메뉴 건너뛰기




Volumn 74, Issue , 2012, Pages 477-502

Sperm-egg interaction

Author keywords

CD9; Cell adhesion; Cell cell fusion; Fertilization; IZUMO; Tetraspanin

Indexed keywords

ADAM PROTEIN; ALPHA6 INTEGRIN; CD9 ANTIGEN; CELL ADHESION MOLECULE; FERTILIN; GLYCOSYLPHOSPHATIDYLINOSITOL ANCHORED PROTEIN; INTEGRIN; MEMBRANE PROTEIN; NERVE CELL ADHESION MOLECULE; PROTEIN; PROTEIN DISULFIDE ISOMERASE; PROTEIN IZUMO1; TETRASPANIN; UNCLASSIFIED DRUG; UVOMORULIN;

EID: 84857342577     PISSN: 00664278     EISSN: 15451585     Source Type: Book Series    
DOI: 10.1146/annurev-physiol-020911-153339     Document Type: Article
Times cited : (70)

References (162)
  • 1
    • 1542440248 scopus 로고    scopus 로고
    • Muscle differentiation: Signalling cell fusion
    • Taylor MV. 2003. Muscle differentiation: signalling cell fusion. Curr. Biol. 13:R964-66
    • (2003) Curr. Biol. , vol.13
    • Taylor, M.V.1
  • 2
    • 17244370591 scopus 로고    scopus 로고
    • Unveiling the mechanisms of cell-cell fusion
    • DOI 10.1126/science.1104799
    • Chen EH, Olson EN. 2005. Unveiling the mechanisms of cell-cell fusion. Science 308:369-73 (Pubitemid 40530066)
    • (2005) Science , vol.308 , Issue.5720 , pp. 369-373
    • Chen, E.H.1    Olson, E.N.2
  • 3
    • 33644816187 scopus 로고    scopus 로고
    • Role of tethering factors in secretory membrane traffic
    • Sztul E, Lupashin V. 2006. Role of tethering factors in secretory membrane traffic. Am. J. Physiol. Cell Physiol. 290:11-26
    • (2006) Am. J. Physiol. Cell Physiol. , vol.290 , pp. 11-26
    • Sztul, E.1    Lupashin, V.2
  • 4
    • 79960937293 scopus 로고    scopus 로고
    • Molecular and cellular mechanisms of mammalian cell fusion
    • Zhou X, Platt JL. 2011. Molecular and cellular mechanisms of mammalian cell fusion. Adv. Exp. Med. Biol. 713:33-64
    • (2011) Adv. Exp. Med. Biol. , vol.713 , pp. 33-64
    • Zhou, X.1    Platt, J.L.2
  • 5
    • 0015405275 scopus 로고
    • Early contact interactions between mammalian gametes in vitro: Evidence that the vitellus influences adherence between sperm and zona pellucida
    • Hartmann JF, Gwatkin RBL, Hutchinson CF. 1972. Early contact interactions between mammalian gametes in vitro: evidence that the vitellus influences adherence between sperm and zona pellucida. Proc. Natl. Acad. Sci. USA 69:2767-69
    • (1972) Proc. Natl. Acad. Sci. USA , vol.69 , pp. 2767-69
    • Hartmann, J.F.1    Gwatkin, R.B.L.2    Hutchinson, C.F.3
  • 6
    • 0032781044 scopus 로고    scopus 로고
    • An improved mouse sperm-oocyte plasmalemma binding assay: Studies on characteristics of sperm binding in medium with or without glucose
    • Redkar AA, Olds-Clarke PJ. 1999. An improved mouse sperm-oocyte plasmalemma binding assay: studies on characteristics of sperm binding in medium with or without glucose. J. Androl. 20:500-8 (Pubitemid 29362634)
    • (1999) Journal of Andrology , vol.20 , Issue.4 , pp. 500-508
    • Redkar, A.A.1    Olds-Clarke, P.J.2
  • 7
    • 33750629399 scopus 로고    scopus 로고
    • Analysis of mammalian sperm-egg membrane interactions during in vitro fertilization
    • Wortzman GB, Gardner AJ, Evans JP. 2006. Analysis of mammalian sperm-egg membrane interactions during in vitro fertilization. Methods Mol. Biol. 341:89-101
    • (2006) Methods Mol. Biol. , vol.341 , pp. 89-101
    • Wortzman, G.B.1    Gardner, A.J.2    Evans, J.P.3
  • 8
    • 0023834422 scopus 로고
    • Pre-loading of mouse oocytes with DNA-specific fluorochrome (Hoechst 33342) permits rapid detection of sperm-oocyte fusion
    • Conover JC, Gwatkin RBL. 1988. Pre-loading of mouse oocytes with DNA-specific fluorochrome (Hoechst 33342) permits rapid detection of sperm oocyte-fusion. J. Reprod. Fertil. 82:681-90 (Pubitemid 18083035)
    • (1988) Journal of Reproduction and Fertility , vol.82 , Issue.2 , pp. 681-690
    • Conover, J.C.1    Gwatkin, R.B.L.2
  • 10
    • 65249141091 scopus 로고    scopus 로고
    • Reduction of mouse egg surface integrinα9 subunit (ITGA9) reduces the eggs ability to support sperm-egg binding and fusion
    • Vjugina U, Zhu X, Oh E, Bracero NJ, Evans JP. 2009. Reduction of mouse egg surface integrinα9 subunit (ITGA9) reduces the eggs ability to support sperm-egg binding and fusion. Biol. Reprod. 80:833-41
    • (2009) Biol. Reprod. , vol.80 , pp. 833-41
    • Vjugina, U.1    Zhu, X.2    Oh, E.3    Bracero, N.J.4    Evans, J.P.5
  • 11
    • 59849083832 scopus 로고    scopus 로고
    • IgSF8 (EWI-2) and CD9 in fertilization: Evidence of distinct functions for CD9 and aCD9-associated protein inmammalian sperm-egg interaction
    • Glazar AI, Evans JP. 2009. IgSF8 (EWI-2) and CD9 in fertilization: evidence of distinct functions for CD9 and aCD9-associated protein inmammalian sperm-egg interaction. Reprod. Fertil. Dev. 21:293-303
    • (2009) Reprod. Fertil. Dev. , vol.21 , pp. 293-303
    • Glazar, A.I.1    Evans, J.P.2
  • 13
    • 77958032520 scopus 로고    scopus 로고
    • Mechanisms of sperm-egg interactions: Between sugars and broken bonds
    • Visconti PE, Florman HM. 2010. Mechanisms of sperm-egg interactions: between sugars and broken bonds. Sci. Signal. 3:pe35
    • (2010) Sci. Signal , vol.3
    • Visconti, P.E.1    Florman, H.M.2
  • 15
    • 0022349031 scopus 로고
    • Inner acrosomal membrane of mammalian spermatozoa: Its properties and possible functions in fertilization
    • DOI 10.1002/aja.1001740307
    • Huang TT Jr, Yanagimachi R. 1985. Inner acrosomal membrane of mammalian spermatozoa: its properties and possible functions in fertilization. Am. J. Anat. 174:249-68 (Pubitemid 16204127)
    • (1985) American Journal of Anatomy , vol.174 , Issue.3 , pp. 249-268
    • Huang Jr., T.T.F.1    Yanagimachi, R.2
  • 17
    • 0002302562 scopus 로고
    • Mammalian fertilization
    • ed. E Knobil, JD Neill New York: Raven
    • Yanagimachi R. 1994. Mammalian fertilization. In The Physiology of Reproduction, ed. E Knobil, JD Neill, pp. 189-317. New York: Raven
    • (1994) The Physiology of Reproduction , pp. 189-317
    • Yanagimachi, R.1
  • 19
    • 0033555056 scopus 로고    scopus 로고
    • Sperm disintegrins, egg integrins, and other cell adhesion molecules of mammalian gamete plasma membrane interactions
    • Evans JP. 1999. Sperm disintegrins, egg integrins, and other cell adhesion molecules of mammalian gamete plasma membrane interactions. Front. Biosci. 4:D114-31
    • (1999) Front. Biosci. , vol.4
    • Evans, J.P.1
  • 20
    • 38449103840 scopus 로고    scopus 로고
    • New insights into the molecular basis of mammalian sperm-egg membrane interactions
    • DOI 10.2741/2693
    • Vjugina U, Evans JP. 2008. New insights into the molecular basis of mammalian sperm-egg membrane interactions. Front. Biosci. 13:462-76 (Pubitemid 351599758)
    • (2008) Frontiers in Bioscience , vol.13 , Issue.2 , pp. 462-476
    • Vjugina, U.1    Evans, J.P.2
  • 21
