High membrane potential promotes alkenal-induced mitochondrial uncoupling and influences adenine nucleotide translocase conformation
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Mitochondria generate reactive oxygen species, whose downstream lipid peroxidation products, such as 4-hydroxynonenal, induce uncoupling of oxidative phosphorylation by increasing proton leak through mitochondrial inner membrane proteins such as the uncoupling proteins and adenine nucleotide translocase. Using mitochondria from rat liver, which lack uncoupling proteins, in the present study we show that energization (specifically, high membrane potential) is required for 4-hydroxynonenal to activate proton conductance mediated by adenine nucleotide translocase. Prolonging the time at high membrane potential promotes greater uncoupling. 4-Hydroxynonenal-induced uncoupling via adenine nucleotide translocase is prevented but not readily reversed by addition of carboxyatractylate, suggesting a permanent change (such as adduct formation) that renders the translocase leaky to protons. In contrast with the irreversibility of proton conductance, carboxyatractylate added after 4-hydroxynonenal still inhibits nucleotide translocation, implying that the proton conductance and nucleotide translocation pathways are different. We propose a model to relate adenine nucleotide translocase conformation to proton conductance in the presence or absence of 4-hydroxynonenal and/or carboxyatractylate.
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Synchronized oscillations in ΔΨm, the redox states of NADH, GSH/GSSG and other redox pairs, and ROS can occur across isolated cardiomyocytes.
“Synchronized oscillations in ΔΨm, the redox states of NADH, GSH/GSSG and other redox pairs, and ROS can occur across isolated cardiomyocytes (11)”
From Mitochondrial reactive oxygen species production in excitable cells: Modulators of mitochondrial and cell function (2009) · cites this paper as [11]
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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
LAEMMLI, U. K. (1970) · Nature · doi:10.1038/227680a0 · Cited by 249,961 · see citing works
Raza, H., John, A., & Nemmar, A. (2013) · Cellular Physiology and Biochemistry · doi:10.1159/000350087 · Cited by 47,311 · see citing works
Free Radicals in the Physiological Control of Cell Function
Dröge, W. (2002) · Physiological Reviews · doi:10.1152/physrev.00018.2001 · Cited by 9,855 · see citing works
Oxyl radicals, redox-sensitive signalling cascades and antioxidants
Genestra, M. (2007) · Cellular Signalling · doi:10.1016/j.cellsig.2007.04.009 · Cited by 4,930 · see citing works
Korshunov, S. S., Skulachev, V. P., & Starkov, A. A. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)01159-9 · Cited by 1,727 · see citing works
Superoxide activates mitochondrial uncoupling proteins
Echtay, K. S., Roussel, D., St-Pierre, J., Jekabsons, M. B., Cadenas, S., Stuart, J. A., Harper, J. A., Roebuck, S. J., Morrison, A., Pickering, S., et al. (2002) · Nature · doi:10.1038/415096a · Cited by 1,382 · see citing works
Self-citationMitochondrial superoxide: production, biological effects, and activation of uncoupling proteins
Brand, M. D., Affourtit, C., Esteves, T. C., Green, K., Lambert, A. J., Miwa, S., Pakay, J. L., & Parker, N. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.05.034 · Cited by 1,032 · see citing works
Self-citationProtein carbonylation, cellular dysfunction, and disease progression
Dalle‐Donne, I., Aldini, G., Carini, M., Colombo, R., Rossi, R., & Milzani, A. (2006) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2006.tb00407.x · Cited by 836 · see citing works
Skulachev, V. P. (1996) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583500005795 · Cited by 703 · see citing works
A signalling role for 4‐hydroxy‐2‐nonenal in regulation of mitochondrial uncoupling
Echtay, K. S., Esteves, T. C., Pakay, J. L., Jekabsons, M. B., Lambert, A. J., Portero‐Otín, M., Pamplona, R., Vidal‐Puig, A. J., Wang, S., Roebuck, S. J., et al. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg412 · Cited by 597 · see citing works
Self-citationLenaz, G. (2001) · IUBMB Life · doi:10.1080/15216540152845957 · Cited by 585 · see citing works
