The 2-oxoacid dehydrogenase complexes in mitochondria can produce superoxide/hydrogen peroxide at much higher rates than complex I

How mitochondria produce reactive oxygen species

Murphy, M. P. (2009) · Biochemical Journal · doi:10.1042/bj20081386 · Cited by 8,207 · 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

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

Activation of molecular oxygen by flavins and flavoproteins.

Massey, V. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31664-2 · Cited by 818 · see citing works

The mechanism of superoxide production by NADH:ubiquinone oxidoreductase (complex I) from bovine heart mitochondria

Kußmaul, L., & Hirst, J. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0510977103 · Cited by 720 · 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

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

α-KETO ACID DEHYDROGENASE COMPLEXES, X. REGULATION OF THE ACTIVITY OF THE PYRUVATE DEHYDROGENASE COMPLEX FROM BEEF KIDNEY MITOCHONDRIA BY PHOSPHORYLATION AND DEPHOSPHORYLATION

Linn, T. C., Pettit, F. H., & Reed, L. J. (1969) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.62.1.234 · Cited by 671 · see citing works

Mitochondrial Complex II Can Generate Reactive Oxygen Species at High Rates in Both the Forward and Reverse Reactions

Quinlan, C. L., Orr, A. L., Perevoshchikova, I. V., Treberg, J. R., Ackrell, B. A., & Brand, M. D. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.374629 · Cited by 670 · see citing works

Sites of reactive oxygen species generation by mitochondria oxidizing different substrates

Quinlan, C. L., Perevoshchikova, I. V., Hey‐Mogensen, M., Orr, A. L., & Brand, M. D. (2013) · Redox Biology · doi:10.1016/j.redox.2013.04.005 · Cited by 595 · see citing works

The pharmacology of dichloroacetate

Stacpoole, P. W. (1989) · Metabolism · doi:10.1016/0026-0495(89)90051-6 · Cited by 485 · see citing works

Inhibitors of the quinone-binding site allow rapid superoxide production from mitochondrial nadh:Ubiquinone oxidoreductase (complex i)

Lambert, A. J., & Brand, M. D. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406576200 · Cited by 480 · 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

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

Alpha-ketoglutarate dehydrogenase: a target and generator of oxidative stress

Tretter, L., & Adam-Vizi, V. (2005) · Philosophical Transactions of the Royal Society B: Biological Sciences · doi:10.1098/rstb.2005.1764 · Cited by 434 · see citing works

The production of superoxide anion radicals in the reaction of reduced flavins and flavoproteins with molecular oxygen

Massey, V., Strickland, S., Mayhew, S. G., Howell, L. G., Engel, P. C., Matthews, R. G., Schuman, M., & Sullivan, P. A. (1969) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(69)90287-3 · Cited by 426 · see citing works

Domains, motifs, and linkers in 2-oxo acid dehydrogenase multienzyme complexes: a paradigm in the design of a multifunctional protein

Perham, R. N. (1991) · Biochemistry · doi:10.1021/bi00099a001 · Cited by 422 · see citing works

Regulation of pyruvate dehydrogenase in rat heart. Mechanism of regulation of proportions of dephosphorylated and phosphorylated enzyme by oxidation of fatty acids and ketone bodies and of effects of diabetes: role of coenzyme A, acetyl-coenzyme A and reduced and oxidized nicotinamide-adenine dinucleotide

Kerbey, A. L., Randle, P. J., Cooper, R., Whitehouse, S., Pask, H. T., & Denton, R. M. (1976) · Biochemical Journal · doi:10.1042/bj1540327 · Cited by 399 · see citing works

The Reactivity of Flavoproteins with Sulfite

Massey, V., Müller, F., Feldberg, R. S., Schuman, M., Sullivan, P. A., Howell, L. G., Mayhew, S. G., Matthews, R. G., & Foust, G. P. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)36376-7 · Cited by 343 · see citing works

The mammalian pyruvate dehydrogenase complex: Structure and regulation

WIELAND, O. H. (1983) · Reviews of physiology, biochemistry and pharmacology · doi:10.1007/bfb0031008 · Cited by 342 · see citing works

Superoxide Is Produced by the Reduced Flavin in Mitochondrial Complex I

Pryde, K. R., & Hirst, J. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.186841 · Cited by 301 · see citing works

The role of mitochondrial function and cellular bioenergetics in ageing and disease

Brand, M. D., Orr, A. L., Perevoshchikova, I. V., & Quinlan, C. L. (2013) · British Journal of Dermatology · doi:10.1111/bjd.12208 · Cited by 292 · see citing works

Sites of phosphorylation on pyruvate dehydrogenase from bovine kidney and heart

Yeaman, S. J., Hutcheson, E. T., Roche, T. E., Pettit, F. H., Brown, J. R., Reed, L. J., Watson, D. C., & Dixon, G. H. (1978) · Biochemistry · doi:10.1021/bi00605a017 · Cited by 291 · 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

Isoenzymes of Pyruvate Dehydrogenase Phosphatase

Huang, B., Gudi, R., Wu, P., Harris, R. A., Hamilton, J. A., & Popov, K. M. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.28.17680 · Cited by 213 · see citing works

Evidence for two sites of superoxide production by mitochondrial NADH-ubiquinone oxidoreductase (complex I)

Treberg, J. R., Quinlan, C. L., & Brand, M. D. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.252502 · Cited by 212 · see citing works

Localization at Complex I and Mechanism of the Higher Free Radical Production of Brain Nonsynaptic Mitochondria in the Short-Lived Rat Than in the Longevous Pigeon

Barja, G., & Herrero, A. (1998) · Journal of Bioenergetics and Biomembranes · doi:10.1023/a:1020592719405 · Cited by 203 · see citing works

The mechanism of superoxide production by the antimycin-inhibited mitochondrial Q-cycle

Quinlan, C. L., Gerencser, A. A., Treberg, J. R., & Brand, M. D. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.267898 · Cited by 200 · see citing works

Principles of quasi-equivalence and Euclidean geometry govern the assembly of cubic and dodecahedral cores of pyruvate dehydrogenase complexes