    • 0020554887 scopus 로고
    • A map of the guinea pig sperm surface constructed with monoclonal antibodies
    • Primakoff P, Myles DG. 1983. A map of the guinea pig sperm surface constructed with monoclonal antibodies. Dev. Biol. 98:417-28 (Pubitemid 13078035)
    • (1983) Developmental Biology , vol.98 , Issue.2 , pp. 417-428
    • Primakoff, P.1    Myles, D.G.2
  • 22
    • 0028955151 scopus 로고
    • Monoclonal antibodies which recognize equatorial segment epitops de novo following the A23187-induced acrosome reaction of guinea pig sperm
    • Allen CA, Green DP. 1995. Monoclonal antibodies which recognize equatorial segment epitops de novo following the A23187-induced acrosome reaction of guinea pig sperm. J. Cell Sci. 108:767-77
    • (1995) J. Cell Sci. , vol.108 , pp. 767-77
    • Allen, C.A.1    Green, D.P.2
  • 23
    • 0031777110 scopus 로고    scopus 로고
    • An MN9 antigenic molecule, equatorin, is required for successful sperm- oocyte fusion in mice
    • DOI 10.1095/biolreprod59.1.22
    • Toshimori K, Saxena DK, Tanii I, Yoshinaga K. 1998. AnMN9antigenic molecule, equatorin, is required for successful sperm-oocyte fusion in mice. Biol. Reprod. 59:22-29 (Pubitemid 28304349)
    • (1998) Biology of Reproduction , vol.59 , Issue.1 , pp. 22-29
    • Toshimori, K.1    Saxena, D.K.2    Tanii, I.3    Yoshinaga, K.4
  • 24
    • 0023801763 scopus 로고
    • Effect of a monoclonal antimouse sperm antibody (OBF13) on the interaction of mouse sperm with zona-free mouse and hamster eggs
    • Okabe M, Yagasaki M, Oda H, Matzno S, Kohama Y, Mimura T. 1988. Effect of a monoclonal antimouse sperm antibody (OBF13) on the interaction of mouse sperm with zona-free mouse and hamster eggs. J. Reprod. Immunol. 13:211-19
    • (1988) J. Reprod. Immunol. , vol.13 , pp. 211-19
    • Okabe, M.1    Yagasaki, M.2    Oda, H.3    Matzno, S.4    Kohama, Y.5    Mimura, T.6
  • 25
    • 0023100910 scopus 로고
    • Identification and purification of a sperm surface protein with a potential role in sperm-egg membrane fusion
    • DOI 10.1083/jcb.104.1.141
    • Primakoff P, Hyatt H, Tredick-Kline J. 1987. Identification and purification of a sperm surface protein with a potential role in sperm-egg membrane fusion. J. Cell Biol. 104:141-49 (Pubitemid 17018665)
    • (1987) Journal of Cell Biology , vol.104 , Issue.1 , pp. 141-149
    • Primakoff, P.1    Hyatt, H.2    Tredick-Kline, J.3
  • 28
    • 33646863600 scopus 로고    scopus 로고
    • Proteomic analysis of sperm regions that mediate sperm-egg interactions
    • DOI 10.1002/pmic.200500845
    • Stein KK, Go JC, Lane WS, Primakoff P, Myles DG. 2006. Proteomic analysis of sperm regions that mediate sperm-egg interactions. Proteomics 6:3533-43 (Pubitemid 44000183)
    • (2006) Proteomics , vol.6 , Issue.12 , pp. 3533-3543
    • Stein, K.K.1    Go, J.C.2    Lane, W.S.3    Primakoff, P.4    Myles, D.G.5
  • 29
    • 43449097896 scopus 로고    scopus 로고
    • Equatorial Segment Protein (ESP) is a human alloantigen involved in sperm-egg binding and fusion
    • DOI 10.2164/jandrol.106.000604
    • Wolkowicz MJ, Digilio L, Klotz K, Shetty J, Flickinger CJ, Herr JC. 2008. Equatorial Segment Protein (ESP) is a human alloantigen involved in sperm-egg binding and fusion. J. Androl. 29:272-82 (Pubitemid 351669017)
    • (2008) Journal of Andrology , vol.29 , Issue.3 , pp. 272-282
    • Wolkowicz, M.J.1    Digilio, L.2    Klotz, K.3    Shetty, J.4    Flickinger, C.J.5    Herr, J.C.6
  • 30
    • 79952822805 scopus 로고    scopus 로고
    • Characterization of mouse sperm TMEM190, a small transmembrane protein with the trefoil domain: Evidence for co-localization with IZUMO1 and complex formation with other sperm proteins
    • Nishimura H, Gupta S, Myles DG, Primakoff P. 2011. Characterization of mouse sperm TMEM190, a small transmembrane protein with the trefoil domain: evidence for co-localization with IZUMO1 and complex formation with other sperm proteins. Reproduction 141:437-51
    • (2011) Reproduction , vol.141 , pp. 437-51
    • Nishimura, H.1    Gupta, S.2    Myles, D.G.3    Primakoff, P.4
  • 33
    • 23244434065 scopus 로고    scopus 로고
    • Mouse SLLP1, a sperm lysozyme-like protein involved in sperm-egg binding and fertilization
    • DOI 10.1016/j.ydbio.2005.05.008, PII S0012160605003003
    • Herrero MB, Mandal A, Digilio LC, Coonrod SA, Maier B, Herr JC. 2005. Mouse SLLP1, a sperm lysozyme-like protein involved in sperm-egg binding and fertilization. Dev. Biol. 284:126-42 (Pubitemid 41096729)
    • (2005) Developmental Biology , vol.284 , Issue.1 , pp. 126-142
    • Herrero, M.B.1    Mandal, A.2    Digilio, L.C.3    Coonrod, S.A.4    Maier, B.5    Herr, J.C.6
  • 35
    • 0038508866 scopus 로고    scopus 로고
    • The Chlamydomonas Fus1 protein is present on the mating type plus fusion organelle and required for a critical membrane adhesion event during fusion with minus gametes
    • DOI 10.1091/mbc.E02-12-0790
    • Misamore MJ, Gupta S, Snell WJ. 2003. The Chlamydomonas Fus1 protein is present on the mating type plus fusion organelle and required for a critical membrane adhesion event during fusion with minus gametes. Mol. Biol. Cell 14:2530-42 (Pubitemid 36724340)
    • (2003) Molecular Biology of the Cell , vol.14 , Issue.6 , pp. 2530-2542
    • Misamore, M.J.1    Gupta, S.2    Snell, W.J.3
  • 36
    • 77951245390 scopus 로고    scopus 로고
    • Membrane fusion triggers a rapid degradation of two gametespecific fusion-essential proteins in a membrane block to polygamy in Chlamydomonas
    • Liu Y, Misamore MJ, Snell WJ. 2010. Membrane fusion triggers a rapid degradation of two gametespecific fusion-essential proteins in a membrane block to polygamy in Chlamydomonas. Development 137:1473-81
    • (2010) Development , vol.137 , pp. 1473-81
    • Liu, Y.1    Misamore, M.J.2    Snell, W.J.3
  • 37
    • 54249101333 scopus 로고    scopus 로고
    • Genes required for the common miracle of fertilization in Caenorhabditis elegans
    • Singson A, Hang JS, Parry JM. 2008. Genes required for the common miracle of fertilization in Caenorhabditis elegans. Int. J. Dev. Biol. 52:647-56
    • (2008) Int. J. Dev. Biol. , vol.52 , pp. 647-56
    • Singson, A.1    Hang, J.S.2    Parry, J.M.3
  • 38
    • 0026510747 scopus 로고
    • A potential fusion peptide and an integrin ligand domain in a protein active in sperm-egg fusion
    • Blobel CP, Wolfsberg TG, Turck CW, Myles DG, Primakoff P, White JM. 1992. A potential fusion peptide and an integrin ligand domain in a protein active in sperm-egg fusion. Nature 356:248-52
    • (1992) Nature , vol.356 , pp. 248-52
    • Blobel, C.P.1    Wolfsberg, T.G.2    Turck, C.W.3    Myles, D.G.4    Primakoff, P.5    White, J.M.6
  • 39
    • 29044433212 scopus 로고    scopus 로고
    • The egg surface LDL receptor repeat-containing proteins EGG-1 and EGG-2 are required for fertilization in Caenorhabditis elegans
