This suggests that the very low levels of H2O2 emission observed during forward electron transport in the respiratory chain are a result of the well-orchestrated actions of the two antioxidant systems working continuously to offset ROS production.
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
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?
A small proportion (~2-11%) of electrons entering the ETC escape from the chain at complex I or III to generate superoxide.
“Although the majority of electrons entering the ETC ultimately reduce oxygen to water at complex IV, a small proportion (~2–11%) of electrons escape from the chain at complex I or III to generate superoxide (34, 115, 678).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [34]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
How mitochondria produce reactive oxygen species
Murphy, M. P. (2009) · Biochemical Journal · doi:10.1042/bj20081386 · Cited by 8,207 · see citing works
The NOX Family of ROS-Generating NADPH Oxidases: Physiology and Pathophysiology
Bedard, K., & Krause, K.-H. (2007) · Physiological Reviews · doi:10.1152/physrev.00044.2005 · Cited by 6,989 · see citing works
Hydroperoxide metabolism in mammalian organs.
Chance, B., Sies, H., & Boveris, A. (1979) · Physiological Reviews · doi:10.1152/physrev.1979.59.3.527 · Cited by 5,827 · see citing works
Mitochondria, Oxidants, and Aging
Balaban, R. S., Nemoto, S., & Finkel, T. (2005) · Cell · doi:10.1016/j.cell.2005.02.001 · Cited by 4,388 · see citing works
The Nrf2-antioxidant response element signaling pathway and its activation by oxidative stress
Nguyen, T., Nioi, P., & Pickett, C. B. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.r900010200 · Cited by 2,655 · see citing works
The cellular production of hydrogen peroxide
Boveris, A., Oshino, N., & Chance, B. (1972) · Biochemical Journal · doi:10.1042/bj1280617 · Cited by 1,549 · see citing works
Topology of superoxide production from different sites in the mitochondrial electron transport chain
St-Pierre, J., Buckingham, J. A., Roebuck, S. J., & Brand, M. D. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207217200 · Cited by 1,545 · see citing works
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 · see citing works
Mitochondria and reactive oxygen species
Kowaltowski, A. J., de Souza-Pinto, N. C., Castilho, R. F., & Vercesi, A. E. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.05.004 · Cited by 1,162 · see citing works
NADPH oxidase 4 (Nox4) is a major source of oxidative stress in the failing heart
Kuroda, J., Ago, T., Matsushima, S., Zhai, P., Schneider, M. D., & Sadoshima, J. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1002178107 · Cited by 772 · see citing works
Imai, H., & Nakagawa, Y. (2003) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)01197-8 · Cited by 763 · see citing works
Mitochondrial α-Ketoglutarate Dehydrogenase Complex Generates Reactive Oxygen Species
Starkov, A. A., Fiskum, G. M., Chinopoulos, C., Lorenzo, B. J., Browne, S. E., Patel, M. S., & Beal, M. F. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.1899-04.2004 · Cited by 692 · see citing works
Peroxiredoxin, a Novel Family of Peroxidases
Rhee, S. G., Kang, S. W., Chang, T., Jeong, W., & Kim, K. (2001) · IUBMB Life · doi:10.1080/15216540252774748 · Cited by 642 · see citing works
Redox compartmentalization in eukaryotic cells.
Go, Y., & Jones, D. P. (2008) · Biochimica et Biophysica Acta · doi:10.1016/j.bbagen.2008.01.011 · Cited by 635 · see citing works
Bioenergetics and the formation of mitochondrial reactive oxygen species
Ádám‐Vizi, V., & Chinopoulos, C. (2006) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2006.10.005 · Cited by 613 · see citing works
New features of the software M at C ont for bifurcation analysis of dynamical systems
Dhooge, A., Govaerts, W. J. F., Kuznetsov, Y. A., et al. (2008) · Mathematical and Computer Modelling of Dynamical Systems · doi:10.1080/13873950701742754 · Cited by 607 · see citing works
Thioredoxin and thioredoxin reductase: Current research with special reference to human disease
Holmgren, A., & Lu, J. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.03.083 · Cited by 577 · see citing works
Detection of catalase in rat heart mitochondria.
