Mitochondrial metabolism of reactive oxygen species

Andreyev, A. Yu.; Kushnareva, Yu. E.; Starkov, A. A.

doi:10.1007/s10541-005-0102-7

Cited by 1,336Mitochondrial Function and PathologyRedox biology and oxidative stressAutophagy in Disease and Therapy

Mitochondrial metabolism of reactive oxygen species

Andreyev, A. Yu., Kushnareva, Yu. E., Starkov, A. A.·2005·Biochemistry (Moscow)

DOI 10.1007/s10541-005-0102-7

Open this paper in CoChat — free account

Abstract

Oxidative stress is considered a major contributor to etiology of both "normal" senescence and severe pathologies with serious public health implications. Mitochondria generate reactive oxygen species (ROS) that are thought to augment intracellular oxidative stress. Mitochondria possess at least nine known sites that are capable of generating superoxide anion, a progenitor ROS. Mitochondria also possess numerous ROS defense systems that are much less studied. Studies of the last three decades shed light on many important mechanistic details of mitochondrial ROS production, but the bigger picture remains obscure. This review summarizes the current knowledge about major components involved in mitochondrial ROS metabolism and factors that regulate ROS generation and removal. An integrative, systemic approach is applied to analysis of mitochondrial ROS metabolism, which is now dissected into mitochondrial ROS production, mitochondrial ROS removal, and mitochondrial ROS emission. It is suggested that mitochondria augment intracellular oxidative stress due primarily to failure of their ROS removal systems, whereas the role of mitochondrial ROS emission is yet to be determined and a net increase in mitochondrial ROS production in situ remains to be demonstrated.

Integrity signals

Registry

Crossref · 10.1007/s10541-005-0102-7

Cites

175 of 175 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

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?

Although nonmitochondrial sources of ROS exist during ischemia, the majority of ROS are likely derived from the mitochondrial respiratory complexes.
“Although nonmitochondrial sources of ROS exist during ischemia [e.g., NAD(P)H oxidase (141, 188, 328) and xanthine oxidase (25) in vasculature], the majority of ROS are likely derived from the mitochondrial respiratory complexes, as shown by the damage to respiratory complexes (212, 213, 245) and the effect of mitochondrial inhibitors (5, 28, 71, 81–86).”
From Mitochondrial reactive oxygen species production in excitable cells: Modulators of mitochondrial and cell function (2009) · cites this paper as [5]
During early ischemia in isolated hearts, ROS increase along with mitochondrial [Ca2+] and the redox state (NADH).
“During early ischemia in isolated hearts, ROS increase along with mitochondrial [Ca2+] and the redox state (NADH), as shown in Fig. 17 (5, 70, 298)”
From Mitochondrial reactive oxygen species production in excitable cells: Modulators of mitochondrial and cell function (2009) · cites this paper as [5]

