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Volumn 139, Issue 3, 2010, Pages 533-544

A model of the acrosome reaction progression via the acrosomal membrane-anchored protein equatorin

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN; PROTEIN MN9; UNCLASSIFIED DRUG;

EID: 77149124254     PISSN: 14701626     EISSN: 17417899     Source Type: Journal    
DOI: 10.1530/REP-09-0434     Document Type: Article
Times cited : (25)

References (55)
  • 1
    • 0028955151 scopus 로고
    • Monoclonal antibodies which recognize equatorial segment epitopes presented de novo following the A23187-induced acrosome reaction of guinea pig sperm
    • Allen CA & Green DP 1995 Monoclonal antibodies which recognize equatorial segment epitopes presented de novo following the A23187-induced acrosome reaction of guinea pig sperm. Journal of Cell Science 108 767-777.
    • (1995) Journal of Cell Science , vol.108 , pp. 767-777
    • Allen, C.A.1    Green, D.P.2
  • 2
    • 55649088022 scopus 로고    scopus 로고
    • Capacitation-dependent reorganization of microdomains in the apical sperm head plasma membrane: Functional relationship with zona binding and the zona-induced acrosome reaction
    • Boerke A, Tsai PS, Garcia-Gil N, Brewis IA & Gadella BM 2008 Capacitation-dependent reorganization of microdomains in the apical sperm head plasma membrane: functional relationship with zona binding and the zona-induced acrosome reaction. Theriogenology 70 1188-1196.
    • (2008) Theriogenology , vol.70 , pp. 1188-1196
    • Boerke, A.1    Tsai, P.S.2    Garcia-Gil, N.3    Brewis, I.A.4    Gadella, B.M.5
  • 4
    • 70350351206 scopus 로고    scopus 로고
    • Functional consequences of cleavage, dissociation and exocytotic release of ZP3R, a C4BP-related protein, from the mouse sperm acrosomal matrix
    • Buffone MG, Kim K-S, Doak BJ, Rodriguez-Miranda E & Gerton GL 2009a Functional consequences of cleavage, dissociation and exocytotic release of ZP3R, a C4BP-related protein, from the mouse sperm acrosomal matrix. Journal of Cell Science 122 3153-3160.
    • (2009) Journal of Cell Science , vol.122 , pp. 3153-3160
    • Buffone, M.G.1    Kim, K.-S.2    Doak, B.J.3    Rodriguez-Miranda, E.4    Gerton, G.L.5
  • 5
    • 67650364012 scopus 로고    scopus 로고
    • Acrosomal exocytosis of mouse sperm progresses in a consistent direction in response to zona pellucida
    • Buffone MG, Rodriguez-Miranda E, Storey BT & Gerton GL 2009b Acrosomal exocytosis of mouse sperm progresses in a consistent direction in response to zona pellucida. Journal of Cellular Physiology 220 611-620.
    • (2009) Journal of Cellular Physiology , vol.220 , pp. 611-620
    • Buffone, M.G.1    Rodriguez-Miranda, E.2    Storey, B.T.3    Gerton, G.L.4
  • 7
    • 0030470756 scopus 로고    scopus 로고
    • Use of peanut agglutinin to assess the acrosomal status and the zona pellucida-induced acrosome reaction in stallion spermatozoa
    • Cheng FP, Fazeli A, Voorhout WF, Marks A, Bevers MM & Colenbrander B 1996 Use of peanut agglutinin to assess the acrosomal status and the zona pellucida-induced acrosome reaction in stallion spermatozoa. Journal of Andrology 17 674-682.
    • (1996) Journal of Andrology , vol.17 , pp. 674-682
    • Cheng, F.P.1    Fazeli, A.2    Voorhout, W.F.3    Marks, A.4    Bevers, M.M.5    Colenbrander, B.6
  • 8
    • 38149145468 scopus 로고
    • Assessing acrosomal status of bovine sperm using fluoresceinated lectins
    • Cross NL & Watson SK 1994 Assessing acrosomal status of bovine sperm using fluoresceinated lectins. Theriogenology 42 89-98.
    • (1994) Theriogenology , vol.42 , pp. 89-98
    • Cross, N.L.1    Watson, S.K.2
  • 9
    • 26444433186 scopus 로고    scopus 로고
    • Dynamics of SNARE assembly and disassembly during sperm acrosomal exocytosis
    • De Blas GA, Roggero CM, Tomes CN & Mayorga LS 2005 Dynamics of SNARE assembly and disassembly during sperm acrosomal exocytosis. PLoS Biology 3 e323.
