Mitochondrial functional state in clonal pancreatic β-cells exposed to free fatty acids.

The mitochondrial generation of hydrogen peroxide. General properties and effect of hyperbaric oxygen

Boveris, A., & Chance, B. (1973) · Biochemical Journal · doi:10.1042/bj1340707 · Cited by 2,626 · see citing works

[7] Mitochondrial respiratory control and the polarographic measurement of ADP : O ratios

Estabrook, R. W. (1967) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(67)10010-4 · Cited by 1,782 · see citing works

Banting Lecture 2001

McGarry, J. D. (2002) · Diabetes · doi:10.2337/diabetes.51.1.7 · Cited by 1,435 · 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

Generation of reactive oxygen species by the mitochondrial electron transport chain

Liu, Y., Fiskum, G., & Schubert, D. (2002) · Journal of Neurochemistry · doi:10.1046/j.0022-3042.2002.00744.x · Cited by 1,260 · see citing works

Antioxidant Therapy: A New Pharmacological Approach in Shock, Inflammation, and Ischemia/Reperfusion Injury

Cuzzocrea, S., Riley, D. P., Caputi, A. P., & Salvemini, D. (2001) · Pharmacological Reviews · doi:10.1016/s0031-6997(24)01484-4 · Cited by 1,087 · 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

Fatty acid import into mitochondria

Kerner, J., & Hoppel, C. L. (2000) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/s1388-1981(00)00044-5 · Cited by 805 · see citing works

Complex I-mediated reactive oxygen species generation: modulation by cytochrome c and NAD(P)+ oxidation–reduction state

Kushnareva, Y., Murphy, A. N., & Andreyev, A. Y. (2002) · Biochemical Journal · doi:10.1042/bj20021121 · Cited by 677 · see citing works

Leptin Induces Mitochondrial Superoxide Production and Monocyte Chemoattractant Protein-1 Expression in Aortic Endothelial Cells by Increasing Fatty Acid Oxidation via Protein Kinase A

Yamagishi, S., Edelstein, D., Du, X.-L., Kaneda, Y., Guzmán, M., & Brownlee, M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m007383200 · Cited by 620 · see citing works

Prolonged Exposure to Free Fatty Acids Has Cytostatic and Pro-Apoptotic Effects on Human Pancreatic Islets

Lupi, R., Dotta, F., Marselli, L., Guerra, S. D., Masini, M., Santangelo, C., Patanè, G., Boggi, U., Piro, S., Anello, M., et al. (2002) · Diabetes · doi:10.2337/diabetes.51.5.1437 · Cited by 595 · see citing works

Superoxide Activates Mitochondrial Uncoupling Protein 2 from the Matrix Side

Echtay, K. S., Murphy, M. P., Smith, R. A. J., Talbot, D. A., & Brand, M. D. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m208262200 · Cited by 388 · see citing works

Pancreatic beta cell line MIN6 exhibits characteristics of glucose metabolism and glucose-stimulated insulin secretion similar to those of normal islets

Ishihara, H., Asano, T., Tsukuda, K., Katagiri, H., Inukai, K., Anai, M., Kikuchi, M., Yazaki, Y., Miyazaki, J.-I., & Oka, Y. (1993) · Diabetologia · doi:10.1007/bf00401058 · Cited by 385 · see citing works

Permeabilized cell and skinned fiber techniques in studies of mitochondrial function in vivo

Saks, V. A., Veksler, V., Kuznetsov, A. V., Kay, L., Sikk, P., Tiivel, T., Tranqui, L., Olivares, J., Winkler, K., Wiedemann, F. R., et al. (1998) · Springer eBooks · doi:10.1007/978-1-4615-5653-4_7 · Cited by 361 · see citing works

Increased Uncoupling Protein-2 Levels in β-cells Are Associated With Impaired Glucose-Stimulated Insulin Secretion

Chan, C. B., De Leo, D., Joseph, J. W., McQuaid, T. S., Ha, X. F., Xu, F., Tsushima, R. G., Pennefather, P. S., Salapatek, A. M. F., & Wheeler, M. B. (2001) · Diabetes · doi:10.2337/diabetes.50.6.1302 · Cited by 341 · see citing works

Physiological Role of UCP3 May Be Export of Fatty Acids from Mitochondria When Fatty Acid Oxidation Predominates: An Hypothesis

