Control of mitochondrial redox balance and cellular defense against oxidative damage by mitochondrial NADP+-dependent isocitrate dehydrogenase
Open accessAbstract
Mitochondria are the major organelles that produce reactive oxygen species (ROS) and the main target of ROS-induced damage as observed in various pathological states including aging. Production of NADPH required for the regeneration of glutathione in the mitochondria is critical for scavenging mitochondrial ROS through glutathione reductase and peroxidase systems. We investigated the role of mitochondrial NADP(+)-dependent isocitrate dehydrogenase (IDPm) in controlling the mitochondrial redox balance and subsequent cellular defense against oxidative damage. We demonstrate in this report that IDPm is induced by ROS and that decreased expression of IDPm markedly elevates the ROS generation, DNA fragmentation, lipid peroxidation, and concurrent mitochondrial damage with a significant reduction in ATP level. Conversely, overproduction of IDPm protein efficiently protected the cells from ROS-induced damage. The protective role of IDPm against oxidative damage may be attributed to increased levels of a reducing equivalent, NADPH, needed for regeneration of glutathione in the mitochondria. Our results strongly indicate that IDPm is a major NADPH producer in the mitochondria and thus plays a key role in cellular defense against oxidative stress-induced damage.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Alternatively, substrate flow through the TCA cycle differs depending on substrates, which might affect the activity of NADP+-dependent isocitrate dehydrogenase and malic enzyme.
“Alternatively, the substrate flow through the TCA cycle differs depending on the substrates, which might affect the activity of the other two mitochondrial NADPH-regenerating enzymes the NADP + -dependent isocitrate dehydrogenase [119,120] and the malic enzyme [118,121].”
From Differential effects of complex II on mitochondrial ROS production and their relation to cardioprotective pre- and postconditioning (2013) · cites this paper as [120]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Aebi, H. (1984) · Methods in Enzymology · doi:10.1016/s0076-6879(84)05016-3 · Cited by 25,696 · see citing works
[30] Microsomal lipid peroxidation
Buege, J. A., & Aust, S. D. (1978) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(78)52032-6 · Cited by 13,437 · see citing works
Marklund, S. L., & MARKLUND, G. (1974) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1974.tb03714.x · Cited by 10,382 · see citing works
Green, D. R., & Reed, J. C. (1998) · Science · doi:10.1126/science.281.5381.1309 · Cited by 8,998 · see citing works
Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes
Esterbauer, H., Schaur, R. J., & Zollner, H. (1991) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(91)90192-6 · Cited by 6,672 · see citing works
Oxidants, antioxidants, and the degenerative diseases of aging.
Ames, B. N., Shigenaga, M. K., & Hagen, T. M. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.17.7915 · Cited by 5,958 · see citing works
Hydroperoxide metabolism in mammalian organs.
Chance, B., Sies, H., & Boveris, A. (1979) · Physiological Reviews · doi:10.1152/physrev.1979.59.3.527 · Cited by 5,827 · see citing works
Molecular characterization of mitochondrial apoptosis-inducing factor
Susin, S. A., Lorenzo, H. K., Zamzami, N., Marzo, I., Snow, B. E., Brothers, G. M., Mangion, J., Jacotot, E., Costantini, P., Loeffler, M., et al. (1999) · Nature · doi:10.1038/17135 · Cited by 4,060 · see citing works
Schreck, R., RIEBER, P., & Baeuerle, P. A. (1991) · The EMBO Journal · doi:10.1002/j.1460-2075.1991.tb07761.x · Cited by 3,816 · see citing works
Bcl-2 functions in an antioxidant pathway to prevent apoptosis
Hockenbery, D. M., Oltvai, Z. N., Yin, X., Milliman, C. L., & Korsmeyer, S. J. (1993) · Cell · doi:10.1016/0092-8674(93)80066-n · Cited by 3,420 · see citing works
[70] Determination of glutathione and glutathione disulfide in biological samples
Anderson, M. E. (1985) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(85)13073-9 · Cited by 2,755 · see citing works
Sundaresan, M., Yu, Z.-X., Ferrans, V. J., Irani, K., & Finkel, T. (1995) · Science · doi:10.1126/science.270.5234.296 · Cited by 2,520 · see citing works
Production of high-titer helper-free retroviruses by transient transfection.
Pear, W. S., Nolan, G. P., Scott, M. L., & Baltimore, D. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.18.8392 · Cited by 2,267 · see citing works
Improved retroviral vectors for gene transfer and expression.
