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Dilated cardiomyopathy and neonatal lethality in mutant mice lacking manganese superoxide dismutase
Abstract
The Sod2 gene for Mn-superoxide dismutase (MnSOD), an intramitochondrial free radical scavenging enzyme that is the first line of defense against superoxide produced as a byproduct of oxidative phosphorylation, was inactivated by homologous recombination. Homozygous mutant mice die within the first 10 days of life with a dilated cardiomyopathy, accumulation of lipid in liver and skeletal muscle, and metabolic acidosis. Cytochemical analysis revealed a severe reduction in succinate dehydrogenase (complex II) and aconitase (a TCA cycle enzyme) activities in the heart and, to a lesser extent, in other organs. These findings indicate that MnSOD is required for normal biological function of tissues by maintaining the integrity of mitochondrial enzymes susceptible to direct inactivation by superoxide.
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“Primary mechanisms of nitrated fatty acid signaling include activation of PPARγ (55, 583) and Michael addition to thiol-containing proteins in a number of signaling pathways (53, 955).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [583]
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“Its deficiency causes early neonatal death in knockout mice, which suffer from dilated cardiomyopathy and neurodegeneration (236, 252).”
From Redox regulation of mitochondrial function (2012) · cites this paper as [252]
In the citing paper
“Sod2−/− mice die before birth”
From Mitochondrial reactive oxygen species regulate cellular signaling and dictate biological outcomes (2010) · cites this paper as [88]
In the citing paper
“their heterozygous littermates exhibit mitochondrial damage and oxidative modifications to both nuclear and mitochondrial DNA”
From Mitochondrial reactive oxygen species regulate cellular signaling and dictate biological outcomes (2010) · cites this paper as [88]
In the citing paper
“However, these heterozygous mice have a normal lifespan 88, 89.”
From Mitochondrial reactive oxygen species regulate cellular signaling and dictate biological outcomes (2010) · cites this paper as [88]
Citations
Cites
Orr, W. C., & Sohal, R. S. (1994) · Science · doi:10.1126/science.8108730 · Cited by 1,461
NMDA-dependent superoxide production and neurotoxicity
Lafon‐Cazal, M., Pietri, S., Culcasi, M., & Bockaert, J. (1993) · Nature · doi:10.1038/364535a0 · Cited by 1,183
The oxidant stress hypothesis in Parkinson's disease: Evidence supporting it
Fahn, S., & Cohen, G. (1992) · Annals of Neurology · doi:10.1002/ana.410320616 · Cited by 927
Bourgeron, T., Rustin, P., Chretien, D., Birch-Machin, M., Bourgeois, M., Viegas-Péquignot, E., Munnich, A., & Rötig, A. (1995) · Nature Genetics · doi:10.1038/ng1095-144 · Cited by 730
The oxidative inactivation of mitochondrial electron transport chain components and ATPase.
Zhang, Y., Marcillat, O., Giulivi, C., Ernster, L., & Davies, K. J. A. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)46227-2 · Cited by 719
Kinouchi, H., Epstein, C. J., Mizui, T., Carlson, E. J., Chen, S. F., & Chan, P. H. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.24.11158 · Cited by 589
Self-citationKu, H., Brunk, U. T., & Sohal, R. S. (1993) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(93)90165-q · Cited by 488
Church, S. L., Grant, J. W., Ridnour, L. A., Oberley, L. W., Swanson, P. E., Meltzer, P. S., & Trent, J. M. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.7.3113 · Cited by 474
Borgstahl, G. E. O., Parge, H. E., Hickey, M. J., Beyer, W. F., Hallewell, R. A., & Tainer, J. A. (1992) · Cell · doi:10.1016/0092-8674(92)90270-m · Cited by 472
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 469
Flagged first, then by citations
Research works printed but not linked: 1
- Fridovich, I. Measuring the activity of superoxide dismutase: an embarrassment of riches. In Superoxide Dismutase 1 (ed. Oberley, C.W.) 69–77 (CRC Press, Boca Raton 1982).
