The basal proton conductance of mitochondria depends on adenine nucleotide translocase content

Brand, Martin D.; Pakay, Julian L.; Ocloo, Augustine; Kokoszka, Jason; Wallace, Douglas C.; Brookes, Paul S.; Cornwall, Emma J.

doi:10.1042/bj20050890

Cited by 410Mitochondrial Function and PathologyATP Synthase and ATPases ResearchMetabolism, Diabetes, and Cancer

The basal proton conductance of mitochondria depends on adenine nucleotide translocase content

Open access

Brand, Martin D., Pakay, Julian L., Ocloo, Augustine, Kokoszka, Jason, Wallace, Douglas C., Brookes, Paul S., Cornwall, Emma J.·2005·Biochemical Journal

DOI 10.1042/bj20050890PMC PMC1316271

Open this paper in CoChat — free account Open PDF

Abstract

The basal proton conductance of mitochondria causes mild uncoupling and may be an important contributor to metabolic rate. The molecular nature of the proton-conductance pathway is unknown. We show that the proton conductance of muscle mitochondria from mice in which isoform 1 of the adenine nucleotide translocase has been ablated is half that of wild-type controls. Overexpression of the adenine nucleotide translocase encoded by the stress-sensitive B gene in Drosophila mitochondria increases proton conductance, and underexpression decreases it, even when the carrier is fully inhibited using carboxyatractylate. We conclude that half to two-thirds of the basal proton conductance of mitochondria is catalysed by the adenine nucleotide carrier, independently of its ATP/ADP exchange or fatty-acid-dependent proton-leak functions.

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/bj20050890

Cites

52 of 52 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?

ANTs can account for up to 50% of basal mitochondrial membrane proton conductance.
“Underlining their importance, ANTs can account for up to 50% of basal mitochondrial membrane proton conductance [25].”
From Mitochondrial Uncoupling: A Key Controller of Biological Processes in Physiology and Diseases (2019) · cites this paper as [25]

