Activity of purified NAD-specific isocitrate dehydrogenase at modulator and substrate concentrations approximating conditions in mitochondria
Abstract
The kinetic parameters of NAD-specific isocitrate dehydrogenase from bovine heart were examined at levels of substrates and effectors approximating the concentrations reported for isolated intact heart mitochondria in different respiratory states. The effect of changing ADP/ATP ratios (with total adenine nucleotides constant at 8 mmol/L) on enzyme activity was measured at constant concentrations of the substrates magnesium D-isocitrate (0.10 mmol/L) and NAD+ (3.0 mmol/L), the positive effector magnesium citrate (1.0 mmol/L) and the negative effector NADPH (1.5 mmol/L) at pH 7.4. Enzyme activity increased with increasing ADP/ATP ratios as a result of activation by rising ADP concentrations and not due to decreasing inhibition by falling levels of ATP. Increasing ADP decreased the inhibition by NADPH, and this effect was enhanced by magnesium citrate and by free Ca2+. In incubation media containing all of the above effectors, the S0.5 for enhancement of activity by free Ca2+ was 10 to 20 mumol/L at ratios of total ADP/total ATP between 2.0 and 0.1. This value is in the range of intramitochondrial concentrations of free Ca2+,1 but it is appreciably larger than S0.5 of Ca2+ (0.6 to 1 mumol/L) for the enhancement of ADP activation, which was determined in the absence of other effectors. When both the NAD+/NADH and the ADP/ATP ratios were decreased, a further decline in activity was found. The effect of the decreasing NAD+/NADH ratio was due to inhibition by NADH (apparent I0.5 = 0.23 +/- 0.03 mmol/L) since NAD+ was saturating over the range examined.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
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?
High ATP/ADP ratios allosterically inhibit IDH, decelerating the cycle upon excess energy supply.
“OXPHOS activity also signals to the TCA cycle at the level of ATP: high ATP/ADP ratios allosterically inhibit IDH, resulting in a deceleration of the cycle upon excess energy supply (135).”
From Regulation and function of the mammalian tricarboxylic acid cycle (2023) · cites this paper as [135]
Cites
Stability constants of metal-ion complexes
Sillén, L. G., Martell, A. E., Bjerrum, J., & Schwarzenbach, G. (1964) · Medical Entomology and Zoology · Cited by 3,983 · see citing works
Stability constants of metal-ion complexes
Furlani, C. (1965) · Journal of Chromatography A · doi:10.1016/s0021-9673(01)80434-9 · Cited by 1,862 · see citing works
Respiratory Enzymes in Oxidative Phosphorylation
Chance, B., & Baltscheffsky, H. (1958) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)64738-6 · Cited by 893 · see citing works
Computer Programmes for Processing Enzyme Kinetic Data
Cleland, W. W. (1963) · Nature · doi:10.1038/198463a0 · Cited by 652 · see citing works
The Concentrations of Free and Bound Magnesium in Rat Tissues
Veloso, D., Guynn, R. W., Oskarsson, M. K., & Veech, R. L. (1973) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)43738-1 · Cited by 383 · 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
Metabolic Effects of Ethanol in Perfused Rat Liver
WILLIAMSON, J. R., Scholz, R., Browning, E. T., Thurman, R. G., & Fukami, M. H. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)94307-3 · Cited by 321 · see citing works
Use of Isolated Liver Cells and Kidney Tubules in Metabolic Studies
Pogson, C. I. (1976) · Biochemical Education · doi:10.1016/0307-4412(76)90085-6 · Cited by 234 · see citing works
Control of Citric Acid Cycle Activity in Rat Heart Mitochondria
LaNoue, K. F., Nicklas, W. J., & WILLIAMSON, J. R. (1970) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)63427-1 · Cited by 227 · see citing works
Activation and Inhibition of DPN-linked Isocitrate Dehydrogenase of Heart by Certain Nucleotides*
Chen, R. F., & Plaut, G. W. E. (1963) · Biochemistry · doi:10.1021/bi00905a020 · Cited by 223 · see citing works
Self-citationFeedback interactions in the control of citric acid cycle activity in rat heart mitochondria