Miller, A. D., & Rosman, G. J. (1989) · PubMed · Cited by 1,990 · see citing works
Bass, D., Parce, J. W., DeChatelet, L. R., Szejda, P., Seeds, M. C., & Thomas, M. (1983) · The Journal of Immunology · doi:10.4049/jimmunol.130.4.1910 · Cited by 1,811 · see citing works
Monoclonal Antibody-Mediated Tumor Regression by Induction of Apoptosis
Trauth, B. C., Klas, C., Peters, A. M. J., Matzku, S., Mӧller, P., Falk, W., Debatin, K., & Krammer, P. H. (1989) · Science · doi:10.1126/science.2787530 · Cited by 1,716 · see citing works
Jiang, Z. Y., Hunt, J. V., & Wolff, S. P. (1992) · Analytical Biochemistry · doi:10.1016/0003-2697(92)90122-n · Cited by 1,624 · see citing works
Akerboom, T. P. M., & Sies, H. (1981) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(81)77050-2 · Cited by 1,580 · see citing works
Lemasters, J. J., Nieminen, A.-L., Qian, T., Trost, L. C., Elmore, S. P., Nishimura, Y., Crowe, R. A., Cascio, W. E., Bradham, C. A., Brenner, D. A., et al. (1998) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(98)00112-1 · Cited by 1,387 · see citing works
Superoxide dismutase as a target for the selective killing of cancer cells
Huang, P., Li, F., Oldham, E. A., Keating, M. J., & Plunkett, W. K. (2000) · Nature · doi:10.1038/35030140 · Cited by 842 · see citing works
García‐Ruiz, C., Colell, A., Marı́, M., Morales, A., & Fernández-Checa, J. C. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.17.11369 · Cited by 808 · see citing works
Michikawa, Y., Mazzucchelli, F., Bresolin, N., Scarlato, G., & Attardi, G. M. (1999) · Science · doi:10.1126/science.286.5440.774 · Cited by 725 · see citing works
Mitochondrial Release of Caspase-2 and -9 during the Apoptotic Process
Susín, S. A., Lorenzo, H. K., Zamzami, N., Marzo, I., Brenner, C., Larochette, N., Prévost, M., Alzari, P. M., & Kroemer, G. (1999) · The Journal of Experimental Medicine · doi:10.1084/jem.189.2.381 · Cited by 710 · see citing works
Kang, S. W., Chae, H. Z., Seo, M. S., Kim, K., Baines, I., & Rhee, S. G. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.11.6297 · Cited by 693 · see citing works
Role of mitochondria in oxidative stress and ageing
Lenaz, G. (1998) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(98)00120-0 · Cited by 650 · see citing works
Mitochondrial disease in mouse results in increased oxidative stress
Esposito, L., Melov, S., Panov, A. V., Cottrell, B. A., & Wallace, D. C. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.9.4820 · Cited by 637 · see citing works
Goossens, V., Grooten, J., Vos, K. J. D., & Fiers, W. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.18.8115 · Cited by 595 · see citing works
Lo, Y. Y. C., & Cruz, T. F. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.20.11727 · Cited by 530 · see citing works
Origin and turnover of mitochondrial glutathione.
Griffith, O. W., & Meister, A. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.14.4668 · Cited by 500 · see citing works
Reactive Oxygen Species Regulate Activation-Induced T Cell Apoptosis
Hildeman, D. A., Mitchell, T., Teague, T. K., Henson, P. M., Day, B. J., Kappler, J. W., & Marrack, P. (1999) · Immunity · doi:10.1016/s1074-7613(00)80072-2 · Cited by 483 · see citing works
Murakami, K., Kondo, T., 川瀬, 誠., Li, Y., Sato, S., Chen, S. F., & Chan, P. H. (1998) · Journal of Neuroscience · doi:10.1523/jneurosci.18-01-00205.1998 · Cited by 467 · see citing works
Differential regulation of antioxidant enzymes in response to oxidants.
