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

Kim, S. C., Sprung, R., Chen, Y., Xu, Y., Ball, H., Pei, J., Cheng, T., Kho, Y., Xiao, H., Xiao, L., et al. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.06.026 · Cited by 1,487

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×

Chemerin regulates glucose and lipid metabolism by changing mitochondrial structure and function associated with androgen/androgen receptor

Yin, L., Tang, H., Qu, J., Jia, Y., Zhang, Q., & Wang, X. (2024) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00104.2023 · Cited by 5

Mitochondrial respiratory complex II is altered in renal carcinoma

Miklovicova, S., Volpini, L., Sanovec, O., Monaco, F., Vanova, K. H., Novák, J., Boukalová, Š., Zobalová, R., Klézl, P., Tomasetti, M., et al. (2024) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2024.167556 · Cited by 5

Modeling succinate dehydrogenase loss disorders in C. elegans through effects on hypoxia-inducible factor

Braun, M. M., Damjanac, T., Zhang, Y., Chen, C., Hu, J., & Maher, L. J., III (2019) · PLoS ONE · doi:10.1371/journal.pone.0227033 · Cited by 6

Effects of aerobic and strength training on aerobic capacity, muscle strength, and gene expression of lymphomonocytes in patients with stable CAD.

Lehti, M., Valkeinen, H., Sipilä, S., Perhonen, M. A., Rottensteiner, M., Pullinen, T., Pietiläinen, R., Nyman, K., Vehkaoja, A. T., Kainulainen, H., et al. (2020) · PubMed Central · Cited by 5

Structure of the II2-III2-IV2 mitochondrial supercomplex from the parasite Perkinsus marinusPreprint

Wú, F., Mühleip, A., Gruhl, T., Sheiner, L., Maréchal, A., & Amunts, A. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.05.25.595893 · Cited by 6

Mitochondrial metabolism: Critical mechanisms underpinning normal hematopoietic stem cell and acute myeloid leukemia stem cell function

Yu, H., & Yan, L. (2025) · Gene · doi:10.1016/j.gene.2025.149685 · Cited by 6

Signaling Pathways Concerning Mitochondrial Dysfunction: Implications in Neurodegeneration and Possible Molecular Targets

Sharma, Y., Gupta, J. K., Babu, M. A., Singh, S., & Sindhu, R. K. (2024) · Journal of Molecular Neuroscience · doi:10.1007/s12031-024-02269-5 · Cited by 6

LRP1 immunotherapy enhances cardiomyocyte respiration by restricting cholesteryl ester accumulation in mitochondria

Amaro, A. B., Garcia, E., Lhoëst, M. T. L. C., Polishchuk, A., Zegrí‐Reiriz, I., Viladés, D., Palmero, M. J. G., Fernández-del-Río, L., Mirabet, S., Samouillan, V., et al. (2025) · Journal of Lipid Research · doi:10.1016/j.jlr.2025.100783 · Cited by 4

Mitochondria are an important target of photobiomodulation in cardiomyocytes

Gao, X., WANG, X., ZHANG, W., LI, H., Yang, F., Ma, W., & LIU, Y. (2022) · Biocell · doi:10.32604/biocell.2022.021033 · Cited by 4

Identification of global transcriptional variations in human peripheral blood mononuclear cells two months postheat injury helps categorization heat-tolerant or heat-intolerant phenotypes

Horowitz, M., Kopeliovich, D., Berdugo, R., Smith, Y., Elgavish, S., Schermann, H., & Moran, D. S. (2023) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00118.2022 · Cited by 4

Role of Succinate Dehydrogenase in Cellular Respiration

Viswalingam, V., & Kumar, D. (2025) · Springer eBooks · doi:10.1007/978-981-96-6831-1_3 · Cited by 3

Metabolic costs and trade-offs of hypermetabolism in human motor neurons with ATP synthase deficiency

Torregrosa‐Muñumer, R., Turkia, J. J., Ermiş, R., Kvist, J., Harjuhaahto, S., Pennonen, J., Hietakangas, V., Ylikallio, E., & Tyynismaa, H. (2025) · Communications Biology · doi:10.1038/s42003-025-09149-7 · Cited by 4