LaNoue, K. F., Bryla, J., & Williamson, J. R. (1972) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)45660-3 · Cited by 181 · see citing works
McCormack, J. G., & Denton, R. M. (1980) · Biochemical Journal · doi:10.1042/bj1900095 · Cited by 165 · see citing works
Coll, K. E., Joseph, S. K., Corkey, B. E., & WILLIAMSON, J. R. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)34184-x · Cited by 147 · see citing works
Fluorescence of Pyridine Nucleotides in Mitochondria
Avi‐Dor, Y., Olson, J. M., Doherty, M. D., & Kaplan, N. O. (1962) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)63448-4 · Cited by 127 · see citing works
Fluorometric measurement of reduced pyridine nucleotide in cellular and subcellular particles
Estabrook, R. W. (1962) · Analytical Biochemistry · doi:10.1016/0003-2697(62)90006-4 · Cited by 127 · see citing works
McCormack, J. G., & Denton, R. M. (1981) · Biochemical Journal · doi:10.1042/bj1960619 · Cited by 93 · see citing works
Hansford, R., & Johnson, R. N. (1975) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)40767-9 · Cited by 91 · see citing works
Diphosphopyridine Nucleotide-linked Isocitrate Dehydrogenase from Bovine Heart
Giorgio, N. A., Yip, A., Fleming, J. E., & Plaut, G. W. E. (1970) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)62777-2 · Cited by 84 · see citing works
Self-citationMagnesium and manganese complexes of citric and isocitric acids
Grzybowski, A. K., Tate, S. S., & Datta, S. P. (1970) · Journal of the Chemical Society A Inorganic Physical Theoretical · doi:10.1039/j19700000241 · Cited by 60 · see citing works
Marshall, S. E., McCormack, J. G., & Denton, R. M. (1984) · Biochemical Journal · doi:10.1042/bj2180249 · Cited by 59 · see citing works
Plaut, G., Schramm, V. L., & Aogaichi, T. (1974) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)42864-0 · Cited by 51 · see citing works
Self-citationActivities of NAD‐Specific and NADP‐Specific Isocitrate Dehydrogenases in Rat‐Liver Mitochondria
Smith, C. M., & Plaut, G. (1979) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1979.tb13113.x · Cited by 38 · see citing works
Self-citationEffect of ammonia on mitochondrial and cytosolic NADH and NADPH systems in isolated rat liver cells
Tischler, M. E., Hecht, P., & WILLIAMSON, J. R. (1977) · FEBS Letters · doi:10.1016/0014-5793(77)80129-4 · Cited by 33 · see citing works
Johnson, R. N., & Hansford, R. G. (1975) · Biochemical Journal · doi:10.1042/bj1460527 · Cited by 33 · see citing works
Gabriel, J. L., & Plaut, G. (1984) · Biochemistry · doi:10.1021/bi00307a037 · Cited by 31 · see citing works
Self-citationInhibition and activation of bovine heart NAD-specific isocitrate dehydrogenase by ATP
Gabriel, J. L., Milner, R. E., & Plaut, G. (1985) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(85)90015-3 · Cited by 27 · see citing works
Self-citationKÖNIG, T., Nicholls, D. G., & Garland, P. B. (1969) · Biochemical Journal · doi:10.1042/bj1140589 · Cited by 25 · see citing works
Citrate activation of NAD-specific isocitrate dehydrogenase from bovine heart.
Gabriel, J. L., & Plaut, G. W. E. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)43454-5 · Cited by 25 · see citing works
Self-citationAogaichi, T., Evans, J., Gabriel, J. L., & Plaut, G. (1980) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(80)90043-0 · Cited by 23 · see citing works
Self-citationLenartowicz, E., WINTER, C., Kunz, W., & Wojtczak, A. (1976) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1976.tb10642.x · Cited by 22 · see citing works
Cc, F., Jp, L., & Plaut, G. W. E. (1975) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)41678-5 · Cited by 19 · see citing works
Self-citationHiltunen, J. K., & Hassinen, I. E. (1977) · International Journal of Biochemistry · doi:10.1016/0020-711x(77)90112-4 · Cited by 14 · see citing works
Calcium Homeostasis and Compartmentation in Liver
WILLIAMSON, J. R., & Murphy, E. (1980) · Springer eBooks · doi:10.1007/978-1-4757-1419-7_70 · Cited by 13 · see citing works
Specific site inhibitors of NAD-specific isocitrate dehydrogenase from bovine heart.