Mitochondrial formation of reactive oxygen species
Turrens, J. F. (2003) · The Journal of Physiology · doi:10.1113/jphysiol.2003.049478 · Cited by 5,084 · see citing works
The mitochondrial generation of hydrogen peroxide. General properties and effect of hyperbaric oxygen
Boveris, A., & Chance, B. (1973) · Biochemical Journal · doi:10.1042/bj1340707 · Cited by 2,626 · see citing works
Structure, mechanism and regulation of peroxiredoxins
Wood, Z. A., Schröder, E., Harris, J. R., & Poole, L. B. (2003) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(02)00003-8 · Cited by 2,546 · see citing works
The Respiratory Chain and Oxidative Phosphorylation
Chance, B., & Williams, G. R. (1956) · Advances in enzymology and related areas of molecular biology/Advances in enzymology and related subjects · doi:10.1002/9780470122624.ch2 · Cited by 2,084 · see citing works
Dilated cardiomyopathy and neonatal lethality in mutant mice lacking manganese superoxide dismutase
Li, Y., Huang, T.-T., Carlson, E. J., Melov, S., Ursell, P. C., Olson, J. L., Noble, L. J., Yoshimura, M. P., Berger, C., Chan, P. H., et al. (1995) · Nature Genetics · doi:10.1038/ng1295-376 · Cited by 1,789 · see citing works
High protonic potential actuates a mechanism of production of reactive oxygen species in mitochondria
Korshunov, S. S., Skulachev, V. P., & Starkov, A. A. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)01159-9 · Cited by 1,727 · see citing works
Self-citation
Metabolism and functions of glutathione in brain
Dringen, R. (2000) · Progress in Neurobiology · doi:10.1016/s0301-0082(99)00060-x · Cited by 1,702 · see citing works
Molecular Pathways of Neurodegeneration in Parkinson's Disease
Dawson, T. M., & Dawson, V. L. (2003) · Science · doi:10.1126/science.1087753 · Cited by 1,659 · see citing works
Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria
Turrens, J. F., & Boveris, A. (1980) · Biochemical Journal · doi:10.1042/bj1910421 · Cited by 1,601 · 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
How super is superoxide?
Sawyer, D. T., & Valentine, J. S. (1981) · Accounts of Chemical Research · doi:10.1021/ar00072a005 · Cited by 1,352 · see citing works
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 · see citing works
Mitochondria and neuronal survival
Nicholls, D. G., & Budd, S. L. (2000) · Physiological Reviews · doi:10.1152/physrev.2000.80.1.315 · Cited by 1,243 · see citing works
Ubisemiquinone is the electron donor for superoxide formation by complex III of heart mitochondria
Turrens, J. F., Alexandre, A., & Lehninger, A. L. (1985) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(85)90293-0 · Cited by 1,214 · see citing works
Analysis of glutathione: implication in redox and detoxification
Pastore, A., Federici, G., Bertini, E., & Piemonte, F. (2003) · Clinica Chimica Acta · doi:10.1016/s0009-8981(03)00200-6 · Cited by 1,185 · see citing works
Low antioxidant enzyme gene expression in pancreatic islets compared with various other mouse tissues
Lenzen, S., Drinkgern, J., & Tiedge, M. (1996) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(96)02051-5 · Cited by 1,167 · see citing works
Mice deficient in cellular glutathione peroxidase show increased vulnerability to malonate, 3-nitropropionic acid, and 1-methyl-4-phenyl-1,2,5,6-tetrahydropyridine
Klivenyi, P., Andreassen, O. A., Ferrante, R. J., Dedeoglu, A., Mueller, G., Lancelot, E., Bogdanov, M., Andersen, J. K., Jiang, D., & Beal, M. F. (2000) · The Journal of Neuroscience · doi:10.1523/jneurosci.20-01-00001.2000 · Cited by 1,111 · see citing works
Electron transfer by domain movement in cytochrome bc1
Zhang, Z., Huang, L.-S., Shulmeister, V. M., Chi, Y., Kim, K. K., Hung, L., Crofts, A. R., Berry, E. A., & Kim, S. (1998) · Nature · doi:10.1038/33612 · Cited by 1,059 · see citing works
Complex iii releases superoxide to both sides of the inner mitochondrial membrane
Muller, F. L., Liu, Y., & Van Remmen, H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m407715200 · Cited by 1,036 · see citing works
Neurodegeneration, myocardial injury, and perinatal death in mitochondrial superoxide dismutase-deficient mice
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 · see citing works
Superoxide production by the mitochondrial respiratory chain
Turrens, J. F. (1997) · Bioscience Reports · doi:10.1023/a:1027374931887 · Cited by 903 · see citing works
Production of superoxide radicals and hydrogen peroxide by NADH-ubiquinone reductase and ubiquinol-cytochrome c reductase from beef-heart mitochondria
Cadenas, E., Boveris, A., Ragan, C. I., & Stoppani, A. O. M. (1977) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(77)90035-2 · Cited by 855 · see citing works
The selenoprotein GPX4 is essential for mouse development and protects from radiation and oxidative damage insults
Yant, L. J., Ran, Q., Rao, L., Van Remmen, H., Shibatani, T., Belter, J. G., Motta, L., Richardson, A., & Prolla, T. A. (2003) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)01360-6 · Cited by 797 · see citing works
Biological significance of phospholipid hydroperoxide glutathione peroxidase (PHGPx, GPx4) in mammalian cells
Imai, H., & Nakagawa, Y. (2003) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)01197-8 · Cited by 763 · see citing works
Molecular pathways to neurodegeneration
Bossy-Wetzel, E., Schwarzenbacher, R., & Lipton, S. A. (2004) · Nature Medicine · doi:10.1038/nm1067 · Cited by 740 · see citing works
Life-long reduction in MnSOD activity results in increased DNA damage and higher incidence of cancer but does not accelerate aging
Van Remmen, H., Ikeno, Y., Hamilton, M., Pahlavani, M., Wolf, N., Thorpe, S. R., Alderson, N. L., Baynes, J. W., Epstein, C. J., Huang, T.-T., et al. (2003) · Physiological Genomics · doi:10.1152/physiolgenomics.00122.2003 · Cited by 734 · see citing works
Role of uncoupled and non-coupled oxidations in maintenance of safely low levels of oxygen and its one-electron reductants
Skulachev, V. P. (1996) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583500005795 · Cited by 703 · 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
Self-citation
Complex I-mediated reactive oxygen species generation: modulation by cytochrome c and NAD(P)+ oxidation–reduction state
Kushnareva, Y., Murphy, A. N., & Andreyev, A. Y. (2002) · Biochemical Journal · doi:10.1042/bj20021121 · Cited by 677 · see citing works
Self-citation
Glutaredoxins: Glutathione-Dependent Redox Enzymes with Functions Far Beyond a Simple Thioredoxin Backup System
Fernandes, A. P., & Holmgren, A. (2004) · Antioxidants and Redox Signaling · doi:10.1089/152308604771978354 · Cited by 670 · see citing works
Role of ubiquinone in the mitochondrial generation of hydrogen peroxide
Boveris, A., Cadenas, E., & Stoppani, A. O. M. (1976) · Biochemical Journal · doi:10.1042/bj1560435 · Cited by 655 · see citing works
Influence of Thyroid Hormones on l-α-Glycerophosphate Dehydrogenases and Other Dehydrogenases in Various Organs of the Rat
Lee, Y., & Lardy, H. A. (1965) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)97593-9 · Cited by 642 · see citing works
Superoxide radicals as precursors of mitochondrial hydrogen peroxide
Loschen, G., Azzi, A., Richter, C., & Flohé, L. (1974) · FEBS Letters · doi:10.1016/0014-5793(74)80281-4 · Cited by 634 · see citing works
The protonmotive Q cycle. Energy transduction by coupling of proton translocation to electron transfer by the cytochrome bc1 complex.
Trumpower, B. L. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)38410-8 · Cited by 596 · see citing works
Mitochondrial respiratory chain-dependent generation of superoxide anion and its release into the intermembrane space
HAN, D., WILLIAMS, E., & CADENAS, E. (2001) · Biochemical Journal · doi:10.1042/bj3530411 · Cited by 593 · see citing works
The Mitochondrial Production of Reactive Oxygen Species: Mechanisms and Implications in Human Pathology
Lenaz, G. (2001) · IUBMB Life · doi:10.1080/15216540152845957 · Cited by 585 · 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
Mice Deficient in Cellular Glutathione Peroxidase Develop Normally and Show No Increased Sensitivity to Hyperoxia
Ho, Y., Magnenat, J.-L., Bronson, R. T., Cao, J., Gargano, M. D., Sugawara, M., & Funk, C. D. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.26.16644 · Cited by 562 · see citing works
Respiratory chain linked H2O2 production in pigeon heart mitochondria
Loschen, G., & Flohé, L. (1971) · FEBS Letters · doi:10.1016/0014-5793(71)80459-3 · Cited by 552 · see citing works