    • DOI 10.1016/j.cub.2005.10.043, PII S0960982205012960
    • Kanandale P, Stewart-Michaelis A, Gordon S, Rubin J, Klancer R, et al. 2005. The egg surface LDL receptor repeat-containing proteins EGG-1 and EGG-2 are required for fertilization in Caenorhabditis elegans. Curr. Biol. 15:2222-29 (Pubitemid 41790615)
    • (2005) Current Biology , vol.15 , Issue.24 , pp. 2222-2229
    • Kadandale, P.1    Stewart-Michaelis, A.2    Gordon, S.3    Rubin, J.4    Klancer, R.5    Schweinsberg, P.6    Grant, B.D.7    Singson, A.8
  • 42
    • 0033964768 scopus 로고    scopus 로고
    • Severely reduced female fertility in CD9-deficient mice
    • DOI 10.1126/science.287.5451.319
    • Le Naour F, Rubinstein E, Jasmin C, Prenant M, Boucheix C. 2000. Severely reduced female fertility in CD9-deficient mice. Science 287:319-21 (Pubitemid 30046762)
    • (2000) Science , vol.287 , Issue.5451 , pp. 319-321
    • Boucheix, C.1
  • 46
    • 0023186231 scopus 로고
    • Capacitation-related changes in antigen distribution on mouse sperm heads and its relation to fertilization rate in vitro
    • DOI 10.1016/0165-0378(87)90014-3
    • Okabe M, Adachi T, Takada K, Oda H, Yagasaki M, et al. 1987. Capacitation-related changes in antigen distribution on mouse sperm heads and its relation to fertilization rate in vitro. J. Reprod. Immunol. 11:91-100 (Pubitemid 17100877)
    • (1987) Journal of Reproductive Immunology , vol.11 , Issue.2 , pp. 91-100
    • Okabe, M.1    Adachi, T.2    Takada, K.3
  • 47
    • 15044362481 scopus 로고    scopus 로고
    • The immunoglobulin superfamily protein Izumo is required for sperm to fuse with eggs
    • DOI 10.1038/nature03362
    • Inoue N, Ikawa M, Isotani A, Okabe M. 2005. The immunoglobulin superfamily protein Izumo is required for sperm to fuse with eggs. Nature 434:234-38 (Pubitemid 40388056)
    • (2005) Nature , vol.434 , Issue.7030 , pp. 234-238
    • Inoue, N.1    Ikawa, M.2    Isotani, A.3    Okabe, M.4
  • 48
    • 34347252299 scopus 로고    scopus 로고
    • Positive expression of the immunoglobulin superfamily protein IZUMO on human sperm of severely infertile male patients
    • DOI 10.1016/j.fertnstert.2006.11.086, PII S001502820604550X
    • Hayasaka S, Terada Y, Inoue N, Okabe M, Yaegashi N, Okamura K. 2007. Positive expression of the immunoglobulin superfamily protein IZUMOon human sperm of severely infertile male patients. Fertil. Steril. 88:214-16 (Pubitemid 47001375)
    • (2007) Fertility and Sterility , vol.88 , Issue.1 , pp. 214-216
    • Hayasaka, S.1    Terada, Y.2    Inoue, N.3    Okabe, M.4    Yaegashi, N.5    Okamura, K.6
  • 50
    • 0035479922 scopus 로고    scopus 로고
    • Immunoglobulin superfamily receptors: Cis-interactions, intracellular adapters and alternative splicing regulate adhesion
    • DOI 10.1016/S0955-0674(00)00259-3
    • Brummendorf T, Lemmon V. 2001. Immunoglobulin superfamily receptors: cis-interactions, intracellular adapters and alternative splicing regulate adhesion. Curr. Opin. Cell Biol. 13:611-18 (Pubitemid 32817021)
    • (2001) Current Opinion in Cell Biology , vol.13 , Issue.5 , pp. 611-618
    • Brummendorf, T.1    Lemmon, V.2
  • 51
    • 56049120533 scopus 로고    scopus 로고
    • Putative sperm fusion protein IZUMO and the role of Nglycosylation
    • Inoue N, Ikawa M, Okabe M. 2008. Putative sperm fusion protein IZUMO and the role of Nglycosylation. Biochem. Biophys. Res. Commun. 377:910-14
    • (2008) Biochem. Biophys. Res. Commun. , vol.377 , pp. 910-14
    • Inoue, N.1    Ikawa, M.2    Okabe, M.3
  • 52
    • 77956401827 scopus 로고    scopus 로고
    • Identification and disruption of sperm-specific angiotensin converting enzyme-3 (ACE3) in mouse
    • Inoue N, Kasahara T, Ikawa M, Okabe M. 2010. Identification and disruption of sperm-specific angiotensin converting enzyme-3 (ACE3) in mouse. PLoS ONE 5:e10301
    • (2010) PLoS ONE , vol.5
    • Inoue, N.1    Kasahara, T.2    Ikawa, M.3    Okabe, M.4
  • 55
    • 70350441635 scopus 로고    scopus 로고
    • Izumo is part of a multiprotein family whose members form large complexes on mammalian sperm
    • Ellerman DA, Pei J, Gupta S, Snell WJ, Myles DG, Primakoff P. 2009. Izumo is part of a multiprotein family whose members form large complexes on mammalian sperm. Mol. Reprod. Dev. 76:1188-99
    • (2009) Mol. Reprod. Dev. , vol.76 , pp. 1188-99
    • Ellerman, D.A.1    Pei, J.2    Gupta, S.3    Snell, W.J.4    Myles, D.G.5    Primakoff, P.6
  • 59
    • 78149486376 scopus 로고    scopus 로고
    • ADAM2 interactions with mouse eggs and cell lines expressing α4/α9 (ITGA4/ITGA9) integrins: Implications for integrin-based adhesion and fertilization
    • Desiderio UV, Zhu X, Evans JP. 2010. ADAM2 interactions with mouse eggs and cell lines expressing α4/α9 (ITGA4/ITGA9) integrins: implications for integrin-based adhesion and fertilization. PLoS ONE 5:e13744
    • (2010) PLoS ONE , vol.5
    • Desiderio, U.V.1    Zhu, X.2    Evans, J.P.3
  • 62
    • 0035337709 scopus 로고    scopus 로고
    • Analysis of loss of adhesive function in sperm lacking cyritestin or fertilin β
    • DOI 10.1006/dbio.2001.0166
    • Nishimura H, Cho C, Branciforte DR, Myles DG, Primakoff P. 2001. Analysis of loss of adhesive function in sperm lacking cyritestin or fertilin β. Dev. Biol. 233:204-13 (Pubitemid 32411305)
    • (2001) Developmental Biology , vol.233 , Issue.1 , pp. 204-213
    • Nishimura, H.1    Cho, C.2    Branciforte, D.R.3    Myles, D.G.4    Primakoff, P.5
  • 63
    • 4544250782 scopus 로고    scopus 로고
    • Possible function of the ADAM1a/ADAM2 fertilin complex in the appearance of ADAM3 on the sperm surface
    • DOI 10.1074/jbc.M314249200
    • Nishimura H, Kim E, Nakanishi T, Baba T. 2004. Possible function of the ADAM1a/ADAM2 fertilin complex in the appearance of ADAM3 on the sperm surface. J. Biol. Chem. 279:34957-62 (Pubitemid 39318132)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.33 , pp. 34957-34962
    • Nishimura, H.1    Kim, E.2    Nakanishi, T.3    Baba, T.4
  • 65
    • 33645061771 scopus 로고    scopus 로고
    • Expression and relationship of male reproductive ADAMs in mouse
    • Kim T, Oh J, Woo JM, Choi E, Im SH, et al. 2006. Expression and relationship of male reproductive ADAMs in mouse. Biol. Reprod. 74:744-50
    • (2006) Biol. Reprod. , vol.74 , pp. 744-50
    • Kim, T.1    Oh, J.2    Woo, J.M.3    Choi, E.4    Im, S.H.5
  • 66
    • 65749101619 scopus 로고    scopus 로고
    • Comprehensive analysis of reproductive ADAMs: Relationship of ADAM4 and ADAM6 with an ADAM complex required for fertilization in mice
    • Han C, Choi E, Park I, Lee B, Jin S, et al. 2009. Comprehensive analysis of reproductive ADAMs: relationship of ADAM4 and ADAM6 with an ADAM complex required for fertilization in mice. Biol. Reprod. 80:1001-8
    • (2009) Biol. Reprod. , vol.80 , pp. 1001-8
    • Han, C.1    Choi, E.2    Park, I.3    Lee, B.4    Jin, S.5
