Alpha-ketoglutarate dehydrogenase: a target and generator of oxidative stress
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Alpha-ketoglutarate dehydrogenase (α-KGDH) is a highly regulated enzyme, which could determine the metabolic flux through the Krebs cycle. It catalyses the conversion of α-ketoglutarate to succinyl-CoA and produces NADH directly providing electrons for the respiratory chain. α-KGDH is sensitive to reactive oxygen species (ROS) and inhibition of this enzyme could be critical in the metabolic deficiency induced by oxidative stress. Aconitase in the Krebs cycle is more vulnerable than α-KGDH to ROS but as long as α-KGDH is functional NADH generation in the Krebs cycle is maintained. NADH supply to the respiratory chain is limited only when α-KGDH is also inhibited by ROS. In addition being a key target, α-KGDH is able to generate ROS during its catalytic function, which is regulated by the NADH/NAD + ratio. The pathological relevance of these two features of α-KGDH is discussed in this review, particularly in relation to neurodegeneration, as an impaired function of this enzyme has been found to be characteristic for several neurodegenerative diseases.
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Other mitochondrial proteins, including the TCA cycle enzymes α-KGDH and aconitase, are especially sensitive to oxidative inactivation.
“Other mitochondrial proteins, including the TCA cycle enzymes α-KGDH and aconitase, are especially sensitive to oxidative inactivation (423).”
From Redox regulation of mitochondrial function (2012) · cites this paper as [423]
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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
Mitochondrial formation of reactive oxygen species
Turrens, J. F. (2003) · The Journal of Physiology · doi:10.1113/jphysiol.2003.049478 · Cited by 5,084 · see citing works
Oxidative Stress, Glutamate, and Neurodegenerative Disorders
Coyle, J. T., & Puttfarcken, P. (1993) · Science · doi:10.1126/science.7901908 · Cited by 3,762 · see citing works
Reactive Oxygen Species and the Central Nervous System
Halliwell, B. (1992) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1992.tb10990.x · Cited by 2,947 · see citing works
Boveris, A., & Chance, B. (1973) · Biochemical Journal · doi:10.1042/bj1340707 · Cited by 2,626 · see citing works
Mitochondrial Complex I Deficiency in Parkinson's Disease
Schapira, A. H. V., Cooper, J. M., Dexter, D., Clark, J. B., Jenner, P., & Marsden, C. D. (1990) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1990.tb02325.x · Cited by 2,283 · see citing works
MITOCHONDRIAL COMPLEX I DEFICIENCY IN PARKINSON'S DISEASE
Schapira, A. H. V., Cooper, J. A. D., Dexter, D. T., Jenner, P. G., Clark, J. B., & MARSDEN, C. D. (1989) · The Lancet · doi:10.1016/s0140-6736(89)92366-0 · Cited by 1,757 · see citing works
Korshunov, S. S., Skulachev, V. P., & Starkov, A. A. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)01159-9 · Cited by 1,727 · see citing works
Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria
Turrens, J. F., & Boveris, A. (1980) · Biochemical Journal · doi:10.1042/bj1910421 · Cited by 1,601 · see citing works
The cellular production of hydrogen peroxide
Boveris, A., Oshino, N., & Chance, B. (1972) · Biochemical Journal · doi:10.1042/bj1280617 · Cited by 1,549 · see citing works
Generation of reactive oxygen species by the mitochondrial electron transport chain
Liu, Y., Fiskum, G., & Schubert, D. (2002) · Journal of Neurochemistry · doi:10.1046/j.0022-3042.2002.00744.x · Cited by 1,260 · see citing works
The Role of Zinc in Selective Neuronal Death After Transient Global Cerebral Ischemia
Koh, J., Suh, S. W., Gwag, B. J., He, Y. Y., Hsu, C. Y., & Choi, D. W. (1996) · Science · doi:10.1126/science.272.5264.1013 · Cited by 1,070 · see citing works
Abnormalities of the electron transport chain in idiopathic parkinson's disease
Parker, W. D., Boyson, S. J., & Parks, J. K. (1989) · Annals of Neurology · doi:10.1002/ana.410260606 · Cited by 1,061 · see citing works
The importance of free radicals and catalytic metal ions in human diseases.
