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Volumn 13, Issue 1, 2011, Pages 88-96

Cellular mechanisms regulating sperm-zona pellucida interaction

Author keywords

capacitation; fertilization; spermatozoa; spermzona pellucida interaction

Indexed keywords

ALPHA 1,3 GALACTOSYLTRANSFERASE; CHAPERONE; CHOLESTEROL; FUCOSYLTRANSFERASE;

EID: 78650971728     PISSN: 1008682X     EISSN: 17457262     Source Type: Journal    
DOI: 10.1038/aja.2010.74     Document Type: Review
Times cited : (65)

References (162)
  • 1
    • 0028932706 scopus 로고
    • Expression of mannose-binding sites on human spermatozoa and their role in sperm-zona pellucida binding
    • Chen JS, Doncel GF, Alvarez C, Acosta AA. Expression of mannose-binding sites on human spermatozoa and their role in sperm-zona pellucida binding. J Androl 1995; 16: 55-63.
    • (1995) J Androl , vol.16 , pp. 55-63
    • Chen, J.S.1    Doncel, G.F.2    Alvarez, C.3    Acosta, A.A.4
  • 2
    • 0030252486 scopus 로고    scopus 로고
    • The role of carbohydrate in sperm-ZP3 adhesion
    • Chapman NR, Barratt CL. The role of carbohydrate in sperm-ZP3 adhesion. Mol Human Reprod 1996; 2: 767-74.
    • (1996) Mol Human Reprod , vol.2 , pp. 767-774
    • Chapman, N.R.1    Barratt, C.L.2
  • 4
    • 54349083578 scopus 로고    scopus 로고
    • The assembly of a zona pellucida binding protein complex in sperm
    • Gadella BM. The assembly of a zona pellucida binding protein complex in sperm. Reprod Domest Anim 2008; 43: 12-9.
    • (2008) Reprod Domest Anim , vol.43 , pp. 12-19
    • Gadella, B.M.1
  • 5
    • 78650972729 scopus 로고    scopus 로고
    • Population Division. World population to exceed 9 billion by 2050. United Nations Department of Economic and Social Affairs: New York, USA, 2009
    • Population Division. World population to exceed 9 billion by 2050. United Nations Department of Economic and Social Affairs: New York, USA, 2009.
  • 6
    • 78650996543 scopus 로고    scopus 로고
    • Guttmacher Institute. Facts on induced abortion worldwide. World Health Organization: Geneva, Switzerland, 2007
    • Guttmacher Institute. Facts on induced abortion worldwide. World Health Organization: Geneva, Switzerland, 2007.
  • 7
    • 34347239001 scopus 로고    scopus 로고
    • Approach to the infertile man
    • Bhasin S. Approach to the infertile man. J Clin Endocrinol Metab 2007; 92: 1995-2004.
    • (2007) J Clin Endocrinol Metab , vol.92 , pp. 1995-2004
    • Bhasin, S.1
  • 9
    • 77950923479 scopus 로고    scopus 로고
    • Surfing the wave, cycle, life history, and genes/proteins expressed by testicular germ cells Part 1: Background to spermatogenesis, spermatogonia, and spermatocytes
    • Hermo L, Pelletier RM, Cyr DG, Smith CE. Surfing the wave, cycle, life history, and genes/proteins expressed by testicular germ cells. Part 1: background to spermatogenesis, spermatogonia, and spermatocytes. Microsc Res Tech 2009; 73: 241-78.
    • (2009) Microsc Res Tech , vol.73 , pp. 241-278
    • Hermo, L.1    Pelletier, R.M.2    Cyr, D.G.3    Smith, C.E.4
  • 10
    • 77950953915 scopus 로고    scopus 로고
    • Surfing the wave, cycle, life history, and genes/proteins expressed by testicular germ cells Part 2: Changes in spermatid organelles associated with development of spermatozoa
    • Hermo L, Pelletier RM, Cyr DG, Smith CE. Surfing the wave, cycle, life history, and genes/proteins expressed by testicular germ cells. Part 2: changes in spermatid organelles associated with development of spermatozoa. Microsc Res Tech 2009; 73: 279-319.
    • (2009) Microsc Res Tech , vol.73 , pp. 279-319
    • Hermo, L.1    Pelletier, R.M.2    Cyr, D.G.3    Smith, C.E.4
  • 11
    • 77950949702 scopus 로고    scopus 로고
    • Surfing the wave, cycle, life history, and genes/proteins expressed by testicular germ cells Part 3: Developmental changes in spermatid flagellum and cytoplasmic droplet and interaction of sperm with the zona pellucida and egg plasma membrane
    • Hermo L, Pelletier RM, Cyr DG, Smith CE. Surfing the wave, cycle, life history, and genes/proteins expressed by testicular germ cells. Part 3: developmental changes in spermatid flagellum and cytoplasmic droplet and interaction of sperm with the zona pellucida and egg plasma membrane. Microsc Res Tech 2009; 73: 320-63.
    • (2009) Microsc Res Tech , vol.73 , pp. 320-363
    • Hermo, L.1    Pelletier, R.M.2    Cyr, D.G.3    Smith, C.E.4
  • 12
    • 77950920343 scopus 로고    scopus 로고
    • Surfing the wave, cycle, life history, and genes/proteins expressed by testicular germ cells Part 4: Intercellular bridges, mitochondria, nuclear envelope, apoptosis, ubiquitination, membrane/voltage-gated channels, methylation/acetylation, and transcription factors
    • Hermo L, Pelletier RM, Cyr DG, Smith CE. Surfing the wave, cycle, life history, and genes/proteins expressed by testicular germ cells. Part 4: intercellular bridges, mitochondria, nuclear envelope, apoptosis, ubiquitination, membrane/voltage-gated channels, methylation/acetylation, and transcription factors. Microsc Res Tech 2009; 73: 364-408.
    • (2009) Microsc Res Tech , vol.73 , pp. 364-408
    • Hermo, L.1    Pelletier, R.M.2    Cyr, D.G.3    Smith, C.E.4
  • 13
    • 77950934505 scopus 로고    scopus 로고
    • Surfing the wave, cycle, life history, and genes/proteins expressed by testicular germ cells Part 5: Intercellular junctions and contacts between germs cells and Sertoli cells and their regulatory interactions, testicular cholesterol, and genes/proteins associated with more than one germ cell generation
    • Hermo L, Pelletier RM, Cyr DG, Smith CE. Surfing the wave, cycle, life history, and genes/proteins expressed by testicular germ cells. Part 5: intercellular junctions and contacts between germs cells and Sertoli cells and their regulatory interactions, testicular cholesterol, and genes/proteins associated with more than one germ cell generation. Microsc Res Tech 2009; 73: 409-94.
    • (2009) Microsc Res Tech , vol.73 , pp. 409-494
    • Hermo, L.1    Pelletier, R.M.2    Cyr, D.G.3    Smith, C.E.4
  • 14
    • 78650973899 scopus 로고    scopus 로고
    • New insights into epididymal biology and function
    • Cornwall GA. New insights into epididymal biology and function. Hum Reprod Update 2009; 1: 1-15.
    • (2009) Hum Reprod Update , vol.1 , pp. 1-15
    • Cornwall, G.A.1
  • 15
    • 0009507838 scopus 로고
    • Morphological changes in rabbit spermatozoa during passage through the epididymis
    • Bedford JM. Morphological changes in rabbit spermatozoa during passage through the epididymis. J Reprod Fertil 1963; 5: 169-77.
    • (1963) J Reprod Fertil , vol.5 , pp. 169-177
    • Bedford, J.M.1
  • 16
    • 0013803771 scopus 로고
    • Changes in fine structure of the rabbit sperm head during passage through the epididymis
    • Bedford JM. Changes in fine structure of the rabbit sperm head during passage through the epididymis. J Anat 1965; 99: 891-906.
    • (1965) J Anat , vol.99 , pp. 891-906
    • Bedford, J.M.1
  • 17
    • 0015395723 scopus 로고
    • Development of the fertilizing ability of spermatozoa in the epididymis of the Syrian hamster
    • Horan AH, Bedford JM. Development of the fertilizing ability of spermatozoa in the epididymis of the Syrian hamster. J Reprod Fertil 1972; 30: 417-23.
    • (1972) J Reprod Fertil , vol.30 , pp. 417-423
    • Horan, A.H.1    Bedford, J.M.2
  • 18
    • 0019972335 scopus 로고
    • Development of the ability to bind to zonae pellucidae during epididymal maturation: Reversible immobilization of mouse-spermatozoa by lanthanum
    • Saling PM. Development of the ability to bind to zonae pellucidae during epididymal maturation: reversible immobilization of mouse-spermatozoa by lanthanum. Biol Reprod 1982; 26: 429-36.
    • (1982) Biol Reprod , vol.26 , pp. 429-436
    • Saling, P.M.1
  • 19
    • 0021337546 scopus 로고
    • Addition of androgens to cultured hamster epididymis increases zona recognition by immature spermatozoa
    • Cuasnicu PS, Gonzalez Echeverria F, Piazza A, Blaquier JA. Addition of androgens to cultured hamster epididymis increases zona recognition by immature spermatozoa. J Reprod Fertil 1984; 70: 541-7.
    • (1984) J Reprod Fertil , vol.70 , pp. 541-547
    • Cuasnicu, P.S.1    Gonzalez Echeverria, F.2    Piazza, A.3    Blaquier, J.A.4
  • 21
    • 0015730288 scopus 로고
    • Protein synthesis by isolated spermatozoa from cauda and caput epididymis of rat
    • Engel JC, Bernard EA, Wassermann GF. Protein synthesis by isolated spermatozoa from cauda and caput epididymis of rat. Acta Physiol Lat Am 1973; 23: 358-62.
