Mitochondrial Respiratory Complex I: Structure, Function and Implication in Human Diseases

Sequence and organization of the human mitochondrial genome

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Parkinson's Disease

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Chronic Parkinsonism in Humans Due to a Product of Meperidine-Analog Synthesis

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Mitochondrial control of cell death

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Mitochondrial DNA mutation associated with Leber’s hereditary optic neuropathy

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Mitochondrial Complex I Deficiency in Parkinson's Disease

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Mitochondria, oxidative stress and cell death

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A Mitochondrial Protein Compendium Elucidates Complex I Disease Biology

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Proteome Oxidative Modifications and Impairment of Specific Metabolic Pathways During Cellular Senescence and Aging

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Molecular genetics of primary open-angle glaucoma

Yadav, M. K., Bhardwaj, A., Yadav, A. K., Dada, R., & Tanwar, M. (2023) · Indian Journal of Ophthalmology · doi:10.4103/ijo.ijo_2570_22 · Cited by 26

Redefining the roles of mitochondrial DNA-encoded subunits in respiratory Complex I assembly

Vartak, R. S., Deng, J., Fang, H., & Bai, Y. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2015.04.008 · Cited by 25

Mitochondrial signaling pathways and their role in cancer drug resistance

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Albumin-impregnated bone granules modulate the interactions between mesenchymal stem cells and monocytes under in vitro inflammatory conditions

Mijiritsky, E., Gardin, C., Ferroni, L., Lacza, Z., & Zavan, B. (2020) · Materials Science and Engineering C · doi:10.1016/j.msec.2020.110678 · Cited by 24

Differential regulation of mitochondrial complex I and oxidative stress based on metastatic potential of colorectal cancer cells

Rai, N. K., Mathur, S., Singh, S. K., Tiwari, M., Singh, V. K., Haque, R., Tiwari, S., & Sharma, L. K. (2020) · Oncology Letters · doi:10.3892/ol.2020.12176 · Cited by 24

Circulating cell-free mitochondrial DNA in brain health and disease: A systematic review and meta-analysis

Park, S. S., Jeong, H., & Andreazza, A. C. (2021) · The World Journal of Biological Psychiatry · doi:10.1080/15622975.2021.1938214 · Cited by 27

Hemocyte Clusters Defined by scRNA-Seq in Bombyx mori: In Silico Analysis of Predicted Marker Genes and Implications for Potential Functional Roles

Feng, M., Swevers, L., & Sun, J. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.852702 · Cited by 24

Biology of macrophage fate decision: Implication in inflammatory disorders

Yadav, S., Dwivedi, A., & Tripathi, A. (2022) · Cell Biology International · doi:10.1002/cbin.11854 · Cited by 26

Post-Translational Oxidative Modifications of Mitochondrial Complex I (NADH: Ubiquinone Oxidoreductase): Implications for Pathogenesis and Therapeutics in Human Diseases

Bharath, M. M. S. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170117 · Cited by 23

Mitochondrial oxidative phosphorylation in peripheral blood mononuclear cells is decreased in chronic HIV and correlates with immune dysregulation

Gangcuangco, L. M. A., Mitchell, B. I., Siriwardhana, C., Kohorn, L. B., Chew, G. M., Bowler, S. A., Kallianpur, K. J., Chow, D. C., Ndhlovu, L. C., Gerschenson, M., et al. (2020) · PLoS ONE · doi:10.1371/journal.pone.0231761 · Cited by 24

A Lethal Genetic Incompatibility between Naturally Hybridizing Species in Mitochondrial Complex IPreprint

Moran, B. M., Payne, C. Y., Powell, D. L., Iverson, E. N. K., Donny, A. E., Banerjee, S. M., Langdon, Q. K., Gunn, T. R., Rodriguez-Soto, R. A., Madero, A. M., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.07.13.452279 · Cited by 24

Proteome and phosphoproteome characterization of liver in the postprandial state from diet-induced obese and lean mice

Zembroski, A. S., Buhman, K. K., & Aryal, U. K. (2020) · Journal of Proteomics · doi:10.1016/j.jprot.2020.104072 · Cited by 22

Diagnostic value of circulating cell-free mtDNA in patients with suspected thyroid cancer: ND4/ND1 ratio as a new potential plasma marker

Jiang, Z., Bahr, T. A., Zhou, C., Jin, T., Chen, H., Song, S., Ikeno, Y., Tian, H., & Bai, Y. (2020) · Mitochondrion · doi:10.1016/j.mito.2020.09.007 · Cited by 23