  • 68
    • 79953901981 scopus 로고    scopus 로고
    • Lack of tyrosylprotein sulfotransferase-2 activity results in altered sperm-egg interactions and loss of ADAM3 and ADAM6 in epididymal sperm
    • Marcello MR, Jia W, Leary JA, Moore KL, Evans JP. 2011. Lack of tyrosylprotein sulfotransferase-2 activity results in altered sperm-egg interactions and loss of ADAM3 and ADAM6 in epididymal sperm. J. Biol. Chem. 286:13060-70
    • (2011) J. Biol. Chem. , vol.286 , pp. 13060-70
    • Marcello, M.R.1    Jia, W.2    Leary, J.A.3    Moore, K.L.4    Evans, J.P.5
  • 69
    • 33750845874 scopus 로고    scopus 로고
    • Aberrant distribution of ADAM3 in sperm from both angiotensin-converting enzyme (Ace)- and calmegin (Clgn)-deficient mice
    • DOI 10.1095/biolreprod.106.052977
    • Yamaguchi R, Yamagata K, Ikawa M, Moss SB, Okabe M. 2006. Aberrant distribution of ADAM3 in sperm from both Angiotensin-converting enzyme (Ace)- and Calmegin (Clgn)-deficient mice. Biol. Reprod. 75:760-66 (Pubitemid 44720396)
    • (2006) Biology of Reproduction , vol.75 , Issue.5 , pp. 760-766
    • Yamaguchi, R.1    Yamagata, K.2    Ikawa, M.3    Moss, S.B.4    Okabe, M.5
  • 70
    • 79953135154 scopus 로고    scopus 로고
    • Calsperin is a testis specific chaperone required for sperm fertility
    • Ikawa M, Tokuhiro K, Yamaguchi R, Benham AM, Tamura T, et al. 2011. Calsperin is a testis specific chaperone required for sperm fertility. J. Biol. Chem. 286:5639-46
    • (2011) J. Biol. Chem. , vol.286 , pp. 5639-46
    • Ikawa, M.1    Tokuhiro, K.2    Yamaguchi, R.3    Benham, A.M.4    Tamura, T.5
  • 72
    • 0032528978 scopus 로고    scopus 로고
    • The gene for the human tMDC I sperm surface protein is non-functional: Implications for its proposed role in mammalian sperm-egg recognition
    • Frayne J, Hall L. 1998. The gene for the human tMDC I sperm surface protein is non-functional: implications for its proposed role in mammalian sperm-egg recognition. Biochem. J. 334:171-76 (Pubitemid 28420986)
    • (1998) Biochemical Journal , vol.334 , Issue.1 , pp. 171-176
    • Frayne, J.1    Hall, L.2
  • 74
    • 77951751489 scopus 로고    scopus 로고
    • Sperm equatorial segment protein 1, SPESP1, is required for fully fertile sperm in the mouse
    • Fujihara Y, Murakami M, Inoue N, Satouh Y, Kaseda K, et al. 2010. Sperm equatorial segment protein 1, SPESP1, is required for fully fertile sperm in the mouse. J. Cell Sci. 123:1531-36
    • (2010) J. Cell Sci. , vol.123 , pp. 1531-36
    • Fujihara, Y.1    Murakami, M.2    Inoue, N.3    Satouh, Y.4    Kaseda, K.5
  • 75
    • 28444441957 scopus 로고    scopus 로고
    • Tetraspanin functions and associated microdomains
    • DOI 10.1038/nrm1736
    • Hemler ME. 2005. Tetraspanin functions and associated microdomains. Nat. Rev. Mol. Cell Biol. 6:801-11 (Pubitemid 41726118)
    • (2005) Nature Reviews Molecular Cell Biology , vol.6 , Issue.10 , pp. 801-811
    • Hemler, M.E.1
  • 76
    • 79953201597 scopus 로고    scopus 로고
    • The complexity of tetraspanins
    • Rubinstein E. 2011. The complexity of tetraspanins. Biochem. Soc. Trans. 39:501-5
    • (2011) Biochem. Soc. Trans. , vol.39 , pp. 501-5
    • Rubinstein, E.1
  • 77
    • 0036302083 scopus 로고    scopus 로고
    • Infertility of CD9-deficient mouse eggs is reversed by mouse CD9, human CD9, or mouse CD81; polyadenylated mRNA injection developed for molecular analysis of sperm-egg fusion
    • DOI 10.1006/dbio.2002.0694
    • Kaji K, Oda S, Miyazaki S, Kudo A. 2002. Infertility of CD9-deficient mouse eggs is reversed by mouse CD9, human CD9, or mouse CD81; polyadenylated mRNA injection developed for molecular analysis of sperm-egg fusion. Dev. Biol. 247:327-34 (Pubitemid 34734868)
    • (2002) Developmental Biology , vol.247 , Issue.2 , pp. 327-334
    • Kaji, K.1    Oda, S.2    Miyazaki, S.3    Kudo, A.4
  • 78
    • 33644977667 scopus 로고    scopus 로고
    • CD9 controls the formation of clusters that contain tetraspanins and the integrin α6β1, which are involved in human and mouse gamete fusion
    • Ziyyat A, Rubinstein E, Monier-Gavelle F, Barraud V, Kulski O, et al. 2006. CD9 controls the formation of clusters that contain tetraspanins and the integrin α6β1, which are involved in human and mouse gamete fusion. J. Cell Sci. 119:416-24
    • (2006) J. Cell Sci. , vol.119 , pp. 416-24
    • Ziyyat, A.1    Rubinstein, E.2    Monier-Gavelle, F.3    Barraud, V.4    Kulski, O.5
  • 80
    • 1542300715 scopus 로고    scopus 로고
    • Localization of CD9 in pig oocytes and its effects on sperm-egg interaction
    • Li YH, Hou Y, Ma W, Yuan JX, Zhang D, et al. 2004. Localization of CD9 in pig oocytes and its effects on sperm-egg interaction. Reproduction 127:151-57 (Pubitemid 38312785)
    • (2004) Reproduction , vol.127 , Issue.2 , pp. 151-157
    • Li, Y.-H.1    Hou, Y.2    Ma, W.3    Yuan, J.-X.4    Zhang, D.5    Sun, Q.-Y.6    Wang, W.-H.7
  • 82
    • 33846895645 scopus 로고    scopus 로고
    • Deletion of tetraspanin Cd151 results in decreased pathologic angiogenesis in vivo and in vitro
    • DOI 10.1182/blood-2006-08-041970
    • Takeda Y, Kazarov AR, Butterfield CE, Hopkins BD, Benjamin LE, et al. 2007. Deletion of tetraspanin Cd151 results in decreased pathologic angiogenesis in vivo and in vitro. Blood 109:1524-32 (Pubitemid 46239585)
    • (2007) Blood , vol.109 , Issue.4 , pp. 1524-1532
    • Takeda, Y.1    Kazarov, A.R.2    Butterfield, C.E.3    Hopkins, B.D.4    Benjamin, L.E.5    Kaipainen, A.6    Hemler, M.E.7
  • 84
    • 4944239350 scopus 로고    scopus 로고
    • CD151, the first member of the tetraspanin (TM4) superfamily detected on erythrocytes, is essential for the correct assembly of human basement membranes in kidney and skin
    • DOI 10.1182/blood-2004-04-1512
    • Karamatic Crew V, Burton N, Kagan A, Green CA, Levene C, et al. 2004. CD151, the first member of the tetraspanin (TM4) superfamily detected on erythrocytes, is essential for the correct assembly of human basement membranes in kidney and skin. Blood 104:2217-23 (Pubitemid 39331816)
    • (2004) Blood , vol.104 , Issue.8 , pp. 2217-2223
    • Crew, V.K.1    Burton, N.2    Kagan, A.3    Green, C.A.4    Levene, C.5    Flinter, F.6    Brady, R.L.7    Daniels, G.8    Anstee, D.J.9
  • 86
    • 15744394653 scopus 로고    scopus 로고
    • A novel tetraspanin fusion protein, peripherin-2, requires a region upstream of the fusion domain for activity
    • DOI 10.1074/jbc.M407166200
    • Damek-Poprawa M, Krouse J, Gretzula C, Boesze-Battaglia K. 2005. A novel tetraspanin fusion protein, peripherin-2, requires a region upstream of the fusion domain for activity. J. Biol. Chem. 280:9217-24 (Pubitemid 40409612)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.10 , pp. 9217-9224
    • Damek-Poprawa, M.1    Krouse, J.2    Gretzula, C.3    Boesze-Battaglia, K.4
  • 89
