Regulation of the pyruvate dehydrogenase multienzyme complex
Abstract
The objective of this review is to provide an overview of intermittent fasting regimens, summarize the evidence on the health benefits of intermittent fasting, and discuss physiological mechanisms by which intermittent fasting might lead to improved ...Read More
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The PDHC is allosterically inhibited by NADH, acetyl-CoA, and ATP, making it a potent sensor of TCA cycle activity and a critical node of TCA cycle regulation.
“The PDHC is allosterically inhibited by NADH, acetyl-CoA, and ATP, making it a potent sensor of TCA cycle activity and thus a critical node of TCA cycle regulation (discussed further) (52).”
From Regulation and function of the mammalian tricarboxylic acid cycle (2023) · cites this paper as [52]
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“The PDHC is allosterically inhibited by NADH, acetyl-CoA, and ATP, making it a potent sensor of TCA cycle activity and thus a critical node of TCA cycle regulation (discussed further) (52).”
BackgroundRegulation of the activity of the pyruvate dehydrogenase complex
Harris, R. A., Bowker-Kinley, M. M., Huang, B., & Wu, P. (2002) · Advances in Enzyme Regulation · doi:10.1016/s0065-2571(01)00061-9 · Cited by 337 · see citing works
Regulation of skeletal muscle glycogen phosphorylase and PDH during maximal intermittent exercise
Parolin, M. L., Chesley, A., Matsos, M. P., Spriet, L. L., Jones, N. L., & Heigenhauser, G. J. F. (1999) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.1999.277.5.e890 · Cited by 334 · see citing works
Diversity of the Pyruvate Dehydrogenase Kinase Gene Family in Humans
Gudi, R., Bowker-Kinley, M. M., Kedishvili, N. Y., Zhao, Y., & Popov, K. M. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.48.28989 · Cited by 287 · see citing works
Isoenzymes of Pyruvate Dehydrogenase Phosphatase
Huang, B., Gudi, R., Wu, P., Harris, R. A., Hamilton, J. A., & Popov, K. M. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.28.17680 · Cited by 213 · see citing works
Starvation Increases the Amount of Pyruvate Dehydrogenase Kinase in Several Mammalian Tissues
Wu, P., Blair, P. V., Sato, J., Jaskiewicz, J. A., Popov, K. M., & Harris, R. A. (2000) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2000.1946 · Cited by 181 · see citing works
Zell, R., Geck, P., Werdan, K., & Boekstegers, P. (1997) · Molecular and Cellular Biochemistry · doi:10.1023/a:1006896832582 · Cited by 175 · see citing works
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Jeoung, N. H., Wu, P., Joshi, M., Jaskiewicz, J. A., Bock, C. B., DePaoli-Roach, A. A., & Harris, R. A. (2006) · Biochemical Journal · doi:10.1042/bj20060125 · Cited by 143 · see citing works
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Leary, S. C., Battersby, B. J., Hansford, R. G., & Moyes, C. D. (1998) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(98)00105-4 · Cited by 118 · see citing works
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Fukuda, R., Marín‐Juez, R., El‐Sammak, H., Beisaw, A., Ramadass, R., Kuenne, C. T., Günther, S., Konzer, A., Bhagwat, A. M., Graumann, J., et al. (2020) · EMBO Reports · doi:10.15252/embr.201949752 · Cited by 119 · see citing works
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Cheeseman, J. M. (2013) · Functional Plant Biology · doi:10.1071/fp12285 · Cited by 120 · see citing works
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Olsen, L. A., Thum, E., & Rohner, N. (2021) · Developmental Cell · doi:10.1016/j.devcel.2021.02.024 · Cited by 99 · see citing works
Effects of short-term submaximal training in humans on muscle metabolism in exercise
Putman, C. T., Jones, N. L., Hultman, E., Hollidge-Horvat, M. G., Bonen, A., McConachie, D., & Heigenhauser, G. J. F. (1998) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.1998.275.1.e132 · Cited by 97 · 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
Glycolysis and pyruvate oxidation in cardiac hypertrophy—Why so unbalanced?
