Cited by 202Mitochondrial Function and PathologyATP Synthase and ATPases ResearchMetabolism and Genetic Disorders

The DOI matches its Crossref record; 44 of the 51 references it cites were found in a registry or an index.

Tissue variation in the control of oxidative phosphorylation: implication for mitochondrial diseases

Open access

ROSSIGNOL, Rodrigue, LETELLIER, Thierry, MALGAT, Monique, ROCHER, Christophe, MAZAT, Jean-Pierre·2000·Biochemical Journal

DOI 10.1042/bj3470045PMC PMC1220929

Open this paper in CoChat — free account Open PDF

Abstract

Metabolic control analysis has often been used for quantitative studies of the regulation of mitochondrial oxidative phosphorylations (OXPHOS). The main contribution of this work has been to show that the control of mitochondrial metabolic fluxes can be shared among several steps of the oxidative phosphorylation process, and that this distribution can vary according to the steady state and the tissue. However, these studies do not show whether this observed variation in the OXPHOS control is due to the experimental conditions or to the nature of the mitochondria. To find out if there actually exists a tissue variation in the distribution of OXPHOS control coefficients, we determined the control coefficients of seven OXPHOS complexes on the oxygen-consumption flux in rat mitochondria isolated from five different tissues under identical experimental conditions. Thus in this work, only the nature of the mitochondria can be responsible for any variation detected in the control coefficient values between different tissues. The analysis of control coefficient distribution shows two tissue groups: (i) the muscle and the heart, controlled essentially at the level of the respiratory chain; and (ii) the liver, the kidney and the brain, controlled mainly at the phosphorylation level by ATP synthase and the phosphate carrier. We propose that this variation in control coefficient according to the tissue origin of the mitochondria can explain part of the tissue specificity observed in mitochondrial cytopathies.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1042/bj3470045

Cites

44 of 44 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

The Respiratory Chain and Oxidative Phosphorylation
Chance, B., & Williams, G. R. (1956) · Advances in enzymology and related areas of molecular biology/Advances in enzymology and related subjects · doi:10.1002/9780470122624.ch2 · Cited by 2,084
The control of flux.
KACSER, H., & Ja, B. (1973) · PubMed · Cited by 1,455
A Linear Steady-State Treatment of Enzymatic Chains. General Properties, Control and Effector Strength
Heinrich, R., & Rapoport, T. A. (1974) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1974.tb03318.x · Cited by 1,400
Diseases of the mitochondrial DNA
Wallace, D. C. (1992) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.61.070192.005523 · Cited by 1,319
THE MOLECULAR BASIS OF DOMINANCE
KACSER, H., & Burns, J. A. (1981) · Genetics · doi:10.1093/genetics/97.3-4.639 · Cited by 1,040
Metabolic control analysis: a survey of its theoretical and experimental development
Fell, D. A. (1992) · Biochemical Journal · doi:10.1042/bj2860313 · Cited by 782
Mitochondrial myopathies
DiMauro, S., Bonilla, E., Zeviani, M., Nakagawa, M., & Vivo, D. C. D. (1985) · Annals of Neurology · doi:10.1002/ana.410170602 · Cited by 703
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
The Metabolism of Rat Brain Mitochondria
Clark, J. B., & Nicklas, W. J. (1970) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)62854-6 · Cited by 560
Metabolic control theory: A structural approach
Reder, C. (1988) · Journal of Theoretical Biology · doi:10.1016/s0022-5193(88)80073-0 · Cited by 551

Show all 51 references

Research works printed but not linked: 3

Kacser, H. and Burns, J. A. in Rate Control of Biological Processes (1973) (Davies, D. D., ed.), pp. 65-104, Cambridge University Press, Cambridge
Jumelle-Laclau, M. (1993) Ph.D. Thesis, Universite! Victor Segalen-Bordeaux 2 11
Morgan-Hughes, J. A. (1986) in Myology (Engel, A. G. and Banker, B. Q., eds.), pp. 1709-1743, McGraw Hill, New York

