Cited by 446Mitochondrial Function and PathologyATP Synthase and ATPases ResearchMetabolism, Diabetes, and Cancer

The DOI matches its Crossref record; 73 of the 73 references it cites were found in a registry or an index.

Regulation of oxidative phosphorylation in the mammalian cell

Balaban, R. S.·1990·American Journal of Physiology-Cell Physiology

DOI 10.1152/ajpcell.1990.258.3.c377

Open this paper in CoChat — free account

Abstract

The cell is capable of maintaining a steady-state flux of energy from mitochondrial oxidative phosphorylation, producing ATP, to the cytosolic adenosinetriphosphatases (ATPases), performing work. Considerable effort has been devoted to investigating the individual mechanisms involved in these two processes. However, less effort has been directed toward learning how these reactions of energy metabolism interact through the cytosol to maintain the observed steady state in the intact cell. The "classical" model for the cytosolic interaction of these two processes involves the feedback of ATP hydrolysis products, ADP and Pi, from the ATPases to oxidative phosphorylation. This model is based on data from isolated mitochondria in which the rate of oxidative phosphorylation is controlled by the concentration of ADP and Pi. Yet, recent data from intact tissues with high oxidative phosphorylation capacities (i.e., heart, brain, and kidney) indicate that the cytosolic concentration of ADP and Pi do not change significantly with work. These data imply that this simple feedback model is not adequate to explain the regulation of energy metabolism in these tissues. Other sites within the oxidative phosphorylation process must be playing a regulatory role or the kinetics of ATP synthesis must be very different than currently believed to establish the steady state. This review covers the potential sites within oxidative phosphorylation which may be regulated through cytosolic transducers to result in the necessary feedback network regulating the steady-state flow of energy in the cell. These sites will include substrate delivery to the cytochrome chain, the processes involved in the phosphorylation of ADP to ATP, and the delivery of oxygen.

Integrity signals

Registry

Crossref · 10.1152/ajpcell.1990.258.3.c377

Cites

73 of 73 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

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?

Oxygenation dependence of the transverse relaxation time of water protons in whole blood at high field
Thulborn, K. R., Waterton, J. C., Matthews, P. M., & Radda, G. K. (1982) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(82)90333-6 · Cited by 1,134
Cytosolic phosphorylation potential.
Veech, R. L., Lawson, J., Cornell, N. W., & Krebs, H. A. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)50401-4 · Cited by 919
OXIDATIVE PHOSPHORYLATIONS: RÔLE OF INORGANIC PHOSPHATE AND ACCEPTOR SYSTEMS IN CONTROL OF METABOLIC RATES
Lardy, H. A., & Wellman, H. (1952) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)50892-4 · Cited by 777
Oxidative Phosphorylation and Photophosphorylation
Boyer, P. D., Chance, B., Ernster, L., Mitchell, P. D., Racker, E., & Slater, E. C. (1977) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.46.070177.004515 · Cited by 750
Endothelium‐derived nitric oxide: actions and properties
Ignarro, L. J. (1989) · The FASEB Journal · doi:10.1096/fasebj.3.1.2642868 · Cited by 679
Quantification of the contribution of various steps to the control of mitochondrial respiration.
Groen, A. K., Wanders, R. J. A., Westerhoff, H. V., van der Meer, R., & Tager, J. M. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)81026-8 · Cited by 629
Metabolite Transport in Mitochondria
LaNoue, K. F., & Schoolwerth, A. C. (1979) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.48.070179.004255 · Cited by 622
Transport Of Oxygen In Muscle
Wittenberg, B. A., & Wittenberg, J. B. (1989) · Annual Review of Physiology · doi:10.1146/annurev.ph.51.030189.004233 · Cited by 469
Regulation of cellular energy metabolism
Erecińska, M., & Wilson, D. F. (1982) · The Journal of Membrane Biology · doi:10.1007/bf01871584 · Cited by 442
Regulation of pyruvate dehydrogenase in rat heart. Mechanism of regulation of proportions of dephosphorylated and phosphorylated enzyme by oxidation of fatty acids and ketone bodies and of effects of diabetes: role of coenzyme A, acetyl-coenzyme A and reduced and oxidized nicotinamide-adenine dinucleotide
Kerbey, A. L., Randle, P. J., Cooper, R., Whitehouse, S., Pask, H. T., & Denton, R. M. (1976) · Biochemical Journal · doi:10.1042/bj1540327 · Cited by 399