Fatty acid circuit as a physiological mechanism of uncoupling of oxidative phosphorylation
Skulachev, V. P. (1991) · FEBS Letters · doi:10.1016/0014-5793(91)80658-p · Cited by 467 · see citing works
Subcellular components: preparation and fractionation;
Birnie, G. D. (1972) · Cited by 422 · see citing works
Mitochondrial adenine nucleotide translocase is modified oxidatively during aging
Yan, L.-J., & Sohal, R. S. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.22.12896 · Cited by 414 · see citing works
Effect of fatty acids on energy coupling processes in mitochondria
Wojtczak, L., & Schönfeld, P. (1993) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(93)90004-y · Cited by 363 · see citing works
The ATP/ADP‐antiporter is involved in the uncoupling effect of fatty acids on mitochondria
Andreyev, A. Y., BONDAREVA, T. O., Dedukhova, V. I., MOKHOVA, E. N., Skulachev, V. P., TSOFINA, L. M., Волков, Н. И., & VYGODINA, T. V. (1989) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1989.tb14867.x · Cited by 302 · see citing works
Beyer, K., & Klingenberg, M. (1985) · Biochemistry · doi:10.1021/bi00336a001 · Cited by 301 · see citing works
Intervention strategies to inhibit protein carbonylation by lipoxidation‐derived reactive carbonyls
Aldini, G., Dalle‐Donne, I., Facino, R. M., Milzani, A., & Carini, M. (2006) · Medicinal Research Reviews · doi:10.1002/med.20073 · Cited by 289 · see citing works
The Contribution of Mitochondrial Respiratory Complexes to the Production of Reactive Oxygen Species
McLennan, H. R., & Esposti, M. D. (2000) · Journal of Bioenergetics and Biomembranes · doi:10.1023/a:1005507913372 · Cited by 264 · see citing works
Molecular aspects of the adenine nucleotide carrier from mitochondria
Klingenberg, M. (1989) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(89)90001-5 · Cited by 236 · see citing works
Hoffmann, B., Stöckl, A., Schlame, M., Beyer, K., & Klingenberg, M. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)42117-x · Cited by 217 · see citing works
Effect of fatty acids on H+ transport activity of the reconstituted uncoupling protein.
Winkler, E., & Klingenberg, M. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)41974-0 · Cited by 214 · see citing works
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 · see citing works
Rial, E., POUSTIE, A., & Nicholls, D. G. (1983) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1983.tb07815.x · Cited by 186 · see citing works
Reactive Oxygen Species Mediate Cellular Damage in Alzheimer Disease
Perry, G. L., Castellani, R. J., Hirai, K., & Smith, M. A. (1998) · Journal of Alzheimer s Disease · doi:10.3233/jad-1998-1103 · Cited by 184 · see citing works
Uncoupling proteins: A role in protection against reactive oxygen species—or not?
Cannon, B., Shabalina, I. G., Kramarova, T. V., Petrovic, N., & Nedergaard, J. (2006) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2006.05.016 · Cited by 182 · see citing works
Shabalina, I. G., Jacobsson, A., Cannon, B., & Nedergaard, J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m402375200 · Cited by 162 · see citing works
Lee, J. F. Y., Li, Y., Zhu, H., Yang, S., Lin, H. Z., Trush, M. A., & Diehl, A. M. (1999) · Hepatology · doi:10.1002/hep.510290320 · Cited by 155 · see citing works
Fatty Acids as Acute Regulators of the Proton Conductance of Hamster Brown‐Fat Mitochondria
LOCKE, R. M., Rial, E., SCOTT, I. D., & Nicholls, D. G. (1982) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1982.tb07060.x · Cited by 150 · see citing works
Carboxyatractylate inhibits the uncoupling effect of free fatty acids
Andreyev, A. Y., BONDAREVA, T. O., Dedukhova, V. I., MOKHOVA, E. N., Skulachev, V. P., & Волков, Н. И. (1988) · FEBS Letters · doi:10.1016/0014-5793(88)81436-4 · Cited by 149 · see citing works
Mitochondrial uncouplers with an extraordinary dynamic range
Lou, P.-H., Hansen, B. S., Olsen, P. H., Tullin, S., Murphy, M. P., & Brand, M. D. (2007) · Biochemical Journal · doi:10.1042/bj20070606 · Cited by 141 · see citing works
Self-citationInvolvement of aspartate/glutamate antiporter in fatty acid-induced uncoupling of liver mitochondria
Samartsev, V. N., Smirnov, A. V., Zeldi, I. P., Маркова, О. В., MOKHOVA, E. N., & Skulachev, V. P. (1997) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(96)00166-1 · Cited by 135 · see citing works