    • (2005) PLoS Biology , vol.3
    • De Blas, G.A.1    Roggero, C.M.2    Tomes, C.N.3    Mayorga, L.S.4
  • 10
    • 0034634709 scopus 로고    scopus 로고
    • Dynamics of the mammalian sperm plasma membrane in the process of fertilization
    • Flesch FM & Gadella BM 2000 Dynamics of the mammalian sperm plasma membrane in the process of fertilization. Biochimica et Biophysica Acta 1469 197-235.
    • (2000) Biochimica et Biophysica Acta , vol.1469 , pp. 197-235
    • Flesch, F.M.1    Gadella, B.M.2
  • 12
    • 0030974131 scopus 로고    scopus 로고
    • AM67, a secretory component of the guinea pig sperm acrosomal matrix, is related to mouse sperm protein sp56 and the complement component 4-binding proteins
    • Foster JA, Friday BB, Maulit MT, Blobel C,Winfrey VP, Olson GE, Kim KS & Gerton GL 1997 AM67, a secretory component of the guinea pig sperm acrosomal matrix, is related to mouse sperm protein sp56 and the complement component 4-binding proteins. Journal of Biological Chemistry 272 12714-12722.
    • (1997) Journal of Biological Chemistry , vol.272 , pp. 12714-12722
    • Foster, J.A.1    Friday, B.B.2    Maulit, M.T.3    Blobel, C.4    Winfrey, V.P.5    Olson, G.E.6    Kim, K.S.7    Gerton, G.L.8
  • 13
    • 0028986027 scopus 로고
    • Glycolipid migration from the apical to the equatorial subdomains of the sperm head plasma membrane precedes the acrosome reaction. Evidence for a primary capacitation event in boar spermatozoa
    • Gadella BM, Lopes-Cardozo M, Golde LMV, Colenbrander B & Gadella TW 1995 Glycolipid migration from the apical to the equatorial subdomains of the sperm head plasma membrane precedes the acrosome reaction. Evidence for a primary capacitation event in boar spermatozoa. Journal of Cell Science 108 935-946.
    • (1995) Journal of Cell Science , vol.108 , pp. 935-946
    • Gadella, B.M.1    Lopes-Cardozo, M.2    Golde, L.M.V.3    Colenbrander, B.4    Gadella, T.W.5
  • 14
    • 0032489040 scopus 로고    scopus 로고
    • Species diversity in the structure of zonadhesin, a sperm-specific membrane protein containing multiple cell adhesion molecule-like domains
    • Gao Z & Garbers DL 1998 Species diversity in the structure of zonadhesin, a sperm-specific membrane protein containing multiple cell adhesion molecule-like domains. Journal of Biological Chemistry 273 3415-3421.
    • (1998) Journal of Biological Chemistry , vol.273 , pp. 3415-3421
    • Gao, Z.1    Garbers, D.L.2
  • 16
    • 0025791006 scopus 로고
    • A mechanism for differential release of acrosomal enzymes during the acrosome reaction
    • Hardy DM, Oda MN, Friend DS & Huang TT 1991 A mechanism for differential release of acrosomal enzymes during the acrosome reaction. Biochemical Journal 275 759-766.
    • (1991) Biochemical Journal , vol.275 , pp. 759-766
    • Hardy, D.M.1    Oda, M.N.2    Friend, D.S.3    Huang, T.T.4
  • 18
    • 0026000449 scopus 로고
    • Staining of the inner acrosomal membrane of human spermatozoa with concanavalin A lectin as an indicator of potential egg penetration ability
    • Holden CA & Trounson AO 1991 Staining of the inner acrosomal membrane of human spermatozoa with concanavalin A lectin as an indicator of potential egg penetration ability. Fertility and Sterility 56 967-974.
    • (1991) Fertility and Sterility , vol.56 , pp. 967-974
    • Holden, C.A.1    Trounson, A.O.2
  • 20
    • 0036751233 scopus 로고    scopus 로고
    • Role of acrosomal matrix proteases in sperm-zona pellucida interactions
    • Honda A, Siruntawineti J & Baba T 2002 Role of acrosomal matrix proteases in sperm-zona pellucida interactions. Human Reproduction Update 8 405-412.