Sorted by citations

Mitochondrial threshold effects
Rossignol, R., Faustin, B., Rocher, C., Malgat, M., Mazat, J., & Letellier, T. (2003) · Biochemical Journal · doi:10.1042/bj20021594 · Cited by 816
Self-citation
Complex I-mediated reactive oxygen species generation: modulation by cytochrome c and NAD(P)+ oxidation–reduction state
Kushnareva, Y., Murphy, A. N., & Andreyev, A. Y. (2002) · Biochemical Journal · doi:10.1042/bj20021121 · Cited by 696
The role of mitochondria in insulin resistance and type 2 diabetes mellitus
Szendroedi, J., Phielix, E., & Roden, M. (2012) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2011.138 · Cited by 600
Choosing between glycolysis and oxidative phosphorylation: a tumor’s dilemma?
Jose, C., Bellance, N., & Rossignol, R. (2011) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.10.012 · Cited by 518
Self-citation
Oxidative stress, mitochondrial dysfunction and cellular stress response in Friedreich's ataxia
Calabrese, V., Lodi, R., Tonon, C., D’Agata, V., Sapienza, M. A., Scapagnini, G., Mangiameli, A., Pennisi, G., Stella, A. M. G., & Butterfield, D. A. (2005) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2005.03.012 · Cited by 411
New insights into doxorubicin-induced cardiotoxicity: The critical role of cellular energetics
Tokarska-Schlattner, M., Zaugg, M., Zuppinger, C., Wallimann, T., & Schlattner, U. (2006) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2006.06.009 · Cited by 353
Cytochrome c oxidase and mitochondrial F1F0-ATPase (ATP synthase) activities in platelets and brain from patients with Alzheimer’s disease
Bosetti, F. (2002) · Neurobiology of Aging · doi:10.1016/s0197-4580(01)00314-1 · Cited by 348
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
Physiological diversity of mitochondrial oxidative phosphorylation
Benard, G., Faustin, B., Passerieux, E., Galinier, A., Rocher, C., Bellance, N., Delage, J.-P., Casteilla, L., Letellier, T., & Rossignol, R. (2006) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00195.2006 · Cited by 297
Self-citation
Mitochondrial dysfunction, free radical generation and cellular stress response in neurodegenerative disorders
Mancuso, C. (2006) · Frontiers in bioscience · doi:10.2741/2130 · Cited by 290
Metabolic control analysis in drug discovery and disease
Cascante, M., Boros, L. G., Comı́n-Anduix, B., de Atauri, P., Centelles, J. J., & Lee, P. W. N. (2002) · Nature Biotechnology · doi:10.1038/nbt0302-243 · Cited by 281
Mitochondrial involvement in brain function and dysfunction: relevance to aging, neurodegenerative disorders and longevity
Calabrese, V., Scapagnini, G., Giuffrida Stella, A. M., Bates, T. E., & Clark, J. B. (2001) · Neurochemical Research · doi:10.1023/a:1010955807739 · Cited by 263
Association of mitochondrial function and feed efficiency in poultry and livestock species1
Bottje, W. G., & Carstens, G. E. (2008) · Journal of Animal Science · doi:10.2527/jas.2008-1379 · Cited by 268
Mitochondrial energy generation disorders: genes, mechanisms, and clues to pathology
Frazier, A. E., Thorburn, D. R., & Compton, A. G. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.r117.809194 · Cited by 267
Biochemical dysfunction in heart mitochondria exposed to ischaemia and reperfusion
Solaini, G., & Harris, D. A. (2005) · Biochemical Journal · doi:10.1042/bj20042006 · Cited by 255
Mitochondrial medicine: A metabolic perspective on the pathology of oxidative phosphorylation disorders
Smeitink, J. A. M., Zeviani, M., Turnbull, D. M., & Jacobs, H. T. (2006) · Cell Metabolism · doi:10.1016/j.cmet.2005.12.001 · Cited by 251
Gradual Alteration of Mitochondrial Structure and Function by β-Amyloids: Importance of Membrane Viscosity Changes, Energy Deprivation, Reactive Oxygen Species Production, and Cytochrome c Release
Aleardi, A. M., Benard, G., Augereau, O., Malgat, M., Talbot, J.-C., Mazat, J., Letellier, T., Dachary-Prigent, J., Solaini, G., & Rossignol, R. (2005) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-005-6631-3 · Cited by 227
Self-citation
Metabolic Control Analysis: A Tool for Designing Strategies to Manipulate Metabolic Pathways
Moreno‐Sánchez, R., Saavedra, E., Rodríguez‐Enríquez, S., & Olín‐Sandoval, V. (2008) · BioMed Research International · doi:10.1155/2008/597913 · Cited by 208
