Cited by 306Mitochondrial Function and PathologyCoenzyme Q10 studies and effectsATP Synthase and ATPases Research

The DOI matches its Crossref record; 187 of the 187 references it cites were found in a registry or an index.

Functional role of mitochondrial respiratory supercomplexes

Open access

Genova, Maria Luisa, Lenaz, Giorgio·2014·Biochimica et Biophysica Acta (BBA) - Bioenergetics

DOI 10.1016/j.bbabio.2013.11.002

Open this paper in CoChat — free account Open PDF

Abstract

Recent experimental evidence has replaced the random diffusion model of electron transfer with a model of supramolecular organisation based upon specific interactions between individual respiratory complexes. These supercomplexes were found to be functionally relevant by flux control analysis and to confer a kinetic advantage to NAD-linked respiration (channelling). However, the Coenzyme Q pool is still required for FAD-linked oxidations and for the proper equilibrium with Coenzyme Q bound in the supercomplex. Channelling in the cytochrome c region probably also occurs but does not seem to confer a particular kinetic advantage. The supramolecular association of individual complexes strongly depends on membrane lipid amount and composition and is affected by lipid peroxidation; it also seems to be modulated by membrane potential and protein phosphorylation. Additional properties of supercomplexes are stabilisation of Complex I, as evidenced by the destabilising effect on Complex I of mutations in either Complex III or IV, and prevention of excessive generation of reactive oxygen species. The dynamic character of the supercomplexes allows their involvement in metabolic adaptations and in control of cellular signalling pathways. This article is part of a Special Issue entitled: Dynamic and ultrastructure of bioenergetic membranes and their components.

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 · 10.1016/j.bbabio.2013.11.002

Cites

187 of 187 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.

