{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,30]],"date-time":"2026-07-30T14:45:11Z","timestamp":1785422711158,"version":"3.56.0"},"reference-count":73,"publisher":"MDPI AG","issue":"5","license":[{"start":{"date-parts":[[2026,5,9]],"date-time":"2026-05-09T00:00:00Z","timestamp":1778284800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100000024","name":"Canadian Institutes of Health Research","doi-asserted-by":"crossref","award":["PJT-165962"],"award-info":[{"award-number":["PJT-165962"]}],"id":[{"id":"10.13039\/501100000024","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100000024","name":"Canadian Institutes of Health Research","doi-asserted-by":"crossref","award":["PJT-191704"],"award-info":[{"award-number":["PJT-191704"]}],"id":[{"id":"10.13039\/501100000024","id-type":"DOI","asserted-by":"crossref"}]},{"award":["PJT-165962"],"award-info":[{"award-number":["PJT-165962"]}],"id":[{"id":"https:\/\/ror.org\/01gavpb45","id-type":"ROR","asserted-by":"publisher"}]},{"award":["PJT-191704"],"award-info":[{"award-number":["PJT-191704"]}],"id":[{"id":"https:\/\/ror.org\/01gavpb45","id-type":"ROR","asserted-by":"publisher"}]},{"name":"Faculty of Medicine and Health Sciences, McGill University Studentship"},{"id":[{"id":"https:\/\/ror.org\/01pxwe438","id-type":"ROR","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Antioxidants"],"abstract":"<jats:p>Infertility is a global health problem, with male factors contributing to nearly half of all cases. Up to 30% of male infertility is classified as idiopathic, in part because routine semen analysis does not assess sperm fertilizing competence. Capacitation is a complex process that endows spermatozoa with the competence to fertilize the oocyte, and it depends on oxidant-driven phosphorylation events. These events include increased PKA substrate and tyrosine phosphorylation, which promote hyperactivated motility and the acrosome reaction. These pathways are normally restrained by decapacitation factors that must be relieved in the female reproductive tract before capacitation can proceed. Protein CoAlation is an antioxidant modification of protein thiols through a disulfide bond with coenzyme A (CoASH). We previously detected protein CoAlation in human spermatozoa and observed that its levels decline during capacitation, but its function was unknown. We hypothesized that protein CoAlation functions as a decapacitation mechanism that prevents redox signalling, enabling oxidative activation of phosphorylation events during capacitation. Using spermatozoa from healthy human donors, we leveraged subcellular fractionation, immunocytochemistry, computer-assisted sperm analysis (CASA), and immunoblotting to determine the sperm protein CoAlation profile, assess CoASH biosynthetic enzymes, and test how pharmacological modulation of CoAlation levels influences capacitation. CoAlated proteins were distributed across intracellular sperm compartments, and spermatozoa possess the CoASH biosynthetic enzymes PANK2 and CoASY, indicating an intrinsic capacity for CoAlation. Inhibition of CoASH biosynthesis reduced CoAlation and enhanced PKA substrate phosphorylation, tyrosine phosphorylation, hyperactivated motility, and the progesterone-induced acrosome reaction under capacitating conditions. Pantothenic acid supplementation increased CoAlation and suppressed these processes without impairing viability or baseline motility. These findings indicate that high levels of protein CoAlation in several protein bands are a pre-existing feature of the non-capacitated state that restrains the redox-regulated events of capacitation and that its decline is required to permit sperm capacitation. CoAlation levels may emerge as a biomarker of sperm capacitation and fertilizing competence.