3-Nitropropionic Acid–Induced Huntington’s Disease in Preclinical Models: Mechanisms, Peripheral Toxicities, Model Gaps, and Future Directions

Dontiboina, H. R., Yadava, S., Nakka, V. P., Dumala, N., Viswanadh, M. K., Guntupalli, C., Nalluri, B. N., Malothu, N., Yadagiri, G., Gujjari, L., et al. (2026) · Molecular Neurobiology · doi:10.1007/s12035-026-05967-w · Cited by 3

Using multi-tissue transcriptome-wide association study to identify candidate susceptibility genes for respiratory infectious diseases

Zhu, X.-B., Zou, Y., Jia, L., Ye, X., Zou, Y., Tu, J., Li, J., Yu, R., Yang, S., & Huang, P. (2023) · Frontiers in Genetics · doi:10.3389/fgene.2023.1164274 · Cited by 6

Molecular mechanisms underlying the renoprotective effects of 1,4,7-triazacyclononane: a βeta-lactamase inhibitor

Tsotetsi, N., Amoako, D. G., Somboro, A. M., Khumalo, H. M., & Khan, R. B. (2020) · Cytotechnology · doi:10.1007/s10616-020-00422-7 · Cited by 3

NEK7 couples SDHB to orchestrate respiratory chain electron transport homeostasis that impedes liver fibrosis

Sun, Z., Sun, L., Hu, H., Ren, Y., Zhu, W., Wang, X., Gu, W., Huang, S., Zhong, D., Sun, Y., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-65790-0 · Cited by 2

SDH mutations, as potential predictor of chemotherapy prognosis in small cell lung cancer patients

Zeng, R., Fan, X., Yang, J. B., Chen, F., Li, J., Wen, W. X., Liu, J., Lv, M., Feng, X., Zhao, X., et al. (2023) · Discover Oncology · doi:10.1007/s12672-023-00685-4 · Cited by 2

Persistent Organic Pollutants released from decomposed adipose tissue affect mitochondrial enzyme function in the brain and eyes other than the liver

Yang, D., Ko, E., Lim, H., Lee, H., Kim, K., Choi, M., & Shin, S. (2024) · Environmental Science and Pollution Research · doi:10.1007/s11356-024-31904-2 · Cited by 2

Echocardiographic surrogate of left ventricular stroke work in a model of brain stem death donors

Sato, K., Hoe, L. E. S., Chan, J. H., Obonyo, N. G., Wildi, K. S., Heinsar, S., Colombo, S. M., Ainola, C., Abbate, G., Sato, N., et al. (2024) · European Journal of Clinical Investigation · doi:10.1111/eci.14259 · Cited by 2

Exposure to the neurotoxin 3-nitropropionic acid in neuronal cells induces unique histone acetylation pattern: Implications for neurodegeneration

Ranganayaki, S., Govindaraj, P., Gayathri, N., & Bharath, M. M. S. (2020) · Neurochemistry International · doi:10.1016/j.neuint.2020.104846 · Cited by 2

Loss of SDHB reprograms energy metabolisms and inhibits high fat diet induced metabolic syndromesPreprint

Mu, C., Ma, B., Zhang, C., Geng, G., Zhang, X., Chen, L., Wang, M., Li, J., Zhao, T., Cheng, H., et al. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/259226 · Cited by 3

Metformin inhibits mitochondrial complex I in intestinal epithelium to promote glycemic controlPreprint

Sebo, Z. L., Chakrabarty, R. P., Grant, R. A., D’Alessandro, K. B., Koss, A. R., Blum, J. L. E., Davidson, S. M., Reczek, C. R., & Chandel, N. S. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.10.02.678294 · Cited by 2

Reductive carboxylation of glutamine as a potential target in acute myeloid leukemia

Roma, A., Goodridge, L. D., & Spagnuolo, P. A. (2023) · Oncotarget · doi:10.18632/oncotarget.28474 · Cited by 1

