메뉴 건너뛰기




Volumn 52, Issue 5-6, 2008, Pages 683-701

Anuran and pig egg zona pellucida glycoproteins in fertilization and early development

Author keywords

Block to polyspermy; Fertilization; Pig; Sperm binding; Xenopus laevis; Zona pellucida

Indexed keywords

GLUCAN SYNTHASE; GLYCOPROTEIN; N ACETYL BETA GLUCOSAMINIDASE; OLIGOSACCHARIDE; OVIDUCTIN; OVOCHYMASE; PROTEINASE; SERINE PROTEINASE; UNCLASSIFIED DRUG;

EID: 54249091677     PISSN: 02146282     EISSN: None     Source Type: Journal    
DOI: 10.1387/ijdb.082580jh     Document Type: Review
Times cited : (49)

References (167)
  • 1
    • 0016353256 scopus 로고
    • Comparative aspects of the ultrastructure of the female gamete
    • ANDERSON, E. (1974). Comparative aspects of the ultrastructure of the female gamete. International Review of Cytology 4: 1-3.
    • (1974) International Review of Cytology , vol.4 , pp. 1-3
    • ANDERSON, E.1
  • 2
    • 0000136575 scopus 로고
    • Early reactions of the rodent egg to spermatozoon penetration
    • AUSTIN, C.R. and BRADEN, A.W.H. (1956). Early reactions of the rodent egg to spermatozoon penetration. Journal of Experimental Biology 33: 358-365.
    • (1956) Journal of Experimental Biology , vol.33 , pp. 358-365
    • AUSTIN, C.R.1    BRADEN, A.W.H.2
  • 4
    • 0025139831 scopus 로고
    • Physicochemical characterization of progressive changes in the xenopus-laevis egg envelope following oviductal transport and fertilization
    • BAKOS, M.A., KUROSKY, A. and HEDRICK, J.L. (1990a). Physicochemical characterization of progressive changes in the xenopus-laevis egg envelope following oviductal transport and fertilization. Biochemistry 29: 609-615.
    • (1990) Biochemistry , vol.29 , pp. 609-615
    • BAKOS, M.A.1    KUROSKY, A.2    HEDRICK, J.L.3
  • 5
    • 0025195001 scopus 로고
    • Enzymatic and envelope-converting activities of pars recta oviductal fluid from xenopus-laevis
    • BAKOS, M.A., KUROSKY, A. and HEDRICK, J.L. (1990b). Enzymatic and envelope-converting activities of pars recta oviductal fluid from xenopus-laevis. Developmental Biology 138: 169-176.
    • (1990) Developmental Biology , vol.138 , pp. 169-176
    • BAKOS, M.A.1    KUROSKY, A.2    HEDRICK, J.L.3
  • 6
    • 0036197619 scopus 로고    scopus 로고
    • Vitelline envelope of Bufo arenarum: Biochemical and biological characterization
    • BARISONE, G.A., HEDRICK, J.L. and CABADA, M.O. (2002). Vitelline envelope of Bufo arenarum: Biochemical and biological characterization. Biology of Reproduction 66: 1203-1209.
    • (2002) Biology of Reproduction , vol.66 , pp. 1203-1209
    • BARISONE, G.A.1    HEDRICK, J.L.2    CABADA, M.O.3
  • 7
    • 33947642540 scopus 로고    scopus 로고
    • Glycoproteins of the vitelline envelope of amphibian oocyte: Biological and molecular characterization of ZPC component (gp41) in Bufo arenarum
    • BARISONE, G.A., KRAPF, D., CORREA-FIZ, F., ARRANZ, S.E. and CABADA, M.O. (2007). Glycoproteins of the vitelline envelope of amphibian oocyte: Biological and molecular characterization of ZPC component (gp41) in Bufo arenarum. Molecular Reproduction and Development 74: 629-640.
    • (2007) Molecular Reproduction and Development , vol.74 , pp. 629-640
    • BARISONE, G.A.1    KRAPF, D.2    CORREA-FIZ, F.3    ARRANZ, S.E.4    CABADA, M.O.5