Radi, R., Turrens, J. F., Chang, L. Y., Bush, K. M., Crapo, J. D., & Freeman, B. A. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54740-2 · Cited by 573 · see citing works
Human Placenta Thioredoxin Reductase
Gromer, S., Arscott, L. D., Williams, C. H., Schirmer, R. H., & Becker, K. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.32.20096 · Cited by 538 · see citing works
Mitochondrial peroxiredoxin involvement in antioxidant defence and redox signalling
Cox, A. G., Winterbourn, C. C., & Hampton, M. B. (2009) · Biochemical Journal · doi:10.1042/bj20091541 · Cited by 530 · see citing works
Dai, D.-F., Johnson, S. C., Villarin, J. J., Chin, M. T., Nieves-Cintrón, M., Chen, T., Marcinek, D. J., Dorn, G. W., Kang, Y. J., Prolla, T. A., et al. (2011) · Circulation Research · doi:10.1161/circresaha.110.232306 · Cited by 527 · see citing works
Han, D., WILLIAMS, E., & Cadenas, E. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3530411 · Cited by 516 · see citing works
Stowe, D. F., & Camara, A. K. S. (2009) · Antioxidants & Redox Signaling · doi:10.1089/ars.2008.2331 · Cited by 471 · see citing works
Mitochondria-targeted antioxidants protect against amyloid-β toxicity in Alzheimer's disease neurons
Manczak, M., Mao, P., Calkins, M. J., Cornea, A., Reddy, A. P., Murphy, M. P., Szeto, H. H., Park, B., & Reddy, P. H. (2010) · Journal of Alzheimer's Disease · doi:10.3233/jad-2010-100564 · Cited by 469 · see citing works
Dependence of H2O2 formation by rat heart mitochondria on substrate availability and donor age
Hansford, R. G., Hogue, B. A., & Mildaziene, V. (1997) · Journal of Bioenergetics and Biomembranes · doi:10.1023/a:1022420007908 · Cited by 447 · see citing works
Fatty acids as modulators of the cellular production of reactive oxygen species
Schönfeld, P., & Wojtczak, L. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.04.029 · Cited by 441 · see citing works
An Attempt to Prevent Senescence: A Mitochondrial Approach
Skulachev, V. P., Anisimov, V. N., Antonenko, Y. N., Bakeeva, L. E., Chernyak, B. V., Erichev, V. P., Filenko, O. F., Kalinina, N. I., Kapelko, V. I., Kolosova, N. G., et al. (2009) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2008.12.008 · Cited by 430 · see citing works
Mitochondria-Targeted Small Molecule Therapeutics and Probes
Smith, R. A. J., Hartley, R. C., & Murphy, M. P. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2011.3969 · Cited by 399 · see citing works
Redox-optimized ROS balance: A unifying hypothesis
Aon, M. A., Cortassa, S. C., & O'Rourke, B. P. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.02.016 · Cited by 376 · see citing works
Self-citationStyskal, J., Remmen, H. V., Richardson, A. G., & Salmon, A. B. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.10.441 · Cited by 286 · see citing works
Hu, J., Dong, L., & Outten, C. E. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803028200 · Cited by 273 · see citing works
Zhong, L., Arnér, E. S. J., Lundström-Ljung, J., Åslund, F., & Holmgren, A. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.15.8581 · Cited by 263 · see citing works
Kinetics and mechanism of the reduction of ferricytochrome c by the superoxide anion.