Cited by
Sorted by citations
Items 601–700 of 1,002
Mayeux, P. R., & MacMillan-Crow, L. A. (2012) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2012.01.004 · Cited by 74
Huang, H., Guo, F., Cao, Y., Shi, W., & Xia, Q. (2012) · CNS Neuroscience & Therapeutics · doi:10.1111/j.1755-5949.2012.00380.x · Cited by 73
Proteomic analysis of autoantibodies in patients with hepatocellular carcinoma
高島, 元., Kuramitsu, Y., Yokoyama, Y., Iizuka, N., HARADA, T., Fujimoto, M., Sakaida, I., Okita, K., Oka, M., & Nakamura, K. (2006) · PROTEOMICS · doi:10.1002/pmic.200500346 · Cited by 73
Kapnick, S. M., Pacheco, S. E., & McGuire, P. J. (2017) · Metabolism · doi:10.1016/j.metabol.2017.11.010 · Cited by 76
Hawgood, S. B., Ochs, M., Jung, A., Akiyama, J. A., Allen, L., Brown, C., Edmondson, J., Levitt, S., Carlson, E. J., Gillespie, A. M., et al. (2002) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00118.2002 · Cited by 74
Self-citationHeusch, P., Canton, M., Aker, S., van de Sand, A., Konietzka, I., Rassaf, T., Menazza, S., Brodde, O. E., Lisa, F. D., Heusch, G., et al. (2010) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2010.00793.x · Cited by 72
Mitochondrial Superoxide Dismutase - Signals of Distinction
Miriyala, S., Holley, A. K., & Clair, D. K. S. (2011) · Anti-Cancer Agents in Medicinal Chemistry · doi:10.2174/187152011795255920 · Cited by 74
Montagner, G. F. F. D. S., Sagrillo, M. R., Machado, M. M., de Almeida, R. C., Mostardeiro, C. P., Duarte, M. M. M. F., & da Cruz, I. B. M. (2010) · Toxicology in Vitro · doi:10.1016/j.tiv.2010.04.010 · Cited by 72
Runko, A. P., Griswold, A. J., & Min, K. (2008) · FEBS Letters · doi:10.1016/j.febslet.2008.01.046 · Cited by 72
Pathophysiological mechanisms of TNF during intoxication with natural or man-made toxins
Schümann, J., & Tiegs, G. (1999) · Toxicology · doi:10.1016/s0300-483x(99)00087-6 · Cited by 72
Fujii, M. (1998) · DNA Research · doi:10.1093/dnares/5.1.25 · Cited by 72
Invertebrate gerontology: The age mutations of Caenorhabditis elegans
Lithgow, G. J. (1996) · BioEssays · doi:10.1002/bies.950181007 · Cited by 72
mtDNA Mutations and Their Role in Aging, Diseases and Forensic Sciences
Zapico, S. C. (2013) · Aging and Disease · doi:10.14336/ad.2013.0400364 · Cited by 78
Belluzzi, E., Bisaglia, M., Lazzarini, E., Tabares, L. C., Beltramini, M., & Bubacco, L. (2012) · PLoS ONE · doi:10.1371/journal.pone.0038026 · Cited by 74
Is the Val16Ala Manganese Superoxide Dismutase Polymorphism Associated With the Aging Process?
Taufer, M., Peres, A., de Andrade, V. M., de Oliveira, G., Sá, G., do Canto, M. E. P., dos Santos, A. R., Bauer, M. E., & da Cruz, I. B. M. (2005) · The Journals of Gerontology Series A · doi:10.1093/gerona/60.4.432 · Cited by 71
Lambert, A. J., Buckingham, J. A., Boysen, H. M., & Brand, M. D. (2009) · Aging Cell · doi:10.1111/j.1474-9726.2009.00538.x · Cited by 70
Models of reactive oxygen species in cancer
Lu, W., Ogasawara, M. A., & Huang, P. (2007) · Drug Discovery Today Disease Models · doi:10.1016/j.ddmod.2007.10.005 · Cited by 72
Protective Mechanisms of Mitochondria and Heart Function in Diabetes
Aon, M. A., Tocchetti, C. G., Bhatt, N., Paolocci, N., & Cortassa, S. C. (2015) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.6123 · Cited by 71
Mitochondria and Cardiac Hypertrophy.