Mitochondrial reprogramming by activating OXPHOS via glutamine metabolism in African American patients with bladder cancer

Reddy, K. R. K., Piyarathna, D. W. B., Park, J. H., Putluri, V., Amara, C. S., Kamal, A. H. M., Xu, J., Kraushaar, D. C., Huang, S., Jung, S. Y., et al. (2024) · JCI Insight · doi:10.1172/jci.insight.172336 · Cited by 22

Comparative bioenergetic study of neuronal and muscle mitochondria during aging

Li, H., Sharma, L. K., Li, Y.-F., Hu, P., Idowu, A., Liu, D., Lü, J., & Bai, Y. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.04.030 · Cited by 24

The complete mitogenome of Arion vulgaris Moquin-Tandon, 1855 (Gastropoda: Stylommatophora): mitochondrial genome architecture, evolution and phylogenetic considerations within Stylommatophora

Doğan, Ö., Schrödl, M., & Chen, Z. (2020) · PeerJ · doi:10.7717/peerj.8603 · Cited by 22

Effect of hypoxia factors gene silencing on ROS production and metabolic status of A375 malignant melanoma cells

Špaková, I., Rabajdová, M., Mičková, H., Graier, W. F., & Mareková, M. (2021) · Scientific Reports · doi:10.1038/s41598-021-89792-2 · Cited by 22

How Machine Perfusion Ameliorates Hepatic Ischaemia Reperfusion Injury

Clarke, G., Mergental, H., Hann, A., Perera, M. T. P. R., Afford, S. C., & Mirza, D. F. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22147523 · Cited by 22

Exogenous succinate impacts mouse brown adipose tissue mitochondrial proteome and potentiates body mass reduction induced by liraglutide

Gaspar, R. S., Delafiori, J., Zuccoli, G. S., Carregari, V. C., do Prado, T. P., Morari, J., Sidarta-Oliveira, D., Solon, C., Catharino, R. R., ARAUJO, E. P. D., et al. (2023) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00231.2022 · Cited by 21

Biotin-conjugated Ru(II) complexes with AIE characteristics as mitochondria-targeted photosensitizers for enhancing photodynamic therapy by disrupting cellular redox balance

Wei, L., He, X., Zhao, D., Kandawa-Shultz, M., Shao, G., & Wang, Y. (2023) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2023.115985 · Cited by 22

Dietary Macronutrient Management to Treat Mitochondrial Dysfunction in Parkinson’s Disease

Bajracharya, R., Youngson, N. A., & Ballard, J. W. O. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20081850 · Cited by 24

Au NHC complexes as anticancer agents: milestones, strategies and future developments

Hoffmann, M. E., & Kühn, F. E. (2025) · Chemical Society Reviews · doi:10.1039/d5cs00924c · Cited by 21

Biophysical characterization of melanoma cell phenotype markers during metastatic progression

Sobiepanek, A., Paone, A., Cutruzzolà, F., & Kobiela, T. (2021) · European Biophysics Journal · doi:10.1007/s00249-021-01514-8 · Cited by 21

Mitochondrial iron-sulfur cluster biogenesis and neurological disorders

Selvanathan, A., & Sankaran, B. P. (2021) · Mitochondrion · doi:10.1016/j.mito.2021.10.004 · Cited by 21

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 23

PAUSE: principled feature attribution for unsupervised gene expression analysis

Janizek, J. D., Spiro, A. E., Çelik, S., Blue, B. W., RUSSELL, J. C., Lee, T.-I., Kaeberlin, M., & Lee, S. (2023) · Genome biology · doi:10.1186/s13059-023-02901-4 · Cited by 26

A novel mutation in the NADH dehydrogenase (ubiquinone) 1 alpha subcomplex 4 (Ndufa4) gene links mitochondrial dysfunction to the development of diabetes in a rodent model

Yagil, C., Varadi-Levi, R., & Yagil, Y. (2018) · Disease Models & Mechanisms · doi:10.1242/dmm.036699 · Cited by 21

Marine heat waves alter gene expression of key enzymes of membrane and storage lipids metabolism in Phaeodactylum tricornutum

Feijão, E., Franzitta, M., Cabrita, M. T., Caçador, I., Duarte, B., Gameiro, C., & Matos, A. R. (2020) · Plant Physiology and Biochemistry · doi:10.1016/j.plaphy.2020.09.022 · Cited by 20

Electron Transfer in Subunit NuoI (TYKY) of Escherichia coli NADH:Quinone Oxidoreductase (NDH-1)

Sinha, P. K., Nakamaru‐Ogiso, E., Torres‐Bacete, J., Sato, M., Castro‐Guerrero, N. A., Ohnishi, T., Matsuno‐Yagi, A., & Yagi, T. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.329649 · Cited by 21

Mitochondrial respiratory complexes: Significance in human mitochondrial disorders and cancers

Vikramdeo, K. S., Sudan, S. K., Singh, A. P., Singh, S., & Dasgupta, S. (2022) · Journal of Cellular Physiology · doi:10.1002/jcp.30869 · Cited by 20

Therapeutic implications of mitochondrial stress–induced proteasome inhibitor resistance in multiple myeloma

Sharma, A., Nair, R., Achreja, A., Mittal, A., Gupta, P., Balakrishnan, K., Edgar, C. L., Animasahun, O. H., Dwivedi, B., Barwick, B. G., et al. (2022) · Science Advances · doi:10.1126/sciadv.abq5575 · Cited by 22

Evaluation of Genotoxicity and Toxicity of Annona muricata L. Seeds and In Silico Studies

Ferreira, G. G., Quaresma, A. C. S., Brandão, D. L. D. N., Marinho, A. M. D. R., Siqueira, J. E. D. S., Correa, K. L., Júnior, J. O. C. S., Percário, S., & Dolabela, M. F. (2022) · Molecules · doi:10.3390/molecules28010231 · Cited by 23

Role of noncoding RNAs in cardiac ageing

Varghese, L. N., Schwenke, D. O., & Katare, R. (2023) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2023.1142575 · Cited by 23

Aging-Related Mitochondrial Dysfunction Is Associated With Fibrosis in Benign Prostatic Hyperplasia

Adrian, A. E., Liu, T. T., Pascal, L. E., Bauer, S. R., DeFranco, D. B., & Ricke, W. A. (2023) · The Journals of Gerontology Series A · doi:10.1093/gerona/glad222 · Cited by 21

Serum coenzyme Q10 levels as a predictor of dementia in a Japanese general population

Momiyama, Y. (2014) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2014.08.056 · Cited by 20

UPRmt activation protects against MPP+-induced toxicity in a cell culture model of Parkinson's disease

Hu, D., Liu, Z., & Qi, X. (2021) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2021.06.079 · Cited by 20

Structure and electrochemistry of proteins harboring iron-sulfur clusters of different nuclearities. Part II. [4Fe-4S] and [3Fe-4S] iron-sulfur proteins

Zanello, P. (2018) · Journal of Structural Biology · doi:10.1016/j.jsb.2018.01.010 · Cited by 18

Four novel mutations in the mitochondrial ND4 gene of complex�I in patients with multiple sclerosis

Alharbi, M. A., Al‐Kafaji, G., Khalaf, N. B., Messaoudi, S. A., Taha, S., Daif, A., & Bakhiet, M. (2019) · Biomedical Reports · doi:10.3892/br.2019.1250 · 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

DJ-1 attenuates the glycation of mitochondrial complex I and complex III in the post-ischemic heart

Pantner, Y., Polavarapu, R., Chin, L., Li, L., Shimizu, Y., & Calvert, J. W. (2021) · Scientific Reports · doi:10.1038/s41598-021-98722-1 · Cited by 19

Multi-omics Analysis Implicates Mitochondrial Complex Assembly Protein COX18 in Mitochondrial Signaling and Tumorigenesis across Cancers

Goswami, D., Ghosh, S., Dutta, R., Ghatak, D., Ranjit, D., & De, R. (2025) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-025-01857-5 · Cited by 18

New approach methods supporting read-across: Two neurotoxicity AOP-based IATA case studies

van der Stel, W. (2021) · ALTEX · doi:10.14573/altex.2103051 · Cited by 24

Mitochondria in Early Life

He, L., & Maheshwari, A. (2022) · Current Pediatric Reviews · doi:10.2174/1573396319666221221110728 · Cited by 17

Regulation of metastatic potential by drug repurposing and mitochondrial targeting in colorectal cancer cells

Mathur, S., Srivastava, P., Srivastava, A., Rai, N. K., Abbas, S., Kumar, A., Tiwari, M., & Sharma, L. K. (2024) · BMC Cancer · doi:10.1186/s12885-024-12064-5 · Cited by 18

Prematurity alters the progenitor cell program of the upper respiratory tract of neonates

Shui, J. E., Wang, W., Liu, H., Степанова, А., Liao, G., Qian, J., Ai, X., Ten, V. S., Lü, J., & Cardoso, W. V. (2021) · Scientific Reports · doi:10.1038/s41598-021-90093-x · Cited by 18

Quaternary ammonium compound exposure causes infertility by altering endocrine signaling and gametogenesis

Kirkpatrick, Z. A., Melin, V. E., & Hrubec, T. C. (2024) · Reproductive Toxicology · doi:10.1016/j.reprotox.2024.108817 · Cited by 17

Profiling of genomic alterations of mitochondrial DNA in gingivobuccal oral squamous cell carcinoma: Implications for disease progress

Palodhi, A., Ghosh, S., Biswas, N. K., Basu, A., Majumder, P. P., & Maitra, A. (2018) · Mitochondrion · doi:10.1016/j.mito.2018.09.006 · Cited by 17

Genetic aberration analysis of mitochondrial respiratory complex I implications in the development of neurological disorders and their clinical significance

Dar, G. M., Ahmad, E., Ali, A., Mahajan, B., Ashraf, G. M., & Saluja, S. S. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.101906 · Cited by 17

Skeletal muscle omics signatures in cancer cachexia: perspectives and opportunities

Gilmore, L. A., Parry, T. L., Thomas, G. A., & Khamoui, A. V. (2023) · JNCI Monographs · doi:10.1093/jncimonographs/lgad006 · Cited by 19

SSH gene expression profile of Eisenia andrei exposed in situ to a naturally contaminated soil from an abandoned uranium mine

Lourenço, J., Pereira, R., Gonçalves, F. J. M., & Mendo, S. (2012) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2012.10.011 · Cited by 17

Systematic analysis of microarray datasets to identify Parkinson's disease-associated pathways and genes

Feng, Y., & Wang, X. (2017) · Molecular Medicine Reports · doi:10.3892/mmr.2017.6124 · Cited by 18

Ndufaf5 deficiency in theDictyosteliummodel: new roles in autophagy and development

Carilla-Latorre, S., Annesley, S. J., Muñoz‐Braceras, S., Fisher, P. R., & Escalante, R. (2013) · Molecular Biology of the Cell · doi:10.1091/mbc.e12-11-0796 · Cited by 17

A Comprehensive Review of Mitochondrial Complex I During Mammalian Oocyte Maturation

Bozdemir, N., Cakir, C., Topcu, U., & Uysal, F. (2025) · genesis · doi:10.1002/dvg.70017 · Cited by 16

HIV-1 Tat and cocaine impact astrocytic energy reservoirs and epigenetic regulation by influencing the LINC01133-hsa-miR-4726-5p-NDUFA9 axis

Doke, M., McLaughlin, J. P., Cai, J. J., Pendyala, G., Kashanchi, F., Khan, M. A., & Samikkannu, T. (2022) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2022.07.001 · Cited by 14

Adipose knockout of H-ferritin improves energy metabolism in mice

Lu, B., Guo, S., Zhao, J., Wang, X., & Zhou, B. (2024) · Molecular Metabolism · doi:10.1016/j.molmet.2024.101871 · Cited by 16

Accessory subunit NDUFB4 participates in mitochondrial complex I supercomplex formation

Parmar, G., Fong-McMaster, C., Pileggi, C. A., Patten, D. A., Cuillerier, A., Myers, S., Wang, Y., Hekimi, S., Čuperlović‐Culf, M., & Harper, M. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.105626 · Cited by 16

Therapeutic effects of OXY- Exo in diabetic wound injury

Miya, M. B., Ashutosh, A., Maulishree, M., Gupta, P. C., Pathak, V., Mishra, R., Chaturvedi, P., & Kalani, A. (2024) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2024.150398 · Cited by 16

Linking Mitochondrial Dysfunction, Neurotransmitter, and Neural Network Abnormalities and Mania: Elucidating Neurobiological Mechanisms of the Therapeutic Effect of the Ketogenic Diet in Bipolar Disorder

Freyberg, Z., Andreazza, A. C., McClung, C. A., & Phillips, M. L. (2024) · Biological Psychiatry Cognitive Neuroscience and Neuroimaging · doi:10.1016/j.bpsc.2024.07.011 · Cited by 20

Mitochondrial metabolism: powering new directions in acute myeloid leukemia

Stubbins, R. J., Maksakova, I. A., Sanford, D., ROUHI, A. M., & Kuchenbauer, F. C. (2021) · Leukemia & lymphoma/Leukemia and lymphoma · doi:10.1080/10428194.2021.1910685 · Cited by 17

Road Runoff Characterization: Ecotoxicological Assessment Combined with (Non-)Target Screenings of Micropollutants for the Identification of Relevant Toxicants in the Dissolved Phase

Fidji, S., Huynh, N., Gromaire, M.-C., Varrault, G., Morin, C., Moilleron, R., Roux, J. L., & Garrigue‐Antar, L. (2022) · Water · doi:10.3390/w14040511 · Cited by 16

Structure and electrochemistry of proteins harboring iron-sulfur clusters of different nuclearities. Part I. [4Fe-4S] + [2Fe-2S] iron-sulfur proteins

Zanello, P. (2017) · Journal of Structural Biology · doi:10.1016/j.jsb.2017.05.010 · Cited by 16

Amelioration of rotenone‐induced alterations in energy/redox system, stress response and cytoskeleton proteins by octanoic acid in zebrafish: A proteomic study

Sürmen, M. G., Sürmen, S., Cansız, D., Ünal, İ., Üstündağ, Ü. V., Alturfan, A. A., Büyükkayhan, D., & Emekli‐Alturfan, E. (2022) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/jbt.23024 · Cited by 15

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

The Mitochondrial Connection: The Nek Kinases’ New Functional Axis in Mitochondrial Homeostasis

Basei, F. L., Silva, I. R. E., Dias, P. R. F., Ferezin, C., de Oliveira, A. P., Issayama, L. K., Moura, L. A. R., Silva, F. R., & Kobarg, J. (2024) · Cells · doi:10.3390/cells13060473 · Cited by 16

Roles of Subunit NuoK (ND4L) in the Energy-transducing Mechanism of Escherichia coli NDH-1 (NADH:Quinone Oxidoreductase)

Torres‐Bacete, J., Sinha, P. K., Sato, M., Patki, G., Kao, M., Matsuno‐Yagi, A., & Yagi, T. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.422824 · Cited by 15

A Primer Genetic Toolkit for Exploring Mitochondrial Biology and Disease Using Zebrafish

Sabharwal, A., Campbell, J. M., Schwab, T. L., WareJoncas, Z., Wishman, M. D., Ata, H., Liu, W., Ichino, N., Hunter, D. E., Bergren, J. D., et al. (2022) · Genes · doi:10.3390/genes13081317 · Cited by 15

From Small Peptides to Large Proteins against Alzheimer’sDisease

Picone, P., Sanfilippo, T., Vasto, S., Baldassano, S., Guggino, R., Nuzzo, D., Bulone, D., Biagio, P. L. S., Muscolino, E., Monastero, R., et al. (2022) · Biomolecules · doi:10.3390/biom12101344 · Cited by 16

Oxidative Damage of Blood Platelets Correlates with the Degree of Psychophysical Disability in Secondary Progressive Multiple Sclerosis

Dziedzic, A., Morel, A., Miller, E. D., Bijak, M., Śliwiński, T., Synowiec, E., Ceremuga, M., & Saluk, J. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/2868014 · Cited by 16

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

3-MCPD Induced Mitochondrial Damage of Renal Cells Via the Rhythmic Protein BMAL1 Targeting SIRT3/SOD2

Guan, S., Wang, Z., Zhang, R., Chen, S., Bu, X., & Lu, J. (2023) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.3c04358 · Cited by 14

A disease-modifying treatment for Alzheimer’s disease: focus on the trans-sulfuration pathway

Berry, T. M., Hamza, E. A., & Moustafa, A. A. (2019) · Reviews in the Neurosciences · doi:10.1515/revneuro-2019-0076 · Cited by 14

Metabolic and Lipidomic Assessment of Kidney Cells Exposed to Nephrotoxic Vancomycin Dosages

Lagies, S., Pichler, R., Vladimirov, G., Gawron, J., Bäzner, F., Schreiner, A., Kadena, D., Plattner, D. A., Lienkamp, S. S., & Kammerer, B. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms221810111 · Cited by 15

Implications of the mitochondrial interactome of mammalian thioredoxin 2 for normal cellular function and disease.

Chasapis, C. T., Makridakis, M., Damdimopoulos, A. E., Zoidakis, J., Lygirou, V., Mavroidis, M., Vlahou, A., Miranda-Vizuete, A., Spyrou, G., & Vlamis-Gardikas, A. (2019) · Free Radical Biology & Medicine · doi:10.1016/j.freeradbiomed.2019.04.018 · Cited by 14

Mitochondrial nicotinamide adenine dinucleotide hydride dehydrogenase (NADH) subunit 4 (MTND4) polymorphisms and their association with male infertility

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