    • 77955033375 scopus 로고    scopus 로고
    • Greasing their way: Lipid modifications determine protein association with membrane rafts
    • Levantal I, Grzybek M, Simons K. 2010. Greasing their way: Lipid modifications determine protein association with membrane rafts. Biochemistry 49:6305-16
    • (2010) Biochemistry , vol.49 , pp. 6305-16
    • Levantal, I.1    Grzybek, M.2    Simons, K.3
  • 91
    • 67949097489 scopus 로고    scopus 로고
    • Exosomes-vesicular carriers for intercellular communication
    • Simons M, Raposo G. 2009. Exosomes-vesicular carriers for intercellular communication. Curr. Opin. Cell Biol. 21:575-81
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 575-81
    • Simons, M.1    Raposo, G.2
  • 92
    • 35948959380 scopus 로고    scopus 로고
    • Transfer of oocyte membrane fragments to fertilizing spermatozoa
    • DOI 10.1096/fj.06-8035hyp
    • Barraud-Lange V, Naud-Barriant N, Bomsel M, Wolf JP, Ziyyat A. 2007. Transfer of oocyte membrane fragments to fertilizing spermatozoa. FASEB J. 21:3446-49 (Pubitemid 350075169)
    • (2007) FASEB Journal , vol.21 , Issue.13 , pp. 3446-3449
    • Barraud-Lange, V.1    Naud-Barriant, N.2    Bomsel, M.3    Wolf, J.-P.4    Ziyyat, A.5
  • 93
    • 51349153446 scopus 로고    scopus 로고
    • The fusing ability of sperm is bestowed by CD9-containing vesicles released from eggs in mice
    • Miyado K, Yoshida K, Yamagata K, Sakakibara K, Okabe M, et al. 2008. The fusing ability of sperm is bestowed by CD9-containing vesicles released from eggs in mice. Proc. Natl. Acad. Sci. USA105:12921-26
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 12921-26
    • Miyado, K.1    Yoshida, K.2    Yamagata, K.3    Sakakibara, K.4    Okabe, M.5
  • 94
    • 67449085966 scopus 로고    scopus 로고
    • Can the presence of wild-type oocytes during insemination rescue the fusion defect of CD9 null oocytes? Mol
    • Gupta S, Primakoff P, Myles DG. 2009. Can the presence of wild-type oocytes during insemination rescue the fusion defect of CD9 null oocytes? Mol. Reprod. Dev. 76:602
    • (2009) Reprod. Dev. , vol.76 , pp. 602
    • Gupta, S.1    Primakoff, P.2    Myles, D.G.3
  • 95
    • 79960628083 scopus 로고    scopus 로고
    • CD9 tetraspanin generates fusion competent sites on the egg membrane formammalian fertilization
    • Jégou A, Ziyyat A, Barraud-Lange V, Perez E, Wolf JP, et al. 2011. CD9 tetraspanin generates fusion competent sites on the egg membrane formammalian fertilization. Proc. Natl. Acad. Sci. USA 108:10946-51
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 10946-51
    • Jégou, A.1    Ziyyat, A.2    Barraud-Lange, V.3    Perez, E.4    Wolf, J.P.5
  • 96
    • 0036197618 scopus 로고    scopus 로고
    • 6 integrins, and CD9 in the interaction of the fertilin β (ADAM2) disintegrin domain with the mouse egg membrane
    • Zhu X, Evans JP. 2002. Analysis of the roles of RGD-binding integrins, α4/α9 integrins, α6 integrins, andCD9 in the interaction of the fertilinβ(ADAM2) disintegrin domain with themouse egg membrane. Biol. Reprod. 66:1193-202 (Pubitemid 34263139)
    • (2002) Biology of Reproduction , vol.66 , Issue.4 , pp. 1193-1202
    • Zhu, X.1    Evans, J.P.2
  • 97
    • 2342653563 scopus 로고    scopus 로고
    • q/11 Association
    • DOI 10.1091/mbc.E03-12-0886
    • Little KD, Hemler ME, Stipp CS. 2004. Dynamic regulation of a GPCR-tetraspanin-G protein complex on intact cells: central role of CD81 in facilitatingGPR56-Gαq/11 association. Mol. Biol. Cell 15:2375-87 (Pubitemid 38580653)
    • (2004) Molecular Biology of the Cell , vol.15 , Issue.5 , pp. 2375-2387
    • Little, K.D.1    Hemler, M.E.2    Stipp, C.S.3
  • 98
    • 36749037222 scopus 로고    scopus 로고
    • A novel cysteine cross-linking method reveals a direct association between claudin-1 and tetraspanin CD9
    • DOI 10.1074/mcp.M700183-MCP200
    • Kovalenko OV, Yang XH, Hemler ME. 2007. A novel cysteine cross-linking method reveals a direct association between claudin-1 and tetraspanin CD9. Mol. Cell Proteomics 6:1855-67 (Pubitemid 350213866)
    • (2007) Molecular and Cellular Proteomics , vol.6 , Issue.11 , pp. 1855-1867
    • Kovalenko, O.V.1    Yang, X.H.2    Hemler, M.E.3
  • 100
    • 0035798537 scopus 로고    scopus 로고
    • EWI-2 is a major CD9 and CD81 partner and member of a novel Ig protein subfamily
    • Stipp CS, Kolesnikova TV, Hemler ME. 2001. EWI-2 is a major CD9 and CD81 partner and member of a novel Ig protein subfamily. J. Biol. Chem. 276:40545-54
    • (2001) J. Biol. Chem. , vol.276 , pp. 40545-54
    • Stipp, C.S.1    Kolesnikova, T.V.2    Hemler, M.E.3
  • 101
    • 0035895876 scopus 로고    scopus 로고
    • FPRP, a major, highly stoichiometric, highly specific CD81- and CD9-associated protein
    • Stipp CS, Orlicky D, Hemler ME. 2001. FPRP, a major, highly stoichiometric, highly specific CD81- and CD9-associated protein. J. Biol. Chem. 276:4853-62
    • (2001) J. Biol. Chem. , vol.276 , pp. 4853-62
    • Stipp, C.S.1    Orlicky, D.2    Hemler, M.E.3
  • 103
    • 0035958026 scopus 로고    scopus 로고
    • Themajor CD9 and CD81 molecular partner: Identification and characterization of the complexes
    • Charrin S, LeNaour F, Oualid M, Billard M, Faure G, et al. 2001. Themajor CD9 and CD81 molecular partner: identification and characterization of the complexes. J. Biol. Chem. 276:14329-37
    • (2001) J. Biol. Chem. , vol.276 , pp. 14329-37
    • Charrin, S.1    Lenaour, F.2    Oualid, M.3    Billard, M.4    Faure, G.5
  • 104
    • 0033559614 scopus 로고    scopus 로고
    • Treatment of mouse oocytes with PI-PLC releases 70-kDa (pI 5) and 35- to 45-kDa (pI 5.5) Protein clusters from the egg surface and inhibits sperm- oolemma binding and fusion
    • DOI 10.1006/dbio.1998.9161
    • Coonrod SA, Naaby-Hansen S, Shetty J, Shibahara H, Chen M, et al. 1999. Treatment ofmouse oocytes with PI-PLC releases 70-kDa (pI 5) and 35- to 45-kDa (pI 5. 5) protein clusters from the egg surface and inhibits sperm-oolemma binding and fusion. Dev. Biol. 207:334-49 (Pubitemid 29136348)
    • (1999) Developmental Biology , vol.207 , Issue.2 , pp. 334-349
    • Coonrod, S.A.1    Naaby-Hansen, S.2    Shetty, J.3    Shibahara, H.4    Chen, M.5    White, J.M.6    Herr, J.C.7
  • 105
    • 0033972925 scopus 로고    scopus 로고
    • Characterisation of the enzymatic complex for the first step in glycosylphosphatidylinositol biosynthesis
    • DOI 10.1016/S1357-2725(99)00122-3, PII S1357272599001223
    • Tiede A, Nischan C, Schubert J, Schmidt RE. 2000. Characterisation of the enzymatic complex for the first step in glycosylphosphatidylinositol biosynthesis. Int. J. Biochem. Cell Biol. 32:339-50 (Pubitemid 30069976)
    • (2000) International Journal of Biochemistry and Cell Biology , vol.32 , Issue.3 , pp. 339-350
    • Tiede, A.1    Nischan, C.2    Schubert, J.3    Schmidt, R.E.4
  • 106
    • 0038687068 scopus 로고    scopus 로고