Facundo, H. D. T. F., Brainard, R. E., Caldas, F. R. D. L., & Lucas, A. M. B. (2017) · Advances in Experimental Medicine and Biology · doi:10.1007/978-3-319-55330-6_11 · Cited by 70
Guo, Z., Boekhoudt, G. H., & Boss, J. M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m303431200 · Cited by 75
Wang, C., Chen, S., Yeo, S., Karsli-Uzunbas, G., White, E., Mizushima, N., Virgin, H. W., & Guan, J.-L. (2016) · Journal of Cell Biology · doi:10.1083/jcb.201507023 · Cited by 69
Boas, S. M., Joyce, K. L., & Cowell, R. M. (2021) · Antioxidants · doi:10.3390/antiox11010008 · Cited by 70
Reactive Oxygen Species: Angels and Demons in the Life of a Neuron
Biswas, K., Alexander, K. D., & Francis, M. M. (2022) · NeuroSci · doi:10.3390/neurosci3010011 · Cited by 74
Mahfouz, M. E. (2015) · Molecular Biology · doi:10.1134/s0026893315020089 · Cited by 69
Kakko, S., Päivänsalo, M. J., Koistinen, P., Kesäniemi, Y. A., Kinnula, V. L., & Savolainen, M. J. (2003) · Atherosclerosis · doi:10.1016/s0021-9150(03)00091-1 · Cited by 69
Dong, P., Pan, L., Zhang, X., Zhang, W., Wang, X., Jiang, M., Chen, Y., Duan, Y., Wu, H., Xu, Y., et al. (2017) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2017.01.040 · Cited by 71
Andreini, C., Rosato, A., & Banci, L. (2017) · PLoS ONE · doi:10.1371/journal.pone.0171279 · Cited by 73
Ahn, B., Ranjit, R., Premkumar, P., Pharaoh, G. A., Piekarz, K. M., Matsuzaki, S., Claflin, D. R., Riddle, K., Judge, J., Bhaskaran, S., et al. (2019) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12375 · Cited by 70
The role of Bcl6 in mature cardiac myocytes
Yoshida, T. (1999) · Cardiovascular Research · doi:10.1016/s0008-6363(99)00007-3 · Cited by 69
Huang, Y., He, T., & Domann, F. E. (1999) · DNA and Cell Biology · doi:10.1089/104454999315051 · Cited by 69
Cellular Senescence: Ageing and Androgenetic Alopecia
Deng, Y., Wang, M., He, Y., Liu, F., Chen, L., & Xia, X. (2023) · Dermatology · doi:10.1159/000530681 · Cited by 68
Lijnen, P. J., van Pelt, J. F., & Fagard, R. H. (2010) · Cardiovascular Therapeutics · doi:10.1111/j.1755-5922.2010.00205.x · Cited by 70
Evidence for differential alternative splicing in blood of young boys with autism spectrum disorders
Stamova, B. S., Tian, Y., Nordahl, C. W., Shen, M. D., Rogers, S. J., Amaral, D. G., & Sharp, F. R. (2013) · Molecular Autism · doi:10.1186/2040-2392-4-30 · Cited by 70
Ocular pathology in mitochondrial superoxide dismutase (Sod2)-deficient mice.
Sandbach, J., Coscun, P. E., GROSSNIKLAUS, H. E., Kokoszka, J. E., Newman, N. J., & Wallace, D. C. (2001) · PubMed · Cited by 68
Self-citationTherapeutics against Mitochondrial Oxidative Stress in Animal Models of Aging
Melov, S. (2002) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2002.tb02104.x · Cited by 68
Self-citationFatty Streak Formation in Fat-Fed Mice Expressing Human Copper-Zinc Superoxide Dismutase
Tribble, D. L., Gong, E. L., Leeuwenburgh, C., Heinecke, J. W., Carlson, E. J., Verstuyft, J. G., & Epstein, C. J. (1997) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.17.9.1734 · Cited by 68
Self-citationExpression of Antioxidant Enzymes in Astrocytic Brain Tumors
Haapasalo, H. K., Kyläniemi, M., Paunu, N., Kinnula, V. L., & Soini, Y. (2003) · Brain Pathology · doi:10.1111/j.1750-3639.2003.tb00015.x · Cited by 69
Interactions of reactive sulfur species with metalloproteins
Domán, A., Dóka, É., Garai, D., Bogdándi, V., Balla, G., Balla, J., & Nagy, P. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102617 · Cited by 68
Mitochondria and Oxidative Stress in the Cardiorenal Metabolic Syndrome
Aroor, A. R., Mandavia, C. H., Ren, J. T., Sowers, J. R., & Pulakat, L. (2012) · Cardiorenal Medicine · doi:10.1159/000335675 · Cited by 67
