{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,14]],"date-time":"2026-06-14T23:15:55Z","timestamp":1781478955024,"version":"3.54.1"},"reference-count":106,"publisher":"Springer Science and Business Media LLC","issue":"1","license":[{"start":{"date-parts":[[2024,8,29]],"date-time":"2024-08-29T00:00:00Z","timestamp":1724889600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0"},{"start":{"date-parts":[[2024,8,29]],"date-time":"2024-08-29T00:00:00Z","timestamp":1724889600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Sci Rep"],"DOI":"10.1038\/s41598-024-71056-4","type":"journal-article","created":{"date-parts":[[2024,8,30]],"date-time":"2024-08-30T07:03:11Z","timestamp":1725001391000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":10,"title":["Bottom-up approach to deciphering the targets of the ubiquitin-proteasome system in porcine sperm capacitation"],"prefix":"10.1038","volume":"14","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-2964-5940","authenticated-orcid":false,"given":"Michal","family":"Zigo","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jacob","family":"Netherton","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nat\u00e1lie","family":"Zelenkov\u00e1","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Karl","family":"Kerns","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Veronika","family":"Kraus","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pavla","family":"Postlerov\u00e1","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mark","family":"Baker","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Peter","family":"Sutovsky","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2024,8,29]]},"reference":[{"key":"71056_CR1","first-page":"581","volume":"4","author":"CR Austin","year":"1951","unstructured":"Austin, C. R. Observations on the penetration of the sperm in the mammalian egg. Aust. J. Sci. Res. Ser. B Biol. Sci. 4, 581\u2013596 (1951).","journal-title":"Aust. J. Sci. Res. Ser. B Biol. Sci."},{"key":"71056_CR2","doi-asserted-by":"publisher","first-page":"697","DOI":"10.1038\/168697b0","volume":"168","author":"MC Chang","year":"1951","unstructured":"Chang, M. C. Fertilizing capacity of spermatozoa deposited into the fallopian tubes. Nature 168, 697\u2013698 (1951).","journal-title":"Nature"},{"key":"71056_CR3","doi-asserted-by":"publisher","first-page":"1105","DOI":"10.1095\/biolreprod58.5.1105","volume":"58","author":"SS Suarez","year":"1998","unstructured":"Suarez, S. S. The oviductal sperm reservoir in mammals: Mechanisms of formation. Biol. Reprod. 58, 1105\u20131107. https:\/\/doi.org\/10.1095\/biolreprod58.5.1105 (1998).","journal-title":"Biol. Reprod."},{"key":"71056_CR4","doi-asserted-by":"publisher","first-page":"55","DOI":"10.1016\/B978-012515400-0\/50007-5","volume-title":"Knobil and Neill's Physiology of Reproduction","author":"HM Florman","year":"2006","unstructured":"Florman, H. M. & Ducibella, T. Fertilization in Mammals. In Knobil and Neill\u2019s Physiology of Reproduction Vol. 1 (ed. Neill, J. D.) 55\u2013112 (Elsevier Academic Press, Inc., 2006)."},{"key":"71056_CR5","doi-asserted-by":"publisher","first-page":"149","DOI":"10.1016\/B978-0-12-397175-3.00004-1","volume-title":"Knobil and Neill's Physiology of Reproduction","author":"HM Florman","year":"2015","unstructured":"Florman, H. M. & Fissore, R. A. Fertilization in Mammals. In Knobil and Neill\u2019s Physiology of Reproduction (eds Plant, T. N. & Zeleznik, A. J.) 149\u2013196 (Elsevier, 2015)."},{"key":"71056_CR6","unstructured":"Yanagimachi, R. in The Physiology of Reproduction Vol. 1 (eds E. Knobil & J.D. Neill) Ch. 2, 189\u2013317 (Raven Press, 1994)."},{"key":"71056_CR7","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0003040","volume":"3","author":"HA Guidobaldi","year":"2008","unstructured":"Guidobaldi, H. A., Teves, M. E., U\u00f1ates, D. R., Anastas\u00eda, A. & Giojalas, L. C. Progesterone from the cumulus cells is the sperm chemoattractant secreted by the rabbit oocyte cumulus complex. PloS One 3, e3040. https:\/\/doi.org\/10.1371\/journal.pone.0003040 (2008).","journal-title":"PloS One"},{"key":"71056_CR8","doi-asserted-by":"publisher","first-page":"2339","DOI":"10.1093\/humrep\/den265","volume":"23","author":"R Oren-Benaroya","year":"2008","unstructured":"Oren-Benaroya, R., Orvieto, R., Gakamsky, A., Pinchasov, M. & Eisenbach, M. The sperm chemoattractant secreted from human cumulus cells is progesterone. Hum. Reproduct. 23, 2339\u20132345. https:\/\/doi.org\/10.1093\/humrep\/den265 (2008).","journal-title":"Hum. Reproduct."},{"key":"71056_CR9","doi-asserted-by":"publisher","first-page":"501","DOI":"10.1530\/rep-15-0582","volume":"151","author":"S P\u00e9rez-Cerezales","year":"2016","unstructured":"P\u00e9rez-Cerezales, S., L\u00f3pez-Cardona, A. P. & Guti\u00e9rrez-Ad\u00e1n, A. Progesterone effects on mouse sperm kinetics in conditions of viscosity. Reproduction 151, 501\u2013507. https:\/\/doi.org\/10.1530\/rep-15-0582 (2016).","journal-title":"Reproduction"},{"key":"71056_CR10","doi-asserted-by":"publisher","first-page":"745","DOI":"10.1016\/j.fertnstert.2006.02.080","volume":"86","author":"ME Teves","year":"2006","unstructured":"Teves, M. E. et al. Progesterone at the picomolar range is a chemoattractant for mammalian spermatozoa. Fertil. Steril. 86, 745\u2013749. https:\/\/doi.org\/10.1016\/j.fertnstert.2006.02.080 (2006).","journal-title":"Fertil. Steril."},{"key":"71056_CR11","doi-asserted-by":"publisher","first-page":"1183","DOI":"10.1016\/s0015-0282(16)57982-5","volume":"64","author":"C Villanueva-D\u00edaz","year":"1995","unstructured":"Villanueva-D\u00edaz, C., Arias-Mart\u00ednez, J., Bermejo-Mart\u00ednez, L. & Vadillo-Ortega, F. Progesterone induces human sperm chemotaxis. Fertil. Steril. 64, 1183\u20131188. https:\/\/doi.org\/10.1016\/s0015-0282(16)57982-5 (1995).","journal-title":"Fertil. Steril."