Mitochondrial Complex II: At the Crossroads

Chromatin modifications and their function

Kouzarides, T. (2007) · Cell · doi:10.1016/j.cell.2007.02.005 · Cited by 10,883

Ischaemic accumulation of succinate controls reperfusion injury through mitochondrial ROS

Chouchani, E. T., Pell, V. R., Gaude, E., Aksentijević, D., Sundier, S. Y., Robb, E. L., Logan, A., Nadtochiy, S. M., Ord, E. N. J., Smith, A. C., et al. (2014) · Nature · doi:10.1038/nature13909 · Cited by 2,907

Succinate Dehydrogenase Supports Metabolic Repurposing of Mitochondria to Drive Inflammatory Macrophages

Mills, E. L., Kelly, B., Logan, A., Costa, A. S. H., Varma, M., Bryant, C. E., Tourlomousis, P., Däbritz, J. H. M., Gottlieb, E., Latorre, I., et al. (2016) · Cell · doi:10.1016/j.cell.2016.08.064 · Cited by 2,291

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 · cited 1×

Itaconate Links Inhibition of Succinate Dehydrogenase with Macrophage Metabolic Remodeling and Regulation of Inflammation

Lampropoulou, V., Sergushichev, A., Bambousková, M., Nair, S., Vincent, E. E., Loginicheva, E., Cervantes‐Barragán, L., Ma, X., Huang, S. C., Griss, T., et al. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.06.004 · Cited by 1,583

Substrate and Functional Diversity of Lysine Acetylation Revealed by a Proteomics Survey

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Sirt5 Is a NAD-Dependent Protein Lysine Demalonylase and Desuccinylase

Du, J., Zhou, Y., Su, X., Yu, J. J., Khan, S., Jiang, H., Kim, J., Woo, J., Kim, J. H., Choi, B. H., et al. (2011) · Science · doi:10.1126/science.1207861 · Cited by 1,429

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 & Development · doi:10.1101/gad.191056.112 · Cited by 1,188

Mitochondrial generation of superoxide and hydrogen peroxide as the source of mitochondrial redox signaling

Brand, M. D. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.04.001 · Cited by 1,063

Role of TET enzymes in DNA methylation, development, and cancer

Rasmussen, K. D., & Helin, K. (2016) · Genes & Development · doi:10.1101/gad.276568.115 · Cited by 1,040 · cited 2×

Anti-aging effects of chlorpropamide depend on mitochondrial complex-II and the production of mitochondrial reactive oxygen species

Mao, Z., Liu, W., Huang, Y., Sun, T., Bao, K., Feng, J., Moskalev, A., Hu, Z., & Li, J. (2021) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2021.08.007 · Cited by 27

Upregulation of Succinate Dehydrogenase (SDHA) Contributes to Enhanced Bioenergetics of Ovarian Cancer Cells and Higher Sensitivity to Anti-Metabolic Agent Shikonin

Wang, L., Cybula, M., Rostworowska, M., Wang, L., Mucha, P. T., Bulicz, M., & Bieniasz, M. (2022) · Cancers · doi:10.3390/cancers14205097 · Cited by 25

STAT3 modulates CD4 +T mitochondrial dynamics and function in aging

Zukowski, E., Sannella, M., Rockhold, J. D., Kalantar, G. H., Yu, J., Calvo, S. S.-C., Kuhn, M. K., Hah, N., Ouyang, L., Wang, T., et al. (2023) · Aging Cell · doi:10.1111/acel.13996 · Cited by 22

The spectrum of neurological manifestations in myeloma.

Camacho, J. E., Arnalich, F., Anciones, B., Peña, J. M., Gil, Á., Barbado, F. J., Puig, J. G., & Vázquez, J. J. (1985) · PubMed · Cited by 24

Crystallographic investigation of the ubiquinone binding site of respiratory Complex II and its inhibitors

Huang, L.-S., Lümmen, P., & Berry, E. A. (2021) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2021.140679 · Cited by 26

Metabolic Sex Dimorphism of the Brain at the Gene, Cell, and Tissue Level

Lee, J. W., Profant, M. R., & Wang, C. (2022) · The Journal of Immunology · doi:10.4049/jimmunol.2100853 · Cited by 25

IFI27 Integrates Succinate and Fatty Acid Oxidation to Promote Adipocyte Thermogenic Adaption