Inactivation of Pyruvate Dehydrogenase Kinase 2 by Mitochondrial Reactive Oxygen Species
Hurd, T. R., Collins, Y., Abakumova, I., Chouchani, E. T., Baranowski, B., Fearnley, I. M., Prime, T. A., Murphy, M. P., & James, A. M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.400002 · Cited by 70
Apoptosis: A Two‐edged Sword in Aging
Warner, H. R. (1999) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1999.tb07917.x · Cited by 67
Discovery of superoxide reductase: an historical perspective
Nivière, V., & Fontecave, M. (2004) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-003-0519-7 · Cited by 72
George, S. K., Jiao, Y., Bishop, C. E., & Lu, B. (2011) · Aging Cell · doi:10.1111/j.1474-9726.2011.00686.x · Cited by 66
Robb, E. L., & Stuart, J. A. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.12.038 · Cited by 68
Oxidative stress and aging inCaenorhabditis elegans
Ishii, N. (2000) · Free Radical Research · doi:10.1080/10715760000301371 · Cited by 66
An active mitochondrial biogenesis occurs during dendritic cell differentiation
Zaccagnino, P., Saltarella, M., Maiorano, S., Gaballo, A., Santoro, G., Nico, B., Lorusso, M. P., & Prete, A. D. (2012) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2012.07.024 · Cited by 65
Benayoun, B. A., Batista, F., Auer, J., Dipietromaria, A., L’Hôte, D., Baere, E. B. W. D., & Veitia, R. A. (2008) · Human Molecular Genetics · doi:10.1093/hmg/ddn389 · Cited by 70
Mitochondrially-targeted treatment strategies
Bozi, L. H. M., Campos, J. C., Zambelli, V. O., Ferreira, N. D., & Ferreira, J. C. B. (2019) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2019.100836 · Cited by 67
Takada, Y., Hachiya, M., Park, S., Osawa, Y., Ozawa, T., & Akashi, M. (2002) · PubMed · Cited by 65
Crow, J. P. (1999) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(99)01078-2 · Cited by 65
Revisiting an age-old question regarding oxidative stress
Edrey, Y. H., & Salmon, A. B. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.03.038 · Cited by 64
Manganese superoxide dismutase vs. p53: Regulation of mitochondrial ROS
Holley, A. K., Dhar, S. K., & Clair, D. K. S. (2010) · Mitochondrion · doi:10.1016/j.mito.2010.06.003 · Cited by 65
Intracellular Na+ and cardiac metabolism
Bay, J., Kohlhaas, M., & Maack, C. (2013) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2013.05.010 · Cited by 66
Sesamin ameliorates doxorubicin-induced cardiotoxicity: Involvement of Sirt1 and Mn-SOD pathway
Su, S., Li, Q., Liu, Y., Chen, X., Li, J., Zhang, R., Niu, Y., Zhao, L., Wang, Y., & Guo, H. (2013) · Toxicology Letters · doi:10.1016/j.toxlet.2013.10.034 · Cited by 64
Wigner, P., Czarny, P. L., Gałecki, P., Su, K., & Śliwiński, T. (2017) · Psychiatry Research · doi:10.1016/j.psychres.2017.09.045 · Cited by 65
Lack of Myoglobin Causes a Switch in Cardiac Substrate Selection
Flögel, U., Laußmann, T., Gödecke, A., Abanador-Kamper, N., Schäfers, M. A., Fingas, C. D., Metzger, S. U., Levkau, B., Jacoby, C., & Schrader, J. (2005) · Circulation Research · doi:10.1161/01.res.0000165481.36288.d2 · Cited by 64
Oxidative stress and superoxide dismutase in development, aging and gene regulation
Allen, R. G. (1998) · AGE · doi:10.1007/s11357-998-0007-7 · Cited by 64
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Mapuskar, K. A., Steinbach, E. J., Zaher, A., Riley, D. P., Beardsley, R. A., Keene, J. L., Holmlund, J., Anderson, C. M., Zepeda‐Orozco, D., Buatti, J. M., et al. (2021) · Antioxidants · doi:10.3390/antiox10091329 · Cited by 63
Aquilano, K., Vigilanza, P., Rotilio, G., & Ciriolo, M. R. (2006) · The FASEB Journal · doi:10.1096/fj.05-5225fje · Cited by 64
