1 |
You M, Yang Y, Zhong C, Chen F, Wang X, Jia T, et al. Efficient mAb production in CHO cells with optimized signal peptide, codon, and UTR. Appl Microbiol Biotechnol. 2018;102:5953-64. https://doi.org/10.1007/s00253-018-8986-5
DOI
|
2 |
Kim WD, Tokunaga M, Ozaki H, Ishibashi T, Honda K, Kajiura H, et al. Glycosylation pattern of humanized IgG-like bispecific antibody produced by recombinant CHO cells. Appl Microbiol Biotechnol. 2010;85:535-42. https://doi.org/10.1007/s00253-009-2152-z
DOI
|
3 |
Kim JY, Kim YG, Lee GM. CHO cells in biotechnology for production of recombinant proteins: current state and further potential. Appl Microbiol Biotechnol. 2012;93:917-30. https://doi.org/10.1007/s00253-011-3758-5
DOI
|
4 |
King GJ, Macpherson JW. A comparison of two methods for boar semen collection. J Anim Sci. 1973;36:563-5. https://doi.org/10.2527/jas1973.363563x
DOI
|
5 |
Brandriff BF, Gordon LA, Haendel S, Ashworth LK, Carrano AV. The chromosomal constitution of human sperm selected for motility. Fertil Steril. 1986;46:686-90. https://doi.org/10.1016/S0015-0282(16)49649-4
DOI
|
6 |
Visconti PE, Westbrook VA, Chertihin O, Demarco I, Sleight S, Diekman AB. Novel signaling pathways involved in sperm acquisition of fertilizing capacity. J Reprod Immunol. 2002;53:133-50. https://doi.org/10.1016/S0165-0378(01)00103-6
DOI
|
7 |
Abeydeera LR, Day BN. Fertilization and subsequent development in vitro of pig oocytes inseminated in a modified tris-buffered medium with frozen-thawed ejaculated spermatozoa. Biol Reprod. 1997;57:729-34. https://doi.org/10.1095/biolreprod57.4.729
DOI
|
8 |
Park HJ, Park JY, Kim JW, Yang SG, Jung JM, Kim MJ, et al. Melatonin improves the meiotic maturation of porcine oocytes by reducing endoplasmic reticulum stress during in vitro maturation. J Pineal Res. 2018;64:e12458. https://doi.org/10.1111/jpi.12458
DOI
|
9 |
Jin SK, Yang WX. Factors and pathways involved in capacitation: how are they regulated? Oncotarget. 2017;8:3600-27. https://doi.org/10.18632/oncotarget.12274
DOI
|
10 |
Okamura N, Tajima Y, Soejima A, Masuda H, Sugita Y. Sodium bicarbonate in seminal plasma stimulates the motility of mammalian spermatozoa through direct activation of adenylate cyclase. J Biol Chem. 1985;260:9699-705. https://doi.org/10.1016/S0021-9258(17)39295-5
DOI
|
11 |
Balbach M, Beckert V, Hansen JN, Wachten D. Shedding light on the role of cAMP in mammalian sperm physiology. Mol Cell Endocrinol. 2018;468:111-20. https://doi.org/10.1016/j.mce.2017.11.008
DOI
|
12 |
Monaco E, Gasparrini B, Boccia L, De Rosa A, Attanasio L, Zicarelli Let al. Effect of osteopontin (OPN) on in vitro embryo development in cattle. Theriogenology. 2009;71:450-7. https://doi.org/10.1016/j.theriogenology.2008.08.012
DOI
|
13 |
Matas C, Vieira L, Garcia-Vazquez FA, Aviles-Lopez K, Lopez-Ubeda R, Carvajal JA, et al. Effects of centrifugation through three different discontinuous Percoll gradients on boar sperm function. Anim Reprod Sci. 2011;127:62-72. https://doi.org/10.1016/j.anireprosci.2011.06.009
DOI
|
14 |
Gervasi MG, Visconti PE. Chang's meaning of capacitation: a molecular perspective. Mol Reprod Dev. 2016;83:860-74. https://doi.org/10.1002/mrd.22663
DOI
|
15 |
Michos I, Tsantarliotou M, Boscos CM, Tsousis G, Basioura A, Tzika ED, et al. Effect of boar sperm proteins and quality changes on field fertility. Animals. 2021;11:1813. https://doi.org/10.3390/ani11061813
DOI
|
16 |
Lv J, Wang S, Zeng C, Huang Y, Chen X. Construction of a shuttle expression vector with a promoter functioning in both halophilic archaea and bacteria. FEMS Microbiol Lett. 2013;349:9-15. https://doi.org/10.1111/1574-6968.12278
DOI
|
17 |
Elmi A, Banchelli F, Barone F, Fantinati P, Ventrella D, Forni M, et al. Semen evaluation and in vivo fertility in a Northern Italian pig farm: can advanced statistical approaches compensate for low sample size? An observational study. Anim Reprod Sci. 2018;192:61-8. https://doi.org/10.1016/j.anireprosci.2018.02.014