Show all 73 references

Sorted by citations

Myocardial Substrate Metabolism in the Normal and Failing Heart
Stanley, W. C., Recchia, F. A., & Lopaschuk, G. D. (2005) · Physiological Reviews · doi:10.1152/physrev.00006.2004 · Cited by 2,095
Intracellular compartmentation, structure and function of creatine kinase isoenzymes in tissues with high and fluctuating energy demands: the “phosphocreatine circuit” for cellular energy homeostasis
Wallimann, T., Wyss, M., Brdiczka, D., Nicolay, K., & Eppenberger, H. M. (1992) · Biochemical Journal · doi:10.1042/bj2810021 · Cited by 2,011
Transcriptional paradigms in mammalian mitochondrial biogenesis and function
Scarpulla, R. C. (2008) · Physiological Reviews · doi:10.1152/physrev.00025.2007 · Cited by 1,666
Towards a molecular understanding of adaptive thermogenesis
Lowell, B. B., & Spiegelman, B. M. (2000) · Nature · doi:10.1038/35007527 · Cited by 1,630
Metabolic control of mitochondrial biogenesis through the PGC-1 family regulatory network
Scarpulla, R. C. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2010.09.019 · Cited by 1,281
Essential Regulation of Cell Bioenergetics by Constitutive InsP3 Receptor Ca2+ Transfer to Mitochondria
Cárdenas, C., Miller, R. A., Smith, I., Bui, T., Molgó, J., Müller, M., Vais, H., Cheung, K.-H., Yang, J., Parker, I., et al. (2010) · Cell · doi:10.1016/j.cell.2010.06.007 · Cited by 1,026
Mitochondrial Dynamics in Mammalian Health and Disease
Liesa, M., Palacín, M., & Zorzano, A. (2009) · Physiological Reviews · doi:10.1152/physrev.00030.2008 · Cited by 953
Transcriptional integration of mitochondrial biogenesis
Scarpulla, R. C., Vega, R. B., & Kelly, D. P. (2012) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2012.06.006 · Cited by 798
Calcium Movements, Distribution, and Functions in Smooth Muscle
Karaki, H., Ozaki, H., Hori, M., Mitsui‐Saito, M., Amano, K.-I., Harada, K.-I., Miyamoto, S., Nakazawa, H., Won, K., & Sato, K. (1997) · Pharmacological Reviews · doi:10.1016/s0031-6997(24)01321-8 · Cited by 745
Is the Failing Heart Energy Starved?: On Using Chemical Energy to Support Cardiac Function
Ingwall, J. S., & Weiss, R. G. (2004) · Circulation Research · doi:10.1161/01.res.0000137170.41939.d9 · Cited by 604
Microcirculatory oxygenation and shunting in sepsis and shock
İnce, C., & Sinaasappel, M. (1999) · Critical Care Medicine · doi:10.1097/00003246-199907000-00031 · Cited by 541
In vivo NAD assay reveals the intracellular NAD contents and redox state in healthy human brain and their age dependences
Zhu, X.-H., Lu, M., Lee, B.-Y., Ugurbil, K., & Chen, W. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1417921112 · Cited by 468
Mitochondrial biogenesis and dynamics in the developing and diseased heart
Dorn, G. W., Vega, R. B., & Kelly, D. P. (2015) · Genes & Development · doi:10.1101/gad.269894.115 · Cited by 470
Mitochondrial reactive oxygen species production in excitable cells: Modulators of mitochondrial and cell function
Stowe, D. F., & Camara, A. K. S. (2009) · Antioxidants & Redox Signaling · doi:10.1089/ars.2008.2331 · Cited by 471
Ions and energy in mammalian brain
Erecińska, M., & Silver, I. A. (1994) · Progress in Neurobiology · doi:10.1016/0301-0082(94)90015-9 · Cited by 464
The Charcot-Marie-Tooth type 2A gene product, Mfn2, up-regulates fuel oxidation through expression of OXPHOS system
Pich, S., Bach, D., Briones, P., Liesa, M., Camps, M., Testar, X., Palacín, M., & Zorzano, A. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi149 · Cited by 455
Mitochondrial creatine kinase: a key enzyme of aerobic energy metabolism
Wyss, M., Smeitink, J. A. M., Wevers, R. A., & Wallimann, T. (1992) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(92)90096-k · Cited by 449
Neuronal Lipid Metabolism: Multiple Pathways Driving Functional Outcomes in Health and Disease