Watanabe, K., Shibuya, S., Ozawa, Y., Nojiri, H., Izuo, N., Yokote, K., & Shimizu, T. (2014) · BioMed Research International · doi:10.1155/2014/140165 · Cited by 63
How genetic analysis tests theories of animal aging
Hekimi, S. (2006) · Nature Genetics · doi:10.1038/ng1881 · Cited by 63
Cottrell, D. A., & Turnbull, D. M. (2000) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/00075197-200011000-00009 · Cited by 64
Irazusta, V. P., Cabiscol, E., Reverter‐Branchat, G., Ros, J., & Tamarit, J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m511649200 · Cited by 63
The Mitochondrial Theory of Aging
Kowald, A. (2001) · Neurosignals · doi:10.1159/000046885 · Cited by 63
Model mice for tissue‐specific deletion of the manganese superoxide dismutase gene
Shimizu, T., Nojiri, H., Kawakami, S., Uchiyama, S., & Shirasawa, T. (2010) · Geriatrics and gerontology international/Geriatrics & gerontology international · doi:10.1111/j.1447-0594.2010.00604.x · Cited by 62
The redox regulation of intermediary metabolism by a superoxide–aconitase rheostat
Armstrong, J. S., Whiteman, M., Yang, H., & Jones, D. P. (2004) · BioEssays · doi:10.1002/bies.20071 · Cited by 61
Gill, T., & Levine, A. D. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.476895 · Cited by 61
Mitochondrial Reactive Oxygen Species in Mice Lacking Superoxide Dismutase 2
Morten, K., Ackrell, B. A. C., & Melov, S. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m509261200 · Cited by 61
Self-citationCatalytic Antioxidants and Neurodegeneration
Golden, T. R., & Patel, M. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2256 · Cited by 62
Zhang, R., Chae, S., Lee, J. H., & Hyun, J. W. (2012) · Journal of Cellular Biochemistry · doi:10.1002/jcb.24068 · Cited by 61
The anti-cancer drug doxorubicin induces substantial epigenetic changes in cultured cardiomyocytes
Hanf, A., Oelze, M. W., Manea, A., Li, H., Münzel, T. F., & Daiber, A. (2019) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2019.108834 · Cited by 61
Prevention of mitochondrial dysfunction in post‐traumatic mouse brain by superoxide dismutase
Xiong, Y., Shie, F., Zhang, J., Lee, C.-P., & Ho, Y. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03412.x · Cited by 61
Kameritsch, P., Singer, M. S., Nuernbergk, C., Ríos, N., Reyes, A. M., Schmidt, K., Kirsch, J., Schneider, H., Müller, S., Pogoda, K., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1921828118 · Cited by 60
Decreased Superoxide Production in Macrophages of Long-lived p66Shc Knock-out Mice
Tomilov, A. A., Bicocca, V. T., Schoenfeld, R. A., Giorgio, M., Migliaccio, E., Ramsey, J. J., Hagopian, K., Pelicci, P. G., & Cortopassi, G. A. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.017491 · Cited by 60
Ganini, D., Santos, J. H., Bonini, M. G., & Mason, R. P. (2018) · Cell Chemical Biology · doi:10.1016/j.chembiol.2018.01.007 · Cited by 59
Liu, S., Yeh, T.-H., Singh, V. P., Shiva, S., Krauland, L., Li, H., Zhang, P., Kharbanda, K., Ritov, V., Monga, S. P. S., et al. (2012) · Hepatology · doi:10.1002/hep.24766 · Cited by 59
Celotto, A. M., Liu, Z., VanDemark, A. P., & Palladino, M. J. (2012) · Brain and Behavior · doi:10.1002/brb3.73 · Cited by 59
Negative air ions created by water shearing improve erythrocyte deformability and aerobic metabolism
Iwama, H. (2004) · Indoor Air · doi:10.1111/j.1600-0668.2004.00254.x · Cited by 59
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Perry, J. J. P., Hearn, A. S., Cabelli, D. E., Nick, H. S., Tainer, J. A., & Silverman, D. N. (2009) · Biochemistry · doi:10.1021/bi8023288 · Cited by 59
Marcu, R., Zheng, Y. Y., & Hawkins, B. J. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-55330-6_21 · Cited by 60