  • 8
    • 0015238694 scopus 로고
    • Induction of zona reaction in golden hamster eggs by cortical granule material
    • BARROS, C. and YANAGIMACHI, R. (1971). Induction of zona reaction in golden hamster eggs by cortical granule material. Nature 233: 268-269.
    • (1971) Nature , vol.233 , pp. 268-269
    • BARROS, C.1    YANAGIMACHI, R.2
  • 9
    • 0024346478 scopus 로고
    • Sperm binding to the pig zona pellucida and inhibition of binding by solubilized components of the zona pellucida
    • BERGER, T., DAVIS, A., WARDRIP, N.J. and HEDRICK, J.L. (1989). Sperm binding to the pig zona pellucida and inhibition of binding by solubilized components of the zona pellucida. Journal of Reproduction and Fertility 86: 559-565.
    • (1989) Journal of Reproduction and Fertility , vol.86 , pp. 559-565
    • BERGER, T.1    DAVIS, A.2    WARDRIP, N.J.3    HEDRICK, J.L.4
  • 10
    • 54249155007 scopus 로고
    • Identification and characterization of proteins of zona pellucida
    • BLEIL, J.D. and WASSARMAN, P.M. (1978). Identification and characterization of proteins of zona pellucida. Journal of Cell Biology 79: A173-A173.
    • (1978) Journal of Cell Biology , vol.79
    • BLEIL, J.D.1    WASSARMAN, P.M.2
  • 11
    • 0018822414 scopus 로고
    • Structure and function of the zona pellucida - identification and characterization of the proteins of the mouse oocytes zona pellucida
    • BLEIL, J.D. and WASSARMAN, P.M. (1980). Structure and function of the zona pellucida - identification and characterization of the proteins of the mouse oocytes zona pellucida. Developmental Biology 76: 185-202.
    • (1980) Developmental Biology , vol.76 , pp. 185-202
    • BLEIL, J.D.1    WASSARMAN, P.M.2
  • 13
    • 0022677334 scopus 로고
    • Changes in the composition of the porcine zona pellucida during development of the oocyte to the 2- to 4-cell embryo
    • BROWN, C.R. and CHENG, W.T.R. (1986). Changes in the composition of the porcine zona pellucida during development of the oocyte to the 2- to 4-cell embryo. Journal of Embryology and Experimental Morphology 92: 183-191.
    • (1986) Journal of Embryology and Experimental Morphology , vol.92 , pp. 183-191
    • BROWN, C.R.1    CHENG, W.T.R.2
  • 14
    • 34347221894 scopus 로고    scopus 로고
    • Expanding the complexity of the human degradome: Polyserases and their tandem serine protease domains
    • CAL, S., MONCADA-PAZOS, A. and LOPEZ-OTIN, C. (2007). Expanding the complexity of the human degradome: Polyserases and their tandem serine protease domains. Frontiers in Bioscience 12: 4661-4669.
    • (2007) Frontiers in Bioscience , vol.12 , pp. 4661-4669
    • CAL, S.1    MONCADA-PAZOS, A.2    LOPEZ-OTIN, C.3
  • 15
    • 34548139046 scopus 로고    scopus 로고
    • Isolated ZP-N domains constitute the N-terminal extensions of zona pellucida proteins
    • CALLEBAUT, I., MORNON, J.P. and MONGET, P. (2007). Isolated ZP-N domains constitute the N-terminal extensions of zona pellucida proteins. Bioinformatics 23: 1871-1874.
    • (2007) Bioinformatics , vol.23 , pp. 1871-1874
    • CALLEBAUT, I.1    MORNON, J.P.2    MONGET, P.3
  • 16
    • 0026452560 scopus 로고
    • Postfertilization changes in Discoglossus-pictus (anura) eggs result in the formation of a capsular chamber where the egg rotates