Self-check

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

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

DETERMINATION OF SERUM PROTEINS BY MEANS OF THE BIURET REACTION
Gornall, A. G., Bardawill, C. J., & David, M. M. (1949) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)57021-6 · Cited by 16,164 · see citing works
Mitochondrial 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
Uncoupling: new approaches to an old problem of bioenergetics
Skulachev, V. P. (1998) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(97)00091-1 · Cited by 893 · see citing works
Role of uncoupled and non-coupled oxidations in maintenance of safely low levels of oxygen and its one-electron reductants
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
A mouse model for mitochondrial myopathy and cardiomyopathy resulting from a deficiency in the heart/muscle isoform of the adenine nucleotide translocator
Graham, B. H., Waymire, K. G., Cottrell, B. A., Trounce, I. A., MacGregor, G. R., & Wallace, D. C. (1997) · Nature Genetics · doi:10.1038/ng0797-226 · Cited by 556 · see citing works
Uncoupling Protein 2, in Vivo Distribution, Induction upon Oxidative Stress, and Evidence for Translational Regulation
Pecqueur, C., Alves‐Guerra, M., Gelly, C., Lévi-Meyrueis, C., Couplan, E., Collins, S., Ricquier, D., Bouillaud, F., & Miroux, B. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m006938200 · Cited by 474 · see citing works
The causes and functions of mitochondrial proton leak
Brand, M. D., Chien, L.-F., Ainscow, E. K., Rolfe, D. F. S., & Porter, R. K. (1994) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(94)90099-x · Cited by 466 · see citing works
Reversible Inhibition of Mitochondrial Adenosine Diphosphate Phosphorylation by Long Chain Acyl Coenzyme A Esters
Pande, S. V., & Blanchaer, M. C. (1971) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)62505-0 · Cited by 355 · see citing works
Mitochondrial carrier proteins
Palmieri, F. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)00329-7 · Cited by 341 · see citing works
Contribution of mitochondrial proton leak to skeletal muscle respiration and to standard metabolic rate
Rolfe, D. F. S., & Brand, M. D. (1996) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1996.271.4.c1380 · Cited by 330 · see citing works
Membranes as Possible Pacemakers of Metabolism
Hulbert, A. J., & Else, P. L. (1999) · Journal of Theoretical Biology · doi:10.1006/jtbi.1999.0955 · Cited by 312 · 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
Superoxide and hydrogen peroxide production by Drosophila mitochondria
Miwa, S., St‐Pierre, J., Partridge, L., & Brand, M. D. (2003) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(03)00464-7 · Cited by 298 · see citing works
Evolution of energy metabolism. Proton permeability of the inner membrane of liver mitochondria is greater in a mammal than in a reptile
Brand, M. D., Couture, P., Else, P. L., Withers, K., & Hulbert, A. J. (1991) · Biochemical Journal · doi:10.1042/bj2750081 · Cited by 287 · see citing works
Contribution of mitochondrial proton leak to respiration rate in working skeletal muscle and liver and to SMR
Rolfe, D. F. S., Newman, J. M. B., Buckingham, J. A., Clark, M. G., & Brand, M. D. (1999) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1999.276.3.c692 · Cited by 277 · see citing works
The proton leak across the mitochondrial inner membrane
Brand, M. D. (1990) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(90)90232-s · Cited by 261 · see citing works
Body mass dependence of H+ leak in mitochondria and its relevance to metabolic rate
Porter, R. K., & Brand, M. D. (1993) · Nature · doi:10.1038/362628a0 · Cited by 257 · see citing works
Characteristics of mitochondrial proton leak and control of oxidative phosphorylation in the major oxygen-consuming tissues of the rat
Rolfe, D. F. S., Hulbert, A. J., & Brand, M. D. (1994) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(94)90062-0 · Cited by 243 · see citing works
The Proton Permeability of the Inner Membrane of Liver Mitochondria from Ectothermic and Endothermic Vertebrates and from Obese Rats: Correlations with Standard Metabolic Rate and Phospholipid Fatty Acid Composition
Brookes, P. S., Buckingham, J. A., Tenreiro, A. M., Hulbert, A. J., & Brand, M. D. (1998) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/s0305-0491(97)00357-x · Cited by 238 · see citing works
The Physiological Significance of Mitochondrial Proton Leak in Animal Cells and Tissues
Rolfe, D. F. S., & Brand, M. D. (1997) · Bioscience Reports · doi:10.1023/a:1027327015957 · Cited by 232 · see citing works
O2 solubility in aqueous media determined by a kinetic method
Reynafarje, B., Costa, L. E., & Lehninger, A. L. (1985) · Analytical Biochemistry · doi:10.1016/0003-2697(85)90381-1 · Cited by 226 · see citing works
Allometry of mitochondrial proton leak: influence of membrane surface area and fatty acid composition
Porter, R. K., Hulbert, A. J., & Brand, M. D. (1996) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.1996.271.6.r1550 · Cited by 208 · see citing works
The basal proton conductance of skeletal muscle mitochondria from transgenic mice overexpressing or lacking uncoupling protein-3
Cadenas, S., Echtay, K. S., Harper, J. A., Jekabsons, M. B., Buckingham, J. A., Grau, E., Abuin, A., Chapman, H., Clapham, J. C., & Brand, M. D. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109736200 · Cited by 199 · see citing works
Self-citation
No Evidence for a Basal, Retinoic, or Superoxide-induced Uncoupling Activity of the Uncoupling Protein 2 Present in Spleen or Lung Mitochondria
Couplan, E., del Mar Gonzalez-Barroso, M., Alves-Guerra, M. C., Ricquier, D., Goubern, M., & Bouillaud, F. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202535200 · Cited by 161 · see citing works
Altered relationship between protonmotive force and respiration rate in non‐phosphorylating liver mitochondria isolated from rats of different thyroid hormone status
Hafner, R. P., Nobes, C. D., McGown, A. D., & Brand, M. D. (1988) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1988.tb14477.x · Cited by 151 · 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
Proton conductance and fatty acyl composition of liver mitochondria correlates with body mass in birds