Tissue-specific differences in mitochondrial activity and biogenesis
Fernández‐Vizarra, E., Enrı́quez, J. A., Martos, A. P., Montoya, J., & Fernández‐Silva, P. (2010) · Mitochondrion · doi:10.1016/j.mito.2010.09.011 · Cited by 195
Mitochondrial medicine--molecular pathology of defective oxidative phosphorylation.
Fosslien, E. (2001) · PubMed · Cited by 186
Mitochondrial genetics and disease
Schon, E. A. (2000) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)01688-1 · Cited by 172
Formulation, construction and analysis of kinetic models of metabolism: A review of modelling frameworks
Saa, P. A., & Nielsen, L. K. (2017) · Biotechnology Advances · doi:10.1016/j.biotechadv.2017.09.005 · Cited by 166
Glutamine homeostasis and mitochondrial dynamics
Matés, J. M., Segura, J. A., Campos-Sandoval, J. A., Lobo, C., Alonso, L., Alonso, F. J., & Márquez, J. (2009) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2009.03.003 · Cited by 157
The role of mitochondrial respiration in physiological and evolutionary adaptation
Das, J. (2006) · BioEssays · doi:10.1002/bies.20463 · Cited by 158
Emerging concepts in bioenergetics and cancer research: metabolic flexibility, coupling, symbiosis, switch, oxidative tumors, metabolic remodeling, signaling and bioenergetic therapy
Obre, E., & Rossignol, R. (2015) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2014.12.008 · Cited by 137
Self-citation
Selection against Pathogenic mtDNA Mutations in a Stem Cell Population Leads to the Loss of the 3243A→G Mutation in Blood
Rajasimha, H. K., Chinnery, P. F., & Samuels, D. C. (2008) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2007.10.007 · Cited by 137
Mitochondrial dysfunction in Huntington’s disease: the bioenergetics of isolated and in situ mitochondria from transgenic mice
Oliveira, J. M. A., Jekabsons, M. B., Chen, S., Lin, A., Rego, A. C., Gonçalves, J., Ellerby, L., & Nicholls, D. G. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04361.x · Cited by 136
Control of glutathione and phytochelatin synthesis under cadmium stress. Pathway modeling for plants
Mendoza‐Cózatl, D. G., & Moreno‐Sánchez, R. (2005) · Journal of Theoretical Biology · doi:10.1016/j.jtbi.2005.07.003 · Cited by 127
Emerging Roles of ROS/RNS in Muscle Function and Fatigue
Westerblad, H., & Allen, D. G. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.3909 · Cited by 130
Review: Quantifying Mitochondrial Dysfunction in Complex Diseases of Aging
Horan, M. P., Pichaud, N., & Ballard, J. W. O. (2012) · The Journals of Gerontology Series A · doi:10.1093/gerona/glr263 · Cited by 136
Redox Regulation of Heat Shock Protein Expression by Signaling Involving Nitric Oxide and Carbon Monoxide: Relevance to Brain Aging, Neurodegenerative Disorders, and Longevity
Calabrese, V., Butterfield, D. A., Scapagnini, G., Stella, A. M. G., & Maines, M. D. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.444 · Cited by 122
Multi-site control and regulation of mitochondrial energy production
Bénard, G., Bellancé, N., José, C., Melser, S., Nouette‐Gaulain, K., & Rossignol, R. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.02.030 · Cited by 126
Self-citation
Bioenergetics shapes cellular death pathways in Leber's hereditary optic neuropathy: a model of mitochondrial neurodegeneration
Carelli, V., Rugolo, M., Sgarbi, G., Ghelli, A. M., Zanna, C., Baracca, A., Lenaz, G., Napoli, E., Martinuzzi, A., & Solaini, G. (2004) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2004.05.009 · Cited by 119
Active oligomeric ATP synthases in mammalian mitochondria
Krause, F., Reifschneider, N. H., Goto, S., & Dencher, N. A. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.02.010 · Cited by 120
Mitochondrial Dysfunction Induced by Sertraline, an Antidepressant Agent
Li, Y., Couch, L., Higuchi, M., Fang, J.-L., & Guo, L. (2012) · Toxicological Sciences · doi:10.1093/toxsci/kfs100 · Cited by 120
Targeting of cancer energy metabolism
Rodríguez‐Enríquez, S., Marín‐Hernández, Á., Gallardo‐Pérez, J. C., Carreño‐Fuentes, L., & Moreno‐Sánchez, R. (2009) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.200700470 · Cited by 119
Control of Mitochondrial Respiration by NO., Effects of Low Oxygen and Respiratory State