Exercise promotes cognition and hippocampal mitochondrial complex II expression in female rats

White, Z. J., Sudasinghe, K., Poole, D. C., & Hall, S. E. (2025) · Experimental Physiology · doi:10.1113/ep092533 · Cited by 1

Nuclear progesterone receptor expression, localization and function during bovine oocyte growth

D’augero, J., Latorraca, L. B., Rabaglino, M. B., de Guevara, M. L., & Fair, T. (2025) · Reproduction · doi:10.1530/rep-25-0080 · Cited by 1

Reactive oxygen species in general

Haidara, M. A., Zarić, B. L., Mubarak, H. A., Dawood, A. F., Ebrahim, H. A., Hassan, F. E., ShamsEldeen, A. M., & Yassin, H. Z. (2025) · Elsevier eBooks · doi:10.1016/b978-0-443-27333-9.00002-6 · Cited by 1

Identification of potential biomarkers of triton WR-1339 induced hyperlipidemia: NMR-based plasma metabolomics approach and gene expression analysis

Alwahsh, M., Alejel, R., Hamadneh, L., Aleidi, S. M., Marchan, R., Hasan, A., Jasim, S., Saqallah, F. G., Al-Kouz, S., Hussein, B., et al. (2025) · Metabolomics · doi:10.1007/s11306-025-02318-z · Cited by 1

Assessing molecular, cellular and transcriptomic bases of laminar perfusion and cytoarchitecture coupling in the human cortex

Guo, F., Zhao, C., Bhatt, R. R., Liu, Z., Kim, A. J., Yang, Z., Xu, S., Jann, K., Shao, X., Mather, M., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-76812-w · Cited by 1

SIRT5 Facilitates Liver Steatosis Progression via Promoting SDH Desuccinylation During High‐Fat Diet Feeding

Liu, Z., Hu, J., Lin, Y., Ge, C., Shao, Y., Bao, M., Liu, M., Jia, S., Li, Y., Xu, X., et al. (2025) · Liver International · doi:10.1111/liv.70433 · Cited by 1

Hereditary Renal Cancer Syndromes

Cornejo, K. M., Machacek, M. E., Lu, Z., Clemente, L. C., Liu, X., Nair, V., & Wu, C. (2026) · Advances in Anatomic Pathology · doi:10.1097/pap.0000000000000521 · Cited by 1

Disparate Hepatic Mitochondrial and Inflammatory Effects of Ketone Supplements

Morris, T. C. M., Morris, M. D., Parker, A. J., Heggie, J. R., Roeth, E. J., Parker, G., Beus, M. K., Ricks, R. F., Shafer, T. L., Poulos, T., et al. (2026) · Nutrients · doi:10.3390/nu18040675 · Cited by 1

Impact of compound heterozygous SDHA variants on mitochondrial function in pediatric with neurological disease

Garrido-Moraga, R., Serrano‐Lorenzo, P., Esteban-Amo, M. J., Bellusci, M., de la Fuente, M. Á., Arenas, J., González-Quintana, A., Ugalde, C., Simarro, M., & Martín, M. A. (2026) · Mitochondrion · doi:10.1016/j.mito.2026.102149 · Cited by 1

Mitochondrial permeability transition in redox homeostasis and ferroptosis

Guo, L. (2026) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2026.113244 · Cited by 1

Using complex II as an emerging therapeutic target for the treatment of muscle lesions

Li, K., Han, W., Zhao, Y., Qi, Y., Li, Y., Bi, J., Wang, Y. H., & Dong, G. (2019) · Saudi Journal of Biological Sciences · doi:10.1016/j.sjbs.2019.07.002 · Cited by 1

Genetics of Mitochondrial Respiratory Chain Disease

Ganetzky, R. D., & Falk, M. J. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-812535-9.00016-9 · Cited by 1

Measurement of Fatty Acid Oxidation by High-Resolution Respirometry: Special Considerations for Analysis of Skeletal and Cardiac Muscle and Adipose Tissue