TGF-β SIGNAL TRANSDUCTION
Massagué, J. (1998) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.67.1.753 · Cited by 7,571
Reactive oxygen species (ROS) homeostasis and redox regulation in cellular signaling
Ray, P. D., Huang, B.-W., & Tsuji, Y. (2012) · Cellular Signalling · doi:10.1016/j.cellsig.2012.01.008 · Cited by 4,373
ROS as signalling molecules: Mechanisms that generate specificity in ROS homeostasis
D'Autréaux, B., & Toledano, M. B. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2256 · Cited by 3,642
Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain
Itoh, K., Wakabayashi, N., Katoh, Y., Ishii, T., Igarashi, K., Engel, J. D., & Yamamoto, M. (1999) · Genes & Development · doi:10.1101/gad.13.1.76 · Cited by 3,634
Mitochondria and cancer
Wallace, D. C. (2012) · Nature Reviews Cancer · doi:10.1038/nrc3365 · Cited by 2,404
Supercomplexes in the respiratory chains of yeast and mammalian mitochondria
Schägger, H., & Pfeiffer, K. (2000) · The EMBO Journal · doi:10.1093/emboj/19.8.1777 · Cited by 1,356
Oxidative Stress, Mitochondrial Dysfunction, and Aging
Cui, H., Kong, Y., & Zhang, H. (2011) · Journal of Signal Transduction · doi:10.1155/2012/646354 · Cited by 1,076
Complexes of sequential metabolic enzymes
Srere, P. A. (1987) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.56.070187.000513 · Cited by 1,058
Cardiolipin Stabilizes Respiratory Chain Supercomplexes
Pfeiffer, K., Gohil, V., Stuart, R. A., Hunte, C., Brandt, U., Greenberg, M. L., & Schägger, H. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m308366200 · Cited by 843
Somatic mutations of the mitochondrial genome in human colorectal tumours
Polyák, K., Li, Y., Zhu, H., Christoph Lengauer, C., Willson, J. K. V., Markowitz, S. D., Trush, M. A., Kinzler, K. W., & Vogelstein, B. (1998) · Nature Genetics · doi:10.1038/3108 · Cited by 834
Supercomplex assembly determines electron flux in the mitochondrial electron transport chain
Lapuente-Brun, E., Moreno-Loshuertos, R., Acín-Pérez, R., Latorre-Pellicer, A., Colás, C., Balsa, E., Perales-Clemente, E., Quirós, P. M., Calvo, E., Rodríguez-Hernández, M. A., et al. (2013) · Science · doi:10.1126/science.1230381 · Cited by 830
Respiratory active mitochondrial supercomplexes
Acín-Pérez, R., Fernández-Silva, P., Peleato, M. L., Pérez-Martos, A., & Enriquez, J. A. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.10.021 · Cited by 817
Crystal structure of the entire respiratory complex I
Baradaran, R., Berrisford, J. M., Minhas, G. S., & Sazanov, L. A. (2013) · Nature · doi:10.1038/nature11871 · Cited by 797
Gluing the Respiratory Chain Together
Zhang, M., Mileykovskaya, E., & Dowhan, W. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c200551200 · Cited by 642
Making heads or tails of phospholipids in mitochondria
Osman, C., Voelker, D. R., & Langer, T. (2011) · The Journal of Cell Biology · doi:10.1083/jcb.201006159 · Cited by 599
Nitric oxide, cell bioenergetics and neurodegeneration
Moncada, S., & Bolaños, J. P. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.03988.x · Cited by 555
Respiratory Complex III Is Required to Maintain Complex I in Mammalian Mitochondria
Acín‐Pérez, R., Bayona‐Bafaluy, M. P., Fernández‐Silva, P., Moreno‐Loshuertos, R., Martos, A. P., Bruno, C., Moraes, C. T., & Enrı́quez, J. A. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00124-8 · Cited by 474
Decrease in Mitochondrial Complex I Activity in Ischemic/Reperfused Rat Heart: Involvement of Reactive Oxygen Species and Cardiolipin
Paradies, G., Petrosillo, G., Pistolese, M., Di Venosa, N., Federici, A., & Ruggiero, F. M. (2004) · Circulation Research · doi:10.1161/01.res.0000109416.56608.64 · Cited by 468
Cyclic AMP Produced inside Mitochondria Regulates Oxidative Phosphorylation
Acín‐Pérez, R., Salazar, E., Kamenetsky, M., Buck, J., Levin, L. R., & Manfredi, G. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2009.01.012 · Cited by 465
Nonbilayer lipids affect peripheral and integral membrane proteins via changes in the lateral pressure profile
der Laan, E. V. D. B.-V., Killian, J. A., & KRUIJFF, B. D. (2004) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2004.06.010 · Cited by 461
Mitochondrial Respiratory Supercomplex Association Limits Production of Reactive Oxygen Species from Complex I
Maranzana, E., Barbero, G., Falasca, A. I., Lenaz, G., & Genova, M. L. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4845 · Cited by 445
Self-citation
Specific roles of protein–phospholipid interactions in the yeast cytochrome bc1 complex structure
Lange, C. M., Nett, J. H., Trumpower, B. L., & Hunte, C. (2001) · The EMBO Journal · doi:10.1093/emboj/20.23.6591 · Cited by 444
Direct Evidence for Increased Hydroxyl Radicals Originating From Superoxide in the Failing Myocardium
Ide, T., Tsutsui, H., Kinugawa, S., Suematsu, N., Hayashidani, S., Ichikawa, K., Utsumi, H., Machida, Y., Egashira, K., & Takeshita, A. (2000) · Circulation Research · doi:10.1161/01.res.86.2.152 · Cited by 427
Mitochondrial Respiratory Chain Supercomplexes Are Destabilized in Barth Syndrome Patients
McKenzie, M., Lazarou, M., Thorburn, D. R., & Ryan, M. T. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.06.057 · Cited by 424
The Ratio of Oxidative Phosphorylation Complexes I–V in Bovine Heart Mitochondria and the Composition of Respiratory Chain Supercomplexes
Schägger, H., & Pfeiffer, K. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106474200 · Cited by 407
Cardiolipin requirement for electron transfer in complex I and III of the mitochondrial respiratory chain.
Fry, M., & Green, D. E. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)69888-1 · Cited by 405
Phosphatidylethanolamine Deficiency in Mammalian Mitochondria Impairs Oxidative Phosphorylation and Alters Mitochondrial Morphology
Tasseva, G., Bai, H. D., Davidescu, M., Haromy, A., Michelakis, E. D., & Vance, J. E. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.434183 · Cited by 385
The random collision model and a critical assessment of diffusion and collision in mitochondrial electron transport
Hackenbrock, C. R., Chazotte, B., & Gupte, S. S. (1986) · Journal of Bioenergetics and Biomembranes · doi:10.1007/bf00743010 · Cited by 384
Reactive oxygen species affect mitochondrial electron transport complex I activity through oxidative cardiolipin damage
Paradies, G., Petrosillo, G., Pistolese, M., & Ruggiero, F. M. (2002) · Gene · doi:10.1016/s0378-1119(01)00814-9 · Cited by 384
Cardiac mitochondria in heart failure: decrease in respirasomes and oxidative phosphorylation
Rosca, M. G., Vazquez, E. J., Kerner, J., Parland, W., Chandler, M. P., Stanley, W. C., Sabbah, H. N., & Hoppel, C. L. (2008) · Cardiovascular Research · doi:10.1093/cvr/cvn184 · Cited by 373
Studies on the Electron Transfer System
Hatefi, Y., Haavik, A. G., & Griffiths, D. (1962) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)83761-4 · Cited by 370
Structure of the membrane domain of respiratory complex I
Efremov, R. G., & Sazanov, L. A. (2011) · Nature · doi:10.1038/nature10330 · Cited by 370
Electron and proton transfers through quinones and cytochrome bc complexes
Rich, P. R. (1984) · Biochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics · doi:10.1016/0304-4173(84)90007-7 · Cited by 348
The Kinetics of the Redox Reactions of Ubiquinone Related to the Electron‐Transport Activity in the Respiratory Chain