Brookes, P. S., Kraus, D. W., Shiva, S., Doeller, J. E., Barone, M.-C., Patel, R. P., Lancaster, J. R., & Darley-Usmar, V. M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m211784200 · Cited by 118
Cancer cachexia is associated with a decrease in skeletal muscle mitochondrial oxidative capacities without alteration of ATP production efficiency
Julienne, C. M., Dumas, J., Goupille, C., Pinault, M., Berri, C., Collin, A., Tesseraud, S., Couet, C., & Servais, S. (2012) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1007/s13539-012-0071-9 · Cited by 116
Oxazolidinones Inhibit Cellular Proliferation via Inhibition of Mitochondrial Protein Synthesis
Nagiec, E. E., Wu, L., Swaney, S. M., Chosay, J. G., Ross, D. E., Brieland, J. K., & Leach, K. L. (2005) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.49.9.3896-3902.2005 · Cited by 113
In Vivo Fluorescent Adenosine 5′-Triphosphate (ATP) Imaging of Drosophila melanogaster and Caenorhabditis elegans by Using a Genetically Encoded Fluorescent ATP Biosensor Optimized for Low Temperatures
Tsuyama, T., Kishikawa, J.-I., Han, Y.-W., Harada, Y., Tsubouchi, A., Noji, H., Kakizuka, A., Yokoyama, K., Uemura, T., & Imamura, H. (2013) · Analytical Chemistry · doi:10.1021/ac4015325 · Cited by 111
Altered zinc transport disrupts mitochondrial protein processing/import in fragile X-associated tremor/ataxia syndrome
Napoli, E., Ross‐Inta, C., Wong, S., Omanska-Klusek, A., Barrow, C., Iwahashi, C., Garcia-Arocena, D., Sakaguchi, D., Berry‐Kravis, E., Hagerman, R. J., et al. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr211 · Cited by 107
Training at high exercise intensity promotes qualitative adaptations of mitochondrial function in human skeletal muscle
Daussin, F., Zoll, J., Ponsot, E., Dufour, S. P., Doutreleau, S., Lonsdorfer‐Wolf, E., Ventura‐Clapier, R., Mettauer, B., Piquard, F., Gény, B., et al. (2008) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01135.2007 · Cited by 112
Alterations in renal mitochondrial respiration in response to the reactive oxoaldehyde methylglyoxal
Rosca, M. G., Monnier, V. M., Szweda, L. I., & Weiss, M. F. (2002) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00302.2001 · Cited by 104
A Novel Kinetic Assay of Mitochondrial ATP-ADP Exchange Rate Mediated by the ANT
Chinopoulos, C., Vajda, S., Csanády, L., Mándi, M., Mathe, K., & Ádám‐Vizi, V. (2009) · Biophysical Journal · doi:10.1016/j.bpj.2008.12.3915 · Cited by 104
Glutaredoxin-2 Is Required to Control Oxidative Phosphorylation in Cardiac Muscle by Mediating Deglutathionylation Reactions
Mailloux, R. J., Xuan, J. Y., McBride, S., Maharsy, W. M., Thorn, S., Holterman, C. E., Kennedy, C., Rippstein, P. U., deKemp, R. A., da Silva, J., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.550574 · Cited by 101
RETRACTED: mTERF2 Regulates Oxidative Phosphorylation by Modulating mtDNA Transcription
Wenz, T., Luca, C. C., Torraco, A., & Moraes, C. T. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2009.04.010 · Cited by 99
Retracted
Increased Mitochondrial Mass in Cells with Functionally Compromised Mitochondria after Exposure to both Direct γ Radiation and Bystander Factors
Nugent, S., Mothersill, C. E., Seymour, C. B., McClean, B., Lyng, F. M., & Murphy, J. E. J. (2007) · Radiation Research · doi:10.1667/rr0769.1 · Cited by 98
Flux Control of Cytochrome c Oxidase in Human Skeletal Muscle
Kunz, W. S., Kudin, A. P., Vielhaber, S., Elger, C. E., Attardi, G. M., & Villani, G. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m004833200 · Cited by 96
Mitochondria in the human heart
Lemieux, H., & Hoppel, C. L. (2009) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-009-9211-0 · Cited by 93
Control by cytochromecoxidase of the cellular oxidative phosphorylation system depends on the mitochondrial energy state
Piccoli, C., Scrima, R., Boffoli, D., & Capitanio, N. (2006) · Biochemical Journal · doi:10.1042/bj20060077 · Cited by 92
Disorders of mitochondrial protein synthesis
Jacobs, H. T. (2003) · Human Molecular Genetics · doi:10.1093/hmg/ddg285 · Cited by 91
The reduced concentration of citrate in cancer cells: An indicator of cancer aggressiveness and a possible therapeutic target
Icard, P., & Lincet, H. (2016) · Drug Resistance Updates · doi:10.1016/j.drup.2016.09.003 · Cited by 86