Butler, J., Koppenol, W. H., & Margoliash, E. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)33886-9 · Cited by 261 · see citing works
Mitochondrial Free Radical Production and Aging in Mammals and Birdsa
Barja, G. (1998) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1998.tb09905.x · Cited by 246 · see citing works
Redox compartmentalization and cellular stress
Jones, D. P., & Go, Y.-M. (2010) · Diabetes Obesity and Metabolism · doi:10.1111/j.1463-1326.2010.01266.x · Cited by 246 · see citing works
A Mitochondrial Oscillator Dependent on Reactive Oxygen Species
Cortassa, S., Aon, M. A., Winslow, R. L., & O’Rourke, B. (2004) · Biophysical Journal · doi:10.1529/biophysj.104.041749 · Cited by 235 · see citing works
Self-citationCatalase Takes Part in Rat Liver Mitochondria Oxidative Stress Defense
Salvi, M., Battaglia, V., Brunati, A. M., La Rocca, N., Tibaldi, E., Pietrangeli, P., Marcocci, L., Mondovi, B., Rossi, C. A., & Toninello, A. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m701589200 · Cited by 231 · see citing works
Kaludercic, N., Takimoto, E., Nagayama, T., Feng, N., Lai, E. W., Bedja, D., Chen, K., Gabrielson, K. L., Blakely, R., Shih, J. C., et al. (2009) · Circulation Research · doi:10.1161/circresaha.109.198366 · Cited by 222 · see citing works
Self-citationHan, D., Canali, R., Rettori, D., & Kaplowitz, N. (2003) · Molecular Pharmacology · doi:10.1124/mol.64.5.1136 · Cited by 212 · see citing works
Sazanov, L. A., & Jackson, J. B. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)00370-x · Cited by 205 · see citing works
Sequential Opening of Mitochondrial Ion Channels as a Function of Glutathione Redox Thiol Status
Aon, M. A., Cortassa, S. C., Maack, C., & O'Rourke, B. P. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702841200 · Cited by 200 · see citing works
Self-citationRespiration-dependent H2O2 removal in brain mitochondria via the thioredoxin/peroxiredoxin system
Drechsel, D. A., & Patel, M. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.101196 · Cited by 199 · see citing works
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 197 · see citing works
Self-citationRackham, O., Nichols, S. J., Leedman, P. J., Berners‐Price, S. J., & Filipovska, A. (2007) · Biochemical Pharmacology · doi:10.1016/j.bcp.2007.07.022 · Cited by 185 · see citing works
Hoffman, D. L., & Brookes, P. S. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m809512200 · Cited by 182 · see citing works
Garcia, J., Han, D., Sancheti, H., Yap, L.-P., Kaplowitz, N., & Cadenas, E. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.164160 · Cited by 178 · see citing works
A Model of Redox Kinetics Implicates the Thiol Proteome in Cellular Hydrogen Peroxide Responses
Adimora, N. J., Jones, D. P., & Kemp, M. L. (2010) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.2968 · Cited by 175 · see citing works
The Putative Glutathione Peroxidase Gene ofPlasmodium falciparum Codes for a Thioredoxin Peroxidase
Sztajer, H., Gamain, B., Aumann, K.-D., Slomianny, C., Becker, K., Brigelius‐Flohé, R., & Flohé, L. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008631200 · Cited by 153 · see citing works
Cytochrome c, an ideal antioxidant
Pereverzev, M. O., Vygodina, T. V., Konstantinov, A. A., & Skulachev, V. P. (2003) · Biochemical Society Transactions · doi:10.1042/bst0311312 · Cited by 150 · see citing works
Mitochondrial Approaches to Protect Against Cardiac Ischemia and Reperfusion Injury
Camara, A. K. S., Bienengraeber, M., & Stowe, D. F. (2011) · Frontiers in Physiology · doi:10.3389/fphys.2011.00013 · Cited by 150 · see citing works
Mitochondrial criticality: A new concept at the turning point of life or death