Cui, X., Liu, H., Shi, T., Zhao, Q., Li, F., Lv, W., Yu, C. Y., Huang, H., Tang, Q., & Pan, D. (2023) · Advanced Science · doi:10.1002/advs.202301855 · Cited by 22

Caffeic Acid Phenethyl Ester Protects Kidney Mitochondria against Ischemia/Reperfusion Induced Injury in an In Vivo Rat Model

Kamarauskaitė, J., Banienė, R., Trumbeckas, D., Strazdauskas, A., & Trumbeckaitė, S. (2021) · Antioxidants · doi:10.3390/antiox10050747 · Cited by 24

Drp1 controls complex II assembly and skeletal muscle metabolism by Sdhaf2 action on mitochondria

Zhou, Z., Ma, A., Moore, T. M., Wolf, D. M., Yang, N. L., Tran, P. H., Segawa, M., Strumwasser, A. R., Ren, W., Fu, K., et al. (2024) · Science Advances · doi:10.1126/sciadv.adl0389 · Cited by 22

SDH defective cancers: molecular mechanisms and treatment strategies

Wang, J., Yuan, T., Yang, B. W., He, Q., & Zhu, H. (2025) · Cell Biology and Toxicology · doi:10.1007/s10565-025-10022-w · Cited by 24

A novel target-site mutation (H146Q) outside the ubiquinone binding site of succinate dehydrogenase confers high levels of resistance to cyflumetofen and pyflubumide in Tetranychus urticae

İnak, E., Rouck, S. D., Demirci, B., Dermauw, W., Geibel, S., & Leeuwen, T. V. (2024) · Insect Biochemistry and Molecular Biology · doi:10.1016/j.ibmb.2024.104127 · Cited by 21

Mitochondrial function is impaired in the primary visual cortex in an experimental glaucoma model

Arana, A. G. H., Vitar, R. M. L., Reides, C. G., Calabró, V., Marchini, T., Lerner, S. F., Evelson, P., & Ferreira, S. M. (2021) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2021.108815 · Cited by 21

Exploring the Leukemogenic Potential of GATA-1S, the Shorter Isoform of GATA-1: Novel Insights into Mechanisms Hampering Respiratory Chain Complex II Activity and Limiting Oxidative Phosphorylation Efficiency

Trombetti, S., Sessa, R., Catapano, R., Rinaldi, L., Bianco, A. L., Feliciello, A., Izzo, P., & Grosso, M. (2021) · Antioxidants · doi:10.3390/antiox10101603 · Cited by 21

SDHA Germline Mutations in SDH-Deficient GISTs: A Current Update

Schipani, A., Nannini, M., Astolfi, A., & Pantaleo, M. A. (2023) · Genes · doi:10.3390/genes14030646 · Cited by 21

Effects of melatonin on cardiac metabolic reprogramming in doxorubicin‐induced heart failure rats: A metabolomics study for potential therapeutic targets

Thonusin, C., Nawara, W., Arinno, A., Khuanjing, T., Prathumsup, N., Ongnok, B., Chattipakorn, S. C., & Chattipakorn, N. (2023) · Journal of Pineal Research · doi:10.1111/jpi.12884 · Cited by 24

Genetics of enzymatic dysfunctions in metabolic disorders and cancer

Mahé, M., Rios-Fuller, T. J., Karolin, A., & Schneider, R. J. (2023) · Frontiers in Oncology · doi:10.3389/fonc.2023.1230934 · Cited by 23

Succinate dehydrogenase is essential for epigenetic and metabolic homeostasis in hearts

Li, W., Li, Q., Peng, K., Wang, Y., Wang, X., Chen, Q., Cheng, H., & Ma, Q. (2023) · Basic Research in Cardiology · doi:10.1007/s00395-023-01015-z · Cited by 21

Monocytic Differentiation in Acute Myeloid Leukemia Cells: Diagnostic Criteria, Biological Heterogeneity, Mitochondrial Metabolism, Resistance to and Induction by Targeted Therapies

Bruserud, Ø., Selheim, F., Hernandez-Valladares, M., & Reikvam, H. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25126356 · Cited by 23

MicroRNA-101-3p Modulates Mitochondrial Metabolism via the Regulation of Complex II Assembly

Ziemann, M., Lim, S. C., Kang, Y., Samuel, S., Sanchez, M. I. G. L., Gantier, M. P., Stojanovski, D., & McKenzie, M. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167361 · Cited by 23