Do Mitochondria Produce Oxygen Radicals in vivo?
Nohl, H., & HEGNER, D. (1978) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1978.tb12051.x · Cited by 523 · see citing works
Protective action of phospholipid hydroperoxide glutathione peroxidase against membrane-damaging lipid peroxidation. In situ reduction of phospholipid and cholesterol hydroperoxides.
Thomas, J. P., Maiorino, M., Ursini, F., & Girotti, A. W. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)40252-4 · Cited by 522 · see citing works
Molecular Aspects of α-Tocotrienol Antioxidant Action and Cell Signalling
Packer, L., Weber, S. U., & Rimbach, G. H. (2001) · Journal of Nutrition · doi:10.1093/jn/131.2.369s · Cited by 520 · see citing works
Mitochondrial respiratory chain-dependent generation of superoxide anion and its release into the intermembrane space
Han, D., WILLIAMS, E., & Cadenas, E. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3530411 · Cited by 516 · see citing works
Characterization of Superoxide-producing Sites in Isolated Brain Mitochondria
Kudin, A. P., Bimpong‐Buta, N., Vielhaber, S., Elger, C. E., & Kunz, W. S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m310341200 · Cited by 505 · see citing works
Origin and turnover of mitochondrial glutathione.
Griffith, O. W., & Meister, A. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.14.4668 · Cited by 500 · see citing works
Mitochondrial Oxygen Radical Generation and Leak: Sites of Production in States 4 and 3, Organ Specificity, and Relation to Aging and Longevity
Barja, G. (1999) · Journal of Bioenergetics and Biomembranes · doi:10.1023/a:1005427919188 · Cited by 494 · see citing works
Isolated Cerebral and Cerebellar Mitochondria Produce Free Radicals when Exposed to Elevated Ca2+ and Na+: Implications for Neurodegeneration
Dykens, J. A. (1994) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1994.63020584.x · Cited by 493 · see citing works
Regulation of brain mitochondrial H 2 O 2 production by membrane potential and NAD(P)H redox state
Starkov, A. A., & Fiskum, G. M. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01908.x · Cited by 491 · see citing works
Self-citation
The thioredoxin system—From science to clinic
Gromer, S., Urig, S., & Becker, K. (2003) · Medicinal Research Reviews · doi:10.1002/med.10051 · Cited by 482 · see citing works
Superoxide Radical and Iron Modulate Aconitase Activity in Mammalian Cells
Gardner, P. R., Raineri, I., Epstein, L. B., & White, C. W. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.22.13399 · Cited by 471 · see citing works
Superoxide production by NADH:ubiquinone oxidoreductase (complex I) depends on the pH gradient across the mitochondrial inner membrane
LAMBERT, A. J., & BRAND, M. D. (2004) · Biochemical Journal · doi:10.1042/bj20040485 · Cited by 470 · see citing works
Generation of Reactive Oxygen Species in the Reaction Catalyzed by α-Ketoglutarate Dehydrogenase
Tretter, L., & Ádám‐Vizi, V. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.1842-04.2004 · Cited by 455 · see citing works
Increased Oxidative Damage Is Correlated to Altered Mitochondrial Function in Heterozygous Manganese Superoxide Dismutase Knockout Mice
Williams, M. D., Remmen, H. V., Conrad, C. C., Huang, T., Epstein, C. J., & Richardson, A. G. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.43.28510 · Cited by 454 · see citing works
Mice with a Homozygous Null Mutation for the Most Abundant Glutathione Peroxidase, Gpx1, Show Increased Susceptibility to the Oxidative Stress-inducing Agents Paraquat and Hydrogen Peroxide
de Haan, J. B., Bladier, C., Griffiths, P., Kelner, M. J., O’Shea, R. D., Cheung, N. S., Bronson, R. T., Silvestro, M. J., Wild, S., Zheng, S. S., et al. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.35.22528 · Cited by 450 · 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
The Absence of Mitochondrial Thioredoxin 2 Causes Massive Apoptosis, Exencephaly, and Early Embryonic Lethality in Homozygous Mice
Nonn, L., Williams, R. R., Erickson, R. P., & Powis, G. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.3.916-922.2003 · Cited by 438 · see citing works
Mitochondria, free radicals, and neurodegeneration
Beal, M. F. (1996) · Current Opinion in Neurobiology · doi:10.1016/s0959-4388(96)80100-0 · Cited by 422 · see citing works
Mice Lacking Catalase Develop Normally but Show Differential Sensitivity to Oxidant Tissue Injury
Ho, Y.-S., Xiong, Y., Ma, W., Spector, A., & Ho, D. S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404800200 · Cited by 403 · see citing works
Characterization of three isoforms of mammalian peroxiredoxin that reduce peroxides in the presence of thioredoxin
Chae, H. Z., Kim, H. J., Kang, S. W., & Rhee, S. G. (1999) · Diabetes Research and Clinical Practice · doi:10.1016/s0168-8227(99)00037-6 · Cited by 390 · see citing works
The Utility of Superoxide Dismutase in Studying Free Radical Reactions
McCord, J. M., & Fridovich, I. (1970) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)63246-6 · Cited by 389 · see citing works
Superoxide Activates Mitochondrial Uncoupling Protein 2 from the Matrix Side
Echtay, K. S., Murphy, M. P., Smith, R. A. J., Talbot, D. A., & Brand, M. D. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m208262200 · Cited by 388 · see citing works
The random collision model and a critical assessment of diffusion and collision in mitochondrial electron transport
Hackenbrock, C. R., Chazotte, B., & Gupte, S. S. (1986) · Journal of Bioenergetics and Biomembranes · doi:10.1007/bf00743010 · Cited by 384 · see citing works
Permeation of the erythrocyte stroma by superoxide radical
Lynch, R. E., & Fridovich, I. (1978) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)30446-5 · Cited by 370 · see citing works
Advances in our understanding of peroxiredoxin, a multifunctional, mammalian redox protein
Fujii, J., & Ikeda, Y. (2002) · Redox Report · doi:10.1179/135100002125000352 · Cited by 369 · see citing works
Physiological roles of nicotinamide nucleotide transhydrogenase
Hoek, J. B., & Rydström, J. (1988) · Biochemical Journal · doi:10.1042/bj2540001 · Cited by 362 · see citing works
Mitochondria in Neurodegeneration: Acute Ischemia and Chronic Neurodegenerative Diseases
Fiskum, G. M., Murphy, A. N., & Beal, M. F. (1999) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1097/00004647-199904000-00001 · Cited by 351 · see citing works
Mitochondrial Participation in Ischemic and Traumatic Neural Cell Death
Fiskum, G. M. (2000) · Journal of Neurotrauma · doi:10.1089/neu.2000.17.843 · Cited by 348 · see citing works
Phospholipid hydroperoxide glutathione peroxidase.
Ursini, F., Maiorino, M., & Gregolin, C. S. (1986) · PubMed · Cited by 338 · see citing works
NAD(P)H, a directly operating antioxidant?
Kirsch, M., & de GROOT, H. (2001) · The FASEB Journal · doi:10.1096/fj.00-0823hyp · Cited by 331 · see citing works
Human Mitochondrial Glutaredoxin Reduces S-Glutathionylated Proteins with High Affinity Accepting Electrons from Either Glutathione or Thioredoxin Reductase
Johansson, C., Lillig, C. H., & Holmgren, A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312719200 · Cited by 320 · see citing works
Mitochondrial Aconitase Is a Source of Hydroxyl Radical
Vasquez-Vivar, J. M., Kalyanaraman, B., & Kennedy, M. C. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.19.14064 · Cited by 317 · see citing works
Superoxide anion permeability of phospholipid membranes and chloroplast thylakoids
Takahashi, M., & Asada, K. (1983) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(83)90325-9 · Cited by 309 · see citing works
NADH- and NADPH-dependent formation of superoxide anions by bovine heart submitochondrial particles and NADH–ubiquinone reductase preparation
Takeshige, K., & Minakami, S. (1979) · Biochemical Journal · doi:10.1042/bj1800129 · Cited by 299 · see citing works
Superoxide and hydrogen peroxide production by Drosophila mitochondria
Miwa, S., St‐Pierre, J., Partridge, L., & Brand, M. D. (2003) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(03)00464-7 · Cited by 298 · see citing works
The site of production of superoxide radical in mitochondrial Complex I is not a bound ubisemiquinone but presumably iron–sulfur cluster N2
Genova, M. L., Ventura, B., Giuliano, G., Bovina, C., Formiggini, G., Castelli, G. P., & Lenaz, G. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)02850-2 · Cited by 297 · see citing works