What do mitochondrial diseases teach us about normal mitochondrial functions... that we already knew: threshold expression of mitochondrial defects
Mazat, J., Rossignol, R., Malgat, M., Rocher, C., Faustin, B., & Letellier, T. (2001) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(00)00236-x · Cited by 85
Self-citation
Bioenergetics of lung tumors: Alteration of mitochondrial biogenesis and respiratory capacity
Bellancé, N., Bénard, G., Furt, F., Bégueret, H., Smolková, K., Passerieux, E., Delage, J. P., Baste, J., Moreau, P., & Rossignol, R. (2009) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2009.08.012 · Cited by 85
Self-citation
Mitochondrial tissue specificity of substrates utilization in rat cardiac and skeletal muscles
Ponsot, E., Zoll, J., N'Guessan, B., Ribera, F., Lampert, E., Richard, R., Veksler, V., Ventura‐Clapier, R., & Mettauer, B. (2005) · Journal of Cellular Physiology · doi:10.1002/jcp.20245 · Cited by 83
Energy metabolism design of the striated muscle cell
Glancy, B. C., & Balaban, R. S. (2021) · Physiological Reviews · doi:10.1152/physrev.00040.2020 · Cited by 86
Control of Respiration by Cytochrome c Oxidase in Intact Cells
Dalmonte, M. E., Forte, E., Genova, M. L., Giuffrè, A., Sarti, P., & Lenaz, G. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.050146 · Cited by 81
Thermal instability of compound variants of carnitine palmitoyltransferase II and impaired mitochondrial fuel utilization in influenza-associated encephalopathy
Yao, D., Mizuguchi, H., Yamaguchi, M., Yamada, H., Chida, J., Shikata, K., & Kido, H. (2008) · Human Mutation · doi:10.1002/humu.20717 · Cited by 79
Measurement of Mitochondrial Oxygen Consumption Using a Clark Electrode
Li, Z., & Graham, B. H. (2011) · Methods in molecular biology · doi:10.1007/978-1-61779-504-6_5 · Cited by 78
Drug discovery strategies in the field of tumor energy metabolism: Limitations by metabolic flexibility and metabolic resistance to chemotherapy
Amoedo, N. D., Obre, E., & Rossignol, R. (2017) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2017.02.005 · Cited by 76
Self-citation
AMP-activated protein kinase mediates activity-dependent regulation of peroxisome proliferator-activated receptor γ coactivator-1α and nuclear respiratory factor 1 expression in rat visual cortical neurons
Yu, L., & Yang, S. J. (2010) · Neuroscience · doi:10.1016/j.neuroscience.2010.04.063 · Cited by 76
Increased mitochondrial Ca 2+ and decreased sarcoplasmic reticulum Ca 2+ in mitochondrial myopathy
Aydin, J., Andersson, D. C., Hänninen, S. L., Wredenberg, A., Tavi, P., Park, C. B., Larsson, N.-G., Bruton, J. D., & Westerblad, H. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddn355 · Cited by 75
Localization of PTP-1B, SHP-2, and Src Exclusively in Rat Brain Mitochondria and Functional Consequences
Arachiche, A., Augereau, O., Décossas, M., Pertuiset, C., Gontier, É., Letellier, T., & Dachary-Prigent, J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m709217200 · Cited by 73
Self-citation
Defective mitochondrial disulfide relay system, altered mitochondrial morphology and function in Huntington's disease
Napoli, E., Wong, S., Hung, C., Ross‐Inta, C., Bomdica, P. R., & Giulivi, C. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds503 · Cited by 72
Retained features of embryonic metabolism in the adult MRL mouse
Naviaux, R. K., Le, T. P., Bedelbaeva, K., Leferovich, J. M., Gourevitch, D., Sachadyn, P., Zhang, X., Clark, L. D., & Heber‐Katz, E. (2009) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2008.11.164 · Cited by 72
An in situ study of bioenergetic properties of human colorectal cancer: The regulation of mitochondrial respiration and distribution of flux control among the components of ATP synthasome
Kaldma, A., Klepinin, A., Chekulayev, V. A., Mado, K., Shevchuk, I. N., Timohhina, N., Tepp, K., Kandashvili, M., Varikmaa, M., Koit, A., et al. (2014) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2014.09.004 · Cited by 72
Complex I Is Rate-limiting for Oxygen Consumption in the Nerve Terminal
Telford, J. E., Kilbride, S. M., & Davey, G. P. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m809101200 · Cited by 70
Glutathione deficiency in patients with mitochondrial disease: Implications for pathogenesis and treatment