Kupffer Cells Are a Dominant Site of Uncoupling Protein 2 Expression in Rat Liver
Larrouy, D., Laharrague, P. F., Carrera, G., Viguerie, N., Lévi-Meyrueis, C., Fleury, C., Pecqueur, C., Nibbelink, M. M., André, M., Casteilla, L., et al. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.6852 · Cited by 134 · see citing works
Inhibition of adenine nucleotide translocator by lipid peroxidation products
Chen, J. J., Bertrand, H. A., & Yu, B. P. (1995) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(95)00066-7 · Cited by 128 · see citing works
The Binding of Atractylate and Carboxy‐atractylate to Mitochondria
Klingenberg, M., GREBE, K., & Scherer, B. (1975) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1975.tb04003.x · Cited by 106 · see citing works
Haworth, R. A., & Hunter, D. R. (2000) · Journal of Bioenergetics and Biomembranes · doi:10.1023/a:1005568630151 · Cited by 105 · see citing works
HARPER, J. A., STUART, J. A., JEKABSONS, M. B., ROUSSEL, D., BRINDLE, K. M., DICKINSON, K., JONES, R. B., & BRAND, M. D. (2002) · Biochemical Journal · doi:10.1042/bj3610049 · Cited by 87 · see citing works
Self-citationGonzález‐Barroso, M. M., Fleury, C., Bouillaud, F., Nicholls, D. G., & Rial, E. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.25.15528 · Cited by 84 · see citing works
UCP1 and Defense against Oxidative Stress
Shabalina, I. G., Petrovič, N., Kramarova, T. V., Joris Hoeks, J., Cannon, B., & Nedergaard, J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m601387200 · Cited by 82 · see citing works
Vignais, P. V., & Vignais, P. M. (1972) · FEBS Letters · doi:10.1016/0014-5793(72)80534-9 · Cited by 77 · see citing works
Reactive Oxygen Species, Vascular Disease and Cardiovascular Surgery
Jeremy, J. Y., Shukla, N., Muzaffar, S., Handley, A., & Angelini, G. D. (2004) · Current Vascular Pharmacology · doi:10.2174/1570161043385691 · Cited by 75 · see citing works
Energization-dependent endogenous activation of proton conductance in skeletal muscle mitochondria
Parker, N., Affourtit, C., Vidal‐Puig, A., & Brand, M. D. (2008) · Biochemical Journal · doi:10.1042/bj20080006 · Cited by 73 · see citing works
Self-citationAquila, H., EIERMANN, W., Babel, W., & Klingenberg, M. (1978) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1978.tb12270.x · Cited by 73 · see citing works
Stimulation of mitochondrial proton conductance by hydroxynonenal requires a high membrane potential
Parker, N., Vidal‐Puig, A., & Brand, M. D. (2008) · Bioscience Reports · doi:10.1042/bsr20080002 · Cited by 67 · see citing works
Self-citationTransformed but not normal hepatocytes express UCP2
Carretero, M. V., Torres, L., Latasa, M. U., García–Trevijano, E. R., Prìeto, J., Mato, J. M., & Avila, M. A. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)01335-0 · Cited by 54 · see citing works
Ullrich, O., Grune, T., Henke, W., Esterbauer, H., & Siems, W. G. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)00922-8 · Cited by 53 · see citing works
Beck, V., Jabůrek, M., Breen, E. P., Porter, R. K., Ježek, P., & Pohl, E. E. (2006) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2006.03.006 · Cited by 43 · see citing works
The Reactivity of ‐SH Groups in the ADP/ATP Carrier Isolated from Beef Heart Mitochondria
Aquila, H., & Klingenberg, M. (1982) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1982.tb05859.x · Cited by 41 · see citing works
Is there a common binding center in the ADP, ATP carrier for substrate and inhibitors?
Klingenberg, M., & Appel, M. (1980) · FEBS Letters · doi:10.1016/0014-5793(80)81029-5 · Cited by 37 · see citing works
Porter, R. K. (2006) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2006.04.012 · Cited by 32 · see citing works
Block, M. R., Lauquin, J. M., & Vignais, P. V. (1981) · Biochemistry · doi:10.1021/bi00512a051 · Cited by 29 · see citing works
High expression of uncoupling protein 2 in foetal liver
Hodný, Z., Kolářová, P., Rossmeisl, M., Horáková, M., Nibbelink, M. M., Pénicaud, L., Casteilla, L., & Kopecký, J. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)00230-0 · Cited by 29 · see citing works
Flagged first, then by citations
2 of the 54 references couldn’t be matched to a known paper.
