Mitochondrial respiratory chain and thioredoxin reductase regulate intermembrane Cu,Zn-superoxide dismutase activity: implications for mitochondrial energy metabolism and apoptosis
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IMS (intermembrane space) SOD1 (Cu/Zn-superoxide dismutase) is inactive in isolated intact rat liver mitochondria and is activated following oxidative modification of its critical thiol groups. The present study aimed to identify biochemical pathways implicated in the regulation of IMS SOD1 activity and to assess the impact of its functional state on key mitochondrial events. Exogenous H2O2 (5 μM) activated SOD1 in intact mitochondria. However, neither H2O2 alone nor H2O2 in the presence of mitochondrial peroxiredoxin III activated SOD1, which was purified from mitochondria and subsequently reduced by dithiothreitol to an inactive state. The reduced enzyme was activated following incubation with the superoxide generating system, xanthine and xanthine oxidase. In intact mitochondria, the extent and duration of SOD1 activation was inversely correlated with mitochondrial superoxide production. The presence of TxrR-1 (thioredoxin reductase-1) was demonstrated in the mitochondrial IMS by Western blotting. Inhibitors of TxrR-1, CDNB (1-chloro-2,4-dinitrobenzene) or auranofin, prolonged the duration of H2O2-induced SOD1 activity in intact mitochondria. TxrR-1 inactivated SOD1 purified from mitochondria in an active oxidized state. Activation of IMS SOD1 by exogenous H2O2 delayed CaCl2-induced loss of transmembrane potential, decreased cytochrome c release and markedly prevented superoxide-induced loss of aconitase activity in intact mitochondria respiring at state-3. These findings suggest that H2O2, superoxide and TxrR-1 regulate IMS SOD1 activity reversibly, and that the active enzyme is implicated in protecting vital mitochondrial functions.
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Overexpressing CuZnSOD lacked any benefit to prolonging life span in mice.
“the lack of any benefit to prolonging life span in mice overexpressing CuZnSOD (166).”
From Mitochondrial reactive oxygen species production in excitable cells: Modulators of mitochondrial and cell function (2009) · cites this paper as [166]
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Cites
Bradford, M. M. (1976) · Analytical Biochemistry · doi:10.1016/0003-2697(76)90527-3 · Cited by 255,302 · see citing works
McCord, J. M., & Fridovich, I. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)63504-5 · Cited by 12,952 · see citing works
Peroxiredoxin Evolution and the Regulation of Hydrogen Peroxide Signaling
Wood, Z. A., Poole, L. B., & Karplus, P. A. (2003) · Science · doi:10.1126/science.1080405 · Cited by 1,369 · see citing works
Subcellular Distribution of Superoxide Dismutases (SOD) in Rat Liver
Okado‐Matsumoto, A., & Fridovich, I. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105395200 · Cited by 1,013 · see citing works
Sturtz, L. A., Diekert, K., Jensen, L. T., Lill, R., & Culotta, V. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105296200 · Cited by 719 · see citing works
HAN, D., WILLIAMS, E., & CADENAS, E. (2001) · Biochemical Journal · doi:10.1042/bj3530411 · Cited by 593 · see citing works
Self-citationHan, D., WILLIAMS, E., & Cadenas, E. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3530411 · Cited by 516 · see citing works
Self-citationSeo, M. S., Kang, S. W., Kim, K., Baines, I., Lee, T., & Rhee, S. G. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m001943200 · Cited by 473 · see citing works
Gardner, P. R., & Fridovich, I. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)50343-x · Cited by 346 · see citing works
Ukeda, H., Maeda, S., ISHII, T., & Sawamura, M. (1997) · Analytical Biochemistry · doi:10.1006/abio.1997.2273 · Cited by 345 · see citing works
Hyslop, P. A., & Sklar, L. A. (1984) · Analytical Biochemistry · doi:10.1016/0003-2697(84)90457-3 · Cited by 316 · see citing works
PETIT, P. X., Goubern, M., Diolez, P., Susín, S. A., Zamzami, N., & Kroemer, G. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)00318-4 · Cited by 290 · see citing works
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
Polarographic assay and intracellular distribution of superoxide dismutase in rat liver.