Gabriel, J. L., & Plaut, G. W. E. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)34291-1 · Cited by 9 · see citing works
Self-citationApparent Stability Constants of Magnesium and Calcium Complexes of Tricarboxylates
Gabriel, J. L., Aogaichi, T., Dearolf, C. R., & Plaut, G. (1983) · Analytical Letters · doi:10.1080/00032718308065155 · Cited by 9 · see citing works
Self-citationFLUORESCENCE OF THE COENZYME ANALOG NICOTINAMIDE FORMYCIN DINUCLEOTIDE
Gabriel, J. L., & Plaut, G. (1981) · Photochemistry and Photobiology · doi:10.1111/j.1751-1097.1981.tb04291.x · Cited by 8 · see citing works
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
What a difference a hydroxyl makes: mutant IDH, (<i>R</i>)-2-hydroxyglutarate, and cancer
Losman, J.-A., & Kaelin, W. G. (2013) · Genes & Development · doi:10.1101/gad.217406.113 · Cited by 570 · see citing works
Reitman, Z. J., & Yan, H. (2010) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/djq187 · Cited by 562 · see citing works
Regulation and function of the mammalian tricarboxylic acid cycle
Arnold, P. K., & Finley, L. W. S. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102838 · Cited by 535 · see citing works
“OXPHOS activity also signals to the TCA cycle at the level of ATP: high ATP/ADP ratios allosterically inhibit IDH, resulting in a deceleration of the cycle upon excess energy supply (135).”
BackgroundTantama, M., Martínez‐François, J. R., Mongeon, R., & Yellen, G. (2013) · Nature Communications · doi:10.1038/ncomms3550 · Cited by 486 · see citing works
Sazanov, L. A., & Jackson, J. B. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)00370-x · Cited by 205 · see citing works
Chemosensitivity of IDH1-Mutated Gliomas Due to an Impairment in PARP1-Mediated DNA Repair
Lu, Y., Kwintkiewicz, J., Liu, Y., Tech, K., Frady, L. N., Su, Y.-T., Bautista, W., Moon, S. I., Macdonald, J. M., Ewend, M. G., et al. (2017) · Cancer Research · doi:10.1158/0008-5472.can-16-2773 · Cited by 203 · see citing works
Alves, F. M., Lane, D. J. R., Nguyen, T. P. M., Bush, A. I., & Ayton, S. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-02088-5 · Cited by 197 · see citing works
Scaini, G., Rezin, G. T., Carvalho, A. F., STRECK, E. L., Berk, M., & Quevedo, J. (2016) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2016.06.040 · Cited by 184 · see citing works
The regulation of neuronal mitochondrial metabolism by calcium
Llorente‐Folch, I., Rueda, C. B., Pardo, B., Szabadkai, G., Duchen, M. R., & Satrústegui, J. (2015) · The Journal of Physiology · doi:10.1113/jp270254 · Cited by 164 · see citing works
Chinopoulos, C. (2013) · Journal of Neuroscience Research · doi:10.1002/jnr.23196 · Cited by 142 · see citing works
Rutter, G. A., & Denton, R. M. (1988) · Biochemical Journal · doi:10.1042/bj2520181 · Cited by 138 · see citing works
Isocitrate dehydrogenases in physiology and cancer: biochemical and molecular insight
Al‐Khallaf, H. (2017) · Cell & Bioscience · doi:10.1186/s13578-017-0165-3 · Cited by 127 · see citing works
Liu, X., Si, W., He, L., Yang, J., Peng, Y., Ren, J., Liu, X., Jin, T., Yu, H., Zhang, Z., et al. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00774-2 · Cited by 97 · see citing works
Rosiers, C. D., Fernandez, C. A., David, F., & Brunengraber, H. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)46965-7 · Cited by 88 · see citing works
Nerve Tissue‐Specific Human Glutamate Dehydrogenase that Is Thermolabile and Highly Regulated by ADP
Shashidharan, P., Clarke, D. D., Ahmed, N., Moschonas, N. Κ., & Plaitakis, A. (1997) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1997.68051804.x · Cited by 85 · see citing works
IDH Mutations in Glioma: Double-Edged Sword in Clinical Applications?