Halliwell, B., & Gutteridge, J. M. C. (1985) · Molecular Aspects of Medicine · doi:10.1016/0098-2997(85)90001-9 · Cited by 941 · see citing works
Cadenas, E., Boveris, A., Ragan, C. I., & Stoppani, A. O. M. (1977) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(77)90035-2 · Cited by 855 · see citing works
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
Mark, R. J., Lovell, M. A., Markesbery, W. R., Uchida, K., & Mattson, M. P. (1997) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1997.68010255.x · Cited by 781 · see citing works
Reynolds, I., & Hastings, T. (1995) · The Journal of Neuroscience · doi:10.1523/jneurosci.15-05-03318.1995 · Cited by 777 · see citing works
A radical hypothesis for neurodegeneration
Olanow, C. W. (1993) · Trends in Neurosciences · doi:10.1016/0166-2236(93)90070-3 · Cited by 722 · see citing works
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 713 · 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
Bolli, R., Patel, B. S., Jeroudi, M. O., Lai, E. K., & McCay, P. B. (1988) · Journal of Clinical Investigation · doi:10.1172/jci113621 · Cited by 685 · see citing works
Role of ubiquinone in the mitochondrial generation of hydrogen peroxide
Boveris, A., Cadenas, E., & Stoppani, A. O. M. (1976) · Biochemical Journal · doi:10.1042/bj1560435 · Cited by 655 · see citing works
Superoxide radicals as precursors of mitochondrial hydrogen peroxide
Loschen, G., Azzi, A., Richter, C., & Flohé, L. (1974) · FEBS Letters · doi:10.1016/0014-5793(74)80281-4 · Cited by 634 · see citing works
Experimental models of Parkinson's disease
Beal, M. F. (2001) · Nature reviews. Neuroscience · doi:10.1038/35072550 · Cited by 634 · see citing works
Votyakova, T. V., & Reynolds, I. J. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00548.x · Cited by 601 · see citing works
White, R. J., & Reynolds, I. J. (1996) · Journal of Neuroscience · doi:10.1523/jneurosci.16-18-05688.1996 · Cited by 592 · see citing works
Zn2+: a novel ionic mediator of neural injury in brain disease
Weiss, J. H., Sensi, S. L., & Koh, J. Y. (2000) · Trends in Pharmacological Sciences · doi:10.1016/s0165-6147(00)01541-8 · Cited by 575 · see citing works
Stimulation by calcium ions of pyruvate dehydrogenase phosphate phosphatase
Denton, R. M., Randle, P. J., & Martin, B. R. (1972) · Biochemical Journal · doi:10.1042/bj1280161 · Cited by 542 · see citing works
Ambrosio, G., Zweier, J. L., Duilio, C., Kuppusamy, P., Santoro, G., Elia, P. P., Tritto, I., Cirillo, P. L., Condorelli, M., & Chiariello, M. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)46660-9 · Cited by 515 · see citing works
Regulation of brain mitochondrial H 2 O 2 production by membrane potential and NAD(P)H redox state
Starkov, A. A., & Fiskum, G. M. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01908.x · Cited by 491 · see citing works
β‐Amyloid inhibits integrated mitochondrial respiration and key enzyme activities
Casley, C. S., Canevari, L., Land, J. M., Clark, J. B., & Sharpe, M. A. (2001) · Journal of Neurochemistry · doi:10.1046/j.0022-3042.2001.00681.x · Cited by 485 · see citing works
Superoxide Radical and Iron Modulate Aconitase Activity in Mammalian Cells
Gardner, P. R., Raineri, I., Epstein, L. B., & White, C. W. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.22.13399 · Cited by 471 · see citing works
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
Self-citationMcCORMACK, J. G., & Denton, R. M. (1979) · Biochemical Journal · doi:10.1042/bj1800533 · Cited by 453 · see citing works