Himms‐Hagen, J., & Harper, M. (2001) · Experimental Biology and Medicine · doi:10.1177/153537020122600204 · Cited by 325 · see citing works

Permeabilized cell and skinned fiber techniques in studies of mitochondrial function in vitro

Veksler, V., Kuznetsov, A. V., Kay, L., Sikk, P., Tiivel, T., Tranqui, L., Olivares, J., Winkler, K., Wiedemann, F. R., & Kunz, W. S. (1998) · Molecular and Cellular Biochemistry · doi:10.1023/a:1006834912257 · Cited by 308 · see citing works

Ceramide Interaction with the Respiratory Chain of Heart Mitochondria

Di Paola, M., Cocco, T., & Lorusso, M. (2000) · Biochemistry · doi:10.1021/bi9924415 · Cited by 262 · see citing works

Sodium Palmitate Induces Partial Mitochondrial Uncoupling and Reactive Oxygen Species in Rat Pancreatic Isletsin Vitro1

Carlsson, C., Borg, L., & Welsh, N. (1999) · Endocrinology · doi:10.1210/endo.140.8.6908 · Cited by 238 · see citing works

Substrate and Site Specificity of Hydrogen Peroxide Generation in Mouse Mitochondria

Kwong, L. K., & Sohal, R. S. (1998) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1997.0489 · Cited by 236 · see citing works

Arachidonic acid interaction with the mitochondrial electron transport chain promotes reactive oxygen species generation

Cocco, T., Di, M., Papa, P., & Lorusso, M. P. (1999) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00034-9 · Cited by 228 · 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

Uncoupling Protein 2: A Possible Link Between Fatty Acid Excess and Impaired Glucose-Induced Insulin Secretion?

Davis‐Lameloise, N., Muzzin, P., Prentki, M., & Assimacopoulos‐Jeannet, F. (2001) · Diabetes · doi:10.2337/diabetes.50.4.803 · Cited by 226 · see citing works

Uncoupling Protein 2 Knockout Mice Have Enhanced Insulin Secretory Capacity After a High-Fat Diet

Joseph, J. W., Koshkin, V., Zhang, C.-Y., Wang, J., Lowell, B. B., Chan, C. B., & Wheeler, M. B. (2002) · Diabetes · doi:10.2337/diabetes.51.11.3211 · Cited by 220 · 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

High content of mitochondrial glycerol-3-phosphate dehydrogenase in pancreatic islets and its inhibition by diazoxide.

MacDonald, M. J. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)68840-x · Cited by 191 · see citing works

Digitonin permeabilization does not affect mitochondrial function and allows the determination of the mitochondrial membrane potential of Trypanosoma cruzi in situ

Vercesi, A. E., Bernardes, C. F., Hoffmann, M. E., Gadelha, F. R., & Docampo, R. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)98703-x · Cited by 188 · see citing works

Expression Profiling of Palmitate- and Oleate-Regulated Genes Provides Novel Insights Into the Effects of Chronic Lipid Exposure on Pancreatic β-Cell Function

Busch, A. K., Cordery, D. V., Denyer, G. S., & Biden, T. J. (2002) · Diabetes · doi:10.2337/diabetes.51.4.977 · Cited by 184 · see citing works

Fatty acids as natural uncouplers preventing generation of O⋅−2 and H2O2 by mitochondria in the resting state

Korshunov, S., Korkina, O. V., Ruuge, E. K., Skulachev, V. P., & Starkov, A. A. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)01073-4 · Cited by 180 · see citing works

A significant portion of mitochondrial proton leak in intact thymocytes depends on expression of UCP2

Krauss, S., Zhang, C., & Lowell, B. B. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.012410699 · Cited by 173 · see citing works

Activation of the potato plant uncoupling mitochondrial protein inhibits reactive oxygen species generation by the respiratory chain

Kowaltowski, A. J., Costa, A. D. T., & Vercesi, A. E. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)00231-2 · Cited by 156 · see citing works

Substrate-dependent changes in mitochondrial function, intracellular free calcium concentration and membrane channels in pancreatic β-cells

Duchen, M. R., Smith, P. A., & Ashcroft, F. M. (1993) · Biochemical Journal · doi:10.1042/bj2940035 · Cited by 150 · see citing works