Tyler, D. D. (1975) · Biochemical Journal · doi:10.1042/bj1470493 · Cited by 247 · see citing works
Koya, R. C., Fujita, H., Shimizu, S., Ohtsu, M., Takimoto, M., Tsujimoto, Y., & Kuzumaki, N. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.20.15343 · Cited by 246 · see citing works
Castilho, R. F., Kowaltowski, A. J., Meinicke, A., Bechara, E. J. H., & Vercesi, A. E. (1995) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(94)00166-h · Cited by 244 · see citing works
Pardo, J., Bosque, A., Brehm, R., Wallich, R., Naval, J., Müllbacher, A., Anel, A., & Simon, M. M. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200406115 · Cited by 157 · see citing works
Subcellular localization of superoxide dismutase in rat liver
Peeters-Joris, C., Am, V., & Baudhuin, P. (1975) · Biochemical Journal · doi:10.1042/bj1500031 · Cited by 154 · see citing works
Reactive Oxygen Species Produced by Liver Mitochondria of Rats in Sepsis
Taylor, D. E., Ghio, A. J., & Piantadosi, C. A. (1995) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1995.1011 · Cited by 147 · see citing works
[3] Aconitases: A class of metalloproteins highly sensitive to nitric oxide synthesis
Drapier, J., & Hibbs, J. B. (1996) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(96)69006-5 · Cited by 145 · see citing works
Superoxide Inhibits 4Fe-4S Cluster Enzymes Involved in Amino Acid Biosynthesis
Wallace, M. A., Liou, L.-L., Martins, J., Clement, M. H. S., Bailey, S., Longo, V. D., Valentine, J. S., & Gralla, E. B. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m403590200 · Cited by 98 · see citing works
Effect of thyroid state on H2O2 production by rat liver mitochondria
Venditti, P., Rosa, R. D., & Meo, S. D. (2003) · Molecular and Cellular Endocrinology · doi:10.1016/s0303-7207(02)00332-5 · Cited by 91 · see citing works
Guidot, D. M., Repine, J. E., Kitlowski, A. D., Flores, S. C., Nelson, S. K., Wright, R. M., & McCord, J. M. (1995) · Journal of Clinical Investigation · doi:10.1172/jci118100 · Cited by 81 · see citing works
Disulphide formation on mitochondrial protein thiols.
Hurd, T., Filipovska, A., Costa, N. J., Dahm, C., & Murphy, M. P. (2005) · Biochemical Society Transactions · doi:10.1042/bst0331390 · Cited by 70 · see citing works
Redox Regulation of the Mitochondrial Permeability Transition Pore
Chernyak, B. V. (1997) · Bioscience Reports · doi:10.1023/a:1027384628678 · Cited by 69 · see citing works
Superoxide from Glucose Oxidase or from Nitroblue Tetrazolium?
Liochev, S. I., & Fridovich, I. (1995) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1995.1247 · Cited by 62 · see citing works
Redox activation of mitochondrial intermembrane space Cu,Zn-superoxide dismutase
Iñarrea, P., Moini, H., Rettori, D., Han, D., MARTÍNEZ, J., García‐Rubio, I., Fernández‐Vizarra, E., Iturralde, M., & Cadenas, E. (2005) · Biochemical Journal · doi:10.1042/bj20041683 · Cited by 59 · see citing works
Self-citationDistribution of protein disulphide isomerase in rat liver mitochondria
Rigobello, M. P., Donella‐Deana, A., Cesaro, L., & Bindoli, A. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3560567 · Cited by 55 · see citing works
Inhibition of Erythrocyte Selenium-Glutathione Peroxidase by Auranofin Analogues and Metabolites
Roberts, J. R., & Shaw, C. F. (1998) · Biochemical Pharmacology · doi:10.1016/s0006-2952(97)00634-5 · Cited by 37 · see citing works
Distribution of protein disulphide isomerase in rat liver mitochondria
Rigobello, M. P., Donella‐Deana, A., Cesaro, L., et al. (2001) · Biochemical Journal · doi:10.1042/bj3560567 · Cited by 34 · see citing works
Cross-compartment protection by SOD1
Liochev, S. I., & Fridovich, I. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.10.017 · Cited by 32 · see citing works
Localization of a sulphate-activating system within Euglena mitochondria
Saidha, T., Stern, A. I., Lee, D. H., & Schiff, J. A. (1985) · Biochemical Journal · doi:10.1042/bj2320357 · Cited by 27 · see citing works
In vivo formation of Cu,Zn superoxide dismutase disulfide bond in Escherichia coli
Battistoni, A., Mazzetti, A. P., & Rotilio, G. (1999) · FEBS Letters · doi:10.1016/s0014-5793(98)01725-6 · Cited by 24 · see citing works
Rotilo, G., Calabrese, L., Finazzi‐Agrò, A., Argento‐Cerù, M. P., Autuori, F., & Mondovı̀, B. (1973) · Biochimica et Biophysica Acta (BBA) - Enzymology · doi:10.1016/0005-2744(73)90063-6 · Cited by 22 · see citing works
Iñarrea, P. (2002) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(02)49326-3 · Cited by 17 · see citing works
Self-citation
Flagged first, then by citations
Research works printed but not linked: 1
- Gardner, P. R., and White, C. W. (1995) In The Oxygen Paradox (Davies, K. J. A., and Ursini, F., eds.), pp. 33-50, Cleup University Press, Padova.