Brand, M. D., Turner, N. A., Ocloo, A., Else, P. L., & Hulbert, A. J. (2003) · Biochemical Journal · doi:10.1042/bj20030984 · Cited by 147 · see citing works
The reactions catalysed by the mitochondrial uncoupling proteins UCP2 and UCP3
Esteves, T. C., & Brand, M. D. (2005) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2005.06.002 · Cited by 146 · see citing works
A mitochondrial uncoupling artifact can be caused by expression of uncoupling protein 1 in yeast
Stuart, J. A., Harper, J. A., Brindle, K. M., Jekabsons, M. B., & Brand, M. D. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3560779 · Cited by 116 · see citing works
Control of respiration in non-phosphorylating mitochondria is shared between the proton leak and the respiratory chain.
Brand, M. D., Hafner, R. P., & Brown, G. C. (1988) · PubMed · Cited by 115 · see citing works
Regulation of adenine nucleotide translocase and glycerol 3-phosphate dehydrogenase expression by thyroid hormones in different rat tissues
DÜMMLER, K., Müller, S. P., & SEITZ, H. J. (1996) · Biochemical Journal · doi:10.1042/bj3170913 · Cited by 112 · see citing works
The mechanism of the increase in mitochondrial proton permeability induced by thyroid hormones
Brand, M. D., Steverding, D., Kadenbach, B., Stevenson, P. M., & Hafner, R. P. (1992) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1992.tb16984.x · Cited by 101 · see citing works
The Proton Permeability of Liposomes Made from Mitochondrial Inner Membrane Phospholipids: Comparison with Isolated Mitochondria
Brookes, P. S., Rolfe, D. F. S., & Brand, M. D. (1997) · The Journal of Membrane Biology · doi:10.1007/s002329900168 · Cited by 97 · see citing works
Isolation of skeletal muscle mitochondria from hamsters using an lonic medium containing ethylenediarninetetraacetic acid and nagarse
Bhattacharya, S. K., Thakar, J. H., Johnson, P. L., & Shanklin, D. R. (1991) · Analytical Biochemistry · doi:10.1016/0003-2697(91)90546-6 · Cited by 97 · see citing works
Measurement of mitochondrial protonmotive force
Brand, M. D. (1995) · doi:10.1093/oso/9780199634897.003.0003 · Cited by 96 · see citing works
stress sensitive B Encodes an Adenine Nucleotide Translocase in Drosophila melanogaster
Zhang, Y., Roote, J., Brogna, S., Davis, A. W., Barbash, D. A., Nash, D., & Ashburner, M. (1999) · Genetics · doi:10.1093/genetics/153.2.891 · Cited by 93 · see citing works
Artifactual uncoupling by uncoupling protein 3 in yeast mitochondria at the concentrations found in mouse and rat skeletal-muscle mitochondria
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
Up-regulation of Nuclear and Mitochondrial Genes in the Skeletal Muscle of Mice Lacking the Heart/Muscle Isoform of the Adenine Nucleotide Translocator
Murdock, D. G., Boone, B. E., Esposito, L., & Wallace, D. C. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.20.14429 · Cited by 85 · see citing works
The proton permeability of liposomes made from mitochondria) inner membrane phospholipids: No effect of fatty acid composition
Brookes, P. S., Hulbert, A. J., & Brand, M. D. (1997) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/s0005-2736(97)00160-0 · Cited by 83 · see citing works
Mitochondrial coupling in vivo in mouse skeletal muscle
Marcinek, D. J., Schenkman, K. A., Ciesielski, W. A., & Conley, K. E. (2004) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00237.2003 · Cited by 81 · see citing works
A mitochondrial uncoupling artifact can be caused by expression of uncoupling protein 1 in yeast
Stuart, J. A., Harper, J. A., Brindle, K. M., et al. (2001) · Biochemical Journal · doi:10.1042/bj3560779 · Cited by 77 · see citing works
Expression of the bovine heart mitochondrial ADP/ATP carrier in yeast mitochondria: significantly enhanced expression by replacement of the N-terminal region of the bovine carrier by the corresponding regions of the yeast carriers
Hashimoto, M., Shinohara, Y., Majima, E., Hatanaka, T., Yamazaki, N., & Terada, H. (1999) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(98)00155-8 · Cited by 71 · see citing works
Proton leak in hepatocytes and liver mitochondria from archosaurs (crocodiles) and allometric relationships for ectotherms
Hulbert, A., Else, P. L., Manolis, S., & Brand, M. D. (2002) · Journal of Comparative Physiology B · doi:10.1007/s00360-002-0264-1 · Cited by 68 · see citing works
AMP decreases the efficiency of skeletal-muscle mitochondria
Cadenas, S., Buckingham, J. A., St‐Pierre, J., Dickinson, K., Jones, R. B., & Brand, M. D. (2000) · Biochemical Journal · doi:10.1042/bj3510307 · Cited by 57 · see citing works
Mitochondrial proton leak in brown adipose tissue mitochondria of Ucp1 -deficient mice is GDP insensitive
Monemdjou, S., Kozak, L. P., & Harper, M. (1999) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.1999.276.6.e1073 · Cited by 53 · see citing works
Effects of magnesium and nucleotides on the proton conductance of rat skeletal-muscle mitochondria
Cadenas, S., & Brand, M. D. (2000) · Biochemical Journal · doi:10.1042/bj3480209 · Cited by 50 · see citing works
The concentration of the mitochondrial pyruvate carrier in rat liver and heart mitochondria determined with α-cyano-β-(1-phenylindol-3-yl)acrylate
Shearman, M. S., & Halestrap, A. P. (1984) · Biochemical Journal · doi:10.1042/bj2230673 · Cited by 47 · see citing works
Does Any Yeast Mitochondrial Carrier Have a Native Uncoupling Protein Function?
Roussel, D., Harding, M., Runswick, M. J., Walker, J. E., & Brand, M. D. (2002) · Journal of Bioenergetics and Biomembranes · doi:10.1023/a:1016027302232 · Cited by 37 · see citing works
31P NMR magnetization transfer study of the control of ATP turnover in Saccharomyces cerevisiae.
Sheldon, J. G., Williams, S. P., Fulton, A. M., & Brindle, K. M. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.13.6399 · Cited by 36 · see citing works
Interaction of α-cyano[14C]cinnamate with the mitochondrial pyruvate translocator
Paradies, G. (1984) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(84)90260-3 · Cited by 36 · see citing works
Use of Carboxyatractylate and Tight-Binding Inhibitor Theory to Determine the Concentration of Functional Mitochondrial Adenine Nucleotide Translocators in a Reconstituted System
Streicherscott, J., Lapidus, R. G., & Sokolove, P. M. (1993) · Analytical Biochemistry · doi:10.1006/abio.1993.1152 · Cited by 13 · see citing works

