{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,2]],"date-time":"2026-06-02T17:02:13Z","timestamp":1780419733701,"version":"3.54.1"},"reference-count":188,"publisher":"MDPI AG","issue":"10","license":[{"start":{"date-parts":[[2024,5,17]],"date-time":"2024-05-17T00:00:00Z","timestamp":1715904000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100003141","name":"CONAHCyT Mexico","doi-asserted-by":"publisher","award":["CF-2023-I-291"],"award-info":[{"award-number":["CF-2023-I-291"]}],"id":[{"id":"10.13039\/501100003141","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003141","name":"CONAHCyT Mexico","doi-asserted-by":"publisher","award":["A1-S-8768"],"award-info":[{"award-number":["A1-S-8768"]}],"id":[{"id":"10.13039\/501100003141","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003141","name":"CONAHCyT Mexico","doi-asserted-by":"publisher","award":["IN204922"],"award-info":[{"award-number":["IN204922"]}],"id":[{"id":"10.13039\/501100003141","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003141","name":"CONAHCyT Mexico","doi-asserted-by":"publisher","award":["IN207122"],"award-info":[{"award-number":["IN207122"]}],"id":[{"id":"10.13039\/501100003141","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003141","name":"CONAHCyT Mexico","doi-asserted-by":"publisher","award":["IN205722"],"award-info":[{"award-number":["IN205722"]}],"id":[{"id":"10.13039\/501100003141","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003141","name":"CONAHCyT Mexico","doi-asserted-by":"publisher","award":["IN218123"],"award-info":[{"award-number":["IN218123"]}],"id":[{"id":"10.13039\/501100003141","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003141","name":"CONAHCyT Mexico","doi-asserted-by":"publisher","award":["PE206424"],"award-info":[{"award-number":["PE206424"]}],"id":[{"id":"10.13039\/501100003141","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003141","name":"CONAHCyT Mexico","doi-asserted-by":"publisher","award":["RO1 HD038082-17A1"],"award-info":[{"award-number":["RO1 HD038082-17A1"]}],"id":[{"id":"10.13039\/501100003141","id-type":"DOI","asserted-by":"publisher"}]},{"name":"DGAPA-PAPIIT","award":["CF-2023-I-291"],"award-info":[{"award-number":["CF-2023-I-291"]}]},{"name":"DGAPA-PAPIIT","award":["A1-S-8768"],"award-info":[{"award-number":["A1-S-8768"]}]},{"name":"DGAPA-PAPIIT","award":["IN204922"],"award-info":[{"award-number":["IN204922"]}]},{"name":"DGAPA-PAPIIT","award":["IN207122"],"award-info":[{"award-number":["IN207122"]}]},{"name":"DGAPA-PAPIIT","award":["IN205722"],"award-info":[{"award-number":["IN205722"]}]},{"name":"DGAPA-PAPIIT","award":["IN218123"],"award-info":[{"award-number":["IN218123"]}]},{"name":"DGAPA-PAPIIT","award":["PE206424"],"award-info":[{"award-number":["PE206424"]}]},{"name":"DGAPA-PAPIIT","award":["RO1 HD038082-17A1"],"award-info":[{"award-number":["RO1 HD038082-17A1"]}]},{"name":"DGAPA-PAPIME","award":["CF-2023-I-291"],"award-info":[{"award-number":["CF-2023-I-291"]}]},{"name":"DGAPA-PAPIME","award":["A1-S-8768"],"award-info":[{"award-number":["A1-S-8768"]}]},{"name":"DGAPA-PAPIME","award":["IN204922"],"award-info":[{"award-number":["IN204922"]}]},{"name":"DGAPA-PAPIME","award":["IN207122"],"award-info":[{"award-number":["IN207122"]}]},{"name":"DGAPA-PAPIME","award":["IN205722"],"award-info":[{"award-number":["IN205722"]}]},{"name":"DGAPA-PAPIME","award":["IN218123"],"award-info":[{"award-number":["IN218123"]}]},{"name":"DGAPA-PAPIME","award":["PE206424"],"award-info":[{"award-number":["PE206424"]}]},{"name":"DGAPA-PAPIME","award":["RO1 HD038082-17A1"],"award-info":[{"award-number":["RO1 HD038082-17A1"]}]},{"name":"NIH","award":["CF-2023-I-291"],"award-info":[{"award-number":["CF-2023-I-291"]}]},{"name":"NIH","award":["A1-S-8768"],"award-info":[{"award-number":["A1-S-8768"]}]},{"name":"NIH","award":["IN204922"],"award-info":[{"award-number":["IN204922"]}]},{"name":"NIH","award":["IN207122"],"award-info":[{"award-number":["IN207122"]}]},{"name":"NIH","award":["IN205722"],"award-info":[{"award-number":["IN205722"]}]},{"name":"NIH","award":["IN218123"],"award-info":[{"award-number":["IN218123"]}]},{"name":"NIH","award":["PE206424"],"award-info":[{"award-number":["PE206424"]}]},{"name":"NIH","award":["RO1 HD038082-17A1"],"award-info":[{"award-number":["RO1 HD038082-17A1"]}]},{"name":"Shirley Ainsworth","award":["CF-2023-I-291"],"award-info":[{"award-number":["CF-2023-I-291"]}]},{"name":"Shirley Ainsworth","award":["A1-S-8768"],"award-info":[{"award-number":["A1-S-8768"]}]},{"name":"Shirley Ainsworth","award":["IN204922"],"award-info":[{"award-number":["IN204922"]}]},{"name":"Shirley Ainsworth","award":["IN207122"],"award-info":[{"award-number":["IN207122"]}]},{"name":"Shirley Ainsworth","award":["IN205722"],"award-info":[{"award-number":["IN205722"]}]},{"name":"Shirley Ainsworth","award":["IN218123"],"award-info":[{"award-number":["IN218123"]}]},{"name":"Shirley Ainsworth","award":["PE206424"],"award-info":[{"award-number":["PE206424"]}]},{"name":"Shirley Ainsworth","award":["RO1 HD038082-17A1"],"award-info":[{"award-number":["RO1 HD038082-17A1"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Cells"],"abstract":"<jats:p>As in most cells, intracellular pH regulation is fundamental for sperm physiology. Key sperm functions like swimming, maturation, and a unique exocytotic process, the acrosome reaction, necessary for gamete fusion, are deeply influenced by pH. Sperm pH regulation, both intracellularly and within organelles such as the acrosome, requires a coordinated interplay of various transporters and channels, ensuring that this cell is primed for fertilization. Consistent with the pivotal importance of pH regulation in mammalian sperm physiology, several of its unique transporters are dependent on cytosolic pH. Examples include the Ca2+ channel CatSper and the K+ channel Slo3. The absence of these channels leads to male infertility. This review outlines the main transport elements involved in pH regulation, including cytosolic and acrosomal pH, that participate in these complex functions. We present a glimpse of how these transporters are regulated and how distinct sets of them are orchestrated to allow sperm to fertilize the egg. Much research is needed to begin to envision the complete set of players and the choreography of how cytosolic and organellar pH are regulated in each sperm function.<\/jats:p>","DOI":"10.3390\/cells13100865","type":"journal-article","created":{"date-parts":[[2024,5,17]],"date-time":"2024-05-17T06:53:49Z","timestamp":1715928829000},"page":"865","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":11,"title":["Cytosolic and Acrosomal pH Regulation in Mammalian Sperm"],"prefix":"10.3390","volume":"13","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-7375-9531","authenticated-orcid":false,"given":"Julio C.","family":"Ch\u00e1vez","sequence":"first","affiliation":[{"name":"Departamento de Gen\u00e9tica del Desarrollo y Fisiolog\u00eda Molecular, Instituto de Biotecnolog\u00eda (IBT), Universidad Nacional Aut\u00f3noma de M\u00e9xico (UNAM), Cuernavaca 62210, Morelos, Mexico"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0006-5868-1541","authenticated-orcid":false,"given":"Gabriela","family":"Carrasquel-Mart\u00ednez","sequence":"additional","affiliation":[{"name":"Departamento de Gen\u00e9tica del Desarrollo y Fisiolog\u00eda Molecular, Instituto de Biotecnolog\u00eda (IBT), Universidad Nacional Aut\u00f3noma de M\u00e9xico (UNAM), Cuernavaca 62210, Morelos, Mexico"},{"name":"CITMER, Medicina Reproductiva, M\u00e9xico City 11520, Mexico"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5447-9350","authenticated-orcid":false,"given":"Sandra","family":"Hern\u00e1ndez-Gardu\u00f1o","sequence":"additional","affiliation":[{"name":"Departamento de Morfolog\u00eda, Facultad de Medicina Veterinaria y Zootecnia, Universidad Nacional Aut\u00f3noma de M\u00e9xico (UNAM), M\u00e9xico City 04510, Mexico"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Arturo","family":"Matamoros Volante","sequence":"additional","affiliation":[{"name":"Department of Electrical and Computer Engineering and School of Biomedical Engineering, Colorado State University, Fort Collins, CO 80523, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Claudia L.","family":"Trevi\u00f1o","sequence":"additional","affiliation":[{"name":"Departamento de Gen\u00e9tica del Desarrollo y Fisiolog\u00eda Molecular, Instituto de Biotecnolog\u00eda (IBT), Universidad Nacional Aut\u00f3noma de M\u00e9xico (UNAM), Cuernavaca 62210, Morelos, Mexico"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Takuya","family":"Nishigaki","sequence":"additional","affiliation":[{"name":"Departamento de Gen\u00e9tica del Desarrollo y Fisiolog\u00eda Molecular, Instituto de Biotecnolog\u00eda (IBT), Universidad Nacional Aut\u00f3noma de M\u00e9xico (UNAM), Cuernavaca 62210, Morelos, Mexico"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0602-1107","authenticated-orcid":false,"given":"Alberto","family":"Darszon","sequence":"additional","affiliation":[{"name":"Departamento de Gen\u00e9tica del Desarrollo y Fisiolog\u00eda Molecular, Instituto de Biotecnolog\u00eda (IBT), Universidad Nacional Aut\u00f3noma de M\u00e9xico (UNAM), Cuernavaca 62210, Morelos, Mexico"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2024,5,17]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"50","DOI":"10.1038\/nrm2820","article-title":"Sensors and Regulators of Intracellular PH","volume":"11","author":"Casey","year":"2009","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"74282","DOI":"10.3389\/fphys.2014.00043","article-title":"Intracellular PH Regulation by Acid-Base Transporters in Mammalian Neurons","volume":"5","author":"Ruffin","year":"2014","journal-title":"Front. Physiol."},{"key":"ref_3","doi-asserted-by":"crossref","unstructured":"Swietach, P., Vaughan-Jones, R.D., Harris, A.L., and Hulikova, A. (2014). The Chemistry, Physiology and Pathology of PH in Cancer. Philos. Trans. R. Soc. B Biol. Sci., 369.","DOI":"10.1098\/rstb.2013.0099"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"515","DOI":"10.1152\/physrev.00009.2022","article-title":"Determinants, Maintenance, and Function of Organellar PH","volume":"103","author":"Freeman","year":"2023","journal-title":"Physiol. Rev."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1093\/molehr\/2.4.219","article-title":"Internal PH of Human Spermatozoa: Effect of Ions, Human Follicular Fluid and Progesterone","volume":"2","author":"Hamamah","year":"1996","journal-title":"Mol. Hum. Reprod."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"1305","DOI":"10.1152\/physrev.00028.2010","article-title":"Calcium Channels in the Development, Maturation, and Function of Spermatozoa","volume":"91","author":"Darszon","year":"2011","journal-title":"Physiol. Rev."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"860","DOI":"10.1002\/mrd.22663","article-title":"Chang\u2019s Meaning of Capacitation: A Molecular Perspective","volume":"83","author":"Gervasi","year":"2016","journal-title":"Mol. Reprod. Dev."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"697","DOI":"10.1038\/168697b0","article-title":"Fertilizing Capacity of Spermatozoa Deposited into the Fallopian Tubes","volume":"168","author":"Chang","year":"1951","journal-title":"Nature"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"581","DOI":"10.1071\/BI9510581","article-title":"Observations on the Penetration of the Sperm in the Mammalian Egg","volume":"4","author":"Austin","year":"1951","journal-title":"Aust. J. Sci. Res. B."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1095\/biolreprod.111.096826","article-title":"The Physiology of Bicarbonate Transporters in Mammalian Reproduction","volume":"86","author":"Liu","year":"2012","journal-title":"Biol. Reprod."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1093\/humupd\/dmx028","article-title":"In Vivo Oxygen, Temperature and PH Dynamics in the Female Reproductive Tract and Their Importance in Human Conception: A Systematic Review","volume":"24","author":"Ng","year":"2018","journal-title":"Hum. Reprod. Update"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"603","DOI":"10.1038\/35098027","article-title":"A Sperm Ion Channel Required for Sperm Motility and Male Fertility","volume":"413","author":"Ren","year":"2001","journal-title":"Nature"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"3509","DOI":"10.1074\/jbc.273.6.3509","article-title":"Slo3, a Novel PH-Sensitive K+ Channel from Mammalian Spermatocytes","volume":"273","author":"Schreiber","year":"1998","journal-title":"J. Biol. Chem."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"1041","DOI":"10.1016\/j.febslet.2010.02.005","article-title":"The SLO3 Sperm-Specific Potassium Channel Plays a Vital Role in Male Fertility","volume":"584","author":"Santi","year":"2010","journal-title":"FEBS Lett."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"19274","DOI":"10.1073\/pnas.1215078109","article-title":"Functional and Structural Analysis of the Human SLO3 PH- and Voltage-Gated K+ Channel","volume":"109","author":"Leonetti","year":"2012","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"1117","DOI":"10.1038\/ncb1072","article-title":"A New Sperm-Specific Na+\/H+ Exchanger Required for Sperm Motility and Fertility","volume":"5","author":"Wang","year":"2003","journal-title":"Nat. Cell Biol."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1530\/REP-22-0101","article-title":"Hyperpolarization Induces Cytosolic Alkalization of Mouse Sperm Flagellum Probably through Sperm Na+\/H+ Exchanger","volume":"164","author":"Torres","year":"2022","journal-title":"Reproduction"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"684","DOI":"10.1111\/cge.13927","article-title":"The Sodium\/Proton Exchanger SLC9C1 (SNHE) Is Essential for Human Sperm Motility and Fertility","volume":"99","author":"Cavarocchi","year":"2021","journal-title":"Clin. Genet."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"589","DOI":"10.1126\/science.1122352","article-title":"A Voltage Sensor-Domain Protein Is a Voltage-Gated Proton Channel","volume":"312","author":"Sasaki","year":"2006","journal-title":"Science"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"327","DOI":"10.1016\/j.cell.2009.12.053","article-title":"Acid Extrusion from Human Spermatozoa Is Mediated by Flagellar Voltage-Gated Proton Channel","volume":"140","author":"Lishko","year":"2010","journal-title":"Cell"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"14864","DOI":"10.1073\/pnas.2536658100","article-title":"CatSper1 Required for Evoked Ca2+ Entry and Control of Flagellar Function in Sperm","volume":"100","author":"Carlson","year":"2003","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"9325","DOI":"10.1073\/pnas.0611296104","article-title":"A Sperm-Specific Na+\/H+ Exchanger (SNHE) Is Critical for Expression and in Vivo Bicarbonate Regulation of the Soluble Adenylyl Cyclase (SAC)","volume":"104","author":"Wang","year":"2007","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1016\/j.devcel.2005.06.007","article-title":"The \u201cSoluble\u201d Adenylyl Cyclase in Sperm Mediates Multiple Signaling Events Required for Fertilization","volume":"9","author":"Hess","year":"2005","journal-title":"Dev. Cell"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"2993","DOI":"10.1073\/pnas.0400050101","article-title":"Mice Deficient for Soluble Adenylyl Cyclase Are Infertile Because of a Severe Sperm-Motility Defect","volume":"101","author":"Esposito","year":"2004","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"475","DOI":"10.1530\/REP-14-0471","article-title":"ATPases, Ion Exchangers and Human Sperm Motility","volume":"149","author":"Camejo","year":"2015","journal-title":"Reproduction"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"196","DOI":"10.1152\/physiol.00033.2019","article-title":"Differences and Similarities: The Richness of Comparative Sperm Physiology","volume":"35","author":"Darszon","year":"2020","journal-title":"Physiology"},{"key":"ref_27","doi-asserted-by":"crossref","unstructured":"Delgado-Berm\u00fadez, A., Yeste, M., Bonet, S., and Pinart, E. (2022). A Review on the Role of Bicarbonate and Proton Transporters during Sperm Capacitation in Mammals. Int. J. Mol. Sci., 23.","DOI":"10.3390\/ijms23116333"},{"key":"ref_28","first-page":"930","article-title":"Why Bicarbonate?","volume":"84","author":"Casey","year":"2006","journal-title":"This Paper Is One of a Selection of Papers Published in This Special Issue, Entitled CSBMCB\u2014Membrane Proteins in Health and Disease."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"1148","DOI":"10.1523\/JNEUROSCI.2377-13.2014","article-title":"The Electrogenic Sodium Bicarbonate Cotransporter NBCe1 Is a High-Affinity Bicarbonate Carrier in Cortical Astrocytes","volume":"34","author":"Theparambil","year":"2014","journal-title":"J. Neurosci."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"603","DOI":"10.2174\/138161208783877884","article-title":"Carbonic Anhydrases An Overview","volume":"14","author":"Supuran","year":"2008","journal-title":"Curr. Pharm. Des."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"1988","DOI":"10.1080\/14756366.2021.1972995","article-title":"An Overview on the Recently Discovered Iota-Carbonic Anhydrases","volume":"36","author":"Nocentini","year":"2021","journal-title":"J. Enzyme Inhib. Med. Chem."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"2499","DOI":"10.1038\/sj.emboj.7600736","article-title":"Metabolon Disruption: A Mechanism That Regulates Bicarbonate Transport","volume":"24","author":"Alvarez","year":"2005","journal-title":"EMBO J."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"47886","DOI":"10.1074\/jbc.M105959200","article-title":"A Transport Metabolon: Functional Interaction of Carbonic Anhydrase Ii and Chloride\/Bicarbonate Exchangers","volume":"276","author":"Sterling","year":"2001","journal-title":"J. Biol. Chem."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1016\/S0378-3782(97)00119-9","article-title":"Carbonic Anhydrase Isoenzymes CAI and CAII in Semen, Decidua, Chorionic Villi and Various Fetal Tissues","volume":"51","author":"Nicolaides","year":"1998","journal-title":"Early Hum. Dev."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"713","DOI":"10.1016\/j.bbrc.2015.11.021","article-title":"Carbonic Anhydrases and Their Functional Differences in Human and Mouse Sperm Physiology","volume":"468","author":"Carta","year":"2015","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"477","DOI":"10.1007\/BF00315743","article-title":"A High Activity Carbonic Anhydrase Isoenzyme (CA II) Is Present in Mammalian Spermatozoa","volume":"95","author":"Parkkila","year":"1991","journal-title":"Histochemistry"},{"key":"ref_37","doi-asserted-by":"crossref","unstructured":"Wandernoth, P.M., Raubuch, M., Mannowetz, N., Becker, H.M., Deitmer, J.W., Sly, W.S., and Wennemuth, G. (2010). Role of Carbonic Anhydrase IV in the Bicarbonate-Mediated Activation of Murine and Human Sperm. PLoS ONE, 5.","DOI":"10.1371\/journal.pone.0015061"},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"29202","DOI":"10.1074\/jbc.M115.698597","article-title":"Normal Fertility Requires the Expression of Carbonic Anhydrases II and IV in Sperm","volume":"290","author":"Wandernoth","year":"2015","journal-title":"J. Biol. Chem."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s41467-023-40855-0","article-title":"Control of Intracellular PH and Bicarbonate by CO2 Diffusion into Human Sperm","volume":"14","author":"Grahn","year":"2023","journal-title":"Nat. Commun."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1023\/B:HIJO.0000023387.02793.af","article-title":"Carbonic Anhydrase in Mouse Testis and Epididymis; Transfer of Isozyme IV to Spermatozoa during Passage","volume":"35","author":"Ekstedt","year":"2004","journal-title":"J. Mol. Histol."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1093\/molehr\/5.3.199","article-title":"Novel Transcripts of Carbonic Anhydrase II in Mouse and Human Testis","volume":"5","author":"Mezquita","year":"1999","journal-title":"Mol. Hum. Reprod."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"2719","DOI":"10.1074\/jbc.M308984200","article-title":"Characterization of CA XIII, a Novel Member of the Carbonic Anhydrase Isozyme Family","volume":"279","author":"Lehtonen","year":"2004","journal-title":"J. Biol. Chem."},{"key":"ref_43","doi-asserted-by":"crossref","unstructured":"Don\u00e0, G., Tibaldi, E., Andrisani, A., Ambrosini, G., Sabbadin, C., Pagano, M.A., Brunati, A.M., Armanini, D., Ragazzi, E., and Bordin, L. (2020). Human Sperm Capacitation Involves the Regulation of the Tyr-Phosphorylation Level of the Anion Exchanger 1 (AE1). Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21114063"},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"15847","DOI":"10.1073\/pnas.2536127100","article-title":"Anion Exchanger 2 Is Essential for Spermiogenesis in Mice","volume":"100","author":"Medina","year":"2003","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"7001","DOI":"10.1074\/jbc.M206284200","article-title":"Involvement of a Na+\/HCO Cotransporter in Mouse Sperm Capacitation","volume":"278","author":"Demarco","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_46","first-page":"14","article-title":"Participation of the Cl\u2212\/HCO3 Exchangers SLC26A3 and SLC26A6, the Cl\u2212 Channel CFTR, and the Regulatory Factor SLC9A3R1 in Mouse Sperm Capacitation","volume":"86","author":"Wertheimer","year":"2012","journal-title":"Biol. Reprod."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1095\/biolreprod.108.068528","article-title":"Cl\u2212 Is Required for HCO3\u2212 Entry Necessary for Sperm Capacitation in Guinea Pig: Involvement of a Cl\u2212\/HCO3\u2212 Exchanger (SLC26A3) and CFTR1","volume":"80","author":"Chen","year":"2009","journal-title":"Biol. Reprod."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1093\/molehr\/gal009","article-title":"Expression of SLC26A3, CFTR and NHE3 in the Human Male Reproductive Tract: Role in Male Subfertility Caused by Congenital Chloride Diarrhoea","volume":"12","author":"Hihnala","year":"2006","journal-title":"Mol. Hum. Reprod."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"317","DOI":"10.1093\/humrep\/dep406","article-title":"CFTR Is Essential for Sperm Fertilizing Capacity and Is Correlated with Sperm Quality in Humans","volume":"25","author":"Li","year":"2010","journal-title":"Hum. Reprod."},{"key":"ref_50","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_51","doi-asserted-by":"crossref","first-page":"1404","DOI":"10.1002\/jcp.25634","article-title":"Essential Role of CFTR in PKA-Dependent Phosphorylation, Alkalinization, and Hyperpolarization During Human Sperm Capacitation","volume":"232","author":"Pinto","year":"2017","journal-title":"J. Cell. Physiol."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"902","DOI":"10.1038\/ncb1047","article-title":"Involvement of CFTR in Uterine Bicarbonate Secretion and the Fertilizing Capacity of Sperm","volume":"5","author":"Wang","year":"2003","journal-title":"Nat. Cell Biol."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"9816","DOI":"10.1073\/pnas.0609253104","article-title":"Cystic Fibrosis Transmembrane Conductance Regulator Is Vital to Sperm Fertilizing Capacity and Male Fertility","volume":"104","author":"Xu","year":"2007","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_54","first-page":"547","article-title":"The Sodium-Proton Exchangers SNHE and NHE1 Control Plasma Membrane Hyperpolarization in Mouse Sperm","volume":"38","author":"Novero","year":"2024","journal-title":"bioRxiv"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"348","DOI":"10.1002\/mrd.90002","article-title":"Roles of the Na,K-ATPase A4 Isoform and the Na+\/H+ Exchanger in Sperm Motility","volume":"62","author":"Woo","year":"2002","journal-title":"Mol. Reprod. Dev."},{"key":"ref_56","doi-asserted-by":"crossref","unstructured":"Balbach, M., Hamzeh, H., Jikeli, J.F., Brenker, C., Schiffer, C., Hansen, J.N., Neugebauer, P., Tr\u00f6tschel, C., Jovine, L., and Han, L. (2020). Molecular Mechanism Underlying the Action of Zona-Pellucida Glycoproteins on Mouse Sperm. Front. Cell Dev. Biol., 8.","DOI":"10.3389\/fcell.2020.572735"},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"e2152","DOI":"10.1038\/cddis.2016.65","article-title":"Sodium\u2013Hydrogen Exchanger NHA1 and NHA2 Control Sperm Motility and Male Fertility","volume":"7","author":"Chen","year":"2016","journal-title":"Cell Death Dis."},{"key":"ref_58","doi-asserted-by":"crossref","unstructured":"Gardner, C.C., and James, P.F. (2023). The SLC9C2 Gene Product (Na+\/H+ Exchanger Isoform 11; NHE11) Is a Testis-Specific Protein Localized to the Head of Mature Mammalian Sperm. Int. J. Mol. Sci., 24.","DOI":"10.3390\/ijms24065329"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"2606","DOI":"10.1016\/j.celrep.2018.08.016","article-title":"Asymmetrically Positioned Flagellar Control Units Regulate Human Sperm Rotation","volume":"24","author":"Miller","year":"2018","journal-title":"Cell Rep."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"E11847","DOI":"10.1073\/pnas.1816189115","article-title":"Role of Human Hv1 Channels in Sperm Capacitation and White Blood Cell Respiratory Burst Established by a Designed Peptide Inhibitor","volume":"115","author":"Zhao","year":"2018","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_61","doi-asserted-by":"crossref","unstructured":"Zhao, R., Dai, H., Arias, R.J., De Blas, G.A., Orta, G., Pavarotti, M.A., Shen, R., Perozo, E., Mayorga, L.S., and Darszon, A. (2021). Direct Activation of the Proton Channel by Albumin Leads to Human Sperm Capacitation and Sustained Release of Inflammatory Mediators by Neutrophils. Nat. Commun., 12.","DOI":"10.1038\/s41467-021-24145-1"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"1341","DOI":"10.1152\/physrev.00032.2008","article-title":"Calcium Pumps in Health and Disease","volume":"89","author":"Brini","year":"2009","journal-title":"Physiol. Rev."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"33742","DOI":"10.1074\/jbc.M404628200","article-title":"Targeted Ablation of Plasma Membrane Ca2+-ATPase (PMCA) 1 and 4 Indicates a Major Housekeeping Function for PMCA1 and a Critical Role in Hyperactivated Sperm Motility and Male Fertility for PMCA4","volume":"279","author":"Okunade","year":"2004","journal-title":"J. Biol. Chem."},{"key":"ref_64","doi-asserted-by":"crossref","unstructured":"Mannowetz, N., Wandernoth, P.M., and Wennemuth, G. (2012). Glucose Is a PH-Dependent Motor for Sperm Beat Frequency during Early Activation. PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0041030"},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"600","DOI":"10.4103\/1008-682X.157650","article-title":"Interaction between Basigin and Monocarboxylate Transporter 2 in the Mouse Testes and Spermatozoa","volume":"18","author":"Chen","year":"2016","journal-title":"Asian J. Androl."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1093\/biolreprod\/78.s1.187b","article-title":"Lactate Dehydrogenase-C4 (LDH-C4) Is Essential for Sperm Function","volume":"78","author":"Odet","year":"2008","journal-title":"Biol. Reprod."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"gaac005","DOI":"10.1093\/molehr\/gaac005","article-title":"Acrosomal Alkalinization Occurs during Human Sperm Capacitation","volume":"28","author":"Aldana","year":"2022","journal-title":"Mol. Hum. Reprod."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"18098","DOI":"10.1074\/jbc.M111567200","article-title":"A Proton Pump ATPase with Testis-Specific E1-Subunit Isoform Required for Acrosome Acidification","volume":"277","author":"Yamamoto","year":"2002","journal-title":"J. Biol. Chem."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"1057","DOI":"10.1095\/biolreprod.105.044123","article-title":"Chloride Channels in Physiological Volume Regulation of Human Spermatozoa","volume":"73","author":"Yeung","year":"2005","journal-title":"Biol. Reprod."},{"key":"ref_70","doi-asserted-by":"crossref","unstructured":"Zhong, J., Dong, J., Ruan, W., and Duan, X. (2023). Potential Theranostic Roles of SLC4 Molecules in Human Diseases. Int. J. Mol. Sci., 24.","DOI":"10.3390\/ijms242015166"},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"3783","DOI":"10.1007\/s00018-019-03170-w","article-title":"PH and Male Fertility: Making Sense on PH Homeodynamics throughout the Male Reproductive Tract","volume":"76","author":"Bernardino","year":"2019","journal-title":"Cell. Mol. Life Sci."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"1139","DOI":"10.1242\/dev.121.4.1139","article-title":"Capacitation of Mouse Spermatozoa: II. Protein Tyrosine Phosphorylation and Capacitation Are Regulated by a CAMP-Dependent Pathway","volume":"121","author":"Visconti","year":"1995","journal-title":"Development"},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"1129","DOI":"10.1242\/dev.121.4.1129","article-title":"Capacitation of Mouse Spermatozoa: I. Correlation between the Capacitation State and Protein Tyrosine Phosphorylation","volume":"121","author":"Visconti","year":"1995","journal-title":"Development"},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"9924","DOI":"10.1074\/jbc.RA118.003166","article-title":"CFTR\/ENaC-Dependent Regulation of Membrane Potential during Human Sperm Capacitation Is Initiated by Bicarbonate Uptake through NBC","volume":"293","author":"Lis","year":"2018","journal-title":"J. Biol. Chem."},{"key":"ref_75","first-page":"1","article-title":"Importance of Slc26 Transmembrane Anion Exchangers in Sperm Post-Testicular Maturation and Fertilization Potential","volume":"7","year":"2019","journal-title":"Front. Cell Dev. Biol."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"511","DOI":"10.1085\/jgp.200509392","article-title":"Coupling Modes and Stoichiometry of Cl\u2212\/HCO3\u2212 Exchange by Slc26a3 and Slc26a6","volume":"127","author":"Shcheynikov","year":"2006","journal-title":"J. Gen. Physiol."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"343","DOI":"10.1038\/ncb1115","article-title":"Gating of CFTR by the STAS Domain of SLC26 Transporters","volume":"6","author":"Ko","year":"2004","journal-title":"Nat. Cell Biol."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"20309","DOI":"10.1074\/jbc.M011740200","article-title":"Tat1, a Novel Sulfate Transporter Specifically Expressed in Human Male Germ Cells and Potentially Linked to RhoGTPase Signaling","volume":"276","author":"Morin","year":"2001","journal-title":"J. Biol. Chem."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"760","DOI":"10.1016\/j.ajhg.2013.03.016","article-title":"Missense Mutations in SLC26A8, Encoding a Sperm-Specific Activator of CFTR, Are Associated with Human Asthenozoospermia","volume":"92","author":"Dirami","year":"2013","journal-title":"Am. J. Hum. Genet."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"37962","DOI":"10.1074\/jbc.M607527200","article-title":"Slc26a3 (Dra)-Deficient Mice Display Chloride-Losing Diarrhea, Enhanced Colonic Proliferation, and Distinct Up-Regulation of Ion Transporters in the Colon","volume":"281","author":"Schweinfest","year":"2006","journal-title":"J. Biol. Chem."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1093\/molehr\/gah140","article-title":"Mutational Analysis of the Human SLC26A8 Gene: Exclusion as a Candidate for Male Infertility Due to Primary Spermatogenic Failure","volume":"11","author":"Eklund","year":"2005","journal-title":"Mol. Hum. Reprod."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"202","DOI":"10.1126\/science.1712984","article-title":"Demonstration That CFTR Is a Chloride Channel by Alteration of Its Anion Selectivity","volume":"253","author":"Anderson","year":"1991","journal-title":"Science"},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"2037","DOI":"10.1016\/S0021-9258(18)53959-4","article-title":"Regulation of the Cystic Fibrosis Transmembrane Conductance Regulator Cl\u2212 Channel by Specific Protein Kinases and Protein Phosphatases","volume":"268","author":"Berger","year":"1993","journal-title":"J. Biol. Chem."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1016\/j.fertnstert.2005.07.1282","article-title":"Increased Frequency of Cystic Fibrosis Transmembrane Conductance Regulator Gene Mutations in Infertile Males","volume":"85","author":"Schulz","year":"2006","journal-title":"Fertil. Steril."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"24397","DOI":"10.1074\/jbc.M701603200","article-title":"Involvement of Cystic Fibrosis Transmembrane Conductance Regulator in Mouse Sperm Capacitation","volume":"282","author":"Castellano","year":"2007","journal-title":"J. Biol. Chem."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"590","DOI":"10.1002\/jcp.24166","article-title":"Electrophysiological Evidence for the Presence of Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) in Mouse Sperm","volume":"228","author":"Acevedo","year":"2013","journal-title":"J. Cell. Physiol."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1007\/s00424-013-1408-8","article-title":"Traditional and Emerging Roles for the SLC9 Na+\/H+ Exchangers","volume":"466","author":"Fuster","year":"2014","journal-title":"Pflugers Arch. Eur. J. Physiol."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"549","DOI":"10.1007\/s00424-003-1110-3","article-title":"Diversity of the Mammalian Sodium\/Proton Exchanger SLC9 Gene Family","volume":"447","author":"Orlowski","year":"2004","journal-title":"Pflugers Arch. Eur. J. Physiol."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"4383","DOI":"10.1074\/jbc.274.7.4383","article-title":"Molecular Cloning and Functional Expression of a Rat Na+\/H+ Exchanger (NHE5) Highly Expressed in Brain","volume":"274","author":"Attaphitaya","year":"1999","journal-title":"J. Biol. Chem."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"2015","DOI":"10.1152\/physrev.00028.2018","article-title":"The SLC9A-C Mammalian Na+\/H+ Exchanger Family: Molecules, Mechanisms, and Physiology","volume":"99","author":"Pedersen","year":"2019","journal-title":"Physiol. Rev."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"2809","DOI":"10.1038\/s41467-018-05253-x","article-title":"The Solute Carrier SLC9C1 Is a Na+\/H+-Exchanger Gated by an S4-Type Voltage-Sensor and Cyclic-Nucleotide Binding","volume":"9","author":"Windler","year":"2018","journal-title":"Nat. Commun."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1007\/s11033-006-0010-y","article-title":"Cloning of a Novel Human NHEDC1 (Na+\/H+ Exchanger like Domain Containing 1) Gene Expressed Specifically in Testis","volume":"33","author":"Ye","year":"2006","journal-title":"Mol. Biol. Rep."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"1547","DOI":"10.1681\/ASN.2007111245","article-title":"Characterization of the Sodium\/Hydrogen Exchanger NHA2","volume":"19","author":"Fuster","year":"2008","journal-title":"J. Am. Soc. Nephrol."},{"key":"ref_94","doi-asserted-by":"crossref","unstructured":"Bernardazzi, C., Sheikh, I.A., Xu, H., and Ghishan, F.K. (2022). The Physiological Function and Potential Role of the Ubiquitous Na+\/H+ Exchanger Isoform 8 (NHE8): An Overview Data. Int. J. Mol. Sci., 23.","DOI":"10.3390\/ijms231810857"},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"10845","DOI":"10.1074\/jbc.M117.784108","article-title":"Loss of the Na+\/H+ Exchanger NHE8 Causes Male Infertility in Mice by Disrupting Acrosome Formation","volume":"292","author":"Oberheide","year":"2017","journal-title":"J. Biol. Chem."},{"key":"ref_96","doi-asserted-by":"crossref","unstructured":"Wang, Y.Y., Chiang, H.S., Cheng, C.Y., Wu, Y.N., Lin, Y.C., Liu, H.C., Tsai, W.K., Chen, Y.L., and Lin, Y.H. (2017). SLC9A3 Protein Is Critical for Acrosomal Formation in Postmeiotic Male Germ Cells. Int. J. Mol. Sci., 19.","DOI":"10.3390\/ijms19010103"},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"C330","DOI":"10.1152\/ajpcell.00289.2014","article-title":"Disruption of NHE8 Expression Impairs Leydig Cell Function in the Testes","volume":"308","author":"Xu","year":"2015","journal-title":"Am. J. Physiol. Cell Physiol."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"202","DOI":"10.1038\/s41586-023-06629-w","article-title":"Structures of a Sperm-Specific Solute Carrier Gated by Voltage and CAMP","volume":"623","author":"Kalienkova","year":"2023","journal-title":"Nature"},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1038\/s41586-023-06518-2","article-title":"Structure and Electromechanical Coupling of a Voltage-Gated Na+\/H+ Exchanger","volume":"623","author":"Yeo","year":"2023","journal-title":"Nature"},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"3925","DOI":"10.1126\/sciadv.abn3925","article-title":"Structural Basis of Autoinhibition of the Human NHE3-CHP1 Complex","volume":"8","author":"Dong","year":"2022","journal-title":"Sci. Adv."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s41467-021-23496-z","article-title":"Structure and Mechanism of the Human NHE1-CHP1 Complex","volume":"12","author":"Dong","year":"2021","journal-title":"Nat. Commun."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"4541","DOI":"10.15252\/embj.2020105908","article-title":"Structure and Elevator Mechanism of the Mammalian Sodium\/Proton Exchanger NHE9","volume":"39","author":"Winkelmann","year":"2020","journal-title":"EMBO J."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"e03579","DOI":"10.7554\/eLife.03579","article-title":"Structure and Substrate Ion Binding in the Sodium\/Proton Antiporter PaNhaP","volume":"3","author":"Yildiz","year":"2014","journal-title":"Elife"},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"1","DOI":"10.7554\/eLife.03583","article-title":"Structure and Transport Mechanism of the Sodium\/Proton Antiporter MjNhaP1","volume":"3","author":"Paulino","year":"2014","journal-title":"Elife"},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"573","DOI":"10.1038\/nature12484","article-title":"A Two-Domain Elevator Mechanism for Sodium\/Proton Antiport","volume":"501","author":"Lee","year":"2013","journal-title":"Nature"},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"1197","DOI":"10.1038\/nature03692","article-title":"Structure of a Na+\/H+ Antiporter and Insights into Mechanism of Action and Regulation by PH","volume":"435","author":"Hunte","year":"2005","journal-title":"Nature"},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"108","DOI":"10.1038\/s41594-022-00738-2","article-title":"Structure, Mechanism and Lipid-Mediated Remodeling of the Mammalian Na+\/H+ Exchanger NHA2","volume":"29","author":"Matsuoka","year":"2022","journal-title":"Nat. Struct. Mol. Biol."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1016\/0012-1606(89)90164-4","article-title":"An Adhesion-Associated Agonist from the Zona Pellucida Activates G Protein-Promoted Elevations of Internal Ca2+ and PH That Mediate Mammalian Sperm Acrosomal Exocytosis","volume":"135","author":"Florman","year":"1989","journal-title":"Dev. Biol."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"e2109993118","DOI":"10.1073\/pnas.2109993118","article-title":"Molecular Mechanisms of Sperm Motility Are Conserved in an Early-Branching Metazoan","volume":"118","author":"Speer","year":"2021","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1186\/s40851-019-0141-3","article-title":"Comparative Genomic Analysis Suggests That the Sperm-Specific Sodium\/Proton Exchanger and Soluble Adenylyl Cyclase Are Key Regulators of CatSper among the Metazoa","volume":"5","author":"Romero","year":"2019","journal-title":"Zool. Lett."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"106172","DOI":"10.1016\/j.pep.2022.106172","article-title":"How to Study a Highly Toxic Protein to Bacteria: A Case of Voltage Sensor Domain of Mouse Sperm-Specific Sodium\/Proton Exchanger","volume":"201","author":"Islas","year":"2023","journal-title":"Protein Expr. Purif."},{"key":"ref_112","doi-asserted-by":"crossref","unstructured":"Ch\u00e1vez, J.C., Darszon, A., Trevi\u00f1o, C.L., and Nishigaki, T. (2020). Quantitative Intracellular PH Determinations in Single Live Mammalian Spermatozoa Using the Ratiometric Dye SNARF-5F. Front. Cell Dev. Biol., 7.","DOI":"10.3389\/fcell.2019.00366"},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"826","DOI":"10.1038\/299826a0","article-title":"Hydrogen Ion Currents and Intracellular PH in Depolarized Voltage-Clamped Snail Neurones","volume":"299","author":"Thomas","year":"1982","journal-title":"Nature"},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"1213","DOI":"10.1038\/nature04700","article-title":"A Voltage-Gated Proton-Selective Channel Lacking the Pore Domain","volume":"440","author":"Ramsey","year":"2006","journal-title":"Nature"},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"3471","DOI":"10.1016\/j.febslet.2015.08.003","article-title":"Voltage-Gated Proton (Hv1) Channels, a Singular Voltage Sensing Domain","volume":"589","author":"Castillo","year":"2015","journal-title":"FEBS Lett."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1038\/nature10557","article-title":"Aspartate\u2009112 Is the Selectivity Filter of the Human Voltage-Gated Proton Channel","volume":"480","author":"Musset","year":"2011","journal-title":"Nature"},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"861","DOI":"10.1085\/jgp.105.6.861","article-title":"The Voltage-Activated Hydrogen Ion Conductance in Rat Alveolar Epithelial Cells Is Determined by the PH Gradient","volume":"105","author":"Cherny","year":"1995","journal-title":"J. Gen. Physiol."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"475","DOI":"10.1152\/physrev.00028.2002","article-title":"Voltage-Gated Proton Channels and Other Proton Transfer Pathways","volume":"83","author":"Decoursey","year":"2003","journal-title":"Physiol. Rev."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"7642","DOI":"10.1073\/pnas.0902761106","article-title":"Hv1 Proton Channels Are Required for High-Level NADPH Oxidase-Dependent Superoxide Production during the Phagocyte Respiratory Burst","volume":"106","author":"Ramsey","year":"2009","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"118","DOI":"10.1016\/j.theriogenology.2019.06.015","article-title":"Functional Insights into Voltage Gated Proton Channel (Hv1) in Bull Spermatozoa","volume":"136","author":"Mishra","year":"2019","journal-title":"Theriogenology"},{"key":"ref_121","doi-asserted-by":"crossref","unstructured":"Yeste, M., Llavanera, M., Mateo-Otero, Y., Catal\u00e1n, J., Bonet, S., and Pinart, E. (2020). HVCN1 Channels Are Relevant for the Maintenance of Sperm Motility During In Vitro Capacitation of Pig Spermatozoa. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21093255"},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"1533","DOI":"10.1113\/JP273189","article-title":"Post-Translational Cleavage of Hv1 in Human Sperm Tunes PH- and Voltage-Dependent Gating","volume":"595","author":"Berger","year":"2017","journal-title":"J. Physiol."},{"key":"ref_123","doi-asserted-by":"crossref","unstructured":"Lishko, P.V., Botchkina, I.L., and Kirichok, Y. (2011). Progesterone Activates the Principal Ca2+ Channel of Human Sperm. Nature, 7\u201312.","DOI":"10.1038\/nature09767"},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1016\/j.mod.2018.04.004","article-title":"Mechanisms of Development Regulation Mechanisms and Implications of Sperm Membrane Hyperpolarization","volume":"154","author":"Ritagliati","year":"2018","journal-title":"Mech. Dev."},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"405","DOI":"10.1085\/jgp.201611672","article-title":"The Hv1 Proton Channel Responds to Mechanical Stimuli","volume":"148","author":"Pathak","year":"2016","journal-title":"J. Gen. Physiol."},{"key":"ref_126","doi-asserted-by":"crossref","unstructured":"Han, S., Peng, S., Vance, J., Tran, K., Do, N., Bui, N., Gui, Z., and Wang, S. (2022). Structural Dynamics Determine Voltage and PH Gating in Human Voltage-Gated Proton Channel. Elife, 11.","DOI":"10.7554\/eLife.73093"},{"key":"ref_127","doi-asserted-by":"crossref","unstructured":"Ferreira, J.J., Lybaert, P., Puga-Molina, L.C., and Santi, C.M. (2021). Conserved Mechanism of Bicarbonate-Induced Sensitization of CatSper Channels in Human and Mouse Sperm. Front. Cell Dev. Biol., 9.","DOI":"10.3389\/fcell.2021.733653"},{"key":"ref_128","doi-asserted-by":"crossref","unstructured":"Soriano-\u00dabeda, C., Romero-Aguirregomezcorta, J., Mat\u00e1s, C., Visconti, P.E., and Garc\u00eda-V\u00e1zquez, F.A. (2019). Manipulation of Bicarbonate Concentration in Sperm Capacitation Media Improves in Vitro Fertilisation Output in Porcine Species. J. Anim. Sci. Biotechnol., 10.","DOI":"10.1186\/s40104-019-0324-y"},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"16830","DOI":"10.1074\/jbc.RA117.001566","article-title":"CatSper Channels Are Regulated by Protein Kinase A","volume":"293","author":"Orta","year":"2018","journal-title":"J. Biol. Chem."},{"key":"ref_130","doi-asserted-by":"crossref","unstructured":"Carlson, A.E., Hille, B., and Babcock, D.F. (2007). External Ca2+ Acts Upstream of Adenylyl Cyclase SACY in the Bicarbonate Signaled Activation of Sperm Motility. Dev. Biol., 312.","DOI":"10.1016\/j.ydbio.2007.09.017"},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"311","DOI":"10.1007\/978-1-60761-700-6_17","article-title":"Measurement of Intracellular PH","volume":"637","author":"Loiselle","year":"2010","journal-title":"Methods Mol. Biol."},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1085\/jgp.200308839","article-title":"Calcium Clearance Mechanisms of Mouse Sperm","volume":"122","author":"Wennemuth","year":"2003","journal-title":"J. Gen. Physiol."},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"28220","DOI":"10.1074\/jbc.M312599200","article-title":"Plasma Membrane Ca2+ ATPase 4 Is Required for Sperm Motility and Male Fertility","volume":"279","author":"Schuh","year":"2004","journal-title":"J. Biol. Chem."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1016\/B978-0-12-394316-3.00009-0","article-title":"The SLC16A Family of Monocarboxylate Transporters (MCTs)\u2014Physiology and Function in Cellular Metabolism, PH Homeostasis, and Fluid Transport","volume":"70","author":"Adijanto","year":"2012","journal-title":"Curr. Top. Membr."},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"619","DOI":"10.1007\/s00424-003-1067-2","article-title":"The SLC16 Gene Family\u2014From Monocarboxylate Transporters (MCTs) to Aromatic Amino Acid Transporters and Beyond","volume":"447","author":"Halestrap","year":"2004","journal-title":"Pflugers Arch. Eur. J. Physiol."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"683","DOI":"10.1095\/biolreprod41.4.683","article-title":"Capacitation of Bovine Sperm by Heparin: Inhibitory Effect of Glucose and Role of Intracellular PH1","volume":"41","author":"PARRISH","year":"1989","journal-title":"Biol. Reprod."},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"540","DOI":"10.1095\/biolreprod.103.026054","article-title":"Glycolysis Plays a Major Role for Adenosine Triphosphate Supplementation in Mouse Sperm Flagellar Movement","volume":"71","author":"Mukai","year":"2004","journal-title":"Biol. Reprod."},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"98","DOI":"10.1177\/26.2.24069","article-title":"The PH of the Hamster Sperm Acrosome","volume":"26","author":"Meizel","year":"1978","journal-title":"J. Histochem. Cytochem."},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1002\/jez.1402270114","article-title":"Correlation of Increased Intraacrosomal PH with the Hamster Sperm Acrosome Reaction","volume":"227","author":"Working","year":"1983","journal-title":"J. Exp. Zool."},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"222","DOI":"10.1006\/dbio.2001.0353","article-title":"Alkalinization of Acrosome Measured by GFP as a PH Indicator and Its Relation to Sperm Capacitation","volume":"237","author":"Nakanishi","year":"2001","journal-title":"Dev. Biol."},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"49326","DOI":"10.1074\/jbc.M208587200","article-title":"The Intraacrosomal Calcium Pool Plays a Direct Role in Acrosomal Exocytosis","volume":"277","author":"Michaut","year":"2002","journal-title":"J. Biol. Chem."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1530\/REP-09-0134","article-title":"Ca2+-Stores in Sperm: Their Identities and Functions","volume":"138","author":"Costello","year":"2009","journal-title":"Reproduction"},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"2513","DOI":"10.1073\/pnas.1917595117","article-title":"Acrosin Is Essential for Sperm Penetration through the Zona Pellucida in Hamsters","volume":"117","author":"Hirose","year":"2020","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"152","DOI":"10.1006\/dbio.1994.1242","article-title":"Sequential Focal and Global Elevations of Sperm Intracellular Ca2+ Are Initiated by the Zona Pellucida during Acrosomal Exocytosis","volume":"165","author":"Florman","year":"1994","journal-title":"Dev. Biol."},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"95","DOI":"10.4161\/spmg.1.2.16820","article-title":"Acrosome Biogenesis","volume":"1","author":"Berruti","year":"2011","journal-title":"Spermatogenesis"},{"key":"ref_146","doi-asserted-by":"crossref","unstructured":"Khawar, M.B., Gao, H., and Li, W. (2019). Mechanism of Acrosome Biogenesis in Mammals. Front. Cell Dev. Biol., 8.","DOI":"10.3389\/fcell.2019.00195"},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"777","DOI":"10.1007\/s11427-016-5090-x","article-title":"Regulation of Lysosomal Ion Homeostasis by Channels and Transporters","volume":"59","author":"Xiong","year":"2016","journal-title":"Sci. China Life Sci."},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"917","DOI":"10.1038\/nrm2272","article-title":"Vacuolar ATPases: Rotary Proton Pumps in Physiology and Pathophysiology","volume":"8","author":"Forgac","year":"2007","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"896","DOI":"10.1002\/pro.3147","article-title":"Breaking up and Making up: The Secret Life of the Vacuolar H+-ATPase","volume":"26","author":"Oot","year":"2017","journal-title":"Protein Sci."},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1186\/s12943-018-0811-3","article-title":"The Curious Case of Vacuolar ATPase: Regulation of Signaling Pathways","volume":"17","author":"Pamarthy","year":"2018","journal-title":"Mol. Cancer"},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"531","DOI":"10.1016\/j.bbrc.2013.12.011","article-title":"Characterization of NAADP-Mediated Calcium Signaling in Human Spermatozoa","volume":"443","author":"Vasudevan","year":"2014","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"C1326","DOI":"10.1152\/ajpcell.00552.2009","article-title":"Proteomic Analysis of V-ATPase-Rich Cells Harvested from the Kidney and Epididymis by Fluorescence-Activated Cell Sorting","volume":"298","author":"Pisitkun","year":"2010","journal-title":"Am. J. Physiol. Physiol."},{"key":"ref_153","doi-asserted-by":"crossref","first-page":"385","DOI":"10.1085\/jgp.201110596","article-title":"Lysosomal PH and Analysis of the Counter Ion Pathways That Support Acidification","volume":"137","author":"DiCiccio","year":"2011","journal-title":"J. Gen. Physiol."},{"key":"ref_154","doi-asserted-by":"crossref","first-page":"28611","DOI":"10.1074\/jbc.M113.509364","article-title":"Common Gating of Both CLC Transporter Subunits Underlies Voltage-Dependent Activation of the 2Cl\u2212\/1H+ Exchanger ClC-7\/Ostm1","volume":"288","author":"Ludwig","year":"2013","journal-title":"J. Biol. Chem."},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"35539","DOI":"10.1074\/jbc.M804586200","article-title":"Chloride Is Essential for Capacitation and for the Capacitation-Associated Increase in Tyrosine Phosphorylation","volume":"283","author":"Wertheimer","year":"2008","journal-title":"J. Biol. Chem."},{"key":"ref_156","doi-asserted-by":"crossref","first-page":"2659","DOI":"10.1113\/jphysiol.2011.224485","article-title":"Human Spermatozoa Possess a Calcium-Dependent Chloride Channel That May Participate in the Acrosomal Reaction","volume":"590","author":"Orta","year":"2012","journal-title":"J. Physiol."},{"key":"ref_157","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1002\/j.1939-4640.2000.tb03281.x","article-title":"The Mouse Sperm Glycine Receptor\/Chloride Channel: Cellular Localization and Involvement in the Acrosome Reaction Initiated by Glycine","volume":"21","author":"SATO","year":"2000","journal-title":"J. Androl."},{"key":"ref_158","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1016\/j.anireprosci.2011.07.001","article-title":"Bull Sperm Acrosome Reaction Induced by Gamma-Aminobutyric Acid (GABA) Is Mediated by GABAergic Receptors Type A","volume":"127","author":"Puente","year":"2011","journal-title":"Anim. Reprod. Sci."},{"key":"ref_159","doi-asserted-by":"crossref","first-page":"5944","DOI":"10.1002\/jcb.26789","article-title":"TMEM16A Inhibition Impedes Capacitation and Acquisition of Hyperactivated Motility in Guinea Pig Sperm","volume":"119","year":"2018","journal-title":"J. Cell. Biochem."},{"key":"ref_160","doi-asserted-by":"crossref","first-page":"4091","DOI":"10.1113\/JP270043","article-title":"Discovery of CLC Transport Proteins: Cloning, Structure, Function and Pathophysiology","volume":"593","author":"Jentsch","year":"2015","journal-title":"J. Physiol."},{"key":"ref_161","doi-asserted-by":"crossref","first-page":"222","DOI":"10.1016\/j.ceca.2014.12.005","article-title":"Evolution of Acidic Ca2+ Stores and Their Resident Ca2+-Permeable Channels","volume":"57","author":"Patel","year":"2015","journal-title":"Cell Calcium"},{"key":"ref_162","doi-asserted-by":"crossref","first-page":"2935","DOI":"10.1113\/JP284247","article-title":"Two-Pore Channel 1 and Ca2+ Release-Activated Ca2+ Channels Contribute to the Acrosomal PH-Dependent Intracellular Ca2+ Increase in Mouse Sperm","volume":"601","author":"Oliver","year":"2023","journal-title":"J. Physiol."},{"key":"ref_163","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1017\/S0967199498000094","article-title":"Localisation of Inositol Trisphosphate and Ryanodine Receptors during Mouse Spermatogenesis: Possible Functional Implications","volume":"6","author":"Santi","year":"1998","journal-title":"Zygote"},{"key":"ref_164","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1093\/molehr\/gam012","article-title":"Identification and Localisation of SERCA 2 Isoforms in Mammalian Sperm","volume":"13","author":"Lawson","year":"2007","journal-title":"Mol. Hum. Reprod."},{"key":"ref_165","doi-asserted-by":"crossref","first-page":"948","DOI":"10.1091\/mbc.e13-09-0523","article-title":"NAADP and the Two-Pore Channel Protein 1 Participate in the Acrosome Reaction in Mammalian Spermatozoa","volume":"25","author":"Arndt","year":"2014","journal-title":"Mol. Biol. Cell"},{"key":"ref_166","doi-asserted-by":"crossref","first-page":"4735","DOI":"10.1002\/jcp.26262","article-title":"Acrosomal Alkalization Triggers Ca2+ Release and Acrosome Reaction in Mammalian Spermatozoa","volume":"233","author":"Torres","year":"2018","journal-title":"J. Cell. Physiol."},{"key":"ref_167","doi-asserted-by":"crossref","first-page":"315","DOI":"10.1038\/361315a0","article-title":"Inositol Trisphosphate and Calcium Signalling","volume":"361","author":"Berridge","year":"1993","journal-title":"Nature"},{"key":"ref_168","doi-asserted-by":"crossref","unstructured":"Zhang, X., Huang, R., Zhou, Y., Zhou, W., and Zeng, X. (2020). Ip3r Channels in Male Reproduction. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21239179"},{"key":"ref_169","doi-asserted-by":"crossref","first-page":"184","DOI":"10.1016\/j.ceca.2011.01.006","article-title":"Ca2+ Signalling in the Golgi Apparatus","volume":"50","author":"Pizzo","year":"2011","journal-title":"Cell Calcium"},{"key":"ref_170","doi-asserted-by":"crossref","first-page":"857","DOI":"10.1083\/jcb.130.4.857","article-title":"Inositol 1,4,5-Trisphosphate Receptors Selectively Localized to the Acrosomes of Mammalian Sperm","volume":"130","author":"Walensky","year":"1995","journal-title":"J. Cell Biol."},{"key":"ref_171","doi-asserted-by":"crossref","unstructured":"Mata-Mart\u00ednez, E., S\u00e1nchez-C\u00e1rdenas, C., Ch\u00e1vez, J.C., Guerrero, A., Trevi\u00f1o, C.L., Corkidi, G., Montoya, F., Hernandez-Herrera, P., Buffone, M.G., and Balestrini, P.A. (2021). Role of Calcium Oscillations in Sperm Physiology. Biosystems, 209.","DOI":"10.1016\/j.biosystems.2021.104524"},{"key":"ref_172","first-page":"1","article-title":"Acrosome Reaction and Ca2+ Imaging in Single Human Spermatozoa: New Regulatory Roles of [Ca2+]I","volume":"91","author":"Darszon","year":"2014","journal-title":"Biol. Reprod."},{"key":"ref_173","doi-asserted-by":"crossref","first-page":"146","DOI":"10.1016\/j.bbrc.2018.02.042","article-title":"PH-Dependent Ca+2 Oscillations Prevent Untimely Acrosome Reaction in Human Sperm","volume":"497","author":"Darszon","year":"2018","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_174","doi-asserted-by":"crossref","unstructured":"Ot\u010den\u00e1\u0161kov\u00e1, T., Mac\u00ed\u010dkov\u00e1, E., Vondr\u00e1kov\u00e1, J., Frol\u00edkov\u00e1, M., Komrskova, K., Stopkov\u00e1, R., and Stopka, P. (2023). Proteomic Analysis of the Mouse Sperm Acrosome - towards an Understanding of an Organelle with Diverse Functionality. Eur. J. Cell Biol., 102.","DOI":"10.1016\/j.ejcb.2023.151296"},{"key":"ref_175","doi-asserted-by":"crossref","first-page":"2495","DOI":"10.1016\/0006-2952(74)90174-9","article-title":"Lysosomotropic Agents","volume":"23","author":"Poole","year":"1974","journal-title":"Biochem. Pharmacol."},{"key":"ref_176","doi-asserted-by":"crossref","first-page":"2624","DOI":"10.1128\/MCB.00073-14","article-title":"Functional Amyloids in the Mouse Sperm Acrosome","volume":"34","author":"Guyonnet","year":"2014","journal-title":"Mol. Cell. Biol."},{"key":"ref_177","doi-asserted-by":"crossref","first-page":"511","DOI":"10.1387\/ijdb.072532mb","article-title":"The Role of the Acrosomal Matrix in Fertilization","volume":"52","author":"Buffone","year":"2008","journal-title":"Int. J. Dev. Biol."},{"key":"ref_178","doi-asserted-by":"crossref","first-page":"930","DOI":"10.1016\/j.fertnstert.2020.10.038","article-title":"Machine-Learning Algorithm Incorporating Capacitated Sperm Intracellular PH Predicts Conventional in Vitro Fertilization Success in Normospermic Patients","volume":"115","author":"Gunderson","year":"2021","journal-title":"Fertil. Steril."},{"key":"ref_179","doi-asserted-by":"crossref","first-page":"114","DOI":"10.1016\/j.jprot.2012.12.008","article-title":"In-Depth Proteomic Analysis of the Human Sperm Reveals Complex Protein Compositions","volume":"79","author":"Wang","year":"2013","journal-title":"J. Proteomics"},{"key":"ref_180","doi-asserted-by":"crossref","unstructured":"Schork, K., Turewicz, M., Uszkoreit, J., Rahnenf\u00fchrer, J., and Eisenacher, M. (2022). Characterization of Peptide-Protein Relationships in Protein Ambiguity Groups via Bipartite Graphs. PLoS One, 17.","DOI":"10.1371\/journal.pone.0276401"},{"key":"ref_181","doi-asserted-by":"crossref","first-page":"5995","DOI":"10.1007\/s00216-021-03566-3","article-title":"Pushing the Detection Limits: Strategies towards Highly Sensitive Optical-Based Protein Detection","volume":"413","author":"Momenbeitollahi","year":"2021","journal-title":"Anal. Bioanal. Chem."},{"key":"ref_182","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1085\/jgp.201511496","article-title":"Currents through Hv1 Channels Deplete Protons in Their Vicinity","volume":"147","author":"Islas","year":"2016","journal-title":"J. Gen. Physiol."},{"key":"ref_183","doi-asserted-by":"crossref","first-page":"808","DOI":"10.1016\/j.cell.2014.02.056","article-title":"Structurally Distinct Ca(2+) Signaling Domains of Sperm Flagella Orchestrate Tyrosine Phosphorylation and Motility","volume":"157","author":"Chung","year":"2014","journal-title":"Cell"},{"key":"ref_184","doi-asserted-by":"crossref","first-page":"746","DOI":"10.1038\/s41586-021-03742-6","article-title":"Structure of a Mammalian Sperm Cation Channel Complex","volume":"595","author":"Lin","year":"2021","journal-title":"Nature"},{"key":"ref_185","doi-asserted-by":"crossref","first-page":"aar1968","DOI":"10.1126\/science.aar1968","article-title":"Asymmetric Distribution and Spatial Switching of Dynein Activity Generates Ciliary Motility","volume":"360","author":"Lin","year":"2018","journal-title":"Science"},{"key":"ref_186","doi-asserted-by":"crossref","first-page":"3439","DOI":"10.1038\/s41467-022-31050-8","article-title":"3D Structure and in Situ Arrangements of CatSper Channel in the Sperm Flagellum","volume":"13","author":"Zhao","year":"2022","journal-title":"Nat. Commun."},{"key":"ref_187","doi-asserted-by":"crossref","first-page":"873","DOI":"10.1016\/0092-8674(80)90334-7","article-title":"Mammalian Sperm-Egg Interaction: Identification of a Glycoprotein in Mouse Egg Zonae Pellucidae Possessing Receptor Activity for Sperm","volume":"20","author":"Bleil","year":"1980","journal-title":"Cell"},{"key":"ref_188","doi-asserted-by":"crossref","first-page":"134","DOI":"10.1093\/biolre\/ioy028","article-title":"Sperm\u2013Egg Interaction and Fertilization: Past, Present, and Future","volume":"99","author":"Okabe","year":"2018","journal-title":"Biol. Reprod."}],"container-title":["Cells"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2073-4409\/13\/10\/865\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T14:44:02Z","timestamp":1760107442000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2073-4409\/13\/10\/865"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,5,17]]},"references-count":188,"journal-issue":{"issue":"10","published-online":{"date-parts":[[2024,5]]}},"alternative-id":["cells13100865"],"URL":"https:\/\/doi.org\/10.3390\/cells13100865","relation":{},"ISSN":["2073-4409"],"issn-type":[{"value":"2073-4409","type":"electronic"}],"subject":[],"published":{"date-parts":[[2024,5,17]]}}}