Kröger, A., & Klingenberg, M. (1973) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1973.tb02767.x · Cited by 344
Arrangement of electron transport chain components in bovine mitochondrial supercomplex I1III2IV1
Althoff, T., Mills, D. J., Popot, J., & Kühlbrandt, W. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.324 · Cited by 334
Significance of Respirasomes for the Assembly/Stability of Human Respiratory Chain Complex I
Schägger, H., de Coo, I. F. M., Bauer, M. F., Hofmann, S., Godinot, C., & Brandt, U. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404033200 · Cited by 324
Cardiolipin defines the interactome of the major ADP/ATP carrier protein of the mitochondrial inner membrane
Claypool, S. M., Oktay, Y., Boontheung, P., Loo, J. A., & Koehler, C. M. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200801152 · Cited by 318
The production of reactive oxygen species by complex I
Hirst, J., King, M. S., & Pryde, K. R. (2008) · Biochemical Society Transactions · doi:10.1042/bst0360976 · Cited by 312
[44] Preparation and properties of reduced coenzyme Q-cytochrome c reductase (complex III of the respiratory chain)
Rieske, J. S. (1967) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(67)10047-5 · Cited by 285
Structure and Organization of Mitochondrial Respiratory Complexes: A New Understanding of an Old Subject
Lenaz, G., & Genova, M. L. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2704 · Cited by 284
Self-citation
Implications of mitochondrial DNA mutations and mitochondrial dysfunction in tumorigenesis
Lü, J., Sharma, L. K., & Bai, Y. (2009) · Cell Research · doi:10.1038/cr.2009.69 · Cited by 284
Isolation of ubiquinol oxidase from Paracoccus denitrificans and resolution into cytochrome bc1 and cytochrome c-aa3 complexes.
Berry, E. A., & Trumpower, B. L. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)89576-x · Cited by 281
The Mitochondrial Respiratory Chain Is Partially Organized in a Supercomplex Assembly
Bianchi, C., Genova, M. L., Castelli, G. P., & Lenaz, G. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m405135200 · Cited by 277
Self-citation
Physiological significance of metabolic channelling
Ovádi, J. (1991) · Journal of Theoretical Biology · doi:10.1016/s0022-5193(05)80500-4 · Cited by 269
Mitochondrial Complex I Plays an Essential Role in Human Respirasome Assembly
Moreno-Lastres, D., Fontanesi, F., García‐Consuegra, I., Martín, M. A., Arenas, J., Barrientos, A., & Ugalde, C. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.01.015 · Cited by 261
Decreased complex III activity in mitochondria isolated from rat heart subjected to ischemia and reperfusion: role of reactive oxygen species and cardiolipin
Petrosillo, G., Francesca, M. R., Di Venosa, N., & Paradies, A. G. (2003) · The FASEB Journal · doi:10.1096/fj.02-0729fje · Cited by 261
The effect of reactive oxygen species generated from the mitochondrial electron transport chain on the cytochrome c oxidase activity and on the cardiolipin content in bovine heart submitochondrial particles
Paradies, G., Petrosillo, G., Pistolese, M., & Ruggiero, F. M. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)01082-6 · Cited by 251
Differential effects of mitochondrial Complex I inhibitors on production of reactive oxygen species
Fato, R., Bergamini, C., Bortolus, M., Maniero, A. L., Leoni, S., Ohnishi, T., & Lenaz, G. (2008) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2008.11.003 · Cited by 238
Self-citation
Mitochondria in heart failure
Rosca, M. G., & Hoppel, C. L. (2010) · Cardiovascular Research · doi:10.1093/cvr/cvq240 · Cited by 237
Further Evidence for the Pool Function of Ubiquinone as Derived from the Inhibition of the Electron Transport by Antimycin
Kröger, A., Klingenberg, M., & Schweidler, S. (1973) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1973.tb03129.x · Cited by 236
Cytochrome c Oxidase Is Required for the Assembly/Stability of Respiratory Complex I in Mouse Fibroblasts
Díaz, F., Fukui, H., García, S., & Moraes, C. T. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.01767-05 · Cited by 236
Studies on the Electron Transfer System
Hatefi, Y., Haavik, A. G., & Griffiths, D. (1962) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)83762-6 · Cited by 234
Assembly of Respiratory Complexes I, III, and IV into NADH Oxidase Supercomplex Stabilizes Complex I in Paracoccus denitrificans
Stroh, A., Anderka, O., Pfeiffer, K., Yagi, T., Finel, M., Ludwig, B., & Schägger, H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m309505200 · Cited by 231
Supramolecular Structure of the Mitochondrial Oxidative Phosphorylation System
Boekema, E. J., & Braun, H. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.r600031200 · Cited by 224
Mitochondria and Reactive Oxygen Species. Which Role in Physiology and Pathology?
Lenaz, G. (2011) · Advances in experimental medicine and biology · doi:10.1007/978-94-007-2869-1_5 · Cited by 219
Self-citation
Supercomplexes and subcomplexes of mitochondrial oxidative phosphorylation
Wittig, I., Carrozzo, R., Santorelli, F. M., & Schägger, H. (2006) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2006.05.006 · Cited by 218
Differences in assembly or stability of complex I and other mitochondrial OXPHOS complexes in inherited complex I deficiency
Ugalde, C. (2004) · Human Molecular Genetics · doi:10.1093/hmg/ddh071 · Cited by 216
Phosphatidylethanolamine and Cardiolipin Differentially Affect the Stability of Mitochondrial Respiratory Chain Supercomplexes
Böttinger, L., Horvath, S. E., Kleinschroth, T., Hunte, C., Daum, G., Pfanner, N., & Becker, T. (2012) · Journal of Molecular Biology · doi:10.1016/j.jmb.2012.09.001 · Cited by 213
Evidence for two sites of superoxide production by mitochondrial NADH-ubiquinone oxidoreductase (complex I)
Treberg, J. R., Quinlan, C. L., & Brand, M. D. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.252502 · Cited by 212
Oxidatively damaged proteins of heart mitochondrial electron transport complexes
Choksi, K. B., Boylston, W. H., Rabek, J. P., Widger, W. R., & Papaconstantinou, J. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2003.11.007 · Cited by 212
Assay conditions for the mitochondrial NADH:coenzyme Q oxidoreductase
Estornell, E., Fato, R., Pallotti, F., & Lenaz, G. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)80498-j · Cited by 209
Self-citation
Taz1, an Outer Mitochondrial Membrane Protein, Affects Stability and Assembly of Inner Membrane Protein Complexes: Implications for Barth Syndrome
Brandner, K., Mick, D. U., Frazier, A. E., Taylor, R. D., Meisinger, C., & Rehling, P. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-03-0256 · Cited by 209
Identification of a Protein Mediating Respiratory Supercomplex Stability
Chen, Y.-C., Taylor, E. B., Dephoure, N., Heo, J.-M., Tonhato, A., Papandreou, I., Nath, N., Denko, N. C., Gygi, S. P., & Rutter, J. P. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.02.006 · Cited by 205
Arrangement of proteins in the mitochondrial inner membrane
Capaldi, R. (1982) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/0304-4157(82)90009-0 · Cited by 201
Rcf1 Mediates Cytochrome Oxidase Assembly and Respirasome Formation, Revealing Heterogeneity of the Enzyme Complex
