메뉴 건너뛰기




Volumn 9, Issue 7, 2012, Pages 365-375

Multifunctional glycoprotein DEFB126ĝ€"a curious story of defensin-clad spermatozoa

Author keywords

[No Author keywords available]

Indexed keywords

BETA DEFENSIN; GLYCOPROTEIN DEFB126; UNCLASSIFIED DRUG; DEFB126 PROTEIN, HUMAN; GLYCOPROTEIN;

EID: 84863716488     PISSN: 17594812     EISSN: 17594820     Source Type: Journal    
DOI: 10.1038/nrurol.2012.109     Document Type: Review
Times cited : (90)

References (108)
  • 1
    • 0037301078 scopus 로고    scopus 로고
    • Glycoconjugates in sperm function and gamete interactions: How much sugar does it take to sweet-talk the egg?
    • Diekman, A. B. Glycoconjugates in sperm function and gamete interactions: how much sugar does it take to sweet-talk the egg? Cell. Mol. Life. Sci. 60, 298-308 (2003).
    • (2003) Cell. Mol. Life. Sci. , vol.60 , pp. 298-308
    • Diekman, A.B.1
  • 3
    • 0037405822 scopus 로고    scopus 로고
    • Contribution of epididymal secretory proteins for spermatozoa maturation
    • Dacheux, J. L., Gatti, J. L. & Dacheux, F. Contribution of epididymal secretory proteins for spermatozoa maturation. Microsc. Res. Tech. 61, 7-17 (2003).
    • (2003) Microsc. Res. Tech. , vol.61 , pp. 7-17
    • Dacheux, J.L.1    Gatti, J.L.2    Dacheux, F.3
  • 4
    • 3543072975 scopus 로고    scopus 로고
    • Post-testicular sperm environment and fertility
    • Gatti, J. L. et al. Post-testicular sperm environment and fertility. Anim. Reprod. Sci. 83, 321-339 (2004).
    • (2004) Anim. Reprod. Sci. , vol.83 , pp. 321-339
    • Gatti, J.L.1
  • 5
    • 0141795538 scopus 로고    scopus 로고
    • ESP13.2, a member of the beta-defensin family, is a macaque sperm surface-coating protein involved in the capacitation process
    • Yudin, A. I. et al. ESP13.2, a member of the beta-defensin family, is a macaque sperm surface-coating protein involved in the capacitation process. Biol. Reprod. 69, 1118-1128 (2003).
    • (2003) Biol. Reprod. , vol.69 , pp. 1118-1128
    • Yudin, A.I.1
  • 6
    • 0032881431 scopus 로고    scopus 로고
    • The novel epididymal secretory protein ESP13.2 in Macaca fascicularis
    • Perry, A. C., Jones, R., Moisyadi, S., Coadwell, J. & Hall, L. The novel epididymal secretory protein ESP13.2 in Macaca fascicularis. Biol. Reprod. 61, 965-972 (1999).
    • (1999) Biol. Reprod. , vol.61 , pp. 965-972
    • Perry, A.C.1    Jones, R.2    Moisyadi, S.3    Coadwell, J.4    Hall, L.5
  • 7
    • 0037293097 scopus 로고    scopus 로고
    • Distribution of new human beta-defensin genes clustered on chromosome 20 in functionally different segments of epididymis
    • Rodriguez-Jimenez, F. J. et al. Distribution of new human beta-defensin genes clustered on chromosome 20 in functionally different segments of epididymis. Genomics 81, 175-183 (2003).
    • (2003) Genomics , vol.81 , pp. 175-183
    • Rodriguez-Jimenez, F.J.1
  • 8
    • 33947537879 scopus 로고    scopus 로고
    • The rat epididymal transcriptome: Comparison of segmental gene expression in the rat and mouse epididymides
    • Jelinsky, S. A. et al. The rat epididymal transcriptome: comparison of segmental gene expression in the rat and mouse epididymides. Biol. Reprod. 76, 561-570 (2007).
    • (2007) Biol. Reprod. , vol.76 , pp. 561-570
    • Jelinsky, S.A.1
  • 9
    • 33645469217 scopus 로고    scopus 로고
    • Cross-species analysis of the mammalian beta-defensin gene family: Presence of syntenic gene clusters and preferential expression in the male reproductive tract
    • Patil, A. A., Cai, Y., Sang, Y., Blecha, F. & Zhang, G. Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. Physiol. Genomics 23, 5-17 (2005).
    • (2005) Physiol. Genomics , vol.23 , pp. 5-17
    • Patil, A.A.1    Cai, Y.2    Sang, Y.3    Blecha, F.4    Zhang, G.5
  • 10
    • 58149287758 scopus 로고    scopus 로고
    • Beta-defensin 22 is a major component of the mouse sperm glyocalyx
    • Yudin, A. et al. Beta-defensin 22 is a major component of the mouse sperm glyocalyx. Reproduction 136, 753-765 (2008).
    • (2008) Reproduction , vol.136 , pp. 753-765
    • Yudin, A.1
  • 11
    • 33645116879 scopus 로고    scopus 로고
    • The carbohydrate structure of DEFB126, the major component of the cynomolgus Macaque sperm plasma membrane glycocalyx
    • Yudin, A. I., Treece, C. A., Tollner, T. L., Overstreet, J. W. & Cherr, G. N. The carbohydrate structure of DEFB126, the major component of the cynomolgus Macaque sperm plasma membrane glycocalyx. J. Membr. Biol. 207, 119-129 (2005).
    • (2005) J. Membr. Biol. , vol.207 , pp. 119-129
    • Yudin, A.I.1    Treece, C.A.2    Tollner, T.L.3    Overstreet, J.W.4    Cherr, G.N.5
  • 12
    • 79960691993 scopus 로고    scopus 로고
    • A common mutation in the defensin DEFB126 causes impaired sperm function and subfertility
    • Tollner, T. L. et al. A common mutation in the defensin DEFB126 causes impaired sperm function and subfertility. Sci. Transl. Med. 3, 92ra65 (2011).
    • (2011) Sci. Transl. Med. , vol.3
    • Tollner, T.L.1
  • 13
    • 0345601208 scopus 로고    scopus 로고
    • Secreted epididymal glycoprotein 2D6 that binds to the sperm's plasma membrane is a member of the beta-defensin superfamily of pore-forming glycopeptides
    • Zanich, A., Pascall, J. C. & Jones, R. Secreted epididymal glycoprotein 2D6 that binds to the sperm's plasma membrane is a member of the beta-defensin superfamily of pore-forming glycopeptides. Biol. Reprod. 69, 1831-1842 (2003).