Hargreaves, I. P., Sheena, Y., Land, J. M., & Heales, S. (2005) · Journal of Inherited Metabolic Disease · doi:10.1007/s10545-005-4160-1 · Cited by 68
The GRACILE mutation introduced into Bcs1l causes postnatal complex III deficiency: A viable mouse model for mitochondrial hepatopathy
Levéen, P., Kotarsky, H., Mörgelin, M., Karikoski, R., Elmér, E., & Fellman, V. (2010) · Hepatology · doi:10.1002/hep.24031 · Cited by 68
A Possible Link Between Skeletal Muscle Mitochondrial Efficiency and Age-Induced Insulin Resistance
Iossa, S., Mollica, M. P., Lionetti, L., Crescenzo, R., Tasso, R., & Liverini, G. (2004) · Diabetes · doi:10.2337/diabetes.53.11.2861 · Cited by 69
Control and Regulation of Mitochondrial Energetics in an Integrated Model of Cardiomyocyte Function
Cortassa, S. C., O'Rourke, B. P., Winslow, R. L., & Aon, M. A. (2009) · Biophysical Journal · doi:10.1016/j.bpj.2008.12.3893 · Cited by 66
Multi-tissue Analysis of Co-expression Networks by Higher-Order Generalized Singular Value Decomposition Identifies Functionally Coherent Transcriptional Modules
Xiao, X., Moreno-Moral, A., Rotival, M., Bottolo, L., & Petretto, E. (2014) · PLoS Genetics · doi:10.1371/journal.pgen.1004006 · Cited by 63
Functional dynamic compartmentalization of respiratory chain intermediate substrates: Implications for the control of energy production and mitochondrial diseases
Benard, G., Faustin, B., Galinier, A., Rocher, C., Bellancé, N., Smolková, K., Casteilla, L., Rossignol, R., & Letellier, T. (2008) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2007.11.023 · Cited by 63
Self-citation
Influence of mitochondrial DNA level on cellular energy metabolism: implications for mitochondrial diseases
Rocher, C., Taanman, J., Pierron, D., Faustin, B., Benard, G., Rossignol, R., Malgat, M., Pédespan, L., & Letellier, T. (2008) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-008-9130-5 · Cited by 63
Self-citation
Gene Expression in Breast Muscle and Duodenum from Low and High Feed Efficient Broilers
Ojano-Dirain, C. P., Toyomizu, M., Wing, T., Cooper, M., & Bottje, W. G. (2007) · Poultry Science · doi:10.1093/ps/86.2.372 · Cited by 67
Oxidative metabolism and efficiency: the delicate balancing act of mitochondria
Bottje, W. G. (2018) · Poultry Science · doi:10.3382/ps/pey405 · Cited by 71
Towards an Understanding of Energy Impairment in Huntington’s Disease Brain
Dubinsky, J. M. (2017) · Journal of Huntington s Disease · doi:10.3233/jhd-170264 · Cited by 63
Top-down control analysis of the effect of temperature on ectotherm oxidative phosphorylation
Chamberlin, M. E. (2004) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00240.2004 · Cited by 60
Mitoenergetic Dysfunction Triggers a Rapid Compensatory Increase in Steady-State Glucose Flux
Liemburg-Apers, D. C., Schirris, T. J. J., Rüssel, F. G. M., Willems, P. H. G. M., & Koopman, W. J. H. (2015) · Biophysical Journal · doi:10.1016/j.bpj.2015.08.002 · Cited by 59
Each‐step activation of oxidative phosphorylation is necessary to explain muscle metabolic kinetic responses to exercise and recovery in humans
Korzeniewski, B., & Rossiter, H. B. (2015) · The Journal of Physiology · doi:10.1113/jp271299 · Cited by 58
How understanding the control of energy metabolism can help investigation of mitochondrial dysfunction, regulation and pharmacology
Murphy, M. P. (2001) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(00)00234-6 · Cited by 56
Training‐induced acceleration of O2uptake on‐kinetics precedes muscle mitochondrial biogenesis in humans
Zoladz, J. A., Grassi, B., Majerczak, J., Szkutnik, Z., Korostyński, M., Karasiński, J., Kilarski, W. M., & Korzeniewski, B. (2012) · Experimental Physiology · doi:10.1113/expphysiol.2012.069443 · Cited by 54
Cardiac cytochrome c and cardiolipin depletion during anthracycline-induced chronic depression of mitochondrial function
Pereira, G. C., Pereira, S. P., Tavares, L. C., Carvalho, F. S., Novais, S. M., Barbosa, I. A., Santos, M. S., Bjork, J. A., Moreno, A. J., Wallace, K. B., et al. (2016) · Mitochondrion · doi:10.1016/j.mito.2016.07.005 · Cited by 51
Regulation of oxidative phosphorylation in intact mammalian heart in vivo
Korzeniewski, B., Noma, A., & Matsuoka, S. (2005) · Biophysical Chemistry · doi:10.1016/j.bpc.2005.04.001 · Cited by 51