    • Infertility in female mice with an oocyte-specific knockout of GPI-anchored protreins
    • DOI 10.1242/jcs.00430
    • Alfieri JA, Martin AD, Takeda J, Kondoh G, Myles DG, Primakoff P. 2003. Infertility in female mice with an oocyte-specific knockout of GPI-anchored proteins. J. Cell Sci. 116:2149-55 (Pubitemid 36722361)
    • (2003) Journal of Cell Science , vol.116 , Issue.11 , pp. 2149-2155
    • Alfieri, J.A.1    Martin, A.D.2    Takeda, J.3    Kondoh, G.4    Myles, D.G.5    Primakoff, P.6
  • 107
    • 0037442567 scopus 로고    scopus 로고
    • None of the integrins known to be present on the mouse egg or to be ADAM receptors are essential for sperm-egg binding and fusion
    • DOI 10.1016/S0012-1606(02)00043-X
    • He Z-Y, Brakebusch C, Fassler R, Kreidberg JA, Primakoff P, Myles DG. 2003. None of the integrins known to be present on the mouse egg or to be ADAM receptors are essential for sperm-egg binding and fusion. Dev. Biol. 254:226-37 (Pubitemid 36268993)
    • (2003) Developmental Biology , vol.254 , Issue.2 , pp. 226-237
    • He, Z.-Y.1    Brakebusch, C.2    Fassler, R.3    Kreidberg, J.A.4    Primakoff, P.5    Myles, D.G.6
  • 108
    • 0034640885 scopus 로고    scopus 로고
    • Normal fertilization occurs with eggs lacking the integrin α6β1 and is CD9-dependent
    • DOI 10.1083/jcb.149.6.1289
    • Miller BJ, Georges-Labouesse E, Primakoff P, Myles DG. 2000. Normal fertilization occurs with eggs lacking the integrin α6β1 and is CD9-dependent. J. Cell Biol. 149:1289-95 (Pubitemid 30399681)
    • (2000) Journal of Cell Biology , vol.149 , Issue.6 , pp. 1289-1295
    • Miller, B.J.1    Georges-Labouesse, E.2    Primakoff, P.3    Myles, D.G.4
  • 109
    • 65749105688 scopus 로고    scopus 로고
    • β1 integrin is an adhesion protein for sperm binding to eggs
    • Baessler K, Lee Y, Sampson N. 2009. β1 integrin is an adhesion protein for sperm binding to eggs. ACS Chem. Biol. 4:357-66
    • (2009) ACS Chem. Biol. , vol.4 , pp. 357-66
    • Baessler, K.1    Lee, Y.2    Sampson, N.3
  • 110
    • 33846148653 scopus 로고    scopus 로고
    • Sperm plasma membrane breakdown during Drosophila fertilization requires Sneaky, an acrosomal membrane protein
    • DOI 10.1242/dev.02671
    • Wilson KL, Fitch KR, Bafus BT, Wakimoto BT. 2006. Sperm plasma membrane breakdown during Drosophila fertilization requires Sneaky, an acrosomal membrane protein. Development 133:4871-79 (Pubitemid 46085053)
    • (2006) Development , vol.133 , Issue.24 , pp. 4871-4879
    • Wilson, K.L.1    Fitch, K.R.2    Bafus, B.T.3    Wakimoto, B.T.4
  • 111
    • 0043033098 scopus 로고    scopus 로고
    • A C. elegans sperm TRP protein required for sperm-egg interactions during fertilization
    • DOI 10.1016/S0092-8674(03)00565-8
    • Xu X-ZS, Sternberg PW. 2003. A C. elegans sperm TRP protein required for sperm-egg interactions during fertilization. Cell 114:285-97 (Pubitemid 36962928)
    • (2003) Cell , vol.114 , Issue.3 , pp. 285-297
    • Xu, X.-Z.S.1    Sternberg, P.W.2
  • 112
    • 25844505696 scopus 로고    scopus 로고
    • The spe-42 gene is required for sperm-egg interactions during C. elegans fertilization and encodes a sperm-specific transmembrane protein
    • DOI 10.1016/j.ydbio.2005.07.020, PII S0012160605004768
    • Kroft TL, Gleason EJ, LHernault SW. 2005. The spe-42 gene is required for sperm-egg interactions during C. elegans fertilization and encodes a sperm-specific transmembrane protein. Dev. Biol. 286:169-81 (Pubitemid 41394055)
    • (2005) Developmental Biology , vol.286 , Issue.1 , pp. 169-181
    • Kroft, T.L.1    Gleason, E.J.2    L'Hernault, S.W.3
  • 113
    • 79951851088 scopus 로고    scopus 로고
    • Fertilization in C. elegans requires an intact C-terminal RING finger in sperm protein SPE-42
    • Wilson LD, Sackett JM, Mieczkowski BD, Richie AL, Thoemke K, et al. 2011. Fertilization in C. elegans requires an intact C-terminal RING finger in sperm protein SPE-42. BMC Dev. Biol. 11:10
    • (2011) BMC Dev. Biol. , vol.11 , pp. 10
    • Wilson, L.D.1    Sackett, J.M.2    Mieczkowski, B.D.3    Richie, A.L.4    Thoemke, K.5
  • 115
    • 0032478522 scopus 로고    scopus 로고
    • The C. elegans spe-9 gene encodes a sperm transmembrane protein that contains EGF-like repeats and is required for fertilization
    • DOI 10.1016/S0092-8674(00)81147-2
    • Singson A, Mercer KB, LHernault SW. 1998. The C. elegans spe-9 gene encodes a sperm transmembrane protein that contains EGF-like repeats and is required for fertilization. Cell 93:71-79 (Pubitemid 28173553)
    • (1998) Cell , vol.93 , Issue.1 , pp. 71-79
    • Singson, A.1    Mercer, K.B.2    L'Hernault, S.W.3
  • 116
    • 21644489538 scopus 로고    scopus 로고
    • The Caenorhabditis elegans spe-38 gene encodes a novel four-pass integral membrane protein required for sperm function at fertilization
    • DOI 10.1242/dev.01868
    • Chatterjee I, Richmond A, Putiri E, Shakes DC, Singson A. 2005. The Caenorhabditis elegans spe-38 gene encodes a novel four-pass integral membrane protein required for sperm function at fertilization. Development 132:2795-808 (Pubitemid 40932869)
    • (2005) Development , vol.132 , Issue.12 , pp. 2795-2808
    • Chatterjee, I.1    Richmond, A.2    Putiri, E.3    Shakes, D.C.4    Singson, A.5
  • 118
    • 34548480470 scopus 로고    scopus 로고
    • Regulation of MBK-2/Dyrk kinase by dynamic cortical anchoring during the oocyte-to-zygote transition
    • DOI 10.1016/j.cub.2007.08.049, PII S0960982207019057
    • Stitzel ML, Cheng KC, Seydoux G. 2007. Regulation of MBK-2/Dyrk kinase by dynamic cortical anchoring during the oocyte-to-zygote transition. Curr. Biol. 17:1545-54 (Pubitemid 47380404)
    • (2007) Current Biology , vol.17 , Issue.18 , pp. 1545-1554
    • Stitzel, M.L.1    Cheng, K.C.-C.2    Seydoux, G.3
  • 119
    • 70350324714 scopus 로고    scopus 로고
    • EGG-4 and EGG-5 link events of the oocyte-to-embryo transition with meiotic progression in C. elegans
    • Parry JM, Velarde NV, Lefkovith AJ, Zegarek MH, Hang JS, et al. 2009. EGG-4 and EGG-5 link events of the oocyte-to-embryo transition with meiotic progression in C. elegans. Curr. Biol. 19:1752-57
    • (2009) Curr. Biol. , vol.19 , pp. 1752-57
    • Parry, J.M.1    Velarde, N.V.2    Lefkovith, A.J.3    Zegarek, M.H.4    Hang, J.S.5
  • 120
    • 70350344970 scopus 로고    scopus 로고
    • Regulation of MBK-2/DYRK by CDK-1 and the pseudophosphatases EGG-4 and EGG-5 during the oocyte-to-embryo transition
    • Cheng KC-C, Klancer R, Singson A, Seydoux G. 2009. Regulation of MBK-2/DYRK by CDK-1 and the pseudophosphatases EGG-4 and EGG-5 during the oocyte-to-embryo transition. Cell 139:560-72
    • (2009) Cell , vol.139 , pp. 560-72
    • Kc-C, C.1    Klancer, R.2    Singson, A.3    Seydoux, G.4
  • 121
    • 77249172226 scopus 로고    scopus 로고
    • Is HAP2-GSC1 an ancestral gamete fusogen?