Functional and biochemical characterization of the Toxoplasma gondii succinate dehydrogenase complex

Silva, M. F., Douglas, K., Sandalli, S., Maclean, A. E., & Sheiner, L. (2023) · PLoS Pathogens · doi:10.1371/journal.ppat.1011867 · Cited by 20

Inhibition of mitochondrial complex II in neuronal cells triggers unique pathways culminating in autophagy with implications for neurodegeneration

Ranganayaki, S., Jamshidi, N., Aiyaz, M., Santhoshkumar, R., Gayathri, N., Harsha, P. K., Padmanabhan, B., & Bharath, M. M. S. (2021) · Scientific Reports · doi:10.1038/s41598-020-79339-2 · Cited by 20

Age-Dependent Decrease of Mitochondrial Complex II Activity in a Familial Mouse Model for Alzheimer’s Disease

Emmerzaal, T. L., Rodenburg, R. J., Tanila, H., Verweij, V., Kiliaan, A. J., & Kozicz, T. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-180337 · Cited by 21

Western Diet Decreases the Liver Mitochondrial Oxidative Flux of Succinate: Insight from a Murine NAFLD Model

Staňková, P., Kučera, O., Peterová, E., Elkalaf, M., Rychtrmoc, D., Melek, J., Podhola, M., Zubáňová, V., & Červinková, Z. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22136908 · Cited by 19

Beta-Caryophyllene, a CB2R Selective Agonist, Protects Against Cognitive Impairment Caused by Neuro-inflammation and Not in Dementia Due to Ageing Induced by Mitochondrial Dysfunction

Kanojia, U., Chaturbhuj, S. G., Sankhe, R., Das, M., Surubhotla, R., Nandakumar, K., Gourishetti, K., Nayak, P. G., & Kishore, A. (2021) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/1871527320666210202121103 · Cited by 19

Sodium disrupts mitochondrial energy metabolism to execute NECSO

Qiao, Y., Wang, J., Wang, B., Zhou, H., Ni, Q., Fu, W., Hu, Z., & Zhong, Q. (2025) · Nature Communications · doi:10.1038/s41467-025-67181-x · Cited by 22

Modular structure of complex II: An evolutionary perspective

Karavaeva, V., & Sousa, F. L. (2022) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2022.148916 · Cited by 18

Effects of microbe-derived antioxidants on growth performance, hepatic oxidative stress, mitochondrial function and cell apoptosis in weaning piglets

Yu, C., Luo, Y., Shen, C. X., Luo, Z., Zhang, H., Zhang, J., Xu, W., & Xu, J. (2024) · Journal of Animal Science and Biotechnology/Journal of animal science and biotechnology · doi:10.1186/s40104-024-01088-3 · Cited by 21

Resistance risk and mechanism of Ustilaginoidea virens to pydiflumetofen

Yin, X., Gao, X., Shen, X., Ren, F., Li, Y., Zhou, M., Zhang, J., & Duan, Y. (2024) · Pesticide Biochemistry and Physiology · doi:10.1016/j.pestbp.2024.106200 · Cited by 17

Androgen receptor (AR) antagonism triggers acute succinate‐mediated adaptive responses to reactivate AR signaling

Saxena, N., Beraldi, E., Fazli, L., Somasekharan, S. P., Adomat, H. H., Zhang, F., Molokwu, C. N., Gleave, A., Nappi, L., Nguyen, K., et al. (2021) · EMBO Molecular Medicine · doi:10.15252/emmm.202013427 · Cited by 16

Cryo-EM structure of the yeast Saccharomyces cerevisiae SDH provides a template for eco-friendly fungicide discovery

Li, Z.-W., Huang, Y.-H., Wei, G., Lu, Z., Wang, Y.-X., Cui, G.-R., Wang, J.-Y., Yu, X., Fu, Y., Fan, E.-D., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-64001-0 · Cited by 19

Metformin inhibits mitochondrial complex I in intestinal epithelium to promote glycaemic control

Sebo, Z. L., Chakrabarty, R. P., Grant, R. A., D’Alessandro, K. B., Koss, A., Blum, J. L. E., Davidson, S. M., Reczek, C. R., & Chandel, N. S. (2026) · Nature Metabolism · doi:10.1038/s42255-026-01530-y · Cited by 21