Mitochondrial DNA Is Required for Regulation of Glucose-stimulated Insulin Secretion in a Mouse Pancreatic Beta Cell Line, MIN6

Soejima, A., Inoue, K., Takai, D., Kaneko, M., Ishihara, H., Oka, Y., & Hayashi, J. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.42.26194 · Cited by 149 · see citing works

Uncoupling Protein-2 Participates in Cellular Defense against Oxidative Stress in Clonal β-Cells

Li, L., Skorpen, F., Egeberg, K. W., Jørgensen, I. H., & Grill, V. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.4577 · Cited by 140 · see citing works

Insulin secretion and differential gene expression in glucose-responsive and -unresponsive MIN6 sublines

Minami, K., Yano, H., Miki, T., Nagashima, K., Wang, C., Tanaka, H., Miyazaki, J., & Seino, S. (2000) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.2000.279.4.e773 · Cited by 133 · see citing works

Spectrofluorometric analysis of hydrogen peroxide

Black, M. J., & Brandt, R. B. (1974) · Analytical Biochemistry · doi:10.1016/0003-2697(74)90464-3 · Cited by 130 · see citing works

Supplementation of N‐acetylcysteine inhibits NFκB activation and protects against alloxan‐induced diabetes in CD‐1 mice

Ho, E., Chen, G., & Bray, T. Μ. (1999) · The FASEB Journal · doi:10.1096/fasebj.13.13.1845 · Cited by 128 · see citing works

Effects of Genetic Background on Thermoregulation and Fatty Acid-induced Uncoupling of Mitochondria in UCP1-deficient Mice

Hofmann, W. E., Liu, X., Bearden, C. M., Harper, M., & Kozak, L. P. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100466200 · Cited by 126 · see citing works

Regulation of the Uncoupling Protein-2 Gene in INS-1 β-Cells by Oleic Acid

Medvedev, A. V., Robidoux, J., Bai, X., Cao, W., Floering, L. M., Daniel, K. W., & Collins, S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m208645200 · Cited by 122 · see citing works

Cytokine-induced apoptosis and necrosis are preceded by disruption of the mitochondrial membrane potential (Δψm) in pancreatic RINm5F cells: prevention by Bcl-2

Barbu, A. R., Welsh, N., & Saldeen, J. (2002) · Molecular and Cellular Endocrinology · doi:10.1016/s0303-7207(02)00009-6 · Cited by 121 · see citing works

Mitochondrial Metabolism Sets the Maximal Limit of Fuel-stimulated Insulin Secretion in a Model Pancreatic Beta Cell

Antinozzi, P. A., Ishihara, H., Newgard, C. B., & Wollheim, C. B. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m108462200 · Cited by 115 · see citing works

Probucol preserves pancreatic β-cell function through reduction of oxidative stress in type 2 diabetes

Gorogawa, S.-I., Kajimoto, Y., Umayahara, Y., Kaneto, H., Watada, H., Kuroda, A., Kawamori, D., Yasuda, T., Matsuhisa, M., Yamasaki, Y., et al. (2002) · Diabetes Research and Clinical Practice · doi:10.1016/s0168-8227(02)00005-0 · Cited by 115 · see citing works

Involvement of the Dicarboxylate Carrier in the Protonophoric Action of Long-Chain Fatty Acids in Mitochondria

Wieckowski, M. R., & Wojtczak, L. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.6298 · Cited by 108 · see citing works

Uncoupling protein-2: evidence for its function as a metabolic regulator

Saleh, M. C., Wheeler, M. B., & Chan, C. B. (2002) · Diabetologia · doi:10.1007/s00125-001-0737-x · Cited by 99 · see citing works

Physiological Levels of Mammalian Uncoupling Protein 2 Do Not Uncouple Yeast Mitochondria

Stuart, J. A., Harper, J. A., Brindle, K. M., Jekabsons, M. B., & Brand, M. D. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m011566200 · Cited by 99 · see citing works

On the Relationship between Rate of ATP Synthesis and H+ Electrochemical Gradient in Rat‐Liver Mitochondria

Zoratti, M., Pietrobon, D., & AZZONE, G. F. (1982) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1982.tb06800.x · Cited by 94 · see citing works

Analyzing mitochondrial changes during apoptosis

Gottlieb, R. A. (2002) · Methods · doi:10.1016/s1046-2023(02)00040-3 · Cited by 89 · see citing works