Cited by
Sorted by citations
Focus on mammalian thioredoxin reductases — Important selenoproteins with versatile functions
Arnér, E. S. J. (2009) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2009.01.014 · Cited by 675 · see citing works
Stowe, D. F., & Camara, A. K. S. (2009) · Antioxidants & Redox Signaling · doi:10.1089/ars.2008.2331 · Cited by 471 · see citing works
Mitochondrial Regulation of Cell Cycle and Proliferation
Arciuch, V. G. A., Elguero, M. E., Poderoso, J. J., & Carreras, M. C. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4085 · Cited by 428 · see citing works
Mitochondrial metabolism of reactive oxygen species
Venditti, P., Stefano, L. D., & Meo, S. D. (2013) · Mitochondrion · doi:10.1016/j.mito.2013.01.008 · Cited by 346 · 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
Glutathione peroxidases in different stages of carcinogenesis
Brigelius‐Flohé, R., & Kipp, A. P. (2009) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2009.03.006 · Cited by 303 · see citing works
Chen, Q., Moghaddas, S., Hoppel, C. L., & Lesnefsky, E. J. (2008) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00211.2007 · Cited by 299 · see citing works
Hardeland, R. (2013) · Journal of Pineal Research · doi:10.1111/jpi.12090 · Cited by 285 · see citing works
Lee, H., & Wei, Y. (2011) · Advances in experimental medicine and biology · doi:10.1007/978-94-007-2869-1_14 · Cited by 201 · see citing works
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
Stanley, B. A., Sivakumaran, V., Shi, S., McDonald, I., Lloyd, D., Watson, W. H., Aon, M. A., & Paolocci, N. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.284612 · Cited by 197 · see citing works
Potential Therapeutic Benefits of Strategies Directed to Mitochondria
Camara, A. K. S., Lesnefsky, E. J., & Stowe, D. F. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2788 · Cited by 195 · see citing works
Is there more to aging than mitochondrial DNA and reactive oxygen species?
ALEXEYEV, M. F. (2009) · FEBS Journal · doi:10.1111/j.1742-4658.2009.07269.x · Cited by 194 · see citing works
Principles in Redox Signaling: From Chemistry to Functional Significance
Bindoli, A., & Rigobello, M. P. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4655 · Cited by 189 · see citing works
Leeuwenburgh, C., Pamplona, R., & Sanz, A. (2011) · Journal of Aging Research · doi:10.4061/2011/782946 · Cited by 186 · see citing works
Thioredoxin Reductase Inhibition for Cancer Therapy
Gencheva, R., & Arnér, E. S. J. (2021) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-052220-102509 · Cited by 178 · see citing works
Cox, A. G., Brown, K., Arnér, E. S. J., & Hampton, M. B. (2008) · Biochemical Pharmacology · doi:10.1016/j.bcp.2008.08.021 · Cited by 164 · see citing works
Mitochondrial protein tyrosine nitration
Castro, L., Demicheli, V., Tórtora, V., & Radí, R. (2010) · Free Radical Research · doi:10.3109/10715762.2010.516254 · Cited by 100 · see citing works
Ježek, P., & Plecitá‐Hlavatá, L. (2009) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2009.02.014 · Cited by 100 · 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
Mitochondria as targets for cancer therapy
Ralph, S. J., & Neužil, J. (2009) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.200800044 · Cited by 97 · see citing works
Auranofin: Past to Present, and repurposing
Yamashita, M. (2021) · International Immunopharmacology · doi:10.1016/j.intimp.2021.108272 · Cited by 92 · see citing works
Ježek, P., Plecitá‐Hlavatá, L., Smolková, K., & Rossignol, R. (2009) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2009.11.008 · Cited by 91 · see citing works