Leong, H. S., Brownsey, R. W., Kulpa, J. E., & Allard, M. F. (2003) · Comparative Biochemistry and Physiology Part A Molecular & Integrative Physiology · doi:10.1016/s1095-6433(03)00007-2 · Cited by 91 · see citing works
Capece, U., Moffa, S., Improta, I., Giuseppe, G. D., Nista, E. C., CEFALO, C. M. A., Cinti, F., Pontecorvi, A., Gasbarrini, A., Giaccari, A., et al. (2022) · Nutrients · doi:10.3390/nu15010018 · Cited by 96 · see citing works
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Wu, J., Zhao, Y., Park, Y., Lee, J., Gao, L., Zhao, J., & Wang, L. (2018) · Hepatology · doi:10.1002/hep.29902 · Cited by 83 · see citing works
The long and winding road to the mitochondrial pyruvate carrier
Schell, J. C., & Rutter, J. P. (2013) · Cancer & Metabolism · doi:10.1186/2049-3002-1-6 · Cited by 83 · see citing works
Pyruvate prevents ischemia-reperfusion mucosal injury of rat small intestine
Cicalese, L., Lee, K., Schraut, W. H., Watkins, S. C., Borle, A. B., & Stanko, R. T. (1996) · The American Journal of Surgery · doi:10.1016/s0002-9610(99)80081-6 · Cited by 81 · see citing works
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Jeoung, N. H., & Harris, R. A. (2010) · Korean Diabetes Journal · doi:10.4093/kdj.2010.34.5.274 · Cited by 78 · see citing works
Metabolic Acidosis and Thiamine Deficiency
Romanski, S. A., & McMahon, M. M. (1999) · Mayo Clinic Proceedings · doi:10.4065/74.3.259 · Cited by 69 · see citing works
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Bhandary, S., & Aguan, K. (2015) · Epilepsy Research · doi:10.1016/j.eplepsyres.2015.07.002 · Cited by 64 · see citing works
Hultman, E. (1995) · Proceedings of The Nutrition Society · doi:10.1079/pns19950041 · Cited by 65 · see citing works
Naia, L., Cunha‐Oliveira, T., Rodrigues, J., Rosenstock, T. R., Oliveira, A. M., Ribeiro, M., Carmo, C., Oliveira-Sousa, S. I., Duarte, A. I., Hayden, M. R., et al. (2017) · Journal of Neuroscience · doi:10.1523/jneurosci.2006-14.2016 · Cited by 64 · see citing works
Energy Metabolism in the Termite and Its Gut Microbiota
Slaytor, M. (2000) · Springer eBooks · doi:10.1007/978-94-017-3223-9_15 · Cited by 58 · see citing works
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McCartney, R. G., Rice, J., Sanderson, S. J., Bunik, V. I., Lindsay, H., & LINDSAY, J. G. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.37.24158 · Cited by 55 · see citing works
PARylated PDHE1α generates acetyl-CoA for local chromatin acetylation and DNA damage repair
Zhang, J., Chen, F., Tian, Y., Xu, W., Zhu, Q., Li, Z., Qiu, L., Lu, X., Peng, B., Liu, X., et al. (2023) · Nature Structural & Molecular Biology · doi:10.1038/s41594-023-01107-3 · Cited by 54 · see citing works
Glowing Locked Nucleic Acids: Brightly Fluorescent Probes for Detection of Nucleic Acids in Cells
Østergaard, M. E., Cheguru, P., Papasani, M. R., et al. (2010) · Journal of the American Chemical Society · doi:10.1021/ja1057295 · Cited by 50 · see citing works
Duarte, I. F., Caio, J. M., Moedas, M. F., Rodrigues, L., Leandro, P., Rivera, I. A., & Silva, M. F. B. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-03996-3 · Cited by 47 · see citing works
Zhu, W., Zhang, H., Li, X., et al. (2015) · Journal of Insect Physiology · doi:10.1016/j.jinsphys.2015.11.008 · Cited by 47 · see citing works
Xu, W., Li, L., Sun, J., Zhu, S., Yan, Z., Gao, L., Gao, C., Cui, Y., & Mao, C. (2018) · Aging · doi:10.18632/aging.101699 · Cited by 46 · see citing works
Mongan, P. D., Karaian, J., Schuur, B. M. V. D., et al. (2003) · Journal of Surgical Research · doi:10.1016/s0022-4804(03)00148-3 · Cited by 44 · see citing works
Slovin, P. N., Huang, C., Cade, J. R., Wood, C. E., Nasıroğlu, Ö., Privette, M., Orbach, P., & Skimming, J. W. (2001) · Resuscitation · doi:10.1016/s0300-9572(01)00325-2 · Cited by 42 · see citing works
Evolution of the Metazoan Protein Phosphatase 2C Superfamily
Stern, A., Privman, E., Rasis, M., Lavi, S., & Pupko, T. (2006) · Journal of Molecular Evolution · doi:10.1007/s00239-006-0033-y · Cited by 41 · see citing works
Zhang, L., Zhang, J., Liu, Y., Zhang, P., Nie, J., Zhao, R., Shi, Q., Sun, H., Jiao, D., Chen, Y., et al. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-03908-0 · Cited by 40 · see citing works
Manipulation of Glycolysis in Malignant Tumors: Fantasy or Therapy?