    • Wong JL, Johnson MA. 2010. Is HAP2-GSC1 an ancestral gamete fusogen? Trends Cell Biol. 20:134-41
    • (2010) Trends Cell Biol. , vol.20 , pp. 134-41
    • Wong, J.L.1    Johnson, M.A.2
  • 123
    • 30344459431 scopus 로고    scopus 로고
    • GENERATIVE CELL SPECIFIC 1 is essential for angiosperm fertilization
    • DOI 10.1038/ncb1345, PII N1345
    • Mori T, Kuriowa H, Higashiyama T, Kuriowa T. 2006. Generative Cell Specific 1 is essential for angiosperm fertilization. Nat. Cell Biol. 8:64-71 (Pubitemid 43064798)
    • (2006) Nature Cell Biology , vol.8 , Issue.1 , pp. 64-71
    • Mori, T.1    Kuroiwa, H.2    Higashiyama, T.3    Kuroiwa, T.4
  • 124
    • 33846094853 scopus 로고    scopus 로고
    • Arabidopsis HAP2 (GCS1) is a sperm-specific gene required for pollen tube guidance and fertilization
    • DOI 10.1242/dev.02683
    • von Besser K, Frank AC, Johnson MA, Preuss D. 2006. Arabidopsis HAP2 (GCS1) is a sperm-specific gene required for pollen tube guidance and fertilization. Development 133:4761-69 (Pubitemid 46063088)
    • (2006) Development , vol.133 , Issue.23 , pp. 4761-4769
    • Von Besser, K.1    Frank, A.C.2    Johnson, M.A.3    Preuss, D.4
  • 126
    • 77950400019 scopus 로고    scopus 로고
    • HAP2(GCS1)-dependent gamete fusion requires a positively charged carboxy-terminal domain
    • Wong JL, Leydon AR, Johnson MA. 2010. HAP2(GCS1)-dependent gamete fusion requires a positively charged carboxy-terminal domain. PLoS Genet. 6:e1000882
    • (2010) PLoS Genet. , vol.6
    • Wong, J.L.1    Leydon, A.R.2    Johnson, M.A.3
  • 127
    • 79251477550 scopus 로고    scopus 로고
    • The functional domain of GCS1-based gamete fusion resides in the amino terminus in plant and parasite species
    • Mori T, Hirai M, Kuriowa T, Miyagishima S. 2010. The functional domain of GCS1-based gamete fusion resides in the amino terminus in plant and parasite species. PLoS ONE 5:e15957
    • (2010) PLoS ONE , vol.5
    • Mori, T.1    Hirai, M.2    Kuriowa, T.3    Miyagishima, S.4
  • 128
    • 0032479148 scopus 로고    scopus 로고
    • Membrane fusion is induced by a distinct peptide sequence of the sea urchin fertilization protein bindin
    • DOI 10.1074/jbc.273.27.16748
    • Ulrich AS, Otter M, Glabe CG, Hoekstra D. 1998. Membrane fusion is induced by a distinct peptide sequence of the sea urchin fertilization protein bindin. J. Biol. Chem. 273:16748-55 (Pubitemid 28311699)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.27 , pp. 16748-16755
    • Ulrich, A.S.1    Otter, M.2    Glabe, C.G.3    Hoekstra, D.4
  • 129
    • 0035826618 scopus 로고    scopus 로고
    • The crystal structure of a fusagenic sperm protein reveals extreme surface properties
    • DOI 10.1021/bi002779v
    • Kresge N, Vacquier VD, Stout CD. 2001. The crystal structure of a fusagenic sperm protein reveals extreme surface properties. Biochemistry 40:5407-13 (Pubitemid 32458241)
    • (2001) Biochemistry , vol.40 , Issue.18 , pp. 5407-5413
    • Kresge, N.1    Vacquier, V.D.2    Stout, C.D.3
  • 130
    • 54249105944 scopus 로고    scopus 로고
    • The evolution of sea urchin bindin
    • Zigler KS. 2008. The evolution of sea urchin bindin. Int. J. Dev. Biol. 52:791-96
    • (2008) Int. J. Dev. Biol. , vol.52 , pp. 791-96
    • Zigler, K.S.1
  • 131
    • 33748648790 scopus 로고    scopus 로고
    • Tracking down the ZP domain: From the mammalian zona pellucida to the molluscan vitelline envelope
    • DOI 10.1055/s-2006-948550
    • Monne M, Han L, Jovine L. 2006. Tracking down the ZP domain: from the mammalian zona pellucida to the molluscan vitelline envelope. Semin. Reprod. Med. 24:204-16 (Pubitemid 44387525)
    • (2006) Seminars in Reproductive Medicine , vol.24 , Issue.4 , pp. 204-216
    • Monne, M.1    Han, L.2    Jovine, L.3
  • 133
    • 0028971528 scopus 로고
    • Liposome function induced by a Mr 18000 protein localized to the acrosomal region of acrosome-reacted abalone spermatozoa
    • Swanson WJ, Vacquier VD. 1995. Liposome fusion induced by a Mr 18000 protein localized to the acrosomal region of acrosome-reacted abalone spermatozoa. Biochemistry 34:14202-8 (Pubitemid 3000605)
    • (1995) Biochemistry , vol.34 , Issue.43 , pp. 14202-14208
    • Swanson, W.J.1    Vazquier, V.D.2
  • 134
    • 72649091351 scopus 로고    scopus 로고
    • ZP domain proteins in the abalone egg coat include a paralog of VERL under positive selection that binds lysin and 18-kDa sperm proteins
    • Aagaard JE, Vacquier VD, MacCoss MJ, Swanson WJ. 2010. ZP domain proteins in the abalone egg coat include a paralog of VERL under positive selection that binds lysin and 18-kDa sperm proteins. Mol. Biol. Evol. 27:193-203
    • (2010) Mol. Biol. Evol. , vol.27 , pp. 193-203
    • Aagaard, J.E.1    Vacquier, V.D.2    MacCoss, M.J.3    Swanson, W.J.4
  • 135
    • 0019160353 scopus 로고
    • Mechanics of in vitro fertilization in the hamster
    • Shalgi R, Phillips DM. 1980. Mechanics of in vitro fertilization in the hamster. Biol. Reprod. 23:433-344
    • (1980) Biol. Reprod. , vol.23 , pp. 433-344
    • Shalgi, R.1    Phillips, D.M.2
  • 136
    • 0019198150 scopus 로고
    • Surface architecture of the mouse and hamster zona pellucida and oocyte
    • DOI 10.1016/S0022-5320(80)90129-X
    • Phillips DM, Shalgi R. 1980. Surface architecture of the mouse and hamster zona pellucida and oocyte. J. Ultrastruct. Res. 72:1-12 (Pubitemid 11232038)
    • (1980) Journal of Ultrastructure Research , vol.72 , Issue.1 , pp. 1-12
    • Phillips, D.M.1    Shalgi, R.2
  • 137
    • 0031011488 scopus 로고    scopus 로고
    • The putative chaperone calmegin is required for sperm fertility
    • Ikawa M, Wada I, Kominami K, Watanabe D, Toshimuri K, et al. 1997. The putative chaperone calmegin is required for sperm fertility. Nature 387:607-11
    • (1997) Nature , vol.387 , pp. 607-11
    • Ikawa, M.1    Wada, I.2    Kominami, K.3    Watanabe, D.4    Toshimuri, K.5
  • 140
    • 77954152541 scopus 로고    scopus 로고
    • Multivariate analysis of male reproductive function in Inpp5b-/- mice reveals heterogeneity in defects in fertility, sperm-egg membrane interaction, and proteolytic cleavage of sperm ADAMs
    • Marcello MR, Evans JP. 2010. Multivariate analysis of male reproductive function in Inpp5b-/- mice reveals heterogeneity in defects in fertility, sperm-egg membrane interaction, and proteolytic cleavage of sperm ADAMs. Mol. Hum. Reprod. 16:492-505
    • (2010) Mol. Hum. Reprod. , vol.16 , pp. 492-505
    • Marcello, M.R.1    Evans, J.P.2
  • 141
    • 0027092647 scopus 로고
    • Impaired long-term potentiation, spatial learning, and hippocampal development in fyn mutant mice
    • Grant SG, ODell TJ, Karl KA, Stein PL, Soriano P, Kandel E. 1992. Impaired long-term potentiation, spatial learning, and hippocampal development in fyn mutant mice. Science 258:1903-10 (Pubitemid 23026728)
    • (1992) Science , vol.258 , Issue.5090 , pp. 1903-1910
    • Grant, S.G.N.1    O'Dell, T.J.2    Karl, K.A.3    Stein, P.L.4    Soriano, P.5    Kandel, E.R.6
  • 142
    • 77954268315 scopus 로고    scopus 로고
    • Role of Fyn kinase in oocyte developmental potential
    • Luo J, McGinnis LK, Kinsey WH. 2010. Role of Fyn kinase in oocyte developmental potential. Reprod. Fertil. Dev. 22:966-76
    • (2010) Reprod. Fertil. Dev. , vol.22 , pp. 966-76
    • Luo, J.1    McGinnis, L.K.2    Kinsey, W.H.3
  • 144
    • 0037119363 scopus 로고    scopus 로고