    • (2002) Human Reproduction Update , vol.8 , pp. 405-412
    • Honda, A.1    Siruntawineti, J.2    Baba, T.3
  • 21
    • 15044362481 scopus 로고    scopus 로고
    • The immunoglobulin superfamily protein Izumo is required for sperm to fuse with eggs
    • Inoue N, Ikawa M, Isotani A & Okabe M 2005 The immunoglobulin superfamily protein Izumo is required for sperm to fuse with eggs. Nature 434 234-238.
    • (2005) Nature , vol.434 , pp. 234-238
    • Inoue, N.1    Ikawa, M.2    Isotani, A.3    Okabe, M.4
  • 22
    • 0023023108 scopus 로고
    • The fate of acrosomal staining during the acrosome reaction of human spermatozoa as revealed by a monoclonal antibody and PNA-lectin
    • Kallajoki M, Virtanen I & Suominen J 1986 The fate of acrosomal staining during the acrosome reaction of human spermatozoa as revealed by a monoclonal antibody and PNA-lectin. International Journal of Andrology 9 181-194.
    • (1986) International Journal of Andrology , vol.9 , pp. 181-194
    • Kallajoki, M.1    Virtanen, I.2    Suominen, J.3
  • 23
    • 0242624744 scopus 로고    scopus 로고
    • Differential release of soluble and matrix components: Evidence for intermediate states of secretion during spontaneous acrosomal exocytosis in mouse sperm
    • Kim KS & Gerton GL 2003 Differential release of soluble and matrix components: evidence for intermediate states of secretion during spontaneous acrosomal exocytosis in mouse sperm. Developmental Biology 264 141-152.
    • (2003) Developmental Biology , vol.264 , pp. 141-152
    • Kim, K.S.1    Gerton, G.L.2
  • 24
    • 0035168574 scopus 로고    scopus 로고
    • Mouse sperm protein sp56 is a component of the acrosomal matrix
    • Kim KS, Cha MC & Gerton GL 2001a Mouse sperm protein sp56 is a component of the acrosomal matrix. Biology of Reproduction 64 36-43.
    • (2001) Biology of Reproduction , vol.64 , pp. 36-43
    • Kim, K.S.1    Cha, M.C.2    Gerton, G.L.3
  • 25
    • 0035159305 scopus 로고    scopus 로고
    • Differential release of guinea pig sperm acrosomal components during exocytosis
    • Kim KS, Foster JA & Gerton GL 2001b Differential release of guinea pig sperm acrosomal components during exocytosis. Biology of Reproduction 64 148-156.
    • (2001) Biology of Reproduction , vol.64 , pp. 148-156
    • Kim, K.S.1    Foster, J.A.2    Gerton, G.L.3
  • 26
    • 0029002382 scopus 로고
    • Assessment of the vitality and acrosomal status of human spermatozoa using fluorescent probes
    • Kinger S & Rajalakshmi M 1995 Assessment of the vitality and acrosomal status of human spermatozoa using fluorescent probes. International Journal of Andrology 18 (Supplement 1) 12-18.
    • (1995) International Journal of Andrology , vol.18 , Issue.SUPPL.EMENT 1 , pp. 12-18
    • Kinger, S.1    Rajalakshmi, M.2
  • 27
    • 0034761261 scopus 로고    scopus 로고
    • Exposure of sperm head equatorin after acrosome reaction and its fate after fertilization in mice
    • Manandhar G & Toshimori K 2001 Exposure of sperm head equatorin after acrosome reaction and its fate after fertilization in mice. Biology of Reproduction 65 1425-1436.
    • (2001) Biology of Reproduction , vol.65 , pp. 1425-1436
    • Manandhar, G.1    Toshimori, K.2
  • 28
    • 0027234804 scopus 로고
    • Sperm require beta-N-acetylglucosaminidase to penetrate through the egg zona pellucida
    • Miller DJ, Gong X & Shur BD 1993 Sperm require beta-N-acetylglucosaminidase to penetrate through the egg zona pellucida. Development 118 1279-1289.
    • (1993) Development , vol.118 , pp. 1279-1289
    • Miller, D.J.1    Gong, X.2    Shur, B.D.3
  • 29
    • 65949096077 scopus 로고    scopus 로고
    • Localization of lowdensity detergent-resistant membrane proteins in intact and acrosomereacted mouse sperm
    • Miranda PV, Allaire A, Sosnik J & Visconti PE 2009 Localization of lowdensity detergent-resistant membrane proteins in intact and acrosomereacted mouse sperm. Biology of Reproduction 80 897-904.