Kayabölen, A., Yilmaz, E., & Onder, T. B. (2021) · Biomedicines · doi:10.3390/biomedicines9070799 · Cited by 83 · see citing works
IDH3α regulates one-carbon metabolism in glioblastoma
May, J., Kouri, F. M., Hurley, L., Liu, J., Tommasini-Ghelfi, S., Ji, Y., Gao, P., Calvert, A. E., Lee, A., Chandel, N. S., et al. (2019) · Science Advances · doi:10.1126/sciadv.aat0456 · Cited by 75 · see citing works
Ruas, J. S., Siqueira-Santos, E. S., Amigo, I., Rodrigues-Silva, E., Kowaltowski, A. J., & Castilho, R. F. (2016) · PLOS ONE · doi:10.1371/journal.pone.0150967 · Cited by 78 · see citing works
Glutamine metabolism in diseases associated with mitochondrial dysfunction
Bornstein, R., Mulholland, M. T., Sedensky, M. M., Morgan, P. G., & Johnson, S. C. (2023) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2023.103887 · Cited by 71 · see citing works
Isocitrate dehydrogenase variants in cancer — Cellular consequences and therapeutic opportunities
Liu, S., Cadoux-Hudson, T. A. D., & Schofield, C. J. (2020) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2020.06.012 · Cited by 70 · see citing works
Reverse flux through cardiac NADP+-isocitrate dehydrogenase under normoxia and ischemia
Comte, B., Vincent, G., Bouchard, B., Benderdour, M., & Rosiers, C. D. (2002) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00287.2002 · Cited by 67 · see citing works
Tai, Y.-H., Engels, D., Locatelli, G., Emmanouilidis, I., Fecher, C., Theodorou, D., Müller, S. A., Licht‐Mayer, S., Kreutzfeldt, M., Wagner, I., et al. (2023) · Nature Metabolism · doi:10.1038/s42255-023-00838-3 · Cited by 60 · see citing works
Metabolic adaptations in cancers expressing isocitrate dehydrogenase mutations
Hvinden, I. C., Cadoux-Hudson, T. A. D., Schofield, C. J., & McCullagh, J. (2021) · Cell Reports Medicine · doi:10.1016/j.xcrm.2021.100469 · Cited by 59 · see citing works
Mutant IDH in Gliomas: Role in Cancer and Treatment Options
Solomou, G., Finch, A., Asghar, A., & Bardella, C. (2023) · Cancers · doi:10.3390/cancers15112883 · Cited by 57 · see citing works
The role of SIRT3 in homeostasis and cellular health
Trinh, D., Halabi, L. A., Brar, H., Kametani, M., & Nash, J. E. (2024) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2024.1434459 · Cited by 56 · see citing works
Gaster, M., Nehlin, J. O., & Minet, A. D. (2012) · Archives of Physiology and Biochemistry · doi:10.3109/13813455.2012.656653 · Cited by 53 · see citing works
Aponte, A. M., Phillips, D. J., Harris, R. A., Blinova, K., French, S. A., Johnson, D., & Balaban, R. S. (2009) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(09)05004-6 · Cited by 52 · see citing works
Allosteric Motions in Structures of Yeast NAD+-specific Isocitrate Dehydrogenase
Taylor, A. B., Hu, G., Hart, P. J., & McAlister-Henn, L. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m708719200 · Cited by 52 · see citing works
Isocitrate dehydrogenase mutations in diffuse gliomas: clinical and aetiological implications
Gupta, R., Webb-Myers, R., Flanagan, S., & Buckland, M. E. (2011) · Journal of Clinical Pathology · doi:10.1136/jclinpath-2011-200227 · Cited by 48 · see citing works
Detailed kinetics and regulation of mammalian NAD-linked isocitrate dehydrogenase
Qi, F., Chen, X., & Beard, D. A. (2008) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2008.07.001 · Cited by 45 · see citing works
Shashidharan, P., & Plaitakis, A. (2014) · Neurochemical Research · doi:10.1007/s11064-013-1227-5 · Cited by 43 · see citing works