Malińska, D., Kulawiak, B., Kudin, A. P., Kovacs, R., Huchzermeyer, C., Kann, O., Szewczyk, A. M., & Kunz, W. S. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.03.001 · Cited by 90 · see citing works
Pereira, C. V., Nadanaciva, S., Oliveira, P. J., & Will, Y. (2012) · Expert Opinion on Drug Metabolism & Toxicology · doi:10.1517/17425255.2012.645536 · Cited by 85 · see citing works
Activation of the lifespan regulator p66 Shc through reversible disulfide bond formation
Gertz, M., Fischer, F. F., Wolters, D. A., & Steegborn, C. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0800691105 · Cited by 82 · see citing works
Tikunov, A. P., Johnson, C. B., Pediaditakis, P., Markevich, N. I., Macdonald, J. M., Lemasters, J. J., & Holmuhamedov, E. (2010) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2010.01.008 · Cited by 74 · see citing works
Thiol switches in mitochondria: operation and physiological relevance
Riemer, J., Schwarzländer, M., Conrad, M., & Herrmann, J. M. (2015) · Biological Chemistry · doi:10.1515/hsz-2014-0293 · Cited by 58 · see citing works
Geldon, S., Fernández‐Vizarra, E., & Tokatlidis, K. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.720656 · Cited by 55 · see citing works
Mutant SOD1 from spinal cord of G93A rats is destabilized and binds to inner mitochondrial membrane
Ahtoniemi, T., Jaronen, M., Keksa-Goldsteine, V., Goldsteins, G., & Koıstınaho, J. (2008) · Neurobiology of Disease · doi:10.1016/j.nbd.2008.08.010 · Cited by 51 · see citing works
Gencheva, R., Cheng, Q., & Arnér, E. S. J. (2022) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2022.07.020 · Cited by 46 · see citing works
An Adaptation to Low Copper in Candida albicans Involving SOD Enzymes and the Alternative Oxidase
Broxton, C. N., & Culotta, V. C. (2016) · PLOS ONE · doi:10.1371/journal.pone.0168400 · Cited by 41 · see citing works
Khalimonchuk, O., & Winge, D. R. (2007) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2007.10.016 · Cited by 39 · see citing works
Skeletal muscle aging: Role of reactive oxygen species
Jackson, M. J. (2009) · Critical Care Medicine · doi:10.1097/ccm.0b013e3181b6f97f · Cited by 38 · see citing works
Mechanism-based Proteomic Screening Identifies Targets of Thioredoxin-like Proteins
Nakao, L. S., Everley, R. A., Marino, S. M., Lo, S. M., de Souza, L. E. R., Gygi, S. P., & Gladyshev, V. N. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.597245 · Cited by 37 · see citing works
Berberine and S allyl cysteine mediated amelioration of DEN+CCl4 induced hepatocarcinoma
Sengupta, D., Chowdhury, K. D., Sarkar, A., Paul, S., & Sadhukhan, G. C. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.08.020 · Cited by 32 · see citing works
Iñarrea, P., Casanova, A., Álava, M. A., Iturralde, M., & Cadenas, E. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.03.003 · Cited by 30 · see citing works
Self-citationAcetylation in Mitochondria Dynamics and Neurodegeneration
Waddell, J., Banerjee, A., & Kristián, T. (2021) · Cells · doi:10.3390/cells10113031 · Cited by 27 · see citing works
Methylglyoxal induces mitochondria-dependent apoptosis in sarcoma
Ghosh, A., Bera, S., Ray, S., Banerjee, T., & Ray, M. (2011) · Biochemistry (Moscow) · doi:10.1134/s0006297911100105 · Cited by 27 · see citing works
Pardo, M., & Tirosh, O. (2009) · Free Radical Research · doi:10.3109/10715760903271256 · Cited by 24 · see citing works
Yan, J., Xu, J., Fei, Y., Jiang, C., Zhu, W., Han, Y., & Lu, S. (2016) · Experimental Cell Research · doi:10.1016/j.yexcr.2016.04.014 · Cited by 24 · see citing works