Tracey, T. J., Steyn, F. J., Wolvetang, E. J., & Ngo, S. T. (2018) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2018.00010 · Cited by 459
Uncoupling proteins 2 and 3: potential regulators of mitochondrial energy metabolism.
Boss, O., Hagen, T., & Lowell, B. B. (2000) · Diabetes · doi:10.2337/diabetes.49.2.143 · Cited by 414
Effect of Photic Stimulation on Human Visual Cortex Lactate and Phosphates Using 1 H and 31 P Magnetic Resonance Spectroscopy
Sappey‐Marinier, D., Calabrese, G., Fein, G., Hugg, J. W., Biggins, C. A., & Weiner, M. W. (1992) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.1992.82 · Cited by 413
Energy metabolism of the heart: From basic concepts to clinical applications applications
Taegtmeyer, H. (1994) · Current Problems in Cardiology · doi:10.1016/0146-2806(94)90008-6 · Cited by 392
Mitochondrial calcium transport: mechanisms and functions
Gunter, T. E., Buntinas, L., Sparagna, G. C., Eliseev, R. A., & Gunter, K. K. (2000) · Cell Calcium · doi:10.1054/ceca.2000.0168 · Cited by 378
Control of mitochondrial ATP synthesis in the heart
Harris, D. A., & Das, A. M. (1991) · Biochemical Journal · doi:10.1042/bj2800561 · Cited by 352
Mitochondrial Ca2+ homeostasis in intact cells.
Rizzuto, R., Bastianutto, C., Brini, M., Murgia, M., & Pozzan, T. (1994) · The Journal of Cell Biology · doi:10.1083/jcb.126.5.1183 · Cited by 323
Effect of Calcium on the Oxidative Phosphorylation Cascade in Skeletal Muscle Mitochondria
Glancy, B. C., Willis, W. T., Chess, D. J., & Balaban, R. S. (2013) · Biochemistry · doi:10.1021/bi3015983 · Cited by 299
Self-citation
Biosensors based on the energy metabolism of living cells: The physical chemistry and cell biology of extracellular acidification
Owicki, J. C., & Parce, J. W. (1992) · Biosensors and Bioelectronics · doi:10.1016/0956-5663(92)87004-9 · Cited by 273
Human muscle performance and PCr hydrolysis with varied inspired oxygen fractions: a 31 P-MRS study
Hogan, M. C., Richardson, R. S., & Haseler, L. J. (1999) · Journal of Applied Physiology · doi:10.1152/jappl.1999.86.4.1367 · Cited by 265
Regulation of oxygen consumption in fast- and slow-twitch muscle
Kushmerick, M. J., Meyer, R. A., & Brown, T. R. (1992) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1992.263.3.c598 · Cited by 258
Separate measures of ATP utilization and recovery in human skeletal muscle.
Blei, M. L., Conley, K. E., & Kushmerick, M. J. (1993) · The Journal of Physiology · doi:10.1113/jphysiol.1993.sp019673 · Cited by 256
Cardiac reperfusion injury: Aging, lipid peroxidation, and mitochondrial dysfunction
Lucas, D. T., & Szweda, L. I. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.2.510 · Cited by 254
Interaction of factors determining oxygen uptake at the onset of exercise
Tschakovsky, M. E., & Hughson, R. L. (1999) · Journal of Applied Physiology · doi:10.1152/jappl.1999.86.4.1101 · Cited by 254
Metabolic compartmentation and substrate channelling in muscle cells
Saks, V. A., Khuchua, Z. A., Vasilyeva, E. V., Belikova, O. Y., & Kuznetsov, A. V. (1994) · Molecular and Cellular Biochemistry · doi:10.1007/bf01267954 · Cited by 254
Altered Ca2+ Responses in Muscles with Combined Mitochondrial and Cytosolic Creatine Kinase Deficiencies
Steeghs, K., Benders, A. A. G. M., Oerlemans, F. T. J. J., HAAN, A. D., Heerschap, A., Ruitenbeek, W., Jost, C. R., van Deursen, J., Perryman, B., Pette, D., et al. (1997) · Cell · doi:10.1016/s0092-8674(00)80186-5 · Cited by 252
Cell Respiration is Controlled by ATP, an Allosteric Inhibitor of Cytochrome‐c Oxidase
Arnold, S., & Kadenbach, B. (1997) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1997.t01-1-00350.x · Cited by 240
Metabolic stress, reactive oxygen species, and arrhythmia
Jeong, E.-M., Liu, M., Sturdy, M., Gao, G., Varghese, S. T., Sovari, A. A., & Dudley, S. C. (2011) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2011.09.018 · Cited by 243