Regulation of pancreatic β-cell mitochondrial metabolism: influence of Ca2+, substrate and ADP

Civelek, V. N., Deeney, J. T., SHALOSKY, N. J., Tornheim, K., Hansford, R. G., Prentki, M., & Corkey, B. E. (1996) · Biochemical Journal · doi:10.1042/bj3180615 · Cited by 85 · see citing works

UCP2-dependent Proton Leak in Isolated Mammalian Mitochondria

Fink, B. D., Hong, Y.-S., Mathahs, M. M., SCHOLZ, T. D., Dillon, J. S., & Sivitz, W. I. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m107955200 · Cited by 74 · see citing works

Apoptosis and Mitochondrial Damage in INS-1 Cells Treated with Alloxan.

Sakurai, K., Katoh, M., SOMENO, K., & FUJIMOTO, Y. (2001) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.24.876 · Cited by 73 · see citing works

Chronic effect of fatty acids on insulin release is not through the alteration of glucose metabolism in a pancreatic beta-cell line (βHC9)

Liang, Y. T., Buettger, C. W., Berner, D. K., & Matschinsky, F. M. (1997) · Diabetologia · doi:10.1007/s001250050783 · Cited by 71 · see citing works

Mitochondrial ATP Synthesis in Permeabilized Cells: Assessment of the ATP/O Valuesin Situ

Ouhabi, R., Boue-Grabot, M., & Mazat, J. (1998) · Analytical Biochemistry · doi:10.1006/abio.1998.2776 · Cited by 70 · see citing works

Cold-induced changes in the energy coupling and the UCP3 level in rodent skeletal muscles

Simonyan, R. A., Jimenez, M., Ceddia, R. B., Giacobino, J., Muzzin, P., & Skulachev, V. P. (2001) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(01)00168-2 · Cited by 55 · see citing works

The role of mild uncoupling and non‐coupled respiration in the regulation of hydrogen peroxide generation by plant mitochondria

Casolo, V., Braidot, E., Chiandussi, E., Macrı̀, F., & Vianello, A. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)01576-3 · Cited by 48 · see citing works

Diabetes, Insulin Secretion, and the Pancreatic Beta-Cell Mitochondrion

Langin, D. (2001) · New England Journal of Medicine · doi:10.1056/nejm200112133452412 · Cited by 46 · see citing works

A threshold membrane potential accounts for controversial effects of fatty acids on mitochondrial oxidative phosphorylation

Köhnke, D., Ludwig, B., & Kadenbach, B. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)81616-8 · Cited by 32 · see citing works

Predominant expression of the mitochondrial dicarboxylate carrier in white adipose tissue

Das, K., Lewis, R. Y., COMBATSIARIS, T. P., Lin, Y. L., Shapiro, L. S., Charron, M. J., & Scherer, P. E. (1999) · Biochemical Journal · doi:10.1042/0264-6021:3440313 · Cited by 32 · see citing works

Predominant expression of the mitochondrial dicarboxylate carrier in white adipose tissue

Das, K., Lewis, R. Y., COMBATSIARIS, T. P., et al. (1999) · Biochemical Journal · doi:10.1042/bj3440313 · Cited by 26 · see citing works

Energetics of Ehrlich ascites mitochondria: Membrane potential of isolated mitochondria and mitochondria within digitonin-permeabilized cells

Bogucka, K., Wroniszewska, A., Bednarek, M., Duszyński, J., & Wojtczak, L. (1990) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(90)90084-h · Cited by 21 · see citing works

Mitochondrial Glycerol-3-Phosphate Dehydrogenase: Cloning of an Alternatively Spliced Human Islet-Cell cDNA, Tissue Distribution, Physical Mapping, and Identification of a Polymorphic Genetic Marker

Ferrer, J. P., Aoki, M., Behn, P., et al. (1996) · Diabetes · doi:10.2337/diab.45.2.262 · Cited by 21 · see citing works

Unique relationships between the rates of oxidation and phosphorylation and the protonmotive force in rat-liver mitochondria

Woelders, H., van der Velden, T., & DAM, K. V. (1988) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(88)90127-2 · Cited by 16 · see citing works

Tissue-specific mitochondrial production of H202: Its dependence on substrates and sensitivity to inhibitors