Vukotic, M., Oeljeklaus, S., Wiese, S., Vögtle, F. ‐., Meisinger, C., Meyer, H. E., Zieseniß, A., Katschinski, D. M., Jans, D. C., Jakobs, S., et al. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.01.016 · Cited by 199
Membrane Deformation under Local pH Gradient: Mimicking Mitochondrial Cristae Dynamics
Khalifat, N., Puff, N., Bonneau, S., Fournier, J., & Angelova, M. I. (2008) · Biophysical Journal · doi:10.1529/biophysj.108.136077 · Cited by 194
Protein Phosphorylation and Prevention of Cytochrome Oxidase Inhibition by ATP: Coupled Mechanisms of Energy Metabolism Regulation
Acin-Perez, R., Gatti, D. L., Bai, Y., & Manfredi, G. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.03.024 · Cited by 190
Interaction of complexes I, III, and IV within the bovine respirasome by single particle cryoelectron tomography
Dudkina, N. V., Kudryashev, M., Stahlberg, H., & Boekema, E. J. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1107819108 · Cited by 190
Features and applications of blue‐native and clear‐native electrophoresis
Wittig, I., & Schägger, H. (2008) · PROTEOMICS · doi:10.1002/pmic.200800017 · Cited by 189
The Respiratory Chain in Yeast Behaves as a Single Functional Unit
Boumans, H., Grivell, L. A., & BERDEN, J. A. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.9.4872 · Cited by 187
Relationship between lateral diffusion, collision frequency, and electron transfer of mitochondrial inner membrane oxidation-reduction components.
Gupte, S., Wu, E. S., Höchli, L., Hoechli, M., Jacobson, K., Sowers, A. E., & Hackenbrock, C. R. (1984) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.81.9.2606 · Cited by 186
Rcf1 and Rcf2, Members of the Hypoxia-Induced Gene 1 Protein Family, Are Critical Components of the Mitochondrial Cytochrome bc1-Cytochrome c Oxidase Supercomplex
Strogolova, V., Furness, A. I., Robb-McGrath, M., Garlich, J., & Stuart, R. A. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.06369-11 · Cited by 185
Oxidative stress, mitochondrial bioenergetics, and cardiolipin in aging
Paradies, G., Petrosillo, G., Paradies, V., & Ruggiero, F. M. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.02.020 · Cited by 181
The retrograde response: When mitochondrial quality control is not enough
Jazwinski, S. M. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.02.010 · Cited by 172
Barth syndrome: Cellular compensation of mitochondrial dysfunction and apoptosis inhibition due to changes in cardiolipin remodeling linked to tafazzin (TAZ) gene mutation
Gonzalvez, F., D’Aurelio, M., Boutant, M., Moustapha, A., Puech, J.-P., Landes, T., Pelloquin, L., Vial, G., Taleux, N., Slomianny, C., et al. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.03.005 · Cited by 170
Phosphoproteome Analysis of Functional Mitochondria Isolated from Resting Human Muscle Reveals Extensive Phosphorylation of Inner Membrane Protein Complexes and Enzymes
Zhao, X., León, I. R., Bak, S. Y., Mogensen, M., Wrzesinski, K., Højlund, K., & Jensen, O. N. (2010) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m110.000299 · Cited by 169
Barth syndrome may be due to an acyltransferase deficiency
Neuwald, A. F. (1997) · Current Biology · doi:10.1016/s0960-9822(06)00237-5 · Cited by 169
Supramolecular organization of protein complexes in the mitochondrial inner membrane
Vonck, J., & Schäfer, E. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2008.05.019 · Cited by 168
Molecular architecture of the inner membrane of mitochondria from rat liver: a combined biochemical and stereological study.
Schwerzmann, K., Cruz-Orive, L. M., Eggman, R., Sänger, A., & Weibel, E. R. (1986) · The Journal of Cell Biology · doi:10.1083/jcb.102.1.97 · Cited by 163
Mitochondrial respiratory complex I dysfunction promotes tumorigenesis through ROS alteration and AKT activation
Sharma, L. K., Fang, H., Liu, J., Vartak, R. S., Deng, J., & Bai, Y. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr395 · Cited by 160
Complex I binds several mitochondrial NAD-coupled dehydrogenases.
Sümegi, B., & Srere, P. A. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)42511-7 · Cited by 159
A Quantitative Map of the Liver Mitochondrial Phosphoproteome Reveals Posttranslational Control of Ketogenesis
Grimsrud, P. A., Carson, J. J., Hebert, A. S., Hubler, S. L., Niemi, N. M., Bailey, D. J., Jochem, A., Stapleton, D. S., Keller, M. P., Westphall, M. S., et al. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.10.004 · Cited by 158
Soluble Cytochrome b-c1 Complex and the Reconstitution of Succinate-Cytochrome c Reductase
Yu, C., Yu, L. P. C., & King, T. E. (1974) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)42407-1 · Cited by 155
Kinetics of integrated electron transfer in the mitochondrial respiratory chain: random collisions vs. solid state electron channeling
Lenaz, G., & Genova, M. L. (2007) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00263.2006 · Cited by 155
Self-citation
Phospholipase A2 Digestion of Cardiolipin Bound to Bovine Cytochrome c Oxidase Alters Both Activity and Quaternary Structure†
Sedlák, E., & Robinson, N. C. (1999) · Biochemistry · doi:10.1021/bi9914053 · Cited by 154
Role of phospholipids in respiratory cytochrome bc1 complex catalysis and supercomplex formation
Wenz, T., Hielscher, R., Hellwig, P., Schägger, H., Richers, S., & Hunte, C. (2009) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2009.02.012 · Cited by 154
Steady-State Kinetics of the Reduction of Coenzyme Q Analogs by Complex I (NADH:Ubiquinone Oxidoreductase) in Bovine Heart Mitochondria and Submitochondrial Particles
Fato, R., Estornell, E., Bernardo, S. D., Pallotti, F., Castelli, G. P., & Lenaz, G. (1996) · Biochemistry · doi:10.1021/bi9516034 · Cited by 153
Self-citation
Three-Dimensional Structure of the Respiratory Chain Supercomplex I1III2IV1 from Bovine Heart Mitochondria,
Schäfer, E., Dencher, N. A., Vonck, J., & Parcej, D. N. (2007) · Biochemistry · doi:10.1021/bi700983h · Cited by 153
Studies on the electron transport system XXX. DPNH-cytochrome c reductase I
Hatefi, Y., Haavik, A. G., & Jurtshuk, P. (1961) · Biochimica et Biophysica Acta · doi:10.1016/0006-3002(61)90908-8 · Cited by 151
Nuclear magnetic resonance investigation of the cytochrome oxidase-phospholipid interaction: a new model for boundary lipid
Kang, S. Y., Gutowsky, H. S., Hshung, J. C., Jacobs, R. E., King, T. E., Rice, D. M., & Oldfield, E. (1979) · Biochemistry · doi:10.1021/bi00582a010 · Cited by 151
Dysfunctions of Cellular Oxidative Metabolism in Patients with Mutations in the NDUFS1 and NDUFS4 Genes of Complex I
Iuso, A., Scacco, S., Piccoli, C., Bellomo, F., Petruzzella, V., Trentadue, R., Minuto, M. N., Ripoli, M. C., Capitanio, N., Zeviani, M., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m513387200 · Cited by 149
Mitochondrial Complex I decrease is responsible for bioenergetic dysfunction in K-ras transformed cells
Baracca, A., Chiaradonna, F., Sgarbi, G., Solaini, G., Alberghina, L., & Lenaz, G. (2009) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2009.11.006 · Cited by 143
Self-citation
Species- and tissue-specific relationships between mitochondrial permeability transition and generation of ROS in brain and liver mitochondria of rats and mice
Panov, A., Dikalov, S., Shalbuyeva, N., Hemendinger, R., Greenamyre, J. T., & Rosenfeld, J. (2007) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00202.2006 · Cited by 141