Mitochondrial Phospholipid Hydroperoxide Glutathione Peroxidase Plays a Major Role in Preventing Oxidative Injury to Cells
Arai, M., Imai, H., Koumura, T., Yoshida, M., Emoto, K., Umeda, M., Chiba, N., & Nakagawa, Y. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.8.4924 · Cited by 297 · see citing works
Aconitase: Sensitive target and measure of superoxide
Gardner, P. R. (2002) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(02)49317-2 · Cited by 295 · see citing works
Mitochondria in Neurodegeneration: Bioenergetic Function in Cell Life and Death
Murphy, A. N., Fiskum, G. M., & Beal, M. F. (1999) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1097/00004647-199903000-00001 · Cited by 288 · see citing works
High-affinity transport of glutathione is part of a multicomponent system essential for mitochondrial function.
Mårtensson, J., Lai, J. C. K., & Meister, A. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.18.7185 · Cited by 282 · see citing works
The Contribution of Mitochondrial Respiratory Complexes to the Production of Reactive Oxygen Species
McLennan, H. R., & Esposti, M. D. (2000) · Journal of Bioenergetics and Biomembranes · doi:10.1023/a:1005507913372 · Cited by 264 · see citing works
Generation of Superoxide Anion by Succinate-Cytochromec Reductase from Bovine Heart Mitochondria
Zhang, L., Yu, L. P. C., & Yu, C. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.51.33972 · Cited by 253 · see citing works
Opening of the mitochondrial permeability transition pore by uncoupling or inorganic phosphate in the presence of Ca2+ is dependent on mitochondrial‐generated reactive oxygen species
Kowaltowski, A. J., Castilho, R. F., & Vercesi, A. E. (1996) · FEBS Letters · doi:10.1016/0014-5793(95)01449-7 · Cited by 249 · see citing works
Superoxide radicals and hydrogen peroxide formation in mitochondria from normal and neoplastic tissues
Dionisi, O., Galeotti, T., Terranova, T., & Azzi, A. (1975) · Biochimica et Biophysica Acta (BBA) - Enzymology · doi:10.1016/0005-2744(75)90059-5 · Cited by 247 · see citing works
Effects of age and caloric restriction on glutathione redox state in mice
Rebrin, I., Kamzalov, S., & Sohal, R. S. (2003) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(03)00388-5 · Cited by 243 · see citing works
Redox-Dependent Modulation of Aconitase Activity in Intact Mitochondria
Bulteau, A.-L., Ikeda-Saito, M., & Szweda, L. I. (2003) · Biochemistry · doi:10.1021/bi0353979 · Cited by 241 · see citing works
Substrate and Site Specificity of Hydrogen Peroxide Generation in Mouse Mitochondria
Kwong, L. K., & Sohal, R. S. (1998) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1997.0489 · Cited by 236 · see citing works
Membrane Bioenergetics
Skulachev, V. P. (1988) · Springer eBooks · doi:10.1007/978-3-642-72978-2 · Cited by 235 · see citing works
Knockout mice heterozygous forSod2show alterations in cardiac mitochondrial function and apoptosis
Remmen, H. V., Williams, M. D., Guo, Z., Estlack, L. E., Yang, H. C., Carlson, E. J., Epstein, C. J., Huang, T., & Richardson, A. G. (2001) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.2001.281.3.h1422 · Cited by 230 · see citing works
Mitochondrial oxidative stress in mice lacking the glutathione peroxidase-1 gene
Esposito, L. A., Kokoszka, J. E., Waymire, K. G., Cottrell, B., MacGregor, G. R., & Wallace, D. C. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00161-1 · Cited by 228 · see citing works
Regulation of hydrogen peroxide production by brain mitochondria by calcium and Bax
Starkov, A. A., Polster, B. M., & Fiskum, G. M. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.01153.x · Cited by 225 · see citing works
Self-citation
Superoxides from mitochondrial complex III: the role of manganese superoxide dismutase
Raha, S., McEachern, G. E., Myint, A. T., & Robinson, B. H. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00338-5 · Cited by 223 · see citing works
The Metabolism of Tyramine by Monoamine Oxidase A/B Causes Oxidative Damage to Mitochondrial DNA
Hauptmann, N., Grimsby, J. S., Shih, J. C., & Cadenas, E. (1996) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1996.0510 · Cited by 221 · see citing works
Cellular Glutathione Peroxidase Is the Mediator of Body Selenium To Protect against Paraquat Lethality in Transgenic Mice
Cheng, W., Ho, Y., Valentine, B. A., Ross, D. A., Combs, G. F., & Lei, X. G. (1998) · Journal of Nutrition · doi:10.1093/jn/128.7.1070 · Cited by 212 · see citing works
Effect of Glutathione Depletion on Sites and Topology of Superoxide and Hydrogen Peroxide Production in Mitochondria
Han, D., Canali, R., Rettori, D., & Kaplowitz, N. (2003) · Molecular Pharmacology · doi:10.1124/mol.64.5.1136 · Cited by 212 · see citing works
Partial Resolution of the Enzymes Catalyzing Oxidative Phosphorylation
Hinkle, P. C., Butow, R. A., Racker, E., & Chance, B. (1967) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)99410-x · Cited by 195 · see citing works
Rat Phospholipid-hydroperoxide Glutathione Peroxidase
Thimmalapura, P., Burdsall, A., Oleksa, L. M., Chisolm, G. M., & Driscoll, D. M. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.45.26993 · Cited by 195 · see citing works
Hepatic mitochondrial and cytosolic glutathione content and the subcellular distribution of GSH‐S‐transferases
Wahlländer, A., Soboll, S., Sies, H., Linke, I. M., & Monika, M. (1979) · FEBS Letters · doi:10.1016/0014-5793(79)80069-1 · Cited by 189 · see citing works
Ca(2+)-induced mitochondrial membrane permeabilization: role of coenzyme Q redox state
Kowaltowski, A. J., Castilho, R. F., & Vercesi, A. E. (1995) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1995.269.1.c141 · Cited by 189 · see citing works
The Thiol-specific Antioxidant Enzyme Prevents Mitochondrial Permeability Transition
Kowaltowski, A. J., Netto, L. E. S., & Vercesi, A. E. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.21.12766 · Cited by 176 · see citing works
Retention of oxidized glutathione by isolated rat liver mitochondria during hydroperoxide treatment
Ólafsdóttir, K. B., & Reed, D. J. (1988) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(88)90038-4 · Cited by 169 · see citing works
Quantitative relationship between inhibition of respiratory complexes and formation of reactive oxygen species in isolated nerve terminals
Sipos, I., Tretter, L., & Ádám‐Vizi, V. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01513.x · Cited by 167 · see citing works
Multiple isoforms of mitochondrial glutathione S-transferases and their differential induction under oxidative stress
Raza, H., Robin, M., Fang, J.-K., & Avadhani, N. G. (2002) · Biochemical Journal · doi:10.1042/bj20020533 · Cited by 167 · see citing works
TheGpx1Gene Encodes Mitochondrial Glutathione Peroxidase in the Mouse Liver
Esworthy, R. S., Ho, Y., & Chu, F. (1997) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1997.9901 · Cited by 165 · see citing works
Oxidative stress in Ca2+‐induced membrane permeability transition in brain mitochondria
Maciel, E. N., Vercesi, A. E., & Castilho, R. F. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00670.x · Cited by 162 · see citing works
Relative contributions of heart mitochondria glutathione peroxidase and catalase to H2O2 detoxification in in vivo conditions
Antunes, F., Han, D., & Cadenas, E. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)01016-x · Cited by 161 · see citing works
Effect of electron transfer inhibitors on superoxide generation in the cytochrome bc1 site of the mitochondrial respiratory chain
Ksenzenko, M. Y., Konstantinov, A. A., Khomutov, G. B., Tikhonov, A. N., & Ruuge, E. K. (1983) · FEBS Letters · doi:10.1016/0014-5793(83)80200-2 · Cited by 160 · see citing works
Evidence for Mitochondrial Uptake of Glutathione by Dicarboxylate and 2-Oxoglutarate Carriers
Chen, Z., & Lash, L. H. (1998) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1016/s0022-3565(24)37484-1 · Cited by 160 · see citing works
Cellular Glutathione Peroxidase Knockout Mice Express Normal Levels of Selenium-Dependent Plasma and Phospholipid Hydroperoxide Glutathione Peroxidases in Various Tissues , ,
Cheng, W., Ho, Y., Ross, D. A., Valentine, B. A., Combs, G. F., & Lei, X. G. (1997) · Journal of Nutrition · doi:10.1093/jn/127.8.1445 · Cited by 159 · see citing works
Mechanism of Ubiquinol Oxidation by the bc1 Complex: Different Domains of the Quinol Binding Pocket and Their Role in the Mechanism and Binding of Inhibitors