    • (2009) Biology of Reproduction , vol.80 , pp. 897-904
    • Miranda, P.V.1    Allaire, A.2    Sosnik, J.3    Visconti, P.E.4
  • 30
    • 33748852206 scopus 로고    scopus 로고
    • The mammalian acrosome as a secretory lysosome: New and old evidence
    • Moreno RD & Alvarado CP 2006 The mammalian acrosome as a secretory lysosome: new and old evidence. Molecular Reproduction and Development 73 1430-1434.
    • (2006) Molecular Reproduction and Development , vol.73 , pp. 1430-1434
    • Moreno, R.D.1    Alvarado, C.P.2
  • 31
    • 0028913751 scopus 로고
    • Amino acid sequences of porcine Sp38 and proacrosin required for binding to the zona pellucida
    • Mori E, Kashiwabara S, Baba T, Inagaki Y & Mori T 1995 Amino acid sequences of porcine Sp38 and proacrosin required for binding to the zona pellucida. Developmental Biology 168 575-583.
    • (1995) Developmental Biology , vol.168 , pp. 575-583
    • Mori, E.1    Kashiwabara, S.2    Baba, T.3    Inagaki, Y.4    Mori, T.5
  • 32
    • 0023232821 scopus 로고
    • Specific labelling by peanut agglutinin of the outer acrosomal membrane of the human spermatozoon
    • Mortimer D, Curtis EF & Miller RG 1987 Specific labelling by peanut agglutinin of the outer acrosomal membrane of the human spermatozoon. Journal of Reproduction and Fertility 81 127-135.
    • (1987) Journal of Reproduction and Fertility , vol.81 , pp. 127-135
    • Mortimer, D.1    Curtis, E.F.2    Miller, R.G.3
  • 35
    • 4544371385 scopus 로고    scopus 로고
    • Zonadhesin assembly into the hamster sperm acrosomal matrix occurs by distinct targeting strategies during spermiogenesis and maturation in the epididymis
    • Olson GE, Winfrey VP, Bi M, Hardy DM & NagDas SK 2004 Zonadhesin assembly into the hamster sperm acrosomal matrix occurs by distinct targeting strategies during spermiogenesis and maturation in the epididymis. Biology of Reproduction 71 1128-1134.
    • (2004) Biology of Reproduction , vol.71 , pp. 1128-1134
    • Olson, G.E.1    Winfrey, V.P.2    Bi, M.3    Hardy, D.M.4    NagDas, S.K.5
  • 36
    • 0017239102 scopus 로고
    • Immunochemical studies on blood groups LXII. Fractionation of hog and human A, H, and AH blood group active substance on insoluble immunoadsorbents of Dolichos and Lotus lectins
    • Pereira ME & Kabat EA 1976 Immunochemical studies on blood groups LXII. Fractionation of hog and human A, H, and AH blood group active substance on insoluble immunoadsorbents of Dolichos and Lotus lectins. Journal of Experimental Medicine 143 422-436.
    • (1976) Journal of Experimental Medicine , vol.143 , pp. 422-436
    • Pereira, M.E.1    Kabat, E.A.2
  • 37
    • 0041732182 scopus 로고    scopus 로고
    • SAMP14, a novel, acrosomal membrane-associated, glycosylphosphatidylinositolanchored member of the Ly-6/urokinase-type plasminogen activator receptor superfamily with a role in sperm-egg interaction
    • Shetty J, Wolkowicz MJ, Digilio LC, Klotz KL, Jayes FL, Diekman AB, Westbrook VA, Farris EM, Hao Z, Coonrod SA et al. 2003 SAMP14, a novel, acrosomal membrane-associated, glycosylphosphatidylinositolanchored member of the Ly-6/urokinase-type plasminogen activator receptor superfamily with a role in sperm-egg interaction. Journal of Biological Chemistry 278 30506-30515.
    • (2003) Journal of Biological Chemistry , vol.278 , pp. 30506-30515
    • Shetty, J.1    Wolkowicz, M.J.2    Digilio, L.C.3    Klotz, K.L.4    Jayes, F.L.5    Diekman, A.B.6    Westbrook, V.A.7    Farris, E.M.8    Hao, Z.9    Coonrod, S.A.10
  • 38
    • 0027327042 scopus 로고
    • Beta-Dgalactosidase of rat spermatozoa: Subcellular distribution, substrate specificity, and molecular changes during epididymal maturation
    • Skudlarek MD, Tulsiani DR, Nagdas SK & Orgebin-Crist MC 1993 Beta-Dgalactosidase of rat spermatozoa: subcellular distribution, substrate specificity, and molecular changes during epididymal maturation. Biology of Reproduction 49 204-213.
