Role of mitochondrial dynamics proteins in the pathophysiology of obesity and type 2 diabetes
Abstract
Mitochondrial dysfunction has been reported in skeletal muscle of obese subjects and of type 2 diabetic patients. Reduced mitochondrial mass and defective activity have been proposed to explain this dysfunction. Alterations in mitochondrial function may be crucial to explain the metabolic changes and insulin resistance that characterize both obesity and type 2 diabetes. Consequently, the identification of the primary mechanisms involved is of great relevance. Mitochondrial dynamics refers to the movement of mitochondria along the cytoskeleton and also to the regulation of mitochondrial morphology and distribution, which depend on fusion and fission events. In recent years, some of the proteins that participate in mitochondrial fusion and fission have been identified in mammalian cells. Recent evidence indicates that proteins participating in these processes are also involved in metabolism. The mitochondrial fusion protein mitofusin 2 stimulates respiration, substrate oxidation and the expression of subunits that participate in respiratory complexes in cultured cells. In this regard, skeletal muscle of obese subjects and of type 2 diabetic patients shows reduced mitofusin 2 expression. Therefore, alterations in the activity of the proteins involved in mitochondrial dynamics, and particularly mitofusin 2, may participate in the reduced mitochondrial function present in skeletal muscle in obesity and in type 2 diabetes.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
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?
Mice with skeletal muscle-specific deletion of Mfn2 exhibit impaired mitochondrial morphology, localization, and calcium uptake, ultimately resulting in decreased muscle cross-sectional area and strength.
“Mice with skeletal muscle-specific deletion of Mfn2 exhibit impaired mitochondrial morphology, localization, and calcium uptake, ultimately resulting in decreased muscle cross-sectional area and strength.”
From Mitochondrial Adaptation in Skeletal Muscle: Impact of Obesity, Caloric Restriction, and Dietary Compounds (2024) · cites this paper as [46]
Skeletal muscle exhibits a high abundance of MFN2, and disruption of MFN2 is related to disruption in mitochondrial membrane potential and cellular oxygen consumption.
“Skeletal muscle exhibits a high abundance of MFN2, and disruption of this protein have been related to disruption in mitochondrial membrane potential and cellular oxygen consumption [46].”
From Mitochondrial Adaptation in Skeletal Muscle: Impact of Obesity, Caloric Restriction, and Dietary Compounds (2024) · cites this paper as [46]
Reduced PGC1α expression in obese and diabetic muscle repressed MFN2 level.
“reduced PGC1α expression in obese and diabetic muscle repressed MFN2 level [46], emphasizing the role of PGC1α as regulators of mitochondrial morphology and insulin sensitivity.”
From Mitochondrial Adaptation in Skeletal Muscle: Impact of Obesity, Caloric Restriction, and Dietary Compounds (2024) · cites this paper as [46]
Overexpression of PGC1α enhanced Mfn2 mRNA and protein levels in cultured muscle cells.
“The transcriptional activity of Mfn2 gene was shown to be stimulated by PGC1α, as overexpression of PGC1α enhanced Mfn2 mRNA and protein levels in cultured muscle cells and”
From Mitochondrial Adaptation in Skeletal Muscle: Impact of Obesity, Caloric Restriction, and Dietary Compounds (2024) · cites this paper as [46]
Alterations in mitochondrial dynamics, particularly in Mfn2, are associated with reduced mitochondrial function in skeletal muscle in obesity and T2DM.
“Further, alterations in mitochondrial dynamics and in particular in Mfn2, have been associated with a reduced mitochondrial function in skeletal muscle in obesity and T2DM (Zorzano et al., 2009) and recently aberrant mitochondrial fission has been also associated with insulin resistance in mouse skeletal muscle (Jheng et al., 2012).”
From Mitochondrial Activity and Dynamics Changes Regarding Metabolism in Ageing and Obesity (2017) · cites this paper as Zorzano et al., 2009
Alterations in mitochondrial dynamics and in particular in Mfn2 have been associated with reduced mitochondrial function in skeletal muscle in obesity and T2DM.
“alterations in mitochondrial dynamics and in particular in Mfn2, have been associated with a reduced mitochondrial function in skeletal muscle in obesity and T2DM (Zorzano et al., 2009)”
From Mitochondrial Activity and Dynamics Changes Regarding Metabolism in Ageing and Obesity (2017) · cites this paper as Zorzano et al., 2009
Cites
Mootha, V. K., Lindgren, C. M., Eriksson, K.-F., Subramanian, A., Sihag, S., Lehar, J., Puigserver, P., Carlsson, E., Ridderstråle, M., Laurila, E., et al. (2003) · Nature Genetics · doi:10.1038/ng1180 · Cited by 10,197 · see citing works
A Cold-Inducible Coactivator of Nuclear Receptors Linked to Adaptive Thermogenesis
Puigserver, P., Wu, Z., Park, C. W., Graves, R., Wright, M., & Spiegelman, B. M. (1998) · Cell · doi:10.1016/s0092-8674(00)81410-5 · Cited by 3,864 · see citing works
Premature ageing in mice expressing defective mitochondrial DNA polymerase
Trifunovic, A., Wredenberg, A., Falkenberg, M., Spelbrink, J. N., Rovio, A. T., Bruder, C. E., Bohlooly-Y, M., Gidlöf, S., Oldfors, A., Wibom, R., et al. (2004) · Nature · doi:10.1038/nature02517 · Cited by 2,734 · see citing works
Chen, H., Detmer, S. A., Ewald, A. J., Griffin, E. E., Fraser, S. E., & Chan, D. C. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200211046 · Cited by 2,601 · see citing works
Dysfunction of Mitochondria in Human Skeletal Muscle in Type 2 Diabetes
Kelley, D. E., He, J., Menshikova, E. V., & Ritov, V. B. (2002) · Diabetes · doi:10.2337/diabetes.51.10.2944 · Cited by 2,321 · see citing works
Impaired Mitochondrial Activity in the Insulin-Resistant Offspring of Patients with Type 2 Diabetes
Petersen, K. F., Dufour, S., Befroy, D., Garcia, R., & Shulman, G. I. (2004) · New England Journal of Medicine · doi:10.1056/nejmoa031314 · Cited by 2,193 · see citing works
Mitochondrial DNA mutations, oxidative stress, and apoptosis in mammalian aging
Kujoth, G. C., Hiona, A., Pugh, T. D., Someya, S., Panzer, K., Wohlgemuth, S. E., Hofer, T., Seo, A. Y., Sullivan, R., Jobling, W. A., et al. (2005) · Science · doi:10.1126/science.1112125 · Cited by 2,165 · see citing works
Mitochondrial dysfunction in the elderly: possible role in insulin resistance
Petersen, K. F., Befroy, D., Dufour, S., Dziura, J., Ariyan, C., Rothman, D. L., DiPietro, L., Cline, G. W., & Shulman, G. I. (2003) · Science · doi:10.1126/science.1082889 · Cited by 2,107 · see citing works
Koves, T. R., Ussher, J. R., Noland, R. C., Slentz, D., Mosedale, M., Ilkayeva, O., Bain, J., Stevens, R., Dyck, J. R. B., Newgard, C. B., et al. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2007.10.013 · Cited by 1,990 · see citing works
Patti, M. E., Butte, A. J., Crunkhorn, S., Cusi, K., Berria, R., Kashyap, S., Miyazaki, Y., Kohane, I., Costello, M., Saccone, R., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1032913100 · Cited by 1,952 · see citing works
OPA1 Controls Apoptotic Cristae Remodeling Independently from Mitochondrial Fusion
Frezza, C., Cipolat, S., Martins de Brito, O., Micaroni, M., Beznoussenko, G. V., Rudka, T., Bartoli, D., Polishuck, R. S., Danial, N. N., De Strooper, B., et al. (2006) · Cell · doi:10.1016/j.cell.2006.06.025 · Cited by 1,673 · see citing works
Disruption of Fusion Results in Mitochondrial Heterogeneity and Dysfunction
Chen, H., Chomyn, A., & Chan, D. C. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m503062200 · Cited by 1,376 · see citing works
Defects in Adaptive Energy Metabolism with CNS-Linked Hyperactivity in PGC-1α Null Mice
Lin, J., Wu, P.-H., Tarr, P. T., Lindenberg, K. S., St-Pierre, J., Zhang, C.-Y., Mootha, V. K., Jäger, S., Vianna, C. R., Reznick, R. M., et al. (2004) · Cell · doi:10.1016/j.cell.2004.09.013 · Cited by 1,162 · see citing works
Kelley, D. E., Goodpaster, B., Wing, R. R., & Simoneau, J.-A. (1999) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.1999.277.6.e1130 · Cited by 1,096 · see citing works
Regulation of Muscle Fiber Type and Running Endurance by PPARδ
Wang, Y.-X., Zhang, C.-L., Yu, R. T., Cho, H. K., Nelson, M. C., Bayuga-Ocampo, C. R., Ham, J., Kang, H., & Evans, R. M. (2004) · PLoS Biology · doi:10.1371/journal.pbio.0020294 · Cited by 1,089 · see citing works
Fuel selection in human skeletal muscle in insulin resistance: a reexamination.