    • (2003) Biol. Reprod. , vol.69 , pp. 1831-1842
    • Zanich, A.1    Pascall, J.C.2    Jones, R.3
  • 14
    • 28144446049 scopus 로고    scopus 로고
    • Beta-defensin 126 on the cell surface protects sperm from immunorecognition and binding of anti-sperm antibodies
    • Yudin, A. et al. Beta-defensin 126 on the cell surface protects sperm from immunorecognition and binding of anti-sperm antibodies. Biol. Reprod. 73, 1243-1252 (2005).
    • (2005) Biol. Reprod. , vol.73 , pp. 1243-1252
    • Yudin, A.1
  • 15
    • 4744352745 scopus 로고    scopus 로고
    • Macaque sperm release ESP13.2 and PSP94 during capacitation: The absence of ESP13.2 is linked to sperm-zona recognition and binding
    • Tollner, T. L., Yudin, A. I., Treece, C. A., Overstreet, J. O. & Cherr, G. N. Macaque sperm release ESP13.2 and PSP94 during capacitation: The absence of ESP13.2 is linked to sperm-zona recognition and binding. Mol. Reprod. Dev. 69, 325-337 (2004).
    • (2004) Mol. Reprod. Dev. , vol.69 , pp. 325-337
    • Tollner, T.L.1    Yudin, A.I.2    Treece, C.A.3    Overstreet, J.O.4    Cherr, G.N.5
  • 16
    • 40949120238 scopus 로고    scopus 로고
    • Beta-defensin 126 on the surface of macaque sperm mediates attachment of sperm to oviductal epithelia
    • Tollner, A. I. et al. Beta-defensin 126 on the surface of macaque sperm mediates attachment of sperm to oviductal epithelia. Biol. Reprod. 78, 400-412 (2008).
    • (2008) Biol. Reprod. , vol.78 , pp. 400-412
    • Tollner, A.I.1
  • 17
    • 0344953549 scopus 로고    scopus 로고
    • (ed. Hardy, D. M.) (Academic Press, San Diego).
    • Jaiswal, B. S. & Eisenbach, M. in Fertilization (ed. Hardy, D. M.) 57-117 (Academic Press, San Diego, 2002).
    • (2002) Fertilization , pp. 57-117
    • Jaiswal, B.S.1    Eisenbach, M.2
  • 18
    • 0004270728 scopus 로고
    • (eds Knobil, E. & Neill, J. D.) (Raven Press, New York).
    • Yanagimachi, R. in The Physiology of Reproduction (eds Knobil, E. & Neill, J. D.) 189-317 (Raven Press, New York, 1994).
    • (1994) The Physiology of Reproduction , pp. 189-317
    • Yanagimachi, R.1
  • 19
    • 84863723218 scopus 로고
    • (eds Asch, R. H., Balmaceda, J. P. & Johnston, I.) (Serona Symposia USA, Norwell).
    • Overstreet, J. W. & VandeVoort, C. A. in Gamete Physiology. (eds Asch, R. H., Balmaceda, J. P. & Johnston, I.) 43-52 (Serona Symposia USA, Norwell, 1990).
    • (1990) Gamete Physiology , pp. 43-52
    • Overstreet, J.W.1    Vandevoort, C.A.2
  • 20
    • 0020015889 scopus 로고
    • The mechanisms and analysis of sperm migration through cervical mucus
    • Katz, D. F. & Overstreet, J. W. The mechanisms and analysis of sperm migration through cervical mucus. Adv. Exp. Med. Biol. 144, 319-330 (1982).
    • (1982) Adv. Exp. Med. Biol. , vol.144 , pp. 319-330
    • Katz, D.F.1    Overstreet, J.W.2
  • 21
    • 0024395077 scopus 로고
    • Human cervical mucus and its interaction with sperm: A fine-structural view
    • Yudin, A. I., Hanson, F. W. & Katz, D. F. Human cervical mucus and its interaction with sperm: A fine-structural view. Biol. Reprod. 40, 661-671 (1989).
    • (1989) Biol. Reprod. , vol.40 , pp. 661-671
    • Yudin, A.I.1    Hanson, F.W.2    Katz, D.F.3
  • 22
    • 0034816264 scopus 로고    scopus 로고
    • Diffusion of macromolecules and virus-like particles in human cervical mucus
    • Olmsted, S. S. et al. Diffusion of macromolecules and virus-like particles in human cervical mucus. Biophys. J. 81, 1930-1937 (2001).
    • (2001) Biophys. J. , vol.81 , pp. 1930-1937
    • Olmsted, S.S.1
  • 23
    • 0042763868 scopus 로고    scopus 로고
    • Morphological characterization of different human cervical mucus types using light and scanning electron microscopy
    • Menarguez, M., Pastor, L. M. & Odeblad, E. Morphological characterization of different human cervical mucus types using light and scanning electron microscopy. Hum. Reprod. 18, 1782-1789 (2003).
    • (2003) Hum. Reprod. , vol.18 , pp. 1782-1789
    • Menarguez, M.1    Pastor, L.M.2    Odeblad, E.3
  • 24
    • 0038238582 scopus 로고    scopus 로고
    • Involvement of the glycoproteic meshwork of cervical mucus in the mechanism of sperm orientation
    • Chretien, F. C. Involvement of the glycoproteic meshwork of cervical mucus in the mechanism of sperm orientation. Acta Obstet. Gynecol. Scand. 82, 449-461 (2003).
    • (2003) Acta Obstet. Gynecol. Scand. , vol.82 , pp. 449-461
    • Chretien, F.C.1
  • 25
    • 0024360509 scopus 로고
    • Factors regulating mammalian sperm migration through the female reproductive tract and oocyte vestments
    • Katz, D. F., Drobnis, E. Z. & Overstreet, J. W. Factors regulating mammalian sperm migration through the female reproductive tract and oocyte vestments. Gamete Res. 22, 443-469 (1989).
    • (1989) Gamete Res. , vol.22 , pp. 443-469
    • Katz, D.F.1    Drobnis, E.Z.2    Overstreet, J.W.3
  • 26
    • 54149114938 scopus 로고    scopus 로고
    • Macaque sperm coating protein DEFB126 facilitates sperm penetration of cervical mucus
    • Tollner, T. L., Yudin, A. I., Treece, C. A., Overstreet, J. W. & Cherr, G. N. Macaque sperm coating protein DEFB126 facilitates sperm penetration of cervical mucus. Hum. Reprod. 23, 2523-2534 (2008).