Research works printed but not linked: 1
- [33]Brand M. D. Brown G. C. Cooper C. E. Measurement of mitochondrial protonmotive force. Bioenergetics A practical approach 1995 Oxford IRL Press 39 62
Cited by
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Stowe, D. F., & Camara, A. K. S. (2009) · Antioxidants & Redox Signaling · doi:10.1089/ars.2008.2331 · Cited by 471 · see citing works
Lagranha, C. J., Deschamps, A. M., Aponte, A. M., Steenbergen, C., & Murphy, E. (2010) · Circulation Research · doi:10.1161/circresaha.109.213645 · Cited by 328 · see citing works
Unearthing the secrets of mitochondrial ROS and glutathione in bioenergetics
Mailloux, R. J., McBride, S., & Harper, M. (2013) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2013.09.001 · Cited by 302 · see citing works
4-Hydroxy-2-nonenal: a critical target in oxidative stress?
Breitzig, M., Bhimineni, C., Lockey, R. F., & Kolliputi, N. (2016) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00101.2016 · Cited by 284 · see citing works
The on-off switches of the mitochondrial uncoupling proteins
Azzu, V., & Brand, M. D. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2009.11.001 · Cited by 239 · see citing works
Self-citationPotential Therapeutic Benefits of Strategies Directed to Mitochondria
Camara, A. K. S., Lesnefsky, E. J., & Stowe, D. F. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2788 · Cited by 195 · see citing works
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Berry, B. J., Trewin, A. J., Amitrano, A. M., Kim, M., & Wojtovich, A. P. (2018) · Journal of Molecular Biology · doi:10.1016/j.jmb.2018.03.025 · Cited by 175 · see citing works
Mitochondrial uncoupling and lifespan
Mookerjee, S. A., Divakaruni, A. S., Jastroch, M., & Brand, M. D. (2010) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2010.03.010 · Cited by 169 · see citing works
Self-citationThe role of aberrant mitochondrial bioenergetics in diabetic neuropathy
Chowdhury, S. R., Smith, D. R., & Fernyhough, P. (2012) · Neurobiology of Disease · doi:10.1016/j.nbd.2012.03.016 · Cited by 166 · see citing works
Akude, E., Zherebitskaya, E., Chowdhury, S. R., Smith, D. R., Dobrowsky, R. T., & Fernyhough, P. (2010) · Diabetes · doi:10.2337/db10-0818 · Cited by 145 · see citing works
Crichton, P. G., Lee, Y., & Kunji, E. R. S. (2017) · Biochimie · doi:10.1016/j.biochi.2016.12.016 · Cited by 144 · see citing works
Superior Intrinsic Mitochondrial Respiration in Women Than in Men
Cardinale, D. A., Larsen, F. J., Schiffer, T. A., Morales‐Álamo, D., Ekblom, B. T., Calbet, J. A. L., Holmberg, H., & Boushel, R. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.01133 · Cited by 136 · see citing works
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 100 · see citing works
Uncoupling protein 1 binds one nucleotide per monomer and is stabilized by tightly bound cardiolipin
Lee, Y., Willers, C., Kunji, E. R. S., & Crichton, P. G. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1503833112 · Cited by 97 · see citing works
Adenine nucleotide translocase family: four isoforms for apoptosis modulation in cancer
Brenner, C., Subramaniam, K., Pertuiset, C., & Pervaiz, S. (2010) · Oncogene · doi:10.1038/onc.2010.501 · Cited by 82 · see citing works
Won, J. C., Park, J., Kim, Y., Koh, E. H., Seol, S. M., Jeon, B. H., Han, J., Kim, J. R., Park, T., Choi, C. S., et al. (2009) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.109.198721 · Cited by 69 · see citing works
Parker, N., Crichton, P. G., Vidal‐Puig, A., & Brand, M. D. (2009) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-009-9232-8 · Cited by 65 · see citing works
Self-citationGlutaredoxin-2 Is Required to Control Proton Leak through Uncoupling Protein-3
Mailloux, R. J., Xuan, J. Y., Beauchamp, B., Jui, L., Lou, M. F., & Harper, M. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.442905 · Cited by 64 · see citing works