    • (1973) Acta Physiol Lat Am , vol.23 , pp. 358-362
    • Engel, J.C.1    Bernard, E.A.2    Wassermann, G.F.3
  • 23
    • 34447266891 scopus 로고    scopus 로고
    • Supramolecular organization of the sperm plasma membrane during maturation and capacitation
    • Jones R, James PS, Howes L, Bruckbauer A, Klenerman D. Supramolecular organization of the sperm plasma membrane during maturation and capacitation. Asian J Androl 2007; 9: 438-44.
    • (2007) Asian J Androl , vol.9 , pp. 438-444
    • Jones, R.1    James, P.S.2    Howes, L.3    Bruckbauer, A.4    Klenerman, D.5
  • 24
    • 0021814123 scopus 로고
    • Changes in the lipid content of boar sperm plasma membranes during epididymal maturation
    • Nikolopoulou M, Soucek DA, Vary JC. Changes in the lipid content of boar sperm plasma membranes during epididymal maturation. Biochim Biophys Acta 1985; 815: 486-98.
    • (1985) Biochim Biophys Acta , vol.815 , pp. 486-498
    • Nikolopoulou, M.1    Soucek, D.A.2    Vary, J.C.3
  • 25
    • 0031451736 scopus 로고    scopus 로고
    • Changes in lipids and membrane anisotropy in human spermatozoa during epididymal maturation
    • Haidl G, Opper C. Changes in lipids and membrane anisotropy in human spermatozoa during epididymal maturation. Hum Reprod 1997; 12: 2720-3.
    • (1997) Hum Reprod , vol.12 , pp. 2720-2723
    • Haidl, G.1    Opper, C.2
  • 26
    • 34447268179 scopus 로고    scopus 로고
    • Proteomic changes in mammalian spermatozoa during epididymal maturation
    • Aitken RJ, Nixon B, Lin M, Koppers AJ, LeeYH et al. Proteomic changes in mammalian spermatozoa during epididymal maturation. Asian J Androl 2007; 9: 554-64.
    • (2007) Asian J Androl , vol.9 , pp. 554-564
    • Aitken, R.J.1    Nixon, B.2    Lin, M.3    Koppers, A.J.4    Lee, Y.H.5
  • 27
    • 0344766114 scopus 로고    scopus 로고
    • Hamster sperm antigen P26h is a phosphatidylinositol-anchored protein
    • Legare C, Berube B, Boue F, Lefievre L, Morales CRet al. Hamster sperm antigen P26h is a phosphatidylinositol-anchored protein. Mol Reprod Dev 1999; 52: 225-33.
    • (1999) Mol Reprod Dev , vol.52 , pp. 225-33
    • Legare, C.1    Berube, B.2    Boue, F.3    Lefievre, L.4    Morales, C.R.5
  • 28
    • 33748548424 scopus 로고    scopus 로고
    • Lipid remodeling of murine epididymosomes and spermatozoa during epididymal maturation
    • Rejraji H, Sion B, Prensier G, Carreras M, Motta C et al. Lipid remodeling of murine epididymosomes and spermatozoa during epididymal maturation. Biol Reprod 2006; 74: 1104-13.
    • (2006) Biol Reprod , vol.74 , pp. 1104-13
    • Rejraji, H.1    Sion, B.2    Prensier, G.3    Carreras, M.4    Motta, C.5
  • 29
    • 33751578251 scopus 로고    scopus 로고
    • Comparison between epididymosomes collected in the intraluminal compartment of the bovine caput and cauda epididymidis
    • Frenette G, Girouard J, Sullivan R. Comparison between epididymosomes collected in the intraluminal compartment of the bovine caput and cauda epididymidis. Biol Reprod 2006; 75: 885-90.
    • (2006) Biol Reprod , vol.75 , pp. 885-90
    • Frenette, G.1    Girouard, J.2    Sullivan, R.3
  • 30
    • 12344309010 scopus 로고    scopus 로고
    • Localization and significance of molecular chaperones, HSP1, and tumor rejection antigen gp96 in the male reproductive tract and during capacitation and acrosome reaction
    • Asquith KL, Harman AJ, McLaughlin EA, Nixon B, Aitken RJ. Localization and significance of molecular chaperones, HSP1, and tumor rejection antigen gp96 in the male reproductive tract and during capacitation and acrosome reaction. Biol Reprod 2005; 72: 328-37.
    • (2005) Biol Reprod , vol.72 , pp. 328-37
    • Asquith, K.L.1    Harman, A.J.2    McLaughlin, E.A.3    Nixon, B.4    Aitken, R.J.5
  • 31
    • 53049103504 scopus 로고    scopus 로고
    • Investigating the role of murine epididymosomes and uterosomes in GPI-linked protein transfer to sperm using SPAM1 as a model
    • Griffiths GS, Galileo DS, Reese K, Martin-Deleon PA. Investigating the role of murine epididymosomes and uterosomes in GPI-linked protein transfer to sperm using SPAM1 as a model. Mol Reprod Dev 2008; 75: 1627-36.
    • (2008) Mol Reprod Dev , vol.75 , pp. 1627-36
    • Griffiths, G.S.1    Galileo, D.S.2    Reese, K.3    Martin-Deleon, P.A.4
  • 32
    • 77950924660 scopus 로고    scopus 로고
    • Bactericidal/ permeability-increasing protein is associated with the acrosome region of rodent epididymal spermatozoa
    • Yano R, Matsuyama T, Kaneko T, Kurio H, Murayama E et al. Bactericidal/ permeability-increasing protein is associated with the acrosome region of rodent epididymal spermatozoa. J Androl 2010; 31: 201-14.
    • (2010) J Androl , Issue.31 , pp. 201-14
    • Yano, R.1    Matsuyama, T.2    Kaneko, T.3    Kurio, H.4    Murayama, E.5
  • 33
    • 76949114656 scopus 로고
    • Observations on the penetration of the sperm in the mammalian egg
    • Austin CR. Observations on the penetration of the sperm in the mammalian egg. Aust J Sci Res B 1951; 4: 581-96.
    • (1951) Aust J Sci Res B , vol.4 , pp. 581-96
    • Austin, C.R.1
  • 34
    • 36949091315 scopus 로고
    • Fertilizing capacity of spermatozoa deposited into the fallopian tubes
    • Chang MC. Fertilizing capacity of spermatozoa deposited into the fallopian tubes. Nature 1951; 168: 697-8.
    • (1951) Nature , vol.168 , pp. 697-8
    • Chang, M.C.1
  • 35
    • 0003178422 scopus 로고
    • The capacitation of the mammalian sperm
    • Austin CR. The capacitation of the mammalian sperm. Nature 1952; 170: 326.
    • (1952) Nature , vol.170 , pp. 326
    • Austin, C.R.1
  • 36
    • 0031890532 scopus 로고    scopus 로고
    • A novel signal transduction cascade in capacitating human spermatozoa characterised by a redox-regulated, cAMP-mediated induction of tyrosine phosphorylation
    • Aitken RJ, Harkiss D, Knox W, Paterson M, Irvine DS. A novel signal transduction cascade in capacitating human spermatozoa characterised by a redox-regulated, cAMP-mediated induction of tyrosine phosphorylation. J Cell Sci 1998; 111: 645-56.
    • (1998) J Cell Sci , vol.111 , pp. 645-56
    • Aitken, R.J.1    Harkiss, D.2    Knox, W.3    Paterson, M.4    Irvine, D.S.5
  • 37
    • 0034321639 scopus 로고    scopus 로고
    • Intracellular events and signaling pathways involved in sperm acquisition of fertilizing capacity and acrosome reaction
    • Baldi E, Luconi M, Bonaccorsi L, Muratori M, Forti G. Intracellular events and signaling pathways involved in sperm acquisition of fertilizing capacity and acrosome reaction. Front Biosci 2000; 5: E110-23.
    • (2000) Front Biosci , vol.5
    • Baldi, E.1    Luconi, M.2    Bonaccorsi, L.3    Muratori, M.4    Forti, G.5
  • 38
    • 0028957362 scopus 로고
    • Capacitation of mouse spermatozoa. I. Correlation between the capacitation state and protein tyrosine phosphorylation
    • Visconti PE, Bailey JL, Moore GD, Pan D, Olds-Clarke P et al. Capacitation of mouse spermatozoa. I. Correlation between the capacitation state and protein tyrosine phosphorylation. Development 1995; 121: 1129-37.
    • (1995) Development , vol.121 , pp. 1129-37
    • Visconti, P.E.1    Bailey, J.L.2    Moore, G.D.3    Pan, D.4    Olds-Clarke, P.5
  • 39
    • 34447635697 scopus 로고    scopus 로고
    • New insights into the molecular mechanisms of sperm-egg interaction
    • Nixon B, Aitken RJ, McLaughlin EA. New insights into the molecular mechanisms of sperm-egg interaction. Cell Mol Life Sci 2007; 64: 1805-23.
    • (2007) Cell Mol Life Sci , vol.64 , pp. 1805-23
    • Nixon, B.1    Aitken, R.J.2    McLaughlin, E.A.3
  • 40
    • 0342800102 scopus 로고
    • Timing of fertilization in mammals: Sperm cholesterol/phospholipid ratio as a determinant of the capacitation interval
    • Davis B. Timing of fertilization in mammals: sperm cholesterol/ phospholipid ratio as a determinant of the capacitation interval. Proc Natl Acad Sci USA 1981; 78: 7560-4.