},{"key":"71056_CR12","doi-asserted-by":"publisher","first-page":"2061","DOI":"10.1038\/s41467-018-04523-y","volume":"9","author":"K Kerns","year":"2018","unstructured":"Kerns, K., Zigo, M., Drobnis, E. Z., Sutovsky, M. & Sutovsky, P. Zinc ion flux during mammalian sperm capacitation. Nat. Commun. 9, 2061. https:\/\/doi.org\/10.1038\/s41467-018-04523-y (2018).","journal-title":"Nat. Commun."},{"key":"71056_CR13","doi-asserted-by":"publisher","first-page":"4097","DOI":"10.3390\/ijms19124097","volume":"19","author":"K Kerns","year":"2018","unstructured":"Kerns, K., Zigo, M. & Sutovsky, P. Zinc: A necessary ion for mammalian sperm fertilization competency. Int. J. Mol. Sci. 19, 4097. https:\/\/doi.org\/10.3390\/ijms19124097 (2018).","journal-title":"Int. J. Mol. Sci."},{"key":"71056_CR14","doi-asserted-by":"publisher","DOI":"10.1242\/dev.176966","author":"HH Bhakta","year":"2019","unstructured":"Bhakta, H. H., Refai, F. H. & Avella, M. A. The molecular mechanisms mediating mammalian fertilization. Development https:\/\/doi.org\/10.1242\/dev.176966 (2019).","journal-title":"Development"},{"key":"71056_CR15","doi-asserted-by":"publisher","DOI":"10.1083\/jcb.202102146","author":"KK Siu","year":"2021","unstructured":"Siu, K. K., Serr\u00e3o, V. H. B., Ziyyat, A. & Lee, J. E. The cell biology of fertilization: Gamete attachment and fusion. J. Cell Biol. https:\/\/doi.org\/10.1083\/jcb.202102146 (2021).","journal-title":"J. Cell Biol."},{"key":"71056_CR16","doi-asserted-by":"publisher","first-page":"133","DOI":"10.3390\/cells10010133","volume":"10","author":"L Tumova","year":"2021","unstructured":"Tumova, L., Zigo, M., Sutovsky, P., Sedmikova, M. & Postlerova, P. Ligands and receptors involved in the sperm-zona pellucida interactions in mammals. Cells 10, 133. https:\/\/doi.org\/10.3390\/cells10010133 (2021).","journal-title":"Cells"},{"key":"71056_CR17","doi-asserted-by":"publisher","first-page":"334","DOI":"10.3109\/19396368.2010.512377","volume":"56","author":"JL Bailey","year":"2010","unstructured":"Bailey, J. L. Factors regulating sperm capacitation. Syst. Biol. Reproduct. Med. 56, 334\u2013348. https:\/\/doi.org\/10.3109\/19396368.2010.512377 (2010).","journal-title":"Syst. Biol. Reproduct. Med."},{"key":"71056_CR18","doi-asserted-by":"publisher","first-page":"650","DOI":"10.1016\/0006-291x(77)90352-7","volume":"74","author":"LT Hunt","year":"1977","unstructured":"Hunt, L. T. & Dayhoff, M. O. Amino-terminal sequence identity of ubiquitin and the nonhistone component of nuclear protein A24. Biochem. Biophys. Res. Commun. 74, 650\u2013655. https:\/\/doi.org\/10.1016\/0006-291x(77)90352-7 (1977).","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"71056_CR19","doi-asserted-by":"publisher","first-page":"1079","DOI":"10.1016\/0006-291x(85)91050-2","volume":"128","author":"A Hershko","year":"1985","unstructured":"Hershko, A. & Heller, H. Occurrence of a polyubiquitin structure in ubiquitin-protein conjugates. Biochem. Biophys. Res. Commun. 128, 1079\u20131086. https:\/\/doi.org\/10.1016\/0006-291x(85)91050-2 (1985).","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"71056_CR20","doi-asserted-by":"publisher","first-page":"2400","DOI":"10.1016\/S0021-9258(17)35950-1","volume":"261","author":"R Hough","year":"1986","unstructured":"Hough, R., Pratt, G. & Rechsteiner, M. Ubiquitin-lysozyme conjugates. Identification and characterization of an ATP-dependent protease from rabbit reticulocyte lysates. J. Biol. Chem. 261, 2400\u20132408 (1986).","journal-title":"J. Biol. Chem."},{"key":"71056_CR21","doi-asserted-by":"publisher","first-page":"2451","DOI":"10.1016\/S0021-9258(18)61525-X","volume":"262","author":"L Waxman","year":"1987","unstructured":"Waxman, L., Fagan, J. M. & Goldberg, A. L. Demonstration of two distinct high molecular weight proteases in rabbit reticulocytes, one of which degrades ubiquitin conjugates. J. Biol. Chem. 262, 2451\u20132457 (1987).","journal-title":"J. Biol. Chem."},{"key":"71056_CR22","doi-asserted-by":"publisher","first-page":"2537","DOI":"10.1016\/S0021-9258(18)34957-3","volume":"257","author":"A Ciechanover","year":"1982","unstructured":"Ciechanover, A., Elias, S., Heller, H. & Hershko, A. \u201cCovalent affinity\u201d purification of ubiquitin-activating enzyme. J. Biol. Chem. 257, 2537\u20132542 (1982).","journal-title":"J. Biol. Chem."},{"key":"71056_CR23","doi-asserted-by":"publisher","first-page":"8206","DOI":"10.1016\/S0021-9258(20)82050-X","volume":"258","author":"A Hershko","year":"1983","unstructured":"Hershko, A., Heller, H., Elias, S. & Ciechanover, A. Components of ubiquitin-protein ligase system. Resolution, affinity purification, and role in protein breakdown. J. Biol. Chem. 258, 8206\u20138214 (1983).","journal-title":"J. Biol. Chem."},{"key":"71056_CR24","doi-asserted-by":"publisher","first-page":"341","DOI":"10.1016\/j.beha.2017.09.001","volume":"30","author":"A Ciechanover","year":"2017","unstructured":"Ciechanover, A. Intracellular protein degradation: From a vague idea thru the lysosome and the ubiquitin-proteasome system and onto human diseases and drug targeting. Best Pract. Res. Clin. Haematol. 30, 341\u2013355. https:\/\/doi.org\/10.1016\/j.beha.2017.09.001 (2017).","journal-title":"Best Pract. Res. Clin. Haematol."},{"key":"71056_CR25","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1530\/rep-11-0041","volume":"142","author":"P Sutovsky","year":"2011","unstructured":"Sutovsky, P. Sperm proteasome and fertilization. Reproduction 142, 1\u201314. https:\/\/doi.org\/10.1530\/rep-11-0041 (2011).","journal-title":"Reproduction"},{"key":"71056_CR26","doi-asserted-by":"publisher","first-page":"373","DOI":"10.1152\/physrev.00027.2001","volume":"82","author":"MH Glickman","year":"2002","unstructured":"Glickman, M. H. & Ciechanover, A. The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction. Physiol. Rev. 82, 373\u2013428. https:\/\/doi.org\/10.1152\/physrev.00027.2001 (2002).","journal-title":"Physiol. Rev."