Requirement for Superoxide in Excitotoxic Cell Death
Patel, M., Day, B. J., Crapo, J. D., Fridovich, I., & McNamara, J. O. (1996) · Neuron · doi:10.1016/s0896-6273(00)80052-5 · Cited by 436 · see citing works
Oxygen free radical involvement in ischemia and reperfusion injury to brain
Cao, W., Carney, J. M., Duchon, A., Floyd, R. A., & Chevion, M. (1988) · Neuroscience Letters · doi:10.1016/0304-3940(88)90132-2 · Cited by 430 · see citing works
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
Gibson, G. E., Sheu, K. ‐. R., Blass, J. P., Baker, A., Carlson, K., Harding, B. N., & Perrino, P. (1988) · Archives of Neurology · doi:10.1001/archneur.1988.00520320022009 · Cited by 425 · see citing works
Tretter, L., & Ádám‐Vizi, V. (2000) · Journal of Neuroscience · doi:10.1523/jneurosci.20-24-08972.2000 · Cited by 422 · see citing works
Self-citationMitochondria, free radicals, and neurodegeneration
Beal, M. F. (1996) · Current Opinion in Neurobiology · doi:10.1016/s0959-4388(96)80100-0 · Cited by 422 · see citing works
Sensi, S. L., Yin, H. Z., Carriedo, S. G., Rao, S. S., & Weiss, J. H. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.5.2414 · Cited by 408 · see citing works
Modulation of Mitochondrial Function by Hydrogen Peroxide
Nulton-Persson, A. C., & Szweda, L. I. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100320200 · Cited by 393 · see citing works
On the role of the calcium transport cycle in heart and other mammalian mitochondria
Denton, R. M., & McCormack, J. G. (1980) · FEBS Letters · doi:10.1016/0014-5793(80)80986-0 · Cited by 388 · see citing works
Denton, R. M., Richards, D. A. R., & Chin, J. (1978) · Biochemical Journal · doi:10.1042/bj1760899 · Cited by 375 · see citing works
Zinc inhibition of cellular energy production: implications for mitochondria and neurodegeneration
Dineley, K. E., Votyakova, T. V., & Reynolds, I. J. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01678.x · Cited by 363 · see citing works
Humphries, K. M., & Szweda, L. I. (1998) · Biochemistry · doi:10.1021/bi981512h · Cited by 357 · 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
Ca2+-dependent changes in the mitochondrial energetics in single dissociated mouse sensory neurons
Duchen, M. R. (1992) · Biochemical Journal · doi:10.1042/bj2830041 · Cited by 338 · see citing works
Hyslop, P. A., Zhang, Z., Pearson, D. V., & Phebus, L. A. (1995) · Brain Research · doi:10.1016/0006-8993(94)01291-o · Cited by 335 · see citing works
Harris‐White, M. E., Hensley, K., Butterfield, D. A., Leedle, R. A., & Carney, J. M. (1995) · Experimental Neurology · doi:10.1016/0014-4886(95)90041-1 · Cited by 331 · see citing works
Schapira, A. H. V. (1999) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(98)00164-9 · Cited by 310 · see citing works
Lai, J. C. K., & Cooper, A. J. L. (1986) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1986.tb00768.x · Cited by 307 · see citing works
Tønder, N., Johansen, F. F., Frederickson, C. J., Zimmer, J., & Diemer, N. H. (1990) · Neuroscience Letters · doi:10.1016/0304-3940(90)90002-q · Cited by 301 · see citing works
Takeshige, K., & Minakami, S. (1979) · Biochemical Journal · doi:10.1042/bj1800129 · Cited by 299 · see citing works
SYNAPTIC AND NON‐SYNAPTIC MITOCHONDRIA FROM RAT BRAIN: ISOLATION AND CHARACTERIZATION
Lai, J. C. K., Walsh, J. M., Dennis, S. C., et al. (1977) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1977.tb10434.x · Cited by 274 · see citing works
Free radicals in central nervous system ischemia.