Sattler, U. G. A., Hirschhaeuser, F., & Mueller-Klieser, W. (2009) · Current Medicinal Chemistry · doi:10.2174/092986710790112657 · Cited by 37 · see citing works
Characterization of the porcine differentially expressed PDK4 gene and association with meat quality
Lan, J., Lei, M., Zhang, Y.-B., Wang, J.-H., Feng, X., Xu, D., Gui, J., & Xiong, Y. (2008) · Molecular Biology Reports · doi:10.1007/s11033-008-9411-4 · Cited by 38 · see citing works
Bradley, N. S., Heigenhauser, G. J. F., Roy, B. D., Staples, E. M., Inglis, J., LeBlanc, P. J., & Peters, S. J. (2007) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00636.2007 · Cited by 37 · see citing works
Selecting exercise regimens and strains to modify obesity and diabetes in rodents: an overview
Ghosh, S., Golbidi, S., Werner, I., Verchere, C. B., & Laher, I. (2010) · Clinical Science · doi:10.1042/cs20090389 · Cited by 37 · see citing works
Löffelhardt, S., Bonaventura, C., Locher, M., et al. (1995) · Biochemical Pharmacology · doi:10.1016/0006-2952(95)00175-y · Cited by 35 · see citing works
Shimomura, Y., Murakami, T., Nakai, N., Nagasaki, M., Obayashi, M., Zhihao, L. I., Xu, M. Q., Sato, Y., Kato, T., Shimomura, N., et al. (2000) · Journal of Nutritional Science and Vitaminology · doi:10.3177/jnsv.46.71 · Cited by 34 · see citing works
Janke, R., Genzel, Y., Wahl, A., & Reichl, U. (2010) · Biotechnology and Bioengineering · doi:10.1002/bit.22817 · Cited by 33 · see citing works
PGC-1α increases PDH content but does not change acute PDH regulation in mouse skeletal muscle
Kiilerich, K., Adser, H., Jakobsen, A. H., Pedersen, P. A., Hardie, D. G., Wojtaszewski, J. F. P., & Pilegaard, H. (2010) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00400.2010 · Cited by 29 · see citing works
A genome-based analysis of amino acid metabolism in the biotrophic plant pathogen Ustilago maydis
McCann, M. P., & Snetselaar, K. M. (2008) · Fungal Genetics and Biology · doi:10.1016/j.fgb.2008.05.006 · Cited by 30 · see citing works
Behal, R. H., DeBuysere, M. S., Demeler, B., et al. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)31703-4 · Cited by 30 · see citing works
Self-citationMcCartney, R. G., Sanderson, S. J., & LINDSAY, J. G. (1997) · Biochemistry · doi:10.1021/bi9630016 · Cited by 28 · see citing works
Effects of IL-6 on pyruvate dehydrogenase regulation in mouse skeletal muscle
Biensø, R. S., Knudsen, J. G., Brandt, N., Pedersen, P. A., & Pilegaard, H. (2013) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-013-1399-5 · Cited by 27 · see citing works
Huang, X., Bedoyan, J. K., Demirbas, D., Harris, D. J., Miron, A., Edelheit, S., Grahame, G. J., DeBrosse, S. D., Wong, L.-J. C., Hoppel, C. L., et al. (2016) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2016.11.005 · Cited by 27 · see citing works
Raddatz, G., & Bisswanger, H. (1997) · Journal of Biotechnology · doi:10.1016/s0168-1656(97)00135-1 · Cited by 26 · see citing works
Pezzato, E., Battaglia, V., Brunati, A. M., et al. (2008) · Amino Acids · doi:10.1007/s00726-008-0099-5 · Cited by 25 · see citing works
Bar, N., & Radde, N. E. (2009) · BMC Systems Biology · doi:10.1186/1752-0509-3-107 · Cited by 24 · see citing works