},{"key":"71056_CR27","doi-asserted-by":"publisher","first-page":"177","DOI":"10.1038\/nrm1336","volume":"5","author":"CM Pickart","year":"2004","unstructured":"Pickart, C. M. & Cohen, R. E. Proteasomes and their kin: Proteases in the machine age. Nat. Rev. Mol. Cell Biol. 5, 177\u2013187. https:\/\/doi.org\/10.1038\/nrm1336 (2004).","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"71056_CR28","doi-asserted-by":"publisher","first-page":"79","DOI":"10.1038\/nrm1552","volume":"6","author":"A Ciechanover","year":"2005","unstructured":"Ciechanover, A. Proteolysis: From the lysosome to ubiquitin and the proteasome. Nat. Rev. Mol. Cell Biol. 6, 79\u201387. https:\/\/doi.org\/10.1038\/nrm1552 (2005).","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"71056_CR29","doi-asserted-by":"publisher","first-page":"2","DOI":"10.1095\/biolreprod.104.031245","volume":"72","author":"G Manandhar","year":"2005","unstructured":"Manandhar, G., Schatten, H. & Sutovsky, P. Centrosome reduction during gametogenesis and its significance. Biol. Reproduct. 72, 2\u201313. https:\/\/doi.org\/10.1095\/biolreprod.104.031245 (2005).","journal-title":"Biol. Reproduct."},{"key":"71056_CR30","doi-asserted-by":"publisher","first-page":"89","DOI":"10.1007\/978-1-4939-0817-2_5","volume":"759","author":"NR Mtango","year":"2014","unstructured":"Mtango, N. R., Latham, K. E. & Sutovsky, P. Deubiquitinating enzymes in oocyte maturation, fertilization and preimplantation embryo development. Adv. Exp. Med. Biol. 759, 89\u2013110. https:\/\/doi.org\/10.1007\/978-1-4939-0817-2_5 (2014).","journal-title":"Adv. Exp. Med. Biol."},{"key":"71056_CR31","doi-asserted-by":"publisher","first-page":"88","DOI":"10.1002\/jemt.10319","volume":"61","author":"P Sutovsky","year":"2003","unstructured":"Sutovsky, P. Ubiquitin-dependent proteolysis in mammalian spermatogenesis, fertilization, and sperm quality control: Killing three birds with one stone. Microscopy Res. Tech. 61, 88\u2013102. https:\/\/doi.org\/10.1002\/jemt.10319 (2003).","journal-title":"Microscopy Res. Tech."},{"key":"71056_CR32","doi-asserted-by":"publisher","first-page":"117","DOI":"10.1095\/biolreprod.115.136622","volume":"94","author":"K Kerns","year":"2016","unstructured":"Kerns, K., Morales, P. & Sutovsky, P. Regulation of sperm capacitation by the 26S proteasome: An emerging new paradigm in spermatology. Biol. Reproduct. 94, 117. https:\/\/doi.org\/10.1095\/biolreprod.115.136622 (2016).","journal-title":"Biol. Reproduct."},{"key":"71056_CR33","doi-asserted-by":"publisher","DOI":"10.1155\/2014\/981867","volume":"2014","author":"WH Song","year":"2014","unstructured":"Song, W. H., Ballard, J. W., Yi, Y. J. & Sutovsky, P. Regulation of mitochondrial genome inheritance by autophagy and ubiquitin-proteasome system: implications for health, fitness, and fertility. BioMed Res. Int. 2014, 981867. https:\/\/doi.org\/10.1155\/2014\/981867 (2014).","journal-title":"BioMed Res. Int."},{"key":"71056_CR34","doi-asserted-by":"publisher","DOI":"10.1017\/s1462399409001045","volume":"11","author":"P Sutovsky","year":"2009","unstructured":"Sutovsky, P. Sperm-egg adhesion and fusion in mammals. Expert Rev. Mol. Med. 11, e11. https:\/\/doi.org\/10.1017\/s1462399409001045 (2009).","journal-title":"Expert Rev. Mol. Med."},{"key":"71056_CR35","doi-asserted-by":"publisher","first-page":"56","DOI":"10.1071\/rd17364","volume":"30","author":"P Sutovsky","year":"2017","unstructured":"Sutovsky, P. & Song, W. H. Post-fertilisation sperm mitophagy: the tale of Mitochondrial Eve and Steve. Reproduct. Fertil. Dev. 30, 56\u201363. https:\/\/doi.org\/10.1071\/rd17364 (2017).","journal-title":"Reproduct. Fertil. Dev."},{"key":"71056_CR36","doi-asserted-by":"publisher","first-page":"24","DOI":"10.1016\/S1472-6483(10)60495-6","volume":"8","author":"P Sutovsky","year":"2004","unstructured":"Sutovsky, P., Van Leyen, K., McCauley, T., Day, B. N. & Sutovsky, M. Degradation of paternal mitochondria after fertilization: Implications for heteroplasmy, assisted reproductive technologies and mtDNA inheritance. Reproduct. Biomed. Online 8, 24\u201333 (2004).","journal-title":"Reproduct. Biomed. Online"},{"key":"71056_CR37","first-page":"385","volume":"63","author":"YJ Yi","year":"2007","unstructured":"Yi, Y. J., Manandhar, G., Oko, R. J., Breed, W. G. & Sutovsky, P. Mechanism of sperm-zona pellucida penetration during mammalian fertilization: 26S proteasome as a candidate egg coat lysin. Soc. Reproduct. Fertil. Suppl. 63, 385\u2013408 (2007).","journal-title":"Soc. Reproduct. Fertil. Suppl."},{"key":"71056_CR38","doi-asserted-by":"publisher","first-page":"237","DOI":"10.1007\/s00441-020-03181-1","volume":"380","author":"M Zigo","year":"2020","unstructured":"Zigo, M. et al. Porcine model for the study of sperm capacitation, fertilization and male fertility. Cell Tissue Res. 380, 237\u2013262. https:\/\/doi.org\/10.1007\/s00441-020-03181-1 (2020).","journal-title":"Cell Tissue Res."},{"key":"71056_CR39","doi-asserted-by":"publisher","first-page":"19","DOI":"10.1016\/j.jri.2009.07.006","volume":"83","author":"S Zimmerman","year":"2009","unstructured":"Zimmerman, S. & Sutovsky, P. The sperm proteasome during sperm capacitation and fertilization. J. Reproduct. Immunol. 83, 19\u201325. https:\/\/doi.org\/10.1016\/j.jri.2009.07.006 (2009).","journal-title":"J. Reproduct. Immunol."},{"key":"71056_CR40","doi-asserted-by":"publisher","first-page":"1665","DOI":"10.1242\/jcs.114.9.1665","volume":"114","author":"P Sutovsky","year":"2001","unstructured":"Sutovsky, P. et al. A putative, ubiquitin-dependent mechanism for the recognition and elimination of defective spermatozoa in the mammalian epididymis. J. Cell Sci. 114, 1665\u20131675 (2001).","journal-title":"J. Cell Sci."