Cells Lacking Rieske Iron-Sulfur Protein Have a Reactive Oxygen Species-Associated Decrease in Respiratory Complexes I and IV
Díaz, F., Enríquez, J. A., & Moraes, C. T. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.06051-11 · Cited by 139
Restricted diffusion of OXPHOS complexes in dynamic mitochondria delays their exchange between cristae and engenders a transitory mosaic distribution
Wilkens, V., Kohl, W., & Busch, K. B. (2012) · Journal of Cell Science · doi:10.1242/jcs.108852 · Cited by 139
Respiratory chain supercomplexes in plant mitochondria
Eubel, H., Heinemeyer, J., Sunderhaus, S., & Braun, H. (2004) · Plant Physiology and Biochemistry · doi:10.1016/j.plaphy.2004.09.010 · Cited by 138
Megacomplex organization of the oxidative phosphorylation system by structural analysis of respiratory supercomplexes from potato
Bultema, J. B., Braun, H., Boekema, E. J., & Kouřil, R. (2008) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2008.10.010 · Cited by 137
A Phosphodiesterase 2A Isoform Localized to Mitochondria Regulates Respiration
Acín‐Pérez, R., Russwurm, M., Günnewig, K., Gertz, M., Zoidl, G., Ramos, L. S., Buck, J., Levin, L. R., Rassow, J., Manfredi, G., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.266379 · Cited by 136
The mitochondrial electron transfer chain
Green, D. E., & Tzagoloff, A. (1966) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(66)90036-1 · Cited by 136
The kinetic basis of threshold effects observed in mitochondrial diseases: a systemic approach
Letellier, T., Heinrich, R., Malgat, M., & Mazat, J. (1994) · Biochemical Journal · doi:10.1042/bj3020171 · Cited by 134
Mitochondrial complex I mutations in Caenorhabditis elegans produce cytochrome c oxidase deficiency, oxidative stress and vitamin-responsive lactic acidosis
Grad, L. I. (2003) · Human Molecular Genetics · doi:10.1093/hmg/ddh027 · Cited by 133
Mitochondrial complex III stabilizes complex I in the absence of NDUFS4 to provide partial activity
Calvaruso, M. A., Willems, P. H. G. M., van den Brand, M., Valsecchi, F., Kruse, S. E., Palmiter, R. D., Smeitink, J. A. M., & Nijtmans, L. G. J. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr446 · Cited by 130
Is supercomplex organization of the respiratory chain required for optimal electron transfer activity?
Genova, M. L., Baracca, A., Biondi, A., Casalena, G., Faccioli, M., Falasca, A. I., Formiggini, G., Sgarbi, G., Solaini, G., & Lenaz, G. (2008) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2008.04.007 · Cited by 128
Self-citation
Arrangement of the Respiratory Chain Complexes in Saccharomyces cerevisiae Supercomplex III2IV2 Revealed by Single Particle Cryo-Electron Microscopy
Mileykovskaya, E., Penczek, P. A., Fang, J., Mallampalli, V. K. P. S., Sparagna, G. C., & Dowhan, W. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.367888 · Cited by 128
Ageing alters the supramolecular architecture of OxPhos complexes in rat brain cortex
Frenzel, M., Rommelspacher, H., Sugawa, M. D., & Dencher, N. A. (2010) · Experimental Gerontology · doi:10.1016/j.exger.2010.02.003 · Cited by 127
Supercomplexes of the mitochondrial electron transport chain decline in the aging rat heart
Gómez, L. A., Monette, J. S., Chavez, J. D., Maier, C. S., & Hagen, T. M. (2009) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2009.08.002 · Cited by 127
Respiratory chain supercomplexes set the threshold for respiration defects in human mtDNA mutant cybrids
D’Aurelio, M., Gajewski, C. D., Lenaz, G., & Manfredi, G. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl141 · Cited by 126
Self-citation
The Molecular Biology of Membranes
Fleischer, S., Hatefi, Y., MacLennan, D. H., & Tzagoloff, A. (1978) · Springer eBooks · doi:10.1007/978-1-4684-2463-8 · Cited by 124
Identification and properties of a quinol oxidase super-complex composed of a bc1 complex and cytochrome oxidase in the thermophilic bacterium PS3.
Sone, N., SEKIMACHI, M., & Kutoh, E. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47736-8 · Cited by 122
Mitochondrial respiratory chain super-complex I–III in physiology and pathology
Lenaz, G., Baracca, A., Barbero, G., Bergamini, C., Dalmonte, M. E., Sole, M. D., Faccioli, M., Falasca, A. I., Fato, R., Genova, M. L., et al. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.01.025 · Cited by 120
Self-citation
Mobility and function of Coenzyme Q (ubiquinone) in the mitochondrial respiratory chain
Lenaz, G., & Genova, M. L. (2009) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2009.02.019 · Cited by 119
Self-citation
MCJ/DnaJC15, an Endogenous Mitochondrial Repressor of the Respiratory Chain That Controls Metabolic Alterations
Hatle, K. M., Gummadidala, P. M., Navasa, N., Bernardo, E., Dodge, J. T., Silverstrim, B., Fortner, K. A., Burg, E., Suratt, B. T., Hammer, J., et al. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.00189-13 · Cited by 117
Control of oxygen free radical formation from mitochondrial complex I: roles for protein kinase A and pyruvate dehydrogenase kinase
Raha, S., Myint, A. T., Johnstone, L., & Robinson, B. H. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(01)00816-4 · Cited by 115
Supramolecular Organisation of the Mitochondrial Respiratory Chain: A New Challenge for the Mechanism and Control of Oxidative Phosphorylation
Lenaz, G., & Genova, M. L. (2012) · Advances in experimental medicine and biology · doi:10.1007/978-1-4614-3573-0_5 · Cited by 114
Self-citation
The three-dimensional structure of complex I from Yarrowia lipolytica: A highly dynamic enzyme
Radermacher, M., Ruíz, T., Clason, T. A., Benjamin, S., Brandt, U., & Zickermann, V. (2006) · Journal of Structural Biology · doi:10.1016/j.jsb.2006.02.011 · Cited by 113
Questioning the functional relevance of mitochondrial supercomplexes by time-resolved analysis of the respiratory chain
Trouillard, M., Meunier, B., & Rappaport, F. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1109510108 · Cited by 112
Modulation of mitochondrial protein phosphorylation by soluble adenylyl cyclase ameliorates cytochrome oxidase defects
Acín‐Pérez, R., Salazar, E., Brosel, S., Yang, H., Schon, E. A., & Manfredi, G. (2009) · EMBO Molecular Medicine · doi:10.1002/emmm.200900046 · Cited by 111
Lateral diffusion of ubiquinone during electron transfer in phospholipid- and ubiquinone-enriched mitochondrial membranes.
Schneider, H., Lemasters, J. J., & Hackenbrock, C. R. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)33893-6 · Cited by 110
A novel nonsense mutation (Q352X) in the mitochondrial cytochrome b gene associated with a combined deficiency of complexes I and III
Lamantea, E., Carrara, F., Mariotti, C., Morandi, L. O., Tiranti, V., & Zeviani, M. (2002) · Neuromuscular Disorders · doi:10.1016/s0960-8966(01)00244-9 · Cited by 105
Saturation kinetics of coenzyme Q in NADH and succinate oxidation in beef heart mitochondria
Estornell, E., Fato, R., Castelluccio, C., Cavazzoni, M., Castelli, G. P., & Lenaz, G. (1992) · FEBS Letters · doi:10.1016/0014-5793(92)81378-y · Cited by 103
Self-citation
Natural Distribution and Occurrence of Coenzyme Q Homologues
Battino, M. A., Ferri, E. N., Gorini, A., Villa, R. F., Huertas, J. R., Fiorella, P. L., Genova, M. L., Lenaz, G., & Marchetti, M. (1990) · Membrane Biochemistry · doi:10.3109/09687689009025839 · Cited by 103
Self-citation
Relevance of Mitochondrial Genetics and Metabolism in Cancer DevelopmentPreprint