    • (1981) Proc Natl Acad Sci USA , vol.78 , pp. 7560-4
    • Davis, B.1
  • 41
    • 0033570112 scopus 로고    scopus 로고
    • Cholesterol efflux-mediated signal transduction in mammalian sperm: Cholesterol release signals an increase in protein tyrosine phosphorylation during mouse sperm capacitation
    • Visconti PE, Ning X, Fornes MW, Alvarez JG, Stein P et al. Cholesterol efflux-mediated signal transduction in mammalian sperm: cholesterol release signals an increase in protein tyrosine phosphorylation during mouse sperm capacitation. Dev Biol 1999; 214: 429-43.
    • (1999) Dev Biol , vol.214 , pp. 429-43
    • Visconti, P.E.1    Ning, X.2    Fornes, M.W.3    Alvarez, J.G.4    Stein, P.5
  • 42
    • 0023774245 scopus 로고
    • Identification of sterol acceptors that stimulate cholesterol efflux from human spermatozoa during in vitro capacitation
    • Langlais J, Kan FW, Granger L, Raymond L, Bleau G et al. Identification of sterol acceptors that stimulate cholesterol efflux from human spermatozoa during in vitro capacitation. Gamete Res 1988; 20: 185-201.
    • (1988) Gamete Res , vol.20 , pp. 185-201
    • Langlais, J.1    Kan, F.W.2    Granger, L.3    Raymond, L.4    Bleau, G.5
  • 44
    • 0000320538 scopus 로고    scopus 로고
    • Membrane lipid dynamics during human sperm capacitation
    • Mart?́nez P, Morros A. Membrane lipid dynamics during human sperm capacitation. Front Biosci 1996; 1: d103-17.
    • (1996) Front Biosci , vol.1
    • Mart́nez, P.1    Morros, A.2
  • 45
    • 0022257352 scopus 로고
    • Sodium bicarbonate in seminal plasma stimulates the motility of mammalian spermatozoa through direct activation of adenylate cyclase
    • Okamura N, Tajima Y, Soejima A, Masuda H, Sugita Y. Sodium bicarbonate in seminal plasma stimulates the motility of mammalian spermatozoa through direct activation of adenylate cyclase. J Biol Chem 1985; 260: 9699-705.
    • (1985) J Biol Chem , vol.260 , pp. 9699-705
    • Okamura, N.1    Tajima, Y.2    Soejima, A.3    Masuda, H.4    Sugita, Y.5
  • 46
    • 0025854824 scopus 로고
    • Bicarbonate: Carbon-dioxide regulation of sperm capacitation, hyperactivated motility, and acrosome reactions
    • Boatman DE, Robbins RS. Bicarbonate: carbon-dioxide regulation of sperm capacitation, hyperactivated motility, and acrosome reactions. Biol Reprod 1991; 44: 806-13.
    • (1991) Biol Reprod , vol.44 , pp. 806-13
    • Boatman, D.E.1    Robbins, R.S.2
  • 47
    • 0023662356 scopus 로고
    • Stimulation of partially purified adenylate cyclase from bull sperm by bicarbonate
    • Garty NB, Salomon Y. Stimulation of partially purified adenylate cyclase from bull sperm by bicarbonate. FEBS Lett 1987; 218: 148-52.
    • (1987) FEBS Lett , vol.218 , pp. 148-52
    • Garty, N.B.1    Salomon, Y.2
  • 48
    • 0034725748 scopus 로고    scopus 로고
    • Soluble adenylyl cyclase as an evolutionarily conserved bicarbonate sensor
    • Chen Y, Cann MJ, Litvin TN, Iourgenko V, SinclairMLet al. Soluble adenylyl cyclase as an evolutionarily conserved bicarbonate sensor. Science 2000; 289: 625-8.
    • (2000) Science , vol.289 , pp. 625-8
    • Chen, Y.1    Cann, M.J.2    Litvin, T.N.3    Iourgenko, V.4    Sinclair, M.L.5
  • 49
    • 0034083188 scopus 로고    scopus 로고
    • The capacitating agent bicarbonate induces protein kinase A-dependent changes in phospholipid transbilayer behavior in the sperm plasma membrane
    • Gadella BM, Harrison RA. The capacitating agent bicarbonate induces protein kinase A-dependent changes in phospholipid transbilayer behavior in the sperm plasma membrane. Development 2000; 127: 2407-20.
    • (2000) Development , vol.127 , pp. 2407-20
    • Gadella, B.M.1    Harrison, R.A.2
  • 50
    • 0036082781 scopus 로고    scopus 로고
    • Capacitation induces cyclic adenosine 39, 59- monophosphate-dependent, but apoptosis-unrelated, exposure of aminophospholipids at the apical head plasma membrane of boar sperm cells
    • Gadella BM, Harrison RA. Capacitation induces cyclic adenosine 39, 59- monophosphate-dependent, but apoptosis-unrelated, exposure of aminophospholipids at the apical head plasma membrane of boar sperm cells. Biol Reprod 2002; 67: 340-50.
    • (2002) Biol Reprod , vol.67 , pp. 340-50
    • Gadella, B.M.1    Harrison, R.A.2
  • 51
    • 0034759226 scopus 로고    scopus 로고
    • Bicarbonate stimulated phospholipid scrambling induces cholesterol redistribution and enables cholesterol depletion in the sperm plasma membrane
    • Flesch FM, Brouwers JF, Nievelstein PF, Verkleij AJ, van Golde LM et al. Bicarbonate stimulated phospholipid scrambling induces cholesterol redistribution and enables cholesterol depletion in the sperm plasma membrane. J Cell Sci 2001; 114: 3543-55.
    • (2001) J Cell Sci , vol.114 , pp. 3543-55
    • Flesch, F.M.1    Brouwers, J.F.2    Nievelstein, P.F.3    Verkleij, A.J.4    Van Golde, L.M.5
  • 52
    • 11144282376 scopus 로고    scopus 로고
    • Bicarbonate-induced membrane processing in sperm capacitation
    • Harrison AP. Bicarbonate-induced membrane processing in sperm capacitation. Theriogenology 2005; 63: 342-51.
    • (2005) Theriogenology , vol.63 , pp. 342-51
    • Harrison, A.P.1
  • 53
    • 0021709251 scopus 로고
    • Mouse sperm capacitation in vitro involves loss of a surface-associated inhibitory component
    • Fraser LR. Mouse sperm capacitation in vitro involves loss of a surface-associated inhibitory component. J Reprod Fertil 1984; 72: 373-84.
    • (1984) J Reprod Fertil , vol.72 , pp. 373-84
    • Fraser, L.R.1
  • 54
    • 69749125786 scopus 로고    scopus 로고
    • HongrES1, a cauda epididymis-specific protein, is involved in capacitation of guinea pig sperm
    • Ni Y, Zhou Y, Chen WY, Zheng M, Yu J et al. HongrES1, a cauda epididymis-specific protein, is involved in capacitation of guinea pig sperm. Mol Reprod Dev 2009; 76: 984-93.
    • (2009) Mol Reprod Dev , vol.76 , pp. 984-93
    • Ni, Y.1    Zhou, Y.2    Chen, W.Y.3    Zheng, M.4    Yu, J.5
  • 55
    • 0031692764 scopus 로고    scopus 로고
    • Interactions between a decapacitation factor and mouse spermatozoa appear to involve fucose residues and a GPI-anchored receptor
    • Fraser LR. Interactions between a decapacitation factor and mouse spermatozoa appear to involve fucose residues and a GPI-anchored receptor. Mol Reprod Dev 1998; 51: 193-202.
    • (1998) Mol Reprod Dev , vol.51 , pp. 193-202
    • Fraser, L.R.1
  • 56
    • 26944457328 scopus 로고    scopus 로고
    • A mouse sperm decapacitation factor receptor is phosphatidylethanolamine- binding protein 1
    • Gibbons R, Adeoya-Osiguwa SA, Fraser LR. A mouse sperm decapacitation factor receptor is phosphatidylethanolamine-binding protein 1. Reproduction 2005; 130: 497-508.
    • (2005) Reproduction , vol.130 , pp. 497-508
    • Gibbons, R.1    Adeoya-Osiguwa, S.A.2    Fraser, L.R.3
  • 57
    • 69249212536 scopus 로고    scopus 로고
    • NYD-SP27 a novel intrinsic decapacitation factor in sperm
    • Bi Y, Xu WM, Wong HY, Zhu H, Zhou ZM et al. NYD-SP27, a novel intrinsic decapacitation factor in sperm. Asian J Androl 2009; 11: 229-39.
    • (2009) Asian J Androl , vol.11 , pp. 229-39
    • Bi, Y.1    Xu, W.M.2    Wong, H.Y.3    Zhu, H.4    Zhou, Z.M.5
  • 58
    • 33746085241 scopus 로고    scopus 로고
    • Rafts defined: A report on the keystone symposium on lipid rafts and cell function
    • Pike LJ. Rafts defined: a report on the keystone symposium on lipid rafts and cell function. J Lipid Res 2006; 47: 1597-8.
    • (2006) J Lipid Res , vol.47 , pp. 1597-8
    • Pike, L.J.1
  • 59
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons K, Ikonen E. Functional rafts in cell membranes. Nature 1997; 387: 569-72.