    • (2008) Hum. Reprod. , vol.23 , pp. 2523-2534
    • Tollner, T.L.1    Yudin, A.I.2    Treece, C.A.3    Overstreet, J.W.4    Cherr, G.N.5
  • 27
    • 0023182947 scopus 로고
    • Structural studies of sialylated oligosaccharides of human midcycle cervical mucin
    • Yurewicz, E. C., Matsuura, F. & Moghissi, K. S. Structural studies of sialylated oligosaccharides of human midcycle cervical mucin. J. Biol. Chem. 262, 4733-4739 (1987).
    • (1987) J. Biol. Chem. , vol.262 , pp. 4733-4739
    • Yurewicz, E.C.1    Matsuura, F.2    Moghissi, K.S.3
  • 28
    • 0142200304 scopus 로고    scopus 로고
    • Role of sialic acid and sulfate groups in cervical mucus physiological functions: Study of Macaca radiata glycoproteins
    • Nasir-ud, D., Hoessli, D. C., Rungger-Brandle, E., Hussain, S. A. & Walker-Nasir, E. Role of sialic acid and sulfate groups in cervical mucus physiological functions: study of Macaca radiata glycoproteins. Biochim. Biophys. Acta 1623, 53-61 (2003).
    • (2003) Biochim. Biophys. Acta , vol.1623 , pp. 53-61
    • Nasir-Ud, D.1    Hoessli, D.C.2    Rungger-Brandle, E.3    Hussain, S.A.4    Walker-Nasir, E.5
  • 29
    • 0033024523 scopus 로고    scopus 로고
    • Characterization of immunoglobulins and cytokines in human cervical mucus: Influence of exogenous and endogenous hormones
    • Franklin, R. D. & Kutteh, W. H. Characterization of immunoglobulins and cytokines in human cervical mucus: influence of exogenous and endogenous hormones. J. Reprod. Immunol. 42, 93-106 (1999).
    • (1999) J. Reprod. Immunol. , vol.42 , pp. 93-106
    • Franklin, R.D.1    Kutteh, W.H.2
  • 30
    • 0031968159 scopus 로고    scopus 로고
    • Mucosal immunity in the female reproductive tract: Correlation of immunoglobulins, cytokines, and reproductive hormones in human cervical mucus around the time of ovulation
    • Kutteh, W. H., Moldoveanu, Z. & Mestecky, J. Mucosal immunity in the female reproductive tract: correlation of immunoglobulins, cytokines, and reproductive hormones in human cervical mucus around the time of ovulation. AIDS Res. Hum. Retroviruses 14 (Suppl. 1), S51-S55 (1998).
    • (1998) AIDS Res. Hum. Retroviruses , vol.14 , Issue.SUPPL. 1
    • Kutteh, W.H.1    Moldoveanu, Z.2    Mestecky, J.3
  • 31
    • 23344453110 scopus 로고    scopus 로고
    • Innate and adaptive immunity in female genital tract: Cellular responses and interactions
    • Wira, C. R., Fahey, J. V., Sentman, C. L., Pioli, P. A. & Shen, L. Innate and adaptive immunity in female genital tract: cellular responses and interactions. Immunol. Rev. 206, 306-335 (2005).
    • (2005) Immunol. Rev. , vol.206 , pp. 306-335
    • Wira, C.R.1    Fahey, J.V.2    Sentman, C.L.3    Pioli, P.A.4    Shen, L.5
  • 32
    • 0036095139 scopus 로고    scopus 로고
    • The age-related changes in the incidence of 'natural' anti-sperm antibodies suggest they are not auto-/isoantibodies
    • Kalaydjiev, S. K. et al. The age-related changes in the incidence of 'natural' anti-sperm antibodies suggest they are not auto-/isoantibodies. Am. J. Reprod. Immunol. 47, 65-71 (2002).
    • (2002) Am. J. Reprod. Immunol. , vol.47 , pp. 65-71
    • Kalaydjiev, S.K.1
  • 33
    • 0028290681 scopus 로고
    • Gamete immunology
    • Jones, W. R. Gamete immunology. Hum. Reprod. 9, 828-841 (1994).
    • (1994) Hum. Reprod. , vol.9 , pp. 828-841
    • Jones, W.R.1
  • 34
    • 0032035448 scopus 로고    scopus 로고
    • Sperm survival in the female reproductive tract: Presence of immunosuppression or absence of recognition?
    • Barratt, C. L. & Pockley, A. G. Sperm survival in the female reproductive tract: presence of immunosuppression or absence of recognition? Mol. Hum. Reprod. 4, 309-313 (1998).
    • (1998) Mol. Hum. Reprod. , vol.4 , pp. 309-313
    • Barratt, C.L.1    Pockley, A.G.2
  • 35
    • 0036297019 scopus 로고    scopus 로고
    • Formation of a reservoir of sperm in the oviduct
    • Suarez, S. S. Formation of a reservoir of sperm in the oviduct. Reprod. Domest. Anim. 37, 140-143 (2002).
    • (2002) Reprod. Domest. Anim. , vol.37 , pp. 140-143
    • Suarez, S.S.1
  • 36
    • 0023263428 scopus 로고
    • Pre-and peri-ovulatory distribution of viable spermatozoa in the pig oviduct: A scanning electron microscope study
    • Hunter, R. H., Flechon, B. & Flechon, J. E. Pre-and peri-ovulatory distribution of viable spermatozoa in the pig oviduct: A scanning electron microscope study. Tissue Cell 19, 423-436 (1987).
    • (1987) Tissue Cell , vol.19 , pp. 423-436
    • Hunter, R.H.1    Flechon, B.2    Flechon, J.E.3
  • 37
    • 0025813502 scopus 로고
    • Distribution, morphology and epithelial interactions of bovine spermatozoa in the oviduct before and after ovulation: A scanning electron microscope study
    • Hunter, R. H., Flechon, B. & Flechon, J. E. Distribution, morphology and epithelial interactions of bovine spermatozoa in the oviduct before and after ovulation: A scanning electron microscope study. Tissue Cell 23, 641-656 (1991).