Metabolic Network Control of Oxidative Phosphorylation
Bose, S., French, S. A., Evans, F. J., Joubert, F., & Balaban, R. S. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306409200 · Cited by 210
Self-citation
Effect of induced metabolic alkalosis on human skeletal muscle metabolism during exercise
Hollidge-Horvat, M. G., Parolin, M. L., Wong, D., Jones, N. L., & Heigenhauser, G. J. F. (2000) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.2000.278.2.e316 · Cited by 208
31 P NMR Spectroscopy Detects Metabolic Abnormalities in Asymptomatic Patients With Hypertrophic Cardiomyopathy
Jung, W.-I., Sieverding, L., Breuer, J., Hoess, T., Widmaier, S., Schmidt, O., Bunse, M., van Erckelens, F., Apitz, J., Lutz, O., et al. (1998) · Circulation · doi:10.1161/01.cir.97.25.2536 · Cited by 197
Efficiency of human skeletal muscle in vivo: comparison of isometric, concentric, and eccentric muscle action
Ryschon, T. W., Fowler, M. D., Wysong, R. E., Anthony, A., & Balaban, R. S. (1997) · Journal of Applied Physiology · doi:10.1152/jappl.1997.83.3.867 · Cited by 196
Self-citation
Striking Differences Between the Kinetics of Regulation of Respiration by ADP in Slow‐Twitch and Fast‐Twitch Muscles In Vivo
Kuznetsov, A. V., Tiivel, T., Sikk, P., Käämbre, T., Kay, L., Daneshrad, Z., Rossi, A., Kadaja, L., Peet, N., Seppet, E. K., et al. (1996) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1996.00909.x · Cited by 199
Optical and pharmacological tools to investigate the role of mitochondria during oxidative stress and neurodegeneration
Foster, K. A., Galeffi, F., Gerich, F. J., Turner, D. A., & Müller, M. (2006) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2006.07.001 · Cited by 190
A model of oxidative phosphorylation in mammalian skeletal muscle
Korzeniewski, B., & Zoladz, J. A. (2001) · Biophysical Chemistry · doi:10.1016/s0301-4622(01)00184-3 · Cited by 183
Control of phosphocreatine resynthesis during recovery from exercise in human skeletal muscle
Kemp, G. J., Taylor, D. J. F., & Radda, G. K. (1993) · NMR in Biomedicine · doi:10.1002/nbm.1940060111 · Cited by 180
Mitochondrial dysfunction in bipolar disorder: Evidence, pathophysiology and translational implications
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 187
Role of mitochondrial calcium transport in the control of substrate oxidation
Hansford, R. G., & Zorov, D. B. (1998) · Springer eBooks · doi:10.1007/978-1-4615-5653-4_23 · Cited by 178
The Ca2+ transport mechanisms of mitochondria and Ca2+ uptake from physiological-type Ca2+ transients
Gunter, T. E., Buntinas, L., Sparagna, G. C., & Gunter, K. K. (1998) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(98)00117-0 · Cited by 166
Energetic costs regulated by cell mechanics and confinement are predictive of migration path during decision-making
Zanotelli, M. R., Rahman-Zaman, A., VanderBurgh, J. A., Taufalele, P. V., Jain, A., Erickson, D., Bordeleau, F., & Reinhart-King, C. A. (2019) · Nature Communications · doi:10.1038/s41467-019-12155-z · Cited by 165
Nucleus-encoded regulators of mitochondrial function: Integration of respiratory chain expression, nutrient sensing and metabolic stress
Scarpulla, R. C. (2011) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2011.10.011 · Cited by 173
Energy Metabolism during Insect Flight: Biochemical Design and Physiological Performance
Suarez, R. K. (2000) · Physiological and Biochemical Zoology · doi:10.1086/318112 · Cited by 160
Metabolic Flexibility: Hibernation, Torpor, and Estivation
Staples, J. F. (2016) · Comprehensive physiology · doi:10.1002/cphy.c140064 · Cited by 161
Direct Evidence for the Control of Mitochondrial Respiration by Mitochondrial Creatine Kinase in Oxidative Muscle Cells in Situ
Kay, L., Nicolay, K., Wieringa, B., Saks, V. A., & Wallimann, T. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.10.6937 · Cited by 159