    • (1997) Nature , vol.387 , pp. 569-72
    • Simons, K.1    Ikonen, E.2
  • 60
    • 0034304851 scopus 로고    scopus 로고
    • Lipid rafts and signal transduction
    • Simons K, Toomre D. Lipid rafts and signal transduction. Nat Rev Mol Cell Biol 2000; 1: 31-9.
    • (2000) Nat Rev Mol Cell Biol , vol.1 , pp. 31-9
    • Simons, K.1    Toomre, D.2
  • 61
    • 0032421354 scopus 로고    scopus 로고
    • Functions of lipid rafts in biological membranes
    • Brown DA, London E. Functions of lipid rafts in biological membranes. Annu Rev Cell Dev Biol 1998; 14: 111-36.
    • (1998) Annu Rev Cell Dev Biol , vol.14 , pp. 111-36
    • Brown, D.A.1    London, E.2
  • 62
    • 0034625373 scopus 로고    scopus 로고
    • Structure and function of sphingolipid- and cholesterol-rich membrane rafts
    • Brown DA, London E. Structure and function of sphingolipid- and cholesterol-rich membrane rafts. J Biol Chem 2000; 275: 17221-4.
    • (2000) J Biol Chem , vol.275 , pp. 17221-4
    • Brown, D.A.1    London, E.2
  • 64
    • 0025653671 scopus 로고
    • Regulation of mammalian fertilization by zona pellucida glycoproteins
    • Wassarman PM. Regulation of mammalian fertilization by zona pellucida glycoproteins. J Reprod Fertil Suppl 1990; 42: 79-87.
    • (1990) J Reprod Fertil Suppl , vol.42 , pp. 79-87
    • Wassarman, P.M.1
  • 65
    • 0028535827 scopus 로고
    • Fertility of mammalian spermatozoa: Its development and relativity
    • Yanagimachi R. Fertility of mammalian spermatozoa: its development and relativity. Zygote 1994; 2: 371-2.
    • (1994) Zygote , vol.2 , pp. 371-2
    • Yanagimachi, R.1
  • 66
    • 54249138250 scopus 로고    scopus 로고
    • Mammalian fertilization: The eggs multifunctional zona pellucida
    • Wassarman PM, Litscher ES. Mammalian fertilization: the eggs multifunctional zona pellucida. Int J Dev Biol 2008; 52: 665-76.
    • (2008) Int J Dev Biol , vol.52 , pp. 665-76
    • Wassarman, P.M.1    Litscher, E.S.2
  • 70
    • 43249100861 scopus 로고    scopus 로고
    • Phylogenetic analysis and identification of pseudogenes reveal a progressive loss of zona pellucida genes during evolution of vertebrates
    • Goudet G, Mugnier S, Callebaut I, Monget P. Phylogenetic analysis and identification of pseudogenes reveal a progressive loss of zona pellucida genes during evolution of vertebrates. Biol Reprod 2008; 78: 796-806.
    • (2008) Biol Reprod , vol.78 , pp. 796-806
    • Goudet, G.1    Mugnier, S.2    Callebaut, I.3    Monget, P.4
  • 71
    • 0022429080 scopus 로고
    • Mouse egg extracellular coat is a matrix of interconnected filaments possessing a structural repeat
    • Greve J, Wassarman P. Mouse egg extracellular coat is a matrix of interconnected filaments possessing a structural repeat. J Mol Biol 1985; 181: 253-64.
    • (1985) J Mol Biol , vol.181 , pp. 253-64
    • Greve, J.1    Wassarman, P.2
  • 72
    • 0026334512 scopus 로고
    • Structure of the mouse egg extracellular coat, the zona pellucida
    • Wassarman P, Mortillo S. Structure of the mouse egg extracellular coat, the zona pellucida. Int Rev Cytol 1991: 85-109.
    • (1991) Int Rev Cytol , pp. 85-109
    • Wassarman, P.1    Mortillo, S.2
  • 73
    • 0029055225 scopus 로고
    • The complexities of conception
    • Aitken R. The complexities of conception. Science 1995; 269: 39-40.
    • (1995) Science , vol.269 , pp. 39-40
    • Aitken, R.1
  • 74
    • 0018831516 scopus 로고
    • Mammalian sperm-egg interaction: Identification of a glycoprotein in mouse egg zonae pellucidae possessing receptor activity for sperm
    • Bleil JD, Wassarman PM. Mammalian sperm-egg interaction: identification of a glycoprotein in mouse egg zonae pellucidae possessing receptor activity for sperm. Cell 1980; 20: 873-82.
    • (1980) Cell , vol.20 , pp. 873-82
    • Bleil, J.D.1    Wassarman, P.M.2
  • 75
    • 0018822414 scopus 로고
    • Structure and function of the zona pellucida: Identification and characterization of the proteins of the mouse oocytes zona pellucida
    • Bleil J, Wassarman P. Structure and function of the zona pellucida: identification and characterization of the proteins of the mouse oocytes zona pellucida. Dev Biol 1980; 76: 185-202.
    • (1980) Dev Biol , vol.76 , pp. 185-202
    • Bleil, J.1    Wassarman, P.2
  • 76
    • 0024642651 scopus 로고
    • Interaction of mouse sperm with purified sperm receptors covalently linked to silica beads
    • Vazquez M, Phillips D, Wassarman P. Interaction of mouse sperm with purified sperm receptors covalently linked to silica beads. J Cell Sci 1989; 92: 713-22.
    • (1989) J Cell Sci , vol.92 , pp. 713-22
    • Vazquez, M.1    Phillips, D.2    Wassarman, P.3
  • 77
    • 0021710179 scopus 로고
    • Enzymatic dissection of the functions of the mouse eggs receptor for sperm
    • Florman H, Bechtol K, Wassarman P. Enzymatic dissection of the functions of the mouse eggs receptor for sperm. Dev Biol 1984; 106: 243-55.
    • (1984) Dev Biol , vol.106 , pp. 243-55
    • Florman, H.1    Bechtol, K.2    Wassarman, P.3
  • 78
    • 0025785915 scopus 로고
    • Differential binding of gold-labeled zona pellucida glycoproteins mZP2 and mZP3 to mouse sperm membrane compartments
    • Mortillo S, Wassarman P. Differential binding of gold-labeled zona pellucida glycoproteins mZP2 and mZP3 to mouse sperm membrane compartments. Development 1991; 113: 141.
    • (1991) Development , vol.113 , pp. 141
    • Mortillo, S.1    Wassarman, P.2
  • 79
    • 9344231925 scopus 로고    scopus 로고
    • Targeted disruption of the mZP3 gene results in production of eggs lacking a zona pellucida and infertility in female mice
    • Liu C, Litscher ES, Mortillo S, Sakai Y, Kinloch RA et al. Targeted disruption of the mZP3 gene results in production of eggs lacking a zona pellucida and infertility in female mice. Proc Natl Acad Sci USA 1996; 93: 5431-6.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 5431-6
    • Liu, C.1    Litscher, E.S.2    Mortillo, S.3    Sakai, Y.4    Kinloch, R.A.5
  • 80
    • 0017352879 scopus 로고
    • Receptor activity of the hamster and mouse solubilized zona pellucida before and after the zona reaction
    • Gwatkin R, Williams D. Receptor activity of the hamster and mouse solubilized zona pellucida before and after the zona reaction. Reproduction 1977; 49: 55-9.
    • (1977) Reproduction , vol.49 , pp. 55-9
    • Gwatkin, R.1    Williams, D.2
  • 81
    • 1842843784 scopus 로고    scopus 로고
    • Insights into the molecular basis of sperm-egg recognition in mammals
    • Hoodbhoy T, Dean J. Insights into the molecular basis of sperm-egg recognition in mammals. Reproduction 2004; 127: 417-22.
    • (2004) Reproduction , vol.127 , pp. 417-22
    • Hoodbhoy, T.1    Dean, J.2
  • 82
    • 0015948215 scopus 로고
    • Inhibition of hamster fertilization by phytoagglutinins
    • Oikawa T, Nicolson G, Yanagimachi R. Inhibition of hamster fertilization by phytoagglutinins. Exp Cell Res 1974; 83: 239-46.
    • (1974) Exp Cell Res , vol.83 , pp. 239-46
    • Oikawa, T.1    Nicolson, G.2    Yanagimachi, R.3
  • 83
    • 0024381288 scopus 로고
    • Significance of D-mannose as a sperm receptor site on the zona pellucida in human fertilization
    • Mori K, Daitoh T, Irahara M, Kamada M, Aono T. Significance of D-mannose as a sperm receptor site on the zona pellucida in human fertilization. Am J Obstet Gynecol 1989; 161: 207-11.
    • (1989) Am J Obstet Gynecol , vol.161 , pp. 207-11
    • Mori, K.1    Daitoh, T.2    Irahara, M.3    Kamada, M.4    Aono, T.5
  • 84
    • 0019969344 scopus 로고
    • Evidence suggesting that L-fucose is part of a recognition signal for sperm-zona pellucida attachment in mammals
    • Huang TT, Ohzu E, Yanagimachi R. Evidence suggesting that L-fucose is part of a recognition signal for sperm-zona pellucida attachment in mammals. Gamete Res 1982; 5: 355-61.
    • (1982) Gamete Res , vol.5 , pp. 355-61
    • Huang, T.T.1    Ohzu, E.2    Yanagimachi, R.3
  • 85
    • 0020410869 scopus 로고
    • A role for mouse sperm surface galactosyltransferase in sperm binding to the egg zona pellucida
    • Shur BD, Hall NG. A role for mouse sperm surface galactosyltransferase in sperm binding to the egg zona pellucida. J Cell Biol 1982; 95: 574-9.