Izard, T., Aevarsson, A., Allen, M. D., Westphal, A. H., Perham, R. N., de Kok, A., & Hol, W. G. J. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.4.1240 · Cited by 180 · see citing works

Regulation of branched-chain α-ketoacid dehydrogenase kinase

Paxton, R., & Harris, R. A. (1984) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(84)90361-8 · Cited by 179 · see citing works

The mechanism of fatty acid uptake by heart mitochondria: An acylcarnitine‐carnitine exchange

Ramsay, R. R., & Tubbs, P. K. (1975) · FEBS Letters · doi:10.1016/0014-5793(75)81059-3 · Cited by 176 · see citing works

A Refined Analysis of Superoxide Production by Mitochondrial sn-Glycerol 3-Phosphate Dehydrogenase

Orr, A. L., Quinlan, C. L., Perevoshchikova, I. V., & Brand, M. D. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.397828 · Cited by 167 · see citing works

Mechanisms responsible for regulation of branched-chain amino acid catabolism

Harris, R. A., Joshi, M., & Jeoung, N. H. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2003.11.007 · Cited by 166 · see citing works

Function of calcium ions in pyruvate dehydrogenase phosphatase activity

Pettit, F. H., Roche, T. E., & Reed, L. J. (1972) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(72)90448-2 · Cited by 163 · see citing works

Native rates of superoxide production from multiple sites in isolated mitochondria measured using endogenous reporters

Quinlan, C. L., Treberg, J. R., Perevoshchikova, I. V., Orr, A. L., & Brand, M. D. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.08.015 · Cited by 151 · see citing works

Characterization of carnitine acylcarnitine translocase system of heart mitochondria.

Pande, S. V., & Parvin, R. (1976) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32999-x · Cited by 143 · see citing works

Expression of two succinyl-CoA synthetases with different nucleotide specificities in mammalian tissues

Lambeth, D. O., Tews, K. N., Adkins, S., Frohlich, D., & Milavetz, B. I. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406884200 · Cited by 138 · see citing works

[15] Sulfur-centered free radicals

Asmus, K. (1990) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(90)86107-7 · Cited by 135 · 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

Architecture of the QoSite of the Cytochromebc1Complex Probed by Superoxide Production

Müller, F. L., Roberts, A. G., Bowman, M. K., & Kramer, D. (2003) · Biochemistry · doi:10.1021/bi0342160 · Cited by 132 · see citing works

Metabolic control exerted by the 2-oxoglutarate dehydrogenase reaction: a cross-kingdom comparison of the crossroad between energy production and nitrogen assimilation

Bunik, V. I., & Fernie, A. R. (2009) · Biochemical Journal · doi:10.1042/bj20090722 · Cited by 128 · see citing works

Contribution of different enzymes to flavoprotein fluorescence of isolated rat liver mitochondria

Kunz, W. S., & Kunz, W. (1985) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(85)90064-9 · Cited by 126 · see citing works

2‐Oxo acid dehydrogenase complexes in redox regulation

Bunik, V. I. (2003) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2003.03470.x · Cited by 125 · see citing works

Sites of superoxide and hydrogen peroxide production during fatty acid oxidation in rat skeletal muscle mitochondria

Perevoshchikova, I. V., Quinlan, C. L., Orr, A. L., Gerencser, A. A., & Brand, M. D. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.04.006 · Cited by 120 · see citing works

Diphenyleneiodonium acutely inhibits reactive oxygen species production by mitochondrial complex I during reverse, but not forward electron transport

Lambert, A. J., Buckingham, J. A., Boysen, H. M., & Brand, M. D. (2008) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2008.03.005 · Cited by 118 · see citing works

Structure and Kinetics of Monofunctional Proline Dehydrogenase from Thermus thermophilus

White, T., Krishnan, N., Becker, D., & Tanner, J. J. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m700912200 · Cited by 116 · see citing works

Some Kinetic Properties of Pig-Heart Oxoglutarate Dehydrogenase that Provide a Basis for Metabolic Control of the Enzyme Activity and also a Stoicheiometric Assay for Coenzyme A in Tissue Extracts

Garland, P. B. (1964) · Biochemical Journal · doi:10.1042/bj0920010c · Cited by 116 · 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

Mitochondrial glutathione depletion reveals a novel role for the pyruvate dehydrogenase complex as a key H2O2-emitting source under conditions of nutrient overload

Fisher‐Wellman, K. H., Gilliam, L. A. A., Lin, C., Cathey, B. L., Lark, D. S., & Neufer, P. D. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.09.008 · Cited by 115 · see citing works

Catalytic Activity of NADH-ubiquinone Oxidoreductase (Complex I) in Intact Mitochondria

Grivennikova, V. G., Kapustin, A. N., & Vinogradov, A. D. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m009661200 · Cited by 110 · see citing works

Partial purification and properties of branched-chain 2-oxo acid dehydrogenase of ox liver

Parker, P. J., & Randle, P. J. (1978) · Biochemical Journal · doi:10.1042/bj1710751 · Cited by 102 · see citing works

Enzyme-catalyzed Free Radical Reactions with Nicotinamide Adenine Nucleotides

Chan, P. C., & Bielski, H. J. (1974) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)42978-5 · Cited by 101 · see citing works

The Determination and Analysis of Site-Specific Rates of Mitochondrial Reactive Oxygen Species Production

Quinlan, C. L., Perevoschikova, I. V., Goncalves, R. L. S., Hey‐Mogensen, M., & Brand, M. D. (2013) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/b978-0-12-405883-5.00012-0 · Cited by 98 · see citing works

Control of succinate dehydrogenase in mitochondria

Gutman, M., Kearney, E. B., & Singer, T. P. (1971) · Biochemistry · doi:10.1021/bi00801a025 · Cited by 97 · see citing works

Hydrogen peroxide efflux from muscle mitochondria underestimates matrix superoxide production – a correction using glutathione depletion

Treberg, J. R., Quinlan, C. L., & Brand, M. D. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07693.x · Cited by 85 · see citing works

Sensitivity of pyruvate dehydrogenase phosphate phosphatase to magnesium ions. Similar effects of spermine and insulin

Thomas, A. P., Diggle, T. A., & Denton, R. M. (1986) · Biochemical Journal · doi:10.1042/bj2380083 · Cited by 85 · see citing works