Schmidley, J. W. (1990) · Stroke · doi:10.1161/01.str.21.7.1086 · Cited by 256 · 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
Inhibition of NADH-Linked Mitochondrial Respiration by 4-Hydroxy-2-nonenal
Humphries, K. M., Yoo, Y., & Szweda, L. I. (1998) · Biochemistry · doi:10.1021/bi971958i · Cited by 231 · see citing works
Brain Hydroxyl Radical Generation in Acute Experimental Head Injury
Hall, E. D., Andrus, P. K., & Yonkers, P. A. (1993) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1993.tb03189.x · Cited by 229 · see citing works
Ballou, D. P., Palmer, G., & Massey, V. (1969) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(69)90288-5 · Cited by 223 · see citing works
Energy‐Metabolising Enzymes in Brain Regions of Adult and Aging Rats
Leong, S. F., Lai, J. C. K., Lim, L., & Clark, J. B. (1981) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1981.tb06326.x · Cited by 220 · see citing works
Glutamate, calcium, and free radicals as mediators of ischemic brain damage
Siesjö, B. K., Zhao, Q., Pahlmark, K., Siesjö, P., Katsura, K., & Folbergrová, J. (1995) · The Annals of Thoracic Surgery · doi:10.1016/0003-4975(95)00077-x · Cited by 201 · see citing works
An immunohistochemical study on α‐ketoglutarate dehydrogenase complex in Parkinson's disease
Mizuno, Y., Matuda, S., Yoshino, H., Mori, H., Hattori, N., & Ikebe, S. (1994) · Annals of Neurology · doi:10.1002/ana.410350212 · Cited by 199 · see citing works
The α-ketoglutarate dehydrogenase complex in neurodegeneration
Gibson, G. E., Park, L. C. H., Sheu, K. R., Blass, J. P., & Calingasan, N. Y. (2000) · Neurochemistry International · doi:10.1016/s0197-0186(99)00114-x · Cited by 199 · see citing works
Butterworth, R. F., Kril, J. J., & Harper, C. G. (1993) · Alcoholism Clinical and Experimental Research · doi:10.1111/j.1530-0277.1993.tb05668.x · Cited by 197 · see citing works
Lafon‐Cazal, M., Culcasi, M., Gaven, F., Pietri, S., & Bockaert, J. (1993) · Neuropharmacology · doi:10.1016/0028-3908(93)90020-4 · Cited by 189 · see citing works
An immunochemical study of the pyruvate dehydrogenase deficit in Alzheimer's disease brain
Sheu, K. R., Kim, Y., Blass, J. P., & Weksler, M. E. (1985) · Annals of Neurology · doi:10.1002/ana.410170505 · Cited by 180 · see citing works
Mitochondrial H2O2 formation: Relationship with energy conservation
Loschen, G., Azzi, A., & Flohé, L. (1973) · FEBS Letters · doi:10.1016/0014-5793(73)80165-6 · Cited by 180 · see citing works
Brain α‐Ketoglutarate Dehydrotenase Complex Activity in Alzheimer's Disease
Mastrogiacomo, F., Bergeron, C., & Kish, S. J. (1993) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1993.tb07436.x · Cited by 176 · see citing works
Gazaryan, I. G., Krasnikov, B. F., ASHBY, G. A., THORNELEY, R. N. F., Kristal, B. S., & Brown, A. M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m108264200 · Cited by 174 · see citing works
Yudkoff, M., NELSON, D. S., Daikhin, Y., & Erecińska, M. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47001-9 · Cited by 169 · see citing works
Sipos, I., Tretter, L., & Ádám‐Vizi, V. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01513.x · Cited by 167 · see citing works
Self-citationMitochondrial dysfunction in parkinson's disease
Mizuno, Y., Yoshino, H., Ikebe, S.-I., Hattori, N., Kobayashi, T., Shimoda‐Matsubayashi, S., Matsumine, H., & Kondo, T. (1998) · Annals of Neurology · doi:10.1002/ana.410440715 · Cited by 164 · see citing works
Sequestration of glutamate-induced Ca2+ loads by mitochondria in cultured rat hippocampal neurons
Wang, G. J., & Thayer, S. A. (1996) · Journal of Neurophysiology · doi:10.1152/jn.1996.76.3.1611 · Cited by 164 · see citing works
Thiamine-dependent enzyme changes in temporal cortex of patients with Alzheimer's disease
Butterworth, R. F., & Besnard, A.-M. (1990) · Metabolic Brain Disease · doi:10.1007/bf00997071 · Cited by 164 · see citing works
Brown, A. M., Kristal, B. S., Effron, M. S., Shestopalov, A. I., Ullucci, P. A., Sheu, K. ‐. R., Blass, J. P., & Cooper, A. J. L. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.18.13441 · Cited by 164 · 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
Tricarboxylic acid cycle flux and enzyme activities in the isolated working rat heart
Cooney, G. J., Taegtmeyer, H., & Newsholme, E. A. (1981) · Biochemical Journal · doi:10.1042/bj2000701 · Cited by 159 · see citing works
Control of Mitochondrial Substrate Oxidation