Huang, Q., Wang, H., Perry, S. W., & Figueiredo‐Pereira, M. E. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.464552 · Cited by 62 · see citing works
Mitochondria as a Source and a Target for Uremic Toxins
Popkov, V. A., Silachev, D. N., Zalevsky, A. O., Zorov, D. B., & Plotnikov, E. Y. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20123094 · Cited by 62 · see citing works
Woyda-Ploszczyca, A. M., & Jarmuszkiewicz, W. (2016) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2016.10.003 · Cited by 52 · see citing works
The Plant Mitochondrial Transportome: Balancing Metabolic Demands with Energetic Constraints
Lee, C. P., & Millar, A. H. (2016) · Trends in Plant Science · doi:10.1016/j.tplants.2016.04.003 · Cited by 45 · see citing works
Fernyhough, P., & McGavock, J. (2014) · Handbook of clinical neurology · doi:10.1016/b978-0-444-53480-4.00027-8 · Cited by 47 · see citing works
Kadenbach, B., Ramzan, R., & Vogt, S. K. (2012) · Mitochondrion · doi:10.1016/j.mito.2012.11.005 · Cited by 41 · see citing works
Aguirre, E., & Cadenas, S. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.06.009 · Cited by 40 · see citing works
Fatty Acids are Key in 4-Hydroxy-2-Nonenal-Mediated Activation of Uncoupling Proteins 1 and 2
Malingriaux, E. A., Rupprecht, A., Gille, L., Jovanović, O., Ježek, P., Jabůrek, M., & Pohl, E. E. (2013) · PLoS ONE · doi:10.1371/journal.pone.0077786 · Cited by 40 · see citing works
Friederich‐Persson, M., Aslam, S., Nordquist, L., Welch, W. J., Wilcox, C. S., & Palm, F. (2012) · PLoS ONE · doi:10.1371/journal.pone.0039635 · Cited by 38 · see citing works
Transcription factor NF-kappa B represses ANT1 transcription and leads to mitochondrial dysfunctions
Zhang, C., Jiang, H., Wang, P., Liu, H., & Sun, X. (2017) · Scientific Reports · doi:10.1038/srep44708 · Cited by 37 · see citing works
Different Effects of Guanine Nucleotides (GDP and GTP) on Protein-Mediated Mitochondrial Proton Leak
Woyda-Ploszczyca, A. M., & Jarmuszkiewicz, W. (2014) · PLoS ONE · doi:10.1371/journal.pone.0098969 · Cited by 33 · see citing works
Involvement of 4-hydroxy-2-nonenal in the pathogenesis of pulmonary fibrosis
Reyes-Jiménez, E., Ramírez-Hernández, A. A., Santos-Álvarez, J. C., Velázquez-Enríquez, J. M., Pina-Canseco, M. D. S., Baltiérrez‐Hoyos, R., & Vásquez-Garzón, V. R. (2021) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-021-04244-9 · Cited by 29 · see citing works
The cause of cancer: The unifying theory
Majérus, M.-A. (2022) · Advances in Cancer Biology - Metastasis · doi:10.1016/j.adcanc.2022.100034 · Cited by 28 · see citing works
Schmitz, J. P. J., Jeneson, J. A. L., van Oorschot, J. W. M., Prompers, J. J., Nicolay, K., Hilbers, P. A. J., & van Riel, N. A. W. (2012) · PLoS ONE · doi:10.1371/journal.pone.0034118 · Cited by 28 · see citing works
Petrick, H. L., Foley, K. P., Zlitni, S., Brunetta, H. S., Paglialunga, S., Miotto, P. M., Politis‐Barber, V., O’Dwyer, C., Philbrick, D. J., Fullerton, M. D., et al. (2020) · Function · doi:10.1093/function/zqaa013 · Cited by 26 · see citing works
Devaux, J. B. L., Hickey, A. J., & Renshaw, G. M. C. (2019) · Journal of Experimental Biology · doi:10.1242/jeb.191353 · Cited by 24 · see citing works
Cardinale, D. A., Gejl, K. D., Petersen, K. G., Nielsen, J., Ørtenblad, N., & Larsen, F. J. (2021) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00829.2020 · Cited by 21 · see citing works
Liu, Y., Sun, B., Zhang, S., Li, J., Qi, J., Bai, C., Zhang, J., & Liang, S. (2021) · Reproduction in Domestic Animals · doi:10.1111/rda.13930 · Cited by 21 · see citing works
Rogers, C., Davis, B., Neufer, P. D., Murphy, M. P., Anderson, E. J., & Robidoux, J. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.11.012 · Cited by 19 · see citing works
Reactive Carbonyl Species and Protein Lipoxidation in Atherogenesis