    • (1991) Tissue Cell , vol.23 , pp. 641-656
    • Hunter, R.H.1    Flechon, B.2    Flechon, J.E.3
  • 38
    • 54249143638 scopus 로고    scopus 로고
    • Regulation of sperm storage and movement in the mammalian oviduct
    • Suarez, S. S. Regulation of sperm storage and movement in the mammalian oviduct. Int. J. Dev. Biol. 52, 455-462 (2008).
    • (2008) Int. J. Dev. Biol. , vol.52 , pp. 455-462
    • Suarez, S.S.1
  • 39
    • 78649598304 scopus 로고    scopus 로고
    • The oviduct as a complex mediator of mammalian sperm function and selection
    • Holt, W. V. & Fazeli, A. The oviduct as a complex mediator of mammalian sperm function and selection. Mol. Reprod. Dev. 77, 934-943 (2010).
    • (2010) Mol. Reprod. Dev. , vol.77 , pp. 934-943
    • Holt, W.V.1    Fazeli, A.2
  • 40
    • 0026752204 scopus 로고
    • Natural history of mammalian spermatozoa in the female reproductive tract
    • Drobnis, E. Z. & Overstreet, J. W. Natural history of mammalian spermatozoa in the female reproductive tract. Oxf. Rev. Reprod. Biol. 14, 1-45 (1992).
    • (1992) Oxf. Rev. Reprod. Biol. , vol.14 , pp. 1-45
    • Drobnis, E.Z.1    Overstreet, J.W.2
  • 41
    • 19944390602 scopus 로고    scopus 로고
    • Boar spermatozoa in the oviduct
    • Rodriguez-Martinez, H. et al. Boar spermatozoa in the oviduct. Theriogenology 63, 514-535 (2005).
    • (2005) Theriogenology , vol.63 , pp. 514-535
    • Rodriguez-Martinez, H.1
  • 42
    • 0346098209 scopus 로고    scopus 로고
    • Capacitation of mammalian spermatozoa in vivo, with a specific focus on events in the Fallopian tubes
    • Hunter, R. H. & Rodriguez-Martinez, H. Capacitation of mammalian spermatozoa in vivo, with a specific focus on events in the Fallopian tubes. Mol. Reprod. Dev. 67, 243-250 (2004).
    • (2004) Mol. Reprod. Dev. , vol.67 , pp. 243-250
    • Hunter, R.H.1    Rodriguez-Martinez, H.2
  • 43
    • 0023850630 scopus 로고
    • The formation and function of oviduct fluid
    • Leese, H. J. The formation and function of oviduct fluid. J. Reprod. Fertil. 82, 843-856 (1988).
    • (1988) J. Reprod. Fertil. , vol.82 , pp. 843-856
    • Leese, H.J.1
  • 44
    • 1542286240 scopus 로고    scopus 로고
    • Bovine sperm capacitation: Assessment of phosphodiesterase activity and intracellular alkalinization on capacitation-associated protein tyrosine phosphorylation
    • Galantino-Homer, H. L., Florman, H. M., Storey, B. T., Dobrinski, I. & Kopf, G. S. Bovine sperm capacitation: assessment of phosphodiesterase activity and intracellular alkalinization on capacitation-associated protein tyrosine phosphorylation. Mol. Reprod. Dev. 67, 487-500 (2004).
    • (2004) Mol. Reprod. Dev. , vol.67 , pp. 487-500
    • Galantino-Homer, H.L.1    Florman, H.M.2    Storey, B.T.3    Dobrinski, I.4    Kopf, G.S.5
  • 45
    • 0035077068 scopus 로고    scopus 로고
    • Formation of Fallopian tubal fluid: Role of a neglected epithelium
    • Leese, H. J., Tay, J. I., Reischl, J. & Downing, S. J. Formation of Fallopian tubal fluid: role of a neglected epithelium. Reproduction 121, 339-346 (2001).
    • (2001) Reproduction , vol.121 , pp. 339-346
    • Leese, H.J.1    Tay, J.I.2    Reischl, J.3    Downing, S.J.4
  • 46
    • 0030020930 scopus 로고    scopus 로고
    • Environment of the preimplantation human embryo in vivo: Metabolite analysis of oviduct and uterine fluids and metabolism of cumulus cells
    • Gardner, D. K., Lane, M., Calderon, I. & Leeton, J. Environment of the preimplantation human embryo in vivo: metabolite analysis of oviduct and uterine fluids and metabolism of cumulus cells. Fertil. Steril. 65, 349-353 (1996).
    • (1996) Fertil. Steril. , vol.65 , pp. 349-353
    • Gardner, D.K.1    Lane, M.2    Calderon, I.3    Leeton, J.4
  • 47
    • 0345426292 scopus 로고    scopus 로고
    • Ovarian follicular fluid, progesterone and Ca2+ ion influences on sperm release from the fallopian tube reservoir
    • Hunter, R. H., Petersen, H. H. & Greve, T. Ovarian follicular fluid, progesterone and Ca2+ ion influences on sperm release from the fallopian tube reservoir. Mol. Reprod. Dev. 54, 283-291 (1999).
    • (1999) Mol. Reprod. Dev. , vol.54 , pp. 283-291
    • Hunter, R.H.1    Petersen, H.H.2    Greve, T.3
  • 48
    • 0027934980 scopus 로고
    • Effect of macromolecules from oviductal conditioned medium on bovine sperm motion and capacitation
    • Anderson, S. H. & Killian, G. J. Effect of macromolecules from oviductal conditioned medium on bovine sperm motion and capacitation. Biol. Reprod. 51, 795-799 (1994).
    • (1994) Biol. Reprod. , vol.51 , pp. 795-799
    • Anderson, S.H.1    Killian, G.J.2
  • 49
    • 0033630830 scopus 로고    scopus 로고
    • Induction of dog sperm capacitation by glycosaminoglycans and glycosaminoglycan amounts of oviductal and uterine fluids in bitches
    • Kawakami, E., Arai, T., Oishi, I., Hori, T. & Tsutsu, T. Induction of dog sperm capacitation by glycosaminoglycans and glycosaminoglycan amounts of oviductal and uterine fluids in bitches. J. Vet. Med. Sci. 62, 65-68 (2000).
    • (2000) J. Vet. Med. Sci. , vol.62 , pp. 65-68
    • Kawakami, E.1    Arai, T.2    Oishi, I.3    Hori, T.4    Tsutsu, T.5
  • 50
    • 34547107589 scopus 로고    scopus 로고
    • Role of the oviduct in sperm capacitation
    • Rodriguez-Martinez, H. Role of the oviduct in sperm capacitation. Theriogenology 68 (Suppl. 1), S138-S146 (2007).