Kelley, D. E., & Mandarino, L. J. (2000) · Diabetes · doi:10.2337/diabetes.49.5.677 · Cited by 1,017 · see citing works
Control of mitochondrial morphology by a human mitofusin
Santel, A., & Fuller, M. T. (2001) · Journal of Cell Science · doi:10.1242/jcs.114.5.867 · Cited by 1,012 · see citing works
Leone, T. C., Lehman, J. J., Finck, B. N., Schaeffer, P. J., Wende, A. R., Boudina, S., Courtois, M., Wozniak, D. F., Sambandam, N., Bernal-Mizrachi, C., et al. (2005) · PLoS Biology · doi:10.1371/journal.pbio.0030101 · Cited by 951 · see citing works
Bereiter‐Hahn, J., & Vöth, M. (1994) · Microscopy Research and Technique · doi:10.1002/jemt.1070270303 · Cited by 900 · see citing works
Regulation of mitochondrial morphology through proteolytic cleavage of OPA1
Ishihara, N., Fujita, Y., Oka, T., & Mihara, K. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601184 · Cited by 899 · see citing works
Deficiency of subsarcolemmal mitochondria in obesity and type 2 diabetes
Ritov, V. B., Menshikova, E. V., He, J., Ferrell, R. E., Goodpaster, B. H., & Kelley, D. E. (2005) · Diabetes · doi:10.2337/diabetes.54.1.8 · Cited by 887 · see citing works
Exercise induces transient transcriptional activation of the PGC‐1α gene in human skeletal muscle
Pilegaard, H., Saltin, B., & Neufer, P. D. (2003) · The Journal of Physiology · doi:10.1113/jphysiol.2002.034850 · Cited by 885 · see citing works
Mitofusin-2 Determines Mitochondrial Network Architecture and Mitochondrial Metabolism
Bach, D., Pich, S., Soriano, F. X., Vega, N., Baumgartner, B., Oriola, J., Daugaard, J. R., Lloberas, J., Camps, M., Zierath, J. R., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212754200 · Cited by 832 · see citing works
Self-citationYoon, Y., Krueger, E. W., Oswald, B. J., & McNiven, M. A. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.15.5409-5420.2003 · Cited by 820 · see citing works
Bonnard, C., Durand, A., Peyrol, S., Chanseaume, E., Chauvin, M.-A., Morio, B., Vidal, H., & Rieusset, J. (2008) · Journal of Clinical Investigation · doi:10.1172/jci32601 · Cited by 819 · see citing works
Song, Z., Chen, H., Fiket, M., Alexander, C., & Chan, D. C. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200704110 · Cited by 818 · see citing works
Morino, K. (2005) · Journal of Clinical Investigation · doi:10.1172/jci25151 · Cited by 811 · see citing works
Cipolat, S., Rudka, T., Hartmann, D., Costa, V., Serneels, L., Craessaerts, K., Metzger, K., Frezza, C., Annaert, W. G., D'adamio, L., et al. (2006) · Cell · doi:10.1016/j.cell.2006.06.021 · Cited by 735 · see citing works
A Human Dynamin-related Protein Controls the Distribution of Mitochondria
Смирнова, Е. А., Shurland, D., Ryazantsev, S. N., & van der Bliek, A. M. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.143.2.351 · Cited by 734 · see citing works
Mootha, V. K., Handschin, C., Arlow, D., Xie, X., St. Pierre, J., Sihag, S., Yang, W., Altshuler, D., Puigserver, P., Patterson, N., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0401401101 · Cited by 688 · see citing works
Legros, F., Lombès, A., Frachon, P., & Rojo, M. (2002) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-06-0330 · Cited by 676 · see citing works
hFis1, a Novel Component of the Mammalian Mitochondrial Fission Machinery
James, D. I., Parone, P. A., Mattenberger, Y., & Martinou, J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m303758200 · Cited by 653 · see citing works
Hyperlipidemic Effects of Dietary Saturated Fats Mediated through PGC-1β Coactivation of SREBP
Lin, J. D., Yang, R., Tarr, P. T., Wu, P., Handschin, C., Li, S., Yang, W., Pei, L., Uldry, M., Tontonoz, P., et al. (2005) · Cell · doi:10.1016/j.cell.2004.11.043 · Cited by 618 · see citing works
Mitochondrial respiration is decreased in skeletal muscle of patients with type 2 diabetes
Mogensen, M., Sahlin, K., Fernström, M., Glintborg, D., Vind, B. F., Beck-Nielsen, H., & Højlund, K. (2007) · Diabetes · doi:10.2337/db06-0981 · Cited by 573 · see citing works
Lin, J., Puigserver, P., Donovan, J., Tarr, P., & Spiegelman, B. M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c100631200 · Cited by 552 · see citing works
St‐Pierre, J., Lin, J. D., Krauss, S., Tarr, P. T., Yang, R., Newgard, C. B., & Spiegelman, B. M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301850200 · Cited by 543 · see citing works
Patients with type 2 diabetes have normal mitochondrial function in skeletal muscle
Boushel, R., Gnaiger, E., Schjerling, P., Skovbro, M., Kraunsøe, R., & Dela, F. (2007) · Diabetologia · doi:10.1007/s00125-007-0594-3 · Cited by 519 · see citing works
Wasiak, S., Zunino, R., & McBride, H. M. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200610042 · Cited by 519 · see citing works
Nunnari, J. M., Marshall, W. F., Straight, A. F., Murray, A., Sedat, J. W., & Walter, P. (1997) · Molecular Biology of the Cell · doi:10.1091/mbc.8.7.1233 · Cited by 514 · see citing works
The Machinery of Mitochondrial Inheritance and Behavior
Yaffe, M. P. (1999) · Science · doi:10.1126/science.283.5407.1493 · Cited by 496 · see citing works
Stump, C. S., Short, K. R., Bigelow, M. L., Schimke, J. M., & Nair, K. S. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1332551100 · Cited by 477 · see citing works
Mitochondrial filaments and clusters as intracellular power-transmitting cables
Skulachev, V. P. (2001) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)01735-7 · Cited by 477 · see citing works
Griparić, L., van der Wel, N. N., Orozco, I. J., Peters, P. J., & van der Bliek, A. M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m400920200 · Cited by 468 · see citing works
Mitochondrial Fusion Intermediates Revealed in Vitro
Meeusen, S. L., McCaffery, J., & Nunnari, J. (2004) · Science · doi:10.1126/science.1100612 · Cited by 466 · see citing works
Cusi, K. J., Consoli, A., & DeFronzo, R. A. (1996) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jcem.81.11.8923861 · Cited by 456 · see citing works
Pich, S., Bach, D., Briones, P., Liesa, M., Camps, M., Testar, X., Palacín, M., & Zorzano, A. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi149 · Cited by 455 · see citing works
Self-citationMitofusin-1 protein is a generally expressed mediator of mitochondrial fusion in mammalian cells
Santel, A., Frank, S., Gaume, B. R., Herrler, M., Youle, R. J., & Fuller, M. T. (2003) · Journal of Cell Science · doi:10.1242/jcs.00479 · Cited by 445 · see citing works
Mitofusins 1/2 and ERRα expression are increased in human skeletal muscle after physical exercise