<\/jats:p>","DOI":"10.3390\/antiox15050600","type":"journal-article","created":{"date-parts":[[2026,5,20]],"date-time":"2026-05-20T16:39:34Z","timestamp":1779295174000},"page":"600","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Levels of Protein CoAlation Regulate Redox Signaling Events of Human Sperm Capacitation"],"prefix":"10.3390","volume":"15","author":[{"ORCID":"https:\/\/orcid.org\/0009-0007-3251-3897","authenticated-orcid":false,"given":"Chika","family":"Onochie","sequence":"first","affiliation":[{"name":"Department of Pharmacology and Therapeutics, McGill University, Montreal, QC H3G 1Y6, Canada"},{"name":"Department of Surgery, Urology Division, McGill University, Montreal, QC H4A 3J1, Canada"},{"name":"The Research Institute, McGill University Health Centre, Montreal, QC H4A 3J1, Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0001-6480-0619","authenticated-orcid":false,"given":"Valeriy","family":"Filonenko","sequence":"additional","affiliation":[{"name":"Department of Cell Signaling, Institute of Molecular Biology and Genetics, 03680 Kyiv, Ukraine"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9179-8393","authenticated-orcid":false,"given":"Ivan","family":"Gout","sequence":"additional","affiliation":[{"name":"Department of Cell Signaling, Institute of Molecular Biology and Genetics, 03680 Kyiv, Ukraine"},{"name":"Department of Structural and Molecular Biology, University College London, London WC1E 7JE, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8884-1274","authenticated-orcid":false,"given":"Cristian","family":"O\u2019Flaherty","sequence":"additional","affiliation":[{"name":"Department of Pharmacology and Therapeutics, McGill University, Montreal, QC H3G 1Y6, Canada"},{"name":"Department of Surgery, Urology Division, McGill University, Montreal, QC H4A 3J1, Canada"},{"name":"The Research Institute, McGill University Health Centre, Montreal, QC H4A 3J1, Canada"},{"name":"Anatomy and Cell Biology, McGill University, Montreal, QC H3A 0C7, Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2026,5,9]]},"reference":[{"key":"ref_1","unstructured":"WHO (2023). Infertility Prevalence Estimates, 1990\u20132021."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"F67","DOI":"10.1530\/REP-22-0200","article-title":"Oxidative stress and reproductive function: The protection of mammalian spermatozoa against oxidative stress","volume":"164","author":"Scarlata","year":"2022","journal-title":"Reproduction"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1080\/20905998.2024.2381972","article-title":"Idiopathic male infertility\u2014What are we missing?","volume":"23","author":"Boeri","year":"2025","journal-title":"Arab J. Urol."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"108","DOI":"10.5653\/cerm.2014.41.3.108","article-title":"Empirical medical therapy in idiopathic male infertility: Promise or panacea?","volume":"41","author":"Jung","year":"2014","journal-title":"Clin. Exp. Reprod. Med."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"1502","DOI":"10.1016\/j.fertnstert.2014.10.021","article-title":"Limitations of semen analysis as a test of male fertility and anticipated needs from newer tests","volume":"102","author":"Wang","year":"2014","journal-title":"Fertil. Steril."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"426","DOI":"10.4103\/1008-682X.175781","article-title":"Seminal biomarkers for the evaluation of male infertility","volume":"18","author":"Bieniek","year":"2016","journal-title":"Asian J. Androl."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"326","DOI":"10.1038\/170326a0","article-title":"The \u2018Capacitation\u2019 of the Mammalian Sperm","volume":"170","author":"Austin","year":"1952","journal-title":"Nature"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"1039","DOI":"10.1002\/mrd.22871","article-title":"Reactive oxygen species as mediators of sperm capacitation and pathological damage","volume":"84","author":"Aitken","year":"2017","journal-title":"Mol. Reprod. Dev."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1095\/biolreprod59.1.7","article-title":"Role of cholesterol in sperm capacitation","volume":"59","author":"Cross","year":"1998","journal-title":"Biol. Reprod."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"jcs238816","DOI":"10.1242\/jcs.238816","article-title":"Capacitation-associated alkalization in human sperm is differentially controlled at the subcellular level","volume":"133","year":"2020","journal-title":"J. Cell Sci."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"20979","DOI":"10.1038\/s41598-021-00494-1","article-title":"Nitric oxide-targeted protein phosphorylation during human sperm capacitation","volume":"11","author":"Staicu","year":"2021","journal-title":"Sci. Rep."