Palmfeldt, J., Vang, S., Stenbroen, V., Pedersen, C. B., Christensen, J., Bross, P., & Gregersen, N. (2009) · Proteome Science · doi:10.1186/1477-5956-7-20 · Cited by 42 · see citing works
Improving the description of metabolic networks: the TCA cycle as example
Stobbe, M. D., Houten, S. M., van Kampen, A. H. C., Wanders, R. J. A., & Moerland, P. D. (2012) · The FASEB Journal · doi:10.1096/fj.11-203091 · Cited by 42 · see citing works
Modeling mitochondrial function
Balaban, R. S. (2006) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00223.2006 · Cited by 41 · see citing works
Ruas, J. S., Siqueira‐Santos, E. S., Rodrigues-Silva, E., & Castilho, R. F. (2018) · Scientific Reports · doi:10.1038/s41598-018-35679-8 · Cited by 35 · see citing works
Yamada, S., Kotake, Y., Demizu, Y., Kurihara, M., Sekino, Y., & Kanda, Y. (2014) · Scientific Reports · doi:10.1038/srep05952 · Cited by 35 · see citing works
Isocitrate dehydrogenase 3b is required for spermiogenesis but dispensable for retinal viability
Zhu, S., Huang, J., Xu, R., Wang, Y., Wan, Y., McNeel, R., Parker, E. D., Kolson, D. R., Yam, M., Webb, B. A., et al. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102387 · Cited by 34 · see citing works
Curative role of pantothenic acid in brain damage of gamma irradiated rats
Shedid, S. M., Saada, H. N., Na, E., & Hammad, A. (2017) · Indian Journal of Clinical Biochemistry · doi:10.1007/s12291-017-0683-0 · Cited by 30 · see citing works
Transduction Process‐Based Classification of Biosensors
Yang, F., Ma, Y., Stanciu, S. G., & Wu, A. (2020) · doi:10.1002/9783527345137.ch2 · Cited by 29 · see citing works
Liu, X., Qiao, Y., Ting, X., & Si, W. (2020) · PubMed Central · Cited by 28 · see citing works
Huang, Q., & Huang, H. (2011) · PROTEOMICS · doi:10.1002/pmic.201100084 · Cited by 28 · see citing works
The role of mutation of metabolism-related genes in genomic hypermethylation
Waterfall, J. J., Killian, J. K., & Meltzer, P. S. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.08.003 · Cited by 23 · see citing works
Rutter, G. A., & Denton, R. M. (1989) · Biochemical Journal · doi:10.1042/bj2630445 · Cited by 23 · see citing works
Activation of glutamate dehydrogenase by l-leucine
Couée, I., & Tipton, K. F. (1989) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(89)90239-2 · Cited by 22 · see citing works
Important role of Ser443 in different thermal stability of human glutamate dehydrogenase isozymes1
Yang, S.-J., Huh, J., Hong, H., Kim, T. U., & Cho, S. (2004) · FEBS Letters · doi:10.1016/s0014-5793(04)00183-8 · Cited by 21 · see citing works
Léger, A., Cormier, S. B., Blanchard, A., Menail, H. A., & Pichaud, N. (2024) · Journal of Experimental Biology · doi:10.1242/jeb.247221 · Cited by 20 · see citing works
Hetero-oligomeric glutamate dehydrogenase from Thermus thermophilus
Tomita, T., Miyazaki, T., Miyazaki, J., Kuzuyama, T., & Nishiyama, M. (2010) · Microbiology · doi:10.1099/mic.0.042721-0 · Cited by 18 · see citing works
Mechanisms underlying neonate-specific metabolic effects of volatile anesthetics
Stokes, J., Freed, A., Bornstein, R., Su, K. N., Snell, J., Pan, A., Sun, G. X., Park, K. Y., Jung, S., Worstman, H. M., et al. (2021) · eLife · doi:10.7554/elife.65400 · Cited by 16 · see citing works
Savoia, M., Cencioni, C., Mori, M., Atlante, S., Zaccagnini, G., Devanna, P., Marcotullio, L. D., Botta, B., Martelli, F., Zeiher, A. M., et al. (2018) · The FASEB Journal · doi:10.1096/fj.201800788r · Cited by 16 · see citing works