    • (1982) J Cell Biol , vol.95 , pp. 574-9
    • Shur, B.D.1    Hall, N.G.2
  • 86
    • 0022618897 scopus 로고
    • The role of carbohydrates in sperm-egg interaction in rats
    • Shalgi R, Matityahu A, Nebel L. The role of carbohydrates in sperm-egg interaction in rats. Biol Reprod 1986; 34: 446-52.
    • (1986) Biol Reprod , vol.34 , pp. 446-52
    • Shalgi, R.1    Matityahu, A.2    Nebel, L.3
  • 87
    • 0025190765 scopus 로고
    • Antagonistic and agonistic properties of saccharide moieties in the hemizona assay
    • Oehninger S, Acosta A, Hodgen G. Antagonistic and agonistic properties of saccharide moieties in the hemizona assay. Fertil Steril 1990; 53: 143.
    • (1990) Fertil Steril , vol.53 , pp. 143
    • Oehninger, S.1    Acosta, A.2    Hodgen, G.3
  • 88
    • 0022272133 scopus 로고
    • Involvement of sperm sulphatases in early sperm-zona interactions in the hamster
    • Ahuja K, Gilburt D. Involvement of sperm sulphatases in early sperm-zona interactions in the hamster. J Cell Sci 1985; 78: 247-61.
    • (1985) J Cell Sci , vol.78 , pp. 247-61
    • Ahuja, K.1    Gilburt, D.2
  • 89
    • 0025967952 scopus 로고
    • Nature of the inhibitory effect of complex saccharide moieties on the tight binding of human spermatozoa to the human zona pellucida
    • Oehninger S, Clark GF, Acosta AA, Hodgen GD. Nature of the inhibitory effect of complex saccharide moieties on the tight binding of human spermatozoa to the human zona pellucida. Fertil Steril 1991; 55: 165-9.
    • (1991) Fertil Steril , vol.55 , pp. 165-9
    • Oehninger, S.1    Clark, G.F.2    Acosta, A.A.3    Hodgen, G.D.4
  • 90
    • 0032568506 scopus 로고    scopus 로고
    • Inactivation of the mouse sperm receptor, mZP3, by site-directed mutagenesis of individual serine residues located at the combining site for sperm
    • Chen J, Litscher ES, Wassarman PM. Inactivation of the mouse sperm receptor, mZP3, by site-directed mutagenesis of individual serine residues located at the combining site for sperm. Proc Natl Acad Sci USA 1998; 95: 6193-7.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 6193-7
    • Chen, J.1    Litscher, E.S.2    Wassarman, P.M.3
  • 91
    • 0021874149 scopus 로고
    • O-linked oligosaccharides of mouse egg ZP3 account for its sperm receptor activity
    • Florman HM, Wassarman PM. O-linked oligosaccharides of mouse egg ZP3 account for its sperm receptor activity. Cell 1985; 41: 313-24.
    • (1985) Cell , vol.41 , pp. 313-24
    • Florman, H.M.1    Wassarman, P.M.2
  • 92
    • 0029946034 scopus 로고    scopus 로고
    • Characterization of a mouse ZP3-derived glycopeptide, gp55, that exhibits sperm receptor and acrosome reaction-inducing activity in vitro
    • Litscher ES, Wassarman PM. Characterization of a mouse ZP3-derived glycopeptide, gp55, that exhibits sperm receptor and acrosome reaction-inducing activity in vitro. Biochemistry 1996; 35: 3980-5.
    • (1996) Biochemistry , vol.35 , pp. 3980-5
    • Litscher, E.S.1    Wassarman, P.M.2
  • 93
    • 0028902581 scopus 로고
    • Oligosaccharide constructs with defined structures that inhibit binding of mouse sperm to unfertilized eggs in vitro
    • Litscher ES, Juntunen K, Seppo A, Penttila L, Niemela R et al. Oligosaccharide constructs with defined structures that inhibit binding of mouse sperm to unfertilized eggs in vitro. Biochemistry (Mosc) 1995; 34: 4662-9.
    • (1995) Biochemistry (Mosc) , vol.34 , pp. 4662-9
    • Litscher, E.S.1    Juntunen, K.2    Seppo, A.3    Penttila, L.4    Niemela, R.5
  • 94
    • 0026439753 scopus 로고
    • Identification of a region of mouse zona pellucida glycoprotein mZP3 that possesses sperm receptor activity
    • Rosiere T, Wassarman P. Identification of a region of mouse zona pellucida glycoprotein mZP3 that possesses sperm receptor activity. Dev Biol 1992; 154: 309-17.
    • (1992) Dev Biol , vol.154 , pp. 309-317
    • Rosiere, T.1    Wassarman, P.2
  • 96
    • 0032428668 scopus 로고    scopus 로고
    • Core 2 oligosaccharide biosynthesis distinguishes between selectin ligands essential for leukocyte homing and inflammation
    • Ellies LG, Tsuboi S, Petryniak B, Lowe JB, Fukuda M et al. Core 2 oligosaccharide biosynthesis distinguishes between selectin ligands essential for leukocyte homing and inflammation. Immunity 1998; 9: 881-90.
    • (1998) Immunity , vol.9 , pp. 881-90
    • Ellies, L.G.1    Tsuboi, S.2    Petryniak, B.3    Lowe, J.B.4    Fukuda, M.5
  • 97
    • 67650069705 scopus 로고    scopus 로고
    • Glycosyltransferase function in core 2-type protein O glycosylation
    • Stone EL, Ismail MN, Lee SH, Luu Y, Ramirez K et al. Glycosyltransferase function in core 2-type protein O glycosylation. Mol Cell Biol 2009; 29: 3770-82.
    • (2009) Mol Cell Biol , vol.29 , pp. 3770-82
    • Stone, E.L.1    Ismail, M.N.2    Lee, S.H.3    Luu, Y.4    Ramirez, K.5
  • 98
    • 7644233735 scopus 로고    scopus 로고
    • Inactivation of the Mgat1 gene in oocytes impairs oogenesis, but embryos lacking complex and hybrid N-glycans develop and implant
    • Shi S, Williams SA, Seppo A, Kurniawan H, Chen W et al. Inactivation of the Mgat1 gene in oocytes impairs oogenesis, but embryos lacking complex and hybrid N-glycans develop and implant. Mol Cell Biol 2004; 24: 9920-9.
    • (2004) Mol Cell Biol , vol.24 , pp. 9920-9
    • Shi, S.1    Williams, S.A.2    Seppo, A.3    Kurniawan, H.4    Chen, W.5
  • 99
    • 0028877229 scopus 로고
    • Involvement of N-linked carbohydrate chains of pig zona pellucida in sperm-egg binding
    • Yonezawa N, Aoki H, Hatanaka Y, Nakano M. Involvement of N-linked carbohydrate chains of pig zona pellucida in sperm-egg binding. Eur J Biochem 1995; 233: 35-41.
    • (1995) Eur J Biochem , vol.233 , pp. 35-41
    • Yonezawa, N.1    Aoki, H.2    Hatanaka, Y.3    Nakano, M.4
  • 100
    • 0030333226 scopus 로고    scopus 로고
    • Structure and function of the Nlinked carbohydrate chains of pig zona pellucida glycoproteins
    • Nakano M, Yonezawa N, Hatanaka Y, Noguchi S. Structure and function of the Nlinked carbohydrate chains of pig zona pellucida glycoproteins. J Reprod Fertil Suppl 1996; 50: 25-34.
    • (1996) J Reprod Fertil Suppl , vol.50 , pp. 25-34
    • Nakano, M.1    Yonezawa, N.2    Hatanaka, Y.3    Noguchi, S.4
  • 101
    • 55549122993 scopus 로고    scopus 로고
    • Effects of native human zona pellucida glycoproteins 3 and 4 on acrosome reaction and zona pellucida binding of human spermatozoa
    • Chiu PC, Wong BS, Chung MK, Lam KK, Pang RT et al. Effects of native human zona pellucida glycoproteins 3 and 4 on acrosome reaction and zona pellucida binding of human spermatozoa. Biol Reprod 2008; 79: 869-77.
    • (2008) Biol Reprod , vol.79 , pp. 869-77
    • Chiu, P.C.1    Wong, B.S.2    Chung, M.K.3    Lam, K.K.4    Pang, R.T.5
  • 102
    • 0032030791 scopus 로고    scopus 로고
    • The polypeptide backbone of recombinant human zona pellucida glycoprotein-3 initiates acrosomal exocytosis in human spermatozoa in vitro
    • Chapman N, Kessopoulou E, Andrews P, Hornby D, Barratt CR. The polypeptide backbone of recombinant human zona pellucida glycoprotein-3 initiates acrosomal exocytosis in human spermatozoa in vitro. Biochem J 1998; 330 (Pt 2): 839-45.
    • (1998) Biochem J , vol.330 , Issue.PART 2 , pp. 839-45
    • Chapman, N.1    Kessopoulou, E.2    Andrews, P.3    Hornby, D.4    Barratt, C.R.5
  • 103
    • 14744281877 scopus 로고    scopus 로고
    • A synthetic decapeptide from a conserved ZP3 protein domain induces the G protein-regulated acrosome reaction in bovine spermatozoa
    • Hinsch E, Aires VA, Hedrich F, Oehninger S, Hinsch KD. A synthetic decapeptide from a conserved ZP3 protein domain induces the G protein-regulated acrosome reaction in bovine spermatozoa. Theriogenology 2005; 63: 1682-94.