Hansford, R. G. (1980) · Current topics in bioenergetics · doi:10.1016/b978-0-12-152510-1.50012-2 · Cited by 157 · see citing works
Chinopoulos, C., Tretter, L., & Ádám‐Vizi, V. (1999) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1999.0730220.x · Cited by 154 · see citing works
Self-citationHerrero, A., & Barja, G. (2000) · Journal of Bioenergetics and Biomembranes · doi:10.1023/a:1005626712319 · Cited by 149 · see citing works
Lucas, D. T., & Szweda, L. I. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.12.6689 · Cited by 147 · see citing works
Shank, R. P., & Campbell, G. L. M. (1984) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1984.tb12724.x · Cited by 144 · see citing works
Park, L. C. H., Zhang, H., Sheu, K. R., Calingasan, N. Y., Kristal, B. S., LINDSAY, J. G., & Gibson, G. E. (1999) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1999.0721948.x · Cited by 139 · 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
Ambrosio, G. (1991) · Journal of Molecular and Cellular Cardiology · doi:10.1016/0022-2828(91)90183-m · Cited by 134 · see citing works
Myxothiazol Induces H2O2 Production from Mitochondrial Respiratory Chain
Starkov, A. A., & Fiskum, G. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.4409 · Cited by 133 · see citing works
Mizuno, Y., Suzuki, K., & Ohta, S. (1990) · Journal of the Neurological Sciences · doi:10.1016/0022-510x(90)90056-s · Cited by 129 · see citing works
Smith, C. M., Bryła, J., & WILLIAMSON, J. R. (1974) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)42910-4 · Cited by 128 · see citing works
FREE RADICALS, LIPID PEROXIDATION, AND CELL DAMAGE
Halliwell, B. B., & Gutteridge, J. M. C. (1984) · The Lancet · doi:10.1016/s0140-6736(84)91530-7 · Cited by 127 · see citing works
Zinc and Excitotoxic Brain Injury: A New Model
Frederickson, C. J., Maret, W., & Cuajungco, M. P. (2004) · The Neuroscientist · doi:10.1177/1073858403255840 · Cited by 127 · 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
Garland, P. B. (1964) · Biochemical Journal · doi:10.1042/bj0920010c · Cited by 116 · see citing works
α‐ketoglutarate dehydrogenase in alzheimer brains bearing the APP670/671 mutation
Gibson, G. E., Zhang, H., Sheu, K. ‐. R., Bogdanovich, N. K., LINDSAY, J. G., Lannfelt, L., Vestling, M., & Cowburn, R. F. (1998) · Annals of Neurology · doi:10.1002/ana.410440414 · Cited by 108 · see citing works
Sheu, K. R., Cooper, A. J. L., Koike, K., Koike, M., LINDSAY, J. G., & Blass, J. P. (1994) · Annals of Neurology · doi:10.1002/ana.410350311 · Cited by 108 · see citing works
Pralong, W. F., Hunyady, L., Várnai, P., Wollheim, C. B., & Spät, A. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.1.132 · Cited by 104 · see citing works
Andersson-Hall, U. K., Leighton, B., Young, M. E., Blomstrand, E., & Newsholme, E. A. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.9171 · Cited by 99 · see citing works
Frontotemporal dementia: Neuropil spheroids and presynaptic terminal degeneration
Zhou, L., Miller, B. L., McDaniel, C. H., Kelly, L. K., Kim, O. J., & Miller, C. A. (1998) · Annals of Neurology · doi:10.1002/ana.410440116 · Cited by 98 · see citing works
Influence of NAD-linked dehydrogenase activity on flux through oxidative phosphorylation
Moreno‐Sánchez, R., Hogue, B. A., & Hansford, R. G. (1990) · Biochemical Journal · doi:10.1042/bj2680421 · Cited by 93 · see citing works
Selective inactivation of redox-sensitive mitochondrial enzymes during cardiac reperfusion
Sadek, H. A., Humphries, K. M., Szweda, P. A., & Szweda, L. I. (2002) · Archives of Biochemistry and Biophysics · doi:10.1016/s0003-9861(02)00446-0 · Cited by 91 · see citing works
Influence of the Malate‐Aspartate Shuttle on Oxidative Metabolism in Synaptosomes
Cheeseman, A. J., & Clark, J. B. (1988) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1988.tb03044.x · Cited by 89 · see citing works
Gibson, G. E., Park, L. C. H., Zhang, H., Sorbi, S., & Calingasan, N. Y. (1999) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1999.tb07819.x · Cited by 85 · see citing works
4-Hydroxynonenal, a novel indicator of lipid peroxidation for reperfusion injury of the myocardium
Blasig, I. E., Grune, T., Schönheit, K., et al. (1995) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.1995.269.1.h14 · Cited by 83 · see citing works
The respiratory burst oxidase of neutrophils. Separation of an FAD enzyme and its characterization.