Flagged first, then by citations

Research works printed but not linked: 1

Cornwall, E. (2004) The role of the adenine nucleotide translocase in mitochondrial proton leak, PhD thesis, pp. 197, University of Cambridge, Cambridge 42

Sorted by citations

Molecular Aspects of Thyroid Hormone Actions
Cheng, S.-Y., Leonard, J. L., & Davis, P. J. (2010) · Endocrine Reviews · doi:10.1210/er.2009-0007 · Cited by 1,384 · see citing works
Mitochondrial electron transport chain, ROS generation and uncoupling (Review)
Zhao, R., Jiang, S., Zhang, L., & Yu, Z. (2019) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2019.4188 · Cited by 1,415 · see citing works
Mitochondrial proton and electron leaks
Jastroch, M., Divakaruni, A. S., Mookerjee, S., Treberg, J. R., & Brand, M. D. (2010) · Essays in Biochemistry · doi:10.1042/bse0470053 · Cited by 829 · see citing works
New Advances in Adaptive Thermogenesis: UCP1 and Beyond
Chouchani, E. T., Kazak, L., & Spiegelman, B. M. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.11.002 · Cited by 797 · see citing works
Dietary Inorganic Nitrate Improves Mitochondrial Efficiency in Humans
Larsen, F. J., Schiffer, T. A., Borniquel, S., Sahlin, K., Ekblom, B., Lundberg, J. O., & Weitzberg, E. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.01.004 · Cited by 689 · see citing works
The ADP and ATP transport in mitochondria and its carrier
Klingenberg, M. (2008) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2008.04.011 · Cited by 613 · see citing works
Bioenergetics and the formation of mitochondrial reactive oxygen species
Ádám‐Vizi, V., & Chinopoulos, C. (2006) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2006.10.005 · Cited by 613 · see citing works
Increased Adipocyte O2 Consumption Triggers HIF-1α, Causing Inflammation and Insulin Resistance in Obesity
Lee, Y. S., Kim, J.-W., Osborne, O., Oh, D. Y., Sasik, R., Schenk, S., Chen, A., Chung, H., Murphy, A., Watkins, S. M., et al. (2014) · Cell · doi:10.1016/j.cell.2014.05.012 · Cited by 598 · see citing works
Mitochondrial Energetics in the Heart in Obesity-Related Diabetes
Boudina, S., Sena, S., Theobald, H., Sheng, X., Wright, J. J., Hu, X. X., Aziz, S., Johnson, J. I., Bugger, H., Zaha, V. G., et al. (2007) · Diabetes · doi:10.2337/db07-0481 · Cited by 586 · see citing works
Mitochondrial uncoupling, ROS generation and cardioprotection
Cadenas, S. (2018) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2018.05.019 · Cited by 591 · see citing works
Somatic Mitochondrial DNA Mutations in Mammalian Aging
Larsson, N. (2010) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060408-093701 · Cited by 543 · see citing works
Analysis and Interpretation of Microplate-Based Oxygen Consumption and pH Data
Divakaruni, A. S., Paradyse, A. R., Ferrick, D. A., Murphy, A. N., & Jastroch, M. (2014) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/b978-0-12-801415-8.00016-3 · Cited by 525 · see citing works
The Regulation and Physiology of Mitochondrial Proton Leak
Divakaruni, A. S., & Brand, M. D. (2011) · Physiology · doi:10.1152/physiol.00046.2010 · Cited by 484 · see citing works
Mitochondrial Uncoupling: A Key Controller of Biological Processes in Physiology and Diseases
Demine, S., Renard, P., & Arnould, T. (2019) · Cells · doi:10.3390/cells8080795 · Cited by 476 · see citing works
“Underlining their importance, ANTs can account for up to 50% of basal mitochondrial membrane proton conductance [25].”
Background
PGC-1α-mediated regulation of mitochondrial function and physiological implications
Halling, J. F., & Pilegaard, H. (2020) · Applied Physiology, Nutrition, and Metabolism · doi:10.1139/apnm-2020-0005 · Cited by 418 · see citing works
The efficiency and plasticity of mitochondrial energy transduction.
Brand, M. D. (2005) · Biochemical Society Transactions · doi:10.1042/bst0330897 · Cited by 406 · see citing works
Self-citation
Mitochondrial Metabolism in Aging Heart
Lesnefsky, E. J., Chen, Q., & Hoppel, C. L. (2016) · Circulation Research · doi:10.1161/circresaha.116.307505 · Cited by 350 · 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
Electron Transport Chain-dependent and -independent Mechanisms of Mitochondrial H2O2 Emission during Long-chain Fatty Acid Oxidation
Seifert, E. L., Estey, C., Xuan, J. Y., & Harper, M. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.026203 · Cited by 278 · see citing works
Temperature, metabolic power and the evolution of endothermy
Clarke, A., & Pörtner, H. (2010) · Biological reviews/Biological reviews of the Cambridge Philosophical Society · doi:10.1111/j.1469-185x.2010.00122.x · Cited by 271 · see citing works
Creatine metabolism: energy homeostasis, immunity and cancer biology
Kazak, L., & Cohen, P. (2020) · Nature Reviews Endocrinology · doi:10.1038/s41574-020-0365-5 · Cited by 260 · see citing works
Mitochondria in the diabetic heart
Bugger, H., & Abel, E. D. (2010) · Cardiovascular Research · doi:10.1093/cvr/cvq239 · Cited by 261 · see citing works
The Secreted Enzyme PM20D1 Regulates Lipidated Amino Acid Uncouplers of Mitochondria
Long, J. Z., Svensson, K. J., Bateman, L. A., Lin, H., Kamenecka, T., Lokurkar, I. A., Lou, J., Rao, R. R., Chang, M. R., Jedrychowski, M. P., et al. (2016) · Cell · doi:10.1016/j.cell.2016.05.071 · Cited by 257 · see citing works
H+ transport is an integral function of the mitochondrial ADP/ATP carrier
Bertholet, A. M., Chouchani, E. T., Kazak, L., Angelin, A., Fedorenko, A., Long, J. Z., Vidoni, S., Garrity, R., Cho, J., Terada, N., et al. (2019) · Nature · doi:10.1038/s41586-019-1400-3 · Cited by 256 · see citing works
Bioenergetics in environmental adaptation and stress tolerance of aquatic ectotherms: linking physiology and ecology in a multi-stressor landscape
Sokolova, I. M. (2021) · Journal of Experimental Biology · doi:10.1242/jeb.236802 · Cited by 240 · 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
The energetic brain—A review from students to students