    • (1993) Biology of Reproduction , vol.49 , pp. 204-213
    • Skudlarek, M.D.1    Tulsiani, D.R.2    Nagdas, S.K.3    Orgebin-Crist, M.C.4
  • 39
    • 0023177789 scopus 로고
    • The acrosome reaction in human sperm from men of proven fertility
    • Stock CE & Fraser LR 1987 The acrosome reaction in human sperm from men of proven fertility. Human Reproduction 2 109-119.
    • (1987) Human Reproduction , vol.2 , pp. 109-119
    • Stock, C.E.1    Fraser, L.R.2
  • 40
    • 0035887056 scopus 로고    scopus 로고
    • A mouse acrosomal cortical matrix protein, MC41, has ZP2-binding activity and forms a complex with a 75-kDa serine protease
    • Tanii I, Oh-oka T, Yoshinaga K & Toshimori K 2002 A mouse acrosomal cortical matrix protein, MC41, has ZP2-binding activity and forms a complex with a 75-kDa serine protease. Developmental Biology 238 332-341.
    • (2002) Developmental Biology , vol.238 , pp. 332-341
    • Tanii, I.1    Oh-oka, T.2    Yoshinaga, K.3    Toshimori, K.4
  • 41
    • 67649840837 scopus 로고    scopus 로고
    • Dynamics of the mammalian sperm head: Modifications and maturation events from spermatogenesis to egg activation
    • Toshimori K 2009 Dynamics of the mammalian sperm head: modifications and maturation events from spermatogenesis to egg activation. Advances in Anatomy, Embryology and Cell Biology 204 5-94.
    • (2009) Advances in Anatomy, Embryology and Cell Biology , vol.204 , pp. 5-94
    • Toshimori, K.1
  • 42
    • 1642422832 scopus 로고    scopus 로고
    • Formation and organization of the mammalian sperm head
    • Toshimori K & Ito C 2004 Formation and organization of the mammalian sperm head. Archives of Histology and Cytology 66 383-396.
    • (2004) Archives of Histology and Cytology , vol.66 , pp. 383-396
    • Toshimori, K.1    Ito, C.2
  • 43
    • 0026458684 scopus 로고
    • Characterization of the antigen recognized by amonoclonal antibody MN9: Unique transport pathway to the equatorial segment of sperm head during spermiogenesis
    • Toshimori K, Tanii I, Araki S & Oura C 1992 Characterization of the antigen recognized by amonoclonal antibody MN9: unique transport pathway to the equatorial segment of sperm head during spermiogenesis. Cell and Tissue Research 270 459-468.
    • (1992) Cell and Tissue Research , vol.270 , pp. 459-468
    • Toshimori, K.1    Tanii, I.2    Araki, S.3    Oura, C.4
  • 44
    • 0031777110 scopus 로고    scopus 로고
    • An MN9 antigenic molecule, equatorin, is required for successful sperm-oocyte fusion in mice
    • Toshimori K, Saxena DK, Tanii I & Yoshinaga K 1998 An MN9 antigenic molecule, equatorin, is required for successful sperm-oocyte fusion in mice. Biology of Reproduction 59 22-29.
    • (1998) Biology of Reproduction , vol.59 , pp. 22-29
    • Toshimori, K.1    Saxena, D.K.2    Tanii, I.3    Yoshinaga, K.4
  • 45
    • 0000617199 scopus 로고
    • Studies on the fertilization of mouse eggs in vitro. I. In vitro fertilization of eggs by fresh epididymal sperm
    • Toyoda Y, Yokoyama M & Hoshi T 1971 Studies on the fertilization of mouse eggs in vitro. I. In vitro fertilization of eggs by fresh epididymal sperm. Japanese Journal of Animal Reproduction 16 147-151.
    • (1971) Japanese Journal of Animal Reproduction , vol.16 , pp. 147-151
    • Toyoda, Y.1    Yokoyama, M.2    Hoshi, T.3
  • 46
    • 0031826659 scopus 로고    scopus 로고
    • The biological and functional significance of the sperm acrosome and acrosomal enzymes in mammalian fertilization
    • Tulsiani DR, Abou-Haila A, Loeser CR & Pereira BM 1998 The biological and functional significance of the sperm acrosome and acrosomal enzymes in mammalian fertilization. Experimental Cell Research 240 151-164.