The mitochondrial LYR protein SDHAF1 is required for succinate dehydrogenase activity in Arabidopsis

Li, Y., Belt, K., Alqahtani, S. F., Saha, S., Fenske, R., Aken, O. V., Whelan, J., Millar, A. H., Murcha, M. W., & Huang, S. (2022) · The Plant Journal · doi:10.1111/tpj.15684 · Cited by 16

Hibernation is super complex: distribution, dynamics, and stability of electron transport system supercomplexes in Ictidomys tridecemlineatus

Hutchinson, A. J., Duffy, B. M., & Staples, J. F. (2022) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00008.2022 · Cited by 13

Metabolic enzymes function as epigenetic modulators: A Trojan Horse for chromatin regulation and gene expression

Liao, X., Guo, Y., He, Y., Xiao, Y., Li, J., & Liu, R. (2021) · Pharmacological Research · doi:10.1016/j.phrs.2021.105834 · Cited by 14

Biochemical, Molecular, and Clinical Characterization of Succinate Dehydrogenase Subunit A Variants of Unknown Significance

Bannon, A. E., Kent, J. D., Forquer, I., Town, A., Klug, L. R., McCann, K. E., Beadling, C., Harismendy, O., Sicklick, J. K., Corless, C. L., et al. (2017) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-17-1397 · Cited by 15

IsoSearch: An Untargeted and Unbiased Metabolite and Lipid Isotopomer Tracing Strategy from HR-LC-MS/MS Datasets

Huang, H., Yuan, M., Seitzer, P., Ludwigsen, S., & Asara, J. M. (2020) · Methods and Protocols · doi:10.3390/mps3030054 · Cited by 15

Structural basis of mitochondrial membrane bending by I-II-III2-IV2 supercomplexPreprint

Mühleip, A., Flygaard, R. K., Haapanen, O., Baradaran, R., Gruhl, T., Tobiasson, V., Maréchal, A., Sharma, V., & Amunts, A. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.06.26.497646 · Cited by 15

A metabolic regulatory network for the Caenorhabditis elegans intestine

Bhattacharya, S., Horowitz, B. B., Zhang, J., Li, X., Zhang, H., Giese, G. E., Holdorf, A. D., & Walhout, A. J. M. (2022) · iScience · doi:10.1016/j.isci.2022.104688 · Cited by 14

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 15

Permeabilised skeletal muscle reveals mitochondrial deficiency in malignant hyperthermia-susceptible individuals

Chang, L., Daly, C. L., Miller, D., Allen, P. D., Boyle, J. P., Hopkins, P. M., & Shaw, M. (2019) · British Journal of Anaesthesia · doi:10.1016/j.bja.2019.02.010 · Cited by 14

Proteomic Analysis Identifies NDUFS1 and ATP5O as Novel Markers for Survival Outcome in Prostate Cancer

Wiebringhaus, R., Pecoraro, M., Neubauer, H. A., Trachtová, K., Trimmel, B., Wieselberg, M., Pěnčík, J., Egger, G., Krall, C., Moriggl, R., et al. (2021) · Cancers · doi:10.3390/cancers13236036 · Cited by 14

ROS control in human iPS cells reveals early events in spontaneous carcinogenesis

Oka, S., Hayashi, M., Taguchi, K., Hidaka, M., Tsuzuki, T., & Sekiguchi, M. (2019) · Carcinogenesis · doi:10.1093/carcin/bgz081 · Cited by 14

Adaptation of Mitochondrial Substrate Flux in a Mouse Model of Nonalcoholic Fatty Liver Disease

Staňková, P., Kučera, O., Peterová, E., Lotková, H., Maseko, T. E., Nozickova, K., & Červinková, Z. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21031101 · Cited by 16

MitoPlex: A targeted multiple reaction monitoring assay for quantification of a curated set of mitochondrial proteins

Stotland, A. B., Spivia, W. R., Orosco, A., Andres, A. M., Gottlieb, R. A., Eyk, J. E. V., & Parker, S. J. (2020) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2020.03.011 · Cited by 14

The translation initiation factor homolog eif4e1c regulates cardiomyocyte metabolism and proliferation during heart regeneration

Rao, A., Lyu, B., Jahan, I., Lubertozzi, A., Zhou, G., Tedeschi, F., Jankowsky, E., Kang, J., Carstens, B., Poss, K. D., et al. (2023) · Development · doi:10.1242/dev.201376 · Cited by 13