    • CAMPANELLA, C., AMORE, F., PITARI, G., FUSCO, C., MAURIZI, G. and DUPRE, S. (1992). Postfertilization changes in Discoglossus-pictus (anura) eggs result in the formation of a capsular chamber where the egg rotates. International Journal of Developmental Biology 36: 413-422.
    • (1992) International Journal of Developmental Biology , vol.36 , pp. 413-422
    • CAMPANELLA, C.1    AMORE, F.2    PITARI, G.3    FUSCO, C.4    MAURIZI, G.5    DUPRE, S.6
  • 18
    • 0035146060 scopus 로고    scopus 로고
    • Following passage through the oviduct, the coelomic envelope of Discoglossus pictus (amphibia) acquires fertilizability upon reorganization, conversion of gp 42 to gp 40, extensive glycosylation, and formation of a specific layer
    • CAPUTO, M., INFANTE, V., TALEVI, R., VACCARO, M.C., CAROTENUTO, R. and CAMPANELLA, C. (2001). Following passage through the oviduct, the coelomic envelope of Discoglossus pictus (amphibia) acquires fertilizability upon reorganization, conversion of gp 42 to gp 40, extensive glycosylation, and formation of a specific layer. Molecular Reproduction and Development 58: 318-329.
    • (2001) Molecular Reproduction and Development , vol.58 , pp. 318-329
    • CAPUTO, M.1    INFANTE, V.2    TALEVI, R.3    VACCARO, M.C.4    CAROTENUTO, R.5    CAMPANELLA, C.6
  • 20
    • 0016194810 scopus 로고
    • Hatching in toad xenopus-laevis - morphological events and evidence for a hatching enzyme
    • CARROLL, E.J. and HEDRICK, J.L. (1974). Hatching in toad xenopus-laevis - morphological events and evidence for a hatching enzyme. Developmental Biology 38: 1-13.
    • (1974) Developmental Biology , vol.38 , pp. 1-13
    • CARROLL, E.J.1    HEDRICK, J.L.2
  • 21
    • 0023917119 scopus 로고
    • Localization of cortical granule constituents befor and after exocytosis in the hamster egg
    • CHERR, G.N., DROBNIS, E.Z. and KATZ, D.F. (1988). Localization of cortical granule constituents befor and after exocytosis in the hamster egg. Journal of Experimental Zoology 246: 81-93.
    • (1988) Journal of Experimental Zoology , vol.246 , pp. 81-93
    • CHERR, G.N.1    DROBNIS, E.Z.2    KATZ, D.F.3
  • 23
    • 0034596130 scopus 로고    scopus 로고
    • Reproductive biotechnologies: Current status in porcine reproduction
    • DAY, B.N. (2000). Reproductive biotechnologies: Current status in porcine reproduction. Animal Reproduction Science 60: 161-172.
    • (2000) Animal Reproduction Science , vol.60 , pp. 161-172
    • DAY, B.N.1
  • 24
    • 0023949528 scopus 로고
    • Biophysical properties of the zona pellucida measured by capillary suction. Is zona hardening a mechanical phenomenon?
    • DROBNIS, E.Z., ANDREW, J.B. and KATZ, D.F. (1988). Biophysical properties of the zona pellucida measured by capillary suction. Is zona hardening a mechanical phenomenon? Journal of Experimental Zoology 245: 206-219.
    • (1988) Journal of Experimental Zoology , vol.245 , pp. 206-219
    • DROBNIS, E.Z.1    ANDREW, J.B.2    KATZ, D.F.3
  • 25
    • 0015292069 scopus 로고
    • Oogenesis in Xenopus laevis. Part 1. Stages of oocyte development in laboratory maintained animals
    • DUMONT, J.N. (1972). Oogenesis in Xenopus laevis. Part 1. Stages of oocyte development in laboratory maintained animals. Journal of Morphology 136: 153-180.