Shull, S., Heintz, N. H., Periasamy, M., Manohar, M., Janssen, Y. M., Marsh, J. P., & Mossman, B. T. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54242-3 · Cited by 403 · see citing works
Perspectives on Oxygen Sensing
Semenza, G. L. (1999) · Cell · doi:10.1016/s0092-8674(00)81957-1 · Cited by 385 · see citing works
Pinto, R., & Bartley, W. (1969) · Biochemical Journal · doi:10.1042/bj1120109 · Cited by 378 · see citing works
Salvemini, F., Franzè, A., Iervolino, A., Filosa, S., Salzano, S., & Ursini, M. V. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.5.2750 · Cited by 333 · see citing works
Arai, M., Imai, H., Koumura, T., Yoshida, M., Emoto, K., Umeda, M., Chiba, N., & Nakagawa, Y. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.8.4924 · Cited by 296 · see citing works
Nomura, K., Imai, H., Koumura, T., Arai, M., & Nakagawa, Y. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.41.29294 · Cited by 285 · see citing works
Mårtensson, J., Lai, J. C. K., & Meister, A. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.18.7185 · Cited by 282 · see citing works
Spragg, R. G., Hinshaw, D. B., Hyslop, P. A., Schraufstätter, I. U., & Cochrane, C. G. (1985) · Journal of Clinical Investigation · doi:10.1172/jci112126 · Cited by 265 · see citing works
Knoops, B., Clippe, A., Bogard, C., Arsalane, K., Wattiez, R., Hermans, C. R. J. R., Duconseille, E., Falmagne, P., & Bernard, A. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.43.30451 · Cited by 245 · see citing works
Zerez, C. R., Lee, S. J., & Tanaka, K. R. (1987) · Analytical Biochemistry · doi:10.1016/0003-2697(87)90506-9 · Cited by 180 · see citing works
Self-citationInvolvement of Sphingosine in Mitochondria-dependent Fas-induced Apoptosis of Type II Jurkat T Cells
Cuvillier, O., Edsall, L. C., & Spiegel, S. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000280200 · Cited by 176 · see citing works
Retention of oxidized glutathione by isolated rat liver mitochondria during hydroperoxide treatment
Ólafsdóttir, K. B., & Reed, D. J. (1988) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(88)90038-4 · Cited by 169 · see citing works
TheGpx1Gene Encodes Mitochondrial Glutathione Peroxidase in the Mouse Liver
Esworthy, R. S., Ho, Y., & Chu, F. (1997) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1997.9901 · Cited by 165 · see citing works
Function and expression of yeast mitochondrial NAD- and NADP-specific isocitrate dehydrogenases
Haselbeck, R. J., & McAlister-Henn, L. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)50315-5 · Cited by 160 · see citing works
The Rat Quinone Reductase Antioxidant Response Element
Favreau, L. V., & Pickett, C. B. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.41.24468 · Cited by 152 · see citing works
Cupp, J. R., & McAlister-Henn, L. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54554-3 · Cited by 141 · see citing works
Ravindranath, V., & Reed, D. J. (1990) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(90)92004-j · Cited by 134 · see citing works
Antioxidant Function of the Mitochondrial Protein SP-22 in the Cardiovascular System
Araki, M., Nanri, H., 江島, 邦., Murasato, Y., Fujiwara, T., Nakashima, Y., & Ikeda, M. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.4.2271 · Cited by 128 · see citing works
Vogel, R., Wiesinger, H., Hamprecht, B., & Dringen, R. (1999) · Neuroscience Letters · doi:10.1016/s0304-3940(99)00748-x · Cited by 115 · see citing works
Isotopomer Analysis of Citric Acid Cycle and Gluconeogenesis in Rat Liver
Rosiers, C. D., Donato, L. D., Comte, B., Laplante, A., Marcoux, C., David, F., Fernandez, C. A., & Brunengraber, H. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.17.10027 · Cited by 114 · see citing works
Packer, L., Maguire, J. J., Mehlhorn, R. J., et al. (1989) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(89)92427-3 · Cited by 96 · see citing works
Biochemistry of Metabolic Processes
Mowbray, J. (1983) · FEBS Letters · doi:10.1016/0014-5793(83)81083-7 · Cited by 93 · see citing works