Bordone, M. P., Salman, M. M., Titus, H. E., Amini, E., Andersen, J. V., Chakraborti, B., Diuba, A. V., Dubouskaya, T. G., Ehrke, E., Espindola de Freitas, A., et al. (2019) · Journal of Neurochemistry · doi:10.1111/jnc.14829 · Cited by 205 · see citing works
Mitochondrial Uncoupling: A Key Contributor to Reduced Cardiac Efficiency in Diabetes
Boudina, S., & Abel, E. D. (2006) · Physiology · doi:10.1152/physiol.00008.2006 · Cited by 199 · see citing works
Molecular mechanisms for myocardial mitochondrial dysfunction in the metabolic syndrome
Bugger, H., & Abel, E. D. (2008) · Clinical Science · doi:10.1042/cs20070166 · Cited by 195 · see citing works
Thyroid Hormone Effects on Mitochondrial Energetics
Harper, M.-E., & Seifert, E. L. (2008) · Thyroid · doi:10.1089/thy.2007.0250 · Cited by 194 · see citing works
A high fat diet increases mitochondrial fatty acid oxidation and uncoupling to decrease efficiency in rat heart
Cole, M. A., Murray, A. J., Cochlin, L. E., Heather, L. C., McAleese, S., Knight, N. S., Sutton, E. R., Jamil, A. H. A., Parassol, N., & Clarke, K. (2011) · Basic Research in Cardiology · doi:10.1007/s00395-011-0156-1 · Cited by 190 · see citing works
Cardiolipin and mitochondrial carriers
Klingenberg, M. (2009) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2009.06.007 · Cited by 182 · see citing works
Adenine nucleotide translocase 2 is a key mitochondrial protein in cancer metabolism
Chevrollier, A., Loiseau, D., Reynier, P., & Stepien, G. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.10.008 · Cited by 182 · see citing works
Use the Protonmotive Force: Mitochondrial Uncoupling and Reactive Oxygen Species
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
Low-Dose Sorafenib Acts as a Mitochondrial Uncoupler and Ameliorates Nonalcoholic Steatohepatitis
Jian, C., Fu, J., Cheng, X., Shen, L., Ji, Y., Wang, X., Pan, S., Tian, H., Tian, S., Liao, R., et al. (2020) · Cell Metabolism · doi:10.1016/j.cmet.2020.04.011 · Cited by 172 · see citing works
Mitochondrial Proton Leak Plays a Critical Role in Pathogenesis of Cardiovascular Diseases
Cheng, J., Nanayakkara, G., Shao, Y., Cueto, R., Wang, L., Yang, W. Y., Tian, Y., Wang, H., & Yang, X. (2017) · Advances in Experimental Medicine and Biology · doi:10.1007/978-3-319-55330-6_20 · Cited by 168 · see citing works
Brown and Beige Adipose Tissues in Health and Disease
Rui, L. (2017) · Comprehensive physiology · doi:10.1002/cphy.c170001 · Cited by 177 · see citing works
A carbon monoxide-releasing molecule (CORM-3) uncouples mitochondrial respiration and modulates the production of reactive oxygen species
Iacono, L. L., Boczkowski, J., Zini, R., Salouage, I., Berdeaux, A., Motterlini, R., & Morin, D. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.02.033 · Cited by 160 · see citing works
Pathogenic VCP Mutations Induce Mitochondrial Uncoupling and Reduced ATP Levels
Bartolome, F., Wu, H.-C., Burchell, V. S., Preza, E., Wray, S., Mahoney, C. J., Fox, N. C., Calvo, A., Canosa, A., Moglia, C., et al. (2013) · Neuron · doi:10.1016/j.neuron.2013.02.028 · Cited by 156 · see citing works
“This ADP/ATP translocase is responsible for the transport of adenine nucleotides across the mitochondrial inner membrane, but it is also thought to have an intrinsic uncoupling property (Brand et al., 2005).”
Background
Generation of mature compact ventricular cardiomyocytes from human pluripotent stem cells
Funakoshi, S., Fernandes, I. M., Mastikhina, O., Wilkinson, D., Tran, T. N., Dhahri, W., Mazine, A., Yang, D., Burnett, B. J., Lee, J., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-23329-z · Cited by 155 · see citing works
UCP1-independent thermogenesis
Roesler, A. A., & Kazak, L. (2020) · Biochemical Journal · doi:10.1042/bcj20190463 · Cited by 153 · see citing works
Mitochondrial membrane lipids in the regulation of bioenergetic flux
Decker, S. T., & Funai, K. (2024) · Cell Metabolism · doi:10.1016/j.cmet.2024.07.024 · Cited by 152 · see citing works
Cellular energetic metabolism in sepsis: The need for a systems approach
Carré, J. E., & Singer, M. (2008) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2008.04.024 · Cited by 147 · see citing works
The regulation and turnover of mitochondrial uncoupling proteins
Azzu, V., Jastroch, M., Divakaruni, A. S., & Brand, M. D. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.02.035 · Cited by 146 · see citing works
Coevolution of body size and metabolic rate in vertebrates: a life‐history perspective
Kozłowski, J., Konarzewski, M., & Czarnołęski, M. (2020) · Biological reviews/Biological reviews of the Cambridge Philosophical Society · doi:10.1111/brv.12615 · Cited by 143 · 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
Beyond appetite regulation: Targeting energy expenditure, fat oxidation, and lean mass preservation for sustainable weight loss
Christoffersen, B. Ø., Sanchez‐Delgado, G., John, L. M., Ryan, D. H., Raun, K., & Ravussin, E. (2022) · Obesity · doi:10.1002/oby.23374 · Cited by 142 · see citing works
“The mitochondrial proton leak consists of a basal component associated with the adenine nucleotide translocases (primarily ANT1 in muscles and ANT2 in other tissues) and uncoupling protein 1 (UCP1) in BAT, and an inducible part mediated by activation of ANT, UCP1, UCP2, and UCP3, with UCP3 being the most abundant UCP…”
Background
Physiological and pathological roles of mitochondrial SLC25 carriers
Gutiérrez‐Aguilar, M., & Baines, C. P. (2013) · Biochemical Journal · doi:10.1042/bj20121753 · Cited by 140 · see citing works
Uncoupling protein‐3: clues in an ongoing mitochondrial mystery
Bézaire, V., Seifert, E. L., & Harper, M. (2007) · The FASEB Journal · doi:10.1096/fj.06-6966rev · Cited by 140 · see citing works
A Conserved Role for Phosphatidylinositol 3-Kinase but Not Akt Signaling in Mitochondrial Adaptations that Accompany Physiological Cardiac Hypertrophy
O'Neill, B. T., Kim, J., Wende, A. R., Theobald, H. A., Tuinei, J., Buchanan, J., Guo, A., Zaha, V. G., Davis, D. K., Schell, J. C., et al. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.09.001 · Cited by 137 · see citing works
Uncoupling protein-3 lowers reactive oxygen species production in isolated mitochondria