    • (2007) Theriogenology , vol.68 , Issue.SUPPL. 1
    • Rodriguez-Martinez, H.1
  • 51
    • 33947528213 scopus 로고    scopus 로고
    • Redox regulation of sperm surface thiols modulates adhesion to the fallopian tube epithelium
    • Talevi, R., Zagami, M., Castaldo, M. & Gualtieri, R. Redox regulation of sperm surface thiols modulates adhesion to the fallopian tube epithelium. Biol. Reprod. 76, 728-735 (2007).
    • (2007) Biol. Reprod. , vol.76 , pp. 728-735
    • Talevi, R.1    Zagami, M.2    Castaldo, M.3    Gualtieri, R.4
  • 52
    • 70449377242 scopus 로고    scopus 로고
    • Redox control of surface protein sulphhydryls in bovine spermatozoa reversibly modulates sperm adhesion to the oviductal epithelium and capacitation
    • Gualtieri, R., Mollo, V., Duma, G. & Talevi, R. Redox control of surface protein sulphhydryls in bovine spermatozoa reversibly modulates sperm adhesion to the oviductal epithelium and capacitation. Reproduction 138, 33-43 (2009).
    • (2009) Reproduction , vol.138 , pp. 33-43
    • Gualtieri, R.1    Mollo, V.2    Duma, G.3    Talevi, R.4
  • 53
    • 66749154693 scopus 로고    scopus 로고
    • Release of DEFB126 from macaque sperm and completion of capacitation are triggered by conditions that simulate periovulatory oviductal fluid
    • Tollner, T. et al. Release of DEFB126 from macaque sperm and completion of capacitation are triggered by conditions that simulate periovulatory oviductal fluid. Mol. Reprod. Dev. 76, 431-443 (2009).
    • (2009) Mol. Reprod. Dev. , vol.76 , pp. 431-443
    • Tollner, T.1
  • 54
    • 0017642776 scopus 로고
    • Hydrogen ion and carbon dioxide content of the oviductal fluid of the rhesus monkey (Macaca mulatta)
    • Maas, D. H., Storey, B. T. & Mastroianni, L. Jr. Hydrogen ion and carbon dioxide content of the oviductal fluid of the rhesus monkey (Macaca mulatta). Fertil. Steril. 28, 981-985 (1977).
    • (1977) Fertil. Steril. , vol.28 , pp. 981-985
    • Maas, D.H.1    Storey, B.T.2    Mastroianni Jr., L.3
  • 55
    • 0024828501 scopus 로고
    • Capacitation of bovine sperm by heparin: Inhibitory effect of glucose and role of intracellular pH
    • Parrish, J. J., Susko-Parrish, J. L. & First, N. L. Capacitation of bovine sperm by heparin: inhibitory effect of glucose and role of intracellular pH. Biol. Reprod. 41, 683-699 (1989).
    • (1989) Biol. Reprod. , vol.41 , pp. 683-699
    • Parrish, J.J.1    Susko-Parrish, J.L.2    First, N.L.3
  • 56
    • 0028935169 scopus 로고
    • Intracellular pH of bovine sperm increases during capacitation
    • Vredenburgh-Wilberg, W. L. & Parrish, J. J. Intracellular pH of bovine sperm increases during capacitation. Mol. Reprod. Dev. 40, 490-502 (1995).
    • (1995) Mol. Reprod. Dev. , vol.40 , pp. 490-502
    • Vredenburgh-Wilberg, W.L.1    Parrish, J.J.2
  • 57
    • 29144451321 scopus 로고    scopus 로고
    • Role of acid/base transporters in the male reproductive tract and potential consequences of their malfunction
    • Pastor-Soler, N., Piétrement, C. & Breton, S. Role of acid/base transporters in the male reproductive tract and potential consequences of their malfunction. Physiology 20, 417-428 (2005).
    • (2005) Physiology , vol.20 , pp. 417-428
    • Pastor-Soler, N.1    Piétrement, C.2    Breton, S.3
  • 59
    • 0019200297 scopus 로고
    • Concentrations of seven elements in the intraluminal fluids of the rat seminiferous tubules, rate testis, and epididymis
    • Jenkins, A. D., Lechene, C. P. & Howards, S. S. Concentrations of seven elements in the intraluminal fluids of the rat seminiferous tubules, rate testis, and epididymis. Biol. Reprod. 23, 981-987 (1980).
    • (1980) Biol. Reprod. , vol.23 , pp. 981-987
    • Jenkins, A.D.1    Lechene, C.P.2    Howards, S.S.3
  • 61
    • 29544450106 scopus 로고    scopus 로고
    • Sperm transport in the female reproductive tract
    • Suarez, S. S. & Pacey, A. A. Sperm transport in the female reproductive tract. Hum. Reprod. Update 12, 23-37 (2006).
    • (2006) Hum. Reprod. Update , vol.12 , pp. 23-37
    • Suarez, S.S.1    Pacey, A.A.2
  • 62
    • 0026493539 scopus 로고
    • Cation concentrations in fluid from the oviduct ampulla and isthmus of cows during the estrous cycle
    • Grippo, A. A., Henault, M. A., Anderson, S. H. & Killian, G. J. Cation concentrations in fluid from the oviduct ampulla and isthmus of cows during the estrous cycle. J. Dairy Sci. 75, 58-65 (1992).
    • (1992) J. Dairy Sci. , vol.75 , pp. 58-65
    • Grippo, A.A.1    Henault, M.A.2    Anderson, S.H.3    Killian, G.J.4
  • 63
    • 33645756342 scopus 로고    scopus 로고
    • Sperm guidance in mammals-An unpaved road to the egg
    • Eisenbach, M. & Giojalas, L. C. Sperm guidance in mammals-an unpaved road to the egg. Nat. Rev. Mol. Cell. Biol. 7, 276-285 (2006).
    • (2006) Nat. Rev. Mol. Cell. Biol. , vol.7 , pp. 276-285
    • Eisenbach, M.1    Giojalas, L.C.2
  • 64
    • 10844220712 scopus 로고    scopus 로고
    • Nonsense-mediated and nonstop decay of ribosomal protein S19 mRNA in Diamond-Blackfan anemia
    • Chatr-Aryamontri, A. et al. Nonsense-mediated and nonstop decay of ribosomal protein S19 mRNA in Diamond-Blackfan anemia. Hum. Mutat. 24, 526-533 (2004).