Nègre‐Salvayre, A., & Salvayre, R. (2024) · Antioxidants · doi:10.3390/antiox13020232 · Cited by 18 · see citing works
Podinić, T., Limoges, L., Mónaco, C., MacAndrew, A., Minhas, M., Nederveen, J. P., & Raha, S. (2024) · Cells · doi:10.3390/cells13060486 · Cited by 18 · see citing works
Ferreira, D. J. S., Pedroza, A. A. D. S., Braz, G. R. F., Fernandes, M. P., & Lagranha, C. J. (2018) · Nutritional Neuroscience · doi:10.1080/1028415x.2018.1444543 · Cited by 17 · see citing works
Braz, G. R. F., da Silva, A. I., Silva, S. C. A., Pedroza, A. A. D. S., de Lemos, M. D. T. B., de Lima, F. A. S., Silva, T. L. A., & Lagranha, C. J. (2020) · Life Sciences · doi:10.1016/j.lfs.2020.117307 · Cited by 16 · see citing works
Baliūtytė, G., Trumbeckaitė, S., Banienė, R., Borutaitė, V., & Toleikis, A. (2014) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-014-9590-8 · Cited by 13 · see citing works
Mitochondrial Respiration-Dependent ANT2-UCP2 Interaction
Schiffer, T. A., Löf, L., Gallini, R., Kamali‐Moghaddam, M., Carlström, M., & Palm, F. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.866590 · Cited by 9 · see citing works
Woyda-Ploszczyca, A. M., & Jarmuszkiewicz, W. (2012) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-012-9456-x · Cited by 7 · see citing works
Samartsev, V. N., & Kozhina, O. V. (2010) · Biochemistry (Moscow) · doi:10.1134/s0006297910050093 · Cited by 5 · see citing works
Adakeeva, S. I., Dubinin, M. V., & Samartsev, V. N. (2015) · Biochemistry (Moscow) Supplement Series A Membrane and Cell Biology · doi:10.1134/s199074781501002x · Cited by 4 · see citing works
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Llontop, N., Mancilla, C., Ojeda-Provoste, P., Torres, A. K., Godoy, A., Tapia‐Rojas, C., & Kerr, B. (2025) · Life Sciences · doi:10.1016/j.lfs.2025.123478 · Cited by 2 · see citing works
Friedman, N. S., Britto, G. J. D., & Lehner, A. N. (2025) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-025-01844-w · Cited by 2 · see citing works
Samartsev, V. N., Dubinin, M. V., & Krasnoshchekova, O. E. (2015) · Biochemistry (Moscow) Supplement Series A Membrane and Cell Biology · doi:10.1134/s1990747815020178 · Cited by 1 · see citing works
Systems biology of energy metabolism in skeletal muscle
Schmitz, J. J. (2012) · TU/e Research Portal · doi:10.6100/ir739234
- Authors
- Azzu, V., Parker, N., & Brand, M. D.
- Affiliations
- MRC Mitochondrial Biology Unit (GB)
- Corresponding author
- Azzu, Vian
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 2008-06-26
- Volume
- 413
- Issue
- 2
- Pages
- 323-332
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- PMC
- PMC2474560
- OpenAlex
- W1976727447
- Cited by
- 52
- References
- 54
- Citations by year
- 2025: 2 · 2024: 2 · 2022: 2 · 2021: 3 · 2020: 2 · 2019: 2 · 2018: 3 · 2017: 2 · 2016: 3 · 2015: 3 · 2014: 4 · 2013: 5 · 2012: 6
- FWCI
- 1.64
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Biochemical Journal (publishedVersion, cc-by-nc)
- PubMed Central (publishedVersion, cc-by-nc)
- PubMed (publishedVersion)
- HAL (submittedVersion, other-oa)
- UCL Discovery (University College London) (submittedVersion)
- Trinity's Access to Research Output (TARA) (Trinity College Dublin) (submittedVersion, other-oa)
- Funders
- Wellcome Trust (066750, 065326)
- 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 › Redox biology and oxidative stress
- Keywords
- mitochondrial membrane potential, 4-hydroxynonenal, alkenals, mitochondrial uncoupling, adenine nucleotide translocase, proton leak, oxidative phosphorylation, carboxyatractylate, protein conformation, lipid peroxidation, rat liver mitochondria
- MeSH terms
- Mitochondrial ADP, ATP Translocases, Aldehydes, Animals, Biological Transport, Female, Kinetics, Membrane Potentials, Mitochondria, Mitochondria, Liver, Nucleotides, Oxidative Phosphorylation, Oxygen Consumption, Protein Conformation, Protons, Rats
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