DOI
|
18 |
Gil MA, Cuello C, Parrilla I, Vazquez JM, Roca J, Martinez EA. Advances in swine in vitro embryo production technologies. Reprod Domest Anim. 2010;45:40-8. https://doi.org/10.1111/j.1439-0531.2010.01623.x
DOI
|
19 |
Goncalves RF, Wolinetz CD, Killian GJ. Influence of arginine-glycine-aspartic acid (RGD), integrins (αV and α5) and osteopontin on bovine sperm-egg binding, and fertilization in vitro. Theriogenology. 2007;67:468-74. https://doi.org/10.1016/j.theriogenology.2006.08.013
DOI
|
20 |
Hao Y, Mathialagan N, Walters E, Mao J, Lai L, Becker D, et al. Osteopontin reduces polyspermy during in vitro fertilization of porcine oocytes. Biol Reprod. 2006;75:726-33. https://doi.org/10.1095/biolreprod.106.052589
DOI
|
21 |
Kober L, Zehe C, Bode J. Optimized signal peptides for the development of high expressing CHO cell lines. Biotechnol Bioeng. 2013;110:1164-73. https://doi.org/10.1002/bit.24776
DOI
|
22 |
Ohlweiler LU, Mezzalira JC, Mezzalira A. Porcine IVF embryo development and estrogen receptors are influenced by the concentration of percoll gradients during sperm selection. Mol Reprod Dev. 2020;87:135-41. https://doi.org/10.1002/mrd.23290
DOI
|
23 |
Knox RV. Impact of swine reproductive technologies on pig and global food production. Adv Exp Med Biol. 2014;752:131-60. https://doi.org/10.1007/978-1-4614-8887-3_7
DOI
|
24 |
Leno-Colorado J, Hudson NJ, Reverter A, Perez-Enciso M. A pathway-centered analysis of pig domestication and breeding in Eurasia. G3 (Bethesda). 2017;7:2171-84. https://doi.org/10.1534/g3.117.042671
DOI
|
25 |
Dinnyes A, Liu J, Nedambale TL. Novel gamete storage. Reprod Fertil Dev. 2007;19:719-31. https://doi.org/10.1071/RD07035
DOI
|
26 |
Boccia L, Di Francesco S, Neglia G, De Blasi M, Longobardi V, Campanile G, et al. Osteopontin improves sperm capacitation and in vitro fertilization efficiency in buffalo (Bubalus bubalis). Theriogenology. 2013;80:212-7. https://doi.org/10.1016/j.theriogenology.2013.04.017
DOI
|
27 |
Lin C, Tholen E, Jennen D, Ponsuksili S, Schellander K, Wimmers K. Evidence for effects of testis and epididymis expressed genes on sperm quality and boar fertility traits. Reprod Domest Anim. 2006;41:538-43. https://doi.org/10.1111/j.1439-0531.2006.00710.x
DOI
|
28 |
Hao Y, Murphy CN, Spate L, Wax D, Zhong Z, Samuel M, et al. Osteopontin improves in vitro development of porcine embryos and decreases apoptosis. Mol Reprod Dev. 2008;75:291-8. https://doi.org/10.1002/mrd.20794
DOI
|
29 |
Signorelli J, Diaz ES, Morales P. Kinases, phosphatases and proteases during sperm capacitation. Cell Tissue Res. 2012;349:765-82. https://doi.org/10.1007/s00441-012-1370-3
DOI
|
30 |
Moura AA, Koc H, Chapman DA, Killian GJ. Identification of proteins in the accessory sex gland fluid associated with fertility indexes of dairy bulls: a proteomic approach. J Androl. 2006;27:201-11. https://doi.org/10.2164/jandrol.05089
DOI
|
31 |
Park CH, Lee SG, Choi DH, Lee CK. A modified swim-up method reduces polyspermy during in vitro fertilization of porcine oocytes. Anim Reprod Sci. 2009;115:169-81. https://doi.org/10.1016/j.anireprosci.2008.12.004
DOI
|
32 |
Wrana JL, Zhang Q, Sodek J. Full length cDNA sequence of porcine secreted phosphoprotein-I (SPP-I, osteopontin). Nucleic Acids Res. 1989;17:10119. https://doi.org/10.1093/nar/17.23.10119
DOI
|
33 |
Li X, Wang L, Li Y, Zhao N, Zhen L, Fu J, et al. Calcium regulates motility and protein phosphorylation by changing cAMP and ATP concentrations in boar sperm in vitro. Anim Reprod Sci. 2016;172:39-51. https://doi.org/10.1016/j.anireprosci.2016.07.001
DOI
|
34 |
Okamura N, Sugita Y. Activation of spermatozoan adenylate cyclase by a low molecular weight factor in porcine seminal plasma. J Biol Chem. 1983;258:13056-62. https://doi.org/10.1016/S0021-9258(17)44079-8
DOI
|