Antioxidant effects of pyruvate in isolated rat hearts
Marcengill, M. B. (1995) · Journal of Molecular and Cellular Cardiology · doi:10.1016/0022-2828(95)90027-6 · Cited by 23 · see citing works
Morales‐Álamo, D., Guerra, B., Santana, A., Martín-Rincón, M., Gelabert‐Rebato, M., Dorado, C., & Calbet, J. A. L. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.00188 · Cited by 22 · see citing works
Zhu, Y., Li, D., Bao, G., Wang, S., Mao, S., Song, J., Li, Y., & Zhang, Y. (2014) · Applied and Environmental Microbiology · doi:10.1128/aem.03327-13 · Cited by 22 · see citing works
Transport of pyruvate into mitochondria is involved in methylmercury toxicity
Lee, J.-Y., Ishida, Y., Takahashi, T., Naganuma, A., & Hwang, G. (2016) · Scientific Reports · doi:10.1038/srep21528 · Cited by 23 · see citing works
A Radiochemical pyruvate dehydrogenase assay: activity in heart
Sterk, J. P., Stanley, W. C., Hoppel, C. L., & Kerner, J. (2003) · Analytical Biochemistry · doi:10.1016/s0003-2697(02)00538-9 · Cited by 22 · see citing works
Bajotto, G., Murakami, T., Nagasaki, M., et al. (2006) · Metabolism · doi:10.1016/j.metabol.2005.09.014 · Cited by 21 · see citing works
Doi, Y., & Ikegami, Y. (2014) · Journal of Bacteriology · doi:10.1128/jb.01512-14 · Cited by 19 · see citing works
Ramanathan, R., Nair, M., Wang, Y.-F., Li, S.-T., Beach, C., Mancini, R., Belskie, K., & Suman, S. (2021) · Meat and Muscle Biology · doi:10.22175/mmb.11705 · Cited by 13 · see citing works
Kumar, H., Frischknecht, F., Mair, G. R., & Gomes, J. (2015) · Infection Genetics and Evolution · doi:10.1016/j.meegid.2015.09.002 · Cited by 18 · see citing works
Stapel, B., Kotsiari, A., Scherr, M., Hilfiker‐Kleiner, D., Bleich, S., Frieling, H., & Kahl, K. G. (2016) · Journal of Psychiatric Research · doi:10.1016/j.jpsychires.2016.12.012 · Cited by 18 · see citing works
Ono, Y., Lin, L. Q., Storey, B. T., et al. (1996) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1996.270.1.c98 · Cited by 18 · see citing works
Zeng, C., Wu, J., & Li, J.-M. (2024) · Journal of Cardiovascular Pharmacology · doi:10.1097/fjc.0000000000001568 · Cited by 17 · see citing works
V˙ o 2kinetics of mild exercise are altered by RER
Mole, P. A., & Hoffmann, J. J. (1999) · Journal of Applied Physiology · doi:10.1152/jappl.1999.87.6.2097 · Cited by 16 · see citing works
Elnwasany, A., Ewida, H. A., Szweda, P. A., & Szweda, L. I. (2023) · Antioxidants · doi:10.3390/antiox12030756 · Cited by 18 · see citing works
Patel, M. S., & Korotchkina, L. G. (2003) · Humana Press eBooks · doi:10.1385/1-59259-173-6:255 · Cited by 16 · see citing works
Yuan, H., Xun, H., Wang, J., Wang, J., Yao, X., & Tang, F. (2024) · Molecules · doi:10.3390/molecules29102266 · Cited by 16 · see citing works
Metabolic analysis of 13C‐labeled pyruvate for noninvasive assessment of mitochondrial function
Wu, I., Ohsawa, I., Fuku, N., & Tanaka, M. (2010) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2010.05636.x · Cited by 15 · see citing works
Ghosh, J., & Kapur, R. (2016) · Current Stem Cell Reports · doi:10.1007/s40778-016-0067-z · Cited by 15 · see citing works