A new family of protein kinases— The mitochondrial protein kinases

Harris, R. A., Popov, K. M., Zhao, Y., Kedishvili, N. Y., Shimomura, Y., & Crabb, D. W. (1995) · Advances in Enzyme Regulation · doi:10.1016/0065-2571(94)00020-4 · Cited by 82 · see citing works

Measurement of Proton Leak and Electron Leak in Isolated Mitochondria

Affourtit, C., Quinlan, C. L., & Brand, M. D. (2011) · Methods in molecular biology · doi:10.1007/978-1-61779-382-0_11 · Cited by 82 · see citing works

Phosphonate Analogues of α-Ketoglutarate Inhibit the Activity of the α-Ketoglutarate Dehydrogenase Complex Isolated from Brain and in Cultured Cells

Bunik, V. I., Denton, T. T., Xu, H., Thompson, C. M., Cooper, A. J. L., & Gibson, G. E. (2005) · Biochemistry · doi:10.1021/bi0503100 · Cited by 81 · see citing works

Inhibitors of ros production by the ubiquinone-binding site of mitochondrial complex i identified by chemical screening

Orr, A. L., Ashok, D., Sarantos, M. R., Shi, T., Hughes, R. E., & Brand, M. D. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.08.170 · Cited by 80 · see citing works

α-Ketoglutarate dehydrogenase contributes to production of reactive oxygen species in glutamate-stimulated hippocampal neurons in situ

Zündorf, G., Kahlert, S., Bunik, V. I., & Reiser, G. (2008) · Neuroscience · doi:10.1016/j.neuroscience.2008.10.015 · Cited by 76 · see citing works

Branched chain 2‐oxo‐acid dehydrogenase complex of rat liver

Parker, P. J., & Randle, P. J. (1978) · FEBS Letters · doi:10.1016/0014-5793(78)80325-1 · Cited by 75 · see citing works

Quantification of the Content of Fluorescent Flavoproteins in Mitochondria from Liver, Kidney Cortex, Skeletal Muscle, and Brain

Kunz, W. S., & Gellerich, F. N. (1993) · Biochemical Medicine and Metabolic Biology · doi:10.1006/bmmb.1993.1051 · Cited by 74 · see citing works

Essential roles of lipoyl domains in the activated function and control of pyruvate dehydrogenase kinases and phosphatase isoform 1

Roche, T. E., Hiromasa, Y., Türkan, A., Gong, X., Peng, T., Yan, X., Kasten, S. A., Bao, H., & Dong, J. (2003) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2003.03468.x · Cited by 73 · see citing works

Development and Characterization of a Conditional Mitochondrial Complex I Assembly System

Yadava, N., Houchens, T., Potluri, P., & Scheffler, I. E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313588200 · Cited by 68 · see citing works

Partitioning of superoxide and hydrogen peroxide production by mitochondrial respiratory complex I

Grivennikova, V. G., & Vinogradov, A. D. (2013) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2013.01.002 · Cited by 64 · see citing works

Reactive oxygen species regulation by AIF- and complex I-depleted brain mitochondria

Chinta, S. J., Rane, A., Yadava, N., Andersen, J. K., Nicholls, D. G., & Polster, B. M. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.01.010 · Cited by 62 · see citing works

Inhibition by the branched-chain 2-oxo acids of the 2-oxoglutarate dehydrogenase complex in developing rat and human brain

Patel, M. S. (1974) · Biochemical Journal · doi:10.1042/bj1440091 · Cited by 54 · see citing works

Q-Cycle Bypass Reactions at the Qo Site of the Cytochrome bc1 (and Related) Complexes

Kramer, D., Roberts, A. G., Müller, F. L., Cape, J. L., & Bowman, M. K. (2004) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(04)82002-0 · Cited by 51 · see citing works

Handbook of the Biology of Aging

Watt, D. F. (2012) · Archives of Clinical Neuropsychology · doi:10.1093/arclin/acr108 · Cited by 49 · see citing works

Investigations of the potential effects of phosphorylation of the MWFE and ESSS subunits on complex I activity and assembly

Yadava, N., Potluri, P., & Scheffler, I. E. (2007) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2007.08.015 · Cited by 46 · see citing works

Mitochondrial hydrogen peroxide production as determined by the pyridine nucleotide pool and its redox state

Kareyeva, A. V., Grivennikova, V. G., & Vinogradov, A. D. (2012) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2012.03.033 · Cited by 45 · see citing works

Detailed kinetics and regulation of mammalian 2-oxoglutarate dehydrogenase

Qi, F., Pradhan, R. K., Dash, R. K., & Beard, D. A. (2011) · BMC Biochemistry · doi:10.1186/1471-2091-12-53 · Cited by 44 · see citing works

Molecular identification of the enzyme responsible for the mitochondrial NADH-supported ammonium-dependent hydrogen peroxide production

Kareyeva, A. V., Grivennikova, V. G., Cecchini, G., & Vinogradov, A. D. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.12.019 · Cited by 43 · see citing works

Dissociation of superoxide production by mitochondrial complex I from NAD(P)H redox state

Lambert, A. J., Buckingham, J. A., & Brand, M. D. (2008) · FEBS Letters · doi:10.1016/j.febslet.2008.04.030 · Cited by 38 · see citing works

Kinetic properties of the 2‐oxoglutarate dehydrogenase complex from Azotobacter vinelandii

Bunik, V. I., Westphal, A. H., & de Kok, A. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2000.01387.x · Cited by 34 · see citing works

Molecular dynamics study of the structural basis of dysfunction and the modulation of reactive oxygen species generation by pathogenic mutants of human dihydrolipoamide dehydrogenase

Ambrus, A., & Ádám‐Vizi, V. (2013) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2013.08.015 · Cited by 31 · see citing works

Succinyl phosphonate inhibits α‐ketoglutarate oxidative decarboxylation, catalyzed by α‐ketoglutarate dehydrogenase complexes from E. coli and pigeon breast muscle

Biryukov, A. I., Bunik, V. I., Zhukov, Y. N., Khurs, E. N., & Khomutov, R. M. (1996) · FEBS Letters · doi:10.1016/0014-5793(96)00166-4 · Cited by 28 · see citing works