    • (2004) Hum. Mutat. , vol.24 , pp. 526-533
    • Chatr-Aryamontri, A.1
  • 65
    • 36949010143 scopus 로고    scopus 로고
    • Nonstop mutation in the factor (F)X gene of a severely haemorrhagic patient with complete absence of coagulation FX
    • Ameri, A. et al. Nonstop mutation in the factor (F)X gene of a severely haemorrhagic patient with complete absence of coagulation FX. Thromb. Haemost. 98, 1165-1169 (2007).
    • (2007) Thromb. Haemost. , vol.98 , pp. 1165-1169
    • Ameri, A.1
  • 66
    • 0037155592 scopus 로고    scopus 로고
    • An mRNA surveillance mechanism that eliminates transcripts lacking termination codons
    • Frischmeyer, P. A. et al. An mRNA surveillance mechanism that eliminates transcripts lacking termination codons. Science 295, 2258-2261 (2002).
    • (2002) Science , vol.295 , pp. 2258-2261
    • Frischmeyer, P.A.1
  • 67
    • 0037155579 scopus 로고    scopus 로고
    • Molecular biology. Skiing toward nonstop mRNA decay
    • Maquat, L. E. Molecular biology. Skiing toward nonstop mRNA decay. Science 295, 2221-2222 (2002).
    • (2002) Science , vol.295 , pp. 2221-2222
    • Maquat, L.E.1
  • 68
    • 34547623918 scopus 로고    scopus 로고
    • Quality control of eukaryotic mRNA: Safeguarding cells from abnormal mRNA function
    • Isken, O. & Maquat, L. E. Quality control of eukaryotic mRNA: safeguarding cells from abnormal mRNA function. Genes Dev. 21, 1833-1856 (2007).
    • (2007) Genes Dev. , vol.21 , pp. 1833-1856
    • Isken, O.1    Maquat, L.E.2
  • 69
    • 34247580913 scopus 로고    scopus 로고
    • Translation of nonSTOP mRNA is repressed post-initiation in mammalian cells
    • Akimitsu, N., Tanaka, J. & Pelletier, J. Translation of nonSTOP mRNA is repressed post-initiation in mammalian cells. EMBO J. 26, 2327-2338 (2007).
    • (2007) EMBO J. , vol.26 , pp. 2327-2338
    • Akimitsu, N.1    Tanaka, J.2    Pelletier, J.3
  • 71
    • 65749086514 scopus 로고    scopus 로고
    • Mammalian epididymal proteome
    • Dacheux, J. L. et al. Mammalian epididymal proteome. Mol. Cell Endocrinol. 306, 45-50 (2009).
    • (2009) Mol. Cell Endocrinol. , vol.306 , pp. 45-50
    • Dacheux, J.L.1
  • 72
    • 33745104040 scopus 로고    scopus 로고
    • Large-scale and high-confidence proteomic analysis of human seminal plasma
    • Pilch, B. & Mann, M. Large-scale and high-confidence proteomic analysis of human seminal plasma. Genome Biol. 7, R40 (2006).
    • (2006) Genome Biol. , vol.7
    • Pilch, B.1    Mann, M.2
  • 73
    • 18444403465 scopus 로고    scopus 로고
    • Identification, characterization, and evolution of a primate beta-defensin gene cluster
    • Radhakrishnan, Y. et al. Identification, characterization, and evolution of a primate beta-defensin gene cluster. Genes Immun. 6, 203-210 (2005).
    • (2005) Genes Immun. , vol.6 , pp. 203-210
    • Radhakrishnan, Y.1
  • 74
    • 62649085569 scopus 로고    scopus 로고
    • Defensin-like polypeptide LUREs are pollen tube attractants secreted from synergid cells
    • Okuda, S. H. et al. Defensin-like polypeptide LUREs are pollen tube attractants secreted from synergid cells. Nature 458, 357-361 (2009).
    • (2009) Nature , vol.458 , pp. 357-361
    • Okuda, S.H.1
  • 75
    • 57049185361 scopus 로고    scopus 로고
    • Expression of avian beta-defensin 3, an antimicrobial peptide, by sperm in the male reproductive organs and oviduct in chickens: An immunohistochemical study
    • Shimizu, M., Watanabe, Y., Isobe, N. & Yoshimura, Y. Expression of avian beta-defensin 3, an antimicrobial peptide, by sperm in the male reproductive organs and oviduct in chickens: an immunohistochemical study. Poult. Sci. 87, 2653-2659 (2008).
    • (2008) Poult. Sci. , vol.87 , pp. 2653-2659
    • Shimizu, M.1    Watanabe, Y.2    Isobe, N.3    Yoshimura, Y.4
  • 76
    • 78650920452 scopus 로고    scopus 로고
    • Antibacterial and antiviral roles of a fish beta-defensin expressed both in pituitary and testis
    • Jin, J. Y. et al. Antibacterial and antiviral roles of a fish beta-defensin expressed both in pituitary and testis. PLoS ONE 5, e12883 (2010).
    • (2010) PLoS ONE , vol.5
    • Jin, J.Y.1
  • 77
    • 68749119445 scopus 로고    scopus 로고
    • Soluble fusion expression and characterization of bioactive human beta-defensin 26 and 27
    • Huang, L., Leong, S. S. & Jiang, R. Soluble fusion expression and characterization of bioactive human beta-defensin 26 and 27. Appl. Microbiol. Biotechnol. 84, 301-308 (2009).
    • (2009) Appl. Microbiol. Biotechnol , vol.84 , pp. 301-308
    • Huang, L.1    Leong, S.S.2    Jiang, R.3
  • 78
    • 79952389475 scopus 로고    scopus 로고
    • Rat recombinant defensin 22 is a heparin-binding protein with antimicrobial activity
    • Diao, H., Yu, H. G., Sun, F., Zhang, Y. L. & Tanphaichitr, N. Rat recombinant defensin 22 is a heparin-binding protein with antimicrobial activity. Asian J. Androl. 13, 305-311 (2011).
    • (2011) Asian J. Androl. , vol.13 , pp. 305-311
    • Diao, H.1    Yu, H.G.2    Sun, F.3    Zhang, Y.L.4    Tanphaichitr, N.5
  • 80
    • 80052232241 scopus 로고    scopus 로고
    • Mechanisms of sperm storage in the female reproductive tract: An interspecies comparison
    • Holt, W. V. Mechanisms of sperm storage in the female reproductive tract: an interspecies comparison. Reprod. Domest. Anim. 46 (Suppl. 2), 68-74 (2011).