Regulation of mammalian pyruvate dehydrogenase α subunit gene expression by glucose in HepG2 cells
Tan, J., Yang, H., & Patel, M. S. (1998) · Biochemical Journal · doi:10.1042/bj3360049 · Cited by 14 · see citing works
Gene Regulation and Genetic Defects in the Pyruvate Dehydrogenase Complex
Patel, M. S., Naik, S., Wexler, I. D., et al. (1995) · Journal of Nutrition · doi:10.1093/jn/125.suppl_6.1753s · Cited by 13 · see citing works
Marsden, S. R., McMillan, D. G. G., & Hanefeld, U. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21228641 · Cited by 12 · see citing works
Love, L. K., LeBlanc, P. J., Inglis, J., Bradley, N. S., Choptiany, J. R., Heigenhauser, G. J. F., & Peters, S. J. (2011) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00672.2010 · Cited by 12 · see citing works
Song, H., & Komuniecki, R. W. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)31732-0 · Cited by 12 · see citing works
Reciprocal regulation of cardiac β-oxidation and pyruvate dehydrogenase by insulin
Elnwasany, A., Ewida, H. A., Menendez-Montes, I., Mizerska, M., Fu, X.-R., Kim, C.-W., Horton, J. D., Burgess, S. C., Rothermel, B. A., Szweda, P. A., et al. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107412 · Cited by 12 · see citing works
Can, E., Bastiaansen, J., Couturier, D., Rolf Gruetter, A., Yoshihara, H. A. I., & Comment, A. (2021) · Apollo (University of Cambridge) · doi:10.17863/cam.80029 · Cited by 11 · see citing works
Nasiri, A., Sadeghi, M., Vaisi‐Raygani, A., Kiani, S., Aghelan, Z., & Khodarahmi, R. (2020) · Biomedical Research and Therapy · doi:10.15419/bmrat.v7i2.591 · Cited by 10 · see citing works
Can, E., Bastiaansen, J., Couturier, D., Gruetter, R., Yoshihara, H. A. I., & Comment, A. (2022) · Communications Biology · doi:10.1038/s42003-021-02978-2 · Cited by 10 · see citing works
Pharmacokinetics and pharmacodynamics of dichloroacetate in patients with cirrhosis*1
Shangraw, R. E. (1999) · Clinical Pharmacology & Therapeutics · doi:10.1053/cp.1999.v66.a101340 · Cited by 10 · see citing works
Ketones in the Life Sciences – Biochemistry, Metabolism, and Medicinal Significances
Kuykendall, N. S., & Kuykendall, J. R. (2024) · Biochemistry · doi:10.5772/intechopen.114276 · Cited by 9 · see citing works
Pinckaers, P. J., Petrick, H. L., Horstman, A. M. H., et al. (2025) · Journal of Nutrition · doi:10.1016/j.tjnut.2025.02.015 · Cited by 9 · see citing works
Steensma, H. Y., Tomáška, Ľ., Reuven, P., et al. (2007) · Yeast · doi:10.1002/yea.1543 · 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
Pyruvate Dehydrogenase Complex
Patel, M. S., & Korotchkina, L. G. (2002) · Wiley Encyclopedia of Molecular Medicine · doi:10.1002/0471203076.emm0691 · Cited by 9 · see citing works
Engineering pathways to biofuels in photoautotrophic microorganisms
Posewitz, M. C. (2013) · Biofuels · doi:10.4155/bfs.13.67 · Cited by 8 · see citing works
Smith, G. I., Jeukendrup, A. E., & Ball, D. R. (2013) · International Journal of Sport Nutrition and Exercise Metabolism · doi:10.1123/ijsnem.23.4.357 · Cited by 8 · see citing works