Differential expression of nuclear-derived mitochondrial succinate dehydrogenase genes in metabolically active buffalo tissues

Sadeesh, E. M., Malik, A., Lahamge, M. S., & Singh, P. (2024) · Molecular Biology Reports · doi:10.1007/s11033-024-10022-9 · Cited by 14

Astaxanthin Is Able to Prevent Alcohol-Induced Dysfunction of Liver Mitochondria

Krestinina, O. V., Odinokova, I. V., Sotnikova, L. D., Krestinin, R. R., Zvyagina, A. I., & Baburina, Y. L. (2022) · Antioxidants · doi:10.3390/antiox11102019 · Cited by 13

Targeting the Host Mitochondria as a Novel Human Cytomegalovirus Antiviral Strategy

Bachman, L. O., & Zwezdaryk, K. J. (2023) · Viruses · doi:10.3390/v15051083 · Cited by 14

The resistance mechanism of B_P225F and B_H272R mutations in succinate dehydrogenase in Botrytis cinerea

Ma, J.-H., Ying, M.-X., Lu, Z., Guan, Z.-W., Zhang, C., Zhu, X., & Yang, G. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.139360 · Cited by 12

Knockdown of NDUFC1 inhibits cell proliferation, migration, and invasion of hepatocellular carcinoma

Han, F., Liu, J., Chu, H., Cao, D., Jia Rui, W. U., Fu, H. Y., Guo, A., Chen, W., Xu, Y., Cheng, X., et al. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.860084 · Cited by 12

Alleles in metabolic and oxygen‐sensing genes are associated with antagonistic pleiotropic effects on life history traits and population fitness in an ecological model insect*

Marden, J. H., Langford, E. A., Robertson, M. A., & Fescemyer, H. W. (2020) · Evolution · doi:10.1111/evo.14095 · Cited by 11

Disordered-to-ordered transitions in assembly factors allow the complex II catalytic subunit to switch binding partners

Sharma, P., Maklashina, E., Voehler, M., Balintova, S., Dvorakova, S., Kraus, M., Vanova, K. H., Nahácka, Z., Zobalová, R., Boukalová, Š., et al. (2024) · Nature Communications · doi:10.1038/s41467-023-44563-7 · Cited by 11

A New Perspective on the Role of Alterations in Mitochondrial Proteins Involved in ATP Synthesis and Mobilization in Cardiomyopathies

Vázquez-Carrada, M., Vilchis‐Landeros, M. M., Vázquez‐Meza, H., Uribe-Ramírez, D., & Matuz‐Mares, D. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26062768 · Cited by 12

Oxaliplatin-induced cardiotoxicity in mice is connected to the changes in energy metabolism in the heart tissue

Du, J., Sudlow, L. C., Shahverdi, K., Zhou, H., Michie, M. S., Schindler, T. H., Mitchell, J. D., Mollah, S. A., & Berezin, M. Y. (2026) · Cardio-Oncology · doi:10.1186/s40959-026-00453-7 · Cited by 12

AUF1 gene transfer increases exercise performance and improves skeletal muscle deficit in adult mice

Abbadi, D., Andrews, J. J., Katsara, O., & Schneider, R. J. (2021) · Molecular Therapy — Methods & Clinical Development · doi:10.1016/j.omtm.2021.07.005 · Cited by 12

In vitro antifungal activity of Shikonin against Candida albicans by inducing cellular apoptosis and necrosis

Pang, C., Chen, J., Liu, S., Cao, Y., & Hao, M. (2022) · Molecular Biology Reports · doi:10.1007/s11033-022-08093-7 · Cited by 12

Novel potential causative genes in carotid paragangliomas

Snezhkina, A. V., Lukyanova, E., Zaretsky, A. R., Kalinin, D. V., Pokrovsky, A. V., Golovyuk, A. L., Krasnov, G. S., Fedorova, M., Pudova, E. A., Kharitonov, S., et al. (2019) · BMC Medical Genetics · doi:10.1186/s12881-019-0770-6 · Cited by 11

The effects of ozone exposure and sedentary lifestyle on neuronal microglia and mitochondrial bioenergetics of female Long-Evans rats