    • (2011) Reprod. Domest. Anim. , vol.46 , Issue.SUPPL. 2 , pp. 68-74
    • Holt, W.V.1
  • 81
    • 2142796392 scopus 로고    scopus 로고
    • Ultrastructure of the annual cycle of female sperm storage in spermathecae of the torrent Salamander, Rhyacotriton variegatus (Amphibia: Rhyacotritonidae)
    • Sever, D. M., Tait, C. K., Diller, L. V. & Burkholder, L. Ultrastructure of the annual cycle of female sperm storage in spermathecae of the torrent Salamander, Rhyacotriton variegatus (Amphibia: Rhyacotritonidae). J. Morphol. 261, 1-17 (2004).
    • (2004) J. Morphol. , vol.261 , pp. 1-17
    • Sever, D.M.1    Tait, C.K.2    Diller, L.V.3    Burkholder, L.4
  • 82
    • 79952200990 scopus 로고    scopus 로고
    • Reproductive histology of Tomeurus gracilis Eigenmann, 1909 (Teleostei: Atherinomorpha: Poeciliidae) with comments on evolution of viviparity in atherinomorph fishes
    • Parenti, L. R., LoNostro, F. L. & Grier, H. J. Reproductive histology of Tomeurus gracilis Eigenmann, 1909 (Teleostei: Atherinomorpha: Poeciliidae) with comments on evolution of viviparity in atherinomorph fishes. J. Morphol. 271, 1399-1406 (2010).
    • (2010) J. Morphol. , vol.271 , pp. 1399-1406
    • Parenti, L.R.1    Lonostro, F.L.2    Grier, H.J.3
  • 83
    • 34547534717 scopus 로고    scopus 로고
    • Spermathecae of the mangrove crab Ucides cordatus: A histological and histochemical view
    • Sant'Anna, B. S., Pinheiro, M. A. A., Mataqueiro, M. & Zara, F. J. Spermathecae of the mangrove crab Ucides cordatus: A histological and histochemical view. J. Mar. Biol. Assoc. UK 87, 903-911 (2007).
    • (2007) J. Mar. Biol. Assoc. UK , vol.87 , pp. 903-911
    • Sant'anna, B.S.1    Pinheiro, M.A.A.2    Mataqueiro, M.3    Zara, F.J.4
  • 84
    • 0031105559 scopus 로고    scopus 로고
    • Tokens of love: Functions and regulation of Drosophila male accessory gland products
    • Wolfner, M. F. Tokens of love: functions and regulation of Drosophila male accessory gland products. Insect Biochem. Molec. Biol. 27, 179-192 (1997).
    • (1997) Insect Biochem. Molec. Biol. , vol.27 , pp. 179-192
    • Wolfner, M.F.1
  • 85
    • 85047683172 scopus 로고    scopus 로고
    • The gifts that keep on giving: Physiological functions and evolutionary dynamics of male seminal proteins in Drosophila
    • Wolfner, M. F. The gifts that keep on giving: physiological functions and evolutionary dynamics of male seminal proteins in Drosophila. Heredity 88, 85-93 (2002).
    • (2002) Heredity , vol.88 , pp. 85-93
    • Wolfner, M.F.1
  • 87
    • 33947263854 scopus 로고    scopus 로고
    • Characterizing the glycocalyx of poultry spermatozoa: I. Identification and distribution of carbohydrate residues using flow cytometry and epifluorescence microscopy
    • Pelaez, J. & Long, J. A. Characterizing the glycocalyx of poultry spermatozoa: I. Identification and distribution of carbohydrate residues using flow cytometry and epifluorescence microscopy. J. Androl. 28, 342-352 (2007).
    • (2007) J. Androl. , vol.28 , pp. 342-352
    • Pelaez, J.1    Long, J.A.2
  • 88
    • 46449115553 scopus 로고    scopus 로고
    • Characterizing the glycocalyx of poultry spermatozoa: II. in vitro storage of turkey semen and mobility phenotype affects the carbohydrate component of sperm membrane glycoconjugates
    • Pelaez, J. & Long, J. A. Characterizing the glycocalyx of poultry spermatozoa: II. In vitro storage of turkey semen and mobility phenotype affects the carbohydrate component of sperm membrane glycoconjugates. J. Androl. 29, 431-439 (2008).
    • (2008) J. Androl. , vol.29 , pp. 431-439
    • Pelaez, J.1    Long, J.A.2
  • 89
    • 0030587693 scopus 로고    scopus 로고
    • Demonstration that the removal of sialic acid from the surface of chicken spermatozoa impedes their transvaginal migration
    • Steele, M. G. & Wishart, G. J. Demonstration that the removal of sialic acid from the surface of chicken spermatozoa impedes their transvaginal migration. Theriogenology 46, 1037-1044 (1996).
    • (1996) Theriogenology , vol.46 , pp. 1037-1044
    • Steele, M.G.1    Wishart, G.J.2
  • 90
    • 0024623451 scopus 로고
    • Alteration of the spermatozoal glycocalyx and its effect on duration of fertility in the fowl (Gallus domesticus)
    • Froman, D. P. & Engel, H. N. Jr. Alteration of the spermatozoal glycocalyx and its effect on duration of fertility in the fowl (Gallus domesticus). Biol. Reprod. 40, 615-621 (1989).
    • (1989) Biol. Reprod. , vol.40 , pp. 615-621
    • Froman, D.P.1    Engel Jr., H.N.2
  • 91
    • 0025178704 scopus 로고
    • Influence of neuraminidase on fertility and on sperm storage in the hen's oviduct
    • Howarth, B. Jr. Influence of neuraminidase on fertility and on sperm storage in the hen's oviduct. Poult. Sci. 69, 119-123 (1990).
    • (1990) Poult. Sci. , vol.69 , pp. 119-123
    • Howarth Jr., B.1
  • 92
    • 0021338946 scopus 로고
    • Biochemical characterization of a human spermatozoal sialoglycoprotein with respect to antigenicity masking by its sialic acid moieties
    • Czuppon, A. B. Biochemical characterization of a human spermatozoal sialoglycoprotein with respect to antigenicity masking by its sialic acid moieties. Biochem. Int. 8, 9-18 (1984).