Benítez, R., Núñez, Y., Ayuso, M., Isabel, B., Fernández‐Barroso, M. Á., de Mercado, E., Gómez-Izquierdo, E., Casco, J. M. G., López-Bote, C. J., & Óvilo, C. (2021) · Animals · doi:10.3390/ani11123505 · Cited by 8 · see citing works
Mechanism of the acceleration of CO2 production from pyruvate in liver mitochondria by HCO3-
Taguchi, Y., Ono, Y., Lin, L., et al. (1997) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1997.273.1.c92 · Cited by 8 · see citing works
Amessou, M., Fouque, F., Soussi, N., Desbuquois, B., Hainaut, I., Girard, J., & Benelli, C. (1998) · Molecular and Cellular Endocrinology · doi:10.1016/s0303-7207(98)00132-4 · Cited by 8 · see citing works
Cardiac Regeneration in Adult Zebrafish: A Review of Signaling and Metabolic Coordination
Mitra, A., Mandal, S., Banerjee, K., Ganguly, N., Sasmal, P., Banerjee, D., & Gupta, S. (2025) · Current Cardiology Reports · doi:10.1007/s11886-024-02162-y · Cited by 7 · see citing works
Long-term regulation and promoter analysis of mammalian pyruvate dehydrogenase complex
Patel, M. S., Naik, S., Johnson, M., et al. (1996) · Birkhäuser Basel eBooks · doi:10.1007/978-3-0348-8981-0_15 · Cited by 6 · see citing works
Histone modification as a reflection of metabolism
Suganuma, T., & Workman, J. L. (2016) · Cell Cycle · doi:10.1080/15384101.2015.1128190 · Cited by 5 · see citing works
Torres, J., & Touati, E. (2023) · Current topics in microbiology and immunology · doi:10.1007/978-3-031-47331-9_3 · Cited by 4 · see citing works
Wang, X. X., Qi, H. Y., Chen, J., et al. (2018) · Journal of Plant Pathology · doi:10.1007/s42161-018-0137-4 · Cited by 4 · see citing works
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Xie, S., Wang, Y., Zhao, C., et al. (2024) · Reproductive BioMedicine Online · doi:10.1016/j.rbmo.2024.104495 · Cited by 3 · see citing works
- Authors
- Behal, R. H., Buxton, D. B., Robertson, J. G., & Olson, M. S.
- Affiliations
- The University of Texas at San Antonio Health Science Center (US)
- Venue
- Annual Review of Nutrition
- Publisher
- Annual Reviews
- Published
- 1993-07
- Volume
- 13
- Issue
- 1
- Pages
- 497-520
- ISSN
- 0199-9885 (ISSN-L)
- 1545-4312
- OpenAlex
- W2173424827
- Cited by
- 132
- References
- 0
- Citations by year
- 2026: 3 · 2025: 3 · 2024: 7 · 2023: 3 · 2022: 3 · 2021: 7 · 2020: 3 · 2018: 4 · 2017: 2 · 2016: 6 · 2015: 3 · 2014: 3 · 2013: 5 · 2012: 4
- FWCI
- 3.63
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Annual Review of Nutrition (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r01hl024654-10)
- National Heart, Lung, and Blood Institute (HL-24654)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Biochemical Acid Research Studies
- Health Sciences › Medicine › Physiology › Dietary Effects on Health
- Health Sciences › Medicine › Neurology › Alcoholism and Thiamine Deficiency
- Keywords
- pyruvate dehydrogenase complex, enzyme regulation, intermittent fasting, health benefits of fasting, physiological mechanisms, metabolic regulation
- MeSH terms
- Animals, Catalysis, Homeostasis, Hormones, Humans, Pyruvate Dehydrogenase Complex, Pyruvate Dehydrogenase Complex Deficiency Disease
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