Crofts, A. R., Barquera, B., Gennis, R. B., Kuras, R., Guergova-Kuras, M., & Berry, E. A. (1999) · Biochemistry · doi:10.1021/bi990962m · Cited by 158 · see citing works
ATP-dependent Regulation of Sodium-Calcium Exchange in Chinese Hamster Ovary Cells Transfected with the Bovine Cardiac Sodium-Calcium Exchanger
Condrescu, M., Gardner, J. P., Chernaya, G., Aceto, J. F., Κroupis, C., & Reeves, J. P. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.16.9137 · Cited by 157 · see citing works
Age-dependent increase in hydrogen peroxide production by cardiac monoamine oxidase A in rats
Ribes, A. M., Hernandez, C., Kunduzova, O., Bompart, G., Cambon, C., Parini, A., & Francès, B. (2003) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00700.2002 · Cited by 153 · see citing works
Characterization of the Antioxidant Status of the Heterozygous Manganese Superoxide Dismutase Knockout Mouse
Remmen, H. V., Salvador, C., Yang, H. C., Huang, T., Epstein, C. J., & Richardson, A. G. (1999) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1998.1060 · Cited by 152 · 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
Localization of the Site of Oxygen Radical Generation inside the Complex I of Heart and Nonsynaptic Brain Mammalian Mitochondria
Herrero, A., & Barja, G. (2000) · Journal of Bioenergetics and Biomembranes · doi:10.1023/a:1005626712319 · Cited by 149 · see citing works
Mitochondrial Production of Oxygen Radical Species and the Role of Coenzyme Q as an Antioxidant
Genova, M. L., Pich, M. M., Biondi, A., Bernacchia, A., Falasca, A. I., Bovina, C., Formiggini, G., Castelli, G. P., & Lenaz, G. (2003) · Experimental Biology and Medicine · doi:10.1177/15353702-0322805-14 · Cited by 148 · see citing works
Effects of coenzyme Q10 and α-tocopherol administration on their tissue levels in the mouse: elevation of mitochondrial α-tocopherol by coenzyme Q10
Lass, A., Forster, M. J., & Sohal, R. S. (1999) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(98)00330-x · Cited by 148 · see citing works
Antimycin-insensitive oxidation of succinate and reduced nicotinamide-adenine dinucleotide in electron-transport particles I. pH dependency and hydrogen peroxide formation
Pk, J. (1966) · Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation · doi:10.1016/0926-6593(66)90057-9 · Cited by 147 · see citing works
The sites of superoxide anion generation in higher plant mitochondria
Rich, P. R., & Bonner, W. D. (1978) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(78)90373-9 · Cited by 146 · see citing works
Mitochondrial Thioredoxin System
Patenaude, A., Murthy, M. R. V., & Mirault, M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m402496200 · Cited by 140 · see citing works
Inactivation of the 2‐oxo acid dehydrogenase complexes upon generation of intrinsic radical species
Bunik, V. I., & Sievers, C. (2002) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2002.03204.x · Cited by 134 · see citing works
Myxothiazol Induces H2O2 Production from Mitochondrial Respiratory Chain
Starkov, A. A., & Fiskum, G. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.4409 · Cited by 133 · see citing works
Self-citation
Mitochondrial peroxiredoxin‐3 protects hippocampal neurons from excitotoxic injury in vivo
Hattori, F., Murayama, N., Noshita, T., & Oikawa, S. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01918.x · Cited by 132 · see citing works
Respiration-dependent Removal of Exogenous H2O2 in Brain Mitochondria
Zoccarato, F., Cavallini, L., & Alexandre, A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m308143200 · Cited by 130 · see citing works
Studies on the electron transfer pathway, topography of iron-sulfur centers, and site of coupling in NADH-Q oxidoreductase.
Krishnamoorthy, G., & Hinkle, P. C. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)77873-9 · Cited by 130 · see citing works
Antioxidant Function of the Mitochondrial Protein SP-22 in the Cardiovascular System
Araki, M., Nanri, H., 江島, 邦., Murasato, Y., Fujiwara, T., Nakashima, Y., & Ikeda, M. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.4.2271 · Cited by 128 · see citing works
In VitroIschemia Promotes Glutamate-Mediated Free Radical Generation and Intracellular Calcium Accumulation in Hippocampal Pyramidal Neurons
Velázquez, J. L. P., Frantseva, M. V., & Carlen, P. L. (1997) · Journal of Neuroscience · doi:10.1523/jneurosci.17-23-09085.1997 · Cited by 125 · see citing works
H2O2 detection from intact mitochondria as a measure for one-electron reduction of dioxygen requires a non-invasive assay system11Dedicated to Prof. E. Elstner, on the occasion of his 60th anniversary.
Staniek, K., & Nohl, H. (1999) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(99)00083-3 · Cited by 124 · see citing works
Oxidative α-Ketoglutarate Dehydrogenase Inhibition via Subtle Elevations in Monoamine Oxidase B Levels Results in Loss of Spare Respiratory Capacity
Kumar, M. J., Nicholls, D. G., & Andersen, J. K. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306378200 · Cited by 120 · see citing works
“Mild” Uncoupling of Mitochondria
Starkov, A. A. (1997) · Bioscience Reports · doi:10.1023/a:1027380527769 · Cited by 119 · see citing works
Self-citation
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
Superoxide production and electron transport in mitochondrial oxidation of dihydroorotic acid
Forman, H. J., & Kennedy, J. (1975) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)41421-x · Cited by 115 · see citing works
The regeneration of reduced glutathione in rat forebrain mitochondria identifies metabolic pathways providing the NADPH required
Vogel, R., Wiesinger, H., Hamprecht, B., & Dringen, R. (1999) · Neuroscience Letters · doi:10.1016/s0304-3940(99)00748-x · Cited by 115 · see citing works
Mitochondria and Dopamine
Shen, J., & Cookson, M. (2004) · Neuron · doi:10.1016/j.neuron.2004.07.012 · Cited by 114 · see citing works
Enhanced N-Methyl-4-Phenyl-1,2,3,6-Tetrahydropyridine Toxicity in Mice Deficient in CuZn-Superoxide Dismutase or Glutathione Peroxidase
Zhang, J., Graham, D. G., Montine, T. J., & Ho, Y.-S. (2000) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/59.1.53 · Cited by 114 · see citing works
Overexpression of human peroxiredoxin 5 in subcellular compartments of chinese hamster ovary cells: effects on cytotoxicity and DNA damage caused by peroxides
Banmeyer, I., Marchand, C., Verhaeghe, C., Vucic, B., Rees, J., & Knoops, B. (2003) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2003.10.019 · Cited by 113 · see citing works
Regulation of adenine nucleotide translocase and glycerol 3-phosphate dehydrogenase expression by thyroid hormones in different rat tissues
DÜMMLER, K., Müller, S. P., & SEITZ, H. J. (1996) · Biochemical Journal · doi:10.1042/bj3170913 · Cited by 112 · see citing works
Permeability of bilayer lipid membranes for superoxide (O2−) radicals
Gus'kova, R. A., Ivanov, I. I., Koltover, V. K., Akhobadze, V. V., & Rubin, A. (1984) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(84)90409-7 · Cited by 112 · see citing works
On the Mechanism of Quinol Oxidation in thebc1 Complex
Jünemann, S., Heathcote, P., & Rich, P. R. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.34.21603 · Cited by 108 · see citing works
Hydrogen Peroxide Production by Monoamine Oxidase during Ischemia-Reperfusion in the Rat Brain
Simonson, S. G., Zhang, J., Canada, A. T., Su, Y.-F., Benveniste, H., & Piantadosi, C. A. (1993) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.1993.15 · Cited by 107 · see citing works
Mitochondrial involvement in schizophrenia and other functional psychoses
Whatley, S. A., Curti, D., & Marchbanks, R. M. (1996) · Neurochemical Research · doi:10.1007/bf02532409 · Cited by 103 · see citing works
Superoxide generation by the respiratory chain of tumor mitochondria
Konstantinov, A. A., Peskin, A. V., Popova, E. Y., Khomutov, G. B., & Ruuge, E. K. (1987) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(87)90206-4 · Cited by 103 · see citing works
Cloning of bovine peroxiredoxins—gene expression in bovine tissues and amino acid sequence comparison with rat, mouse and primate peroxiredoxins
Leyens, G., Donnay, I., & Knoops, B. (2003) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/s1096-4959(03)00290-2 · Cited by 98 · see citing works
Dihydroorotate-dependent superoxide producton in rat brain and liver
Forman, H. J., & Kennedy, J. (1976) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(76)90252-6 · Cited by 95 · see citing works