Valdez, M. C., Valdez, J. M., Freeborn, D. L., Johnstone, A. F. M., & Kodavanti, P. R. S. (2020) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2020.115254 · Cited by 11

Organization of the Respiratory Supercomplexes in Cells with Defective Complex III: Structural Features and Metabolic Consequences

Rugolo, M., Zanna, C., & Ghelli, A. M. (2021) · Life · doi:10.3390/life11040351 · Cited by 13

Exploring the impact of flavin homeostasis on cancer cell metabolism

Nisco, A. D., Tolomeo, M., Scalise, M., Zanier, K., & Barile, M. (2024) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2024.189149 · Cited by 11

Mitochondrial complex-1 as a therapeutic target for cardiac diseases

Rai, N. K., Venugopal, H., Rajesh, R., Ancha, P., & Venkatesh, S. (2024) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-024-05074-1 · Cited by 12

F-ATP synthase inhibitory factor 1 and mitochondria-organelle interactions: New insight and implications

Guo, L. (2024) · Pharmacological Research · doi:10.1016/j.phrs.2024.107393 · Cited by 13

Placental mitochondrial metabolic adaptation maintains cellular energy balance in pregnancy complicated by gestational hypoxia

Tong, W., Allison, B. J., Brain, K. L., Patey, O. V., Niu, Y., Botting, K. J., Ford, S. G., Garrud, T. A. C., Wooding, F. B. P., Lyu, Q., et al. (2025) · The Journal of Physiology · doi:10.1113/jp287897 · Cited by 14

Mitochondrial respiration of complex II is not lower than that of complex I in mouse skeletal muscle

Maekawa, S., Takada, S., Furihata, T., Fukushima, A., Yokota, T., & Kinugawa, S. (2019) · Biochemistry and Biophysics Reports · doi:10.1016/j.bbrep.2019.100717 · Cited by 10

Perturbed Brain Glucose Metabolism Caused by Absent SIRT3 Activity

Kristián, T., Karimi, A. J., Fearnow, A. D., Waddell, J., & McKenna, M. C. (2021) · Cells · doi:10.3390/cells10092348 · Cited by 10

Mitofusin 2 is involved in chemotaxis of neutrophil-like differentiated HL-60 cells

Mazaki, Y., Takada, S., Nio‐Kobayashi, J., Maekawa, S., Higashi, T., Onodera, Y., & Sabe, H. (2019) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2019.04.037 · Cited by 10

The ER thioredoxin-related transmembrane protein TMX2 controls redox-mediated tethering of ER-mitochondria contacts

Chen, J., Yap, M. C., Bassot, A., Pascual, D. M., Makio, T., Zimmermann, J., Mast, H., Bhat, R. K., Fleury, S. G., Fan, Y., et al. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.116486 · Cited by 9

Citrus-derived DHCP inhibits mitochondrial complex II to enhance TRAIL sensitivity via ROS-induced DR5 upregulation

Chen, L., Hao, M., Yan, J., Sun, L., Tai, G., Cheng, H., & Zhou, Y. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100515 · Cited by 9

Caloric restriction overcomes pre-diabetes and hypertension induced by a high fat diet and renal artery stenosis

Faria, M. S. D. S. N., Pimentel, V. E., Helaehil, J. V., Bertolo, M. C., Santos, N. T. H., Silva-Neto, P. V. D., Thomazini, B. F., de Oliveira, C. A., & do Amaral, M. E. C. (2022) · Molecular Biology Reports · doi:10.1007/s11033-022-07370-9 · Cited by 9

Potential use of ubiquinol and d-ribose in patients with heart failure with preserved ejection fraction

Pierce, J. D., Shen, Q., Vacek, J. L., Rahman, F. K., Krueger, K. J., Gupta, B. P., & Hiebert, J. B. (2020) · Annals of Medicine and Surgery · doi:10.1016/j.amsu.2020.05.009 · Cited by 9

The Epithelial to Mesenchymal Transition in Colorectal Cancer Progression: The Emerging Role of Succinate Dehydrogenase Alterations and Succinate Accumulation

Turano, M., Vicidomini, R., Cammarota, F., D’Agostino, V., Duraturo, F., Izzo, P., & Rosa, M. D. (2023) · Biomedicines · doi:10.3390/biomedicines11051428 · Cited by 9

Silybin inhibits succinate production and secretion in hepatocytes to reverse liver fibrosis

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