    • (2005) Theriogenology , vol.63 , pp. 1682-94
    • Hinsch, E.1    Aires, V.A.2    Hedrich, F.3    Oehninger, S.4    Hinsch, K.D.5
  • 104
    • 0347004637 scopus 로고    scopus 로고
    • Reassessing the molecular biology of sperm-egg recognition with mouse genetics
    • Dean J. Reassessing the molecular biology of sperm-egg recognition with mouse genetics. Bioessays 2004; 26: 29-38.
    • (2004) Bioessays , vol.26 , pp. 29-38
    • Dean, J.1
  • 105
    • 33644844770 scopus 로고    scopus 로고
    • Molecular biology of sperm-egg interactions
    • Dean J. Molecular biology of sperm-egg interactions. Andrologia 2005; 37: 198-9.
    • (2005) Andrologia , vol.37 , pp. 198-9
    • Dean, J.1
  • 106
    • 1242307299 scopus 로고    scopus 로고
    • Characterization of a novel ZP3-independent sperm-binding ligand that facilitates sperm adhesion to the egg coat
    • Rodeheffer C, Shur BD. Characterization of a novel ZP3-independent sperm-binding ligand that facilitates sperm adhesion to the egg coat. Development 2004; 131: 503-12.
    • (2004) Development , vol.131 , pp. 503-12
    • Rodeheffer, C.1    Shur, B.D.2
  • 107
    • 70450269238 scopus 로고    scopus 로고
    • Mouse oviduct-specific glycoprotein is an egg-associated ZP3- independent sperm-adhesion ligand
    • Lyng R, Shur BD. Mouse oviduct-specific glycoprotein is an egg-associated ZP3- independent sperm-adhesion ligand. J Cell Sci 2009; 122: 3894-906.
    • (2009) J Cell Sci , vol.122 , pp. 3894-906
    • Lyng, R.1    Shur, B.D.2
  • 108
    • 0026611050 scopus 로고
    • Complementarity between sperm surface beta-1,4- galactosyltransferase and egg-coat ZP3 mediates sperm-egg binding
    • Miller DJ, Macek MB, Shur BD. Complementarity between sperm surface beta-1,4- galactosyltransferase and egg-coat ZP3 mediates sperm-egg binding. Nature 1992; 357: 589-93.
    • (1992) Nature , vol.357 , pp. 589-93
    • Miller, D.J.1    MacEk, M.B.2    Shur, B.D.3
  • 109
    • 0024297290 scopus 로고
    • Plasma membrane association, purification, and partial characterization of mouse sperm beta 1,4-galactosyltransferase
    • Shur BD, Neely CA. Plasma membrane association, purification, and partial characterization of mouse sperm beta 1,4-galactosyltransferase. J Biol Chem 1988; 263: 17706-14.
    • (1988) J Biol Chem , vol.263 , pp. 17706-14
    • Shur, B.D.1    Neely, C.A.2
  • 110
    • 0029094342 scopus 로고
    • Activation of a G protein complex by aggregation of beta-1,4- galactosyltransferase on the surface of sperm
    • Gong X, Dubois DH, Miller DJ, Shur BD. Activation of a G protein complex by aggregation of beta-1,4-galactosyltransferase on the surface of sperm. Science 1995; 269: 1718-21.
    • (1995) Science , vol.269 , pp. 1718-21
    • Gong, X.1    Dubois, D.H.2    Miller, D.J.3    Shur, B.D.4
  • 111
    • 33846828527 scopus 로고    scopus 로고
    • SeppalaMet al. Glycodelin-A interacts with fucosyltransferase on human sperm plasma membrane to inhibit spermatozoa- zona pellucida binding
    • Chiu PC, Chung MK, Koistinen R, Koistinen H, SeppalaMet al. Glycodelin-A interacts with fucosyltransferase on human sperm plasma membrane to inhibit spermatozoa- zona pellucida binding. J Cell Sci 2007; 120: 33-44.
    • (2007) J Cell Sci , vol.120 , pp. 33-44
    • Chiu, P.C.1    Chung, M.K.2    Koistinen, R.3    Koistinen, H.4
  • 112
    • 0025801542 scopus 로고
    • Inhibition of the mouse sperm surface alpha- D-mannosidase inhibits sperm-egg binding in vitro
    • Cornwall G, Tulsiani D, Orgebin-Crist M. Inhibition of the mouse sperm surface alpha- D-mannosidase inhibits sperm-egg binding in vitro. Biol Reprod 1991; 44: 913-21.
    • (1991) Biol Reprod , vol.44 , pp. 913-21
    • Cornwall, G.1    Tulsiani, D.2    Orgebin-Crist, M.3
  • 113
    • 0030728461 scopus 로고    scopus 로고
    • Sperm from beta 1,4-galactosyltransferase-null mice are refractory to ZP3-induced acrosome reactions and penetrate the zona pellucida poorly
    • Lu Q, Shur BD. Sperm from beta 1,4-galactosyltransferase-null mice are refractory to ZP3-induced acrosome reactions and penetrate the zona pellucida poorly. Development 1997; 124: 4121-31.
    • (1997) Development , vol.124 , pp. 4121-31
    • Lu, Q.1    Shur, B.D.2
  • 114
    • 0023718418 scopus 로고
    • Characterization of the rabbit sperm membrane autoantigen, RSA, as a lectin-like zona binding protein
    • ORand MG, Widgren EE, Fisher SJ. Characterization of the rabbit sperm membrane autoantigen, RSA, as a lectin-like zona binding protein. Dev Biol 1988; 129: 231-40.
    • (1988) Dev Biol , vol.129 , pp. 231-40
    • Orand, M.G.1    Widgren, E.E.2    Fisher, S.J.3
  • 115
    • 0025075878 scopus 로고
    • Identification of a ZP3-binding protein on acrosomeintact mouse sperm by photoaffinity crosslinking
    • Bleil JD, Wassarman PM. Identification of a ZP3-binding protein on acrosomeintact mouse sperm by photoaffinity crosslinking. Proc Natl Acad Sci USA 1990; 87: 5563-7.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 5563-7
    • Bleil, J.D.1    Wassarman, P.M.2
  • 116
    • 0343435291 scopus 로고
    • Galactose at the nonreducing terminus of O-linked oligosaccharides of mouse egg zona pellucida glycoprotein ZP3 is essential for the glycoproteins sperm receptor activity
    • Bleil J, Wassarman P. Galactose at the nonreducing terminus of O-linked oligosaccharides of mouse egg zona pellucida glycoprotein ZP3 is essential for the glycoproteins sperm receptor activity. Proc Natl Acad Sci USA 1988; 85: 6778-82.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 6778-82
    • Bleil, J.1    Wassarman, P.2
  • 117
    • 45549097542 scopus 로고    scopus 로고
    • Recombinant mouse sperm ZP3- binding protein (ZP3R/sp56) forms a high order oligomer that binds eggs and inhibits mouse fertilization in vitro
    • Buffone MG, Zhuang T, Ord TS, Hui L, Moss SB et al. Recombinant mouse sperm ZP3- binding protein (ZP3R/sp56) forms a high order oligomer that binds eggs and inhibits mouse fertilization in vitro. J Biol Chem 2008; 283: 12438-45.
    • (2008) J Biol Chem , vol.283 , pp. 12438-45
    • Buffone, M.G.1    Zhuang, T.2    Ord, T.S.3    Hui, L.4    Moss, S.B.5
  • 118
    • 0028227343 scopus 로고
    • Sperm-egg recognition in the mouse: Characterization of sp56, a sperm protein having specific affinity for ZP3
    • Cheng A, Le T, Palacios M, Bookbinder LH, Wassarman PM et al. Sperm-egg recognition in the mouse: characterization of sp56, a sperm protein having specific affinity for ZP3. J Cell Biol 1994; 125: 867-78.
    • (1994) J Cell Biol , vol.125 , pp. 867-78
    • Cheng, A.1    Le Palacios, T.M.2    Bookbinder, L.H.3    Wassarman, P.M.4
  • 119
    • 0035168574 scopus 로고    scopus 로고
    • Mouse sperm protein sp56 is a component of the acrosomal matrix
    • Kim KS, Cha MC, Gerton GL. Mouse sperm protein sp56 is a component of the acrosomal matrix. Biol Reprod 2001; 64: 36-43.
    • (2001) Biol Reprod , vol.64 , pp. 36-43
    • Kim, K.S.1    Cha, M.C.2    Gerton, G.L.3
  • 120
    • 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 et al. 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. J Biol Chem 1997; 272: 12714-22.
    • (1997) J Biol Chem , vol.272 , pp. 12714-22
    • Foster, J.A.1    Friday, B.B.2    Maulit, M.T.3    Blobel, C.4    Winfrey, V.P.5
  • 121
    • 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. Differential release of soluble and matrix components: evidence for intermediate states of secretion during spontaneous acrosomal exocytosis in mouse sperm. Dev Biol 2003; 264: 141-52.
    • (2003) Dev Biol , vol.264 , pp. 141-52
    • Kim, K.S.1    Gerton, G.L.2
  • 122
    • 1542284264 scopus 로고    scopus 로고
    • Is sperm capacitation analogous to early phases of Ca21- triggered membrane fusion in somatic cells and viruses?
    • Tulsiani DRP, Abou-Haila A. Is sperm capacitation analogous to early phases of Ca21- triggered membrane fusion in somatic cells and viruses? Bioessays 2004; 26: 281-90.