Gasparre, G., Porcelli, A. M., Lenaz, G., & Romeo, G. C. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a011411 · Cited by 102
Self-citation
cAMP-dependent protein kinase regulates the mitochondrial import of the nuclear encoded NDUFS4 subunit of complex I
Rasmo, D. D., Panelli, D., Sardanelli, A. M., & Papa, S. (2008) · Cellular Signalling · doi:10.1016/j.cellsig.2008.01.017 · Cited by 101
Phosphoproteome Analysis Reveals Regulatory Sites in Major Pathways of Cardiac Mitochondria
Deng, N., Zhang, J., Zong, C., Wang, Y., Lu, H., Yang, P., Wang, W., Young, G. W., Wang, Y., Kôrge, P., et al. (2010) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m110.000117 · Cited by 101
Lipid packing variations induced by pH in cardiolipin-containing bilayers: The driving force for the cristae-like shape instability
Khalifat, N., Fournier, J., Angelova, M. I., & Puff, N. (2011) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2011.07.013 · Cited by 101
The interaction between mitochondrial NADH-ubiquinone oxidoreductase and ubiquinol-cytochrome c oxidoreductase. Evidence for stoicheiometric association
RAGAN, C. I., & Heron, C. (1978) · Biochemical Journal · doi:10.1042/bj1740783 · Cited by 100
The Composition of Plant Mitochondrial Supercomplexes Changes with Oxygen Availability
Ramírez-Aguilar, S. J., Keuthe, M., Rocha, M., Fedyaev, V. V., Kramp, K., Gupta, K. J., Rasmusson, A. G., Schulze, W. X., & van Dongen, J. T. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.252544 · Cited by 100
Metabolic channelling and control of the flux
Kholodenko, B. Ν., & Westerhoff, H. V. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)81660-r · Cited by 98
Targeting the NAD7 Subunit to Mitochondria Restores a Functional Complex I and a Wild Type Phenotype in the Nicotiana sylvestris CMS II Mutant Lacking nad7
Pineau, B., Mathieu, C., Gérard‐Hirne, C., Paepe, R. D., & Chétrit, P. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500508200 · Cited by 98
CREB activation induced by mitochondrial dysfunction triggers triglyceride accumulation in 3T3-L1 preadipocytes
Vankoningsloo, S., Pauw, A. D., Houbion, A., Tejerina, S., Demazy, C., de Longueville, F., Bertholet, V., Renard, P., Remacle, J., Holvoet, P., et al. (2006) · Journal of Cell Science · doi:10.1242/jcs.02848 · Cited by 96
Age-related decline in mitochondrial bioenergetics: Does supercomplex destabilization determine lower oxidative capacity and higher superoxide production?
Gómez, L. A., & Hagen, T. M. (2012) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2012.04.002 · 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
Loss of tafazzin in yeast leads to increased oxidative stress during respiratory growth
Chen, S., He, Q., & Greenberg, M. L. (2008) · Molecular Microbiology · doi:10.1111/j.1365-2958.2008.06216.x · Cited by 92
Major changes in complex I activity in mitochondria from aged rats may not be detected by direct assay of NADH:coenzyme Q reductase
Genova, M. L., Castelluccio, C., Fato, R., Castelli, G. P., Pich, M. M., Formiggini, G., Bovina, C., Marchetti, M., & Lenaz, G. (1995) · Biochemical Journal · doi:10.1042/bj3110105 · Cited by 91
Self-citation
Mammalian complex I: A regulable and vulnerable pacemaker in mitochondrial respiratory function
Papa, S., Rasmo, D. D., Scacco, S., Signorile, A., Technikova-Dobrova, Z., Palmisano, G., Sardanelli, A. M., Papa, F., Panelli, D., Scaringi, R., et al. (2008) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2008.04.005 · Cited by 90
Resolution of the Aerobic Respiratory System of the Thermoacidophilic Archaeon, Sulfolobus sp. Strain 7:
Iwasaki, T., Matsuura, K., & Oshima, T. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.52.30881 · Cited by 89
The role of cytochrome c diffusion in mitochondrial electron transport.
Gupte, S. S., & Hackenbrock, C. R. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)60707-0 · Cited by 88
Cardiac mitochondria in heart failure: Normal cardiolipin profile and increased threonine phosphorylation of complex IV
Rosca, M. G., Minkler, P. E., & Hoppel, C. L. (2011) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2011.02.003 · Cited by 88
The kinetics of quinone pools in electron transport
RAGAN, C. I., & COTTINGHAM, I. R. (1985) · Biochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics · doi:10.1016/0304-4173(85)90003-5 · Cited by 87
Mitochondrial Signaling: Forwards, Backwards, and In Between
Whelan, S. P., & Zuckerbraun, B. S. (2013) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2013/351613 · Cited by 87
The interaction between mitochondrial NADH-ubiquinone oxidoreductase and ubiquinol-cytochrome c oxidoreductase. Restoration of ubiquinone-pool behaviour
Heron, C., RAGAN, C. I., & Trumpower, B. L. (1978) · Biochemical Journal · doi:10.1042/bj1740791 · Cited by 86
Complex I Function Is Defective in Complex IV-deficient Caenorhabditis elegans
Suthammarak, W., Yang, Y.-Y., Morgan, P. G., & Sedensky, M. M. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m805733200 · Cited by 86
Role of mobility of redox components in the inner mitochondrial membrane
Lenaz, G. (1988) · The Journal of Membrane Biology · doi:10.1007/bf01872322 · Cited by 84
Self-citation
The structure of the mitochondrial inner membrane-matrix compartment
Srere, P. A. (1982) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(82)90119-0 · Cited by 83
Redox sensitive signaling pathways in cardiac remodeling, hypertrophy and failure
Anilkumar, N. P. (2009) · Frontiers in bioscience · doi:10.2741/3443 · Cited by 81
Localization and mobility of coenzyme Q in lipid bilayers and membranes
Lenaz, G., Fato, R., Bernardo, S. D., Jarreta, D., Costa, A., Genova, M. L., & Castelli, G. P. (1999) · BioFactors · doi:10.1002/biof.5520090202 · Cited by 81
Self-citation
Molecular mechanisms of superoxide production by complex III: A bacterial versus human mitochondrial comparative case study
Lanciano, P., Khalfaoui-Hassani, B., Selamoglu, N., Ghelli, A. M., Rugolo, M., & Daldal, F. (2013) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2013.03.009 · Cited by 81
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
Self-citation
Multidimensional diffusion modes and collision frequencies of cytochrome c with its redox partners.
Gupte, S. S., & Hackenbrock, C. R. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)60706-9 · Cited by 78
Substrate Channeling of NADH and Binding of Dehydrogenases to Complex I
Fukushima, T., Decker, R. V., Anderson, W. M., & Spivey, H. O. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)84731-2 · Cited by 78
Respiratory Chain Complexes in Dynamic Mitochondria Display a Patchy Distribution in Life Cells
Muster, B., Kohl, W., Wittig, I., Strecker, V., Joos, F., Haase, W., Bereiter‐Hahn, J., & Busch, K. B. (2010) · PLoS ONE · doi:10.1371/journal.pone.0011910 · Cited by 74
[26] Subchloroplast fragments: Digitonin method
Boardman, N. K. (1971) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(71)23102-5 · Cited by 73
Rotation of cytochrome oxidase in phospholipid vesicles. Investigations of interactions between cytochrome oxidases and between cytochrome oxidase and cytochrome bc1 complex.
Kawato, S., Sigel, E., Carafoli, E., & Cherry, R. J. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)68993-3 · Cited by 73
New developments on the functions of coenzyme Q in mitochondria