Reactivity of Phospholipid Hydroperoxide Glutathione Peroxidase with Membrane and Lipoprotein Lipid Hydroperoxides
Maiorino, M., Thomas, J. P., Girotti, A. W., & Ursini, F. (1991) · Free Radical Research Communications · doi:10.3109/10715769109145777 · Cited by 94 · see citing works
Ca2+-Stimulated Mitochondrial Reactive Oxygen Species Generation and Permeability Transition Are Inhibited by Dibucaine or Mg2+
Kowaltowski, A. J., Naia-da-Silva, E. S., Castilho, R. F., & Vercesi, A. E. (1998) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1998.0870 · Cited by 92 · see citing works
Superoxide, neuroleptics and the ubiquinone and cytochrome b5 reductases in brain and lymphocytes from normals and schizophrenic patients
Whatley, S. A., Curti, D., Gupta, F. D., Ferrier, I. N., Jones, S., Taylor, C., & Marchbanks, R. M. (1998) · Molecular Psychiatry · doi:10.1038/sj.mp.4000375 · Cited by 92 · see citing works
The effects of focal ischemia and reperfusion on the glutathione content of mitochondria from rat brain subregions
Anderson, M. F., & Sims, N. R. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.00836.x · Cited by 84 · see citing works
Relation of superoxide generation and lipid peroxidation to the inhibition of NADH-Q oxidoraductase by rotenone, piericidin A, and MPP+
Ramsay, R. R., & Singer, T. P. (1992) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(92)91523-s · Cited by 79 · see citing works
Susceptibility of Heterozygous MnSOD Gene-Knockout Mice to Oxygen Toxicity
Tsan, M., White, J. E., Caska, B. A., et al. (1998) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/ajrcmb.19.1.3066 · Cited by 78 · see citing works
Sequence and tissue-dependent RNA expression of mouse FAD-linked glycerol-3-phosphate dehydrogenase
Koza, R. A., Kozak, U. C., Brown, L. J., Leiter, E. H., Macdonald, M. J., & Kozak, L. P. (1996) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1996.0536 · Cited by 76 · see citing works
Strain-dependent high-level expression of a transgene for manganese superoxide dismutase is associated with growth retardation and decreased fertility
Raineri, I., Carlson, E. J., Gacayan, R., Carra, S., Oberley, T. D., Huang, T.-T., & Epstein, C. J. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(01)00686-4 · Cited by 73 · see citing works
Distribution of glutathione peroxidases glutathione reductase in rat brain mitochondria
Panfili, E., Sandri, G., & Ernster, L. (1991) · FEBS Letters · doi:10.1016/0014-5793(91)81219-x · Cited by 72 · see citing works
Electron spin resonance study on the permeability of superoxide radicals in lipid bilayers and biological membranes
Mao, G. D., & Poznansky, M. J. (1992) · FEBS Letters · doi:10.1016/0014-5793(92)80675-7 · Cited by 70 · see citing works
Structural Organization of the Human Glutathione Reductase Gene: Determination of Correct cDNA Sequence and Identification of a Mitochondrial Leader Sequence
Kelner, M. J., & Montoya, M. A. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.2267 · Cited by 67 · see citing works
Variation in Cellular Glutathione Peroxidase Activity in Lens Epithelial Cells, Transgenics and Knockouts Does Not Significantly Change the Response to H2O2Stress
Spector, A., Yang, Y., Ho, Y., Magnenat, J.-L., Wang, R.-R., Ma, W., & Li, W. (1996) · Experimental Eye Research · doi:10.1006/exer.1996.0063 · Cited by 66 · see citing works
Reduction of thymine hydroperoxide by phospholipid hydroperoxide glutathione peroxidase and glutathione transferases
Bao, Y., Jemth, P., Mannervik, B., & Williamson, G. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00591-7 · Cited by 62 · see citing works
Murine phospholipid hydroperoxide glutathione peroxidase: cDNA sequence, tissue expression, and mapping
Knopp, E. A., Arndt, T. L., Eng, K., Caldwell, M., LeBoeuf, R. C., Deeb, S. S., & O’Brien, K. D. (1999) · Mammalian Genome · doi:10.1007/s003359901053 · Cited by 61 · see citing works
Hydrogen peroxide production by monoamine oxidase during ischemia/reperfusion
Kunduzova, O., Bianchi, P., Parini, A., & Cambon, C. (2002) · European Journal of Pharmacology · doi:10.1016/s0014-2999(02)01913-1 · Cited by 60 · see citing works
Purification and immunoelectron microscopic localization of cellular glutathione peroxidase in rat hepatocytes: quantitative analysis by postembedding method
Asayama, K., Dobashi, K., Hayashibe, H., Nakazawa, S., Yokota, S., & Kawaoi, A. (1994) · Histochemistry and Cell Biology · doi:10.1007/bf00268898 · Cited by 57 · see citing works
Superoxide radical as electron donor for oxidative phosphorylation of ADP
Mailer, K. (1990) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(90)91240-s · Cited by 55 · see citing works
Catalytic enzyme histochemistry and biochemical analysis of dihydroorotate dehydrogenase/oxidase and succinate dehydrogenase in mammalian tissues, cells and mitochondria
Löffler, M., Becker, C., Wegerle, E., & Schuster, G. U. (1996) · Histochemistry and Cell Biology · doi:10.1007/bf01696151 · Cited by 49 · see citing works
Localization of the α‐oxoacid dehydrogenase multienzyme complexes within the mitochondrion
Maas, E., & Bisswanger, H. (1990) · FEBS Letters · doi:10.1016/0014-5793(90)80840-f · Cited by 45 · see citing works
Pathways of hydrogen peroxide generation in guinea pig cerebral cortex mitochondria
Zoccarato, F., Cavallini, L., Deana, R., & Alexandre, A. (1988) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(88)90200-8 · Cited by 43 · see citing works
Exact ultrastructural localization of glutathione peroxidase in normal rat hepatocytes: advantages of microwave fixation.
Utsunomiya, H., Komatsu, N., Yoshimura, S., et al. (1991) · Journal of Histochemistry & Cytochemistry · doi:10.1177/39.9.1918936 · Cited by 42 · see citing works
Calcium- and phosphate-dependent release and loading of glutathione by liver mitochondria
Savage, M. K., Jones, D. P., & Reed, D. J. (1991) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(91)90590-f · Cited by 40 · see citing works
Subcellular Distribution of OM Cytochrome b-Mediated NADH-Semidehydroascorbate Reductase Activity in Rat Liver
Nishino, H., & Ito, A. (1986) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a121859 · Cited by 36 · see citing works
Effect of ammonia on mitochondrial and cytosolic NADH and NADPH systems in isolated rat liver cells
Tischler, M. E., Hecht, P., & WILLIAMSON, J. R. (1977) · FEBS Letters · doi:10.1016/0014-5793(77)80129-4 · Cited by 33 · see citing works
Kinetic of Superoxide Formation by Respiratory Chain NADH-Dehydrogenase of Bovine Heart Mitochondria
Kang, D., Narabayashi, H., Sata, T., et al. (1983) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a134475 · Cited by 32 · see citing works
Can superoxide organic chemistry be observed within the liposomal bilayer?
Frimer, A. A., Strul, G., Hameiri-Buch, J., & Gottlieb, H. E. (1996) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(95)02148-5 · Cited by 30 · see citing works
Relationships between the effects of redox potential, α‐Thenoyltrifluoroacetone and malonate on O2− and H2O2 generation by submitochondrial particles in the presence of succinate and antimycin
Ksenzenko, M. Y., Konstantinov, A. A., Khomutov, G. B., Tikhonov, A. N., & Ruuge, E. K. (1984) · FEBS Letters · doi:10.1016/0014-5793(84)80579-7 · Cited by 25 · see citing works
SURVIVAL, LUNG INJURY, AND LUNG PROTEIN NITRATION IN HETEROZYGOUS MnSOD KNOCKOUT MICE IN HYPEROXIA
Jackson, R. M. (1999) · Experimental Lung Research · doi:10.1080/019021499270060 · Cited by 22 · see citing works
Hydrogen peroxide production in mouse tissues after acute d -amphetamine administration. Influence of monoamine oxidase inhibition
Carvalho, F. D., Duarte, J. A., Neuparth, M. J., et al. (2001) · Archives of Toxicology · doi:10.1007/s002040100264 · Cited by 20 · see citing works
Mechanism accounting for the induction of nonspecific permeability of the inner mitochondrial membrane by hydroperoxides
Novgorodov, S. A., Gudz, T. I., Kushnareva, Y. E., et al. (1991) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(05)80243-9 · Cited by 19 · see citing works
Self-citation
Complete inhibition of dihydro-orotate oxidation and superoxide production by 1,1,1-trifluoro-3-thenoylacetone in rat liver mitochondria
Dileepan, K. N., & Kennedy, J. (1985) · Biochemical Journal · doi:10.1042/bj2250189 · Cited by 17 · see citing works
NAD(P)+ decomposition and antioxidant defense of the cell
Skulachev, V. P. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)02197-4 · Cited by 6 · see citing works