A Survey of Oxidative Paracatalytic Reactions Catalyzed by Enzymes that Generate Carbanionic Intermediates: Implications for ROS Production, Cancer Etiology, and Neurodegenerative Diseases

Bunik, V. I., Schloss, J. V., Pinto, J. T., Dudareva, N., & Cooper, A. J. L. (2011) · Advances in enzymology and related areas of molecular biology/Advances in enzymology and related subjects · doi:10.1002/9780470920541.ch7 · Cited by 27 · see citing works

Inhibition of pigeon breast muscle α‐ketoglutarate dehydrogenase by phosphonate analogues of α‐ketoglutarate

Bunik, V. I., Biryukov, A. I., & YuN, Z. (1992) · FEBS Letters · doi:10.1016/0014-5793(92)80518-l · Cited by 27 · see citing works

Hsp-antigen fusion and their use for immunization

Udono, H., Saito, T., Ogawa, M., & Yui, Y. (2003) · Methods · doi:10.1016/s1046-2023(03)00182-8 · Cited by 22 · see citing works

Translating Enzymology into Metabolic Regulation: The Case of the 2- Oxoglutarate Dehydrogenase Multienzyme Complex

Bunik, V. I., Raddatz, G., & Strumiło, S. (2013) · Current Chemical Biology · doi:10.2174/2212796811307010008 · Cited by 19 · see citing works

Branched Chain Keto-Acids Exert Biphasic Effects on α-Ketoglutarate-Stimulated Respiration in Intact Rat Liver Mitochondria

Shestopalov, A. I., & Kristal, B. S. (2007) · Neurochemical Research · doi:10.1007/s11064-007-9291-3 · Cited by 13 · see citing works

Mechanisms of Mitochondrial Free Radical Production and their Relationship to the Aging Process

Quinlan, C. L., Treberg, J. R., & Brand, M. D. (2010) · Elsevier eBooks · doi:10.1016/b978-0-12-378638-8.00003-8 · Cited by 12 · see citing works

Effect of α‐ketoglutarate and its structural analogues on hysteretic properties of α‐ketoglutarate dehydrogenase

Bunik, V. I., Romash, O. G., & Gomazkova, V. S. (1991) · FEBS Letters · doi:10.1016/0014-5793(91)80104-b · Cited by 11 · see citing works

Reactive Oxygen Species in Metabolic and Inflammatory Signaling

Forrester, S. J., Kikuchi, D. S., Hernandes, M. S., Xu, Q., & Griendling, K. K. (2018) · Circulation Research · doi:10.1161/circresaha.117.311401 · Cited by 2,081 · see citing works

Lipid peroxidation and ferroptosis: The role of GSH and GPx4

Ursini, F., & Maiorino, M. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.02.027 · Cited by 1,954 · see citing works

Mitochondrial ROS in cancer: initiators, amplifiers or an Achilles' heel?

Sabharwal, S. S., & Schumacker, P. T. (2014) · Nature reviews. Cancer · doi:10.1038/nrc3803 · Cited by 1,643 · see citing works

Reperfusion injury and reactive oxygen species: The evolution of a concept

Granger, D. N., & Kvietys, P. R. (2015) · Redox Biology · doi:10.1016/j.redox.2015.08.020 · Cited by 1,510 · see citing works

The Role of the Reactive Oxygen Species and Oxidative Stress in the Pathomechanism of the Age‐Related Ocular Diseases and Other Pathologies of the Anterior and Posterior Eye Segments in Adults

Nita, M., & Grzybowski, A. E. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/3164734 · Cited by 1,451 · see citing works

Reactive oxygen species and mitochondria: A nexus of cellular homeostasis

Dunn, J. D., Álvarez, L., Zhang, X., & Soldati, T. (2015) · Redox Biology · doi:10.1016/j.redox.2015.09.005 · Cited by 1,199 · 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

The Redox Code

Jones, D. P., & Sies, H. (2015) · Antioxidants & Redox Signaling · doi:10.1089/ars.2015.6247 · Cited by 647 · see citing works

Glutathione and mitochondria

Ribas, V., García‐Ruiz, C., & Fernández-Checa, J. C. (2014) · Frontiers in Pharmacology · doi:10.3389/fphar.2014.00151 · Cited by 572 · see citing works

Lipoic acid metabolism and mitochondrial redox regulation

Solmonson, A., & DeBerardinis, R. J. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.tm117.000259 · Cited by 492 · see citing works

Production of superoxide and hydrogen peroxide from specific mitochondrial sites under different bioenergetic conditions

Wong, H. S., Dighe, P. A., Mezera, V., Monternier, P., & Brand, M. D. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.r117.789271 · Cited by 478 · see citing works

Generation of Reactive Oxygen Species by Mitochondria

Hernansanz‐Agustín, P., & Enrı́quez, J. A. (2021) · Antioxidants · doi:10.3390/antiox10030415 · Cited by 414 · see citing works

Mitochondrial metabolism mediates oxidative stress and inflammation in fatty liver

Satapati, S., Kucejová, B., Duarte, J. A. G., Fletcher, J. A., Reynolds, L., Sunny, N. E., He, T., Nair, L. A., Livingston, K. A., Fu, X., et al. (2015) · Journal of Clinical Investigation · doi:10.1172/jci82204 · Cited by 400 · see citing works

Pathogenesis of Chronic Hyperglycemia: From Reductive Stress to Oxidative Stress

Yan, L. (2014) · Journal of Diabetes Research · doi:10.1155/2014/137919 · Cited by 403 · see citing works

Interactions between mitochondrial reactive oxygen species and cellular glucose metabolism

Liemburg-Apers, D. C., Willems, P. H. G. M., Koopman, W. J. H., & Grefte, S. (2015) · Archives of Toxicology · doi:10.1007/s00204-015-1520-y · Cited by 391 · see citing works

Reactive oxygen species, nutrition, hypoxia and diseases: Problems solved?