Shan, X., Jones, D. P., Hashmi, M., & Anders, M. W. (1993) · Chemical Research in Toxicology · doi:10.1021/tx00031a012 · Cited by 86 · see citing works
Stein, A. M., Stein, J. H., & Kirkman, S. K. (1967) · Biochemistry · doi:10.1021/bi00857a020 · Cited by 64 · see citing works
Watabe, S., Hasegawa, H., Takimoto, K., et al. (1995) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1995.2229 · Cited by 61 · see citing works
García‐Ruiz, C., Morales, A., Colell, A., et al. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.27.15946 · Cited by 55 · see citing works
Matteo, M. A. D., Loweth, A. C., Thomas, S., Mabley, J. G., Morgan, N. G., Thorpe, J. R., & Green, I. C. (1997) · APOPTOSIS · doi:10.1023/a:1026412414666 · Cited by 54 · see citing works
Kim, Y., Koh, H., Kim, S.-H., et al. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.52.36866 · Cited by 53 · see citing works
Self-citationHaselbeck, R. J., Colman, R. F., & McAlister-Henn, L. (1992) · Biochemistry · doi:10.1021/bi00142a007 · Cited by 51 · see citing works
Huh, T., Ryu, J., Huh, J., et al. (1993) · Biochemical Journal · doi:10.1042/bj2920705 · Cited by 37 · see citing works
SUBCELLULAR DISTRIBUTION OF ISOCITRATE DEHYDROGENASES IN NEONATAL AND ADULT MOUSE BRAIN
Loverde, A. W., & Lehrer, G. M. (1973) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1973.tb12143.x · Cited by 37 · see citing works
Musgrove, E. A., Šarčević, B., & Sutherland, R. L. (1996) · Journal of Cellular Biochemistry · doi:10.1002/(sici)1097-4644(19960301)60:3 · Cited by 37 · see citing works
Oh, I.-U., Inazawa, J., Kim, Y., et al. (1996) · Genomics · doi:10.1006/geno.1996.0602 · Cited by 28 · see citing works
Self-citationHuh, T., Kim, Y., Oh, I.-U., et al. (1996) · Genomics · doi:10.1006/geno.1996.0120 · Cited by 23 · see citing works
Self-citationRadiation Sensitivity of anEscherichia coliMutant Lacking NADP+-Dependent Isocitrate Dehydrogenase
Lee, S. M., Koh, H., Huh, T., et al. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.0125 · Cited by 20 · see citing works
Self-citationYang, L., Luo, H., Vinay, P., & Wu, J. (1996) · PubMed · doi:10.1002/(sici)1097-4644(19960301)60:3%3c400::aid-jcb11%3e3.0.co;2-o · Cited by 16 · see citing works
Kim, Y., Park, S.-H., Kang, Y.-W., et al. (1999) · Cytogenetic and Genome Research · doi:10.1159/000015348 · Cited by 12 · see citing works
Self-citationLund, L. G., Paraidathathu, T., & Kehrer, J. P. (1994) · Toxicology · doi:10.1016/0300-483x(94)90082-5 · Cited by 11 · see citing works
Flagged first, then by citations
Research works printed but not linked: 8
- Ames, B. N., Shigenaga, M. K., and Hagen, T. M. (1993) Proc. Natl. Acad. Sci.
- Esposito, L. A., Melov, S., Panov, A., Cottrell, B. A., and Wallace, D. C. (1999) Proc. Natl. Acad. Sci. U. S. A. 96, 4820 -4825
- Goossens, V., Grooten, J., De Vos, K., and Fiers, W. (1995) Proc. Natl. Acad. Sci. U. S. A. 92, 8115-8119
- Griffith, O. W., and Meister, A. (1985) Proc. Natl. Acad. Sci. U. S. A. 82, 4668 -4672
- Martensson, J., Lai, J. C. K., and Meister, A. (1990) Proc. Natl. Acad. Sci.
- Plaut, G. W. E., and Gabriel, J. L. (1983) Biochemistry of Metabolic Process, pp. 285-301, Elsevier Science Publishing Co., Inc., New York
- Pear, W. S., Nolan, G. P., Scott, M. L., and Baltimore, D. (1993) Proc. Natl. Acad. Sci. U. S. A. 90, 8392-8396
- Kehrer, J. P., Paraidathathu, T., and Lund, L. G. (1993) Proc. West. Pharma- col. Soc. 36, 45-52
Cited by
Sorted by citations
The Role of Oxidative Stress in Parkinson's Disease
Dias, V., Junn, E., & Mouradian, M. M. (2013) · Journal of Parkinson’s Disease · doi:10.3233/jpd-130230 · Cited by 1,845 · see citing works
Ying, W. (2008) · Antioxidants & Redox Signaling · doi:10.1089/ars.2007.1672 · Cited by 1,494 · see citing works
Someya, S., Yu, W., Hallows, W. C., Xu, J., Vann, J. M., Leeuwenburgh, C., Tanokura, M., Denu, J. M., & Prolla, T. A. (2010) · Cell · doi:10.1016/j.cell.2010.10.002 · Cited by 1,150 · see citing works
Mitochondria and reactive oxygen species