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"315","DOI":"10.1080\/19396368.2022.2122761","article-title":"Participation of signaling proteins in sperm hyperactivation","volume":"68","year":"2022","journal-title":"Syst. Biol. Reprod. Med."},{"key":"ref_13","doi-asserted-by":"crossref","unstructured":"Gupta, S.K. (2021). Human Zona Pellucida Glycoproteins: Binding Characteristics with Human Spermatozoa and Induction of Acrosome Reaction. Front. Cell Dev. Biol., 9.","DOI":"10.3389\/fcell.2021.619868"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"437","DOI":"10.1089\/ars.2021.0117","article-title":"Redox Regulation to Modulate Phosphorylation Events in Human Spermatozoa","volume":"37","author":"Serafini","year":"2022","journal-title":"Antioxid. Redox Signal."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1093\/molehr\/gah046","article-title":"Phosphorylation of the Arginine-X-X-(Serine\/Threonine) motif in human sperm proteins during capacitation: Modulation and protein kinase A dependency","volume":"10","author":"Gagnon","year":"2004","journal-title":"Mol. Hum. Reprod."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"528","DOI":"10.1016\/j.freeradbiomed.2006.04.027","article-title":"Positive role of reactive oxygen species in mammalian sperm capacitation: Triggering and modulation of phosphorylation events","volume":"41","author":"Gagnon","year":"2006","journal-title":"Free Radic. Biol. Med."},{"key":"ref_17","first-page":"289","article-title":"Biological basis for human capacitation\u2014Revisited","volume":"23","year":"2017","journal-title":"Hum. Reprod. Update"},{"key":"ref_18","first-page":"167","article-title":"Decapacitation factors in semen","volume":"1","author":"Begley","year":"1982","journal-title":"Clin. Reprod. Fertil."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"R73","DOI":"10.1530\/REP-23-0188","article-title":"The other side of capacitation: Role of mouse male molecules in the regulation of time and place of capacitation","volume":"166","author":"Nicolli","year":"2023","journal-title":"Reproduction"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"672","DOI":"10.1002\/j.1939-4640.2001.tb02228.x","article-title":"Semenogelin, the main protein of semen coagulum, inhibits human sperm capacitation by interfering with the superoxide anion generated during this process","volume":"22","author":"Yoshida","year":"2001","journal-title":"J. Androl."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"25580","DOI":"10.1074\/jbc.M504103200","article-title":"Glycodelin-S in Human Seminal Plasma Reduces Cholesterol Efflux andInhibits Capacitation ofSpermatozoa","volume":"280","author":"Chiu","year":"2005","journal-title":"J. Biol. Chem."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"R21","DOI":"10.1530\/REP-13-0058","article-title":"Epididymosomes, prostasomes, and liposomes: Their roles in mammalian male reproductive physiology","volume":"146","author":"Sullivan","year":"2013","journal-title":"Reproduction"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1095\/biolreprod.105.044644","article-title":"The Identification of Mouse Sperm-Surface-Associated Proteins and Characterization of Their Ability to Act as Decapacitation Factors1","volume":"74","author":"Nixon","year":"2006","journal-title":"Biol. Reprod."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"334","DOI":"10.3109\/19396368.2010.512377","article-title":"Factors Regulating Sperm Capacitation","volume":"56","author":"Bailey","year":"2010","journal-title":"Syst. Biol. Reprod. Med."},{"key":"ref_25","doi-asserted-by":"crossref","unstructured":"Onochie, C., Evi, K., and O\u2019Flaherty, C. (2025). Role of Redox-Induced Protein Modifications in Spermatozoa in Health and Disease. Antioxidants, 14.","DOI":"10.3390\/antiox14060720"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"14","DOI":"10.1016\/j.freeradbiomed.2019.05.035","article-title":"The role of thiols in antioxidant systems","volume":"140","author":"Ulrich","year":"2019","journal-title":"Free Radic. Biol. Med."},{"key":"ref_27","doi-asserted-by":"crossref","unstructured":"Federici, L., Masulli, M., Laurenzi, V.D., Allocati, N., Federici, L., Masulli, M., De Laurenzi, V., and Allocati, N. (2024). The Role of S-Glutathionylation in Health and Disease: A Bird\u2019s Eye View. Nutrients, 16.","DOI":"10.3390\/nu16162753"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"641","DOI":"10.1095\/biolreprod12.5.641","article-title":"The glutathione and thiol content of mammalian spermatozoa and seminal plasma","volume":"12","author":"Li","year":"1975","journal-title":"Biol. Reprod."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"721","DOI":"10.1042\/BST20170506","article-title":"Coenzyme A, protein CoAlation and redox regulation in mammalian cells","volume":"46","author":"Gout","year":"2018","journal-title":"Biochem. Soc. Trans."},{"key":"ref_30","doi-asserted-by":"crossref","unstructured":"Petrone, O., Serafini, S., Yu, B.Y.K., Filonenko, V., Gout, I., and O\u2019Flaherty, C. (2023). Changes of the Protein CoAlation Pattern in Response to Oxidative Stress and Capacitation in Human Spermatozoa. Int. J. Mol. Sci., 24.","DOI":"10.3390\/ijms241512526"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"187","DOI":"10.7124\/bc.0008DF","article-title":"Generation and characterization of monoclonal antibodies specific to Coenzyme A","volume":"31","author":"Malanchuk","year":"2015","journal-title":"Biopolymers Cell"},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"502","DOI":"10.1016\/j.freeradbiomed.2008.11.004","article-title":"Reactive oxygen-induced reactive oxygen formation during human sperm capacitation","volume":"46","author":"Lamothe","year":"2009","journal-title":"Free Radic. Biol. Med."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"48","DOI":"10.1530\/ror.0.0020048","article-title":"Reactive oxygen species and sperm physiology","volume":"2","author":"Lamirande","year":"1997","journal-title":"Rev. Reprod."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1016\/0891-5849(93)90006-G","article-title":"Human sperm hyperactivation and capacitation as parts of an oxidative process","volume":"14","author":"Lamirande","year":"1993","journal-title":"Free Radic. Biol. Med."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"643","DOI":"10.1016\/S0891-5849(96)00379-6","article-title":"Regulation of protein-tyrosine phosphorylation and human sperm capacitation by reactive oxygen derivatives","volume":"22","author":"Leclerc","year":"1997","journal-title":"Free Radic. Biol. Med."},{"key":"ref_36","first-page":"238","article-title":"Hydrogen Peroxide Modifies Human Sperm Peroxiredoxins in a Dose-Dependent Manner1","volume":"84","year":"2010","journal-title":"Biol. Reprod."},{"key":"ref_37","doi-asserted-by":"crossref","unstructured":"Ramu, S., and Jeyendran, R.S. (2012). The hypo-osmotic swelling test for evaluation of sperm membrane integrity. Spermatogenesis: Methods and Protocols, Springer.","DOI":"10.1007\/978-1-62703-038-0_3"},{"key":"ref_38","unstructured":"Carrell, D.T., and Aston, K.I. (2013). Computer-Aided Sperm Analysis (CASA) of Sperm Motility and Hyperactivation. Spermatogenesis: Methods and Protocols, Humana Press."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"418","DOI":"10.1093\/humrep\/det454","article-title":"The CatSper calcium channel in human sperm: Relation with motility and involvement in progesterone-induced acrosome reaction","volume":"29","author":"Tamburrino","year":"2014","journal-title":"Hum. Reprod."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1016\/j.plipres.2005.04.001","article-title":"Coenzyme A: Back in action","volume":"44","author":"Leonardi","year":"2005","journal-title":"Prog. Lipid Res."},{"key":"ref_41","unstructured":"The Human Protein Atlas (2026, February 13). PANK2\u2014Tissue Expression in Testis. Available online: https:\/\/www.proteinatlas.org\/ENSG00000125779-PANK2\/tissue\/testis."},{"key":"ref_42","unstructured":"The Human Protein Atlas (2026, February 13). PANK4\u2014Tissue Expression in Testis. Available online: https:\/\/www.proteinatlas.org\/ENSG00000157881-PANK4\/tissue\/testis."},{"key":"ref_43","unstructured":"The Human Protein Atlas (2026, February 13). PANK3\u2014Tissue Expression in Testis. Available online: https:\/\/www.proteinatlas.org\/ENSG00000120137-PANK3\/tissue\/testis."},{"key":"ref_44","unstructured":"The Human Protein Atlas (2026, February 13). PANK1\u2014Tissue Expression in Testis. Available online: https:\/\/www.proteinatlas.org\/ENSG00000152782-PANK1\/tissue\/testis."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1093\/hmg\/ddi005","article-title":"Deficiency of pantothenate kinase 2 (Pank2) in mice leads to retinal degeneration and azoospermia","volume":"14","author":"Kuo","year":"2005","journal-title":"Hum. Mol. Genet."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1093\/hmg\/ddg026","article-title":"An isoform of hPANK2, deficient in pantothenate kinase-associated neurodegeneration, localizes to mitochondria","volume":"12","author":"Prokisch","year":"2003","journal-title":"Hum. Mol. Genet."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"2401","DOI":"10.1021\/acschembio.1c00535","article-title":"The Coenzyme A Level Modulator Hopantenate (HoPan) Inhibits Phosphopantotenoylcysteine Synthetase Activity","volume":"16","author":"Mostert","year":"2021","journal-title":"ACS Chem. Biol."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1038\/aja.2009.6","article-title":"NYD-SP27, a novel intrinsic decapacitation factor in sperm","volume":"11","author":"Bi","year":"2009","journal-title":"Asian J. Androl."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"21827","DOI":"10.1074\/jbc.M603952200","article-title":"Oxidant-induced Activation of Type I Protein Kinase A Is Mediated by RI Subunit Interprotein Disulfide Bond Formation","volume":"281","author":"Brennan","year":"2006","journal-title":"J. Biol. Chem."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"101318","DOI":"10.1016\/j.redox.2019.101318","article-title":"Covalent Aurora A regulation by the metabolic integrator coenzyme A","volume":"28","author":"Tsuchiya","year":"2020","journal-title":"Redox Biol."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"1603","DOI":"10.1093\/biolre\/ioab168","article-title":"Aurora A Kinase (AURKA) is required for male germline maintenance and regulates sperm motility in the mouse","volume":"105","author":"Lester","year":"2021","journal-title":"Biol. Reprod."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1016\/j.bbrc.2018.05.170","article-title":"Novel localization of Aurora A kinase in mouse testis suggests multiple roles in spermatogenesis","volume":"503","author":"Johnson","year":"2018","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_53","first-page":"256","article-title":"Redox regulation of cardiac protein kinase C","volume":"10","author":"Korichneva","year":"2005","journal-title":"Exp. Clin. Cardiol."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"230","DOI":"10.1016\/j.ydbio.2003.10.034","article-title":"Crosstalk between protein kinase A and C regulates phospholipase D and F-actin formation during sperm capacitation","volume":"267","author":"Cohen","year":"2004","journal-title":"Dev. Biol."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"2652","DOI":"10.1093\/humrep\/den314","article-title":"Src activation triggers capacitation and acrosome reaction but not motility in human spermatozoa","volume":"23","author":"Varano","year":"2008","journal-title":"Hum. Reprod."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"4522","DOI":"10.1038\/s41467-018-06790-1","article-title":"Direct cysteine sulfenylation drives activation of the Src kinase","volume":"9","author":"Heppner","year":"2018","journal-title":"Nat. Commun."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1016\/j.ydbio.2009.06.022","article-title":"Phosphorylation and consequent stimulation of the tyrosine kinase c-Abl by PKA in mouse spermatozoa; its implications during capacitation","volume":"333","author":"Baker","year":"2009","journal-title":"Dev. Biol."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"12961","DOI":"10.1074\/jbc.M300058200","article-title":"Functional Interaction between the c-Abl and Arg Protein-tyrosine Kinases in the Oxidative Stress Response","volume":"278","author":"Cao","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"72","DOI":"10.1186\/s12964-023-01080-w","article-title":"New insights into posttranslational modifications of proteins during bull sperm capacitation","volume":"21","author":"Majewska","year":"2023","journal-title":"Cell Commun. Signal."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"1271","DOI":"10.1016\/S0891-5849(03)00501-X","article-title":"Redox control of changes in protein sulfhydryl levels during human sperm capacitation","volume":"35","author":"Lamirande","year":"2003","journal-title":"Free Radic. Biol. Med."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"3410","DOI":"10.1128\/JB.185.11.3410-3415.2003","article-title":"Role of feedback regulation of pantothenate kinase (CoaA) in control of coenzyme A levels in Escherichia coli","volume":"185","author":"Rock","year":"2003","journal-title":"J. Bacteriol."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1111\/j.1365-2605.2010.01078.x","article-title":"Evaluation of mitochondrial respiratory efficiency during in vitro capacitation of human spermatozoa","volume":"34","author":"Stendardi","year":"2011","journal-title":"Int. J. Androl."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"e23486","DOI":"10.1096\/fj.202301957RR","article-title":"Mitochondrial function and reactive oxygen species production during human sperm capacitation: Unraveling key players","volume":"38","author":"Irigoyen","year":"2024","journal-title":"FASEB J."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"172","DOI":"10.1016\/S0015-0282(16)38822-7","article-title":"Metabolic changes in human spermatozoa related to capacitation","volume":"23","author":"Hicks","year":"1972","journal-title":"Fertil. Steril."},{"key":"ref_65","doi-asserted-by":"crossref","unstructured":"Bakovi\u0107, J., Mart\u00ednez, D.L., Nikolaou, S., Yu, B.Y.K., Tossounian, M.-A., Tsuchiya, Y., Thrasivoulou, C., Filonenko, V., and Gout, I. (2021). Regulation of the CoA Biosynthetic Complex Assembly in Mammalian Cells. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms22031131"},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"R163","DOI":"10.1530\/REP-13-0178","article-title":"Mitochondria functionality and sperm quality","volume":"146","author":"Amaral","year":"2013","journal-title":"Reproduction"},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"524","DOI":"10.1002\/prca.200601013","article-title":"Identification of gene products present in Triton X-100 soluble and insoluble fractions of human spermatozoa lysates using LC-MS\/MS analysis","volume":"1","author":"Baker","year":"2007","journal-title":"Proteom. Clin. Appl."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"4639","DOI":"10.1016\/j.febslet.2007.08.056","article-title":"Localization and regulation of mouse pantothenate kinase 2","volume":"581","author":"Leonardi","year":"2007","journal-title":"FEBS Lett."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"313","DOI":"10.1093\/humupd\/dml057","article-title":"Altered protamine expression and diminished spermatogenesis: What is the link?","volume":"13","author":"Carrell","year":"2007","journal-title":"Hum. Reprod. Update"},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"1025","DOI":"10.2164\/jandrol.111.015982","article-title":"Human Sperm Chromatin Undergoes Physiological Remodeling During In Vitro Capacitation and Acrosome Reaction","volume":"33","author":"Gabriel","year":"2012","journal-title":"J. Androl."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1089\/152308604771978327","article-title":"The mammalian testis-specific thioredoxin system","volume":"6","author":"Sadek","year":"2004","journal-title":"Antioxid. Redox Signal"},{"key":"ref_72","unstructured":"The Human Protein Atlas (2026, February 13). TXNRD3\u2014Tissue Expression in Testis. Available online: https:\/\/www.proteinatlas.org\/ENSG00000197763-TXNRD3\/tissue\/testis."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"547","DOI":"10.1089\/ars.2007.1821","article-title":"Expression pattern of human glutaredoxin 2 isoforms: Identification and characterization of two testis\/cancer cell-specific isoforms","volume":"10","author":"Hudemann","year":"2008","journal-title":"Antioxid. Redox Signal"}],"container-title":["Antioxidants"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2076-3921\/15\/5\/600\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,5,21]],"date-time":"2026-05-21T04:32:30Z","timestamp":1779337950000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2076-3921\/15\/5\/600"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,5,9]]},"references-count":73,"journal-issue":{"issue":"5","published-online":{"date-parts":[[2026,5]]}},"alternative-id":["antiox15050600"],"URL":"https:\/\/doi.org\/10.3390\/antiox15050600","relation":{},"ISSN":["2076-3921"],"issn-type":[{"value":"2076-3921","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,5,9]]}}}