    • (2004) Bioessays , vol.26 , pp. 281-90
    • Drp, T.1    Abou-Haila, A.2
  • 123
    • 0037378638 scopus 로고    scopus 로고
    • Disruption of mouse CD46 causes an accelerated spontaneous acrosome reaction in sperm
    • Inoue N, Ikawa M, Nakanishi T, Matsumoto M, Nomura M et al. Disruption of mouse CD46 causes an accelerated spontaneous acrosome reaction in sperm. Mol Cell Biol 2003; 23: 2614-22.
    • (2003) Mol Cell Biol , vol.23 , pp. 2614-22
    • Inoue, N.1    Ikawa, M.2    Nakanishi, T.3    Matsumoto, M.4    Nomura, M.5
  • 124
    • 0032544623 scopus 로고    scopus 로고
    • Fertilization defects in sperm from mice lacking fertilin beta
    • Cho C, ODell Bunch D, Faure JE, Goulding EH, Eddy EM et al. Fertilization defects in sperm from mice lacking fertilin beta. Science 1998; 281: 1857-9.
    • (1998) Science , vol.281 , pp. 1857-9
    • Cho, C.1    Odell Bunch, D.2    Faure, J.E.3    Goulding, E.H.4    Eddy, E.M.5
  • 125
    • 0043029287 scopus 로고    scopus 로고
    • Identification of mouse sperm SED1, a bimotif EGF repeat and discoidin-domain protein involved in sperm-egg binding
    • Ensslin MA, Shur BD. Identification of mouse sperm SED1, a bimotif EGF repeat and discoidin-domain protein involved in sperm-egg binding. Cell 2003; 114: 405-17.
    • (2003) Cell , vol.114 , pp. 405-17
    • Ensslin, M.A.1    Shur, B.D.2
  • 127
    • 0036086126 scopus 로고    scopus 로고
    • Arylsulfatase A is present on the pig sperm surface and is involved in sperm-zona pellucida binding
    • Carmona E, Weerachatyanukul W, Soboloff T, Fluharty A, White Det al. Arylsulfatase A is present on the pig sperm surface and is involved in sperm-zona pellucida binding. Dev Biol 2002; 247: 182-96.
    • (2002) Dev Biol , vol.247 , pp. 182-96
    • Carmona, E.1    Weerachatyanukul, W.2    Soboloff, T.3    Fluharty, A.4    White, D.5
  • 129
    • 0024439966 scopus 로고
    • Novel alpha-D-mannosidase of rat sperm plasma membranes: Characterization and potential role in sperm-egg interactions
    • Tulsiani D, Skudlarek M, Orgebin-Crist M. Novel alpha-D-mannosidase of rat sperm plasma membranes: characterization and potential role in sperm-egg interactions. J Cell Biol 1989; 109: 1257-67.
    • (1989) J Cell Biol , vol.109 , pp. 1257-67
    • Tulsiani, D.1    Skudlarek, M.2    Orgebin-Crist, M.3
  • 130
    • 0025327871 scopus 로고
    • Human sperm plasma membranes possess alpha-D-mannosidase activity but no galactosyltransferase activity
    • Tulsiani D, Skudlarek M, Orgebin-Crist M. Human sperm plasma membranes possess alpha-D-mannosidase activity but no galactosyltransferase activity. Biol Reprod 1990; 42: 843-58.
    • (1990) Biol Reprod , vol.42 , pp. 843-58
    • Tulsiani, D.1    Skudlarek, M.2    Orgebin-Crist, M.3
  • 131
    • 77955291176 scopus 로고    scopus 로고
    • Zonadhesin is essential for species specificity of sperm adhesion to the eggs zona pellucida
    • Tardif S, Wilson MD, Wagner R, Hunt P, GertsensteinM et al. Zonadhesin is essential for species specificity of sperm adhesion to the eggs zona pellucida. J Biol Chem 2010; 285: 24863-70.
    • (2010) J Biol Chem , vol.285 , pp. 24863-70
    • Tardif, S.1    Wilson, M.D.2    Wagner, R.3    Gertsensteinm, H.P.4
  • 132
    • 23644440524 scopus 로고    scopus 로고
    • The role of molecular chaperones in mouse sperm-egg interactions
    • Nixon B, Asquith KL, John Aitken R. The role of molecular chaperones in mouse sperm-egg interactions. Mol Cell Endocrinol 2005; 240: 1-10.
    • (2005) Mol Cell Endocrinol , vol.240 , pp. 1-10
    • Nixon, B.1    Asquith, K.L.2    John Aitken, R.3
  • 133
    • 0034661419 scopus 로고    scopus 로고
    • Mammalian sperm acrosome: Formation, contents, and function
    • Abou-Haila A, Tulsiani DR. Mammalian sperm acrosome: formation, contents, and function. Arch Biochem Biophys 2000; 379: 173-82.
    • (2000) Arch Biochem Biophys , vol.379 , pp. 173-82
    • Abou-Haila, A.1    Tulsiani, D.R.2
  • 134
    • 0037363251 scopus 로고    scopus 로고
    • Evidence for the capacitation-associated membrane priming of mouse spermatozoa
    • Abou-Haila A, Tulsiani DR. Evidence for the capacitation-associated membrane priming of mouse spermatozoa. Histochem Cell Biol 2003; 119: 179-87.
    • (2003) Histochem Cell Biol , vol.119 , pp. 179-87
    • Abou-Haila, A.1    Tulsiani, D.R.2
  • 135
    • 0015963344 scopus 로고
    • Purification and properties of aryl sulfatases from rabbit sperm acrosomes
    • Yang CH, Srivastava PN, Williams WL. Purification and properties of aryl sulfatases from rabbit sperm acrosomes. Proc Soc Exp Biol Med 1974; 145: 721-5.
    • (1974) Proc Soc Exp Biol Med , vol.145 , pp. 721-5
    • Yang, C.H.1    Srivastava, P.N.2    Williams, W.L.3
  • 136
    • 0025114177 scopus 로고
    • Acrosin activation follows its surface exposure and precedes membrane fusion in human sperm acrosome reaction
    • Tesarik J, Drahorad J, Testart J, Mendoza C. Acrosin activation follows its surface exposure and precedes membrane fusion in human sperm acrosome reaction. Development 1990; 110: 391-400.
    • (1990) Development , vol.110 , pp. 391-400
    • Tesarik, J.1    Drahorad, J.2    Testart, J.3    Mendoza, C.4
  • 137
    • 0032766878 scopus 로고    scopus 로고
    • A plasma membrane-associated hyaluronidase is localized to the posterior acrosomal region of stallion sperm and is associated with spermatozoal function
    • Meyers SA, Rosenberger AE. A plasma membrane-associated hyaluronidase is localized to the posterior acrosomal region of stallion sperm and is associated with spermatozoal function. Biol Reprod 1999; 61: 444-51.
    • (1999) Biol Reprod , vol.61 , pp. 444-51
    • Meyers, S.A.1    Rosenberger, A.E.2
  • 138
    • 0035159305 scopus 로고    scopus 로고
    • Differential release of guinea pig sperm acrosomal components during exocytosis
    • Kim KS, Foster JA, Gerton GL. Differential release of guinea pig sperm acrosomal components during exocytosis. Biol Reprod 2001; 64: 148-56.
    • (2001) Biol Reprod , vol.64 , pp. 148-56
    • Kim, K.S.1    Foster, J.A.2    Gerton, G.L.3
  • 139
    • 70449715103 scopus 로고    scopus 로고
    • The biological significance of detergent-resistant membranes in spermatozoa
    • Nixon B, Aitken RJ. The biological significance of detergent-resistant membranes in spermatozoa. J Reprod Immunol 2009; 83: 8-13.
    • (2009) J Reprod Immunol , vol.83 , pp. 8-13
    • Nixon, B.1    Aitken, R.J.2
  • 140
    • 1842482773 scopus 로고    scopus 로고
    • Model systems, lipid rafts, and cell membranes
    • Simons K, Vaz WLC. Model systems, lipid rafts, and cell membranes. Annu Rev Biophys Biomol Struct 2004; 33: 269-95.
    • (2004) Annu Rev Biophys Biomol Struct , vol.33 , pp. 269-95
    • Simons, K.1    Wlc, V.2
  • 141
    • 3142724785 scopus 로고    scopus 로고
    • Cholesterol efflux alters lipid raft stability and distribution during capacitation of boar spermatozoa
    • Shadan S, James PS, Howes EA, Jones R. Cholesterol efflux alters lipid raft stability and distribution during capacitation of boar spermatozoa. Biol Reprod 2004; 71: 253-65.
    • (2004) Biol Reprod , vol.71 , pp. 253-65
    • Shadan, S.1    James, P.S.2    Howes, E.A.3    Jones, R.4
  • 142
    • 77953174328 scopus 로고    scopus 로고
    • Glioma pathogenesis-related 1-like 1 is testis enriched, dynamically modified, and redistributed during male germ cell maturation and has a potential role in sperm-oocyte binding
    • Gibbs GM, Lo JC, Nixon B, Jamsai D, OConnor AE et al. Glioma pathogenesis-related 1-like 1 is testis enriched, dynamically modified, and redistributed during male germ cell maturation and has a potential role in sperm-oocyte binding. Endocrinology 2010; 151: 2331-42.