},{"key":"71056_CR41","doi-asserted-by":"publisher","first-page":"684","DOI":"10.1002\/jcp.21349","volume":"215","author":"KM Baska","year":"2008","unstructured":"Baska, K. M. et al. Mechanism of extracellular ubiquitination in the mammalian epididymis. J. Cell. Physiol. 215, 684\u2013696. https:\/\/doi.org\/10.1002\/jcp.21349 (2008).","journal-title":"J. Cell. Physiol."},{"key":"71056_CR42","doi-asserted-by":"publisher","first-page":"6446","DOI":"10.1038\/s41598-022-10390-x","volume":"12","author":"M Sharif","year":"2022","unstructured":"Sharif, M. et al. Hyperactivation is sufficient to release porcine sperm from immobilized oviduct glycans. Sci. Rep. 12, 6446. https:\/\/doi.org\/10.1038\/s41598-022-10390-x (2022).","journal-title":"Sci. Rep."},{"key":"71056_CR43","doi-asserted-by":"publisher","first-page":"449","DOI":"10.1530\/rep-20-0474","volume":"161","author":"M Sharif","year":"2021","unstructured":"Sharif, M., Kerns, K., Sutovsky, P., Bovin, N. & Miller, D. J. Progesterone induces porcine sperm release from oviduct glycans in a proteasome-dependent manner. Reproduction 161, 449\u2013457. https:\/\/doi.org\/10.1530\/rep-20-0474 (2021).","journal-title":"Reproduction"},{"key":"71056_CR44","doi-asserted-by":"publisher","first-page":"283","DOI":"10.1530\/rep-18-0413","volume":"157","author":"M Zigo","year":"2019","unstructured":"Zigo, M., Jonakova, V., Manaskova-Postlerova, P., Kerns, K. & Sutovsky, P. Ubiquitin-proteasome system participates in the de-aggregation of spermadhesin and DQH protein during boar sperm capacitation. Reproduction 157, 283\u2013295. https:\/\/doi.org\/10.1530\/rep-18-0413 (2019).","journal-title":"Reproduction"},{"key":"71056_CR45","doi-asserted-by":"publisher","first-page":"591","DOI":"10.1007\/s00441-017-2786-6","volume":"372","author":"M Zigo","year":"2018","unstructured":"Zigo, M., Kerns, K., Sutovsky, M. & Sutovsky, P. Modifications of the 26S proteasome during boar sperm capacitation. Cell Tissue Res. 372, 591\u2013601. https:\/\/doi.org\/10.1007\/s00441-017-2786-6 (2018).","journal-title":"Cell Tissue Res."},{"key":"71056_CR46","doi-asserted-by":"publisher","first-page":"996","DOI":"10.3390\/biom13060996","volume":"13","author":"M Zigo","year":"2023","unstructured":"Zigo, M., Kerns, K. & Sutovsky, P. The ubiquitin-proteasome system participates in sperm surface subproteome remodeling during boar sperm capacitation. Biomolecules 13, 996. https:\/\/doi.org\/10.3390\/biom13060996 (2023).","journal-title":"Biomolecules"},{"key":"71056_CR47","doi-asserted-by":"publisher","first-page":"12583","DOI":"10.1038\/s41598-019-49024-0","volume":"9","author":"M Zigo","year":"2019","unstructured":"Zigo, M., Manaskova-Postlerova, P., Jonakova, V., Kerns, K. & Sutovsky, P. Compartmentalization of the proteasome-interacting proteins during sperm capacitation. Sci. Rep. 9, 12583. https:\/\/doi.org\/10.1038\/s41598-019-49024-0 (2019).","journal-title":"Sci. Rep."},{"key":"71056_CR48","doi-asserted-by":"publisher","first-page":"197","DOI":"10.1007\/7651_2018_158","volume":"1854","author":"WH Song","year":"2019","unstructured":"Song, W. H. & Sutovsky, P. Porcine cell-free system to study mammalian sperm mitophagy. Methods Mol. Biol. 1854, 197\u2013207. https:\/\/doi.org\/10.1007\/7651_2018_158 (2019).","journal-title":"Methods Mol. Biol."},{"key":"71056_CR49","doi-asserted-by":"publisher","first-page":"2510","DOI":"10.1080\/15548627.2016.1239004","volume":"12","author":"WH Song","year":"2016","unstructured":"Song, W. H., Yi, Y. J., Sutovsky, M., Meyers, S. & Sutovsky, P. The ART and science of sperm mitophagy. Autophagy 12, 2510\u20132511. https:\/\/doi.org\/10.1080\/15548627.2016.1239004 (2016).","journal-title":"Autophagy"},{"key":"71056_CR50","doi-asserted-by":"publisher","first-page":"E5261","DOI":"10.1073\/pnas.1605844113","volume":"113","author":"WH Song","year":"2016","unstructured":"Song, W. H., Yi, Y. J., Sutovsky, M., Meyers, S. & Sutovsky, P. Autophagy and ubiquitin-proteasome system contribute to sperm mitophagy after mammalian fertilization. Proc. Natl. Acad. Sci. USA 113, E5261-5270. https:\/\/doi.org\/10.1073\/pnas.1605844113 (2016).","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"71056_CR51","doi-asserted-by":"publisher","DOI":"10.7554\/eLife.85596","author":"D Zuidema","year":"2023","unstructured":"Zuidema, D., Jones, A., Song, W. H., Zigo, M. & Sutovsky, P. Identification of candidate mitochondrial inheritance determinants using the mammalian cell-free system. Elife https:\/\/doi.org\/10.7554\/eLife.85596 (2023).","journal-title":"Elife"},{"key":"71056_CR52","doi-asserted-by":"publisher","DOI":"10.1242\/bio.035717","author":"J Mao","year":"2018","unstructured":"Mao, J. et al. Ubiquitin A-52 residue ribosomal protein fusion product 1 (Uba52) is essential for preimplantation embryo development. Biol. Open https:\/\/doi.org\/10.1242\/bio.035717 (2018).","journal-title":"Biol. Open"},{"key":"71056_CR53","doi-asserted-by":"publisher","first-page":"245","DOI":"10.1007\/978-1-4939-6988-3_17","volume":"1605","author":"V Benesova","year":"2017","unstructured":"Benesova, V., Kinterova, V., Kanka, J. & Toralova, T. Potential involvement of SCF-complex in zygotic genome activation during early bovine embryo development. Methods Mol. Biol. 1605, 245\u2013257. https:\/\/doi.org\/10.1007\/978-1-4939-6988-3_17 (2017).","journal-title":"Methods Mol. Biol."},{"key":"71056_CR54","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0068873","volume":"8","author":"P Hillman","year":"2013","unstructured":"Hillman, P., Ickowicz, D., Vizel, R. & Breitbart, H. Dissociation between AKAP3 and PKARII promotes AKAP3 degradation in sperm capacitation. PloS One 8, e68873. https:\/\/doi.org\/10.1371\/journal.pone.0068873 (2013).","journal-title":"PloS One"},{"key":"71056_CR55","doi-asserted-by":"publisher","first-page":"3501","DOI":"10.3390\/cells10123501","volume":"10","author":"H Zapata-Carmona","year":"2021","unstructured":"Zapata-Carmona, H., Bar\u00f3n, L., Kong, M. & Morales, P. Protein kinase a (PRKA) activity is regulated by the proteasome at the onset of human sperm capacitation. Cells 10, 3501. https:\/\/doi.org\/10.3390\/cells10123501 (2021).","journal-title":"Cells"},{"key":"71056_CR56","doi-asserted-by":"publisher","DOI":"10.1016\/j.anireprosci.2022.107079","volume":"247","author":"X Qu","year":"2022","unstructured":"Qu, X. et al. Inhibition of 26S proteasome enhances AKAP3-mediated cAMP-PKA signaling during boar sperm capacitation. Anim Reprod. Sci. 247, 107079. https:\/\/doi.org\/10.1016\/j.anireprosci.2022.107079 (2022).","journal-title":"Anim Reprod. Sci."},{"key":"71056_CR57","doi-asserted-by":"publisher","first-page":"114","DOI":"10.1111\/j.1439-0272.2009.01031.x","volume":"43","author":"R Sanchez","year":"2011","unstructured":"Sanchez, R. et al. Participation of the sperm proteasome during in vitro fertilisation and the acrosome reaction in cattle. Andrologia 43, 114\u2013120. https:\/\/doi.org\/10.1111\/j.1439-0272.2009.01031.x (2011).","journal-title":"Andrologia"},{"key":"71056_CR58","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0034524","volume":"7","author":"YJ Yi","year":"2012","unstructured":"Yi, Y. J., Sutovsky, M., Kennedy, C. & Sutovsky, P. Identification of the inorganic pyrophosphate metabolizing, ATP substituting pathway in mammalian spermatozoa. PloS One 7, e34524. https:\/\/doi.org\/10.1371\/journal.pone.0034524 (2012).","journal-title":"PloS One"},{"key":"71056_CR59","doi-asserted-by":"publisher","DOI":"10.3389\/fvets.2023.1116891","author":"L Hackerova","year":"2023","unstructured":"Hackerova, L. et al. Modulatory effect of MG-132 proteasomal inhibition on boar sperm motility during in vitro capacitation. Front. Vet. Sci. https:\/\/doi.org\/10.3389\/fvets.2023.1116891 (2023).","journal-title":"Front. Vet. Sci."},{"key":"71056_CR60","doi-asserted-by":"publisher","first-page":"6256","DOI":"10.3390\/ijms21176256","volume":"21","author":"A Taraschi","year":"2020","unstructured":"Taraschi, A. et al. Two-player game in a complex landscape: 26S Proteasome, PKA, and intracellular calcium concentration modulate mammalian sperm capacitation by creating an integrated dialogue-a computational analysis. Int. J. Mol. Sci. 21, 6256. https:\/\/doi.org\/10.3390\/ijms21176256 (2020).","journal-title":"Int. J. Mol. Sci."},{"key":"71056_CR61","doi-asserted-by":"publisher","first-page":"1026","DOI":"10.1095\/biolreprod.108.073924","volume":"80","author":"M Kong","year":"2009","unstructured":"Kong, M., Diaz, E. S. & Morales, P. Participation of the human sperm proteasome in the capacitation process and its regulation by protein kinase A and tyrosine kinase. Biol. Reproduct. 80, 1026\u20131035. https:\/\/doi.org\/10.1095\/biolreprod.108.073924 (2009).","journal-title":"Biol. Reproduct."},{"key":"71056_CR62","doi-asserted-by":"publisher","first-page":"587","DOI":"10.1093\/molehr\/gaz037","volume":"25","author":"H Zapata-Carmona","year":"2019","unstructured":"Zapata-Carmona, H. et al. The activation of the chymotrypsin-like activity of the proteasome is regulated by soluble adenyl cyclase\/cAMP\/protein kinase a pathway and required for human sperm capacitation. Mol. Hum. Reproduct. 25, 587\u2013600. https:\/\/doi.org\/10.1093\/molehr\/gaz037 (2019).","journal-title":"Mol. Hum. Reproduct."},{"key":"71056_CR63","unstructured":"Blighe, K., Rana, S. & Lewis, M. EnhancedVolcano: Publication-ready volcano plots with enhanced colouring and labeling. R package version 1.8.0, 2020)."},{"key":"71056_CR64","doi-asserted-by":"publisher","first-page":"27","DOI":"10.1093\/nar\/28.1.27","volume":"28","author":"M Kanehisa","year":"2000","unstructured":"Kanehisa, M. & Goto, S. KEGG: Kyoto encyclopedia of genes and genomes. Nucleic Acids Res. 28, 27\u201330. https:\/\/doi.org\/10.1093\/nar\/28.1.27 (2000).","journal-title":"Nucleic Acids Res."},{"key":"71056_CR65","doi-asserted-by":"publisher","first-page":"1947","DOI":"10.1002\/pro.3715","volume":"28","author":"M Kanehisa","year":"2019","unstructured":"Kanehisa, M. Toward understanding the origin and evolution of cellular organisms. Protein Sci. 28, 1947\u20131951. https:\/\/doi.org\/10.1002\/pro.3715 (2019).","journal-title":"Protein Sci."},{"key":"71056_CR66","doi-asserted-by":"publisher","first-page":"D587","DOI":"10.1093\/nar\/gkac963","volume":"51","author":"M Kanehisa","year":"2023","unstructured":"Kanehisa, M., Furumichi, M., Sato, Y., Kawashima, M. & Ishiguro-Watanabe, M. KEGG for taxonomy-based analysis of pathways and genomes. Nucleic Acids Res. 51, D587-d592. https:\/\/doi.org\/10.1093\/nar\/gkac963 (2023).","journal-title":"Nucleic Acids Res."},{"key":"71056_CR67","doi-asserted-by":"publisher","first-page":"418","DOI":"10.1016\/j.ymgme.2010.12.005","volume":"102","author":"M He","year":"2011","unstructured":"He, M. et al. Identification and characterization of new long chain acyl-CoA dehydrogenases. Mol. Genet. Metab. 102, 418\u2013429. https:\/\/doi.org\/10.1016\/j.ymgme.2010.12.005 (2011).","journal-title":"Mol. Genet. Metab."},{"key":"71056_CR68","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0103566","volume":"9","author":"KF Arroteia","year":"2014","unstructured":"Arroteia, K. F. et al. Albumin is synthesized in epididymis and aggregates in a high molecular mass glycoprotein complex involved in sperm-egg fertilization. PloS One 9, e103566. https:\/\/doi.org\/10.1371\/journal.pone.0103566 (2014).","journal-title":"PloS One"},{"key":"71056_CR69","doi-asserted-by":"publisher","first-page":"13333","DOI":"10.1038\/s41598-021-92495-3","volume":"11","author":"A Beckers","year":"2021","unstructured":"Beckers, A. et al. The highly conserved FOXJ1 target CFAP161 is dispensable for motile ciliary function in mouse and Xenopus. Sci. Rep. 11, 13333. https:\/\/doi.org\/10.1038\/s41598-021-92495-3 (2021).","journal-title":"Sci. Rep."},{"key":"71056_CR70","doi-asserted-by":"publisher","first-page":"2313","DOI":"10.1093\/hmg\/ddt624","volume":"23","author":"L Strittmatter","year":"2014","unstructured":"Strittmatter, L. et al. CLYBL is a polymorphic human enzyme with malate synthase and \u03b2-methylmalate synthase activity. Hum. Mol. Genet. 23, 2313\u20132323. https:\/\/doi.org\/10.1093\/hmg\/ddt624 (2014).","journal-title":"Hum. Mol. Genet."},{"key":"71056_CR71","doi-asserted-by":"publisher","first-page":"8","DOI":"10.1186\/s12958-018-0327-0","volume":"16","author":"RK Lee","year":"2018","unstructured":"Lee, R. K. et al. Expression of cystatin C in the female reproductive tract and its effect on human sperm capacitation. Reproduct. Biol. Endocrinol. RB&E 16, 8. https:\/\/doi.org\/10.1186\/s12958-018-0327-0 (2018).","journal-title":"Reproduct. Biol. Endocrinol. RB&E"},{"key":"71056_CR72","doi-asserted-by":"publisher","first-page":"227","DOI":"10.1159\/000104169","volume":"20","author":"K Eckhardt","year":"2007","unstructured":"Eckhardt, K. et al. Male germ cell expression of the PAS domain kinase PASKIN and its novel target eukaryotic translation elongation factor eEF1A1. Cell Physiol. Biochem. 20, 227\u2013240. https:\/\/doi.org\/10.1159\/000104169 (2007).","journal-title":"Cell Physiol. Biochem."},{"key":"71056_CR73","doi-asserted-by":"publisher","first-page":"32431","DOI":"10.1074\/jbc.M303786200","volume":"278","author":"PR Tovich","year":"2003","unstructured":"Tovich, P. R. & Oko, R. J. Somatic histones are components of the perinuclear theca in bovine spermatozoa. J. Biol. Chem. 278, 32431\u201332438. https:\/\/doi.org\/10.1074\/jbc.M303786200 (2003).","journal-title":"J. Biol. Chem."},{"key":"71056_CR74","doi-asserted-by":"publisher","first-page":"8119","DOI":"10.3390\/ijms22158119","volume":"22","author":"LE Hamilton","year":"2021","unstructured":"Hamilton, L. E. et al. Core histones are constituents of the perinuclear theca of murid spermatozoa: an assessment of their synthesis and assembly during spermiogenesis and function after gametic fusion. Int. J. Mol. Sci. 22, 8119. https:\/\/doi.org\/10.3390\/ijms22158119 (2021).","journal-title":"Int. J. Mol. Sci."},{"key":"71056_CR75","doi-asserted-by":"publisher","first-page":"780","DOI":"10.3389\/fgene.2020.00780","volume":"11","author":"U Torres-Flores","year":"2020","unstructured":"Torres-Flores, U. & Hern\u00e1ndez-Hern\u00e1ndez, A. The interplay between replacement and retention of histones in the sperm genome. Front. Genet. 11, 780. https:\/\/doi.org\/10.3389\/fgene.2020.00780 (2020).","journal-title":"Front. Genet."},{"key":"71056_CR76","doi-asserted-by":"publisher","first-page":"551","DOI":"10.1146\/annurev-biochem-070511-103700","volume":"82","author":"J Hirst","year":"2013","unstructured":"Hirst, J. Mitochondrial complex I. Ann. Rev. Biochem. 82, 551\u2013575. https:\/\/doi.org\/10.1146\/annurev-biochem-070511-103700 (2013).","journal-title":"Ann. Rev. Biochem."},{"key":"71056_CR77","doi-asserted-by":"publisher","DOI":"10.1242\/dev.199644","author":"A Morohoshi","year":"2021","unstructured":"Morohoshi, A. et al. FAM71F1 binds to RAB2A and RAB2B and is essential for acrosome formation and male fertility in mice. Development https:\/\/doi.org\/10.1242\/dev.199644 (2021).","journal-title":"Development"},{"key":"71056_CR78","doi-asserted-by":"publisher","first-page":"223","DOI":"10.1095\/biolreprod.107.065060","volume":"79","author":"JR Mountjoy","year":"2008","unstructured":"Mountjoy, J. R., Xu, W., McLeod, D., Hyndman, D. & Oko, R. RAB2A: A major subacrosomal protein of bovine spermatozoa implicated in acrosomal biogenesis. Biol. Reproduct. 79, 223\u2013232. https:\/\/doi.org\/10.1095\/biolreprod.107.065060 (2008).","journal-title":"Biol. Reproduct."},{"key":"71056_CR79","doi-asserted-by":"publisher","DOI":"10.3389\/fcell.2022.836208","volume":"10","author":"M Zhang","year":"2022","unstructured":"Zhang, M. et al. High resolution proteomic analysis of subcellular fractionated boar spermatozoa provides comprehensive insights into perinuclear theca-residing proteins. Front. Cell Dev. Biol. 10, 836208. https:\/\/doi.org\/10.3389\/fcell.2022.836208 (2022).","journal-title":"Front. Cell Dev. Biol."},{"key":"71056_CR80","doi-asserted-by":"publisher","first-page":"895","DOI":"10.1007\/s00441-014-2072-9","volume":"359","author":"M Zigo","year":"2015","unstructured":"Zigo, M. et al. Panel of monoclonal antibodies to sperm surface proteins as a tool for monitoring localization and identification of sperm-zona pellucida receptors. Cell Tissue Res. 359, 895\u2013908. https:\/\/doi.org\/10.1007\/s00441-014-2072-9 (2015).","journal-title":"Cell Tissue Res."},{"key":"71056_CR81","doi-asserted-by":"publisher","first-page":"6334","DOI":"10.1073\/pnas.1220910110","volume":"110","author":"EL Miles","year":"2013","unstructured":"Miles, E. L. et al. Transgenic pig carrying green fluorescent proteasomes. Proc. Natl. Acad. Sci. USA 110, 6334\u20136339. https:\/\/doi.org\/10.1073\/pnas.1220910110 (2013).","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"71056_CR82","doi-asserted-by":"publisher","first-page":"739","DOI":"10.1016\/s1074-5521(01)00056-4","volume":"8","author":"AF Kisselev","year":"2001","unstructured":"Kisselev, A. F. & Goldberg, A. L. Proteasome inhibitors: From research tools to drug candidates. Chem. Biol. 8, 739\u2013758. https:\/\/doi.org\/10.1016\/s1074-5521(01)00056-4 (2001).","journal-title":"Chem. Biol."},{"key":"71056_CR83","doi-asserted-by":"publisher","first-page":"449","DOI":"10.1002\/jcp.24728","volume":"230","author":"K Kongmanas","year":"2015","unstructured":"Kongmanas, K. et al. Proteomic characterization of pig sperm anterior head plasma membrane reveals roles of acrosomal proteins in ZP3 binding. J. Cell. Physiol. 230, 449\u2013463. https:\/\/doi.org\/10.1002\/jcp.24728 (2015).","journal-title":"J. Cell. Physiol."},{"key":"71056_CR84","doi-asserted-by":"publisher","first-page":"574","DOI":"10.4103\/1008-682x.152817","volume":"17","author":"N Tanphaichitr","year":"2015","unstructured":"Tanphaichitr, N. et al. Remodeling of the plasma membrane in preparation for sperm-egg recognition: Roles of acrosomal proteins. Asian J. Androl. 17, 574\u2013582. https:\/\/doi.org\/10.4103\/1008-682x.152817 (2015).","journal-title":"Asian J. Androl."},{"key":"71056_CR85","doi-asserted-by":"publisher","first-page":"122","DOI":"10.1002\/jcp.21575","volume":"218","author":"B Nixon","year":"2009","unstructured":"Nixon, B. et al. Composition and significance of detergent resistant membranes in mouse spermatozoa. J. Cell. Physiol. 218, 122\u2013134. https:\/\/doi.org\/10.1002\/jcp.21575 (2009).","journal-title":"J. Cell. Physiol."},{"key":"71056_CR86","doi-asserted-by":"publisher","first-page":"3494","DOI":"10.1002\/pmic.201000002","volume":"10","author":"A Asano","year":"2010","unstructured":"Asano, A., Nelson, J. L., Zhang, S. & Travis, A. J. Characterization of the proteomes associating with three distinct membrane raft sub-types in murine sperm. Proteomics 10, 3494\u20133505. https:\/\/doi.org\/10.1002\/pmic.201000002 (2010).","journal-title":"Proteomics"},{"key":"71056_CR87","doi-asserted-by":"publisher","first-page":"583","DOI":"10.1093\/molehr\/gah200","volume":"11","author":"RA van Gestel","year":"2005","unstructured":"van Gestel, R. A. et al. Capacitation-dependent concentration of lipid rafts in the apical ridge head area of porcine sperm cells. Mol. Hum. Reproduct. 11, 583\u2013590. https:\/\/doi.org\/10.1093\/molehr\/gah200 (2005).","journal-title":"Mol. Hum. Reproduct."},{"key":"71056_CR88","doi-asserted-by":"publisher","first-page":"721","DOI":"10.1095\/biolreprod.105.041533","volume":"73","author":"SB Sleight","year":"2005","unstructured":"Sleight, S. B. et al. Isolation and proteomic analysis of mouse sperm detergent-resistant membrane fractions: Evidence for dissociation of lipid rafts during capacitation. Biol. Reproduct. 73, 721\u2013729. https:\/\/doi.org\/10.1095\/biolreprod.105.041533 (2005).","journal-title":"Biol. Reproduct."},{"key":"71056_CR89","doi-asserted-by":"publisher","first-page":"220","DOI":"10.1016\/j.ydbio.2005.11.030","volume":"290","author":"M Bou Khalil","year":"2006","unstructured":"Bou Khalil, M. et al. Sperm capacitation induces an increase in lipid rafts having zona pellucida binding ability and containing sulfogalactosylglycerolipid. Dev. Biol. 290, 220\u2013235. https:\/\/doi.org\/10.1016\/j.ydbio.2005.11.030 (2006).","journal-title":"Dev. Biol."},{"key":"71056_CR90","doi-asserted-by":"publisher","first-page":"8","DOI":"10.1016\/j.jri.2009.06.258","volume":"83","author":"B Nixon","year":"2009","unstructured":"Nixon, B. & Aitken, R. J. The biological significance of detergent-resistant membranes in spermatozoa. J. Reproduct. Immunol. 83, 8\u201313. https:\/\/doi.org\/10.1016\/j.jri.2009.06.258 (2009).","journal-title":"J. Reproduct. Immunol."},{"key":"71056_CR91","doi-asserted-by":"publisher","first-page":"2651","DOI":"10.1002\/jcp.22615","volume":"226","author":"B Nixon","year":"2011","unstructured":"Nixon, B. et al. Proteomic and functional analysis of human sperm detergent resistant membranes. J. Cell. Physiol. 226, 2651\u20132665. https:\/\/doi.org\/10.1002\/jcp.22615 (2011).","journal-title":"J. Cell. Physiol."},{"key":"71056_CR92","doi-asserted-by":"publisher","first-page":"538","DOI":"10.1038\/s42003-022-03485-8","volume":"5","author":"M Zigo","year":"2022","unstructured":"Zigo, M. et al. Zinc is a master-regulator of sperm function associated with binding, motility, and metabolic modulation during porcine sperm capacitation. Commun. Biol. 5, 538. https:\/\/doi.org\/10.1038\/s42003-022-03485-8 (2022).","journal-title":"Commun. Biol."},{"key":"71056_CR93","doi-asserted-by":"publisher","first-page":"356","DOI":"10.1016\/j.repbio.2019.10.001","volume":"19","author":"JW Bae","year":"2019","unstructured":"Bae, J. W. et al. Ras-related proteins (Rab) are key proteins related to male fertility following a unique activation mechanism. Reproduct. Biol. 19, 356\u2013362. https:\/\/doi.org\/10.1016\/j.repbio.2019.10.001 (2019).","journal-title":"Reproduct. Biol."},{"key":"71056_CR94","doi-asserted-by":"publisher","first-page":"897","DOI":"10.1186\/1471-2164-15-897","volume":"15","author":"WS Kwon","year":"2014","unstructured":"Kwon, W. S. et al. A comprehensive proteomic approach to identifying capacitation related proteins in boar spermatozoa. BMC Genom. 15, 897. https:\/\/doi.org\/10.1186\/1471-2164-15-897 (2014).","journal-title":"BMC Genom."},{"key":"71056_CR95","doi-asserted-by":"publisher","first-page":"1084","DOI":"10.1095\/biolreprod62.4.1084","volume":"62","author":"R Yunes","year":"2000","unstructured":"Yunes, R., Michaut, M., Tomes, C. & Mayorga, L. S. Rab3A triggers the acrosome reaction in permeabilized human spermatozoa. Biol. Reproduct. 62, 1084\u20131089. https:\/\/doi.org\/10.1095\/biolreprod62.4.1084 (2000).","journal-title":"Biol. Reproduct."},{"key":"71056_CR96","doi-asserted-by":"publisher","first-page":"393","DOI":"10.1016\/j.ydbio.2005.07.001","volume":"285","author":"SA Belmonte","year":"2005","unstructured":"Belmonte, S. A. et al. Cholesterol content regulates acrosomal exocytosis by enhancing Rab3A plasma membrane association. Dev. Biol. 285, 393\u2013408. https:\/\/doi.org\/10.1016\/j.ydbio.2005.07.001 (2005).","journal-title":"Dev. Biol."},{"key":"71056_CR97","doi-asserted-by":"publisher","first-page":"4121","DOI":"10.1096\/fj.06-7716com","volume":"21","author":"CI Lopez","year":"2007","unstructured":"Lopez, C. I., Belmonte, S. A., De Blas, G. A. & Mayorga, L. S. Membrane-permeant Rab3A triggers acrosomal exocytosis in living human sperm. FASEB J. Off. Publ. Fed. Am. Soc. Exp. Biol. 21, 4121\u20134130. https:\/\/doi.org\/10.1096\/fj.06-7716com (2007).","journal-title":"FASEB J. Off. Publ. Fed. Am. Soc. Exp. Biol."},{"key":"71056_CR98","doi-asserted-by":"publisher","first-page":"15654","DOI":"10.1038\/srep15654","volume":"5","author":"WS Kwon","year":"2015","unstructured":"Kwon, W. S., Rahman, M. S., Ryu, D. Y., Park, Y. J. & Pang, M. G. Increased male fertility using fertility-related biomarkers. Sci. Rep. 5, 15654. https:\/\/doi.org\/10.1038\/srep15654 (2015).","journal-title":"Sci. Rep."},{"key":"71056_CR99","doi-asserted-by":"publisher","first-page":"568","DOI":"10.1111\/andr.12332","volume":"5","author":"WS Kwon","year":"2017","unstructured":"Kwon, W. S., Rahman, M. S., Ryu, D. Y., Khatun, A. & Pang, M. G. Comparison of markers predicting litter size in different pig breeds. Andrology 5, 568\u2013577. https:\/\/doi.org\/10.1111\/andr.12332 (2017).","journal-title":"Andrology"},{"key":"71056_CR100","doi-asserted-by":"publisher","first-page":"51","DOI":"10.1016\/j.theriogenology.2022.02.021","volume":"184","author":"SM Zoca","year":"2022","unstructured":"Zoca, S. M., Northrop-Albrecht, E. J., Walker, J. A., Cushman, R. A. & Perry, G. A. Proteomic analyses identify differences between bovine epididymal and ejaculated spermatozoa that contribute to longevity. Theriogenology 184, 51\u201360. https:\/\/doi.org\/10.1016\/j.theriogenology.2022.02.021 (2022).","journal-title":"Theriogenology"},{"key":"71056_CR101","doi-asserted-by":"publisher","first-page":"6105","DOI":"10.1007\/s00018-021-03899-3","volume":"78","author":"J Magalh\u00e3es","year":"2021","unstructured":"Magalh\u00e3es, J., Eira, J. & Liz, M. A. The role of transthyretin in cell biology: Impact on human pathophysiology. Cell. Mol. Life Sci. CMLS 78, 6105\u20136117. https:\/\/doi.org\/10.1007\/s00018-021-03899-3 (2021).","journal-title":"Cell. Mol. Life Sci. CMLS"},{"key":"71056_CR102","doi-asserted-by":"publisher","first-page":"273","DOI":"10.1615\/CritRevEukaryotGeneExpr.2016017323","volume":"26","author":"Q Wang","year":"2016","unstructured":"Wang, Q., Liu, C. & Zhang, Z. Transthyretin and normal human pregnancy: Mini review. Crit. Rev. Eukaryot. Gene. Expr. 26, 273\u2013277. https:\/\/doi.org\/10.1615\/CritRevEukaryotGeneExpr.2016017323 (2016).","journal-title":"Crit. Rev. Eukaryot. Gene. Expr."},{"key":"71056_CR103","doi-asserted-by":"publisher","first-page":"68","DOI":"10.1262\/jrd.19116","volume":"54","author":"YJ Choi","year":"2008","unstructured":"Choi, Y. J. et al. Cytochrome c upregulation during capacitation and spontaneous acrosome reaction determines the fate of pig sperm cells: linking proteome analysis. J. Reproduct. Dev. 54, 68\u201383. https:\/\/doi.org\/10.1262\/jrd.19116 (2008).","journal-title":"J. Reproduct. Dev."},{"key":"71056_CR104","doi-asserted-by":"publisher","first-page":"1309","DOI":"10.1002\/elps.201000558","volume":"32","author":"M Zigo","year":"2011","unstructured":"Zigo, M., Jonakova, V. & Manaskova-Postlerova, P. Electrophoretic and zymographic characterization of proteins isolated by various extraction methods from ejaculated and capacitated boar sperms. Electrophoresis 32, 1309\u20131318. https:\/\/doi.org\/10.1002\/elps.201000558 (2011).","journal-title":"Electrophoresis"},{"key":"71056_CR105","doi-asserted-by":"publisher","first-page":"322","DOI":"10.1016\/j.ijbiomac.2013.07.014","volume":"61","author":"M Zigo","year":"2013","unstructured":"Zigo, M., Jonakova, V., Sulc, M. & Manaskova-Postlerova, P. Characterization of sperm surface protein patterns of ejaculated and capacitated boar sperm, with the detection of ZP binding candidates. Int. J. Biol. Macromol. 61, 322\u2013328. https:\/\/doi.org\/10.1016\/j.ijbiomac.2013.07.014 (2013).","journal-title":"Int. J. Biol. Macromol."},{"key":"71056_CR106","doi-asserted-by":"publisher","first-page":"436","DOI":"10.1002\/mrd.22309","volume":"81","author":"CE Kennedy","year":"2014","unstructured":"Kennedy, C. E. et al. Protein expression pattern of PAWP in bull spermatozoa is associated with sperm quality and fertility following artificial insemination. Mol. Reproduct. Dev. 81, 436\u2013449. https:\/\/doi.org\/10.1002\/mrd.22309 (2014).","journal-title":"Mol. Reproduct. Dev."}],"container-title":["Scientific Reports"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.nature.com\/articles\/s41598-024-71056-4.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41598-024-71056-4","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41598-024-71056-4.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,8,30]],"date-time":"2024-08-30T07:08:30Z","timestamp":1725001710000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/s41598-024-71056-4"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,8,29]]},"references-count":106,"journal-issue":{"issue":"1","published-online":{"date-parts":[[2024,12]]}},"alternative-id":["71056"],"URL":"https:\/\/doi.org\/10.1038\/s41598-024-71056-4","relation":{},"ISSN":["2045-2322"],"issn-type":[{"value":"2045-2322","type":"electronic"}],"subject":[],"published":{"date-parts":[[2024,8,29]]},"assertion":[{"value":"1 February 2024","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"23 August 2024","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"29 August 2024","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"The authors declare no competing interests. It is disclosed that PS and KK are the founders and owners of AndroLabb LLC, Columbia, MO, a biotech startup involved with sperm processing and sperm quality diagnostics, which did not play any role in the investigations described herein.","order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing interests"}}],"article-number":"20159"}}