In vivo regulation of mitochondrial respiration in cardiomyocytes: specific restrictions for intracellular diffusion of ADP
Saks, V. A., Belikova, Y. O., & Kuznetsov, A. V. (1991) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(91)90168-g · Cited by 156
The role of phosphorylcreatine and creatine in the regulation of mitochondrial respiration in human skeletal muscle
Walsh, B. J., Tonkonogi, M., Söderlund, K., Hultman, E., Saks, V. A., & Sahlin, K. (2001) · The Journal of Physiology · doi:10.1111/j.1469-7793.2001.00971.x · Cited by 172
ADP-Regulation of Mitochondrial Free Radical Production Is Different with Complex I- or Complex II-Linked Substrates: Implications for the Exercise Paradox and Brain Hypermetabolism
Herrero, A., & Barja, G. (1997) · Journal of Bioenergetics and Biomembranes · doi:10.1023/a:1022458010266 · Cited by 152
Progressive recruitment of muscle fibers is not necessary for the slow component of V o 2kinetics
Zoladz, J. A., Gladden, L. B., Hogan, M. C., Nieckarz, Z., & Grassi, B. (2008) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01129.2007 · Cited by 151
Role of mitochondrial calcium transport in the control of substrate oxidation
Hansford, R. G., & Zorov, D. B. (1998) · Molecular and Cellular Biochemistry · doi:10.1023/a:1006893903113 · Cited by 151
Mitochondrial Approaches to Protect Against Cardiac Ischemia and Reperfusion Injury
Camara, A. K. S., Bienengraeber, M., & Stowe, D. F. (2011) · Frontiers in Physiology · doi:10.3389/fphys.2011.00013 · Cited by 155
Substrate-dependent changes in mitochondrial function, intracellular free calcium concentration and membrane channels in pancreatic β-cells
Duchen, M. R., Smith, P. A., & Ashcroft, F. M. (1993) · Biochemical Journal · doi:10.1042/bj2940035 · Cited by 150
Fueling the cytoskeleton – links between cell metabolism and actin remodeling
DeWane, G., Salvi, A. M., & DeMali, K. A. (2021) · Journal of Cell Science · doi:10.1242/jcs.248385 · Cited by 156
The rapid mode of calcium uptake into heart mitochondria (RaM): comparison to RaM in liver mitochondria
Buntinas, L., Gunter, K. K., Sparagna, G. C., & Gunter, T. E. (2001) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(00)00254-1 · Cited by 149
Dynamics of oxygen uptake following exercise onset in rat skeletal muscle
Behnke, B. J., Barstow, T. J., Kindig, C. A., McDonough, P., Musch, T. I., & Poole, D. C. (2002) · Respiratory Physiology & Neurobiology · doi:10.1016/s1569-9048(02)00183-0 · Cited by 148
Integrating Metabolic Pathways in Post-Exercise Recovery of White Muscle
Schulte, P. M., Moyes, C. D., & Hochachka, P. W. (1992) · Journal of Experimental Biology · doi:10.1242/jeb.166.1.181 · Cited by 148
Declines in mitochondrial respiration during cardiac reperfusion: Age-dependent inactivation of α-ketoglutarate dehydrogenase
Lucas, D. T., & Szweda, L. I. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.12.6689 · Cited by 147
Retarded diffusion of ADP in cardiomyocytes: possible role of mitochondrial outer membrane and creatine kinase in cellular regulation of oxidative phosphorylation
Saks, V. A., Vasil'eva, E., Belikova, Y., Kuznetsov, A. V., Lyapina, S., Petrova, L., & Perov, N. A. (1993) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(93)90166-d · Cited by 145
Cellular Metabolic Homeostasis During Large-Scale Change in Atp Turnover Rates in Muscles
Hochachka, P. W., & McClelland, G. B. (1997) · Journal of Experimental Biology · doi:10.1242/jeb.200.2.381 · Cited by 142
Nutrient-sensing pathways and metabolic regulation in stem cells
Ochocki, J. D., & Simon, M. C. (2013) · Journal of Cell Biology · doi:10.1083/jcb.201303110 · Cited by 140
The metabolic implications of intracellular circulation
Hochachka, P. W. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.22.12233 · Cited by 137
Flying insects: model systems in exercise physiology