Aon, M. A., Cortassa, S. C., Akar, F. G., & O'Rourke, B. P. (2005) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2005.06.008 · Cited by 146 · see citing works
Self-citationPasdois, P., Parker, J. E., Griffiths, E. J., & Halestrap, A. P. (2011) · Biochemical Journal · doi:10.1042/bj20101957 · Cited by 127 · see citing works
Pérez, V. I., Lew, C. M., Cortez, L. A., Webb, C. R., Rodriguez, M. R., Liu, Y.-H., Qi, W., Li, Y., Chaudhuri, A., Remmen, H. V., et al. (2008) · Free Radical Biology & Medicine · doi:10.1016/j.freeradbiomed.2007.11.018 · Cited by 118 · see citing works
The antioxidant functions of cytochrome c
Korshunov, S., Krasnikov, B. F., PEREVERZEV, M. O., & Skulachev, V. P. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)01525-2 · Cited by 117 · see citing works
From mitochondrial dynamics to arrhythmias
Aon, M. A., Cortassa, S. C., Akar, F. G., Brown, D. A., Zhou, L., & O'Rourke, B. P. (2009) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2009.02.016 · Cited by 116 · see citing works
Self-citationBrown, D. A., Aon, M. A., Frasier, C. R., Sloan, R. C., Maloney, A. H., Anderson, E. J., & O'Rourke, B. P. (2009) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2009.11.011 · Cited by 106 · see citing works
Self-citationRedox Signaling and Regulation in Biology and Medicine
(2009) · Wiley eBooks · doi:10.1002/9783527627585 · Cited by 93 · see citing works
Glutathione oxidation as a trigger of mitochondrial depolarization and oscillation in intact hearts
Slodzinski, M. K., Aon, M. A., & O'Rourke, B. P. (2008) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2008.07.017 · Cited by 93 · see citing works
Self-citationSheeran, F. L., Rydström, J., Shakhparonov, M. I., Pestov, N. B., & Pepe, S. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.04.002 · Cited by 91 · see citing works
Aon, M. A., Cortassa, S. C., Wei, A., Grunnet, M., & O'Rourke, B. P. (2009) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2009.08.002 · Cited by 90 · see citing works
Self-citationSemisynthesis and Characterization of Mammalian Thioredoxin Reductase
Eckenroth, B. E., Harris, K. M., Turanov, A. A., et al. (2006) · Biochemistry · doi:10.1021/bi0517887 · Cited by 82 · see citing works
Rigobello, M. P., Gandin, V., Folda, A., Rundlöf, A.-K., Fernandes, A. P., Bindoli, A., Marzano, C., & Björnstedt, M. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.05.027 · Cited by 75 · see citing works
Iñarrea, P., Moini, H., Han, D., Rettori, D., Aguiló, I., Alava, M. A., Iturralde, M., & Cadenas, E. (2007) · Biochemical Journal · doi:10.1042/bj20061809 · Cited by 73 · see citing works
Biary, N., Xie, C., Kauffman, J., & Akar, F. G. (2011) · The Journal of Physiology · doi:10.1113/jphysiol.2011.214239 · Cited by 55 · see citing works
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 · see citing works
Mitochondrial transhydrogenase – a key enzyme in insulin secretion and, potentially, diabetes
Rydström, J. (2006) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2006.05.003 · Cited by 39 · see citing works
Novogrodsky, A., Nehring, R. E., & Meister, A. (1979) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.76.10.4932 · Cited by 37 · see citing works
Pillay, C. S., Hofmeyr, J. S., Olivier, B. G., Snoep, J. L., & Rohwer, J. M. (2008) · Biochemical Journal · doi:10.1042/bj20080690 · Cited by 37 · see citing works
Mitochondrial Respiratory Chain
Rustin, P. (2008) · Springer eBooks · doi:10.1007/978-3-540-76698-8_16 · Cited by 13 · see citing works
Chockalingam, K., Luba, J. P., Nick, H. S., et al. (2006) · FEBS Journal · doi:10.1111/j.1742-4658.2006.05484.x · Cited by 13 · see citing works
Free Radicals and Mammalian Aging