Kowaltowski, A. J., de Souza-Pinto, N. C., Castilho, R. F., & Vercesi, A. E. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.05.004 · Cited by 1,162 · see citing works
Cogswell, J. P., Ward, J., Taylor, I. A., Waters, M., Shi, Y., Cannon, B., Kelnar, K., Kemppainen, J., Brown, D., Chen, C., et al. (2008) · Journal of Alzheimer s Disease · doi:10.3233/jad-2008-14103 · Cited by 943 · see citing works
Alcohol and mitochondria: a dysfunctional relationship
Hoek, J. B., Cahill, A., & Pastorino, J. G. (2002) · Gastroenterology · doi:10.1053/gast.2002.33613 · Cited by 553 · see citing works
Quantifying Reductive Carboxylation Flux of Glutamine to Lipid in a Brown Adipocyte Cell Line
Yoo, H., Antoniewicz, M. R., Stephanopoulos, G., & Kelleher, J. K. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m706494200 · Cited by 301 · see citing works
Dröse, S. (2013) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2013.01.004 · Cited by 201 · see citing works
2-Hydroxyglutarate in Cancer Cells
Ježek, P. (2020) · Antioxidants & Redox Signaling · doi:10.1089/ars.2019.7902 · Cited by 130 · see citing works
Tian, G., Sawashita, J., Kubo, H., Nishio, S.-Y., Hashimoto, S., Suzuki, N., Yoshimura, H., Tsuruoka, M., Wang, Y., Liu, Y., et al. (2014) · Antioxidants & Redox Signaling · doi:10.1089/ars.2013.5406 · Cited by 123 · see citing works
Song, B.-J., Akbar, M., Abdelmegeed, M. A., Byun, K., Lee, B., Yoon, S. K., & Hardwick, J. P. (2014) · Redox Biology · doi:10.1016/j.redox.2014.10.004 · Cited by 123 · see citing works
Self-citationCeccarelli, C., Grodsky, N. B., Ariyaratne, N., Colman, R. F., & Bahnson, B. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207306200 · Cited by 116 · see citing works
Multifunctional Mitochondrial Epac1 Controls Myocardial Cell Death
Fazal, L., Laudette, M., Paula-Gomes, S., Pons, S., Conte, C., Tortosa, F., Sicard, P., Sainte-Marie, Y., Bisserier, M., Lairez, O., et al. (2017) · Circulation Research · doi:10.1161/circresaha.116.309859 · Cited by 111 · see citing works
Suh, S., Hood, B. L., Kim, B., Conrads, T. P., Veenstra, T. D., & Song, B. J. (2004) · PROTEOMICS · doi:10.1002/pmic.200400971 · Cited by 76 · see citing works
Self-citation
- Authors
- Jo, S.-H., Son, M.-K., Koh, H.-J., Lee, S.-M., Song, I.-H., Kim, Y.-O., Lee, Y.-S., Jeong, K.-S., Kim, W. B., Park, J.-W., Song, B. J., & Huhe, T.-L.
- Affiliations
- Kyungpook National University (KR)
- Yeungnam University (KR)
- National Institutes of Health (US)
- Dong-A Pharmaceutical (South Korea) (KR)
- Corresponding author
- Huhe, Tae-Lin
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2001-05
- Volume
- 276
- Issue
- 19
- Pages
- 16168-16176
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2131960328
- Cited by
- 536
- References
- 69
- Citations by year
- 2026: 10 · 2025: 15 · 2024: 15 · 2023: 18 · 2022: 8 · 2021: 34 · 2020: 34 · 2019: 33 · 2018: 32 · 2017: 29 · 2016: 21 · 2015: 19 · 2014: 25 · 2013: 24 · 2012: 23
- FWCI
- 6.13
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- Korea Science and Engineering Foundation
- National Institutes of Health
- 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
- Health Sciences › Medicine › Pathology and Forensic Medicine › Cardiac Ischemia and Reperfusion
- Keywords
- NADP-isocitrate dehydrogenase, mitochondrial redox balance, reactive oxygen species, oxidative stress, NADPH production, glutathione regeneration, glutathione reductase, lipid peroxidation, DNA fragmentation, mitochondrial damage, ATP depletion, aging
- MeSH terms
- Amino Acid Sequence, Animals, Antibodies, Cattle, Cell Survival, Cloning, Molecular, Glutathione Peroxidase, Glutathione Reductase, Homeostasis, Humans, Isocitrate Dehydrogenase, Kinetics, Mitochondria, Molecular Sequence Data, Oxidation-Reduction, Peptide Fragments, Recombinant Proteins, Superoxide Dismutase, Swine, Sequence Alignment, 3T3 Cells, Apoptosis, Reactive Oxygen Species, Sequence Homology, Amino Acid, Oxidative Stress, Mice, DNA Fragmentation
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review