Wegener, G. (1996) · Cellular and Molecular Life Sciences · doi:10.1007/bf01919307 · Cited by 134
Adjustment of K′ to Varying pH and pMg for the Creatine Kinase, Adenylate Kinase and Atp Hydrolysis Equilibria Permitting Quantitative Bioenergetic Assessment
Golding, E. M., Teague, W. E., & Dobson, G. P. (1995) · Journal of Experimental Biology · doi:10.1242/jeb.198.8.1775 · Cited by 134
Mitochondrial biogenesis as a cellular signaling framework
Nisoli, E., Clementi, E., Moncada, S., & Carruba, M. O. (2003) · Biochemical Pharmacology · doi:10.1016/j.bcp.2003.10.015 · Cited by 131
Mitochondrial pathology in cardiac failure
Marín-García, J. (2001) · Cardiovascular Research · doi:10.1016/s0008-6363(00)00241-8 · Cited by 128
Fall in intracellular P o 2at the onset of contractions inXenopussingle skeletal muscle fibers
Hogan, M. C. (2001) · Journal of Applied Physiology · doi:10.1152/jappl.2001.90.5.1871 · Cited by 129
Diabetes, Oxidative Stress, Nitric Oxide and Mitochondria Function
Friederich, M., Hansell, P., & Palm, F. (2009) · Current Diabetes Reviews · doi:10.2174/157339909788166800 · Cited by 128
Elevated Medium-Chain Acylcarnitines Are Associated With Gestational Diabetes Mellitus and Early Progression to Type 2 Diabetes and Induce Pancreatic β-Cell Dysfunction
Batchuluun, B., Rijjal, D. A., Prentice, K. J., Eversley, J. A., Burdett, E., Mohan, H., Bhattacharjee, A., Gunderson, E. P., Liu, Y., & Wheeler, M. B. (2018) · Diabetes · doi:10.2337/db17-1150 · Cited by 134
The Oxygen Paradox of Neurovascular Coupling
Leithner, C., & Royl, G. (2013) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.2013.181 · Cited by 126
Mitochondrial Pathophysiology, Reactive Oxygen Species, and Cardiovascular Diseases
Gao, L., Laude, K. M., & Cai, H. “. (2008) · Veterinary Clinics of North America Small Animal Practice · doi:10.1016/j.cvsm.2007.10.004 · Cited by 128
Mitochondria-controlled signaling mechanisms of brain protection in hypoxia
Lukyanova, L. D., & Kirova, Y. I. (2015) · Frontiers in Neuroscience · doi:10.3389/fnins.2015.00320 · Cited by 126
Role of AHR and HIF-1α in Glioblastoma Metabolism
Gabriely, G., Wheeler, M. A., Takenaka, M. C., & Quintana, F. J. (2017) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2017.02.009 · Cited by 124
The osteopetrotic mutation toothless ( tl ) is a loss-of-function frameshift mutation in the rat Csf1 gene: Evidence of a crucial role for CSF-1 in osteoclastogenesis and endochondral ossification
Wesenbeeck, L. V., Odgren, P. R., MacKay, C. A., D’Angelo, M., Safadi, F. F., Popoff, S. N., Hul, W. V., & Marks, S. C. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.202332999 · Cited by 122
Role of convective O2 delivery in determiningV˙ o 2 on-kinetics in canine muscle contracting at peak V˙ o 2
Grassi, B., Hogan, M. C., Kelley, K. M., Aschenbach, W. G., Hamann, J. J., Evans, R. K., Patillo, R. E., & Gladden, L. B. (2000) · Journal of Applied Physiology · doi:10.1152/jappl.2000.89.4.1293 · Cited by 121
Oxygen uptake on‐kinetics in dog gastrocnemius in situ following activation of pyruvate dehydrogenase by dichloroacetate
Grassi, B., Hogan, M. C., Greenhaff, P. L., Hamann, J. J., Kelley, K. M., Aschenbach, W. G., Constantin‐Teodosiu, D., & Gladden, L. B. (2002) · The Journal of Physiology · doi:10.1113/jphysiol.2001.012984 · Cited by 120
Substrate Metabolism as a Determinant for Postischemic Functional Recovery of the Heart
Taegtmeyer, H., Goodwin, G. W., Doenst, T., & Frazier, O. H. (1997) · The American Journal of Cardiology · doi:10.1016/s0002-9149(97)00452-9 · Cited by 120
Effect of amyloid β‐peptide on permeability transition pore: A comparative study
Moreira, P. I., Santos, M. S., Moreno, A. J., Rego, A. C., & Oliveira, C. R. (2002) · Journal of Neuroscience Research · doi:10.1002/jnr.10282 · Cited by 120
Phosphate metabolite concentrations and ATP hydrolysis potential in normal and ischaemic hearts
