[1] DANTUMA N P, LINDSTEN K.Stressing the ubiquitin-proteasome system[J].Cardiovascular Research, 2010, 85(2):263-271. [2] SWATEK K N, KOMANDER D.Ubiquitin modifications[J].Cell Research, 2016, 26:399-422. [3] SUTOVSKY P.Sperm proteasome and fertilization[J].Reproduction, 2011, 142(1):1-14. [4] KERNS K, MORALES P, SUTOVSKY P.Regulation of sperm capacitation by the 26S proteasome:An emerging new paradigm in spermatology[J].Biology of Reproduction, 2016, 94(5):117. [5] VISCONTI P E, BAILEY J L, MOORE G D, et al.Capacitation of mouse spermatozoa.Ⅰ.Correlation between the capacitation state and protein tyrosine phosphorylation[J].Development, 1995, 121(4):1129-1137. [6] COHEN-KAPLAN V, LIVNEH I, AVNI N, et al.The ubiquitin-proteasome system and autophagy:Coordinated and independent activities[J].International Journal of Biochemistry, 2016, 79:403-418. [7] EKHLASI-HUNDRIESER M, GOHR K, WAGNER A, et al.Spermadhesin AQN1 is a candidate receptor molecule involved in the formation of the oviductal sperm reservoir in the pig[J].Biology of Reproduction, 2005, 73:536-545. [8] ZIMMERMAN S, SUTOVSKY P.The sperm proteasome during sperm capacitation and fertilization[J].Journal of Reproductive Immunology, 2009, 83(1-2):19-25. [9] AUSTIN C R.The capacitation of the mammalian sperm[J].Nature, 1952, 170(4321):326. [10] LEE J, YOU J, LEE G S, et al.Pig oocytes with a large perivitelline space matured in vitro show greater developmental competence after parthenogenesis and somatic cell nuclear transfer[J].Molecular Reproduction and Development, 2013, 80(9):753-762. [11] HYER M L, MILHOLLEN M A, CIAVARRI J, et al.A small-molecule inhibitor of the ubiquitin activating enzyme for cancer treatment[J].Nature Medicine, 2018, 24(2):186-193. [12] BASKA K M, MANANDHAR G, FENG D, et al.Mechanism of extracellular ubiquitination in the mammalian epididymis[J].Cell Physiology, 2008, 215(3):684-696. [13] KWON W S, RAHMAN M, LEE J S, et al.A comprehensive proteomic approach to identifying capacitation related proteins in boar spermatozoa[J].BMC Genomics, 2014, 15(1):897. [14] DUBE C, LECLERC P, BABA T, et al.The proacrosin binding protein, sp32, is tyrosine phosphorylated during capacitation of pig sperm[J].Andrology, 2005, 26(4):519-528. [15] BAKER M A, SMITH N D, HETHERINGTON L, et al.Label-free quantitation of phosphopeptide changes during rat sperm capacitation[J].Proteome Research, 2010, 9(2):718-729. [16] PLATT M D, SALICIONI A M, HUNT D F, et al.Use of differential isotopic labeling and mass spectrometry to analyze capacitation-associated changes in the phosphorylation status of mouse sperm proteins[J].Proteome Research, 2009, 8(3):1431-1440. [17] KIJMA K, KUBOTA K, HARA M, et al.The acute phase serum zinc concentration is a reliable biomarker for predicting the functional outcome after spinal cord injury[J].eBioMedicine, 2019, 41:659-669. [18] KERNS K, ZIGO M, DROBNIS E Z, et al.Zinc ion flux during mammalian sperm capacitation[J].Nature Communications, 2018, 9(1):2061. [19] QU J, ZOU T, LIN Z.The roles of the ubiquitin-proteasome system in the endoplasmic reticulum stress pathway[J].International Journal of Molecular Sciences, 2021, 22(4):1526. [20] YANG Y, KITAGAKI J, DAI R M, et al.Inhibitors of ubiquitin-activating enzyme (E1), a new class of potential cancer therapeutics[J].Cancer Research, 2007, 67(19):9472-9481. [21] DOSTALOVA Z, CALVETE J J, SANZ L, et al.Boar sperm adhesin AWN-1 ligosaccharide and zona pellucida binding characteristics[J].Biochemistry, 1995, 230(1):329-336. [22] JONAKOVA V, MANASKOVA P, KRAUS M, et al.Sperm surface proteins in mammalian fertilization[J].Molecular Reproduction and Development, 2000, 56(2):275-277. [23] DAVIDOVA N, JONAKOVA V, MANASKOVA-POSTLEROVA P.Expression and localization of acrosin inhibitor in boar reproductive tract[J].Cell Tissue Research, 2009, 338(2):303-311. [24] YI Y J, PARK C S, KIM E S, et al.Sperm-surface ATP in boar spermatozoa is required for fertilization:Relevance to sperm proteasomal function[J].Systems Biology Reproductive, 2009, 55:85-96. |