Kwong, L. K., & Sohal, R. S. (2002) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(02)49349-4 · Cited by 8 · see citing works

Mitochondrial dysfunction and type 2 diabetes

Lowell, B. B., & Shulman, G. I. (2005) · Science · doi:10.1126/science.1104343 · Cited by 2,070 · 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

Physiological functions of the mitochondrial uncoupling proteins UCP2 and UCP3

Brand, M. D., & Esteves, T. C. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.06.002 · Cited by 785 · see citing works

The Role of Oxidative Stress and Hypoxia in Pancreatic Beta-Cell Dysfunction in Diabetes Mellitus

Gerber, P. A., & Rutter, G. A. (2017) · Antioxidants & Redox Signaling · doi:10.1089/ars.2016.6755 · Cited by 654 · see citing works

The role of mitochondria in the pathogenesis of type 2 diabetes

Patti, M.-E., & Corvera, S. (2010) · Endocrine Reviews · doi:10.1210/er.2009-0027 · Cited by 551 · see citing works

An immune origin of type 2 diabetes?

Kolb, H., & Mandrup-Poulsen, T. (2005) · Diabetologia · doi:10.1007/s00125-005-1764-9 · Cited by 394 · see citing works

Superoxide-mediated activation of uncoupling protein 2 causes pancreatic β cell dysfunction

Krauss, S., Zhang, C.-Y., Scorrano, L., Dalgaard, L. T., St-Pierre, J., Grey, S. T., & Lowell, B. B. (2003) · Journal of Clinical Investigation · doi:10.1172/jci200319774 · Cited by 401 · see citing works

Diabetes and apoptosis: lipotoxicity

Kusminski, C. M., Shetty, S., Orci, L., Unger, R. H., & Scherer, P. E. (2009) · Apoptosis · doi:10.1007/s10495-009-0352-8 · Cited by 302 · see citing works

Free Fatty Acid-induced β-Cell Defects Are Dependent on Uncoupling Protein 2 Expression

Joseph, J. W., Koshkin, V., Saleh, M. C., Sivitz, W. I., Zhang, C.-Y., Lowell, B. B., Chan, C. B., & Wheeler, M. B. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409189200 · Cited by 206 · see citing works

The sensitivity of pancreatic β-cells to mitochondrial injuries triggered by lipotoxicity and oxidative stress.

Li, N., Frigerio, F., & Maechler, P. (2008) · Biochemical Society Transactions · doi:10.1042/bst0360930 · Cited by 114 · 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

Uncoupling Proteins: Role in Insulin Resistance and Insulin Insufficiency

B.Chan, C., & Harper, M.-E. (2006) · Current Diabetes Reviews · doi:10.2174/157339906777950660 · Cited by 71 · see citing works

Glutathionylation State of Uncoupling Protein-2 and the Control of Glucose-stimulated Insulin Secretion

Mailloux, R. J., Fu, A., Robson-Doucette, C., Allister, E. M., Wheeler, M. B., Screaton, R., & Harper, M.-E. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.393538 · Cited by 66 · see citing works

Ascorbate reduces superoxide production and improves mitochondrial respiratory chain function in human fibroblasts with electron transport chain deficiencies

Sharma, P., & Morgan, P. D. (2001) · Mitochondrion · doi:10.1016/s1567-7249(01)00016-2 · Cited by 39 · see citing works

[Oxidative phosphorylation uncoupling by fatty acids in liver and muscle mitochondria].

Mokhova, E. N., Starkov, A. A., & Bobyleva, V. A. (1993) · PubMed · Cited by 2 · see citing works

The effect of clidanac, a potent anti-inflammatory drug, on mitochondrial respiration: a consideration on the uncoupling activity of optical enantiomers.

Kawai, K., Shiojiri, H., Fukushima, H., et al. (1984) · PubMed · Cited by 4 · see citing works

[On the reversibility of oxidative phosphorylation. III. Effect of adenosine triphosphate on the respiratory chain in respiratory inhibited mitochondria].

Klingenberg, M., & Schollmeyer, P. J. (1961) · PubMed · Cited by 9 · see citing works

Scopafungin, an inhibitor of oxidative phosphorylation in mitochondria

Reusser, F. (1972) · Biochemical Pharmacology · doi:10.1016/0006-2952(72)90408-x · Cited by 8 · see citing works