Wu, F., Zhang, E. Y., Zhang, J. J., Bache, R. J., & Beard, D. A. (2008) · The Journal of Physiology · doi:10.1113/jphysiol.2008.154732 · Cited by 119
Coupling between cytosolic and mitochondrial calcium oscillations: role in the regulation of hepatic metabolism
Gaspers, L. D., Rutter, G. A., Burnett, P., Hajnóczky, G., Denton, R. M., & Thomas, A. P. (1998) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(98)00118-2 · Cited by 113
Untitled work
(1996) · doi:10.1002/cphy.cp120118 · Cited by 113
Measuring mitochondrial function in intact cardiac myocytes
Dedkova, E. N., & Blatter, L. A. (2011) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2011.08.030 · Cited by 118
Compartmentalized energy transfer in cardiomyocytes: use of mathematical modeling for analysis of in vivo regulation of respiration
Aliev, M., & Saks, V. A. (1997) · Biophysical Journal · doi:10.1016/s0006-3495(97)78082-2 · Cited by 111
In vivo ATP synthesis rates in single human muscles during high intensity exercise
Walter, G., Vandenborne, K., Elliott, M. A., & LEIGH, J. S. J. (1999) · The Journal of Physiology · doi:10.1111/j.1469-7793.1999.0901n.x · Cited by 110
Carbon monoxide released by CORM-3 inhibits human platelets by a mechanism independent of soluble guanylate cyclase
Chłopicki, S., Olszanecki, R., Marcinkiewicz, E., Łomnicka, M., & Motterlini, R. (2006) · Cardiovascular Research · doi:10.1016/j.cardiores.2006.03.011 · Cited by 108
Mitochondrial creatine kinase: a key enzyme of aerobic energy metabolism
Wyss, M., Smeitink, J. A. M., Wevers, R. A., & Wallimann, T. (1992) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(92)90506-9 · Cited by 108
Metabolic compartmentation and substrate channelling in muscle cells
Saks, V. A., Khuchua, Z. A., Vasilyeva, E. V., Belikova, O. Y., & Kuznetsov, A. V. (1994) · Springer eBooks · doi:10.1007/978-1-4615-2612-4_12 · Cited by 107
31P magnetic resonance spectroscopy of the Sherpa heart: a phosphocreatine/adenosine triphosphate signature of metabolic defense against hypobaric hypoxia.
Hochachka, P. W., Clark, C. M., Holden, J. E., Stanley, C., Uǧurbil, K., & Menon, R. S. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.3.1215 · Cited by 106
Fatigue and its impact on patients with myasthenia gravis
Paul, R. H., Cohen, R. A., Goldstein, J. M., & Gilchrist, J. M. (2000) · Muscle & Nerve · doi:10.1002/1097-4598(200009)23:9 · Cited by 95
Noninvasive Assessment of Changes in Cytochrome- c Oxidase Oxidation in Human Subjects during Visual Stimulation
Heekeren, H. R., Kohl, M., Obrig, H., Wenzel, R., Pannwitz, W. V., Matcher, S. J., Dirnagl, U., Cooper, C. E., & Villringer, A. (1999) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1097/00004647-199906000-00002 · Cited by 102
Efficiency of oxidative work performance of skeletal muscle in patients with cystic fibrosis.
de Meer, K., Jeneson, J. A. L., Gulmans, V. A. M., van der Laag, J., & Berger, R. (1995) · Thorax · doi:10.1136/thx.50.9.980 · Cited by 99
A metabolic control analysis of kinetic controls in ATP free energy metabolism in contracting skeletal muscle.
Jeneson, J. A., Westerhoff, H. V., & Kushmerick, M. (2000) · American Journal of Physiology - Cell Physiology · doi:10.1152/ajpcell.2000.279.3.c813 · Cited by 99
Myocardial Energy Metabolism During Ischemia and the Mechanisms of Metabolic Therapies
Stanley, W. C. (2004) · Journal of Cardiovascular Pharmacology and Therapeutics · doi:10.1177/107424840400900104 · Cited by 94
Bioenergetics of skeletal muscle in mitochondrial myopathy
Taylor, D. J., Kemp, G. J., & Radda, G. K. (1994) · Journal of the Neurological Sciences · doi:10.1016/0022-510x(94)90073-6 · Cited by 94
Pyridine Nucleotide Regulation of Cardiac Intermediary Metabolism
Ussher, J. R., Jaswal, J. S., & Lopaschuk, G. D. (2012) · Circulation Research · doi:10.1161/circresaha.111.246371 · Cited by 94