Zemanovic, S., Ivanov, M. V., Ivanova, L. V., Bhatnagar, A., Michalkiewicz, T., Teng, R., Kumar, S. N., Rathore, R., Pritchard, K. A., Konduri, G. G., et al. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.11.015 · Cited by 59
Ambivalent role of BCL6 in cell survival and transformation
Albagli, O. (2003) · Oncogene · doi:10.1038/sj.onc.1206152 · Cited by 59
Lee, S. J., Choi, M. G., Kim, D. S., & Kim, T. W. (2005) · Metabolism · doi:10.1016/j.metabol.2005.04.030 · Cited by 59
Marino, A., Battaglini, M., Desii, A., Lavarello, C., Genchi, G. G., Petretto, A., & Ciofani, G. (2021) · Biomaterials Science · doi:10.1039/d1bm01202a · Cited by 58
Cytochrome peroxidase contributes to the antioxidant defense of
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de Paula, W. B. M., Lucas, C. H., Agip, A.-N. A., Vizcay‐Barrena, G., & Allen, J. F. (2013) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2012.0263 · Cited by 59
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Riemer, J., Schwarzländer, M., Conrad, M., & Herrmann, J. M. (2015) · Biological Chemistry · doi:10.1515/hsz-2014-0293 · Cited by 58
miR-23a Regulates Cardiomyocyte Apoptosis by Targeting Manganese Superoxide Dismutase
Long, B., Gan, T., Zhang, R., & Zhang, Y.-H. (2017) · Molecules and Cells · doi:10.14348/molcells.2017.0012 · Cited by 61
Daiber, A., Steven, S., Vujačić-Mirski, K., Kalinovic, S., Oelze, M. W., Lisa, F. D., & Münzel, T. F. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21103405 · Cited by 59
Marelja, Z., Leimkühler, S., & Missirlis, F. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.00050 · Cited by 61
Soo, S. K., Rudich, Z. D., Ko, B., Moldakozhayev, A., AlOkda, A., & Raamsdonk, J. M. V. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.101941 · Cited by 58
Mitochondria and the aging heart
Chaudhary, K. R., El-Sikhry, H. E., & Seubert John, M. (2011) · 老年心脏病学杂志:英文版 · doi:10.3724/sp.j.1263.2011.00159 · Cited by 57
Mele, J., Remmen, H. V., Vijg, J., & Richardson, A. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.628 · Cited by 57
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Metadata
- Authors
- 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., Wallace, D. C., & Epstein, C. J.
- Affiliations
- University of California, San Francisco (US)
- Emory University (US)
- Children's Medical Research Institute (AU)
- Venue
- Nature Genetics
- Published
- 1995-12
- Volume
- 11
- Issue
- 4
- Pages
- 376-381
- ISSN
- 1061-4036 (ISSN-L)
- 1546-1718
- OpenAlex
- W2094655287
- Cited by
- 1,789
- References
- 32
- Citations by year
- 2026: 20 · 2025: 35 · 2024: 23 · 2023: 31 · 2022: 32 · 2021: 48 · 2020: 39 · 2019: 36 · 2018: 42 · 2017: 52 · 2016: 58 · 2015: 62 · 2014: 102 · 2013: 87 · 2012: 101
- FWCI
- 9.79
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Genetics (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute on Aging (P30AG010130, AG-10130, AG-13154, AG-08938, P01AG008938, R01AG013154)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Metabolism and Genetic Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Keywords
- manganese superoxide dismutase, dilated cardiomyopathy, neonatal lethality, mitochondrial superoxide, oxidative phosphorylation, succinate dehydrogenase, complex II, aconitase, TCA cycle, lipid accumulation, metabolic acidosis, Sod2 knockout mice
- MeSH terms
- Acidosis, Animals, Animals, Newborn, Base Sequence, Cardiomyopathy, Dilated, Electron Transport Complex IV, Genes, Lethal, Homozygote, Lipids, Liver, Mice, Mutant Strains, Mitochondria, Heart, Mitochondria, Muscle, Molecular Sequence Data, Succinate Dehydrogenase, Superoxide Dismutase, Lipid Peroxidation, Sequence Deletion, Gene Targeting, Muscle, Skeletal, Mice
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