Sanz, A., Barja, G., Pamplona, R., & Leeuwenburgh, C. (2009) · Wiley eBooks · doi:10.1002/9783527627585.ch19 · Cited by 7 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Mitochondrial Reactive Oxygen Species (ROS) and ROS-Induced ROS Release
Zorov, D. B., Juhaszova, M., & Sollott, S. J. (2014) · Physiological Reviews · doi:10.1152/physrev.00026.2013 · Cited by 5,383 · see citing works
Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation
Tejero, J., Shiva, S., & Gladwin, M. T. (2019) · Physiological Reviews · doi:10.1152/physrev.00036.2017 · Cited by 541 · see citing works
Mitochondrial and cellular mechanisms for managing lipid excess
Aon, M. A., Bhatt, N., & Cortassa, S. C. (2014) · Frontiers in Physiology · doi:10.3389/fphys.2014.00282 · Cited by 253 · see citing works
Self-citationInflammasome and Autophagy Regulation: A Two-way Street
Sun, Q., Fan, J., Billiar, T. R., & Scott, M. J. (2017) · Molecular Medicine · doi:10.2119/molmed.2017.00077 · Cited by 203 · see citing works
Wang, X., Liu, R., Zhang, W., Zhang, X., Liao, N., Wang, Z., Li, W., Qin, X., & Hai, C. (2013) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2013.06.014 · Cited by 172 · see citing works
Physical Exercise: A Novel Tool to Protect Mitochondrial Health
Sorriento, D., Di Vaia, E., & Iaccarino, G. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.660068 · Cited by 118 · see citing works
Tyagi, P., Tasleem, M., Prakash, S., & Chouhan, G. (2020) · Food Research International · doi:10.1016/j.foodres.2020.109489 · Cited by 42 · see citing works
Ježek, J., Engstová, H., & Ježek, P. (2017) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2017.05.005 · Cited by 30 · see citing works
Bacci, A., Runfola, M., Sestito, S., & Rapposelli, S. (2021) · Antioxidants · doi:10.3390/antiox10030367 · Cited by 23 · see citing works
- Authors
- Aon, M. A., Stanley, B. A., Sivakumaran, V., Kembro, J. M., O'Rourke, B., Paolocci, N., & Cortassa, S.
- Affiliations
- Johns Hopkins University (US)
- Corresponding author
- Cortassa, Sonia
- Venue
- Journal of General Physiology
- Publisher
- Rockefeller University Press
- Published
- 2012-05-14
- Volume
- 139
- Issue
- 6
- Pages
- 479-491
- ISSN
- 0022-1295 (ISSN-L)
- 1540-7748
- PMC
- PMC3362521
- OpenAlex
- W2131211730
- Cited by
- 200
- References
- 71
- Citations by year
- 2026: 10 · 2025: 9 · 2024: 13 · 2023: 10 · 2022: 14 · 2021: 19 · 2020: 8 · 2019: 15 · 2018: 17 · 2017: 18 · 2016: 10 · 2015: 21 · 2014: 19 · 2013: 14 · 2012: 3
- FWCI
- 7.32
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The Journal of General Physiology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Padua Research Archive (University of Padova) (submittedVersion, cc-by-nc-sa)
- Americanae (AECID Library) (submittedVersion, cc-by-nc-sa)
- LA Referencia (Red Federada de Repositorios Institucionales de Publicaciones Científicas) (submittedVersion, cc-by-nc-sa)
- Funders
- National Heart, Lung, and Blood Institute (R37-HL-54598, R37HL054598, R01HL091923, R21HL106054, P01HL107153)
- 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
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glutathione Transferases and Polymorphisms
- Keywords
- glutathione, thioredoxin, thioredoxin reductase, auranofin, 1-chloro-2,4-dinitrobenzene, reactive oxygen species scavenging, electron transport chain, state 3 respiration, state 4 respiration, species differences, antioxidant defense
- MeSH terms
- Animals, Antioxidants, Electron Transport, Glutathione, Guinea Pigs, Hydrogen Peroxide, Kinetics, Mitochondria, Heart, Models, Theoretical, Thioredoxins, Reactive Oxygen Species, Cell Respiration, Mice, Rats
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