Mechanisms responsible for the acceleration of pulmonary V o 2on-kinetics in humans after prolonged endurance training
Zoladz, J. A., Grassi, B., Majerczak, J., Szkutnik, Z., Korostyński, M., Grandys, M., Jarmuszkiewicz, W., & Korzeniewski, B. (2014) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00046.2014 · Cited by 51
Metabolic control analysis of cellular respiration in situ in intraoperational samples of human breast cancer
Käämbre, T., Chekulayev, V. A., Shevchuk, I. N., Karu-Varikmaa, M., Timohhina, N., Tepp, K., Bogovskaja, J., Kütner, R., Valvere, V., & Saks, V. A. (2012) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-012-9457-9 · Cited by 48
Characterization of mitochondrial function in cells with impaired cystic fibrosis transmembrane conductance regulator (CFTR) function
Atlante, A., Favia, M., Bobba, A., Guerra, L., Casavola, V., & Reshkin, S. J. (2016) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-016-9663-y · Cited by 48
Increase in the adenine nucleotide translocase content of duckling subsarcolemmal mitochondria during cold acclimation
Roussel, D., Chaînier, F., Rouanet, J., & Barré, H. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)01790-7 · Cited by 48
Mitochondrial energetic metabolism—some general principles
Mazat, J., Ransac, S., Heiske, M., Devin, A., & Rigoulet, M. (2013) · IUBMB Life · doi:10.1002/iub.1138 · Cited by 48
Self-citation
Resveratrol-induced limitation of dysfunction of mitochondria isolated from rat brain in an anoxia-reoxygenation model
Zini, R., Morin, C., Bertelli, A., Bertelli, A. A. E., & Tillement, J. P. (2002) · Life Sciences · doi:10.1016/s0024-3205(02)02161-6 · Cited by 45
Transcriptional Regulation of Metabolism Associated With the Increased Desiccation Resistance of the Cactophilic Drosophila mojavensis
Matzkin, L. M., & Markow, T. A. (2009) · Genetics · doi:10.1534/genetics.109.104927 · Cited by 46
Is defective electron transport at the hub of aging?
Maklashina, E., & Ackrell, B. A. C. (2003) · Aging Cell · doi:10.1111/j.1474-9728.2003.00078.x · Cited by 43
Control of oxidative phosphorylation in skeletal muscle
Kunz, W. S. (2001) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(00)00235-8 · Cited by 42
Age-dependent Bupivacaine-induced Muscle Toxicity during Continuous Peripheral Nerve Block in Rats
Nouette‐Gaulain, K., Dadure, C., Morau, D., Pertuiset, C., Galbès, O., Hayot, M., Mercier, J. G., Sztark, F., Rossignol, R., & Capdevila, X. (2009) · Anesthesiology · doi:10.1097/aln.0b013e3181bbc949 · Cited by 41
Self-citation
Metabolic Engineering: Advances in Modeling and Intervention in Health and Disease
Yarmush, M. L., & Banta, S. A. (2003) · Annual Review of Biomedical Engineering · doi:10.1146/annurev.bioeng.5.031003.163247 · Cited by 40
The impact of mitochondrial tRNA mutations on the amount of ATP synthase differs in the brain compared to other tissues
Fornůsková, D., Brantová, O., Tesařová, M., Stibůrek, L., Honzík, T., Wenchich, L., Tietzeova, E., Hansíková, H., & Zeman, J. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2008.02.001 · Cited by 39
Regulation of succinate-fueled mitochondrial respiration in liver and skeletal muscle of hibernating thirteen-lined ground squirrels
Brown, J. C. L., Chung, D. J., Cooper, A. N., & Staples, J. F. (2013) · Journal of Experimental Biology · doi:10.1242/jeb.078519 · Cited by 39
Variation of flux control coefficient of cytochrome c oxidase and of the other respiratory chain complexes at different values of protonmotive force occurs by a threshold mechanism
Quarato, G., Piccoli, C., Scrima, R., & Capitanio, N. (2011) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2011.04.001 · Cited by 38
Effects of aging on mitochondrial function in skeletal muscle of American American Quarter Horses
Li, C., White-Springer, S. H., Warren, L. K., & Wohlgemuth, S. E. (2016) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01077.2015 · Cited by 39
Increased mitochondrial energy efficiency in skeletal muscle after long-term fasting. Its relevance to animal performance
Bourguignon, A., Rameau, A., Toullec, G., Romestaing, C., & Roussel, D. (2017) · Journal of Experimental Biology · doi:10.1242/jeb.159087 · Cited by 38