Flagged first, then by citations

Sorted by citations

How mitochondria produce reactive oxygen species
Murphy, M. P. (2009) · Biochemical Journal · doi:10.1042/bj20081386 · Cited by 8,207 · see citing works
Mitochondrial Dysfunction and Oxidative Stress in Neurodegenerative Diseases
Lin, M. T., & Beal, M. F. (2006) · Nature · doi:10.1038/nature05292 · Cited by 6,455 · see citing works
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
Reactive oxygen species, cellular redox systems, and apoptosis
Circu, M. L., & Aw, T. Y. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.12.022 · Cited by 3,340 · see citing works
Lifestyle, oxidative stress, and antioxidants: Back and forth in the pathophysiology of chronic diseases
Sharifi-Rad, M., Anil Kumar, N. V., Zucca, P., Varoni, E. M., Dini, L., Panzarini, E., Rajkovic, J., Tsouh Fokou, P. V., Azzini, E., Peluso, I., et al. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.00694 · Cited by 1,971 · see citing works
Mitochondrial dysfunction and oxidative stress in metabolic disorders - A step towards mitochondria based therapeutic strategies
Bhatti, J. S., Bhatti, G. K., & Reddy, P. H. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2016.11.010 · Cited by 1,655 · see citing works
The sites and topology of mitochondrial superoxide production
Brand, M. D. (2010) · Experimental Gerontology · doi:10.1016/j.exger.2010.01.003 · Cited by 1,217 · see citing works
Nrf2 and Oxidative Stress: A General Overview of Mechanisms and Implications in Human Disease
Ngo, V., & Duennwald, M. L. (2022) · Antioxidants · doi:10.3390/antiox11122345 · Cited by 1,130 · see citing works
Mitochondrial generation of superoxide and hydrogen peroxide as the source of mitochondrial redox signaling
Brand, M. D. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.04.001 · Cited by 1,063 · see citing works
Role of oxidative stress in Alzheimer’s disease
HUANG, W.-J., ZHANG, X., & CHEN, W.-W. (2016) · Biomedical Reports · doi:10.3892/br.2016.630 · Cited by 1,023 · see citing works
Role of oxidative stress in the pathogenesis of nonalcoholic steatohepatitis
Rolo, A. P., Teodoro, J. S., & Palmeira, C. M. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.10.003 · Cited by 955 · see citing works
Oxidative Stress in Human Pathology and Aging: Molecular Mechanisms and Perspectives
Hajam, Y. A., Rani, R., Ganie, S. Y., Sheikh, T. A., Javaid, D., Qadri, S. S., Pramodh, S., Alsulimani, A., Alkhanani, M. F., Harakeh, S., et al. (2022) · Cells · doi:10.3390/cells11030552 · Cited by 915 · see citing works
The role of mitochondria in reactive oxygen species metabolism and signaling
Starkov, A. A. (2008) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1427.015 · Cited by 846 · see citing works
Self-citation
Necrosis, a well-orchestrated form of cell demise: Signalling cascades, important mediators and concomitant immune response
Festjens, N., Vanden Berghe, T., & Vandenabeele, P. (2006) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2006.06.014 · Cited by 710 · see citing works
Mitochondrial dysfunction in Parkinson's disease
Winklhofer, K. F., & Haass, C. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.08.013 · Cited by 688 · see citing works
Ageing, age-related diseases and oxidative stress: What to do next?
Luo, J., Mills, K., le Cessie, S., Noordam, R., & van Heemst, D. (2020) · Ageing Research Reviews · doi:10.1016/j.arr.2019.100982 · Cited by 581 · see citing works
Iron behaving badly: inappropriate iron chelation as a major contributor to the aetiology of vascular and other progressive inflammatory and degenerative diseases
Kell, D. B. (2009) · BMC Medical Genomics · doi:10.1186/1755-8794-2-2 · Cited by 554 · see citing works
Mitochondrial reactive oxygen species production in excitable cells: Modulators of mitochondrial and cell function
Stowe, D. F., & Camara, A. K. S. (2009) · Antioxidants & Redox Signaling · doi:10.1089/ars.2008.2331 · Cited by 471 · see citing works
Mitochondrial changes within axons in multiple sclerosis
Mahad, D. J., Ziabreva, I., Campbell, G., Lax, N., White, K., Hanson, P. S., Lassmann, H., & Turnbull, D. M. (2009) · Brain · doi:10.1093/brain/awp046 · Cited by 454 · see citing works
Generation of superoxide by the mitochondrial Complex I
Grivennikova, V. G., & Vinogradov, A. D. (2006) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2006.03.013 · Cited by 379 · see citing works
Endothelial Mitochondria: Contributing to Vascular Function and Disease
Davidson, S. M., & Duchen, M. R. (2007) · Circulation Research · doi:10.1161/01.res.0000261970.18328.1d · Cited by 381 · see citing works
Denervation-Induced Skeletal Muscle Atrophy Is Associated with Increased Mitochondrial Ros Production
Muller, F. L., Song, W., Jang, Y. C., Liu, Y., Sabia, M., Richardson, A., & Van Remmen, H. (2007) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00767.2006 · Cited by 355 · see citing works
Manganese Superoxide Dismutase: Guardian of the Powerhouse
Holley, A. K., Bakthavatchalu, V., Velez-Roman, J. M., & St. Clair, D. K. (2011) · International Journal of Molecular Sciences · doi:10.3390/ijms12107114 · Cited by 358 · see citing works
Obesity-related derangements in metabolic regulation
Muoio, D. M., & Newgard, C. B. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.103004.142512 · Cited by 345 · see citing works
Mitochondria-targeted peptide antioxidants: Novel neuroprotective agents
Szeto, H. H. (2006) · The AAPS Journal · doi:10.1208/aapsj080362 · Cited by 332 · see citing works
Sites of superoxide and hydrogen peroxide production by muscle mitochondria assessed ex vivo under conditions mimicking rest and exercise
Goncalves, R. L. S., Quinlan, C. L., Perevoshchikova, I. V., Hey-Mogensen, M., & Brand, M. D. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.619072 · Cited by 329 · see citing works
Mitochondrion-derived reactive oxygen species lead to enhanced amyloid beta formation
Leuner, K., Schütt, T., Kurz, C., Eckert, S. H., Schiller, C., Occhipinti, A., Mai, S., Jendrach, M., Eckert, G. P., Kruse, S. E., et al. (2012) · Antioxidants & Redox Signaling · doi:10.1089/ars.2011.4173 · Cited by 354 · see citing works
The 2-oxoacid dehydrogenase complexes in mitochondria can produce superoxide/hydrogen peroxide at much higher rates than complex I
Quinlan, C. L., Goncalves, R. L. S., Hey-Mogensen, M., Yadava, N., Bunik, V. I., & Brand, M. D. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.545301 · Cited by 310 · see citing works
Antioxidant Protective Mechanisms against Reactive Oxygen Species (ROS) Generated by Mitochondrial P450 Systems in Steroidogenic Cells
Hanukoglu, I. (2006) · Drug Metabolism Reviews · doi:10.1080/03602530600570040 · Cited by 293 · see citing works
Redox interplay between mitochondria and peroxisomes
Lismont, C., Nordgren, M., Van Veldhoven, P. P., & Fransen, M. (2015) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2015.00035 · Cited by 214 · see citing works
Involvement of NOX2 in the Development of Behavioral and Pathologic Alterations in Isolated Rats
Schiavone, S., Sorce, S., Dubois-Dauphin, M., Jaquet, V., Colaianna, M., Zotti, M., Cuomo, V., Trabace, L., & Krause, K.-H. (2009) · Biological Psychiatry · doi:10.1016/j.biopsych.2009.04.033 · Cited by 208 · see citing works
NADPH oxidase- and mitochondria-derived reactive oxygen species in proinflammatory microglial activation: A bipartisan affair?
Bordt, E. A., & Polster, B. M. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.07.033 · Cited by 202 · see citing works
Respiration-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
Glutathione/thioredoxin systems modulate mitochondrial H2O2 emission: An experimental-computational study
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 · see citing works
Review: Mitochondria and disease progression in multiple sclerosis
Mahad, D., Lassmann, H., & Turnbull, D. (2008) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.2008.00987.x · Cited by 193 · see citing works
Sex differences in Parkinson’s disease: Features on clinical symptoms, treatment outcome, sexual hormones and genetics
Jurado-Coronel, J. C., Cabezas, R., Ávila Rodríguez, M. F., Echeverria, V., García-Segura, L. M., & Barreto, G. E. (2018) · Frontiers in Neuroendocrinology · doi:10.1016/j.yfrne.2017.09.002 · Cited by 180 · see citing works
Hypoxia-inducible Factor-1 Activation in Nonhypoxic Conditions: The Essential Role of Mitochondrial-derived Reactive Oxygen Species
Patten, D. A., Lafleur, V. N., Robitaille, G. A., Chan, D. A., Giaccia, A. J., & Richard, D. E. (2010) · Molecular Biology of the Cell · doi:10.1091/mbc.e10-01-0025 · Cited by 171 · see citing works
Mitochondrial uncoupling and lifespan
Mookerjee, S. A., Divakaruni, A. S., Jastroch, M., & Brand, M. D. (2010) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2010.03.010 · Cited by 169 · see citing works
Lifestyle Modifications and Nutritional Interventions in Aging-Associated Cognitive Decline and Alzheimer's Disease
Bhatti, G. K., Reddy, A. P., Reddy, P. H., & Bhatti, J. S. (2020) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2019.00369 · Cited by 145 · see citing works
Oxidative and nitrosative stress pathways in the brain of socially isolated adult male rats demonstrating depressive- and anxiety-like symptoms
Filipović, D., Todorović, N., Bernardi, R. E., & Gass, P. (2017) · Brain Structure and Function · doi:10.1007/s00429-016-1218-9 · Cited by 138 · see citing works
Skeletal muscle adaptation to fatty acid depends on coordinated actions of the PPARs and PGC1α: implications for metabolic disease
Muoio, D. M., & Koves, T. R. (2007) · Applied Physiology, Nutrition, and Metabolism · doi:10.1139/h07-083 · Cited by 129 · see citing works
Manganese superoxide dismutase: Beyond life and death
Holley, A. K., Dhar, S. K., Xu, Y., & St. Clair, D. K. (2012) · Amino Acids · doi:10.1007/s00726-010-0600-9 · Cited by 122 · see citing works
Xanthine oxidase and mitochondria contribute to vascular superoxide anion generation in DOCA-salt hypertensive rats
Viel, E. C., Benkirane, K., Javeshghani, D., Touyz, R. M., & Schiffrin, E. L. (2008) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00304.2008 · Cited by 116 · see citing works
The role of mitochondria in aging of skeletal muscle
Figueiredo, P. A., Mota, M. P., Appell, H. J., & Duarte, J. A. (2008) · Biogerontology · doi:10.1007/s10522-007-9121-7 · Cited by 109 · see citing works
Development of Mitochondria‐targeted Aromatic‐cationic Peptides for Neurodegenerative Diseases
Szeto, H. H. (2008) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1427.013 · Cited by 100 · see citing works
Mitochondrial dysfunction as a central event for mechanisms underlying insulin resistance: The roles of long chain fatty acids
Hafizi Abu Bakar, M., Kian Kai, C., Wan Hassan, W. N., Sarmidi, M. R., Yaakob, H., & Zaman Huri, H. (2015) · Diabetes/Metabolism Research and Reviews · doi:10.1002/dmrr.2601 · Cited by 91 · see citing works
Ambivalent effects of diazoxide on mitochondrial ROS production at respiratory chain complexes I and III
Dröse, S., Hanley, P. J., & Brandt, U. (2009) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2009.01.011 · Cited by 72 · see citing works
Mitochondrial respiratory chain is involved in insulin-stimulated hydrogen peroxide production and plays an integral role in insulin receptor autophosphorylation in neurons
Storozhevykh, T. P., Senilova, Y. E., Persiyantseva, N. A., Pinelis, V. G., & Pomytkin, I. A. (2007) · BMC Neuroscience · doi:10.1186/1471-2202-8-84 · Cited by 69 · see citing works
The role of mitochondria in <scp>mTOR</scp>‐regulated longevity
Wei, Y., Zhang, Y., Cai, Y., & Xu, M. (2015) · Biological Reviews · doi:10.1111/brv.12103 · Cited by 56 · see citing works
Decoding the Rosetta stone of mitonuclear communication
English, J., Son, J. M., Cardamone, M. D., Lee, C., & Perissi, V. (2020) · Pharmacological Research · doi:10.1016/j.phrs.2020.105161 · Cited by 55 · see citing works
Overexpression of twinkle-helicase protects cardiomyocytes from genotoxic stress caused by reactive oxygen species
Pohjoismäki, J. L. O., Williams, S. L., Boettger, T., Goffart, S., Kim, J., Suomalainen, A., Moraes, C. T., & Braun, T. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1303046110 · Cited by 45 · see citing works
Mitochondria and Cellular Redox State on the Route from Ageing to Alzheimer's Disease
Abate, G., Vezzoli, M., Sandri, M., Rungratanawanich, W., Memo, M., & Uberti, D. (2020) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2020.111385 · Cited by 41 · see citing works
The emerging neuroprotective role of mitochondrial uncoupling protein-2 in traumatic brain injury
Normoyle, K. P., Kim, M., Farahvar, A., Llano, D., Jackson, K., & Wang, H. (2015) · Translational Neuroscience · doi:10.1515/tnsci-2015-0019 · Cited by 36 · see citing works
Integrated Single‐Cell RNA‐seq and ATAC‐seq Reveals Heterogeneous Differentiation of CD4 + Naive T Cell Subsets is Associated with Response to Antidepressant Treatment in Major Depressive Disorder
Sun, Z., Zhang, B., Zhou, J., Luo, Y., Zhu, X., Wang, Y., He, Y., Zheng, P., Zhang, L., Yang, J., et al. (2024) · Advanced Science · doi:10.1002/advs.202308393 · Cited by 20 · see citing works