Kakinuma, K., Fukuhara, Y., & Kaneda, M. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)45354-9 · Cited by 81 · see citing works
Scanlon, J. M., & Reynolds, I. J. (1998) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1998.71062392.x · Cited by 74 · see citing works
Chinopoulos, C., Tretter, L., Rozsa, A., & Ádám‐Vizi, V. (2000) · Journal of Neuroscience · doi:10.1523/jneurosci.20-06-02094.2000 · Cited by 73 · see citing works
Self-citationChinopoulos, C., & Ádám‐Vizi, V. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00060.x · Cited by 73 · see citing works
Glucose-induced activation of pyruvate dehydrogenase in isolated rat pancreatic islets
McCormack, J. G., Longo, E., & Corkey, B. E. (1990) · Biochemical Journal · doi:10.1042/bj2670527 · Cited by 72 · see citing works
Hansford, R. G., & Castro, F. (1981) · Biochemical Journal · doi:10.1042/bj1980525 · Cited by 70 · see citing works
Regional enzyme development in rat brain. Enzymes of energy metabolism
Leong, S. F., & Clark, J. B. (1984) · Biochemical Journal · doi:10.1042/bj2180139 · Cited by 68 · see citing works
A familial progressive neurodegenerative disease with 2-oxoglutaric aciduria
Kohlsch�tter, A., Behbehani, A. W., Langenbeck, U., et al. (1982) · European Journal of Pediatrics · doi:10.1007/bf00442325 · Cited by 63 · see citing works
Selective Loss of KGDHC-Enriched Neurons in Alzheimer Temporal Cortex
Ko, L., Sheu, K. R., Thaler, H. T., Markesbury William, R., & Blass, J. P. (2001) · Journal of Molecular Neuroscience · doi:10.1385/jmn:17:3:361 · Cited by 56 · see citing works
AN OXIDASE FOR REDUCED DIPHOSPHOPYRIDINE NUCLEOTIDE
Huennekens, F. M., BASFORD, R. E., Gabrio, B. W., Felton, S. P., & Nurk, E. (1955) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)98227-x · Cited by 55 · see citing works
Sipos, I., Tretter, L., & Ádám‐Vizi, V. (2003) · Neurochemical Research · doi:10.1023/a:1025634728227 · Cited by 55 · see citing works
Self-citationAffected enzyme activities in Alzheimer's disease are sensitive to antemortem hypoxia
Terwel, D., Bothmer, J., Wolf, E., Meng, F., & JOLLES, J. (1998) · Journal of the Neurological Sciences · doi:10.1016/s0022-510x(98)00240-8 · Cited by 52 · see citing works
H�roux, M., & Butterworth, R. F. (1995) · Neurochemical Research · doi:10.1007/bf00995157 · Cited by 46 · see citing works
McNaught, K. S. P., Altomare, C., Cellamare, S., et al. (1995) · Neuroreport · doi:10.1097/00001756-199505300-00008 · Cited by 43 · see citing works
Mastrogiacomo, F., Lamarche, J. B., Dozić, S., Lindsay, G., Bettendorff, L., Robitaille, Y., Schut, L. J., & Kish, S. J. (1996) · Neurodegeneration · doi:10.1006/neur.1996.0004 · Cited by 42 · see citing works
Tretter, L., Chinopoulos, C., & Ádám‐Vizi, V. (1997) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1997.69062529.x · Cited by 42 · see citing works
Self-citationProperties and Subunit Composition of the Pig Heart 2-Oxoglutarate Dehydrogenase
Koike, K., HAMADA, M., Tanaka, N., Otsuka, K.-I., Ogasahara, K., & Koike, M. (1974) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)42550-7 · Cited by 41 · see citing works
Structure, assembly and function of mammalian alpha-keto acid dehydrogenase complexes.