Görlach, A., Dimova, E. Y., Petry, A., Martı́nez-Ruiz, A., Hernansanz‐Agustín, P., Rolo, A. P., Palmeira, C. M., & Kietzmann, T. (2015) · Redox Biology · doi:10.1016/j.redox.2015.08.016 · Cited by 351 · see citing works

The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications

Carrico, C., Meyer, J. G., He, W., Gibson, B. W., & Verdin, E. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.01.016 · Cited by 331 · 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

Superoxide Radicals in the Execution of Cell Death

Fujii, J., Homma, T., & Osaki, T. (2022) · Antioxidants · doi:10.3390/antiox11030501 · Cited by 321 · see citing works

Mitochondrial Management of Reactive Oxygen Species

Napolitano, G., Fasciolo, G., & Venditti, P. (2021) · Antioxidants · doi:10.3390/antiox10111824 · Cited by 296 · see citing works

Teaching the fundamentals of electron transfer reactions in mitochondria and the production and detection of reactive oxygen species

Mailloux, R. J. (2015) · Redox Biology · doi:10.1016/j.redox.2015.02.001 · Cited by 286 · see citing works

An Update on Mitochondrial Reactive Oxygen Species Production

Mailloux, R. J. (2020) · Antioxidants · doi:10.3390/antiox9060472 · Cited by 286 · see citing works

Sulforaphane reactivates cellular antioxidant defense by inducing Nrf2/ARE/Prdx6 activity during aging and oxidative stress

Kubo, E., Chhunchha, B., Singh, P., Sasaki, H., & Singh, D. P. (2017) · Scientific Reports · doi:10.1038/s41598-017-14520-8 · Cited by 231 · see citing works

Suppressors of Superoxide-H 2 O 2 Production at Site I Q of Mitochondrial Complex I Protect against Stem Cell Hyperplasia and Ischemia-Reperfusion Injury

Brand, M. D., Goncalves, R. L. S., Orr, A. L., Vargas, L., Gerencser, A. A., Borch Jensen, M., Wang, Y. T., Melov, S., Turk, C. N., Matzen, J. T., et al. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.08.012 · Cited by 228 · see citing works

Antioxidant supplements and endurance exercise: Current evidence and mechanistic insights

Mason, S. A., Trewin, A. J., Parker, L., & Wadley, G. D. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101471 · Cited by 226 · see citing works

Exploring the molecular interface between hypoxia-inducible factor signalling and mitochondria

Thomas, L. W., & Ashcroft, M. A. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03039-y · Cited by 211 · see citing works

Dichloroacetate and cancer: New home for an orphan drug?

Kankotia, S., & Stacpoole, P. W. (2014) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2014.08.005 · Cited by 212 · see citing works

Cross-Talk between Oxidative Stress and Inflammation in Preeclampsia

Tenório, M. B., Ferreira, R. C., Moura, F. A., Bueno, N. B., de Oliveira, A. C. M., & Goulart, M. O. F. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/8238727 · Cited by 206 · see citing works

Elucidating the contribution of mitochondrial glutathione to ferroptosis in cardiomyocytes

Jang, S., Chapa‐Dubocq, X. R., Tyurina, Y. Y., Croix, C. M. S., Kapralov, A. A., Tyurin, V. A., Bayır, H., Kagan, V. E., & Javadov, S. A. (2021) · Redox Biology · doi:10.1016/j.redox.2021.102021 · Cited by 207 · see citing works

Increased reactive oxygen species production during reductive stress: The roles of mitochondrial glutathione and thioredoxin reductases

Kôrge, P., Calmettes, G., & Weiss, J. N. (2015) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2015.02.012 · Cited by 199 · see citing works

Sources and implications of NADH/NAD+ redox imbalance in diabetes and its complications

Yan, L.-J., Wu, J., Jin, Z., & Zheng, H. (2016) · Diabetes, Metabolic Syndrome and Obesity: Targets and Therapy · doi:10.2147/dmso.s106087 · Cited by 198 · see citing works

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 194 · see citing works

Flavonoids and type 2 diabetes: Evidence of efficacy in clinical and animal studies and delivery strategies to enhance their therapeutic efficacy

Hussain, T., Tan, B., Murtaza, G., Liu, G., Rahu, N., Kalhoro, M. S., Kalhoro, D. H., Adebowale, T. O., Mazhar, M. U., Rehman, Z. U., et al. (2020) · Pharmacological Research · doi:10.1016/j.phrs.2020.104629 · Cited by 202 · see citing works

Amino acid catabolism in Alzheimer’s disease brain: Friend or foe?

Griffin, J. W. D., & Bradshaw, P. C. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/5472792 · Cited by 185 · see citing works

Insights into the respiratory chain and oxidative stress

Larosa, V., & Remacle, C. (2018) · Bioscience Reports · doi:10.1042/bsr20171492 · Cited by 183 · see citing works

Mitochondrial protein interaction landscape of SS-31

Chavez, J. D., Tang, X., Campbell, M. D., Reyes, G., Kramer, P. A., Stuppard, R., Keller, A., Zhang, H., Rabinovitch, P. S., Marcinek, D. J., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2002250117 · Cited by 183 · see citing works

Modelling mitochondrial ROS production by the respiratory chain

Mazat, J., Devin, A., & Ransac, S. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03381-1 · Cited by 180 · see citing works

Dihydrolipoamide dehydrogenase regulates cystine deprivation-induced ferroptosis in head and neck cancer

Shin, D., Lee, J., You, J. H., Kim, D., & Roh, J. (2020) · Redox Biology · doi:10.1016/j.redox.2019.101418 · Cited by 179 · see citing works

Use the Protonmotive Force: Mitochondrial Uncoupling and Reactive Oxygen Species

Berry, B. J., Trewin, A. J., Amitrano, A. M., Kim, M., & Wojtovich, A. P. (2018) · Journal of Molecular Biology · doi:10.1016/j.jmb.2018.03.025 · Cited by 175 · see citing works

Heat exposure induces oxidative stress and DNA damage in the male germ line†

Houston, B. J., Nixon, B., Martin, J. H., Iuliis, G. N. D., Trigg, N. A., Bromfield, E. G., McEwan, K. E., & Aitken, R. J. (2018) · Biology of Reproduction · doi:10.1093/biolre/ioy009 · Cited by 162 · see citing works