    • (1998) Experimental Cell Research , vol.240 , pp. 151-164
    • Tulsiani, D.R.1    Abou-Haila, A.2    Loeser, C.R.3    Pereira, B.M.4
  • 47
    • 0342601496 scopus 로고    scopus 로고
    • Assessment of the acrosomal status of membrane-intact ram spermatozoa after freezing and thawing, by simultaneous lectin/Hoechst 33258 staining
    • Valcárcel A, de las Heras MA, Pérez L, Moses DF & Baldassarre H 1997 Assessment of the acrosomal status of membrane-intact ram spermatozoa after freezing and thawing, by simultaneous lectin/Hoechst 33258 staining. Animal Reproduction Science 45 299-309.
    • (1997) Animal Reproduction Science , vol.45 , pp. 299-309
    • Valcárcel, A.1    de las Heras, M.A.2    Pérez, L.3    Moses, D.F.4    Baldassarre, H.5
  • 48
    • 0028343144 scopus 로고
    • A domain-specific 50-kilodalton structural protein of the acrosomal matrix is processed and released during the acrosome reaction in the guinea pig
    • Westbrook-Case VA, Winfrey VP & Olson GE 1994 A domain-specific 50-kilodalton structural protein of the acrosomal matrix is processed and released during the acrosome reaction in the guinea pig. Biology of Reproduction 51 1-13.
    • (1994) Biology of Reproduction , vol.51 , pp. 1-13
    • Westbrook-Case, V.A.1    Winfrey, V.P.2    Olson, G.E.3
  • 51
    • 0002302562 scopus 로고
    • Mammalian fertilization
    • edn 2, pp, Eds E Knobil & JD Neill. New York: Raven Press
    • Yanagimachi R 1994 Mammalian fertilization. In The Physiology of Reproduction, edn 2, pp 189-317. Eds E Knobil & JD Neill. New York: Raven Press.
    • (1994) The Physiology of Reproduction , pp. 189-317
    • Yanagimachi, R.1
  • 52
    • 0034769291 scopus 로고    scopus 로고
    • Inhibition of mouse fertilization in vivo by intra-oviductal injection of an antiequatorin monoclonal antibody
    • Yoshinaga K, Saxena DK, Oh-oka T, Tanii I & Toshimori K 2001 Inhibition of mouse fertilization in vivo by intra-oviductal injection of an antiequatorin monoclonal antibody. Reproduction 122 649-655.
    • (2001) Reproduction , vol.122 , pp. 649-655
    • Yoshinaga, K.1    Saxena, D.K.2    Oh-oka, T.3    Tanii, I.4    Toshimori, K.5
  • 53
    • 30544449581 scopus 로고    scopus 로고
    • The extracellular protein coat of the inner acrosomal membrane is involved in zona pellucida binding and penetration during fertilization: Characterization of its most prominent polypeptide (IAM38)
    • Yu Y, Xu W, Yi YJ, Sutovsky P & Oko R 2006 The extracellular protein coat of the inner acrosomal membrane is involved in zona pellucida binding and penetration during fertilization: characterization of its most prominent polypeptide (IAM38). Developmental Biology 290 32-43.
    • (2006) Developmental Biology , vol.290 , pp. 32-43
    • Yu, Y.1    Xu, W.2    Yi, Y.J.3    Sutovsky, P.4    Oko, R.5
  • 54
    • 0023922798 scopus 로고
    • Ultrastructural studies of the early events of the human sperm acrosome reaction as initiated by human follicular fluid
    • Yudin AI, Gottlieb W & Meizel S 1988 Ultrastructural studies of the early events of the human sperm acrosome reaction as initiated by human follicular fluid. Gamete Research 20 11-24.
    • (1988) Gamete Research , vol.20 , pp. 11-24
    • Yudin, A.I.1    Gottlieb, W.2    Meizel, S.3
  • 55
    • 68049126532 scopus 로고    scopus 로고
    • Acrosomal swelling and membrane docking are required for hybrid vesicle formation during the human sperm acrosome reaction
    • Zanetti N & Mayorga LS 2009 Acrosomal swelling and membrane docking are required for hybrid vesicle formation during the human sperm acrosome reaction. Biology of Reproduction 81 396-405.
    • (2009) Biology of Reproduction , vol.81 , pp. 396-405
    • Zanetti, N.1    Mayorga, L.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.