Toime, L. J., & Brand, M. D. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.05.010 · Cited by 135 · see citing works
Mitochondrial proton leaks and uncoupling proteins
Nicholls, D. G. (2021) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2021.148428 · Cited by 133 · see citing works
Plasticity of Oxidative Metabolism in Variable Climates: Molecular Mechanisms
Seebacher, F., Brand, M. D., Else, P. L., Guderley, H., Hulbert, A. J., & Moyes, C. D. (2010) · Physiological and Biochemical Zoology · doi:10.1086/649964 · Cited by 133 · see citing works
Mitochondrial oxidative metabolism and uncoupling proteins in the failing heart
Akhmedov, A. T., Rybin, V. O., & Marı́n-Garcı́a, J. (2014) · Heart Failure Reviews · doi:10.1007/s10741-014-9457-4 · Cited by 125 · see citing works
UCPs, at the interface between bioenergetics and metabolism
Bouillaud, F., Alves‐Guerra, M., & Ricquier, D. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2016.04.013 · Cited by 125 · see citing works
Exploring the therapeutic potential of mitochondrial uncouplers in cancer
Shrestha, R., Johnson, E., & Byrne, F. L. (2021) · Molecular Metabolism · doi:10.1016/j.molmet.2021.101222 · Cited by 125 · see citing works
A Novel High-Throughput Assay for Islet Respiration Reveals Uncoupling of Rodent and Human Islets
Wikström, J. D., Sereda, S. B., Stiles, L., Elorza, Á. A., Allister, E. M., Neilson, A., Ferrick, D. A., Wheeler, M. B., & Shirihai, O. S. (2012) · PLoS ONE · doi:10.1371/journal.pone.0033023 · Cited by 123 · see citing works
Different mechanisms of mitochondrial proton leak in ischaemia/reperfusion injury and preconditioning: implications for pathology and cardioprotection
Nadtochiy, S. M., Tompkins, A. J., & Brookes, P. S. (2006) · Biochemical Journal · doi:10.1042/bj20051927 · Cited by 123 · see citing works
The efficiency of cellular energy transduction and its implications for obesity
Harper, M.-E., Green, K., & Brand, M. D. (2008) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.28.061807.155357 · Cited by 121 · see citing works
Increased substrate oxidation and mitochondrial uncoupling in skeletal muscle of endurance-trained individuals
Befroy, D. E., Petersen, K. F., Dufour, S., Mason, G. F., Rothman, D. L., & Shulman, G. I. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0808889105 · Cited by 120 · see citing works
Beetroot juice supplementation reduces whole body oxygen consumption but does not improve indices of mitochondrial efficiency in human skeletal muscle
Whitfield, J., Ludzki, A., Heigenhauser, G. J. F., Senden, J. M. G., Verdijk, L. B., van Loon, L. J. C., Spriet, L. L., & Holloway, G. P. (2016) · The Journal of Physiology · doi:10.1113/jp270844 · Cited by 115 · see citing works
Mitochondrial Dysfunction in the Pathogenesis of Rett Syndrome: Implications for Mitochondria-Targeted Therapies
Shulyakova, N., Andreazza, A. C., Mills, L. R., & Eubanks, J. H. (2017) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2017.00058 · Cited by 115 · see citing works
Low Doses of Insulin-Like Growth Factor-I Induce Mitochondrial Protection in Aging Rats
Puche, J. E., Garcia‐Fernandez, M. I., Muntané, J., Rioja, J., González-Barón, S., & Castilla‐Cortázar, I. (2008) · Endocrinology · doi:10.1210/en.2007-1563 · Cited by 112 · see citing works
Mitochondrial metabolism in hibernation and daily torpor: a review
Staples, J. F., & Brown, J. C. L. (2008) · Journal of Comparative Physiology B · doi:10.1007/s00360-008-0282-8 · Cited by 111 · see citing works
Reduction of elevated proton leak rejuvenates mitochondria in the aged cardiomyocyte
Zhang, H., Alder, N. N., Wang, W., Szeto, H. H., Marcinek, D. J., & Rabinovitch, P. S. (2020) · eLife · doi:10.7554/elife.60827 · Cited by 102 · see citing works
Endothermy in birds: underlying molecular mechanisms
Walter, I. J., & Seebacher, F. (2009) · Journal of Experimental Biology · doi:10.1242/jeb.029009 · Cited by 101 · 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
The Pancreatic β-Cell: A Bioenergetic Perspective
Nicholls, D. G. (2016) · Physiological Reviews · doi:10.1152/physrev.00009.2016 · Cited by 95 · see citing works
Proton leak regulates mitochondrial reactive oxygen species generation in endothelial cell activation and inflammation - A novel concept
Nanayakkara, G., Wang, H., & Yang, X. (2018) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2018.12.002 · Cited by 95 · see citing works
Insights into Membrane Protein–Lipid Interactions from Free Energy Calculations
Corey, R. A., Vickery, O. N., Sansom, M. S. P., & Stansfeld, P. J. (2019) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.9b00548 · Cited by 94 · see citing works
Uncoupling protein-1 is not leaky
Shabalina, I. G., Ost, M., Petrovič, N., Vrbacký, M., Nedergaard, J., & Cannon, B. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.04.007 · Cited by 94 · see citing works
Dietary nitrate reduces resting metabolic rate: A randomized, crossover study in humans
Larsen, F. J., Schiffer, T. A., Ekblom, B., Mattsson, M. P., Checa, A., Wheelock, C. E., Nyström, T., Lundberg, J. O., & Weitzberg, E. (2014) · The American Journal of Clinical Nutrition · doi:10.3945/ajcn.113.079491 · Cited by 92 · see citing works
Mitochondria-Centric Review of Polyphenol Bioactivity in Cancer Models
Stevens, J. F., Revel, J. S., & Maier, C. S. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7404 · Cited by 92 · see citing works
Mitochondrial H + Leak and Thermogenesis
Bertholet, A. M., & Kirichok, Y. (2021) · Annual Review of Physiology · doi:10.1146/annurev-physiol-021119-034405 · Cited by 92 · see citing works
Carboxyatractyloside effects on brown-fat mitochondria imply that the adenine nucleotide translocator isoforms ANT1 and ANT2 may be responsible for basal and fatty-acid-induced uncoupling respectively
Shabalina, I. G., Kramarova, T. V., Nedergaard, J., & Cannon, B. (2006) · Biochemical Journal · doi:10.1042/bj20060706 · Cited by 92 · see citing works
Uncoupling Protein 1 Decreases Superoxide Production in Brown Adipose Tissue Mitochondria