Targeting Ferroptosis against Ischemia/Reperfusion Cardiac Injury

Lillo‐Moya, J., Rojas-Solé, C., Muñoz-Salamanca, D., Panieri, E., Saso, L., & Rodrigo, R. (2021) · Antioxidants · doi:10.3390/antiox10050667 · Cited by 161 · see citing works

The RNA-binding protein HuR is essential for the B cell antibody response

Díaz‐Muñoz, M. D., Bell, S. E., Fairfax, K. A., Monzón‐Casanova, E., Cunningham, A. F., Gonzàlez-Porta, M., Andrews, S., Bunik, V. I., Zarnack, K., Curk, T., et al. (2015) · Nature Immunology · doi:10.1038/ni.3115 · Cited by 159 · see citing works

The mitochondrial unfolded protein response (UPRmt): shielding against toxicity to mitochondria in cancer

Inigo, J. R., & Chandra, D. (2022) · Journal of Hematology & Oncology · doi:10.1186/s13045-022-01317-0 · Cited by 154 · see citing works

Metabolic Flexibility in Cancer: Targeting the Pyruvate Dehydrogenase Kinase:Pyruvate Dehydrogenase Axis

Woolbright, B. L., Rajendran, G., Harris, R. A., & Taylor, J. A. (2019) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-19-0079 · Cited by 153 · see citing works

The redox language in neurodegenerative diseases: oxidative post-translational modifications by hydrogen peroxide

Lee, Y. M., He, W., & Liou, Y. (2021) · Cell Death and Disease · doi:10.1038/s41419-020-03355-3 · Cited by 150 · see citing works

Cellular and mitochondrial mechanisms of atrial fibrillation

Mason, F. E., Pronto, J. R. D., Alhussini, K., Maack, C., & Voigt, N. (2020) · Basic Research in Cardiology · doi:10.1007/s00395-020-00827-7 · Cited by 147 · see citing works

Polyol pathway and redox balance in diabetes

Garg, S. S., & Gupta, J. (2022) · Pharmacological Research · doi:10.1016/j.phrs.2022.106326 · Cited by 151 · see citing works

Mitochondrial Dysfunction in the Aging Retina

Eells, J. T. (2019) · Biology · doi:10.3390/biology8020031 · Cited by 139 · see citing works

Ischemic A/D transition of mitochondrial complex I and its role in ROS generation

Dröse, S., Степанова, А., & Galkin, A. S. (2016) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2015.12.013 · Cited by 137 · see citing works

Intracellular Sources of ROS/H2O2 in Health and Neurodegeneration: Spotlight on Endoplasmic Reticulum

Konno, T., Melo, E. P., Chambers, J. E., & Avezov, E. (2021) · Cells · doi:10.3390/cells10020233 · Cited by 140 · see citing works

Linking Oxidative Stress and Proteinopathy in Alzheimer’s Disease

Sharma, C., & Kim, S. R. (2021) · Antioxidants · doi:10.3390/antiox10081231 · Cited by 136 · see citing works

Hypoxia Dictates Metabolic Rewiring of Tumors: Implications for Chemoresistance

Belisario, D. C., Kopecka, J., Pasino, M., Akman, M., De Smaele, E., Donadelli, M., & Riganti, C. (2020) · Cells · doi:10.3390/cells9122598 · Cited by 133 · see citing works

Hyperglycemic Stress and Carbon Stress in Diabetic Glucotoxicity

Luo, X., Wu, J., Jing, S., & Yan, L. (2016) · Aging and Disease · doi:10.14336/ad.2015.0702 · Cited by 136 · see citing works

Protein S-glutathionlyation links energy metabolism to redox signaling in mitochondria

Mailloux, R. J., & Treberg, J. R. (2015) · Redox Biology · doi:10.1016/j.redox.2015.12.010 · Cited by 132 · see citing works

The α-ketoglutarate dehydrogenase complex in cancer metabolic plasticity

Vatrinet, R., Leone, G., Luise, M. D., Girolimetti, G., Vidone, M., Gasparre, G., & Porcelli, A. M. (2017) · Cancer & Metabolism · doi:10.1186/s40170-017-0165-0 · Cited by 130 · see citing works

S-glutathionylation reactions in mitochondrial function and disease

Mailloux, R. J., & Willmore, W. G. (2014) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2014.00068 · Cited by 125 · see citing works

Molecular mechanisms of the non-coenzyme action of thiamin in brain: biochemical, structural and pathway analysis

Mkrtchyan, G. V., Aleshin, V. A., IuM, P., Kaehne, T., di Salvo, M. L., Parroni, A., Contestabile, R., Vovk, A. I., Bettendorff, L., & Bunik, V. I. (2015) · Scientific Reports · doi:10.1038/srep12583 · Cited by 128 · see citing works

Riding the tiger – physiological and pathological effects of superoxide and hydrogen peroxide generated in the mitochondrial matrix

Brand, M. D. (2020) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2020.1828258 · Cited by 123 · see citing works

Protein-mediated assembly of succinate dehydrogenase and its cofactors

Vranken, J. G. V., Na, U., Winge, D. R., & Rutter, J. P. (2014) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2014.990556 · Cited by 122 · see citing works

Pyruvate dehydrogenase complex and nicotinamide nucleotide transhydrogenase constitute an energy-consuming redox circuit

Fisher‐Wellman, K. H., Lin, C., RYAN, T. E., Reese, L., Gilliam, L. A. A., Cathey, B. L., Lark, D. S., Smith, C. D., Muoio, D. M., & Neufer, P. D. (2015) · Biochemical Journal · doi:10.1042/bj20141447 · Cited by 121 · see citing works

Mitochondrial reactive oxygen species production by fish muscle mitochondria: Potential role in acute heat-induced oxidative stress

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 · see citing works

The Contribution of Nicotinamide Nucleotide Transhydrogenase to Peroxide Detoxification Is Dependent on the Respiratory State and Counterbalanced by Other Sources of NADPH in Liver Mitochondria

Ronchi, J. A., Francisco, A., Passos, L. A., Figueira, T. R., & Castilho, R. F. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.730473 · Cited by 119 · see citing works