Genova, M. L., & Lenaz, G. (2011) · BioFactors · doi:10.1002/biof.168 · Cited by 69
Self-citation
Lack of Cytochrome c in Mouse Fibroblasts Disrupts Assembly/Stability of Respiratory Complexes I and IV
Vempati, U. D., Han, X., & Moraes, C. T. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m805972200 · Cited by 69
Src kinases are important regulators of mitochondrial functions
Hébert-Chatelain, É. (2012) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2012.08.014 · Cited by 66
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
Mobility in the mitochondrial electron transport chain
Hochman, J. H., Ferguson-Miller, S. M., & Schindler, M. (1985) · Biochemistry · doi:10.1021/bi00331a017 · Cited by 63
Bioenergetics : structure and function of energy transducing systems
小澤, 高., & Papa, S. (1987) · Medical Entomology and Zoology · Cited by 62
Mitochondrial biogenesis in mtDNA‐depleted cells involves a Ca2+‐dependent pathway and a reduced mitochondrial protein import
Mercy, L., Pauw, A. D., Payen, L., Tejerina, S., Houbion, A., Demazy, C., Raes, M. J., Renard, P., & Arnould, T. (2005) · FEBS Journal · doi:10.1111/j.1742-4658.2005.04913.x · Cited by 59
From protons to OXPHOS supercomplexes and Alzheimer's disease: Structure–dynamics–function relationships of energy-transducing membranes
Seelert, H., Dani, D. N., Dante, S., Hauß, T., Krause, F., Schäfer, E., Frenzel, M., Poetsch, A., Rexroth, S., Schwaßmann, H. J., et al. (2009) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2009.02.028 · Cited by 58
Riboflavin enhances the assembly of mitochondrial cytochrome c oxidase in C. elegans NADH-ubiquinone oxidoreductase mutants
Grad, L. I., & Lemire, B. D. (2006) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2005.11.009 · Cited by 57
New aspects of impaired mitochondrial function in heart failure
Rosca, M. G., & Hoppel, C. L. (2009) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-009-9215-9 · Cited by 55
Mutations in Mitochondrial Complex III Uniquely Affect Complex I in Caenorhabditis elegans
Suthammarak, W., Morgan, P. G., & Sedensky, M. M. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.159608 · Cited by 54
Structural and functional organization of Complex I in the mitochondrial respiratory chain
Bianchi, C., Fato, R., Genova, M. L., Castelli, G. P., & Lenaz, G. (2003) · BioFactors · doi:10.1002/biof.5520180202 · Cited by 51
Self-citation
The mitochondrial and prokaryotic proton-translocating NADH:ubiquinone oxidoreductases: similarities and dissimilarities of the quinone-junction sites
Grivennikova, V. G., Roth, R. G., Zakharova, N. V., Hägerhäll, C., & Vinogradov, A. D. (2003) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2003.09.001 · Cited by 48
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
The cytochrome b p.278Y>C mutation causative of a multisystem disorder enhances superoxide production and alters supramolecular interactions of respiratory chain complexes
Ghelli, A. M., Tropeano, C. V., Calvaruso, M. A., Marchesini, A., Iommarini, L., Porcelli, A. M., Zanna, C., Nardo, V. D., Martinuzzi, A., Wibrand, F., et al. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt067 · Cited by 47
A critical appraisal of the role of respiratory supercomplexes in mitochondria
Genova, M. L., & Lenaz, G. (2013) · Biological Chemistry · doi:10.1515/hsz-2012-0317 · Cited by 44
Self-citation
Respiratory Complexes III and IV Are Not Essential for the Assembly/Stability of Complex I in Fungi
Maas, M. F. P. M., Krause, F., Dencher, N. A., & Sainsard‐Chanet, A. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.12.025 · Cited by 41
Regulation by the cAMP Cascade of Oxygen Free Radical Balance in Mammalian Cells
Bellomo, F., Piccoli, C., Cocco, T., Scacco, S., Papa, F., Gaballo, A., Boffoli, D., Signorile, A., D’Aprile, A., Scrima, R., et al. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.495 · Cited by 40
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
Steady-state kinetics of the overall oxidative phosphorylation reaction in heart mitochondria. Determination of the coupling relationships between the respiratory reactions and miscellaneous observations concerning rate-limiting steps
Stoner, C. D. (1984) · Journal of Bioenergetics and Biomembranes · doi:10.1007/bf00743044 · Cited by 30
Steady-State Kinetics of Reduction of Coenzyme Q Analogs by Glycerol-3-phosphate Dehydrogenase in Brown Adipose Tissue Mitochondria
Rauchová, H., Fato, R., Drahota, Z., & Lenaz, G. (1997) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1997.0150 · Cited by 30
Self-citation
Modulation of sulfide oxidation and toxicity in rat mitochondria by dehydroascorbic acid
Hildebrandt, T. M. (2011) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2011.06.003 · Cited by 29
Metabolic control analysis of respiration in human cancer tissue
Käämbre, T., Chekulayev, V. A., Shevchuk, I. N., Tepp, K., Timohhina, N., Varikmaa, M., Quetglas, R. B., Klepinin, A., Anmann, T., Koit, A., et al. (2013) · Frontiers in Physiology · doi:10.3389/fphys.2013.00151 · Cited by 27
Regulation of NADH/CoQ Oxidoreductase: Do Phosphorylation Events Affect Activity?
Maj, M. C., Raha, S., Myint, T., & Robinson, B. H. (2004) · The Protein Journal · doi:10.1023/b:jopc.0000016255.17077.2c · Cited by 26
Binding of malate dehydrogenase and NADH channelling to complex I
Ovádi, J., Huang, Y. L., & Spivey, H. O. (1994) · Journal of Molecular Recognition · doi:10.1002/jmr.300070405 · Cited by 25
Relationships Between Mitochondrial Dynamics and Bioenergetics
Bénard, G., Bellancé, N., José, C., & Rossignol, R. (2011) · Springer eBooks · doi:10.1007/978-94-007-1291-1_2 · Cited by 24
Cytochrome c-mediated electron transfer between ubiquinol-cytochrome c reductase and cytochrome c oxidase. Kinetic evidence for a mobile cytochrome c pool
Froud, R. J., & RAGAN, C. I. (1984) · Biochemical Journal · doi:10.1042/bj2170551 · Cited by 22
Adaptative Capacity of Mitochondrial Biogenesis and of Mitochondrial Dynamics in Response to Pathogenic Respiratory Chain Dysfunction
Bénard, G., Trian, T., Bellancé, N., Berger, P., Lavie, J., Espil‐Taris, C., Rocher, C., Bouillot‐Eimer, S., Goizet, C., Nouette‐Gaulain, K., et al. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4244 · Cited by 22
Physiological significance of metabolite channelling: Author's response to commentaries
Ovádi, J. (1991) · Journal of Theoretical Biology · doi:10.1016/s0022-5193(05)80528-4 · Cited by 22
Organization of Protein and Lipid Components in Membranes
Vanderkooi, G. (1978) · Springer eBooks · doi:10.1007/978-1-4684-2463-8_4 · Cited by 16
Absence of NADH channeling in coupled reaction of mitochondrial malate dehydrogenase and complex I in alamethicin-permeabilized rat liver mitochondria
Kotlyar, A. B., Maklashina, E., & Cecchini, G. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.04.131 · Cited by 14
Mitochondrial Dynamics and Neurodegeneration
Lu, B. (2011) · Springer eBooks · doi:10.1007/978-94-007-1291-1 · Cited by 11
Coupling between the Charge-Separating Devices of the Mitochondrion: Intra- or Extramembrane?
Baum, H. (1978) · Springer eBooks · doi:10.1007/978-1-4684-2463-8_14 · Cited by 10
Energized cation transport by Complex III (ubiquinone-cytochrome c reductase)
Fry, M., & Green, D. E. (1980) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(80)91455-2 · Cited by 6