Louer, E., Yi, G., Carmone, C., Robben, J., Stunnenberg, H. G., den Hollander, A. I., & Deen, P. M. T. (2020) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.61.5.49 · Cited by 15 · see citing works
Ishitani, Y., Ciacci, C., Ujiié, Y., Tame, A., Tiboni, M., Tanifuji, G., Inagaki, Y., & Frontalini, F. (2023) · Environmental Pollution · doi:10.1016/j.envpol.2023.121538 · Cited by 13 · see citing works
Emerging drug profile: Krebs cycle and cancer: IDH mutations and therapeutic implications
Lee, S. M., Urman, A. R., & Desai, P. M. (2019) · Leukemia & lymphoma/Leukemia and lymphoma · doi:10.1080/10428194.2019.1602260 · Cited by 13 · see citing works
Emerging Roles of Wild-type and Mutant IDH1 in Growth, Metabolism and Therapeutics of Glioma
Garrett, M. C., Fujii, Y., Osaka, N., Ito, D., Hirota, Y., & Sasaki, A. T. (2021) · Exon Publications eBooks · doi:10.36255/exonpublications.gliomas.2021.chapter4 · Cited by 13 · see citing works
Bioenergetic Heterogeneity in Mycobacterium tuberculosis Residing in Different Subcellular Niches
Akela, A. K., & Kumar, A. (2021) · mBio · doi:10.1128/mbio.01088-21 · Cited by 17 · see citing works
McAlister-Henn, L. (2011) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2011.10.003 · Cited by 12 · see citing works
Kinetic regulation of yeast NAD-specific isocitrate dehydrogenase by citrate
Gabriel, J. L., & Plaut, G. (1991) · Biochemistry · doi:10.1021/bi00224a005 · Cited by 10 · see citing works
Self-citationConstruction and Analyses of Tetrameric Forms of Yeast NAD+-Specific Isocitrate Dehydrogenase
Lin, A., Demeler, B., Minard, K. I., Anderson, S. L., Schirf, V. R., Galaleldeen, A., & McAlister-Henn, L. (2010) · Biochemistry · doi:10.1021/bi101401h · Cited by 9 · see citing works
Fuel selection at the level of mitochondria in mammalian tissues
Denton, R. M., & McCormack, J. G. (1995) · Proceedings of The Nutrition Society · doi:10.1079/pns19950034 · Cited by 9 · see citing works
Proteomic analysis of cardiac metabolic enzymes in asphyxiated newborn piglets
Fert‐Bober, J., Sawicki, G., Lopaschuk, G. D., & Cheung, P. (2008) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-008-9852-z · Cited by 8 · see citing works
Lin, Z., Chang, S.-Y., Shen, W.-C., Lin, Y.-H., Shen, C.-L., Liao, S.-B., Liu, Y.-C., Chen, C., Ching, T., & Wang, H. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms24010612 · Cited by 6 · see citing works
Isocitrate Dehydrogenase Inhibitors in Glioma: From Bench to Bedside
Ser, M. H., Webb, M., Thomsen, A., & Sener, U. T. (2024) · Pharmaceuticals · doi:10.3390/ph17060682 · Cited by 6 · see citing works
IDH1-mutated transgenic zebrafish lines: An in-vivo model for drug screening and functional analysis
Gao, Y., de Wit, M., Struys, E. A., van der Linde, H. C. Z., Salomons, G. S., Lamfers, M. L. M., Willemsen, R., Smitt, P. A. E. S., & French, P. J. (2018) · PLoS ONE · doi:10.1371/journal.pone.0199737 · Cited by 6 · see citing works
Gabriel, J. L., & Plaut, G. (1990) · Biochemistry · doi:10.1021/bi00466a016 · Cited by 6 · see citing works
Self-citationBiochemical production from sustainable carbon sources by Komagataella phaffii
Raja, W. A., & Çalı́k, P. (2025) · Biochemical Engineering Journal · doi:10.1016/j.bej.2025.109702 · Cited by 6 · see citing works
Murphy, A. N., Kelleher, J. K., & Fiskum, G. M. (1988) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(88)81004-0 · Cited by 5 · see citing works