Oelkrug, R., Kutschke, M., Meyer, C. W., Heldmaier, G., & Jastroch, M. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.122861 · Cited by 92 · see citing works
Reduced cytosolic protein synthesis suppresses mitochondrial degeneration
Wang, X., Zuo, X., Kucejová, B., & Chen, X. J. (2008) · Nature Cell Biology · doi:10.1038/ncb1769 · Cited by 92 · see citing works
Enhanced Cardiac Akt/Protein Kinase B Signaling Contributes to Pathological Cardiac Hypertrophy in Part by Impairing Mitochondrial Function via Transcriptional Repression of Mitochondrion-Targeted Nuclear Genes
Wende, A. R., O'Neill, B. T., Bugger, H., Riehle, C., Tuinei, J., Buchanan, J., Tsushima, K., Wang, L., Caro, P., Guo, A., et al. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.01109-14 · Cited by 91 · see citing works
Direct real-time quantification of mitochondrial oxidative phosphorylation efficiency in permeabilized skeletal muscle myofibers
Lark, D. S., Torres, M. J., Lin, C., RYAN, T. E., Anderson, E. J., & Neufer, P. D. (2016) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00124.2016 · Cited by 89 · see citing works
Ectotherm mitochondrial economy and responses to global warming
Sokolova, I. M. (2023) · Acta Physiologica · doi:10.1111/apha.13950 · Cited by 87 · see citing works
Uncoupling protein-2 contributes significantly to high mitochondrial proton leak in INS-1E insulinoma cells and attenuates glucose-stimulated insulin secretion
Affourtit, C., & Brand, M. D. (2008) · Biochemical Journal · doi:10.1042/bj20070954 · Cited by 85 · see citing works
A Metabolomics-driven Elucidation of the Anti-obesity Mechanisms of Xanthohumol
Kirkwood, J. S., Legette, L. L., Miranda, C. L., Jiang, Y., & Stevens, J. F. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.445452 · Cited by 85 · see citing works
Adenine Nucleotide Translocase, Mitochondrial Stress, and Degenerative Cell Death
Liu, Y., & Chen, X. J. (2013) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2013/146860 · Cited by 80 · see citing works
PGC-1α regulates mitochondrial properties beyond biogenesis with aging and exercise training
Halling, J. F., Jessen, H., Nøhr-Meldgaard, J., Buch, B. T., Christensen, N. M., Gudiksen, A., Ringholm, S., Neufer, P. D., Prats, C., & Pilegaard, H. (2019) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00059.2019 · Cited by 82 · see citing works
On the role of uncoupling protein-2 in pancreatic beta cells
Affourtit, C., & Brand, M. D. (2008) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2008.03.022 · Cited by 78 · see citing works
Mitochondrial DNA Variation Dictates Expressivity and Progression of Nuclear DNA Mutations Causing Cardiomyopathy
McManus, M. J., Picard, M. A., Chen, H.-W., de Haas, H. J., Potluri, P., Leipzig, J. N., Towheed, A., Angelin, A., Sengupta, P. P., Morrow, R. M., et al. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.08.002 · Cited by 78 · see citing works
Nucleic acid import into mitochondria: New insights into the translocation pathways.
Weber-Lotfi, F., Koulintchenko, M., Ibrahim, N., Hammann, P., Mileshina, D., Konstantinov, Y., & Dietrich, A. (2015) · Biochimica et Biophysica Acta · doi:10.1016/j.bbamcr.2015.09.011 · Cited by 28 · see citing works
Role of the Transmembrane Potential in the Membrane Proton Leak
Rupprecht, A., Sokolenko, E. A., Beck, V., Ninnemann, O., Jabůrek, M., Trimbuch, T., Klishin, S. S., Ježek, P., Skulachev, V. P., & Pohl, E. E. (2010) · Biophysical Journal · doi:10.1016/j.bpj.2009.12.4301 · 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
Stronger control of ATP/ADP by proton leak in pancreatic β-cells than skeletal muscle mitochondria
Affourtit, C., & Brand, M. D. (2006) · Biochemical Journal · doi:10.1042/bj20051280 · Cited by 71 · see citing works
Self-citation
The still uncertain identity of the channel-forming unit(s) of the mitochondrial permeability transition pore
Baines, C. P., & Gutiérrez‐Aguilar, M. (2018) · Cell Calcium · doi:10.1016/j.ceca.2018.05.003 · Cited by 70 · see citing works
Thyroid Hormone Mediated Modulation of Energy Expenditure
Vaitkus, J. A., Farrar, J. S., & Celi, F. S. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms160716158 · Cited by 71 · see citing works
Why cancer cells have a more hyperpolarised mitochondrial membrane potential and emergent prospects for therapyPreprint
Forrest, M. (2015) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/025197 · Cited by 71 · see citing works
Nitric oxide regulation of cellular metabolism: Adaptive tuning of cellular energy
Pappas, G., Wilkinson, M. L., & Gow, A. J. (2022) · Nitric Oxide · doi:10.1016/j.niox.2022.11.006 · Cited by 71 · see citing works
High‐intensity exercise training enhances mitochondrial oxidative phosphorylation efficiency in a temperature‐dependent manner in human skeletal muscle: implications for exercise performance
Fiorenza, M., Lemminger, A. K., Marker, M., Eibye, K., Iaia, F. M., Bangsbo, J., & Hostrup, M. (2019) · The FASEB Journal · doi:10.1096/fj.201900106rrr · Cited by 69 · see citing works
Peroxisome Proliferator-Activated Receptor-γ Coactivator 1-α Overexpression Prevents Endothelial Apoptosis by Increasing ATP/ADP Translocase Activity
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
The effects of fasting and cold exposure on metabolic rate and mitochondrial proton leak in liver and skeletal muscle of an amphibian, the cane toad Bufo marinus
Trzcionka, M., Withers, K., Klingenspor, M., & Jastroch, M. (2008) · Journal of Experimental Biology · doi:10.1242/jeb.016519 · Cited by 68 · see citing works
Hyperglycemia Alters the Schwann Cell Mitochondrial Proteome and Decreases Coupled Respiration in the Absence of Superoxide Production
Zhang, L., Yu, C. R., Vasquez, F. E., Galeva, N., Onyango, I. G., Swerdlow, R. H., & Dobrowsky, R. T. (2009) · Journal of Proteome Research · doi:10.1021/pr900818g · Cited by 67 · 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
Uncoupling protein-1 (UCP1) contributes to the basal proton conductance of brown adipose tissue mitochondria
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