Koike, M., & Koike, K. (1976) · PubMed · Cited by 41 · see citing works
Bando, Y., & Aki, K. (1991) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a123402 · Cited by 38 · see citing works
Chan, P. C., & Bielski, B. H. J. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)86113-6 · Cited by 32 · see citing works
Limitation of glycolysis by hexokinase in rat brain synaptosomes during intense ion pumping
Erecińska, M., NELSON, D. S., Deas, J., & Silver, I. A. (1996) · Brain Research · doi:10.1016/0006-8993(96)00324-1 · Cited by 31 · see citing works
Secondary inhibition of 2-ketoglutarate dehydrogenase complex by MPTP
Joffe, G. T., Parks, J. K., & Parker, W. D. (1998) · Neuroreport · doi:10.1097/00001756-199808240-00018 · Cited by 17 · see citing works
Bulos, B. A., Thomas, B. J., & Sacktor, B. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)90955-5 · Cited by 7 · see citing works
Willoughby, J., Craig, F. E., Harvey, S. A. K., et al. (1989) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1989.tb02539.x · Cited by 7 · see citing works
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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
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Handy, D. E., & Loscalzo, J. (2012) · Antioxidants & Redox Signaling · doi:10.1089/ars.2011.4123 · Cited by 588 · see citing works
Mantena, S. K., King, A. L., Andringa, K. K., Eccleston, H. B., & Bailey, S. M. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.12.029 · Cited by 429 · see citing works
Quinlan, C. L., Goncalves, R. L. S., Hey-Mogensen, M., Yadava, N., Bunik, V. I., & Brand, M. D. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.545301 · Cited by 310 · see citing works
Andrés, C. M. C., Pérez de la Lastra, J. M., Juan, C. A., Plou, F. J., & Pérez-Lebeña, E. (2022) · Stresses · doi:10.3390/stresses2030019 · Cited by 218 · see citing works
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Pilchova, I., Klacanova, K., Tatarkova, Z., Kaplan, P., & Racay, P. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/6797460 · Cited by 198 · see citing works
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Liu, Y., Borchert, G. L., Donald, S. P., Diwan, B. A., Anver, M., & Phang, J. M. (2009) · Cancer Research · doi:10.1158/0008-5472.can-09-1223 · Cited by 132 · see citing works
He, D., Wang, Q., Li, M., Damaris, R. N., Yi, X., Cheng, Z., & Yang, P. (2016) · Journal of Proteome Research · doi:10.1021/acs.jproteome.5b00805 · Cited by 124 · see citing works
Mehta, R., Shangari, N., & O'Brien, P. J. (2008) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.200600190 · Cited by 42 · see citing works
Kuehne, A., Mayr, U., Sévin, D. C., Claassen, M., & Zamboni, N. (2017) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1005577 · Cited by 9 · see citing works
- Authors
- Tretter, L., & Adam-Vizi, V.
- Affiliations
- Department of Medical Biochemistry, Szentagothai Janos Knowledge Center, Semmelweis University and Neurobiochemical Group, Hungarian Academy of SciencesPO Box 262, Budapest 1444, Hungary
- Venue
- Philosophical Transactions of the Royal Society B: Biological Sciences
- Publisher
- The Royal Society
- Published
- 2005-11-04
- Volume
- 360
- Issue
- 1464
- Pages
- 2335-2345
- ISSN
- 0962-8436 (ISSN-L)
- 1471-2970
- PMC
- PMC1569585
- OpenAlex
- W2156107840
- Cited by
- 434
- References
- 128
- Citations by year
- 2026: 21 · 2025: 31 · 2024: 25 · 2023: 29 · 2022: 31 · 2021: 41 · 2020: 27 · 2019: 26 · 2018: 18 · 2017: 34 · 2016: 20 · 2015: 17 · 2014: 24 · 2013: 10 · 2012: 10
- FWCI
- 4.25
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Philosophical Transactions of the Royal Society B Biological Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Hungarian Scientific Research Fund
- Magyar Tudományos Akadémia
- Nemzeti Kutatási és Technológiai Hivatal
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Biochemical Acid Research Studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Keywords
- alpha-ketoglutarate dehydrogenase, oxidative stress, reactive oxygen species, TCA cycle, NADH generation, electron transport chain, aconitase, NAD+/NADH ratio, enzyme inhibition, neurodegenerative diseases, metabolic regulation
- MeSH terms
- Citric Acid Cycle, Humans, Ketoglutarate Dehydrogenase Complex, Mitochondria, NAD, Reactive Oxygen Species, Oxidative Stress, Neurodegenerative Diseases
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.
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