Reactive Oxygen Species and Oxidative Stress in Obesity—Recent Findings and Empirical Approaches
McMurray, F., Patten, D. A., & Harper, M. (2016) · Obesity · doi:10.1002/oby.21654 · Cited by 245 · see citing works
The role of mitochondria in reactive oxygen species metabolism and signaling
Starkov, A. A. (2008) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1427.015 · Cited by 846 · see citing works
Self-citation
Gold-induced reactive oxygen species (ROS) do not mediate suppression of monocytic mitochondrial or secretory function
Omata, Y., Lewis, J. B., Lockwood, P. E., Tseng, W., Messer, R. L. W., Bouillaguet, S., & Wataha, J. C. (2005) · Toxicology in Vitro · doi:10.1016/j.tiv.2005.11.001 · Cited by 14 · see citing works
Autophagy is required during cycling hypoxia to lower production of reactive oxygen species
Rouschop, K. M. A., Ramaekers, C. H. M. A., Schaaf, M. B. E., Keulers, T. G., Savelkouls, K. G. M., Lambin, P., Koritzinsky, M., & Wouters, B. G. (2009) · Radiotherapy and Oncology · doi:10.1016/j.radonc.2009.06.029 · Cited by 141 · see citing works
Measurement of reactive oxygen species (ros) and mitochondrial ros in ampk knockout mice blood vessels
Wang, Q., & Zou, M.-H. (2018) · Methods in Molecular Biology · doi:10.1007/978-1-4939-7598-3_32 · Cited by 125 · see citing works

Authors: Andreyev, A. Y., Kushnareva, Y. E., & Starkov, A. A.
Affiliations: Lomonosov Moscow State University (RU)
Corresponding author: Starkov, A. A.
ORCID: Andreyev, A. Yu.
Starkov, A. A.
Venue: Biochemistry (Moscow)
Publisher: Springer Science and Business Media LLC
Published: 2005-02
Volume: 70
Issue: 2
Pages: 200-214
ISSN: 0006-2979 (ISSN-L)
1608-3040
DOI: 10.1007/s10541-005-0102-7
OpenAlex: W2111757377
Cited by: 1,336
References: 175
Citations by year: 2026: 17 · 2025: 37 · 2024: 59 · 2023: 76 · 2022: 72 · 2021: 78 · 2020: 61 · 2019: 49 · 2018: 66 · 2017: 65 · 2016: 78 · 2015: 81 · 2014: 79 · 2013: 70 · 2012: 94
FWCI: 3.91
Type: journal article
Language: en
Open access: closed
Licence: www.springernature.com/gp/researchers/text-and-data-mining (tdm)
www.springernature.com/gp/researchers/text-and-data-mining (vor)
Locations: Biochemistry (Moscow) (publishedVersion)
PubMed (publishedVersion)
Topics: 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
Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
Keywords: reactive oxygen species, oxidative stress, superoxide, mitochondrial ROS production, aging
MeSH terms: Animals, Enzymes, Intracellular Membranes, Mitochondria, Models, Biological, Multienzyme Complexes, Oxidation-Reduction, Superoxides, Reactive Oxygen Species

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

Mitochondrial metabolism of reactive oxygen species

Abstract

Integrity signals

Claims the paper makes

Claims other papers make about this one

Cites

Cited by

Related

Record

About these checks