Cartoni, R., Léger, B., Hock, M. B., Praz, M., Crettenand, A., Pich, S., Ziltener, J., Luthi, F., Dériaz, O., Zorzano, A., et al. (2005) · The Journal of Physiology · doi:10.1113/jphysiol.2005.092031 · Cited by 406 · see citing works
Self-citationPospisilik, J. A., Knauf, C., Joza, N., Benit, P., Orthofer, M., Cani, P. D., Ebersberger, I., Nakashima, T., Sarao, R., Neely, G., et al. (2007) · Cell · doi:10.1016/j.cell.2007.08.047 · Cited by 404 · see citing works
Arany, Z., Lebrasseur, N., Morris, C., Smith, E., Yang, W., Ma, Y., Chin, S., & Spiegelman, B. M. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2006.12.003 · Cited by 370 · see citing works
Expression of <i>Mfn2</i>, the Charcot-Marie-Tooth Neuropathy Type 2A Gene, in Human Skeletal Muscle
Bach, D., Naon, D., Pich, S., Soriano, F. X., Vega, N., Rieusset, J., Laville, M., Guillet, C., Boirie, Y., Wallberg-Henriksson, H., et al. (2005) · Diabetes · doi:10.2337/diabetes.54.9.2685 · Cited by 369 · see citing works
Self-citationSchuler, M. J., Ali, F., Chambon, C., Duteil, D., Bornert, J., Tardivel, A., Desvergne, B., Wahli, W., Chambon, P., & METZGER, D. (2006) · Cell Metabolism · doi:10.1016/j.cmet.2006.10.003 · Cited by 368 · see citing works
Soriano, F. X., Liesa, M., Bach, D., Chan, D. C., Palacín, M., & Zorzano, A. (2006) · Diabetes · doi:10.2337/db05-0509 · Cited by 343 · see citing works
Self-citationHandschin, C., Choi, C. S., Chin, S., Kim, S., Kawamori, D., Kurpad, A. J., Neubauer, N., Hu, J., Mootha, V. K., Kim, Y.-B., et al. (2007) · Journal of Clinical Investigation · doi:10.1172/jci31785 · Cited by 335 · see citing works
Toledo, F. G. S., Menshikova, E. V., Ritov, V. B., Azuma, K., Radikova, Z., DeLany, J., & Kelley, D. E. (2007) · Diabetes · doi:10.2337/db07-0141 · Cited by 321 · see citing works
Ek, J., Andersen, G., Urhammer, S. A., Gæde, P. H., Drivsholm, T., Borch-Johnsen, K., Hansen, T., & Pedersen, O. (2001) · Diabetologia · doi:10.1007/s001250100032 · Cited by 293 · see citing works
Zhang, D., Liu, Z.-X., Choi, C. S., Tian, L., Kibbey, R., Dong, J., Cline, G. W., Wood, P. A., & Shulman, G. I. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0707060104 · Cited by 291 · see citing works
Storlien, L., Oakes, N. D., & Kelley, D. E. (2004) · Proceedings of the Nutrition Society · doi:10.1079/pns2004349 · Cited by 291 · see citing works
Cogswell, A. M., Stevens, R. J., & Hood, D. A. (1993) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1993.264.2.c383 · Cited by 286 · see citing works
Amchenkova, A. A., Bakeeva, L. E., Chentsov, Y. S., Skulachev, V. P., & Zorov, D. B. (1988) · The Journal of cell biology · doi:10.1083/jcb.107.2.481 · Cited by 284 · see citing works
Targeted disruption of the insulin receptor gene in the mouse results in neonatal lethality.
Joshi, R. L., Lamothe, B., Cordonnier, N., Mesbah, K., Monthioux, E., Jami, J., & Bucchini, D. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00498.x · Cited by 281 · see citing works
Lelliott, C. J., Medina-Gomez, G., Petrovic, N., Kis, A., Feldmann, H. M., Bjursell, M., Parker, N., Curtis, K., Campbell, M., Hu, P., et al. (2006) · PLoS Biology · doi:10.1371/journal.pbio.0040369 · Cited by 280 · see citing works
Role of Lipid Oxidation in Pathogenesis of Insulin Resistance of Obesity and Type II Diabetes
Jp, F., Ferrannini, E., Golay, A., Meyer, H. U., Theibaud, D., Curchod, B., Maeder, E., Jéquier, E., & DeFronzo, R. A. (1987) · Diabetes · doi:10.2337/diab.36.11.1341 · Cited by 277 · see citing works
Sonoda, J., Mehl, I. R., Chong, L.-W., Nofsinger, R. R., & Evans, R. M. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0611623104 · Cited by 266 · see citing works
The mitochondrial protein MTP18 contributes to mitochondrial fission in mammalian cells
Tondera, D., Czauderna, F., Paulick, K., Schwarzer, R., Kaufmann, J., & Santel, A. (2005) · Journal of Cell Science · doi:10.1242/jcs.02415 · Cited by 239 · see citing works
Separate fusion of outer and inner mitochondrial membranes
Malka, F., Guillery, O., Cifuentes-Díaz, C., Guillou, E., Belenguer, P., Lombès, A., & Rojo, M. (2005) · EMBO Reports · doi:10.1038/sj.embor.7400488 · Cited by 233 · see citing works
Mitochondrial framework (reticulum mitochondriale) in rat diaphragm muscle
Bakeeva, L. E., Chentsov, Y. S., & Skulachev, V. P. (1978) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(78)90104-4 · Cited by 227 · see citing works
Hara, K., Tobe, K., Okada, T., Kadowaki, H., Akanuma, Y., Ito, C., Kimura, S., & Kadowaki, T. (2002) · Diabetologia · doi:10.1007/s00125-002-0803-z · Cited by 224 · see citing works
Toledo, F. G. S., Menshikova, E. V., Azuma, K., Radiková, Z., Kelley, C. A., Ritov, V. B., & Kelley, D. E. (2008) · Diabetes · doi:10.2337/db07-1429 · Cited by 218 · see citing works
Meirhaeghe, A., Crowley, V., Lenaghan, C., Lelliott, C. J., GREEN, K., Stewart, A., Kevin, H. A. R. T., Schinner, S., Sethi, J. K., Yeo, G. S. H., et al. (2003) · Biochemical Journal · doi:10.1042/bj20030200 · Cited by 210 · see citing works
Metabolic Effects of Dichloroacetate in Patients with Diabetes Mellitus and Hyperlipoproteinemia
Stacpoole, P. W., Moore, G. W., & Kornhauser, D. M. (1978) · New England Journal of Medicine · doi:10.1056/nejm197803092981002 · Cited by 207 · see citing works
Consoli, A., Nurjhan, N., Reilly, J. J., Bier, D. M., & Gerich, J. E. (1990) · Journal of Clinical Investigation · doi:10.1172/jci114940 · Cited by 204 · see citing works
Metalloprotease‐mediated OPA1 processing is modulated by the mitochondrial membrane potential
Guillery, O., Malka, F., Landes, T., Guillou, E., Blackstone, C. D., Lombès, A., Belenguer, P., Arnoult, D., & Rojo, M. (2008) · Biology of the Cell · doi:10.1042/bc20070110 · Cited by 189 · see citing works
Effects of weight loss and physical activity on skeletal muscle mitochondrial function in obesity
Menshikova, E. V., Ritov, V. B., Toledo, F. G. S., Ferrell, R. E., Goodpaster, B. H., & Kelley, D. E. (2005) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00322.2004 · Cited by 189 · see citing works
Nair, K. S., Bigelow, M. L., Asmann, Y. W., Chow, L. S., Coenen-Schimke, J. M., Klaus, K. A., Guo, Z.-K., Sreekumar, R., & Irving, B. A. (2008) · Diabetes · doi:10.2337/db07-1556 · Cited by 187 · see citing works
Yoon, Y., Pitts, K. R., Dahan, S., & McNiven, M. A. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.140.4.779 · Cited by 183 · see citing works
Hypomorphic mutation of PGC-1β causes mitochondrial dysfunction and liver insulin resistance.
Vianna, C. R., Huntgeburth, M., Coppari, R., Choi, C. S., Lin, J., Krauss, S., Barbatelli, G., Tzameli, I., Kim, Y.-B., Cinti, S., et al. (2006) · Cell Metabolism · doi:10.1016/j.cmet.2006.11.003 · Cited by 181 · see citing works
Mitochondrial Fusion Is Increased by the Nuclear Coactivator PGC-1β
Liesa, M., Borda-d'Agua, B., Medina‐Gómez, G., Lelliott, C. J., Paz, J. C., Rojo, M., Palacı́n, M., Vidal‐Puig, A., & Zorzano, A. (2008) · PLoS ONE · doi:10.1371/journal.pone.0003613 · Cited by 175 · see citing works
Self-citationMitochondria in Tissue Culture
Lewis, M. R., & Lewis, W. H. (1914) · Science · doi:10.1126/science.39.1000.330 · Cited by 166 · see citing works
Recombination of mitochondrial drug-resistance factors in Saccharomyces, cerevisiae
Thomas, D. Y., & Wilkie, D. R. (1968) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(68)90753-5 · Cited by 152 · see citing works
Tondera, D., Santel, A., Schwarzer, R., Dames, S., Giese, K., Klippel, A., & Kaufmann, J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404704200 · Cited by 143 · see citing works
Synthesis Rate of Muscle Proteins, Muscle Functions, and Amino Acid Kinetics in Type 2 Diabetes
Halvatsiotis, P., Short, K. R., Bigelow, M. L., & Nair, K. S. (2002) · Diabetes · doi:10.2337/diabetes.51.8.2395 · Cited by 143 · see citing works
Respiratory chain dysfunction in skeletal muscle does not cause insulin resistance
Wredenberg, A., Freyer, C., Sandström, M. E., Katz, A., Wibom, R., Westerblad, H., & Larsson, N.-G. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.09.029 · Cited by 141 · see citing works
Tissue-specific regulation of mitochondrial and cytoplasmic protein synthesis rates by insulin
Boirie, Y., Short, K. R., Ahlman, B., Charlton, M., & Nair, K. S. (2001) · Diabetes · doi:10.2337/diabetes.50.12.2652 · Cited by 137 · see citing works
Control of mitochondrial biogenesis during myogenesis
Kraft, C. S., LeMoine, C. M. R., Lyons, C. N., Michaud, D., Mueller, C. R., & Moyes, C. D. (2006) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00463.2005 · Cited by 132 · see citing works
Twig, G., Graf, S. A., Wikström, J. D., Mohamed, H., Haigh, S. E., Elorza, Á. A., Deutsch, M., Zurgil, N., Reynolds, N., & Shirihai, O. S. (2006) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00348.2005 · Cited by 129 · see citing works
Toledo, F. G. S., Watkins, S., & Kelley, D. E. (2006) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2006-0002 · Cited by 126 · see citing works
Meta-analysis of the Gly482Ser variant in PPARGC1A in type 2 diabetes and related phenotypes
Barroso, I., Luan, J., Sandhu, M. S., Franks, P. W., Crowley, V., Schafer, A. J., O’Rahilly, S., & Wareham, N. J. (2006) · Diabetologia · doi:10.1007/s00125-005-0130-2 · Cited by 116 · see citing works
Menshikova, E. V., Ritov, V. B., Ferrell, R. E., Azuma, K., Goodpaster, B. H., & Kelley, D. E. (2007) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01228.2006 · Cited by 113 · see citing works
Boss, O., Bachman, E. S., Vidal‐Puig, A., Zhang, C., Peroni, O. D., & Lowell, B. B. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.1145 · Cited by 100 · see citing works
Gastaldi, G., Russell, A. P., Golay, A., Giacobino, J., Habicht, F., Barthassat, V., Muzzin, P., & Bobbioni-Harsch, E. (2007) · Diabetologia · doi:10.1007/s00125-007-0782-1 · Cited by 85 · see citing works
The mitochondrial rhomboid protease PSARL is a new candidate gene for type 2 diabetes
Walder, K., Kerr-Bayles, L., Civitarese, A., Jowett, J., Curran, J., Elliott, K., Trevaskis, J., Bishara, N., Zimmet, P., Mandarino, L., et al. (2005) · Diabetologia · doi:10.1007/s00125-005-1675-9 · Cited by 85 · see citing works
Stacpoole, P. W., & Greene, Y. J. (1992) · Diabetes Care · doi:10.2337/diacare.15.6.785 · Cited by 79 · see citing works
Jofuku, A., Ishihara, N., & Mihara, K. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.05.154 · Cited by 73 · see citing works
Mingrone, G., Manco, M., Calvani, M., Castagneto, M., Naon, D., & Zorzano, A. (2005) · Diabetologia · doi:10.1007/s00125-005-1918-9 · Cited by 68 · see citing works
Self-citationRole of lipid oxidation in pathogenesis of insulin resistance of obesity and type II diabetes
Felber, J. P., Ferrannini, E., Golay, A., et al. (1987) · Diabetes · doi:10.2337/diabetes.36.11.1341 · Cited by 68 · see citing works
Ontogenesis of mitochondrial reticulum in rat diaphragm muscle.
Bakeeva, L. E., Chentsov, Y. S., & Skulachev, V. P. (1981) · PubMed · Cited by 56 · see citing works
Pawlikowska, P., Gajkowska, B., Hocquette, J.-F. J.-F., & Orzechowski, A. (2006) · Cell Proliferation · doi:10.1111/j.1365-2184.2006.00376.x · Cited by 45 · see citing works
Lelliott, C. J., Ljungberg, A., Ahnmark, A., William‐Olsson, L., Ekroos, K., Elmgren, A., Arnerup, G., Shoulders, C. C., Oscarsson, J., & Lindén, D. (2007) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.107.155739 · Cited by 44 · see citing works
Schrauwen‐Hinderling, V. B., Mensink, M., Hesselink, M. K. C., Sels, J.-P. J. E., Kooi, M. E., & Schrauwen, P. (2008) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2008-0267 · Cited by 43 · see citing works
Mosaic analysis of insulin receptor function
Kitamura, T., Kitamura, Y., Nakae, J., Giordano, A., Cinti, S., Kahn, C. R., Efstratiadis, A., & Accili, D. (2004) · Journal of Clinical Investigation · doi:10.1172/jci17810 · Cited by 42 · see citing works
Mitofusin 2 (Mfn2): a key player in insulin-dependent myogenesis in vitro
Pawlikowska, P., Gajkowska, B., & Orzechowski, A. (2006) · Cell and Tissue Research · doi:10.1007/s00441-006-0320-3 · Cited by 40 · see citing works
MECHANISM OF THE FORMATION OF MEGAMITOCHONDRIA INDUCED BY COPPER‐CHELATING AGENTS
Wakabayashi, T., Asano, M., & Kurono, C. (1975) · Acta Pathologica Japonica · doi:10.1111/j.1440-1827.1975.tb00147.x · Cited by 30 · see citing works
Cortese, J. D. (1998) · Experimental Cell Research · doi:10.1006/excr.1998.4004 · Cited by 17 · see citing works
Membrane Fusion in Mitochondria I. Ultrastructural Basis for Fusion
Wakabayashi, T., & Green, D. E. (1977) · Journal of Electron Microscopy · doi:10.1093/oxfordjournals.jmicro.a050077 · Cited by 15 · see citing works
PARL Leu262Val is not associated with fasting insulin levels in UK populations
Fawcett, K. A., Wareham, N. J., Luan, J., Syddall, H. E., Cooper, C. C., O’Rahilly, S., Day, I. N. M., Sandhu, M. S., & Barroso, I. (2006) · Diabetologia · doi:10.1007/s00125-006-0443-9 · Cited by 14 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Mitochondrial Dynamics — Mitochondrial Fission and Fusion in Human Diseases
Archer, S. L. (2013) · New England Journal of Medicine · doi:10.1056/nejmra1215233 · Cited by 1,103 · see citing works
Adipose tissue and insulin resistance in obese
Ahmed, B., Sultana, R., & Greene, M. W. (2021) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2021.111315 · Cited by 1,059 · see citing works
MAM (mitochondria-associated membranes) in mammalian cells: Lipids and beyond
Vance, J. E. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2013.11.014 · Cited by 665 · see citing works
Mitochondrial dynamics, mitophagy and cardiovascular disease
Vásquez-Trincado, C., García‐Carvajal, I., Pennanen, C., Parra, V., Hill, J. A., Rothermel, B. A., & Lavandero, S. (2015) · The Journal of Physiology · doi:10.1113/jp271301 · Cited by 625 · see citing works
Altered mitochondrial dynamics contributes to endothelial dysfunction in diabetes mellitus
Shenouda, S. M., Widlansky, M. E., Chen, K., Xu, G., Holbrook, M., Tabit, C. E., Hamburg, N. M., Frame, A. A., Caiano, T. L., Kluge, M. A., et al. (2011) · Circulation · doi:10.1161/circulationaha.110.014506 · Cited by 570 · see citing works
Endothelial dysfunction in diabetes mellitus: Molecular mechanisms and clinical implications
Tabit, C. E., Chung, W. B., Hamburg, N. M., & Vita, J. A. (2010) · Reviews in Endocrine and Metabolic Disorders · doi:10.1007/s11154-010-9134-4 · Cited by 584 · see citing works
Mitochondrial dysfunction and insulin resistance: an update
Montgomery, M. K., & Turner, N. A. (2014) · Endocrine Connections · doi:10.1530/ec-14-0092 · Cited by 530 · see citing works
Mitochondrial dysfunction in obesity
de Mello, A. H., Costa, A. B., Engel, J. D. G., & Rezin, G. T. (2018) · Life Sciences · doi:10.1016/j.lfs.2017.11.019 · Cited by 508 · see citing works
Raturi, A., & Simmen, T. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.04.013 · Cited by 448 · see citing works
Mitochondrial Regulation of Cell Cycle and Proliferation
Arciuch, V. G. A., Elguero, M. E., Poderoso, J. J., & Carreras, M. C. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4085 · Cited by 428 · see citing works
Figueira, T. R., de Barros, M. H., Camargo, A. A., Castilho, R. F., Ferreira, J. C. B., Kowaltowski, A. J., Sluse, F. E., de Souza-Pinto, N. C., & Vercesi, A. E. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4729 · Cited by 417 · see citing works
Zhao, J., Liu, T., Jin, S., Wang, X., Qu, M., Uhlén, P., Tomilin, N., Shupliakov, O., Lendahl, U., & Nistér, M. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.198 · Cited by 370 · see citing works
A Universal Approach to Analyzing Transmission Electron Microscopy with ImageJ
Lam, J., Katti, P., Biete, M., Mungai, M., AshShareef, S. T., Neikirk, K., Lopez, E. G., Vue, Z., Christensen, T. A., Beasley, H. K., et al. (2021) · Cells · doi:10.3390/cells10092177 · Cited by 352 · see citing works
Tsushima, K., Bugger, H., Wende, A. R., Soto, J. E., Jenson, G. A., Tor, A. R., McGlauflin, R., Kenny, H., Zhang, Y., Souvenir, R., et al. (2017) · Circulation Research · doi:10.1161/circresaha.117.311307 · Cited by 331 · see citing works
Wu, S., Lu, Q., Wang, Q., Ding, Y., Ma, Z., Mao, X., Huang, K., Xie, Z., & Zou, M.-H. (2017) · Circulation · doi:10.1161/circulationaha.117.030235 · Cited by 320 · see citing works
Bullón, P., Newman, H. N., & Battino, M. A. (2013) · Periodontology 2000 · doi:10.1111/j.1600-0757.2012.00455.x · Cited by 304 · see citing works
Mfn2 is critical for brown adipose tissue thermogenic function
Boutant, M., Kulkarni, S. S., Joffraud, M., Ratajczak, J., Valera‐Alberni, M., Combe, R., Zorzano, A., & Cantó, C. (2017) · The EMBO Journal · doi:10.15252/embj.201694914 · Cited by 297 · see citing works
Self-citationObesity May Accelerate the Aging Process
Salvestrini, V., Sell, C., & Lorenzini, A. (2019) · Frontiers in Endocrinology · doi:10.3389/fendo.2019.00266 · Cited by 260 · see citing works
Lepretti, M., Martucciello, S., Burgos Aceves, M., Putti, R., & Lionetti, L. (2018) · Nutrients · doi:10.3390/nu10030350 · Cited by 232 · see citing works
Causal roles of mitochondrial dynamics in longevity and healthy aging
Sharma, A., Smith, H. J., Yao, P., & Mair, W. B. (2019) · EMBO Reports · doi:10.15252/embr.201948395 · Cited by 215 · see citing works
Parra, V., Verdejo, H., Iglewski, M., del Campo, A., Troncoso, R., Jones, D., Zhu, Y., Kuzmicic, J., Pennanen, C., López‐Crisosto, C., et al. (2013) · Diabetes · doi:10.2337/db13-0340 · Cited by 219 · see citing works
Self-citationThe role of mitochondrial dynamics in cardiovascular diseases
Forte, M., Schirone, L., Ameri, P., Basso, C., Catalucci, D., Modica, J., Chimenti, C., Crotti, L., Frati, G., Rubattu, S. D., et al. (2020) · British Journal of Pharmacology · doi:10.1111/bph.15068 · Cited by 221 · see citing works
Davidson, S. M., Adameová, A., Barile, L., Cabrera-Fuentes, H. A., Lazou, A., Pagliaro, P., Stensløkken, K., García‐Dorado, D., & (CA16225), T. E. C. A. (2020) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.15127 · Cited by 206 · see citing works
Drp1-Mediated Mitochondrial Abnormalities Link to Synaptic Injury in Diabetes Model
Huang, S., Wang, Y., Gan, X., Du, F., Zhong, C., Wu, L., Hu, G., Sosunov, A. A., McKhann, G. M., Yu, H., et al. (2014) · Diabetes · doi:10.2337/db14-0758 · Cited by 166 · see citing works
Alterations of Mitochondrial Function and Insulin Sensitivity in Human Obesity and Diabetes Mellitus
Koliaki, C. C., & Roden, M. (2016) · Annual Review of Nutrition · doi:10.1146/annurev-nutr-071715-050656 · Cited by 167 · see citing works
Muscle oxidative capacity during IL-6-dependent cancer cachexia.
White, J. P., Baltgalvis, K. A., Puppa, M. J., Sato, S., Baynes, J., & Carson, J. (2011) · American Journal of Physiology. Regulatory Integrative and Comparative Physiology · doi:10.1152/ajpregu.00300.2010 · Cited by 162 · see citing works
Hernández‐Aguilera, A., Rull, A., Rodríguez‐Gallego, E., Riera-Borrull, M., Luciano‐Mateo, F., Camps, J., Menéndez, J. A., & Joven, J. (2013) · Mediators of Inflammation · doi:10.1155/2013/135698 · Cited by 162 · see citing works
Zuo, W., Zhang, S., Xia, C., Guo, X., He, W., & Chen, N. (2014) · Neuropharmacology · doi:10.1016/j.neuropharm.2014.07.002 · Cited by 157 · see citing works
Impaired Mitochondrial Dynamics and Bioenergetics in Diabetic Skeletal Muscle
Liu, R., Jin, P., LiqunYu, Wang, Y., Han, L., Shi, T., & Li, X. (2014) · PLoS ONE · doi:10.1371/journal.pone.0092810 · Cited by 146 · see citing works
Osataphan, N., Phrommintikul, A., Chattipakorn, S. C., & Chattipakorn, N. (2020) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.15305 · Cited by 141 · see citing works
Crosstalk between mitochondrial (dys)function and mitochondrial abundance
Michel, S., Wanet, A., Pauw, A. D., Rommelaere, G., Arnould, T., & Renard, P. (2011) · Journal of Cellular Physiology · doi:10.1002/jcp.23021 · Cited by 132 · see citing works
Rehman, M. U., Sehar, N., Dar, N. J., Khan, A., Arafah, A., Rashid, S., Rashid, S. M., & Ganaie, M. A. (2023) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2022.104961 · Cited by 130 · see citing works
Stressing out the mitochondria: Mechanistic insights into NLRP3 inflammasome activation
Yabal, M., Calleja, D. J., Simpson, D. S., & Lawlor, K. E. (2018) · Journal of Leukocyte Biology · doi:10.1002/jlb.mr0318-124r · Cited by 109 · see citing works
Inflammatory Signaling and Brown Fat Activity
Omran, F., & Christian, M. (2020) · Frontiers in Endocrinology · doi:10.3389/fendo.2020.00156 · Cited by 107 · see citing works
Sphingolipids as a Culprit of Mitochondrial Dysfunction in Insulin Resistance and Type 2 Diabetes
Roszczyc-Owsiejczuk, K., & Zabielski, P. (2021) · Frontiers in Endocrinology · doi:10.3389/fendo.2021.635175 · Cited by 112 · see citing works
Pennington, E. R., Funai, K., Brown, D. A., & Shaikh, S. R. (2019) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2019.03.012 · Cited by 107 · see citing works
Mitochondrial Activity and Dynamics Changes Regarding Metabolism in Ageing and Obesity
López-Lluch, G. (2017) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2016.12.005 · Cited by 103 · see citing works
“particular in Mfn2, have been associated with a reduced mitochondrial function in skeletal muscle in obesity and T2DM (Zorzano et al., 2009) and recently aberrant mitochondrial fission has been also associated with insulin resistance in mouse skeletal muscle (Jheng et al.”
BackgroundInfluentialLi, H., Slone, J. D., Fei, L., & Huang, T. (2019) · Cells · doi:10.3390/cells8060608 · Cited by 103 · see citing works
Direct cardiovascular impact of SGLT2 inhibitors: mechanisms and effects
Kaplan, A., Abidi, E., EL‐Yazbi, A. F., Eid, A. H., Booz, G. W., & Zouein, F. A. (2018) · Heart Failure Reviews · doi:10.1007/s10741-017-9665-9 · Cited by 103 · see citing works
Regulation of mitochondrial dynamics: convergences and divergences between yeast and vertebrates
Zhao, J., Lendahl, U., & Nistér, M. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-1066-6 · Cited by 99 · see citing works
Lackner, L. L., & Nunnari, J. M. (2010) · Chemistry & Biology · doi:10.1016/j.chembiol.2010.05.016 · Cited by 98 · see citing works
Putti, R., Migliaccio, V., Sica, R., & Lionetti, L. (2016) · Frontiers in Physiology · doi:10.3389/fphys.2015.00426 · Cited by 90 · see citing works
da Costa, R. M., Fais, R. S., Dechandt, C. R. P., Louzada‐Júnior, P., Alberici, L. C., Lobato, N. S., & Tostes, R. C. (2016) · British Journal of Pharmacology · doi:10.1111/bph.13687 · Cited by 90 · see citing works
Mitochondrial fission mediates ceramide-induced metabolic disruption in skeletal muscle
Smith, M. E., Tippetts, T. S., Brassfield, E. S., Tucker, B. J., Ockey, A., Swensen, A. C., Anthonymuthu, T. S., Washburn, T. D., Kane, D. A., Prince, J. T., et al. (2013) · Biochemical Journal · doi:10.1042/bj20130807 · Cited by 87 · see citing works
Mitochondrial function in vascular endothelial cell in diabetes
Pangare, M., & Makino, A. (2012) · Journal of Smooth Muscle Research · doi:10.1540/jsmr.48.1 · Cited by 83 · see citing works
Mitochondrial Dysfunction in Age‐Related Metabolic Disorders
Natarajan, V., Chawla, R., Mah, T. K. L., Vivekanandan, R., Tan, S., Sato, P. Y., & Mallilankaraman, K. B. (2020) · PROTEOMICS · doi:10.1002/pmic.201800404 · Cited by 81 · see citing works
Hepatic miR-144 Drives Fumarase Activity Preventing NRF2 Activation During Obesity
Azzimato, V., Chen, P., Barreby, E., Morgantini, C., Levi, L., Vankova, A., Jager, J., Sulen, A., Diotallevi, M., Shen, J. X., et al. (2021) · Gastroenterology · doi:10.1053/j.gastro.2021.08.030 · Cited by 81 · see citing works
Watanabe, T., Saotome, M., Nobuhara, M., Sakamoto, A., Urushida, T., Katoh, H., Satoh, H., Funaki, M., & Hayashi, H. (2014) · Experimental Cell Research · doi:10.1016/j.yexcr.2014.02.027 · Cited by 81 · see citing works
Crispino, M., Trinchese, G., Penna, E., Cimmino, F., Catapano, A., Villano, I., Perrone‐Capano, C., & Mollica, M. P. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21175964 · Cited by 79 · see citing works
From Obesity to Hippocampal Neurodegeneration: Pathogenesis and Non-Pharmacological Interventions
Lee, T. H.-Y., & Yau, S. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms22010201 · Cited by 76 · see citing works
Use of dicarboxylic acids in type 2 diabetes
Mingrone, G., Castagneto‐Gissey, L., & Macé, K. (2012) · British Journal of Clinical Pharmacology · doi:10.1111/j.1365-2125.2012.04177.x · Cited by 78 · see citing works
Diabetes and Alzheimer’s Disease: Might Mitochondrial Dysfunction Help Deciphering the Common Path?
Potenza, M. A., Sgarra, L., Desantis, V., Nacci, C., & Montagnani, M. (2021) · Antioxidants · doi:10.3390/antiox10081257 · Cited by 77 · see citing works
The Mitochondrial Calcium Uniporter (MCU): Molecular Identity and Role in Human Diseases
D’Angelo, D., & Rizzuto, R. (2023) · Biomolecules · doi:10.3390/biom13091304 · Cited by 80 · see citing works
Mitofusin-2 ameliorates high-fat diet-induced insulin resistance in liver of rats
Gan, K. (2013) · World Journal of Gastroenterology · doi:10.3748/wjg.v19.i10.1572 · Cited by 74 · see citing works
Cardiac Insulin Resistance in Heart Failure: The Role of Mitochondrial Dynamics
Saotome, M., Ikoma, T., Hasan, P., & Maekawa, Y. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20143552 · Cited by 70 · see citing works
Emerging Roles of Mitochondria ROS in Atherosclerotic Lesions: Causation or Association?
Wang, Y., & Tabas, I. A. (2014) · Journal of Atherosclerosis and Thrombosis · doi:10.5551/jat.23929 · Cited by 68 · see citing works
Pant, M., Sopariwala, D. H., Bal, N. C., Lowe, J., Delfín, D. A., Rafael‐Fortney, J. A., & Periasamy, M. (2015) · PLoS ONE · doi:10.1371/journal.pone.0123875 · Cited by 68 · see citing works
Capllonch-Amer, G., Lladó, I., Proenza, A. M., García-Palmer, F. J., & Gianotti, M. (2014) · Journal of Molecular Endocrinology · doi:10.1530/jme-13-0201 · Cited by 67 · see citing works
The suppression of ghrelin signaling mitigates age-associated thermogenic impairment
Lin, L., Lee, J. H., Bongmba, O. Y. N., Ma, X., Zhu, X., Sheikh‐Hamad, D., & Sun, Y. (2014) · Aging · doi:10.18632/aging.100706 · Cited by 67 · see citing works
Metabolic Stress and Disorders Related to Alterations in Mitochondrial Fission or Fusion.
Babbar, M., & Sheikh, M. S. (2013) · PubMed · Cited by 66 · see citing works
Mitochondrial accumulation under oxidative stress is due to defects in autophagy
Luo, C. Y., Li, Y., Wang, H., Feng, Z., Li, Y., Long, J., & Liu, J. (2012) · Journal of Cellular Biochemistry · doi:10.1002/jcb.24356 · Cited by 66 · see citing works
Khalil, M., Shanmugam, H., Abdallah, H., JohnBritto, J. S., Galerati, I., Gómez‐Ambrosi, J., Frühbeck, G., & Portincasa, P. (2022) · Nutrients · doi:10.3390/nu14153112 · Cited by 66 · see citing works
Mishiro, K., Imai, T., Sugitani, S., Kitashoji, A., Suzuki, Y., Takagi, T., Chen, H., Oumi, Y., Tsuruma, K., Shimazawa, M., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0103818 · Cited by 65 · see citing works
Bereiter‐Hahn, J., & Jendrach, M. (2010) · International review of cytology · doi:10.1016/s1937-6448(10)84001-8 · Cited by 64 · see citing works
Role of Mitofusin 2 in the Renal Stress Response
Gall, J. M., Wang, Z., Liesa, M., Molina, A. J. A., Havasi, A., Schwartz, J. H., Shirihai, O. S., Borkan, S. C., & Bonegio, R. G. B. (2012) · PLoS ONE · doi:10.1371/journal.pone.0031074 · Cited by 64 · see citing works
Self-citationProtective role of mitoquinone against impaired mitochondrial homeostasis in metabolic syndrome
Yang, J., Suo, H., & Song, J. (2020) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2020.1809344 · Cited by 66 · see citing works
Stacchiotti, A., Favero, G., Giugno, L., Lavazza, A., Reiter, R. J., Rodella, L. F., & Rezzani, R. (2014) · PLoS ONE · doi:10.1371/journal.pone.0111141 · Cited by 63 · see citing works
Li, S., Wang, J., Zhou, A., Khan, F. A., Hu, L., & Zhang, S. (2016) · Oncotarget · doi:10.18632/oncotarget.10817 · Cited by 61 · see citing works
Ophiopogonin D alleviates diabetic myocardial injuries by regulating mitochondrial dynamics
Li, W., Ji, L., Tian, J., Tang, W., Shan, X., Zhao, P., Chen, H., Zhang, C., Xu, M. G., Lü, R., et al. (2021) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2021.113853 · Cited by 59 · see citing works
Decoding the Rosetta stone of mitonuclear communication
English, J., Son, J. M., Cardamone, M. D., Lee, C., & Perissi, V. (2020) · Pharmacological Research · doi:10.1016/j.phrs.2020.105161 · Cited by 55 · see citing works
Li, F., Munsey, T. S., & Sivaprasadarao, A. (2017) · Cell Death and Differentiation · doi:10.1038/cdd.2017.118 · Cited by 49 · see citing works
The systems biology of mitochondrial fission and fusion and implications for disease and aging
Chauhan, A., Vera, J., & Wolkenhauer, O. (2014) · Biogerontology · doi:10.1007/s10522-013-9474-z · Cited by 52 · see citing works
Ferroptosis increases obesity: Crosstalk between adipocytes and the neuroimmune system
Zhang, S., Sun, Z., Jiang, X. Y., Lu, Z., Ding, L., Li, C., Tian, X., & Wang, Q. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.1049936 · Cited by 52 · see citing works
Metabolic abnormalities of the heart in type II diabetes
Amaral, N., & Okonko, D. O. (2015) · Diabetes and Vascular Disease Research · doi:10.1177/1479164115580936 · Cited by 52 · see citing works
Almeida, C., & Amaral, M. D. (2020) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03523-w · Cited by 51 · see citing works
Mitochondria and Antibiotics: For Good or for Evil?
Suarez-Rivero, J. M., Pastor‐Maldonado, C. J., Povea-Cabello, S., Álvarez-Córdoba, M., Villalón-García, I., Talaverón-Rey, M., Suárez-Carrillo, A., Munuera-Cabeza, M., & Sánchez-Alcázar, J. A. (2021) · Biomolecules · doi:10.3390/biom11071050 · Cited by 51 · see citing works
Glucose intolerance, metabolic syndrome, and neuropathy
Cortez, M. M., Singleton, J. R., & Smith, A. G. (2014) · Handbook of clinical neurology · doi:10.1016/b978-0-444-53480-4.00009-6 · Cited by 51 · see citing works
Role of Mitofusins and Mitophagy in Life or Death Decisions
Joaquim, M., & Escobar‐Henriques, M. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.572182 · Cited by 49 · see citing works
Mitochondrial Perturbation in Alzheimer's Disease and Diabetes
Akhter, F., Chen, D., Yan, S. F., & Yan, S. S. (2017) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2016.12.019 · Cited by 48 · see citing works
Intracellular to Interorgan Mitochondrial Communication in Striated Muscle in Health and Disease
Boardman, N. T., Trani, G., Scalabrin, M., Romanello, V., & Wüst, R. C. I. (2023) · Endocrine Reviews · doi:10.1210/endrev/bnad004 · Cited by 49 · see citing works
Schauss, A. C., Huang, H., Choi, S., Xu, L., Soubeyrand, S., Bilodeau, P. S., Zunino, R., Rippstein, P. U., Frohman, M. A., & McBride, H. M. (2010) · BMC Biology · doi:10.1186/1741-7007-8-100 · Cited by 47 · see citing works
Wang, J., Zhang, J., Yu, Z., Chung, S. K., & Xu, B. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102416 · Cited by 47 · see citing works
Wang, W., Fernández‐Sanz, C., & Sheu, S. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2017.09.004 · Cited by 45 · see citing works
Important mitochondrial proteins in human omental adipose tissue show reduced expression in obesity
Lindinger, P. W., Christe, M., Eberlé, A. N., Kern, B. E., Peterli, R., Peters, T. T. A., Jayawardene, K. J. I., Fearnley, I. M., & Walker, J. E. (2015) · Journal of Proteomics · doi:10.1016/j.jprot.2015.03.037 · Cited by 45 · see citing works
Li, D., Ni, X., Zhang, X., Liu, L., Qu, J., Ding, D., & Qian, J. (2018) · Nano Research · doi:10.1007/s12274-018-2118-5 · Cited by 44 · see citing works
Importance of Mitochondrial Dynamin-Related Protein 1 in Hypothalamic Glucose Sensitivity in Rats
Carneiro, L., Allard, C., Guissard, C., Fioramonti, X., Tourrel‐Cuzin, C., Bailbé, D., Barreau, C., Offer, G., Nédélec, E., Salin, B., et al. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4254 · Cited by 43 · see citing works
Malandraki-Miller, S., Lopez, C. A., Al-Siddiqi, H., & Carr, C. A. (2018) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2018.00119 · Cited by 43 · see citing works
Wu, M., Chou, H., & Huang, C. (2014) · Marine Drugs · doi:10.3390/md12020964 · Cited by 42 · see citing works
Wang, Y., Wu, L., Li, J., Du, F., Zhong, C., Chen, J. X., & Yan, S. S. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-140972 · Cited by 42 · see citing works
Ex Vivo Imaging of Excised Tissue Using Vital Dyes and Confocal Microscopy
Johnson, S. C., & Rabinovitch, P. S. (2012) · Current Protocols in Cytometry · doi:10.1002/0471142956.cy0939s61 · Cited by 42 · see citing works
Mitofusin 2 Deficiency Affects Energy Metabolism and Mitochondrial Biogenesis in MEF Cells
Kawalec, M., Boratyńska-Jasińska, A., Beresewicz, M., Dymkowska, D., Zabłocki, K., & Zabłocka, B. (2015) · PLoS ONE · doi:10.1371/journal.pone.0134162 · Cited by 41 · see citing works
Balasubramaniam, K., Viswanathan, G. N., Marshall, S. M., & Zaman, A. (2012) · Cardiology Research and Practice · doi:10.1155/2012/909154 · Cited by 41 · see citing works
Mitochondrial Dysfunctions: A Thread Sewing Together Alzheimer’s Disease, Diabetes, and Obesity
Rigotto, G., & Basso, E. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/7210892 · Cited by 43 · see citing works
Mitochondrial dynamic modulation exerts cardiometabolic protection in obese insulin-resistant rats
Maneechote, C., Palee, S., Apaijai, N., Kerdphoo, S., Jaiwongkam, T., Chattipakorn, S. C., & Chattipakorn, N. (2019) · Clinical Science · doi:10.1042/cs20190960 · Cited by 41 · see citing works
Maneechote, C., Palee, S., Kerdphoo, S., Jaiwongkam, T., Chattipakorn, S. C., & Chattipakorn, N. (2020) · Biochemical Pharmacology · doi:10.1016/j.bcp.2020.114295 · Cited by 41 · see citing works
Reinhardt, F., Schultz, J., Waterstradt, R., & Baltrusch, S. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.04.142 · Cited by 40 · see citing works
Paraoxonases and chemokine (C-C motif) ligand-2 in noncommunicable diseases.
Camps, J., Rodríguez-Gallego, E., García-Heredia, A., Triguero, I., Riera-Borrull, M., Hernández-Aguilera, A., Luciano-Mateo, F., Fernández-Arroyo, S., & Joven, J. (2014) · Advances in Clinical Chemistry · doi:10.1016/b978-0-12-800094-6.00007-8 · Cited by 41 · see citing works
Hypothalamic Mitochondrial Dysfunction as a Target in Obesity and Metabolic Disease
Cuñarro, J., Casado, S., Lugilde, J., & Tovar, S. A. (2018) · Frontiers in Endocrinology · doi:10.3389/fendo.2018.00283 · Cited by 40 · see citing works
Hepatic Rab24 controls blood glucose homeostasis via improving mitochondrial plasticity
Seitz, S., Kwon, Y., Hartleben, G., Jülg, J., Sekar, R., Krahmer, N., Najafi, B., Loft, A., Gancheva, S., Stemmer, K., et al. (2019) · Nature Metabolism · doi:10.1038/s42255-019-0124-x · Cited by 39 · see citing works
Mitochondrial aconitase controls adipogenesis through mediation of cellular ATP production
Chen, Y., Cai, G. H., Xia, B., Wang, X., Zhang, C. C., Xie, B., Shi, X., Liu, H., Lu, J. F., Zhang, R. X., et al. (2020) · The FASEB Journal · doi:10.1096/fj.201903224rr · Cited by 39 · see citing works
- Authors
- Zorzano, A., Liesa, M., & Palacín, M.
- Affiliations
- Centro de Investigación Biomédica en Red Diabetes y Enfermedades Metabólicas Asociadas (ES)
- ORCID
- Liesa, Marc
- Venue
- The International Journal of Biochemistry & Cell Biology
- Publisher
- Elsevier BV
- Published
- 2009-10
- Volume
- 41
- Issue
- 10
- Pages
- 1846-1854
- ISSN
- 1357-2725 (ISSN-L)
- OpenAlex
- W2056253513
- Cited by
- 209
- References
- 105
- Citations by year
- 2026: 2 · 2025: 5 · 2024: 11 · 2023: 16 · 2022: 13 · 2021: 16 · 2020: 20 · 2019: 13 · 2018: 10 · 2017: 12 · 2016: 12 · 2015: 10 · 2014: 20 · 2013: 17 · 2012: 15
- FWCI
- 0.79
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- The International Journal of Biochemistry & Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Generalitat de Catalunya
- Instituto de Salud Carlos III
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Physiology › Adipose Tissue and Metabolism
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Keywords
- mitochondrial dynamics, mitofusin 2, mitochondrial fusion, mitochondrial fission, mitochondrial dysfunction, skeletal muscle, obesity, type 2 diabetes, insulin resistance, mitochondrial respiration, substrate oxidation
- MeSH terms
- Animals, Diabetes Mellitus, Type 2, Humans, Insulin Resistance, Mitochondria, Obesity, Mitochondrial Proteins
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