Mitochondria in Diabetic Kidney Disease

Ahmad, A. A., Draves, S. O., & Rosca, M. G. (2021) · Cells · doi:10.3390/cells10112945 · Cited by 117 · see citing works

Known unknowns of cardiolipin signaling: The best is yet to come

Maguire, J. J., Tyurina, Y. Y., Mohammadyani, D., Kapralov, A. A., Anthonymuthu, T. S., Qu, F., Amoscato, A. A., Sparvero, L. J., Tyurin, V. A., Planas-Iglesias, J., et al. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2016.08.001 · Cited by 116 · see citing works

Oxidative stress mediates ethanol-induced skeletal muscle mitochondrial dysfunction and dysregulated protein synthesis and autophagy

Kumar, A., Davuluri, G., Welch, N., Kim, A., Gangadhariah, M. H., Allawy, A., Priyadarshini, A., McMullen, M. R., Sandlers, Y. I., Willard, B. B., et al. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2019.09.031 · Cited by 112 · see citing works

Silence superoxide dismutase 1 (SOD1): a promising therapeutic target for amyotrophic lateral sclerosis (ALS)

Abati, E., Bresolin, N., Comi, G. P., & Corti, S. P. (2020) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2020.1738390 · Cited by 104 · see citing works

Mitochondrial Cristae Morphology Reflecting Metabolism, Superoxide Formation, Redox Homeostasis, and Pathology

Ježek, P., Jabůrek, M., Holendová, B., Engstová, H., & Dlasková, A. (2023) · Antioxidants and Redox Signaling · doi:10.1089/ars.2022.0173 · Cited by 111 · see citing works

Mitochondrial Oxidative Stress in the Retinal Pigment Epithelium Leads to Localized Retinal Degeneration

Mao, H., Seo, S. J., Biswal, M. R., Li, H., Conners, M., Nandyala, A. S., Jones, K., Le, Y.-Z., & Lewin, A. S. (2014) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.14-14633 · Cited by 107 · see citing works

The role of mitochondrial ROS in antibacterial immunity

Pinegin, B. V., Vorobjeva, N. V., Pashenkov, M. V., & Chernyak, B. V. (2017) · Journal of Cellular Physiology · doi:10.1002/jcp.26117 · Cited by 105 · see citing works

How Do ROS Induce NETosis? Oxidative DNA Damage, DNA Repair, and Chromatin Decondensation

Azzouz, D., & Palaniyar, N. (2024) · Biomolecules · doi:10.3390/biom14101307 · Cited by 108 · see citing works

Mitochondrial reactive oxygen species: Do they extend or shorten animal lifespan?

Sanz, A. (2016) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2016.03.018 · Cited by 101 · see citing works

Melatonin alleviates heat stress-induced oxidative stress and apoptosis in human spermatozoa

Zhao, F., Whiting, S., Lambourne, S. R., Aitken, R. J., & Sun, Y. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.01.014 · Cited by 102 · see citing works

Escaping Death: Mitochondrial Redox Homeostasis in Cancer Cells

Ciccarese, F., & Ciminale, V. (2017) · Frontiers in Oncology · doi:10.3389/fonc.2017.00117 · Cited by 101 · see citing works

Cysteine-mediated redox signalling in the mitochondria

Bak, D. W., & Weerapana, E. (2014) · Molecular BioSystems · doi:10.1039/c4mb00571f · Cited by 100 · see citing works

Induction of mitochondrial reactive oxygen species production by GSH mediated S-glutathionylation of 2-oxoglutarate dehydrogenase

Mailloux, R. J., Ayre, D. C., & Christian, S. L. (2016) · Redox Biology · doi:10.1016/j.redox.2016.02.002 · Cited by 97 · see citing works

Interplay Between Reactive Oxygen/Reactive Nitrogen Species and Metabolism in Vascular Biology and Disease

Ushio‐Fukai, M., Ash, D., Nagarkoti, S., de Chantemèle, E. J. B., Fulton, D. J., & Fukai, T. (2021) · Antioxidants and Redox Signaling · doi:10.1089/ars.2020.8161 · Cited by 96 · see citing works

Relationship between Oxidative Stress, Circadian Rhythms, and AMD

Fanjul‐Moles, M. L., & López-Riquelme, G. O. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/7420637 · Cited by 95 · see citing works

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 99 · see citing works

Oxidative Stress and Mitochondrial Dysfunction Associated with Peripheral Neuropathy in Type 1 Diabetes

Eftekharpour, E., & Fernyhough, P. (2021) · Antioxidants and Redox Signaling · doi:10.1089/ars.2021.0152 · Cited by 87 · see citing works

Production of superoxide/H2O2 by dihydroorotate dehydrogenase in rat skeletal muscle mitochondria

Hey‐Mogensen, M., Goncalves, R. L. S., Orr, A. L., & Brand, M. D. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.04.007 · Cited by 84 · see citing works

The thioredoxin and glutathione-dependent H2O2 consumption pathways in muscle mitochondria: Involvement in H2O2 metabolism and consequence to H2O2 efflux assays

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 83 · see citing works

Catalytic Coupling of Oxidative Phosphorylation, ATP Demand, and Reactive Oxygen Species Generation

Bazil, J. N., Beard, D. A., & Vinnakota, K. C. (2016) · Biophysical Journal · doi:10.1016/j.bpj.2015.09.036 · Cited by 81 · see citing works

Proteomics characterization of mitochondrial‐derived vesicles under oxidative stress

Vasam, G., Nadeau, R., Cadete, V. J. J., Lavallée‐Adam, M., Menzies, K. J., & Burelle, Y. (2021) · The FASEB Journal · doi:10.1096/fj.202002151r · Cited by 79 · see citing works

Complex I and complex III inhibition specifically increase cytosolic hydrogen peroxide levels without inducing oxidative stress in HEK293 cells

Forkink, M., Basit, F., Teixeira, J., Swarts, H. G. P., Koopman, W. J. H., & Willems, P. H. G. M. (2015) · Redox Biology · doi:10.1016/j.redox.2015.09.003 · Cited by 80 · see citing works