Watt, N. T., MacCannell, A. D. V., & Roberts, L. D. (2023) · Methods in molecular biology · doi:10.1007/978-1-0716-3247-5_3 · Cited by 1

Impacts of iron on ultrastructural features of NCI-H295R cell line related to steroidogenesis

Ďúranová, H., Fialková, V., Šimora, V., Bilčí­ková, J., Massányi, P., Lukáč, N., & Kňažická, Z. (2023) · Acta Histochemica · doi:10.1016/j.acthis.2023.152056 · Cited by 1

Transcriptomic insights into developmental arrest in fluorescent labeling transgenic Asian elephant (Elephas maximus) embryos via inter-order cloning

Pankammoon, P., Qing, Y., Zhao, H., Jiao, D., Li, H., Wang, F., Wiriyahdamrong, T., Guo, J., Li, W., Chuammitri, P., et al. (2025) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2025.1532962 · Cited by 1

Pheochromocytomas, Paragangliomas, and Pituitary Adenomas (3PAs) and Succinate Dehydrogenase Defects

Demidowich, A. P., & Stratakis, C. A. (2021) · Endocrinology · doi:10.1007/978-3-319-89497-3_13 · Cited by 1

Caloric restriction overcomes pre-diabetic and hypertension induced by high fat diet and renal artery stenosisPreprint

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. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.03.30.437684 · Cited by 1

Disordered-to-ordered transitions in assembly factors allow the Complex II catalytic subunit to switch binding partnersPreprint

Sharma, P., Maklashina, E., Voehler, M., Balintova, S., Dvorakova, S., Kraus, M., Vanova, K. H., Nahácka, Z., Zobalová, R., Boukalová, Š., et al. (2022) · Research Square · doi:10.21203/rs.3.rs-2070392/v1 · Cited by 1

Distinct proteomic and acylproteomic adaptations to succinate dehydrogenase loss in two cell contexts

Zhou, S. X., Madden, B. J., Charlesworth, C. M., Hitosugi, T., Favier, J., & Maher, L. J., III (2026) · Journal of Biological Chemistry · doi:10.1101/2025.08.01.668168 · Cited by 1

Pheochromocytomas, Paragangliomas, and Pituitary Adenomas (3PAs) and Succinate Dehydrogenase Defects

Demidowich, A. P., & Stratakis, C. A. (2019) · Endocrinology · doi:10.1007/978-3-319-73082-0_13-1

Metabolic adaptations of neurons to physiological oxygen concentrations

Warde, M. (2018) · Gredos (University of Salamanca) · doi:10.14201/gredos.139770

Insights into the biogenesis of the human mitochondrial ribosomal large subunit – Characterisation of mL44 and mL45

Hanitsch, E. (2020) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-8315

Une signalisation lysosomale permet un dialogue inter-organites améliorant l’activité métabolique, l’homéostasie redox et augmentant la longévité chez Caenorhabditis elegans

Alassaf, A., & Mignotte, B. (2021) · médecine/sciences · doi:10.1051/medsci/2020284

Caloric Restriction Overcomes Pre-Diabetic and Hypertension Induced by High Fat Diet and Renal Artery StenosisPreprint

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. (2021) · Research Square · doi:10.21203/rs.3.rs-1085770/v1

Cardiac Paraganglioma, Recent Advances in Clinicopathologic Features

Alakeel, F. S., Reardon, M. J., & Ro, J. Y. (2021) · Multidisciplinary Cancer Investigation · doi:10.30699/mci.5.2.472-1

Connexin 43-Mediated Mitochondrial Calcium Intake Aggravates Obesity via Promoting Macrophages PolarizationPreprint

Zhou, Q., You, M., Lu, Z., He, C., Li, L., Wang, L., Cao, T., Zhao, Y. X., Li, Q., Sun, F., et al. (2021) · SSRN Electronic Journal · doi:10.2139/ssrn.3962439

A novel sight of the primary active compounds from Umbelliferae: focusing on mitochondria

Yang, L., Ni, N., Hong, Y., & Shen, L. (2022) · Medicinal Chemistry Research · doi:10.1007/s00044-021-02822-6 · Cited by 2

A tanshinone IIA derivative designed to target mitochondria inhibit myocardial ischemia/reperfusion injury in vivo in a GUF1 dependent- pathway

Zhou, W., Fan, K., Yin, X., Wang, Y., Zhang, Y., & Gou, S. (2022) · Pharmacological Research - Modern Chinese Medicine · doi:10.1016/j.prmcm.2022.100066

Vitamin B2 Riboflavin

(2018) · Royal Society of Chemistry eBooks · doi:10.1039/bk9781788014649-00104

Activity and Catalytic Characteristics of Rat Liver Mitochondrial Succinate Dehydrogenase under Moderate Hypothermia

Абдуразакович, Х. Р., Джафарова, А. М., & Абдуллаев, В. Р. (2022) · BIOPHYSICS · doi:10.1134/s0006350922060094

Lipid Rafts in brain cells: From enzymatic activity to lipidomic assays in a novel printed Rafts platform

Sánchez, L. S. (2023) · UVaDOC UVaDOC University of Valladolid Documentary Repository (University of Valladolid) · doi:10.35376/10324/66283

The relation between clinical course of pheochromocytoma-paraganglioma (PPGL) and complex genetic etiology

Szatko, A., Leszczyńska, D., Woźniak, B., & Glinicki, P. (2023) · Wiedza Medyczna · doi:10.36553/wm.150

Identification of a novel transcript of mouse Sdha

Esteban-Amo, M. J., Telleria, A., Gobelli, D., Serrano‐Lorenzo, P., Orriols, J. J. T., Pérez-García, M. T., Kozłowski, P., de la Fuente, M. Á., & Simarro, M. (2025) · BMC Research Notes · doi:10.1186/s13104-025-07149-8

Integrated functional genomics-identified LYRM4 promotes fumarate accumulation and hepatocellular carcinoma progression

Xu, Y., Yang, Y., Yu, X., Han, L., Liu, S., Zhang, N., & Yang, M. (2025) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2025.110448

Implication of Succinate Dehydrogenase in Cancer

Viswalingam, V., & Kumar, D. (2025) · Springer eBooks · doi:10.1007/978-981-96-6831-1_7

The Function of Succinate Dehydrogenase in Maintaining Normal Health

Lari, M. Q., Kumar, D., Kumar, D., & Kumar, A. (2025) · Springer eBooks · doi:10.1007/978-981-96-6831-1_2

Efficacy of ethylmethylhydroxypyridine succinate derivative in a model of intermittent hypoxia in comparison with the reference drug

Алексеевич, П. Г., Ivkin, D. Y., Okovityi, S. V., Bolotova, V. T., Евгеньева, Е. М., Курмазов, Н. С., Pyatiizbyantsev, T. A., Zhuravleva, M. V., Tikhaya, M. A., & Paderina, E. E. (2025) · Drug development & registration · doi:10.33380/2305-2066-2025-14-4-2160

Acromegaly and genetics

de Lapiscina, I. M., Baquero, C., & Castaño, L. (2025) · Vitamins and hormones · doi:10.1016/bs.vh.2025.10.008

Additional file 1 of Acacetin alleviates autoimmune myocarditis by regulating CD4+ T cell mitochondrial respiration

Lu, Y., Wu, Y.-W., Pu, J., Wu, Q.-F., Dong, Q., Zhao, N., Li, G., & Du, Y.-M. (2024) · Figshare · doi:10.6084/m9.figshare.26719710

Effects of endurance training on skeletal muscle mitochondrial respiration in Siberian huskies and Alaskan huskies

Sælen‐Helgesson, S., Hafstad, A. D., Lund, T., Nymo, I. H., Ciccone, C., Wood, S. H., Folkow, L. P., & Sundset, M. A. (2026) · Physiological Reports · doi:10.14814/phy2.70725

Caspase-2 inhibits mitochondrial respiration in colorectal adenocarcinoma cells

Sillapachaiyaporn, C., Yapryntseva, M. A., Mamedova, A. R., Abdelghany, L., Gogvadze, V. G., & Zhivotovsky, B. (2026) · Cell Communication and Signaling · doi:10.1186/s12964-026-02671-z

Molecular Consequences of Pathogenic SDHA Variants: From Defective Flavinylation and Assembly to Lipid RemodelingPreprint

Saucedo-Rodríguez, M. J., Pecina, P., Tauchmannová, K., Čunátová, K., Vrbacký, M., Čajka, T., Houštěk, J., Mráček, T., & Pecinová, A. (2026) · Research Square · doi:10.21203/rs.3.rs-8568560/v1 · Cited by 1

Role of reactive oxygen species in polycystic ovary syndrome: signalling pathways, mechanisms, and traditional Chinese medicine treatment strategies

Wang, Z., Liu, S.-Y., Gao, M., Shen, Y., Sun, M., & Hao, S. (2026) · International Immunopharmacology · doi:10.1016/j.intimp.2026.116251 · Cited by 2

Mitochondrial responses to anoxia-reoxygenation exposure in crucian carp ( Carassius carassius )

Lau, G. Y., Gerber, L., Johansen, A., Dahl, H.-A., Torp, M., Bates, G. R., Murphy, M. P., Eide, L., Stensløkken, K., Ge, N., et al. (2026) · Journal of Experimental Biology · doi:10.1242/jeb.251839

Corrigendum “Role of reactive oxygen species in polycystic ovary syndrome: Signalling pathways, mechanisms, and traditional Chinese medicine treatment strategies” [Int. Immunopharmacol. 173 (2026) 116251]

Wang, Z., Liu, S., Gao, M., Shen, Y., Sun, M., & Hao, S. (2026) · International Immunopharmacology · doi:10.1016/j.intimp.2026.116375

AIE‐Active Cationic Tripyrrole Targeting Mitochondrial SDHAF1 for Acute Myeloid Leukemia Therapy

Lin, W., Cheng, J., Chen, J., Xiao, W., Li, J., Wang, X., & Gao, M. (2026) · Aggregate · doi:10.1002/agt2.70310

Etude des interactions des quinones avec le complexe respiratoire nitrate réductase par spectroscopie RPE à haute résolution

Seif-Eddine, M. (2018) · theses.fr (ABES) · doi:10.70675/26c00bdfzec8dz48e5za05az270fef99935c

Rôle de la protéine virale PA-X dans la pathologie des virus influenza aviaires faiblement pathogènes

Meyer, L. (2017) · theses.fr (ABES) · doi:10.70675/4cc74c2fzcc62z4f43za393zd727cf5f3bee

Functional diversity within a ribosomal-like protein family in Arabidopsis thaliana

Wang, C. (2018) · theses.fr (ABES) · doi:10.70675/29eb14fdzf43cz4134z93bazdb1fc926cca9

Mitochondrial metabolic remodeling in the progression of dilated cardiomyopathy

Vargas, L. (2021) · theses.fr (ABES) · doi:10.70675/2b0e60a0z336az4b99za7bazf7f8f4fb9d74

Mitochondrial physiology within myelinated axons in health and disease : an energetic interplay between counterparts

van Hameren, G. (2018) · theses.fr (ABES) · doi:10.70675/71c15a42zb6d9z4edazb7c1zd3f51e09c949

High-throughput mitochondrial morphology screen identifies PGS1 as a functional suppressor of mitochondrial fragmentation in patient-derived OPA1 mutant fibroblasts

Cretin, E. (2021) · theses.fr (ABES) · doi:10.70675/5eaca89az9b6az4b80z9614z08ea32bd2ac6

Etude des fonctions des Sidéroflexines, une nouvelle famille de protéines mitochondriales

Tifoun, N. (2021) · theses.fr (ABES) · doi:10.70675/19d943dcz4ccfz40b3z8e0ez5530fe24e55f

Role of mitochondrial respiration in Listeria monocytogenes infection

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