Authors: Balaban, R. S.
Affiliations: National Institutes of Health (US)
Corresponding author: Balaban, R. S.
ORCID: Balaban, R. S.
Venue: American Journal of Physiology-Cell Physiology
Publisher: American Physiological Society
Published: 1990-03-01
Volume: 258
Issue: 3
Pages: C377-C389
ISSN: 0363-6143 (ISSN-L)
1522-1563
DOI: 10.1152/ajpcell.1990.258.3.c377
OpenAlex: W2129533522
Cited by: 446
References: 73
Citations by year: 2026: 4 · 2025: 4 · 2024: 6 · 2023: 4 · 2022: 8 · 2021: 11 · 2020: 8 · 2019: 8 · 2018: 9 · 2017: 6 · 2016: 14 · 2015: 11 · 2014: 8 · 2013: 10 · 2012: 14
FWCI: 6.56
Type: journal article
Language: en
Open access: closed
Locations: American Journal of Physiology-Cell Physiology (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
Keywords: oxidative phosphorylation, energy metabolism regulation, ATP hydrolysis, mitochondrial ATP production, oxygen delivery, heart, brain, kidney
MeSH terms: Adenosine Triphosphatases, Adenosine Triphosphate, Animals, Homeostasis, Mammals, Models, Biological, Oxidative Phosphorylation

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

Regulation of oxidative phosphorylation in the mammalian cell

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks