Mitochondrial complex II, a novel target for anti-cancer agents

Hallmarks of Cancer: The Next Generation

Hanahan, D., & Weinberg, R. A. (2011) · Cell · doi:10.1016/j.cell.2011.02.013 · Cited by 66,590 · see citing works

Understanding the Warburg Effect: The Metabolic Requirements of Cell Proliferation

Vander Heiden, M. G., Cantley, L. C., & Thompson, C. B. (2009) · Science · doi:10.1126/science.1160809 · Cited by 16,197 · see citing works

Cancer statistics, 2012

Siegel, R., Naishadham, D., & Jemal, A. (2012) · CA: A Cancer Journal for Clinicians · doi:10.3322/caac.20138 · Cited by 10,679 · see citing works

Intratumor Heterogeneity and Branched Evolution Revealed by Multiregion Sequencing

Gerlinger, M., Rowan, A. J., Horswell, S., Larkin, J., Endesfelder, D., Gronroos, E., Martinez, P., Matthews, N., Stewart, A., Tarpey, P., et al. (2012) · New England Journal of Medicine · doi:10.1056/nejmoa1113205 · Cited by 7,774 · see citing works

An Integrated Genomic Analysis of Human Glioblastoma Multiforme

Parsons, D. W., Jones, S., Zhang, X., Lin, J. C.-H., Leary, R. J., Angenendt, P., Mankoo, P., Carter, H., Siu, I.-M., Gallia, G. L., et al. (2008) · Science · doi:10.1126/science.1164382 · Cited by 5,857 · see citing works

Core Signaling Pathways in Human Pancreatic Cancers Revealed by Global Genomic Analyses

Jones, S., Zhang, X., Parsons, D. W., Lin, J. C.-H., Leary, R. J., Angenendt, P., Mankoo, P., Carter, H., Kamiyama, H., Jimeno, A., et al. (2008) · Science · doi:10.1126/science.1164368 · Cited by 3,969 · see citing works

The Pathophysiology of Mitochondrial Cell Death

Green, D. R., & Kroemer, G. (2004) · Science · doi:10.1126/science.1099320 · Cited by 3,416 · see citing works

Cancer treatment and survivorship statistics, 2012

Siegel, R. L., Desantis, C. E., Virgo, K. S., Stein, K., Mariotto, A. B., Smith, T. G., Cooper, D. L., Gansler, T. S., Lerro, C. C., Fedewa, S. A., et al. (2012) · CA A Cancer Journal for Clinicians · doi:10.3322/caac.21149 · Cited by 2,924 · see citing works

Evidence that metformin exerts its anti-diabetic effects through inhibition of complex 1 of the mitochondrial respiratory chain

OWEN, M. R., DORAN, E., & HALESTRAP, A. P. (2000) · Biochemical Journal · doi:10.1042/bj3480607 · Cited by 2,157 · see citing works

Succinate links TCA cycle dysfunction to oncogenesis by inhibiting HIF-α prolyl hydroxylase

Selak, M. A., Armour, S. M., MacKenzie, E. D., Boulahbel, H., Watson, D. G., Mansfield, K. D., Pan, Y., Simon, M. C., Thompson, C. B., & Gottlieb, E. (2005) · Cancer Cell · doi:10.1016/j.ccr.2004.11.022 · Cited by 2,108 · see citing works

IDH mutation impairs histone demethylation and results in a block to cell differentiation

Lu, C., Ward, P. S., Kapoor, G. S., Rohle, D., Turcan, S., Abdel-Wahab, O., Edwards, C. R., Khanin, R., Figueroa, M. E., Melnick, A., et al. (2012) · Nature · doi:10.1038/nature10860 · Cited by 1,985 · see citing works

Mutations in <i>SDHD</i> , a Mitochondrial Complex II Gene, in Hereditary Paraganglioma

Baysal, B. E., Ferrell, R. E., Willett-Brozick, J. E., Lawrence, E. C., Myssiorek, D., Bosch, A., Mey, A. V. D., Taschner, P. E. M., Rubinstein, W. S., Myers, E. N., et al. (2000) · Science · doi:10.1126/science.287.5454.848 · Cited by 1,638 · see citing works

Targeting mitochondria for cancer therapy

Fulda, S., Galluzzi, L., & Kroemer, G. (2010) · Nature Reviews Drug Discovery · doi:10.1038/nrd3137 · Cited by 1,638 · see citing works

A Mitochondria-K+ Channel Axis Is Suppressed in Cancer and Its Normalization Promotes Apoptosis and Inhibits Cancer Growth

Bonnet, S., Archer, S. L., Allalunis‐Turner, J., Haromy, A., Beaulieu, C., Thompson, R. B., Lee, C. T., Lopaschuk, G. D., Puttagunta, L., Bonnet, S. B., et al. (2007) · Cancer Cell · doi:10.1016/j.ccr.2006.10.020 · Cited by 1,530 · see citing works

Inhibition of lactate dehydrogenase A induces oxidative stress and inhibits tumor progression

Le, A., Cooper, C. R., Gouw, A. M., Dinavahi, R., Maitra, A., Deck, L. M., Royer, R. E., Jagt, D. L. V., Semenza, G. L., & Dang, C. V. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0914433107 · Cited by 1,528 · see citing works

Oxidative Phosphorylation at the fin de siècle

Saraste, M. (1999) · Science · doi:10.1126/science.283.5407.1488 · Cited by 1,318 · see citing works

Inhibition of α-KG-dependent histone and DNA demethylases by fumarate and succinate that are accumulated in mutations of FH and SDH tumor suppressors

Xiao, M., Yang, H., Xu, W., Ma, S., Lin, H., Zhu, H., Liu, L., Liu, Y., Yang, C., Xu, Y., et al. (2012) · Genes &amp; Development · doi:10.1101/gad.191056.112 · Cited by 1,188 · see citing works

Targeting Antioxidants to Mitochondria by Conjugation to Lipophilic Cations

Murphy, M. P., & Smith, R. A. J. (2007) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.47.120505.105110 · Cited by 1,173 · see citing works

Selective Targeting of a Redox-active Ubiquinone to Mitochondria within Cells

Kelso, G. F., Porteous, C. M., Coulter, C. V., Hughes, G., Porteous, W. K., Ledgerwood, E. C., Smith, R. A. J., & Murphy, M. P. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m009093200 · Cited by 1,091 · see citing works

Gene Mutations in the Succinate Dehydrogenase Subunit SDHB Cause Susceptibility to Familial Pheochromocytoma and to Familial Paraganglioma

Astuti, D., Latif, F., Dallol, A., Dahia, P. L. M., Douglas, F., George, E., Sköldberg, F., Husebye, E. S., Eng, C., & Maher, E. R. (2001) · The American Journal of Human Genetics · doi:10.1086/321282 · Cited by 1,087 · see citing works

Energy metabolism in tumor cells

Moreno‐Sánchez, R., Rodríguez‐Enríquez, S., Marín‐Hernández, Á., & Saavedra, E. (2007) · FEBS Journal · doi:10.1111/j.1742-4658.2007.05686.x · Cited by 1,086 · see citing works

Architecture of succinate dehydrogenase and reactive oxygen species generation

Yankovskaya, V., Horsefield, R., Törnroth, S., Luna-Chavez, C., Miyoshi, H., Léger, C., Byrne, B., Cecchini, G., & Iwata, S. (2003) · Science · doi:10.1126/science.1079605 · Cited by 927 · cited 2× · see citing works

Crystal Structure of Mitochondrial Respiratory Membrane Protein Complex II

Sun, F., Huo, X., Zhai, Y., Wang, A., Xu, J., Su, D., Bartlam, M., & Rao, Z. (2005) · Cell · doi:10.1016/j.cell.2005.05.025 · Cited by 881 · see citing works

Mutations in SDHC cause autosomal dominant paraganglioma, type 3

Niemann, S., & Müller, U. (2000) · Nature Genetics · doi:10.1038/81551 · Cited by 875 · see citing works

Accumulation of Krebs cycle intermediates and over-expression of HIF1α in tumours which result from germline FH and SDH mutations

Pollard, P. J., Brière, J. J., Alam, N. A., Barwell, J., Barclay, E., Wortham, N. C., Hunt, T., Mitchell, M., Olpin, S., Moat, S. J., et al. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi227 · Cited by 865 · see citing works

Hexokinase II: Cancer's double-edged sword acting as both facilitator and gatekeeper of malignancy when bound to mitochondria

Mathupala, S. P., Ko, Y. H., & Pedersen, P. L. (2006) · Oncogene · doi:10.1038/sj.onc.1209603 · Cited by 766 · see citing works

Mitochondrial Energetics and Therapeutics

Wallace, D. C., Fan, W., & Procaccio, V. (2010) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev.pathol.4.110807.092314 · Cited by 727 · see citing works

Cancers with increasing incidence trends in the United States: 1999 through 2008

Simard, E. P., Ward, E., Siegel, R. L., & Jemal, A. (2012) · CA A Cancer Journal for Clinicians · doi:10.3322/caac.20141 · Cited by 723 · see citing works

<i>SDH5</i> , a Gene Required for Flavination of Succinate Dehydrogenase, Is Mutated in Paraganglioma

Hao, H.-X., Khalimonchuk, O., Schraders, M., Dephoure, N., Bayley, J.-P., Kunst, H., Devilee, P., Cremers, C. W. R. J., Schiffman, J. D., Bentz, B. G., et al. (2009) · Science · doi:10.1126/science.1175689 · Cited by 702 · see citing works

Mitochondrial Complex II Can Generate Reactive Oxygen Species at High Rates in Both the Forward and Reverse Reactions

Quinlan, C. L., Orr, A. L., Perevoshchikova, I. V., Treberg, J. R., Ackrell, B. A., & Brand, M. D. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.374629 · Cited by 670 · see citing works

SDHA is a tumor suppressor gene causing paraganglioma

Burnichon, N., Brière, J.-J., Libé, R., Vescovo, L., Rivière, J., Tissier, F., Jouanno, E., Jeunemaı̂tre, X., Bénit, P., Tzagoloff, A., et al. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq206 · Cited by 645 · see citing works

Mitochondria in cancer cells: what is so special about them?

Gogvadze, V. G., Orrenius, S., & Zhivotovsky, B. (2008) · Trends in Cell Biology · doi:10.1016/j.tcb.2008.01.006 · Cited by 636 · see citing works

Defects in succinate dehydrogenase in gastrointestinal stromal tumors lacking <i>KIT</i> and <i>PDGFRA</i> mutations

Janeway, K. A., Kim, S. Y., Lodish, M., Nosé, V., Rustin, P., Gaal, J., Dahia, P. L. M., Liegl, B., Ball, E. R., Raygada, M., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1009199108 · Cited by 628 · see citing works

Cancer metabolism: facts, fantasy, and fiction

Zu, X. L., & Guppy, M. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2003.11.136 · Cited by 618 · see citing works

Cell death assays for drug discovery

Kepp, O., Galluzzi, L., Lipinski, M. M., Yuan, J., & Kroemer, G. (2011) · Nature Reviews Drug Discovery · doi:10.1038/nrd3373 · Cited by 556 · see citing works

Function and Structure of Complex II of the Respiratory Chain

Cecchini, G. (2003) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.72.121801.161700 · Cited by 556 · see citing works

An immunohistochemical procedure to detect patients with paraganglioma and phaeochromocytoma with germline SDHB, SDHC, or SDHD gene mutations: a retrospective and prospective analysis

van Nederveen, F. H., Gaal, J., Favier, J., Korpershoek, E., Oldenburg, R. A., de Bruyn, E. M., Sleddens, H. F. B. M., Derkx, P., Rivière, J., Dannenberg, H., et al. (2009) · The Lancet Oncology · doi:10.1016/s1470-2045(09)70164-0 · Cited by 534 · see citing works

Regulation of Succinate Dehydrogenase Activity by SIRT3 in Mammalian Mitochondria

Çimen, H., Han, M., Yang, Y., Tong, Q., Koc, H., & Koc, E. C. (2009) · Biochemistry · doi:10.1021/bi901627u · Cited by 478 · see citing works

Succinate dehydrogenase – Assembly, regulation and role in human disease

Rutter, J. P., Winge, D. R., & Schiffman, J. D. (2010) · Mitochondrion · doi:10.1016/j.mito.2010.03.001 · Cited by 459 · see citing works

Succinate: quinone oxidoreductases

Hägerhäll, C. (1997) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(97)00019-4 · Cited by 439 · see citing works

Loss of the SdhB, but Not the SdhA, Subunit of Complex II Triggers Reactive Oxygen Species-Dependent Hypoxia-Inducible Factor Activation and Tumorigenesis

Guzy, R. D., Sharma, B., Bell, E., Chandel, N. S., & Schumacker, P. T. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01338-07 · Cited by 427 · see citing works

SDH mutations in cancer

Bardella, C., Pollard, P. J., & Tomlinson, I. (2011) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2011.07.003 · Cited by 395 · see citing works

Succinate Dehydrogenase Is a Direct Target of Sirtuin 3 Deacetylase Activity

Finley, L. W. S., Haas, W., Desquiret‐Dumas, V., Wallace, D. C., Procaccio, V., Gygi, S. P., & Haigis, M. C. (2011) · PLoS ONE · doi:10.1371/journal.pone.0023295 · Cited by 364 · see citing works

Cell-Permeating <i>α</i> -Ketoglutarate Derivatives Alleviate Pseudohypoxia in Succinate Dehydrogenase-Deficient Cells

MacKenzie, E. D., Selak, M. A., Tennant, D. A., Payne, L. J., Crosby, S., Frederiksen, C. M., Watson, D. G., & Gottlieb, E. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01927-06 · Cited by 359 · see citing works

Advanced cancers: eradication in all cases using 3-bromopyruvate therapy to deplete ATP

Ko, Y. H., Smith, B. L., Wang, Y., Pomper, M. G., Rini, D. A., Torbenson, M. S., Hullihen, J. M., & Pedersen, P. L. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.09.047 · Cited by 352 · see citing works

The causes of cancer revisited: “Mitochondrial malignancy” and ROS-induced oncogenic transformation – Why mitochondria are targets for cancer therapy

Ralph, S. J., Rodríguez‐Enríquez, S., Neužil, J., Saavedra, E., & Moreno‐Sánchez, R. (2010) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2010.02.008 · Cited by 335 · see citing works

Predictors and Prevalence of Paraganglioma Syndrome Associated With Mutations of the SDHC Gene

Schiavi, F. (2005) · JAMA · doi:10.1001/jama.294.16.2057 · Cited by 328 · see citing works

Measurement of H2O2 within Living Drosophila during Aging Using a Ratiometric Mass Spectrometry Probe Targeted to the Mitochondrial Matrix

Cochemé, H. M., Quin, C., McQuaker, S. J., Cabreiro, F., Logan, A., Prime, T. A., Abakumova, I., Patel, J. V., Fearnley, I. M., James, A. M., et al. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.02.003 · Cited by 313 · see citing works

α-Tocopheryl succinate induces apoptosis by targeting ubiquinone-binding sites in mitochondrial respiratory complex II

Dong, L.-F., Low, P., Dyason, J. C., Wang, X.-F., Procházka, L., Witting, P. K., Freeman, R., Swettenham, E., Vališ, K., Liu, J., et al. (2008) · Oncogene · doi:10.1038/onc.2008.69 · Cited by 297 · see citing works

Structural and Computational Analysis of the Quinone-binding Site of Complex II (Succinate-Ubiquinone Oxidoreductase)

Horsefield, R., Yankovskaya, V., Sexton, G., Whittingham, W., Shiomi, K., Ōmura, S., Byrne, B., Cecchini, G., & Iwata, S. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m508173200 · Cited by 292 · see citing works

Induction of cancer cell apoptosis by α‐tocopheryl succinate: molecular pathways and structural requirements

Neužil, J., WEBER, T., SCHRÖDER, A., Lü, M., Ostermann, G., Gellert, N., Mayne, G. C., Olejnicka, B. T., Nègre‐Salvayre, A., Štícha, M., et al. (2001) · The FASEB Journal · doi:10.1096/fj.00-0251com · Cited by 284 · see citing works

SDH mutations in tumorigenesis and inherited endocrine tumours: lesson from the phaeochromocytoma–paraganglioma syndromes

Pasini, B., & Stratakis, C. A. (2009) · Journal of Internal Medicine · doi:10.1111/j.1365-2796.2009.02111.x · Cited by 268 · see citing works

Atpenins, potent and specific inhibitors of mitochondrial complex II (succinate-ubiquinone oxidoreductase)

Miyadera, H., Shiomi, K., Ui, H., Yamaguchi, Y., Masuma, R., Tomoda, H., Miyoshi, H., Osanai, A., Kita, K., & Ōmura, S. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0237315100 · Cited by 256 · see citing works

A Mutation in the <i>SDHC</i> Gene of Complex II Increases Oxidative Stress, Resulting in Apoptosis and Tumorigenesis

Ishii, T., Yasuda, K., Akatsuka, A., Hino, O., Hartman, P. S., & Ishii, N. (2005) · Cancer Research · doi:10.1158/0008-5472.203.65.1 · Cited by 253 · see citing works

Classification of mitocans, anti-cancer drugs acting on mitochondria

Neužil, J., Dong, L., Rohlena, J., Truksa, J., & Ralph, S. J. (2012) · Mitochondrion · doi:10.1016/j.mito.2012.07.112 · Cited by 248 · see citing works

New Oral Therapies for Type 2 Diabetes Mellitus: The Glitazones or Insulin Sensitizers

Mudaliar, S. R. D., & Henry, R. R. (2001) · Annual Review of Medicine · doi:10.1146/annurev.med.52.1.239 · Cited by 247 · see citing works

Germline SDHD mutation in familial phaeochromocytoma

Astuti, D., Douglas, F., Lennard, T. W., Aligianis, I. A., Woodward, E. R., Evans, D. G. R., Eng, C., Latif, F., & Maher, E. R. (2001) · The Lancet · doi:10.1016/s0140-6736(00)04378-6 · Cited by 246 · see citing works

SDHAF1, encoding a LYR complex-II specific assembly factor, is mutated in SDH-defective infantile leukoencephalopathy

Ghezzi, D., Goffrini, P., Uziel, G., Horváth, R., Klopstock, T., Lochmüller, H., D’Adamo, P., Gasparini, P., Strom, T. M., Prokisch, H., et al. (2009) · Nature Genetics · doi:10.1038/ng.378 · Cited by 244 · see citing works

Selective cancer cell killing by α-tocopheryl succinate

Neužil, J., Weber, T., Gellert, N., & Weber, C. (2001) · British Journal of Cancer · doi:10.1054/bjoc.2000.1559 · Cited by 240 · see citing works

Complex II inhibition by 3-NP causes mitochondrial fragmentation and neuronal cell death via an NMDA- and ROS-dependent pathway

Liot, G., Bossy, B., Lubitz, S., Kushnareva, Y., Sejbuk, N. E., & Bossy‐Wetzel, E. (2009) · Cell Death and Differentiation · doi:10.1038/cdd.2009.22 · Cited by 239 · see citing works

The Warburg effect is genetically determined in inherited pheochromocytomas

Favier, J., Brière, J.-J., Burnichon, N., Rivière, J., Vescovo, L., Benit, P., Giscos-Douriez, I., De Reyniès, A., Bertherat, J., Badoual, C., et al. (2009) · PLoS ONE · doi:10.1371/journal.pone.0007094 · Cited by 232 · see citing works

Role of mitochondria-associated hexokinase II in cancer cell death induced by 3-bromopyruvate

Zhao, C., Zhang, H., Lu, W., & Huang, P. (2009) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2009.03.003 · Cited by 230 · see citing works

Mitochondrial complex II has a key role in mitochondrial-derived reactive oxygen species influence on plant stress gene regulation and defense

Gleason, C., Huang, S., Thatcher, L. F., Foley, R. C., Anderson, C. R., Carroll, A., Millar, A. H., & Singh, K. B. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1016060108 · Cited by 227 · see citing works

Germline Mutations and Variants in the Succinate Dehydrogenase Genes in Cowden and Cowden-like Syndromes

Ni, Y., Zbuk, K. M., Sadler, T. M., Patócs, A., Lobo, G. P., Edelman, E. A., Platzer, P., Orloff, M. S., Waite, K. A., & Eng, C. (2008) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2008.07.011 · Cited by 219 · see citing works

Pheochromocytoma and paraganglioma: understanding the complexities of the genetic background

Fishbein, L. M., & Nathanson, K. L. (2012) · Cancer Genetics · doi:10.1016/j.cancergen.2012.01.009 · Cited by 206 · see citing works

Mitochondrial Targeting of Vitamin E Succinate Enhances Its Pro-apoptotic and Anti-cancer Activity via Mitochondrial Complex II

Dong, L.-F., Jameson, V. J. A., Tilly, D., Cerny, J., Mahdavian, E., Marín-Hernández, A., Hernández-Esquivel, L., Rodríguez-Enríquez, S., Stursa, J., Witting, P. K., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.186643 · Cited by 200 · cited 7× · see citing works

Vitamin E succinate is a potent novel antineoplastic agent with high selectivity and cooperativity with tumor necrosis factor-related apoptosis-inducing ligand (Apo2 ligand) in vivo.

Weber, T., Lu, M., Anděra, L., Lahm, H., Gellert, N., Fariss, M. W., Kořínek, V., Sattler, W., Ucker, D. S., Terman, A., et al. (2002) · PubMed · Cited by 188 · see citing works

Troglitazone-induced liver failure: a case study

Graham, D. J., Green, L., Senior, J. R., & Nourjah, P. A. (2003) · The American Journal of Medicine · doi:10.1016/s0002-9343(02)01529-2 · Cited by 187 · see citing works

Apoptotic Death in Leishmania donovani Promastigotes in Response to Respiratory Chain Inhibition

Mehta, A. K., & Shaha, C. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m309341200 · Cited by 181 · see citing works

Molecular mechanism of ‘mitocan’‐induced apoptosis in cancer cells epitomizes the multiple roles of reactive oxygen species and Bcl‐2 family proteins

Neužil, J., Wang, X., Dong, L., Low, P., & Ralph, S. J. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.05.072 · Cited by 181 · see citing works

Inhibition of energy-producing pathways of HepG2 cells by 3-bromopyruvate1

Silva, A. P. P. D., El‐Bacha, T., Kyaw, N., dos Santos, R. S., da‐Silva, W. S., Almeida, F. C. L., Poian, A. T. D., & Galina, A. (2008) · Biochemical Journal · doi:10.1042/bj20080805 · Cited by 170 · see citing works

Succinate inhibition of α-ketoglutarate-dependent enzymes in a yeast model of paraganglioma

Smith, E. H., Janknecht, R., & Maher, L. J. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddm275 · Cited by 169 · see citing works

Mitochondria Play a Central Role in Apoptosis Induced by α-Tocopheryl Succinate, an Agent with Antineoplastic Activity: Comparison with Receptor-Mediated Pro-Apoptotic Signaling

Weber, T., Dalen, H., Anděra, L., Nègre‐Salvayre, A., Augè, N., Štícha, M., Lloret, A., Terman, A., Witting, P. K., Higuchi, M., et al. (2003) · Biochemistry · doi:10.1021/bi020527j · Cited by 166 · see citing works

A translational study “case report” on the small molecule “energy blocker” 3-bromopyruvate (3BP) as a potent anticancer agent: from bench side to bedside

Ko, Y. H., Verhoeven, H. A., Lee, M. J., Corbin, D., Vogl, T. J., & Pedersen, P. L. (2012) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-012-9417-4 · Cited by 161 · see citing works

RRR-alpha-tocopheryl succinate-induced apoptosis of human breast cancer cells involves Bax translocation to mitochondria.

Yu, W., Sanders, B. G., & Kline, K. A. (2003) · PubMed · Cited by 146 · see citing works

Anaerobic Expression ofEscherichia coliSuccinate Dehydrogenase: Functional Replacement of Fumarate Reductase in the Respiratory Chain during Anaerobic Growth

Maklashina, E., Berthold, D. A., & Cecchini, G. (1998) · Journal of Bacteriology · doi:10.1128/jb.180.22.5989-5996.1998 · Cited by 144 · see citing works

Progress in understanding structure-function relationships in respiratory chain complex II.

Ackrell, B. A. C. (2000) · FEBS Letters · doi:10.1016/s0014-5793(99)01749-4 · Cited by 144 · see citing works

Small mitochondria-targeting molecules as anti-cancer agents

Wang, F., Ogasawara, M. A., & Huang, P. (2009) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2009.12.003 · Cited by 143 · see citing works

Assembly factors of human mitochondrial complex I and their defects in disease

McKenzie, M., & Ryan, M. T. (2010) · IUBMB Life · doi:10.1002/iub.335 · Cited by 139 · see citing works

Vitamin E inhibits melanoma growth in mice

Malafa, M. P., Fokum, F. D., Mowlavi, A., Abusief, M., & King, M. (2002) · Surgery · doi:10.1067/msy.2002.119191 · Cited by 136 · see citing works

Reactive Oxygen Species and p38 Mitogen-Activated Protein Kinase Activate Bax to Induce Mitochondrial Cytochrome c Release and Apoptosis in Response to Malonate

Gómez-Lázaro, M., Galindo, M. F., de Mera, R. M. M.-F., Fernández-Gómez, F.-J., Concannon, C. G., Segura, M. F., Comella, J. X., Prehn, J. H. M., & Jordán, J. (2006) · Molecular Pharmacology · doi:10.1124/mol.106.030718 · Cited by 136 · see citing works

Inhibitors of succinate: quinone reductase/complex II regulate production of mitochondrial reactive oxygen species and protect normal cells from ischemic damage but induce specific cancer cell death

Ralph, S. J., Moreno-Sánchez, R., Neuzil, J., & Rodríguez-Enríquez, S. (2011) · Pharmaceutical Research · doi:10.1007/s11095-011-0566-7 · Cited by 126 · see citing works

α‐Tocopheryl succinate‐induced apoptosis in Jurkat T cells involves caspase‐3 activation, and both lysosomal and mitochondrial destabilisation

Neužil, J., Svensson, I., Weber, T., Weber, C., & Brunk, U. T. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00141-6 · Cited by 126 · see citing works

Vitamin E and Breast Cancer

Kline, K. A., Yu, W., & Sanders, B. G. (2004) · Journal of Nutrition · doi:10.1093/jn/134.12.3458s · Cited by 126 · see citing works

Suppression of Tumor GrowthIn vivoby the Mitocan α-tocopheryl Succinate Requires Respiratory Complex II

Dong, L., Freeman, R., Liu, J., Zobalová, R., Marín‐Hernández, Á., Stantic, M., Rohlena, J., Vališ, K., Rodríguez‐Enríquez, S., Butcher, B., et al. (2009) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-08-2439 · Cited by 125 · see citing works

Mitocans as anti-cancer agents targeting mitochondria: lessons from studies with vitamin E analogues, inhibitors of complex II

Neužil, J., Dyason, J. C., Freeman, R., Dong, L., Procházka, L., Wang, X., Scheffler, I. E., & Ralph, S. J. (2007) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-006-9060-z · Cited by 124 · see citing works

Aerobic glycolysis in cancers: Implications for the usability of oxygen‐responsive genes and fluorodeoxyglucose‐PET as markers of tissue hypoxia

Busk, M., Horsman, M. R., Kristjansen, P. E. G., van der Kogel, A. J., Bussink, J., & Overgaard, J. (2008) · International Journal of Cancer · doi:10.1002/ijc.23449 · Cited by 123 · see citing works

FLX1 Codes for a Carrier Protein Involved in Maintaining a Proper Balance of Flavin Nucleotides in Yeast Mitochondria

Tzagoloff, A., Jang, J., Glerum, D. M., & Wu, M. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.13.7392 · Cited by 120 · see citing works

Reactivating HIF prolyl hydroxylases under hypoxia results in metabolic catastrophe and cell death

Tennant, D. A., Frezza, C., MacKenzie, E. D., Nguyen, Q., Zheng, L., Selak, M. A., Roberts, D. L., Dive, C., Watson, D. G., Aboagye, E. O., et al. (2009) · Oncogene · doi:10.1038/onc.2009.250 · Cited by 117 · see citing works

Germline SDHx variants modify breast and thyroid cancer risks in Cowden and Cowden-like syndrome via FAD/NAD-dependant destabilization of p53

Ni, Y., He, X., Chen, J., Moline, J., Mester, J. L., Orloff, M. S., Ringel, M. D., & Eng, C. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr459 · Cited by 115 · see citing works

α-Tocopheryl succinate, an agent with in vivo anti-tumour activity, induces apoptosis by causing lysosomal instability

Neužil, J., Zhao, M., Ostermann, G., Štícha, M., Gellert, N., Weber, C., Eaton, J. W., & Brunk, U. T. (2002) · Biochemical Journal · doi:10.1042/bj3620709 · Cited by 114 · see citing works

α-Tocopheryl Succinate Induces Apoptosis in Prostate Cancer Cells in Part through Inhibition of Bcl-xL/Bcl-2 Function

Shiau, C.-W., Huang, J.-W., Wang, D.-S., Weng, J.-R., Yang, C.-C., Lin, C.-H., Li, C., & Chen, C.-S. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m511015200 · Cited by 113 · see citing works

3-bromopyruvate (3BP) a fast acting, promising, powerful, specific, and effective “small molecule” anti-cancer agent taken from labside to bedside: introduction to a special issue

Pedersen, P. L. (2012) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-012-9425-4 · Cited by 112 · see citing works

α-Tocopheryl Succinate Inhibits Malignant Mesothelioma byDisrupting the Fibroblast Growth Factor Autocrine Loop

Stapelberg, M., Gellert, N., Swettenham, E., Tomasetti, M., Witting, P. K., Procopio, A. D., & Neužil, J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414498200 · Cited by 112 · see citing works

Effect of α-Tocopherol Succinate on Free Radical and Lipid Peroxidation Levels in BL6 Melanoma Cells

Ottino, P., & Duncan, J. R. (1997) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(96)00529-1 · Cited by 107 · see citing works

The complex II inhibitor atpenin A5 protects against cardiac ischemia-reperfusion injury via activation of mitochondrial KATP channels

Wojtovich, A. P., & Brookes, P. S. (2009) · Basic Research in Cardiology · doi:10.1007/s00395-009-0001-y · Cited by 107 · see citing works

Mitochondrial targeting of α-tocopheryl succinate enhances its pro-apoptotic efficacy: A new paradigm for effective cancer therapy

Dong, L., Jameson, V. J. A., Tilly, D., Procházka, L., Rohlena, J., Vališ, K., Truksa, J., Zobalová, R., Mahdavian, E., Kľučková, K., et al. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.02.032 · Cited by 105 · see citing works

Vitamin E Analogues Inhibit Angiogenesis by Selective Induction of Apoptosis in Proliferating Endothelial Cells: The Role of Oxidative Stress

Dong, L., Swettenham, E., Eliasson, J., Wang, X., Gold, M., Medunic, Y., Stantic, M., Low, P., Procházka, L., Witting, P. K., et al. (2007) · Cancer Research · doi:10.1158/0008-5472.can-07-3034 · Cited by 102 · see citing works

A Peptide Conjugate of Vitamin E Succinate Targets Breast Cancer Cells with High ErbB2 Expression

Wang, X., Birringer, M., Dong, L., Vepřek, P., Low, P., Swettenham, E., Stantic, M., Yuan, L., Zobalová, R., Wu, K., et al. (2007) · Cancer Research · doi:10.1158/0008-5472.can-06-2480 · Cited by 99 · see citing works

Extra-adrenal and adrenal pheochromocytomas associated with a germline SDHC mutation

Pęczkowska, M., Cascón, A., Prejbisz, A., Kubaszek, A., Ćwikła, J. B., Furmanek, M. I., Erlic, Z., Eng, C., Januszewicz, A., & Neumann, H. P. H. (2008) · Nature Clinical Practice Endocrinology &#38 Metabolism · doi:10.1038/ncpendmet0726 · Cited by 99 · see citing works

Cells Silenced for SDHB Expression Display Characteristic Features of the Tumor Phenotype

Cervera, A. M., Apostolova, N., Crespo, F. L., Mata, M., & McCreath, K. J. (2008) · Cancer Research · doi:10.1158/0008-5472.can-07-5580 · Cited by 98 · see citing works

Hippo/Mst1 Stimulates Transcription of the Proapoptotic Mediator NOXA in a FoxO1-Dependent Manner

Vališ, K., Procházka, L., Bouřa, E., Chladova, J., Obšil, T., Rohlena, J., Truksa, J., Dong, L., Ralph, S. J., & Neužil, J. (2011) · Cancer Research · doi:10.1158/0008-5472.can-10-2203 · Cited by 95 · see citing works

Role of reactive oxygen species in the induction of apoptosis by α‐tocopheryl succinate

Kang, Y., Lee, E., Choi, M., Ku, J., Kim, S. H., Park, Y., & Lim, S. (2004) · International Journal of Cancer · doi:10.1002/ijc.20424 · Cited by 92 · see citing works

Anticancer Drugs Targeting the Mitochondrial Electron Transport Chain

Rohlena, J., Dong, L.-F., Ralph, S. J., & Neuzil, J. (2011) · Antioxidants &amp; Redox Signaling · doi:10.1089/ars.2011.3990 · Cited by 91 · cited 7× · see citing works

Mitochondrial fumarate reductase as a target of chemotherapy: From parasites to cancer cells

Sakai, C., Tomitsuka, E., Esumi, H., Harada, S., & Kita, K. (2011) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2011.12.013 · Cited by 91 · see citing works

Two Hydrophobic Subunits Are Essential for the Heme b Ligation and Functional Assembly of Complex II (Succinate-Ubiquinone Oxidoreductase) from Escherichia coli

Nakamura, K., Yamaki, M., Sarada, M., Nakayama, S., Vibat, C. R. T., Gennis, R. B., Nakayashiki, T., Inokuchi, H., Kojima, S., & Kita, K. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.1.521 · Cited by 90 · see citing works

Mechanism of Thiazolidinedione-Dependent Cell Death in Jurkat T Cells

Soller, M., Dröse, S., Brandt, U., Brüne, B., & von Knethen, A. (2007) · Molecular Pharmacology · doi:10.1124/mol.107.034371 · Cited by 89 · see citing works

Assembly factors as a new class of disease genes for mitochondrial complex I deficiency: cause, pathology and treatment options

Nouws, J., Nijtmans, L. G. J., Smeitink, J. A. M., & Vogel, R. O. (2011) · Brain · doi:10.1093/brain/awr261 · Cited by 87 · see citing works

The Saccharomyces cerevisiae TCM62 Gene Encodes a Chaperone Necessary for the Assembly of the Mitochondrial Succinate Dehydrogenase (Complex II)

Dibrov, E., Fu, S., & Lemire, B. D. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.48.32042 · Cited by 82 · see citing works

Dietary Administration of the Proapoptotic Vitamin E Analogue α-Tocopheryloxyacetic Acid Inhibits Metastatic Murine Breast Cancer

Hahn, T., Szabó, L., Gold, M., Ramanathapuram, L. V., Hurley, L. H., & Akporiaye, E. T. (2006) · Cancer Research · doi:10.1158/0008-5472.can-06-2403 · Cited by 77 · see citing works

Mitochondrial Electron Transport Inhibitors Cause Lipid Peroxidation-Dependent and -Independent Cell Death: Protective Role of Antioxidants

Zhang, G., Tirmenstein, M. A., Nicholls-Grzemski, F. A., & Fariss, M. W. (2001) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2001.2486 · Cited by 75 · see citing works

The Tumor Suppressor cybL, a Component of the Respiratory Chain, Mediates Apoptosis Induction

Albayrak, T., Scherhammer, V., Schoenfeld, N., Braziulis, E., Mund, T., Bauer, M. K. A., Scheffler, I. E., & Grimm, S. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-10-0631 · Cited by 75 · see citing works

Pheochromocytoma and Paraganglioma

Kantorovich, V., & Pacák, K. (2010) · Progress in brain research · doi:10.1016/s0079-6123(10)82015-1 · Cited by 75 · see citing works

Cancer complexity slows quest for cure

Hayden, E. C. (2008) · Nature · doi:10.1038/455148a · Cited by 74 · see citing works

(+)α-Tocopheryl succinate inhibits the mitochondrial respiratory chain complex I and is as effective as arsenic trioxide or ATRA against acute promyelocytic leukemia in vivo

dos Santos, G. A., Lima, R. S., Pestana, C. R., Lima, A. S., Scheucher, P. S., Thomé, C. H., Teixeira, H. L. G., Santana-Lemos, B. A. A., Lucena-Araujo, A. R., Rodrigues, F. P., et al. (2011) · Leukemia · doi:10.1038/leu.2011.216 · Cited by 73 · see citing works

Troglitazone: the discovery and development of a novel therapy for the treatment of Type 2 diabetes mellitus

Parker, J. C. (2002) · Advanced Drug Delivery Reviews · doi:10.1016/s0169-409x(02)00093-5 · Cited by 69 · see citing works

Differential Response of Human Ovarian Cancer Cells to Induction of Apoptosis by Vitamin E Succinate and Vitamin E Analogue, α-TEA

Anderson, K., Simmons-Menchaca, M., Lawson, K. A., Atkinson, J., Sanders, B. G., & Kline, K. A. (2004) · Cancer Research · doi:10.1158/0008-5472.can-03-2327 · Cited by 69 · see citing works

Mitochondria as Therapeutic Targets for the Treatment of Malignant Disease

Fulda, S., & Kroemer, G. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4078 · Cited by 65 · see citing works

A common mechanism links differently acting complex II inhibitors to cardioprotection: modulation of mitochondrial reactive oxygen species production

Dröse, S., Bleier, L., & Brandt, U. (2011) · Molecular Pharmacology · doi:10.1124/mol.110.070342 · Cited by 64 · see citing works

SdhE Is a Conserved Protein Required for Flavinylation of Succinate Dehydrogenase in Bacteria

McNeil, M. B., Clulow, J. S., Wilf, N. M., Salmond, G. P. C., & Fineran, P. C. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.293803 · Cited by 63 · see citing works

Identification of the flavoprotein of succinate dehydrogenase and aconitase as in vitro mitochondrial substrates of Fgr tyrosine kinase

Salvi, M., MORRICE, N. A., Brunati, A. M., & Toninello, A. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.11.005 · Cited by 61 · see citing works

Redox stress is not essential for the pseudo-hypoxic phenotype of succinate dehydrogenase deficient cells

Selak, M. A., Durán, R. V., & Gottlieb, E. (2006) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2006.05.015 · Cited by 59 · see citing works

Involvement of Ca2+ and ROS in α‐tocopheryl succinate‐induced mitochondrial permeabilization

Gogvadze, V. G., Norberg, E., Orrenius, S., & Zhivotovsky, B. (2010) · International Journal of Cancer · doi:10.1002/ijc.25204 · Cited by 59 · see citing works

Vitamin E succinate induced apoptosis and enhanced chemosensitivity to paclitaxel in human bladder cancer cells in vitro and in vivo

Kanai, K., Kikuchi, E., Mikami, S., Suzuki, E., Uchida, Y., Kodaira, K., Miyajima, A., Ohigashi, T., Nakashima, J., & Oya, M. (2009) · Cancer Science · doi:10.1111/j.1349-7006.2009.01362.x · Cited by 59 · see citing works

Mzm1 Influences a Labile Pool of Mitochondrial Zinc Important for Respiratory Function

Atkinson, A. E., Khalimonchuk, O., Smith, P. M., Sabic, H., Eide, D. J., & Winge, D. R. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.109793 · Cited by 57 · see citing works

Atpenins, new antifungal antibiotics produced by Penicillium sp. Production, isolation, physico-chemical and biological properties.

Ōmura, S., Tomoda, H., Kimura, K. B., ZHENT, D.-Z., Kumagai, H., Igarashi, K., Imamura, N., Takahashi, Y., Tanaka, Y., & IWAI, Y. (1988) · The Journal of Antibiotics · doi:10.7164/antibiotics.41.1769 · Cited by 56 · see citing works

α-Tocopheryl succinate and TRAIL selectively synergise in induction of apoptosis in human malignant mesothelioma cells

Tomasetti, M., Rippo, M. R., Alleva, R., Moretti, S., Anděra, L., Neužil, J., & Procopio, A. D. (2004) · British Journal of Cancer · doi:10.1038/sj.bjc.6601707 · Cited by 56 · see citing works

Vitamin E analogues as inducers of apoptosis: implications for their potential antineoplastic role

Neužil, J., Weber, T., Terman, A., Weber, C., & Brunk, U. T. (2001) · Redox Report · doi:10.1179/135100001101536247 · Cited by 55 · see citing works

A vitamin E analogue suppresses malignant mesothelioma in a preclinical model: A future drug against a fatal neoplastic disease?

Tomasetti, M., Gellert, N., Procopio, A. D., & Neužil, J. (2004) · International Journal of Cancer · doi:10.1002/ijc.20062 · Cited by 54 · see citing works

α-TEA Plus Cisplatin Reduces Human Cisplatin-Resistant Ovarian Cancer Cell Tumor Burden and Metastasis

Anderson, K., Lawson, K. A., Simmons-Menchaca, M., Sun, L., Sanders, B. G., & Kline, K. A. (2004) · Experimental Biology and Medicine · doi:10.1177/153537020422901112 · Cited by 53 · see citing works

α-Tocopheryl succinate causes mitochondrial permeabilization by preferential formation of Bak channels

Procházka, L., Dong, L., Vališ, K., Freeman, R., Ralph, S. J., Tuřánek, J., & Neužil, J. (2010) · APOPTOSIS · doi:10.1007/s10495-010-0482-z · Cited by 53 · see citing works

Leucinostatin A inhibits prostate cancer growth through reduction of insulin‐like growth factor‐I expression in prostate stromal cells

Kawada, M., Inoue, H., Ohba, S., Masuda, T., Momose, I., & Ikeda, D. (2009) · International Journal of Cancer · doi:10.1002/ijc.24915 · Cited by 53 · see citing works

Genomic instability induced by mutant succinate dehydrogenase subunit D (SDHD) is mediated by O2-• and H2O2

Owens, K. M., Aykin‐Burns, N., Dayal, D., Coleman, M. C., Domann, F. E., & Spitz, D. R. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.10.435 · Cited by 52 · see citing works

Hypoxia and succinate antagonize 2-deoxyglucose effects on glioblastoma

Pistollato, F., Abbadi, S., Rampazzo, E., Viola, G., Puppa, A. D., Cavallini, L., Frasson, C., Persano, L., Panchision, D. M., & Basso, G. (2010) · Biochemical Pharmacology · doi:10.1016/j.bcp.2010.08.003 · Cited by 51 · see citing works

Vitamin E succinate suppresses prostate tumor growth by inducing apoptosis

Malafa, M. P., Fokum, F. D., Andoh, J., Neitzel, L. T., Bandyopadhyay, S., Zhan, R., Iiizumi, M., Furuta, E., Horvath, E., & Watabe, K. (2005) · International Journal of Cancer · doi:10.1002/ijc.21689 · Cited by 49 · see citing works

α-Tocopheryl succinate, an agent with in vivo anti-tumour activity, induces apoptosis by causing lysosomal instability

Neužil, J., Zhao, M., Ostermann, G., Štícha, M., Gellert, N., Weber, C., Eaton, J. W., & Brunk, U. T. (2002) · Biochemical Journal · doi:10.1042/0264-6021:3620709 · Cited by 49 · see citing works

Vitamin E Succinate Decreases Lung Cancer Tumor Growth in Mice

Quin, J. A., Engle, D. L., Litwiller, A. R., Peralta, E. A., Grasch, A. L., Boley, T. M., & Hazelrigg, S. R. (2005) · Journal of Surgical Research · doi:10.1016/j.jss.2005.01.014 · Cited by 48 · see citing works

Reaction site of carboxanilides and of thenoyltrifluoroacetone in complex II.

Ramsay, R. R., Ackrell, B. A. C., Coles, C. J., Singer, T. P., White, G. A., & Thorn, G. D. (1981) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.78.2.825 · Cited by 47 · see citing works

Up-regulation of hexokinaseII in myeloma cells: targeting myeloma cells with 3-bromopyruvate

Nakano, A., Miki, H., Nakamura, S., Harada, T., Oda, A., Amou, H., Fujii, S., Kagawa, K., Takeuchi, K., Ozaki, S., et al. (2012) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-012-9412-9 · Cited by 46 · see citing works

Effect of the antitumoral alkylating agent 3-bromopyruvate on mitochondrial respiration: role of mitochondrially bound hexokinase

Rodrigues-Ferreira, C., da Silva, A. P. P., & Galina, A. (2012) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-012-9413-8 · Cited by 44 · see citing works

New atpenins, NBRI23477 A and B, inhibit the growth of human prostate cancer cells

Kawada, M., Momose, I., Someno, T., Tsujiuchi, G., & Ikeda, D. (2009) · The Journal of Antibiotics · doi:10.1038/ja.2009.20 · Cited by 36 · see citing works

Warburg Effect’s Manifestation in Aggressive Pheochromocytomas and Paragangliomas: Insights from a Mouse Cell Model Applied to Human Tumor Tissue

Fliedner, S. M. J., Kaludercic, N., Jiang, X.-S., Hansíková, H., Hájková, Z., Sládková, J., Limpuangthip, A., Backlund, P. S., WESLEY, R. A., Martiniova, L., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0040949 · Cited by 34 · see citing works

Targeting cholesterol-rich microdomains to circumvent tamoxifen-resistant breast cancer

Tiwary, R., Yu, W., deGraffenried, L. A., Sanders, B. G., & Kline, K. A. (2011) · Breast Cancer Research · doi:10.1186/bcr3063 · Cited by 32 · see citing works

The chaperonin‐related protein Tcm62p ensures mitochondrial gene expresssion under heat stress

Klanner, C., Neupert, W., & Langer, T. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)01322-3 · Cited by 31 · see citing works

Coenzyme Q: Reversal of Inhibition of Succinate Cytochrome c Reductase by Lipophilic Compounds

Takemori, S., & King, T. E. (1964) · Science · doi:10.1126/science.144.3620.852 · Cited by 29 · see citing works

Succinate dehydrogenase flavoprotein subunit expression in Saccharomyces cerevisiae– involvement of the mitochondrial FAD transporter, Flx1p

Giancaspero, T. A., Wait, R., Boles, E., & Barile, M. (2008) · FEBS Journal · doi:10.1111/j.1742-4658.2008.06270.x · Cited by 26 · see citing works

Mitochondrial Toxins in Basal Ganglia Disorders: From Animal Models to Therapeutic Strategies

Bonsi, P., Cuomo, D., Martella, G., Sciamanna, G., Tolu, M., Calabresi, P., Bernardi, G., & Pisani, A. (2005) · Current Neuropharmacology · doi:10.2174/157015906775203039 · Cited by 26 · see citing works

Mechanism of action of atpenin b on raji cells.

Oshino, K., KUMAGAI, H., Tomoda, H., & Ōmura, S. (1990) · The Journal of Antibiotics · doi:10.7164/antibiotics.43.1064 · Cited by 24 · see citing works

α‐Tocopheryloxyacetic acid is superior to α‐tocopheryl succinate in suppressing HER2‐high breast carcinomas due to its higher stability

Dong, L., Grant, G. D., Massa, H. M., Zobalová, R., Akporiaye, E. T., & Neužil, J. (2011) · International Journal of Cancer · doi:10.1002/ijc.26489 · Cited by 24 · see citing works

Vitamin E Protects against Lipid Peroxidation and Rescues Tumorigenic Phenotypes in Cowden/Cowden-like Patient-Derived Lymphoblast Cells with Germline SDHx Variants

Ni, Y., & Eng, C. (2012) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-12-1055 · Cited by 23 · see citing works

Kinetics of ubiquinone reduction by the resolved succinate: Ubiquinone reductase

Grivennikova, V. G., & Vinogradov, A. D. (1982) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(82)90065-2 · Cited by 18 · see citing works

Stereoselective Total Synthesis of Atpenins A4 and B, Harzianopyridone, and NBRI23477 B

Ohtawa, M., Sugiyama, K., Hiura, T., Izawa, S., Shiomi, K., Ōmura, S., & Nagamitsu, T. (2012) · Chemical and Pharmaceutical Bulletin · doi:10.1248/cpb.c12-00266 · Cited by 15 · see citing works

Synthetic atpenin analogs: Potent mitochondrial inhibitors of mammalian and fungal succinate-ubiquinone oxidoreductase

Selby, T. P., Hughes, K. A., Rauh, J. J., & Hanna, W. S. (2010) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2010.01.066 · Cited by 13 · see citing works

3-Nitropropionic Acid Is a Suicide Inhibitor of Mitochondrial Respiration That, upon Oxidation by Complex II, Forms a Covalent Adduct with a Catalytic Base Arginine in the Active Site of the Enzyme

Huang, L.-S., Sun, G., Cobessi, D., Wang, A. C., Shen, J. T., Tung, E. Y., Anderson, V. E., & Berry, E. A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m511270200 · Cited by 10 · see citing works

Revealing human disease genes through analysis of the yeast mitochondrial proteome

Hao, H.-X., & Rutter, J. P. (2009) · Cell Cycle · doi:10.4161/cc.8.24.10205 · Cited by 7 · see citing works

Mitochondrial complex ii: At the crossroads

Bezawork-Geleta, A., Rohlena, J., Dong, L., Pacak, K., & Neuzil, J. (2017) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2017.01.003 · Cited by 295 · see citing works

Oncogenic pathways and the electron transport chain: a dangeROS liaison

Raimondi, V., Ciccarese, F., & Ciminale, V. (2019) · British Journal of Cancer · doi:10.1038/s41416-019-0651-y · Cited by 225 · see citing works

Regulation of succinate dehydrogenase and role of succinate in cancer

Dalla Pozza, E., Dando, I., Pacchiana, R., Liboi, E., Scupoli, M. T., Donadelli, M., & Palmieri, M. (2020) · Seminars in Cell &amp; Developmental Biology · doi:10.1016/j.semcdb.2019.04.013 · Cited by 212 · see citing works

Differential effects of complex II on mitochondrial ROS production and their relation to cardioprotective pre- and postconditioning

Dröse, S. (2013) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2013.01.004 · Cited by 201 · see citing works

Inhibition of Mitochondrial Complex II by the Anticancer Agent Lonidamine

Guo, L., Shestov, A. A., Worth, A. J., Nath, K., NELSON, D. S., Leeper, D. B., Glickson, J. D., & Blair, I. A. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.697516 · Cited by 181 · see citing works

The signaling pathways and therapeutic potential of itaconate to alleviate inflammation and oxidative stress in inflammatory diseases

Shi, X., Zhou, H., Wei, J., Mo, W., Li, Q., & Lv, X. (2022) · Redox Biology · doi:10.1016/j.redox.2022.102553 · Cited by 160 · see citing works

OXPHOS remodeling in high-grade prostate cancer involves mtDNA mutations and increased succinate oxidation

Schöpf, B., Weißensteiner, H., Schäfer, G., Fazzini, F., Charoentong, P., Naschberger, A., Rupp, B., Fendt, L., Bukur, V., Giese, I., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-15237-5 · Cited by 142 · see citing works

Iron metabolism and its contribution to cancer (Review)

Chen, Y., Fan, Z., Yang, Y., & Gu, C. (2019) · International Journal of Oncology · doi:10.3892/ijo.2019.4720 · Cited by 142 · see citing works

Q-site inhibitor induced ROS production of mitochondrial complex II is attenuated by TCA cycle dicarboxylates

Siebels, I., & Dröse, S. (2013) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2013.06.005 · Cited by 130 · see citing works

Succinate in the cancer–immune cycle

Jiang, S., & Yan, W. (2017) · Cancer Letters · doi:10.1016/j.canlet.2017.01.019 · Cited by 109 · see citing works

Adaptive Mitochondrial Reprogramming and Resistance to PI3K Therapy

Ghosh, J. C., Siegelin, M. D., Vaira, V., Faversani, A., Tavecchio, M., Chae, Y. C., Lisanti, S., Rampini, P. M., Giroda, M., Caino, M. C., et al. (2015) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/dju502 · Cited by 108 · see citing works

Inhibition of succinate dehydrogenase by the mitochondrial chaperone TRAP1 has anti-oxidant and anti-apoptotic effects on tumor cells

Guzzo, G., Sciacovelli, M., Bernardi, P., & Rasola, A. (2014) · Oncotarget · doi:10.18632/oncotarget.2472 · Cited by 97 · see citing works

Essentiality of Succinate Dehydrogenase in Mycobacterium smegmatis and Its Role in the Generation of the Membrane Potential Under Hypoxia

Pécsi, I., Hards, K., Ekanayaka, N., Berney, M., Hartman, T. E., Jacobs, W. R., & Cook, G. M. (2014) · mBio · doi:10.1128/mbio.01093-14 · Cited by 92 · see citing works

How does the metabolism of tumour cells differ from that of normal cells

Amoêdo, N. D., Valencia, J. P., Rodrigues, M. F., Galina, A., & Rumjanek, F. D. (2013) · Bioscience Reports · doi:10.1042/bsr20130066 · Cited by 85 · see citing works

Succinate metabolism: a promising therapeutic target for inflammation, ischemia/reperfusion injury and cancer

Zhang, W., & Lang, R. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1266973 · Cited by 78 · see citing works

Mitochondria: The metabolic switch of cellular oncogenic transformation

Tan, Y. Q., Zhang, X., Zhang, S., Zhu, T., Garg, M., Lobie, P. E., & Pandey, V. (2021) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2021.188534 · Cited by 75 · see citing works

Mitochondrially targeted vitamin E succinate efficiently kills breast tumour-initiating cells in a complex II-dependent manner

Yan, B., Stantic, M., Zobalová, R., Bezawork‐Geleta, A., Stapelberg, M., Štursa, J., Rohlenová, K., Dong, L., & Neužil, J. (2015) · BMC Cancer · doi:10.1186/s12885-015-1394-7 · Cited by 72 · see citing works

The natural compound gracillin exerts potent antitumor activity by targeting mitochondrial complex II

Min, H., Jang, H.-J., Park, K. H., Hyun, S. Y., Park, S. J., Kim, J. H., Son, J., Kang, S. S., & Lee, H. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-2041-z · Cited by 73 · see citing works

Ubiquinone-binding site mutagenesis reveals the role of mitochondrial complex II in cell death initiation

Kluckova, K., Sticha, M., Cerny, J., Mracek, T., Dong, L., Drahota, Z., Gottlieb, E., Neuzil, J., & Rohlena, J. (2015) · Cell Death &amp; Disease · doi:10.1038/cddis.2015.110 · Cited by 66 · see citing works

Survival-Associated Metabolic Genes in Human Papillomavirus-Positive Head and Neck Cancers

Prusinkiewicz, M. A., Gameiro, S. F., Ghasemi, F., Dodge, M. J., Zeng, P. Y., Maekebay, H., Barrett, J. W., Nichols, A. C., & Mymryk, J. S. (2020) · Cancers · doi:10.3390/cancers12010253 · Cited by 70 · see citing works

Role of tyrosine phosphorylation in modulating cancer cell metabolism

Taddei, M. L., Pardella, E., Pranzini, E., Raugei, G., & Paoli, P. D. (2020) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2020.188442 · Cited by 70 · see citing works

Targeting the Mitochondrial Metabolic Network: A Promising Strategy in Cancer Treatment

Frattaruolo, L., Brindisi, M., Curcio, R., Marra, F., Dolce, V., & Cappello, A. R. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21176014 · Cited by 66 · see citing works

Conformational profile, vibrational assignments, NLO properties and molecular docking of biologically active herbicide1,1-dimethyl-3-phenylurea

Haruna, K., Kumar, V. S., Mary, Y. S., Popoola, S. A., Thomas, R., Roxy, M. S., & Al‐Saadi, A. A. (2019) · Heliyon · doi:10.1016/j.heliyon.2019.e01987 · Cited by 61 · see citing works

Homopiperazine-rhodamine B adducts of triterpenoic acids are strong mitocans

Wolfram, R. K., Fischer, L., Kluge, R., Ströhl, D., Al‐Harrasi, A., & Csük, R. (2018) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2018.06.051 · Cited by 58 · see citing works

Chrysin as an Anti-Cancer Agent Exerts Selective Toxicity by Directly Inhibiting Mitochondrial Complex II and V in CLL B-lymphocytes

Salimi, A., Roudkenar, M. H., Seydi, E., Sadeghi, L., Mohseni, A., Pirahmadi, N., & Pourahmad, J. (2017) · Cancer Investigation · doi:10.1080/07357907.2016.1276187 · Cited by 57 · see citing works

Synthesis and Antineoplastic Evaluation of Mitochondrial Complex II (Succinate Dehydrogenase) Inhibitors Derived from Atpenin A5

Wang, H., Huwaimel, B., Verma, K., Miller, J. E., Germain, T., Kinarivala, N., Pappas, D., Brookes, P. S., & Trippier, P. C. (2017) · ChemMedChem · doi:10.1002/cmdc.201700196 · Cited by 52 · see citing works

Targeting the Redox Landscape in Cancer Therapy

Narayanan, D., Ma, S., & Özcelik, D. (2020) · Cancers · doi:10.3390/cancers12071706 · Cited by 54 · see citing works

Revealing various coupling of electron transfer and proton pumping in mitochondrial respiratory chain

Sun, F., Zhou, Q., Pang, X., Xu, Y., & Rao, Z. (2013) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2013.06.013 · Cited by 53 · see citing works

Mitochondrial Bioenergetics at the Onset of Drug Resistance in Hematological Malignancies: An Overview

Barbato, A., Scandura, G., Puglisi, F., Cambria, D., Spina, E. L., Palumbo, G. A., Lazzarino, G., Tibullo, D., Raimondo, F. D., Giallongo, C., et al. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.604143 · Cited by 53 · see citing works

Decoding Warburg's hypothesis: tumor-related mutations in the mitochondrial respiratory chain

García-Heredia, J. M., & Carnero, A. (2015) · Oncotarget · doi:10.18632/oncotarget.6057 · Cited by 51 · see citing works

Elevated Endogenous SDHA Drives Pathological Metabolism in Highly Metastatic Uveal Melanoma

Chattopadhyay, C., Oba, J., Roszik, J., Marszalek, J. R., Chen, K., Qi, Y., Eterovic, K. A., Robertson, A. G., Burks, J. K., McCannel, T. A., et al. (2019) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.19-28082 · Cited by 49 · see citing works

A novel agent exerts antitumor activity in breast cancer cells by targeting mitochondrial complex II

Wang, L., Zhang, X., Cui, G., Chan, J. Y., Li, C., Xu, C., Shan, L., Xu, C., Zhang, Q., Wang, Y., et al. (2016) · Oncotarget · doi:10.18632/oncotarget.8410 · Cited by 46 · see citing works

Iterative Catalysis in the Biosynthesis of Mitochondrial Complex II Inhibitors Harzianopyridone and Atpenin B

Bat-Erdene, U., Kanayama, D., Tan, D., Turner, W. C., Houk, K. N., Ōhashi, M., & Tang, Y. (2020) · Journal of the American Chemical Society · doi:10.1021/jacs.0c03438 · Cited by 46 · see citing works

Anticancer and antiangiogenic activity of surfactant-free nanoparticles based on self-assembled polymeric derivatives of vitamin E: structure-activity relationship.

Palao-Suay, R., Aguilar, M., Parra-Ruiz, F., Fernández-Gutiérrez, M., Parra, J., Sánchez-Rodríguez, C., Sanz-Fernández, R., Rodrigáñez, L., & Román, J. (2015) · Biomacromolecules · doi:10.1021/acs.biomac.5b00130 · Cited by 36 · see citing works

Exploring the mystery of tumor metabolism: Warburg effect and mitochondrial metabolism fighting side by side

Yu, Y., Jiang, Y., Glandorff, C., & Sun, M. (2024) · Cellular Signalling · doi:10.1016/j.cellsig.2024.111239 · Cited by 39 · see citing works

Gentamicin Affects the Bioenergetics of Isolated Mitochondria and Collapses the Mitochondrial Membrane Potential in Cochlear Sensory Hair Cells

O’Reilly, M., Young, L., Kirkwood, N. K., Richardson, G. P., Kros, C. J., & Moore, A. L. (2019) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2019.00416 · Cited by 38 · see citing works

Molecular pathogenesis of tumorigenesis caused by succinate dehydrogenase defect

Moosavi, B., Zhu, X., Yang, W., & Yang, G. (2019) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2019.151057 · Cited by 36 · see citing works

Computationally modeling mammalian succinate dehydrogenase kinetics identifies the origins and primary determinants of ROS production

Manhas, N., Duong, Q. V., Lee, P., Richardson, J. D., Robertson, J. D., Moxley, M. A., & Bazil, J. N. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.014483 · Cited by 35 · see citing works

Chromophore-Assisted Light Inactivation of Mitochondrial Electron Transport Chain Complex II in Caenorhabditis elegans

Wojtovich, A. P., Wei, A. Y., Sherman, T. A., Foster, T. H., & Nehrke, K. W. (2016) · Scientific Reports · doi:10.1038/srep29695 · Cited by 34 · see citing works

Co-delivery nanocarriers targeting folate receptor and encapsulating 2-deoxyglucose and α-tocopheryl succinate enhance anti-tumor effect in vivo

Lei, X., Li, K., Liu, Y., Wang, Z. Y., Ruan, B., Wang, L., An, X., Wu, D., & Lu, Z. (2017) · International Journal of Nanomedicine · doi:10.2147/ijn.s135849 · Cited by 34 · see citing works

Effects of copper and temperature on heart mitochondrial hydrogen peroxide production

Isei, M. O., & Kamunde, C. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2019.12.006 · Cited by 35 · see citing works

Mitochondria: A Galaxy in the Hematopoietic and Leukemic Stem Cell Universe

Panuzzo, C., Jovanovski, A., Pergolizzi, B., Pironi, L., Stanga, S., Fava, C., & Cilloni, D. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21113928 · Cited by 34 · see citing works

Mitochondria and the permeability transition pore in cancer metabolic reprogramming

Guo, L. (2021) · Biochemical Pharmacology · doi:10.1016/j.bcp.2021.114537 · Cited by 33 · see citing works

Inhibition of ERAD synergizes with FTS to eradicate pancreatic cancer cells

Du, R., Sullivan, D. K., Azizian, N. G., Liu, Y., & Li, Y. (2021) · BMC Cancer · doi:10.1186/s12885-021-07967-6 · Cited by 32 · see citing works

2-Methoxyestradiol Affects Mitochondrial Biogenesis Pathway and Succinate Dehydrogenase Complex Flavoprotein Subunit A in Osteosarcoma Cancer Cells

Górska‐Ponikowska, M., Kuban‐Jankowska, A., Eisler, S. A., Perricone, U., Bosco, G. L., Barone, G., & Nußberger, S. (2018) · Cancer Genomics & Proteomics · doi:10.21873/cgp.20067 · Cited by 31 · see citing works

Novel Mitochondria-Targeted Furocoumarin Derivatives as Possible Anti-Cancer Agents

Mattarei, A., Romio, M., Managò, A., Zoratti, M., Paradisi, C., Szabó, I., Leanza, L., & Biasutto, L. (2018) · Frontiers in Oncology · doi:10.3389/fonc.2018.00122 · Cited by 31 · see citing works

Complex I and II are required for normal mitochondrial Ca2+ homeostasis

Jaña, F., Bustos, G., Rivas, J., Cruz, P., Urra, F. A., Basualto-Alarcón, C., Sagredo, E. A., Ríos-Morales, M., Lovy, A., Dong, Z., et al. (2019) · Mitochondrion · doi:10.1016/j.mito.2019.07.004 · Cited by 31 · see citing works

NEK10 interactome and depletion reveal new roles in mitochondria

de Oliveira, A. P., Basei, F. L., Slepicka, P. F., Ferezin, C. D. C., Melo-Hanchuk, T. D., de Souza, E. E., Lima, T., dos Santos, V. T., Mendes, D., Silveira, L. R., et al. (2020) · Proteome Science · doi:10.1186/s12953-020-00160-w · Cited by 26 · see citing works

Vitamin E-facilitated carbon monoxide pro-drug nanomedicine for efficient light-responsive combination cancer therapy

Opoku‐Damoah, Y., Zhang, R., Ta, H. T., & Xu, Z. P. (2021) · Biomaterials Science · doi:10.1039/d1bm00941a · Cited by 29 · see citing works

Mitochondrial targeting of α-tocopheryl succinate enhances its anti-mesothelioma efficacy

Kovářová, J., Bajzíková, M., Vondrusová, M., Štursa, J., Goodwin, J., Nguyen, M. N., Zobalová, R., Pasdar, E. A., Truksa, J., Tomasetti, M., et al. (2013) · Redox Report · doi:10.1179/1351000213y.0000000064 · Cited by 29 · see citing works

Mitochondria: 3-bromopyruvate vs. mitochondria? A small molecule that attacks tumors by targeting their bioenergetic diversity

Galina, A. (2014) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2014.05.013 · Cited by 28 · see citing works

Bioisosteric Exchange of C‐Chloro and Methyl Substituents: Synthesis and Initial Biological Studies of Atpenin A5 Analogues

Krautwald, S., Nilewski, C., Mori, M., Shiomi, K., Ōmura, S., & Carreira, E. M. (2016) · Angewandte Chemie International Edition · doi:10.1002/anie.201511672 · Cited by 28 · see citing works

Succinate dehydrogenase complex subunit C: Role in cellular physiology and disease

Wang, Q., Li, M., Zeng, N., Zhou, Y., & Yan, J. (2023) · Experimental Biology and Medicine · doi:10.1177/15353702221147567 · Cited by 27 · see citing works

Melatonin and Docosahexaenoic Acid Decrease Proliferation of PNT1A Prostate Benign Cells via Modulation of Mitochondrial Bioenergetics and ROS Production

Tamarindo, G. H., Ribeiro, D. L., Gobbo, M. G., Guerra, L. H. A., Rahal, P., Taboga, S. R., Gadelha, F. R., & Góes, R. M. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/5080798 · Cited by 27 · see citing works

Succinate Accumulation Is Associated with a Shift of Mitochondrial Respiratory Control and HIF-1α Upregulation in PTEN Negative Prostate Cancer Cells

Weber, A., Klocker, H., Oberacher, H., Gnaiger, E., Neuwirt, H., Sampson, N., & Eder, I. E. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19072129 · Cited by 26 · see citing works

The Assembly Factor SDHAF2 Is Dispensable for Flavination of the Catalytic Subunit of Mitochondrial Complex II in Breast Cancer Cells

Bezawork‐Geleta, A., Dong, L., Rohlena, J., & Neužil, J. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.c116.755017 · Cited by 26 · see citing works

Two for the price of one: Attacking the energetic-metabolic hub of mycobacteria to produce new chemotherapeutic agents

Hards, K., Adolph, C., Harold, L. K., McNeil, M. B., Cheung, C., Jinich, A., Rhee, K. Y., & Cook, G. M. (2019) · Progress in Biophysics and Molecular Biology · doi:10.1016/j.pbiomolbio.2019.11.003 · Cited by 25 · see citing works

Coenzyme Q10 and nicotinamide nucleotide transhydrogenase: Sentinels for mitochondrial hydrogen peroxide signaling

Grayson, C., & Mailloux, R. J. (2023) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2023.08.015 · Cited by 22 · see citing works

Why to compare absolute numbers of mitochondria

Schmitt, S., Schulz, S., Schropp, E.-M., Eberhagen, C., Simmons, A., Beisker, W., Aichler, M., & Zischka, H. (2014) · Mitochondrion · doi:10.1016/j.mito.2014.06.005 · Cited by 22 · see citing works

Water-Soluble Vitamin E—Tocopheryl Phosphate

Zingg, J.-M. A. (2018) · Advances in food and nutrition research · doi:10.1016/bs.afnr.2017.12.007 · Cited by 22 · see citing works

BET inhibitors ( BETi ) influence oxidative phosphorylation metabolism by affecting mitochondrial dynamics leading to alterations in apoptotic pathways in triple‐negative breast cancer ( TNBC ) cells

Rossi, T., Iorio, E., Chirico, M., Pisanu, M. E., Amodio, N., Cantafio, M. E. G., Perrotta, I. D., Colciaghi, F., Fiorillo, M., Gianferrari, A., et al. (2024) · Cell Proliferation · doi:10.1111/cpr.13730 · Cited by 20 · see citing works

Glutamine Metabolism Mediates Sensitivity to Respiratory Complex II Inhibition in Acute Myeloid Leukemia

Roma, A., Tcheng, M., Ahmed, N., Walker, S., Jayanth, P., Minden, M. D., Hope, K. J., Rao, P. P. N., Luc, J., Doxey, A. C., et al. (2022) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-21-1032 · Cited by 21 · see citing works

Analysis of transcriptional profiles of Saccharomyces cerevisiae exposed to bisphenol A

Bereketoğlu, C., Arğa, K. Y., Eraslan, S., & Mertoğlu, B. (2016) · Current Genetics · doi:10.1007/s00294-016-0633-z · Cited by 21 · see citing works

Diverse Stakeholders of Tumor Metabolism: An Appraisal of the Emerging Approach of Multifaceted Metabolic Targeting by 3-Bromopyruvate

Yadav, S., Pandey, S. K., Goel, Y., Temre, M. K., & Singh, S. M. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.00728 · Cited by 19 · see citing works

Rapamycin as a potential treatment for succinate dehydrogenase deficiency

Fan, F., Sam, R., Ryan, E., Alvarado, K., & Villa-Cuesta, E. (2019) · Heliyon · doi:10.1016/j.heliyon.2019.e01217 · Cited by 19 · see citing works

Induction of Mitochondrial Cell Death and Reversal of Anticancer Drug Resistance via Nanocarriers Composed of a Triphenylphosphonium Derivative of Tocopheryl Polyethylene Glycol Succinate

Singh, Y., Viswanadham, K. K. D. R., Pawar, V. K., Meher, J. G., Jajoriya, A. K., Omer, A., Jaiswal, S., Dewangan, J., Bora, H. K., Singh, P. C., et al. (2019) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.9b00177 · Cited by 19 · see citing works

α-TOS-based RAFT block copolymers and their NPs for the treatment of cancer

Palao‐Suay, R., Aguilar, M. R., Parra-Ruiz, F. J., Maji, S., Hoogenboom, R., Rohner, N. A., Thomas, S. N., & Román, J. S. (2015) · Polymer Chemistry · doi:10.1039/c5py01811k · Cited by 19 · see citing works

Mitochondrially Targeted Nanoparticles Based on α‐TOS for the Selective Cancer Treatment

Palao‐Suay, R., Rodrigáñez, L., Aguilar, M. R., Sánchez‐Rodríguez, C., Parra, F., Fernández‐Gutiérrez, M., Parra, J., Riestra‐Ayora, J., Fernández, R. S., & Román, J. S. (2015) · Macromolecular Bioscience · doi:10.1002/mabi.201500265 · Cited by 18 · see citing works

Inhibition of mitochondrial glycerol-3-phosphate dehydrogenase by α-tocopheryl succinate

Rauchová, H., Vokurková, M., & Drahota, Z. (2014) · The International Journal of Biochemistry &amp; Cell Biology · doi:10.1016/j.biocel.2014.06.010 · Cited by 14 · see citing works

Potential candidates from marine and terrestrial resources targeting mitochondrial inhibition: Insights from the molecular approach

Mitra, S., Rauf, A., Sutradhar, H., Sadaf, S., Hossain, M. J., Soma, M. A., Emran, T. B., Ahmad, B., Aljohani, A. S. M., Abdulmonem, W. A., et al. (2022) · Comparative Biochemistry and Physiology Part C Toxicology & Pharmacology · doi:10.1016/j.cbpc.2022.109509 · Cited by 14 · see citing works

Genetic mutations affecting mitochondrial function in cancer drug resistance

Lee, C., Park, S., & Yoon, S. K. (2023) · Genes & Genomics · doi:10.1007/s13258-022-01359-1 · Cited by 15 · see citing works

The phloroglucinol calcitrinone A, a novel mitochondria-targeting agent, induces cell death in breast cancer cells

Gaafary, M. E., Saber, F. R., Mahrous, E. A., Ashour, R. M. S., Okba, M. M., Lu, J., Lang, S. J., Schmiech, M., Simmet, T., & Syrovets, T. (2022) · Food and Chemical Toxicology · doi:10.1016/j.fct.2022.112896 · Cited by 14 · see citing works

High Molecular Weight Forms of Mammalian Respiratory Chain Complex II

Kovářová, N., Mráček, T., Nůsková, H., Holzerová, E., Vrbacký, M., Pecina, P., Tauchmannová, K., Kľučková, K., Rohlena, J., Neužil, J., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0071869 · Cited by 14 · see citing works

ST1926 inhibits glioma progression through regulating mitochondrial complex II

De, L., Yuan, T., & Zheng, Y. (2020) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2020.110291 · Cited by 14 · see citing works

Malonate differentially affects cell survival and confers chemoresistance in cancer cells via the induction of p53-dependent autophagy

Cui, H., Zhu, B. T., Li, H., Meng, Y., Cai, M., Wang, H., Yuan, M., Zhong, X., Wang, B., Shan, H., et al. (2023) · Biochemical Pharmacology · doi:10.1016/j.bcp.2023.115950 · Cited by 13 · see citing works

Discovery of Halogenated Benzothiadiazine Derivatives with Anticancer Activity**

Huwaimel, B., Bhakta, M., Kulkarni, C. A., Milliken, A. S., Wang, F., Peng, A., Brookes, P. S., & Trippier, P. C. (2020) · ChemMedChem · doi:10.1002/cmdc.202000729 · Cited by 13 · see citing works

Shikonin impairs mitochondrial activity to selectively target leukemia cells

Roma, A., Tcheng, M., Ahmed, N., Walker, S., Jayanth, P., Minden, M. D., Reisz, J. A., D’Alessandro, A., Rohlena, J., & Spagnuolo, P. A. (2022) · Phytomedicine Plus · doi:10.1016/j.phyplu.2022.100300 · Cited by 11 · see citing works

Serum Succinate/Fumarate Ratio in Patients With Paraganglioma/Pheochromocytoma Attending an Endocrine Oncogenetic Unit

Bancel, L.-P., Masso, V., Dessein, A., Aubert, S., Leteurtre, E., Coppin, L., Odou, M., Cao, C. D., Cardot-Bauters, C., & Pigny, P. (2023) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/clinem/dgad109 · Cited by 10 · see citing works

Elevated oxygen consumption rate in response to acute low-glucose stress: Metformin restores rate to normal level

Williams, E. D., Rogers, S. C., Zhang, X., Azhar, G., & Wei, J. Y. (2015) · Experimental Gerontology · doi:10.1016/j.exger.2015.08.002 · Cited by 8 · see citing works

Red LED Photobiomodulates the Metabolic Activity of Odontoblast-Like Cells

de Almeida, L. D. F. D., Turrioni, A. P. S., Basso, F. G., Montoro, L. A., Costa, C. A. D. S., & Hebling, J. (2016) · Brazilian Dental Journal · doi:10.1590/0103-6440201600152 · Cited by 7 · see citing works

Bioisosteric Exchange of C‐Chloro and Methyl Substituents: Synthesis and Initial Biological Studies of Atpenin A5 Analogues

Krautwald, S., Nilewski, C., Mori, M., Shiomi, K., Ōmura, S., & Carreira, E. M. (2016) · Angewandte Chemie · doi:10.1002/ange.201511672 · Cited by 7 · see citing works

Vitamin E succinate mediated apoptosis by juxtaposing endoplasmic reticulum and mitochondria

Ray, M. N., Kiyofuji, M., Ozono, M., & Kogure, K. (2023) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2023.130485 · Cited by 6 · see citing works

Mitochondrial reactive oxygen species and complex II levels are associated with the outcome of hepatocellular carcinoma

WU, J., Zhao, F. L., Zhao, Y., & Guo, Z. (2015) · Oncology Letters · doi:10.3892/ol.2015.3621 · Cited by 6 · see citing works

Targeting mitochondrial complexes for cancer therapy

Osman, A. M., & Arabi, A. A. (2026) · Biochemical Pharmacology · doi:10.1016/j.bcp.2026.117695 · Cited by 5 · see citing works

In vivo antitumor activity of PHT-427 inhibitor-loaded polymeric nanoparticles in head and neck squamous cell carcinoma

Yanes‐Diaz, J., Palao‐Suay, R., Camacho, F. I., Riestra‐Ayora, J., Aguilar, M. R., Fernández, R. S., & Sánchez‐Rodríguez, C. (2025) · Drug Delivery · doi:10.1080/10717544.2024.2449376 · Cited by 5 · see citing works

Molecular mechanism of mitoquinol mesylate in mitigating the progression of hepatocellular carcinoma—in silico and in vivo studies

Sulaimon, L. A., Adisa, R. A., Samuel, T. A., Joel, I. Y., Ayankojo, A. G., Abdulkareem, F. B., & Olaniyi, T. O. (2021) · Journal of Cellular Biochemistry · doi:10.1002/jcb.29937 · Cited by 5 · see citing works

A N-(4-chlorophenyl)-γ-amino acid derivatives exerts in vitro anticancer activity on non-small cell lung carcinoma cells and enhances citosine arabinoside (AraC)-induced cell death via mitochondria-targeted pathway

Kavaliauskas, P., Žukauskas, Š., Anusevičius, K., Balandis, B., Vaickelionienė, R., Petraitis, V., & Mickevičius, V. (2021) · Results in Chemistry · doi:10.1016/j.rechem.2021.100193 · Cited by 5 · see citing works

Efficient identification of new small molecules targeting succinate dehydrogenase in non-small cell lung cancer

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Sobotka, O., Drahota, Z., Kučera, O., Endlicher, R., Rauchová, H., & Červinková, Z. (2015) · Physiological Research · doi:10.33549/physiolres.933219 · Cited by 3 · see citing works

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Kovářová, N., Mráček, T., Houštěk, J., & Nůsková, H. (2014) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2014.05.145

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Miklovicova, S. (2025) · Digital Repository (National Repository of Grey Literature)

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Kľučková, K., Neužil, J., & Rohlena, J. (2014) · Springer eBooks · doi:10.1007/978-94-017-8984-4_4

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Neužil, J., Dyason, J. C., Freeman, R., Dong, L., Procházka, L., Wang, X., Scheffler, I. E., & Ralph, S. J. (2007) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-006-9060-z · Cited by 124 · see citing works

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