Authors: ROSSIGNOL, R., LETELLIER, T., MALGAT, M., ROCHER, C., & MAZAT, J.-P.
Affiliations: Inserm (FR)
ORCID: ROSSIGNOL, Rodrigue
LETELLIER, Thierry
ROCHER, Christophe
MAZAT, Jean-Pierre
Venue: Biochemical Journal
Publisher: Portland Press Ltd.
Published: 2000-03-27
Volume: 347
Issue: 1
Pages: 45-53
ISSN: 0264-6021 (ISSN-L)
1470-8728
DOI: 10.1042/bj3470045
PMC: PMC1220929
OpenAlex: W2093325321
Cited by: 202
References: 51
Citations by year: 2026: 1 · 2025: 3 · 2024: 3 · 2023: 3 · 2022: 1 · 2021: 4 · 2020: 4 · 2019: 1 · 2018: 4 · 2017: 7 · 2016: 7 · 2015: 9 · 2014: 11 · 2013: 7 · 2012: 13
FWCI: 3.37
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Biochemical Journal (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: Institut National de la Santé et de la Recherche Médicale
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 › Clinical Biochemistry › Metabolism and Genetic Disorders
Keywords: oxidative phosphorylation, metabolic control analysis, control coefficients, tissue variation, mitochondrial disease, oxygen consumption, ATP synthase, phosphate transporters, electron transport chain, muscle mitochondria, heart mitochondria, liver mitochondria, kidney mitochondria, brain mitochondria
MeSH terms: Animals, Antimycin A, Brain, Kidney, Kinetics, Male, Mitochondria, Mitochondria, Heart, Mitochondria, Liver, Mitochondria, Muscle, Organ Specificity, Oxidative Phosphorylation, Oxygen Consumption, Polarography, Rotenone, Rats, Wistar, Mitochondrial Myopathies, Rats

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

Tissue variation in the control of oxidative phosphorylation: implication for mitochondrial diseases

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks