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Factors and pathways involved in capacitation: how are they regulated? <i>Oncotarget<\/i> 2017; 8: 3600\u20133627."},{"key":"6","doi-asserted-by":"crossref","unstructured":"6. Visconti PE, Bailey JL, Moore GD, Pan D, Olds-Clarke P, Kopf GS. Capacitation of mouse spermatozoa. I. Correlation between the capacitation state and protein tyrosine phosphorylation. <i>Development<\/i> 1995; 121: 1129\u20131137.","DOI":"10.1242\/dev.121.4.1129"},{"key":"7","doi-asserted-by":"crossref","unstructured":"7. Visconti PE, Moore GD, Bailey JL, Leclerc P, Connors SA, Pan D, Olds-Clarke P, Kopf GS. Capacitation of mouse spermatozoa. II. Protein tyrosine phosphorylation and capacitation are regulated by a cAMP-dependent pathway. <i>Development<\/i> 1995; 121: 1139\u20131150.","DOI":"10.1242\/dev.121.4.1139"},{"key":"8","doi-asserted-by":"crossref","unstructured":"8. Col\u00e1s C, Grasa P, Casao A, Gallego M, Abecia JA, Forcada F, Cebri\u00e1n-P\u00e9rez JA, Mui\u00f1o-Blanco T. Changes in calmodulin immunocytochemical localization associated with capacitation and acrosomal exocytosis of ram spermatozoa. <i>Theriogenology<\/i> 2009; 71: 789\u2013800.","DOI":"10.1016\/j.theriogenology.2008.10.003"},{"key":"9","doi-asserted-by":"crossref","unstructured":"9. Gonz\u00e1lez-Fern\u00e1ndez L, Mac\u00edas-Garc\u00eda B, Velez IC, Varner DD, Hinrichs K. Calcium-calmodulin and pH regulate protein tyrosine phosphorylation in stallion sperm. <i>Reproduction<\/i> 2012; 144: 411\u2013422.","DOI":"10.1530\/REP-12-0067"},{"key":"10","doi-asserted-by":"crossref","unstructured":"10. Gonz\u00e1lez-Fern\u00e1ndez L, Mac\u00edas-Garc\u00eda B, Loux SC, Varner DD, Hinrichs K. Focal adhesion kinases and calcium\/calmodulin-dependent protein kinases regulate protein tyrosine phosphorylation in stallion sperm. <i>Biol Reprod<\/i> 2013; 88: 138.","DOI":"10.1095\/biolreprod.112.107078"},{"key":"11","doi-asserted-by":"crossref","unstructured":"11. Li X, Wang L, Li Y, Zhao N, Zhen L, Fu J, Yang Q. Calcium regulates motility and protein phosphorylation by changing cAMP and ATP concentrations in boar sperm in vitro. <i>Anim Reprod Sci<\/i> 2016; 172: 39\u201351.","DOI":"10.1016\/j.anireprosci.2016.07.001"},{"key":"12","doi-asserted-by":"crossref","unstructured":"12. Navarrete FA, Garc\u00eda-V\u00e1zquez FA, Alvau A, Escoffier J, Krapf D, S\u00e1nchez-C\u00e1rdenas C, Salicioni AM, Darszon A, Visconti PE. Biphasic role of calcium in mouse sperm capacitation signaling pathways. <i>J Cell Physiol<\/i> 2015; 230: 1758\u20131769.","DOI":"10.1002\/jcp.24873"},{"key":"13","doi-asserted-by":"crossref","unstructured":"13. Ahmad K, Bracho GE, Wolf DP, Tash JS. Regulation of human sperm motility and hyperactivation components by calcium, calmodulin, and protein phosphatases. <i>Arch Androl<\/i> 1995; 35: 187\u2013208.","DOI":"10.3109\/01485019508987871"},{"key":"14","doi-asserted-by":"crossref","unstructured":"14. Lelkes PI, Miller IR. 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Merocyanine 540 as a probe to monitor the molecular packing of phosphatidylcholine: a monolayer epifluorescence microscopy and spectroscopy study. <i>Biochim Biophys Acta<\/i> 1992; 1107: 245\u2013254.","DOI":"10.1016\/0005-2736(92)90411-E"},{"key":"18","doi-asserted-by":"crossref","unstructured":"18. Harrison RA, Ashworth PJ, Miller NG. Bicarbonate\/CO<sub>2<\/sub>, an effector of capacitation, induces a rapid and reversible change in the lipid architecture of boar sperm plasma membranes. <i>Mol Reprod Dev<\/i> 1996; 45: 378\u2013391.","DOI":"10.1002\/(SICI)1098-2795(199611)45:3<378::AID-MRD16>3.0.CO;2-V"},{"key":"19","doi-asserted-by":"crossref","unstructured":"19. Pinart E, Yeste M, Puigmul\u00e9 M, Barrera X, Bonet S. 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