    • Mouse sperm lacking cell surface hyaluronidase PH-20 can pass through the layer of cumulus cells and fertilize the egg
    • Baba D, Kashiwabara S, Honda A, Yamagata K, Wu Q, et al. 2002. Mouse sperm lacking cell surface hyaluronidase PH-20 can pass through the layer of cumulus cells and fertilize the egg. J. Biol. Chem. 277:30310-14
    • (2002) J. Biol. Chem. , vol.277 , pp. 30310-14
    • Baba, D.1    Kashiwabara, S.2    Honda, A.3    Yamagata, K.4    Wu, Q.5
  • 145
    • 0043029287 scopus 로고    scopus 로고
    • Identification of mouse sperm SED1, a bimotif EGF repeat and discoidin-domain protein involved in sperm-egg binding
    • DOI 10.1016/S0092-8674(03)00643-3
    • Ensslin MA, Shur BD. 2003. Identification of mouse sperm SED1, a bimotif EGF repeat and discoidindomain protein involved in sperm-egg binding. Cell 114:405-17 (Pubitemid 37100990)
    • (2003) Cell , vol.114 , Issue.4 , pp. 405-417
    • Ensslin, M.A.1    Shur, B.D.2
  • 146
    • 48949115341 scopus 로고    scopus 로고
    • Impaired sperm fertilizing ability in mice lacking Cysteine-RIch Secretory Protein 1 (CRISP1)
    • Da Ros VG, Maldera JA, Willis WD, Cohen DJ, Goulding EH, et al. 2008. Impaired sperm fertilizing ability in mice lacking Cysteine-RIch Secretory Protein 1 (CRISP1). Dev. Biol. 320:12-18
    • (2008) Dev. Biol. , vol.320 , pp. 12-18
    • Da Ros, V.G.1    Maldera, J.A.2    Willis, W.D.3    Cohen, D.J.4    Goulding, E.H.5
  • 148
    • 79953232734 scopus 로고    scopus 로고
    • Most fertilizing mouse spermatozoa begin their acrosome reaction before contact with the zona pellucida during in vitro fertilization
    • Jin M, Fujiwara E, Kakiuchi Y, Okabe M, Satouh Y, et al. 2011. Most fertilizing mouse spermatozoa begin their acrosome reaction before contact with the zona pellucida during in vitro fertilization. Proc. Natl. Acad. Sci. USA 108:4892-96
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 4892-96
    • Jin, M.1    Fujiwara, E.2    Kakiuchi, Y.3    Okabe, M.4    Satouh, Y.5
  • 149
    • 73349142368 scopus 로고    scopus 로고
    • Equatorin: Identification and characterization of the epitope of the MN9 antibody in mouse
    • Yamatoya K, Yoshida K, Ito C, Maekawa M, Yanagida M, et al. 2009. Equatorin: identification and characterization of the epitope of the MN9 antibody in mouse. Biol. Reprod. 81:889-97
    • (2009) Biol. Reprod. , vol.81 , pp. 889-97
    • Yamatoya, K.1    Yoshida, K.2    Ito, C.3    Maekawa, M.4    Yanagida, M.5
  • 150
    • 79955569953 scopus 로고    scopus 로고
    • Cysteine-rich secretory protein 4 is an inhibitor of transient receptor potential M8 with a role in establishing sperm function
    • Gibbs GM, Orta G, Reddy T, Koppers AJ, Martínez-Ĺopez P, et al. 2011. Cysteine-rich secretory protein 4 is an inhibitor of transient receptor potential M8 with a role in establishing sperm function. Proc. Natl. Acad. Sci. USA 108:7034-39
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 7034-39
    • Gibbs, G.M.1    Orta, G.2    Reddy, T.3    Koppers, A.J.4    Martínez-Ĺopez, P.5
  • 151
  • 154
    • 0034284687 scopus 로고    scopus 로고
    • A role for a TIMP-3-sensitive Zn2+-dependent metalloprotease in mammalian gamete membrane fusion
    • Correa LM, Cho C, Myles DG, Primakoff P. 2000. A role for a TIMP-3-sensitive Zn2+-dependent metalloprotease in mammalian gamete membrane fusion. Dev. Biol. 225:124-34
    • (2000) Dev. Biol. , vol.225 , pp. 124-34
    • Correa, L.M.1    Cho, C.2    Myles, D.G.3    Primakoff, P.4
  • 155
    • 0031570766 scopus 로고    scopus 로고
    • Involvement of a sperm protein sensitive to sulfhydryl-depleting reagents in mouse sperm-egg fusion
    • DOI 10.1002/(SICI)1097-010X(19970615)278:3<178::AID-JEZ7>3.0.CO;2-L
    • Mammoto A, Masumoto N, Tahara M, Yoneda M, Nishizaki T, et al. 1997. Involvement of a sperm protein sensitive to sulfhydry-depleting reagents in mouse sperm-egg fusion. J. Exp. Zool. 278:178-88 (Pubitemid 27253216)
    • (1997) Journal of Experimental Zoology , vol.278 , Issue.3 , pp. 178-188
    • Mammoto, A.1    Masumoto, N.2    Tahara, M.3    Yoneda, M.4    Nishizaki, T.5    Tasaka, K.6    Miyake, A.7
  • 156
    • 33646882179 scopus 로고    scopus 로고
    • A role for sperm surface protein disulfide isomerase activity in gamete fusion: Evidence for the participation of ERp57
    • DOI 10.1016/j.devcel.2006.03.011, PII S1534580706001572
    • Ellerman DA, Myles DG, Primakoff P. 2006. A role for sperm surface protein disulfide isomerase activity in gamete fusion: evidence for the participation of ERp57. Dev. Cell 10:831-37 (Pubitemid 43779114)
    • (2006) Developmental Cell , vol.10 , Issue.6 , pp. 831-837
    • Ellerman, D.A.1    Myles, D.G.2    Primakoff, P.3
  • 158
    • 0034677883 scopus 로고    scopus 로고
    • Identification of key functional amino acids of the mouse fertilin β (ADAM2) disintegrin loop for cell-cell adhesion during fertilization
    • DOI 10.1074/jbc.275.11.7677
    • Zhu X, Bansal NP, Evans JP. 2000. Identification of key functional amino acids of the mouse fertilin β (ADAM2) disintegrin loop for cell-cell adhesion during fertilization. J. Biol. Chem. 275:7677-83 (Pubitemid 30159670)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.11 , pp. 7677-7683
    • Zhu, X.1    Bansal, N.P.2    Evans, J.P.3
  • 159
    • 0035163797 scopus 로고    scopus 로고
    • Sequence-specific interaction between the disintegrin domain of mouse ADAM 3 and murine eggs: Role of β1 integrin-associated proteins CD9, CD81, and CD98
    • Takahashi Y, Bigler D, Ito Y, White JM. 2001. Sequence-specific interaction between the disintegrin domain of mouse ADAM3 and murine eggs: role of the β1 integrin-associated proteins CD9, CD81, and CD98. Mol. Biol. Cell 12:809-20 (Pubitemid 33051980)
    • (2001) Molecular Biology of the Cell , vol.12 , Issue.4 , pp. 809-820
    • Takahashi, Y.1    Bigler, D.2    Ito, Y.3    White, J.M.4
  • 160
    • 65749091728 scopus 로고    scopus 로고
    • Egg integrins: Back in the game of mammalian fertilization
    • Evans JP. 2009. Egg integrins: back in the game of mammalian fertilization. ACS Chem. Biol. 4:321-23
    • (2009) ACS Chem. Biol. , vol.4 , pp. 321-23
    • Evans, J.P.1
  • 161
    • 33644820905 scopus 로고    scopus 로고
    • Complete predicted three-dimensional structure of the facilitator transmembrane protein and hepatitisCvirus receptorCD81: Conserved and variable structural domains in the tetraspanin superfamily
    • Seigneuret M. 2006. Complete predicted three-dimensional structure of the facilitator transmembrane protein and hepatitisCvirus receptorCD81: conserved and variable structural domains in the tetraspanin superfamily. Biophys. J. 90:212-27
    • (2006) Biophys. J. , vol.90 , pp. 212-27
    • Seigneuret, M.1
  • 162
    • 84857282974 scopus 로고    scopus 로고
    • SAS1B is an egg specific high affinity oolemmal binding partner for sperm specific acrosomal SLLP1 during fertilization
    • Portland, OR
    • Mandal A, Sachdev M, Digilio L, Panneerdoss S, Suryavathi V, et al. 2011. SAS1B is an egg specific high affinity oolemmal binding partner for sperm specific acrosomal SLLP1 during fertilization. Presented at Meet. Soc. Study Reprod. , Portland, OR
    • (2011) Meet. Soc. Study Reprod.
    • Mandal, A.1    Sachdev, M.2    Digilio, L.3    Panneerdoss, S.4    Suryavathi, V.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.