Uncoupling protein-1 (UCP1) contributes to the basal proton conductance of brown adipose tissue mitochondria
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
Interaction of adenine nucleotides with the adenine nucleotide translocase regulates the developmental changes in proton conductance of the inner mitochondrial membrane
Valcarce, C., & Vuezva, J. (1991) · FEBS Letters · doi:10.1016/0014-5793(91)81435-b · Cited by 30 · see citing works
S3.25 Complementation of Bacillus subtilis motility with flagellin gene from thermophilic Bacillus sp. PS3
Hayakawa, J., & Ishizuka, M. (2008) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2008.05.124
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
Contribution of mitochondrial carrier proteins to basal proton conductance
Parker, N., & Brand, M. (2008) · UCL Discovery (University College London)

Authors: Brand, M. D., Pakay, J. L., Ocloo, A., Kokoszka, J., Wallace, D. C., Brookes, P. S., & Cornwall, E. J.
Affiliations: MRC Mitochondrial Biology Unit (GB)
Emory University (US)
Department of Molecular and Cellular Pathology, University of Birmingham, Birmingham, AL 35294, U.S.A.
Corresponding author: Ocloo, Augustine
ORCID: Brand, Martin D.
Ocloo, Augustine
Wallace, Douglas C.
Brookes, Paul S.
Venue: Biochemical Journal
Publisher: Portland Press Ltd.
Published: 2005-11-22
Volume: 392
Issue: 2
Pages: 353-362
ISSN: 0264-6021 (ISSN-L)
1470-8728
DOI: 10.1042/bj20050890
PMC: PMC1316271
OpenAlex: W1996324277
Cited by: 410
References: 52
Citations by year: 2026: 6 · 2025: 20 · 2024: 13 · 2023: 23 · 2022: 25 · 2021: 20 · 2020: 25 · 2019: 17 · 2018: 13 · 2017: 19 · 2016: 14 · 2015: 18 · 2014: 23 · 2013: 21 · 2012: 23
FWCI: 6.60
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Biochemical Journal (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: Cambridge Commonwealth Trust
National Institutes of Health
Medical Research Council
National Institute of Neurological Disorders and Stroke (NS 41850, R01NS041850)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
Keywords: adenine nucleotide translocase, adenine nucleotide carrier, mitochondrial uncoupling, muscle mitochondria, B gene, carboxyatractylate, ADP/ATP exchange, metabolic rate
MeSH terms: Mitochondrial ADP, ATP Translocases, Animals, Cattle, Drosophila melanogaster, Female, Horses, Male, Membrane Potentials, Mitochondria, Phospholipids, Protein Binding, Protons, Rabbits, Swine, Gene Expression Regulation, Enzymologic, Mice, Knockout, Cell Respiration, Drosophila Proteins, Mice, 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

The basal proton conductance of mitochondria depends on adenine nucleotide translocase content

Abstract

Integrity signals

Claims the paper makes

Claims other papers make about this one

Self-check

Cites

Cited by

Related

Record

About these checks