Hirasaka, K., Lago, C. U., Kenaston, M. A., Fathe, K., Nowinski, S. M., Nikawa, T., & Mills, E. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.3888 · Cited by 24 · see citing works
Kurosawa, T., Nakamura, H., Yamaura, E., Fujino, H., Matsuzawa, Y., Kawashima, T., & Murayama, T. (2009) · Journal of Cellular Physiology · doi:10.1002/jcp.21703 · Cited by 24 · see citing works
Yon, J., Baek, I., Lee, S.-R., Jin, Y., Kim, M., Nahm, S., Kim, J.-S., Ahn, B., Lee, B. J., Yun, Y. W., et al. (2007) · Journal of Molecular Histology · doi:10.1007/s10735-007-9134-1 · Cited by 23 · see citing works
p66Shc aging protein in control of fibroblasts cell fate
Suski, J. M., Karkucinska-Wieckowska, A., Lebiedzinska, M., Giorgi, C., Szczepanowska, J., Szabadkai, G., Duszynski, J., Pronicki, M., Pinton, P., & Wieckowski, M. R. (2011) · International Journal of Molecular Sciences · doi:10.3390/ijms12085373 · Cited by 22 · see citing works
Single-lung ventilation and oxidative stress
Heerdt, P. M., & Stowe, D. F. (2016) · Current Opinion in Anaesthesiology · doi:10.1097/aco.0000000000000410 · Cited by 22 · see citing works
Role of NAD+—Modulated Mitochondrial Free Radical Generation in Mechanisms of Acute Brain Injury
Klimova, N., Fearnow, A. D., & Kristián, T. (2020) · Brain Sciences · doi:10.3390/brainsci10070449 · Cited by 21 · see citing works
Identification of potential biomarkers for predicting acute dermal irritation by proteomic analysis
Zhang, Q., Dai, T., Zhang, L., Zhang, M., Xiao, X., Hu, H., Zou, P., Liu, X., Xiang, Q., Su, Z., et al. (2011) · Journal of Applied Toxicology · doi:10.1002/jat.1630 · Cited by 19 · see citing works
Sensing Hypoxia by Mitochondria: A Unifying Hypothesis Involving S-Nitrosation
Ullrich, V., & Schildknecht, S. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4788 · Cited by 18 · see citing works
Perspectives of TrxR1-based cancer therapies
Arnér, E. S. J. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-818606-0.00031-6 · Cited by 17 · see citing works
Crane, M. S., Howie, A. F., Arthur, J. R., Nicol, F., Crosley, L. K., & Beckett, G. J. (2009) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2009.07.001 · Cited by 17 · see citing works
Xu, X. M., Chen, C., Arriaga, E. A., & Thompson, L. V. (2010) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00174.2010 · Cited by 14 · see citing works
In vitro comprehensive analysis of VA692 a new chemical entity for the treatment of osteoarthritis
Cheleschi, S., Calamia, V., Fernández-Moreno, M., Biava, M., Giordani, A., Fioravanti, A., Anzini, M., & Blanco, F. J. (2018) · International Immunopharmacology · doi:10.1016/j.intimp.2018.08.025 · Cited by 14 · see citing works
Effect of a Deficiency of Ceruloplasmin Copper in Blood Plasma on Copper Metabolism in the Brain
Babich, P. S., Васильевна, Ц. Н., Klotchenko, S. A., Платонова, Н. А., Масалова, О. О., Zatulovskiy, E. A., Шавловский, М. М., Сапронов, Н. С., & Puchkova, L. V. (2009) · Bulletin of Experimental Biology and Medicine · doi:10.1007/s10517-010-0772-z · Cited by 10 · see citing works
Wang, X., Gong, J., Liu, X., Zhan, R., Kong, R., Zhao, Y., Wan, D., Leng, X., Chen, M., & Qian, L. (2010) · Cell Stress and Chaperones · doi:10.1007/s12192-010-0185-y · Cited by 10 · see citing works
Mitochondrial transplant: Unravelling a promising treatment for ocular diseases
Yeo, Y., Bhargava, M., Khare, R. S., Parikh, B. H., & Su, X. (2025) · Redox Biology · doi:10.1016/j.redox.2025.103902 · Cited by 6 · see citing works
Xiao, R., Spangler, L., Routt, K., Lan, Z., Johnson, C. A., Prolla, T. A., & Power, R. F. (2014) · Functional Foods in Health and Disease · doi:10.31989/ffhd.v4i3.22 · Cited by 2 · see citing works