Flagged first, then by citations

Sorted by citations

Reperfusion injury and reactive oxygen species: The evolution of a concept
Granger, D. N., & Kvietys, P. R. (2015) · Redox Biology · doi:10.1016/j.redox.2015.08.020 · Cited by 1,550
“increasing the probability of ROS generation [295,312].”
Mitochondrial generation of superoxide and hydrogen peroxide as the source of mitochondrial redox signaling
Brand, M. D. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.04.001 · Cited by 1,063
Role of Cardiolipin in Mitochondrial Function and Dynamics in Health and Disease: Molecular and Pharmacological Aspects
Paradies, G., Paradies, V., Ruggiero, F. M., & Petrosillo, G. (2019) · Cells · doi:10.3390/cells8070728 · Cited by 543
“Several studies indicate that ETC complexes in the IMM are organized in higher order structures, referred generically as supercomplexes or “respirasomes”, rather than existing as individual complexes [48,49].”
Background
Mitochondrial Respiratory Supercomplex Association Limits Production of Reactive Oxygen Species from Complex I
Maranzana, E., Barbero, G., Falasca, A. I., Lenaz, G., & Genova, M. L. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4845 · Cited by 445
Self-citation
Mitochondrial dysfunction in neurodegenerative disorders
Klemmensen, M. M., Borrowman, S. H., Pearce, C., Pyles, B., & Chandra, B. (2024) · Neurotherapeutics · doi:10.1016/j.neurot.2023.10.002 · Cited by 396
“Recent data suggests complexes 1, 3, and 4, can be organized into supercomplexes, supporting more ef ﬁ cient substrate movement [58,59].”
Background

See all 306

Authors: Genova, M. L., & Lenaz, G.
Affiliations: University of Bologna (IT)
Corresponding author: Genova, Maria Luisa
ORCID: Genova, Maria Luisa
Venue: Biochimica et Biophysica Acta (BBA) - Bioenergetics
Publisher: Elsevier BV
Published: 2014-04
Volume: 1837
Issue: 4
Pages: 427-443
ISSN: 0005-2728 (ISSN-L)
DOI: 10.1016/j.bbabio.2013.11.002
OpenAlex: W2006849545
Cited by: 306
References: 187
Citations by year: 2026: 10 · 2025: 8 · 2024: 15 · 2023: 17 · 2022: 17 · 2021: 24 · 2020: 30 · 2019: 27 · 2018: 32 · 2017: 34 · 2016: 43 · 2015: 31 · 2014: 15
FWCI: 2.85
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 365 d)
Locations: Biochimica et Biophysica Acta (BBA) - Bioenergetics (publishedVersion)
PubMed (publishedVersion)
Archivio istituzionale della ricerca (Alma Mater Studiorum Università di Bologna) (submittedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Coenzyme Q10 studies and effects
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
Keywords: electron transfer, supramolecular organization, flux control, channeling, coenzyme Q10, cytochrome c, membrane lipid composition, lipid peroxidation, membrane potential, protein phosphorylation, reactive oxygen species, metabolic adaptation, signal transduction
MeSH terms: Kinetics, Membrane Lipids, Mitochondria, Models, Biological, Multienzyme Complexes, Oxidation-Reduction, Oxidative Phosphorylation, Ubiquinone, Cell Respiration, Mitochondrial Membranes

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

Functional role of mitochondrial respiratory supercomplexes

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