Sources of superoxide/H2O2 during mitochondrial proline oxidation

Goncalves, R. L. S., Rothschild, D. E., Quinlan, C. L., Scott, G. K., Benz, C. C., & Brand, M. D. (2014) · Redox Biology · doi:10.1016/j.redox.2014.07.003 · Cited by 79 · see citing works

Protein S-glutathionylation alters superoxide/hydrogen peroxide emission from pyruvate dehydrogenase complex

O’Brien, M., Chalker, J., Slade, L., Gardiner, D., & Mailloux, R. J. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.02.046 · Cited by 79 · see citing works

2-Oxoglutarate dehydrogenase is a more significant source of O2·−/H2O2 than pyruvate dehydrogenase in cardiac and liver tissue

Mailloux, R. J., Gardiner, D., & O’Brien, M. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.06.014 · Cited by 78 · see citing works

What sustains the multidrug resistance phenotype beyond ABC efflux transporters? Looking beyond the tip of the iceberg

Alexa‐Stratulat, T., Pešić, M., Gašparović, A. Č., Trougakos, I. P., & Riganti, C. (2019) · Drug Resistance Updates · doi:10.1016/j.drup.2019.100643 · Cited by 76 · see citing works

Progress in understanding the molecular oxygen paradox – function of mitochondrial reactive oxygen species in cell signaling

Kuksal, N., Chalker, J., & Mailloux, R. J. (2017) · Biological Chemistry · doi:10.1515/hsz-2017-0160 · Cited by 74 · see citing works

The α-Ketoglutarate Dehydrogenase Complex as a Hub of Plasticity in Neurodegeneration and Regeneration

Hansen, G. E., & Gibson, G. E. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232012403 · Cited by 77 · see citing works

Dietary supplementation of heat-treatedGracilariaandUlvaseaweeds enhanced acute hypoxia tolerance in gilthead seabream (Sparus aurata)

Magnoni, L. J., Martos-Sitcha, J. A., Queiroz, A., Calduch-Giner, J. À., Gonçalves, G. S., Rocha, C. M. R., Abreu, H., Schrama, J. W., Ozório, R. O. A., & Pérez‐Sánchez, J. (2017) · Biology Open · doi:10.1242/bio.024299 · Cited by 72 · see citing works

Production of superoxide/hydrogen peroxide by the mitochondrial 2-oxoadipate dehydrogenase complex

Goncalves, R. L. S., Bunik, V. I., & Brand, M. D. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.12.020 · Cited by 70 · see citing works

The use of site-specific suppressors to measure the relative contributions of different mitochondrial sites to skeletal muscle superoxide and hydrogen peroxide production

Gonçalves, R. L. S., Watson, M. A., Wong, H. S., Orr, A. L., & Brand, M. D. (2019) · Redox Biology · doi:10.1016/j.redox.2019.101341 · Cited by 68 · see citing works

Mitochondrial physiology and reactive oxygen species production are altered by hypoxia acclimation in killifish (Fundulus heteroclitus)

Du, S. N. N., Mahalingam, S., Borowiec, B. G., & Scott, G. R. (2016) · Journal of Experimental Biology · doi:10.1242/jeb.132860 · Cited by 69 · see citing works

An update on methods and approaches for interrogating mitochondrial reactive oxygen species production

Mailloux, R. J. (2021) · Redox Biology · doi:10.1016/j.redox.2021.102044 · Cited by 69 · see citing works

Mito-Nuclear Communication by Mitochondrial Metabolites and Its Regulation by B-Vitamins

Janssen, J. J. E., Grefte, S., Keijer, J., & de Boer, V. C. J. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.00078 · Cited by 68 · see citing works

Reverse electron transfer results in a loss of flavin from mitochondrial complex I: Potential mechanism for brain ischemia reperfusion injury

Степанова, А., Kahl, A., Konràd, C., Ten, V. S., Starkov, A. A., & Galkin, A. S. (2017) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1177/0271678x17730242 · Cited by 65 · see citing works

Antioxidant Systems as Modulators of Ferroptosis: Focus on Transcription Factors

Punziano, C., Trombetti, S., Cesaro, E., Grosso, M., & Faraonio, R. (2024) · Antioxidants · doi:10.3390/antiox13030298 · Cited by 67 · see citing works

Formation of reactive oxygen species by human and bacterial pyruvate and 2-oxoglutarate dehydrogenase multienzyme complexes reconstituted from recombinant components

Ambrus, A., Nemeria, N. S., Törőcsik, B., Tretter, L., Nilsson, M., Jordan, F., & Ádám‐Vizi, V. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.10.001 · Cited by 64 · see citing works

Reactive oxygen species production induced by pore opening in cardiac mitochondria: The role of complex II

Kôrge, P., John, S., Calmettes, G., & Weiss, J. N. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.768325 · Cited by 63 · see citing works

Generation of superoxide and hydrogen peroxide by side reactions of mitochondrial 2-oxoacid dehydrogenase complexes in isolation and in cells

Bunik, V. I., & Brand, M. D. (2018) · Biological Chemistry · doi:10.1515/hsz-2017-0284 · Cited by 29 · see citing works

Production of superoxide/hydrogen peroxide by the mitochondrial 2-oxoadipate dehydrogenase complex

Goncalves, R. L. S., Bunik, V. I., & Brand, M. D. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.12.020 · Cited by 70 · see citing works

Characterization and suppression of mitochondrial production of superoxide and hydrogen peroxide under near-physiological conditions

Brand, M. D., Quinlan, C. L., Goncalves, R. L. S., Perevoshchikova, I. V., Treberg, J. R., Hey‐Mogensen, M., Gerencser, A. A., & Orr, A. L. (2014) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2014.05.224

Dissociation of superoxide production by mitochondrial complex I from NAD(P)H redox state

Lambert, A. J., Buckingham, J. A., & Brand, M. D. (2008) · FEBS Letters · doi:10.1016/j.febslet.2008.04.030 · Cited by 38 · see citing works

Native rates of superoxide production from multiple sites in isolated mitochondria measured using endogenous reporters

Quinlan, C. L., Treberg, J. R., Perevoshchikova, I. V., Orr, A. L., & Brand, M. D. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.08.015 · Cited by 151 · see citing works