    • (2010) Endocrinology , Issue.151 , pp. 2331-42
    • Gibbs, G.M.1    Lo, J.C.2    Nixon, B.3    Jamsai, D.4    Oconnor, A.E.5
  • 143
    • 26944442601 scopus 로고    scopus 로고
    • Capacitationdependent concentration of lipid rafts in the apical ridge head area of porcine sperm cells
    • van Gestel RA, Brewis IA, Ashton PR, Helms JB, Brouwers JF et al. Capacitationdependent concentration of lipid rafts in the apical ridge head area of porcine sperm cells. Mol Hum Reprod 2005; 11: 583-90.
    • (2005) Mol Hum Reprod , vol.11 , pp. 583-90
    • Van Gestel, R.A.1    Brewis, I.A.2    Ashton, P.R.3    Helms, J.B.4    Brouwers, J.F.5
  • 144
    • 76949094130 scopus 로고    scopus 로고
    • Tracking diffusion of GM1 gangliosides and zona pellucida binding molecules in sperm plasma membranes following cholesterol efflux
    • Jones R, Howes E, Dunne PD, James P, Bruckbauer A et al. Tracking diffusion of GM1 gangliosides and zona pellucida binding molecules in sperm plasma membranes following cholesterol efflux. Dev Biol 2010; 339: 398-406.
    • (2010) Dev Biol , Issue.339 , pp. 398-406
    • Jones, R.1    Howes, E.2    Dunne, P.D.3    James, P.4    Bruckbauer, A.5
  • 146
    • 30544450854 scopus 로고    scopus 로고
    • Sperm capacitation induces an increase in lipid rafts having zona pellucida binding ability and containing sulfogalactosylglycerolipid
    • Khalil MB, Chakrabandhu K, Xu H, Weerachatyanukul W, Buhr M et al. Sperm capacitation induces an increase in lipid rafts having zona pellucida binding ability and containing sulfogalactosylglycerolipid. Dev Biol 2006; 290: 220-35.
    • (2006) Dev Biol , vol.290 , pp. 220-35
    • Khalil, M.B.1    Chakrabandhu, K.2    Xu, H.3    Weerachatyanukul, W.4    Buhr, M.5
  • 147
    • 33646127577 scopus 로고    scopus 로고
    • Molecular chaperones and protein quality control
    • Bukau B, Weissman J, Horwich A. Molecular chaperones and protein quality control. Cell 2006; 125: 443-51.
    • (2006) Cell , vol.125 , pp. 443-51
    • Bukau, B.1    Weissman, J.2    Horwich, A.3
  • 148
    • 73149115984 scopus 로고    scopus 로고
    • Heat shock proteins on the human sperm surface
    • Naaby-Hansen S, Herr JC. Heat shock proteins on the human sperm surface. J Reprod Immunol 2010; 84: 32-40.
    • (2010) J Reprod Immunol , Issue.84 , pp. 32-40
    • Naaby-Hansen, S.1    Herr, J.C.2
  • 150
  • 151
    • 0026718176 scopus 로고
    • Characterization and cellular distribution of human spermatozoal heat shock proteins
    • Miller D, Brough S, Al-Harbi O. Characterization and cellular distribution of human spermatozoal heat shock proteins. Hum Reprod 1992; 7: 637-45.
    • (1992) Hum Reprod , vol.7 , pp. 637-45
    • Miller, D.1    Brough, S.2    Al-Harbi, O.3
  • 152
    • 44349152970 scopus 로고    scopus 로고
    • Identification of the molecular chaperone, heat shock protein 1 (chaperonin 10), in the reproductive tract and in capacitating spermatozoa in the male mouse
    • Walsh A, Whelan D, Bielanowicz A, Skinner B, Aitken RJ et al. Identification of the molecular chaperone, heat shock protein 1 (chaperonin 10), in the reproductive tract and in capacitating spermatozoa in the male mouse. Biol Reprod 2008; 78: 983-93.
    • (2008) Biol Reprod , vol.78 , pp. 983-93
    • Walsh, A.1    Whelan, D.2    Bielanowicz, A.3    Skinner, B.4    Aitken, R.J.5
  • 153
    • 4444254836 scopus 로고    scopus 로고
    • Tyrosine phosphorylation activates surface chaperones facilitating sperm-zona recognition
    • Asquith KL, Baleato RM, McLaughlin EA, Nixon B, Aitken RJ. Tyrosine phosphorylation activates surface chaperones facilitating sperm-zona recognition. J Cell Sci 2004; 117: 3645-57.
    • (2004) J Cell Sci , vol.117 , pp. 3645-57
    • Asquith, K.L.1    Baleato, R.M.2    McLaughlin, E.A.3    Nixon, B.4    Aitken, R.J.5
  • 154
    • 0025249857 scopus 로고
    • Characterization of a decapacitation factor associated with epididymal mouse spermatozoa
    • Fraser LR, Harrison RAP, Herod JE. Characterization of a decapacitation factor associated with epididymal mouse spermatozoa. Reproduction 1990; 89: 135-48.
    • (1990) Reproduction , vol.89 , pp. 135-48
    • Fraser, L.R.1    Rap, H.2    Herod, J.E.3
  • 155
    • 0029968485 scopus 로고    scopus 로고
    • Evidence for Ca21-dependent ATPase activity, stimulated by decapacitation factor and calmodulin, in mouse sperm
    • Adeoya-Osiguwa SA, Fraser LR. Evidence for Ca21-dependent ATPase activity, stimulated by decapacitation factor and calmodulin, in mouse sperm. Mol Reprod Dev 1996; 44: 111-20.
    • (1996) Mol Reprod Dev , vol.44 , pp. 111-20
    • Adeoya-Osiguwa, S.A.1    Fraser, L.R.2
  • 156
    • 0033613867 scopus 로고    scopus 로고
    • Cholesterol efflux-mediated signal transduction in mammalian sperm. Beta-cyclodextrins initiate transmembrane signaling leading to an increase in protein tyrosine phosphorylation and capacitation
    • Visconti PE, Galantino-Homer H, Ning X, Moore GD, Valenzuela JP et al. Cholesterol efflux-mediated signal transduction in mammalian sperm. Beta-cyclodextrins initiate transmembrane signaling leading to an increase in protein tyrosine phosphorylation and capacitation. J Biol Chem 1999; 274: 3235-42.
    • (1999) J Biol Chem , vol.274 , pp. 3235-42
    • Visconti, P.E.1    Galantino-Homer, H.2    Ning, X.3    Moore, G.D.4    Valenzuela, J.P.5
  • 157
    • 0037499505 scopus 로고    scopus 로고
    • Caspase-independent exposure of aminophospholipids and tyrosine phosphorylation in bicarbonate responsive human sperm cells
    • de Vries KJ, Wiedmer T, Sims PJ, Gadella BM. Caspase-independent exposure of aminophospholipids and tyrosine phosphorylation in bicarbonate responsive human sperm cells. Biol Reprod 2003; 68: 2122-34.
    • (2003) Biol Reprod , vol.68 , pp. 2122-34
    • De Vries, K.J.1    Wiedmer, T.2    Sims, P.J.3    Gadella, B.M.4
  • 158
    • 58849163274 scopus 로고    scopus 로고
    • Understanding the molecular basis of sperm capacitation through kinase design
    • Visconti PE. Understanding the molecular basis of sperm capacitation through kinase design. Proc Natl Acad Sci USA 2009; 106: 667-8.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 667-8
    • Visconti, P.E.1
  • 159
    • 0028936801 scopus 로고
    • Capacitation of mouse spermatozoa. II. Protein tyrosine phosphorylation and capacitation are regulated by a cAMP-dependent pathway
    • Visconti PE, Moore GD, Bailey JL, Leclerc P, Connors SA et al. Capacitation of mouse spermatozoa. II. Protein tyrosine phosphorylation and capacitation are regulated by a cAMP-dependent pathway. Development 1995; 121: 1139-50.
    • (1995) Development , vol.121 , pp. 1139-50
    • Visconti, P.E.1    Moore, G.D.2    Bailey, J.L.3    Leclerc, P.4    Connors, S.A.5
  • 160
    • 77952477746 scopus 로고    scopus 로고
    • Elucidation of the signaling pathways that underpin capacitation- associated surface phosphotyrosine expression in mouse spermatozoa
    • Nixon B, Bielanowicz A, Anderson AL, Walsh A, Hall T et al. Elucidation of the signaling pathways that underpin capacitation-associated surface phosphotyrosine expression in mouse spermatozoa. J Cell Physiol 2010; 224: 71-83.
    • (2010) J Cell Physiol , Issue.224 , pp. 71-83
    • Nixon, B.1    Bielanowicz, A.2    Anderson, A.L.3    Walsh, A.4    Hall, T.5
  • 161
    • 34248587212 scopus 로고    scopus 로고
    • Sperm binding to the zona pellucida is not sufficient to induce acrosome exocytosis
    • Baibakov B, Gauthier L, Talbot P, Rankin TL, Dean J. Sperm binding to the zona pellucida is not sufficient to induce acrosome exocytosis. Development 2007; 134: 933.
    • (2007) Development , vol.134 , pp. 933
    • Baibakov, B.1    Gauthier, L.2    Talbot, P.3    Rankin, T.L.4    Dean, J.5
  • 162
    • 34248570055 scopus 로고    scopus 로고
    • Acrosomal exocytosis, a special type of regulated secretion
    • Mayorga LS, Tomes CN, Belmonte SA. Acrosomal exocytosis, a special type of regulated secretion. IUBMB life 2007; 59: 286-92.
    • (2007) IUBMB Life , vol.59 , pp. 286-92
    • Mayorga, L.S.1    Tomes, C.N.2    Belmonte, S.A.3


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