Mitochondria as Targets for Cancer Therapy
Ralph, S. J., & Neužil, J. (2008) · Springer eBooks · doi:10.1007/978-0-387-84835-8_12 · Cited by 2 · see citing works
Nogami, A., Amemiya, H. J., Fujiwara, H., Umezawa, Y., Tohda, S., & Nagao, T. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms251910372 · Cited by 1 · see citing works
Wu, T., Hossain, M. N., Hattori, M., & Nagai, T. (2025) · Talanta · doi:10.1016/j.talanta.2025.127576 · Cited by 1 · see citing works
Ovarian Biomarkers in Infertility
Vangelov, I., Dineva, J. D., Todorova, K. O., Hayrabedyan, S., & Maria, D. P. D. S. J. (2012) · InTech eBooks · doi:10.5772/35912 · Cited by 1 · see citing works
Elements of the Cosmos as Precursors for Lifeforms
Stowe, D. F. (2025) · Springer eBooks · doi:10.1007/978-3-031-76668-8_1 · Cited by 1 · see citing works
Reactive Oxygen and Nitrogen Species Signaling in Mitochondria
(2009) · CRC Press eBooks · doi:10.1201/9781420073751.ch3 · Cited by 1 · see citing works
Impact Of Copper, Zinc Superoxide Dismutase Knockout On Lipid Metabolism In Mice
Wang, S. (2009) · eCommons (Cornell University) · Cited by 1 · see citing works
SOD Enzymes in a Human Fungal Pathogen: Oxidative Stress Protection Versus Cellular Signaling
Broxton, C. N. (2017) · Cited by 1 · see citing works
Chen, Q., Moghaddas, S., Hoppel, C. L., & Lesnefsky, E. J. (2007) · Mitochondrion · doi:10.1016/j.mito.2007.08.075
Kinases and Mitochondrial Cycling
Carreras, M. C., & Poderoso, J. J. (2012) · Oxidative stress and disease · doi:10.1201/b12308-13
ROS and RNS Signaling in Apoptosis
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Callegari, M. A., dos Santos, P. P., Monte, M. G., Dorna, M. D. S., Tonon, C. R., Minicucci, M. F., Zornoff, L. A. M., Azevedo, P. S., Polegato, B. F., & de Paiva, S. A. R. (2026) · Research Square · doi:10.21203/rs.3.rs-9784587/v1
- Authors
- Iñarrea, P., Moini, H., Han, D., Rettori, D., Aguiló, I., Alava, M. A., Iturralde, M., & Cadenas, E.
- Affiliations
- Universidad de Zaragoza (ES)
- University of Southern California (US)
- Departamento de Bioquímica y Biología Molecular y Celular, Facultad de Ciencias, Universidad de Zaragoza, 50009-Zaragoza, Spain
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 2007-06-13
- Volume
- 405
- Issue
- 1
- Pages
- 173-179
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- PMC
- PMC1925252
- OpenAlex
- W1813348676
- Cited by
- 73
- References
- 33
- Citations by year
- 2026: 2 · 2025: 4 · 2024: 1 · 2022: 2 · 2021: 4 · 2020: 1 · 2019: 1 · 2018: 1 · 2017: 1 · 2016: 3 · 2015: 3 · 2014: 2 · 2013: 3 · 2012: 6
- FWCI
- 3.84
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Biochemical Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion, other-oa)
- Trinity's Access to Research Output (TARA) (Trinity College Dublin) (submittedVersion, other-oa)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glutathione Transferases and Polymorphisms
- Keywords
- SOD1, Cu/Zn superoxide dismutase, intermembrane space, thioredoxin reductase 1, mitochondrial respiratory chain, superoxide, hydrogen peroxide, peroxiredoxin III, aconitase, cytochrome c release, mitochondrial membrane potential, apoptosis, mitochondrial bioenergetics, thiol oxidation, liver mitochondria
- MeSH terms
- Superoxide Dismutase-1, Aconitate Hydratase, Animals, Antimycin A, Electron Transport, Energy Metabolism, Enzyme Activation, Hydrogen Peroxide, Male, Membrane Potentials, Mitochondria, Liver, Superoxides, Superoxide Dismutase, Thioredoxin-Disulfide Reductase, Oxidants, Rats, Wistar, Apoptosis, Cell Respiration, Cytochromes c, Rats
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