    • (1984) Biochem. Int. , vol.8 , pp. 9-18
    • Czuppon, A.B.1
  • 93
    • 0024273088 scopus 로고
    • Masking of sperm maturation antigen by sialic acid in the epididymis of the mouse. An immunohistochemical study
    • Toshimori, K., Araki, S. & Oura, C. Masking of sperm maturation antigen by sialic acid in the epididymis of the mouse. An immunohistochemical study. Histochemistry 90, 195-200 (1988).
    • (1988) Histochemistry , vol.90 , pp. 195-200
    • Toshimori, K.1    Araki, S.2    Oura, C.3
  • 94
    • 84907134486 scopus 로고
    • Loss of sperm surface sialic acid induces phagocytosis: An assay with a monoclonal antibody T21, which recognizes a 54K sialoglycoprotein
    • Toshimori, K., Araki, S., Oura, C. & Eddy, E. M. Loss of sperm surface sialic acid induces phagocytosis: an assay with a monoclonal antibody T21, which recognizes a 54K sialoglycoprotein. Arch. Androl. 27, 79-86 (1991).
    • (1991) Arch. Androl. , vol.27 , pp. 79-86
    • Toshimori, K.1    Araki, S.2    Oura, C.3    Eddy, E.M.4
  • 95
    • 0026470856 scopus 로고
    • Masking the cryptodeterminant on the 54-kilodalton mouse sperm surface antigen
    • Toshimori, K., Araki, S., Tanii, I. & Oura, C. Masking the cryptodeterminant on the 54-kilodalton mouse sperm surface antigen. Biol. Reprod. 47, 1161-1167 (1992).
    • (1992) Biol. Reprod. , vol.47 , pp. 1161-1167
    • Toshimori, K.1    Araki, S.2    Tanii, I.3    Oura, C.4
  • 96
    • 3242778563 scopus 로고    scopus 로고
    • Defensins: Antimicrobial peptides of vertebrates
    • Ganz, T. Defensins: antimicrobial peptides of vertebrates. C R Biol. 327, 539-549 (2004).
    • (2004) C R Biol. , vol.327 , pp. 539-549
    • Ganz, T.1
  • 97
  • 98
    • 20644462344 scopus 로고    scopus 로고
    • Mammalian defensins in the antimicrobial immune response
    • Selsted, M. E. & Ouellette, A. J. Mammalian defensins in the antimicrobial immune response. Nat. Immunol. 6, 551-557 (2005).
    • (2005) Nat. Immunol. , vol.6 , pp. 551-557
    • Selsted, M.E.1    Ouellette, A.J.2
  • 99
    • 0037133295 scopus 로고    scopus 로고
    • Discovery of five conserved beta-defensin gene clusters using a computational search strategy
    • Schutte, B. C. et al. Discovery of five conserved beta-defensin gene clusters using a computational search strategy. Proc. Natl Acad. Sci. USA 99, 2129-2133 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 2129-2133
    • Schutte, B.C.1
  • 100
    • 0037235102 scopus 로고    scopus 로고
    • Expression of antimicrobial defensins in the male reproductive tract of rats, mice, and humans
    • Com, E. et al. Expression of antimicrobial defensins in the male reproductive tract of rats, mice, and humans. Biol. Reprod. 68, 95-104 (2003).
    • (2003) Biol. Reprod. , vol.68 , pp. 95-104
    • Com, E.1
  • 101
    • 77954697561 scopus 로고    scopus 로고
    • Defensin-like ZmES4 mediates pollen tube burst in maize via opening of the potassium channel KZM1
    • Amien, S. et al. Defensin-like ZmES4 mediates pollen tube burst in maize via opening of the potassium channel KZM1. PLoS Biol. 8, e1000388 (2010).
    • (2010) PLoS Biol. , vol.8
    • Amien, S.1
  • 102
    • 79959801439 scopus 로고    scopus 로고
    • Quantitative gene expression and in situ localization of scygonadin potentially associated with reproductive immunity in tissues of male and female mud crabs, Scylla paramamosain
    • Xu, W. F. et al. Quantitative gene expression and in situ localization of scygonadin potentially associated with reproductive immunity in tissues of male and female mud crabs, Scylla paramamosain. Fish Shellfish Immunol. 31, 243-251 (2011).
    • (2011) Fish Shellfish Immunol. , vol.31 , pp. 243-251
    • Xu, W.F.1
  • 103
    • 33845673334 scopus 로고    scopus 로고
    • Mating and immunity in invertebrates
    • Lawniczak, M. K. et al. Mating and immunity in invertebrates. Trends Ecol. Evol. 22, 48-55 (2007).
    • (2007) Trends Ecol. Evol. , vol.22 , pp. 48-55
    • Lawniczak, M.K.1
  • 105
    • 2342666235 scopus 로고    scopus 로고
    • An epididymis-specific beta-defensin is important for the initiation of sperm maturation
    • Zhou, C. X. et al. An epididymis-specific beta-defensin is important for the initiation of sperm maturation. Nat. Cell. Biol. 6, 458-464 (2004).
    • (2004) Nat. Cell. Biol. , vol.6 , pp. 458-464
    • Zhou, C.X.1
  • 106
    • 79951577288 scopus 로고    scopus 로고
    • The epididymis-specific antimicrobial peptide defensin 15 is required for sperm motility and male fertility in the rat (Rattus norvegicus)
    • Zhao, Y. et al. The epididymis-specific antimicrobial peptide defensin 15 is required for sperm motility and male fertility in the rat (Rattus norvegicus). Cell. Mol. Life Sci. 68, 697-708 (2011).
    • (2011) Cell. Mol. Life Sci. , vol.68 , pp. 697-708
    • Zhao, Y.1
  • 107
    • 1642545489 scopus 로고    scopus 로고
    • Anti-microbial peptides: From invertebrates to vertebrates
    • Bulet, P., Stöcklin, R. & Menin, L. Anti-microbial peptides: from invertebrates to vertebrates. Immunol. Rev. 198, 169-184 (2004).
    • (2004) Immunol. Rev. , vol.198 , pp. 169-184
    • Bulet, P.1    Stöcklin, R.2    Menin, L.3
  • 108
    • 0035044463 scopus 로고    scopus 로고
    • Drosophila males transfer antibacterial proteins from their accessory gland and ejaculatory duct to their mates
    • Lung, O., Kuo, L. & Wolfner, M. F. Drosophila males transfer antibacterial proteins from their accessory gland and ejaculatory duct to their mates. J. Insect Physiol. 47, 617-622 (2001).
    • (2001) J. Insect Physiol. , vol.47 , pp. 617-622
    • Lung, O.1    Kuo, L.2    Wolfner, M.F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.