Bajaj, M., Kumar, R., Pandey, V., Parvez, S., Tanneru, H. K., Aparoy, P., & Karnati, R. (2025) · RSC Advances · doi:10.1039/d5ra06290j · Cited by 4 · see citing works
Chen, Y., Huang, L., Zhang, Y., Ke, C., & Huang, H. (2013) · Environmental Science and Pollution Research · doi:10.1007/s11356-013-2210-z · Cited by 4 · see citing works
Basis for Half-Site Ligand Binding in Yeast NAD+-Specific Isocitrate Dehydrogenase
Lin, A., & McAlister-Henn, L. (2011) · Biochemistry · doi:10.1021/bi201088m · Cited by 4 · see citing works
Klemcke, H. G., DeKroon, R. M., Mocanu, M., Robinette, J. B., & Álzate, Ó. (2013) · Physiological Genomics · doi:10.1152/physiolgenomics.00118.2012 · Cited by 3 · see citing works
Isocitrate dehydrogenase 3b is required for spermiogenesis but dispensable for retinal degenerationPreprint
Zhu, S., Huang, J., Xu, R., Wang, Y., Wan, Y., McNeel, R., Parker, E. D., Kolson, D. R., Yam, M., Webb, B. A., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.02.09.479735 · Cited by 3 · see citing works
Scaffold modification and synthesis routes for targeting mutant IDH 1: a review
Pai, V. S., & Kumar, N. (2025) · Discover Applied Sciences · doi:10.1007/s42452-025-07293-7 · Cited by 2 · see citing works
Josephine, A., Kumar, S. A., Varalakshmi, S., & Rajendran, P. (2026) · 3 Biotech · doi:10.1007/s13205-026-04753-8 · Cited by 1 · see citing works
Mitochondrial pathways in bipolar disorder: Mechanisms and implications
Scaini, G., Andrews, T., Benevenuto, D., & Quevedo, J. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-819182-8.00005-3 · Cited by 1 · see citing works
Li, Q., Tian, M., Peng, G., Jie, T., Bing, W., Qing, T., & Hong, W. (2021) · International Journal of Applied Electromagnetics and Mechanics · doi:10.3233/jae-210054 · Cited by 1 · see citing works
Sen, A., Qu, W., Nuga, O. O., Liu, J., Burl, R. B., Gurdziel, K., Piqué-Regi, R., Hüttemann, M., & Ruden, D. M. (2016) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/077214 · Cited by 1 · see citing works
Linking enzyme expression to metabolic fluxPreprint
Li, X., Walhout, A. J. M., & Yilmaz, L. S. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.11.17.516982
ATALAY, E. B. (2024) · Gümüşhane Üniversitesi Fen Bilimleri Enstitüsü Dergisi · doi:10.17714/gumusfenbil.1353355
Zhu, S. (2025) · Theoretical and Natural Science · doi:10.54254/2753-8818/2025.au25075
- Authors
- Gabriel, J. L., Zervos, P. R., & Plaut, G. W. E.
- Affiliations
- Temple University (US)
- Venue
- Metabolism
- Publisher
- Elsevier BV
- Published
- 1986-07
- Volume
- 35
- Issue
- 7
- Pages
- 661-667
- ISSN
- 0026-0495 (ISSN-L)
- OpenAlex
- W1996736495
- Cited by
- 79
- References
- 36
- Citations by year
- 2026: 1 · 2025: 5 · 2024: 4 · 2023: 5 · 2022: 5 · 2021: 7 · 2020: 5 · 2019: 2 · 2018: 3 · 2017: 3 · 2016: 3 · 2015: 1 · 2014: 2 · 2013: 6 · 2012: 2
- FWCI
- 0.58
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Metabolism (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (AM 15404)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Biochemical Acid Research Studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Molecular Research
- Keywords
- enzyme kinetics, ATP/ADP ratio, NAD+/NADH ratio, NADPH inhibition, magnesium citrate, free calcium, heart mitochondria, substrate inhibition, enzyme activation, bovine heart
- MeSH terms
- Adenosine Diphosphate, Adenosine Triphosphate, Animals, Cattle, Isocitrate Dehydrogenase, Kinetics, Mitochondria, Heart, NAD, In Vitro Techniques
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