    • (1972) Journal of Morphology , vol.136 , pp. 153-180
    • DUMONT, J.N.1
  • 26
    • 0022163241 scopus 로고
    • Egg envelopes in vertebrates
    • BROWDER, L.W, Ed, Plenum Press, New York, pp
    • DUMONT, J.N. and BRUMMETT, A.N. (1985). Egg envelopes in vertebrates. In: BROWDER, L.W., Ed. Oogenesis. Plenum Press, New York, pp. 235-288.
    • (1985) Oogenesis , pp. 235-288
    • DUMONT, J.N.1    BRUMMETT, A.N.2
  • 27
    • 54249114380 scopus 로고
    • Isolation and physicochemical properties of porcine zona pellucida
    • DUNBAR, B.S., WARDRIP, N.J. and HEDRICK, J.L. (1978). Isolation and physicochemical properties of porcine zona pellucida. Journal of Cell Biology 79: A163-A163.
    • (1978) Journal of Cell Biology , vol.79
    • DUNBAR, B.S.1    WARDRIP, N.J.2    HEDRICK, J.L.3
  • 28
    • 0018871935 scopus 로고
    • Isolation, physicochemical properties, and macromolecular-composition of zone pellucida from porcine oocytes
    • DUNBAR, B.S., WARDRIP, N.J. and HEDRICK, J.L. (1980). Isolation, physicochemical properties, and macromolecular-composition of zone pellucida from porcine oocytes. Biochemistry 19: 356-365.
    • (1980) Biochemistry , vol.19 , pp. 356-365
    • DUNBAR, B.S.1    WARDRIP, N.J.2    HEDRICK, J.L.3
  • 29
    • 0001987828 scopus 로고
    • Comparative structure and funciton of mammalian zonae pellucidae
    • DUNBAR, B.S. and O'RAND, M.G, Eds, Plenum Press, New York
    • DUBAR, B.S., PRASAD, M. and TIMMONS, T.M. (1991). Comparative structure and funciton of mammalian zonae pellucidae. In: DUNBAR, B.S. and O'RAND, M.G., Eds., A Comparative Overview of Mammalian Fertilization. Plenum Press, New York.
    • (1991) A Comparative Overview of Mammalian Fertilization
    • DUBAR, B.S.1    PRASAD, M.2    TIMMONS, T.M.3
  • 30
    • 0034795758 scopus 로고    scopus 로고
    • Properties of the hatching enzyme from Xenopus laevis
    • FAN, T.J. and KATAGIRI, C. (2001). Properties of the hatching enzyme from Xenopus laevis. European Journal of Biochemistry 268: 4892-4898.
    • (2001) European Journal of Biochemistry , vol.268 , pp. 4892-4898
    • FAN, T.J.1    KATAGIRI, C.2
  • 31
    • 4444370949 scopus 로고    scopus 로고
    • Texture of the zona pellucida of the mature pig oocyte. The mammalian egg envelope revisited
    • FLECHON, J.E., KOPECNY, V., PIVKO, J., PAVLOK, A. and MOTLIK, J. (2004). Texture of the zona pellucida of the mature pig oocyte. The mammalian egg envelope revisited. Reproduction Nutrition Development 44: 207-218.
    • (2004) Reproduction Nutrition Development , vol.44 , pp. 207-218
    • FLECHON, J.E.1    KOPECNY, V.2    PIVKO, J.3    PAVLOK, A.4    MOTLIK, J.5
  • 32
    • 0020198127 scopus 로고
    • A gel eluter for recovery of proteins separated by polyacrylamide-gel electrophoresis
    • GERTON, G.L., WARDRIP, N.J. and HEDRICK, J.L. (1982). A gel eluter for recovery of proteins separated by polyacrylamide-gel electrophoresis. Analytical Biochemistry 126: 116-121.
    • (1982) Analytical Biochemistry , vol.126 , pp. 116-121
    • GERTON, G.L.1    WARDRIP, N.J.2    HEDRICK, J.L.3
  • 33
    • 0022573194 scopus 로고
    • The celomic envelope to vitelline envelope conversion in eggs of xenopus-laevis
    • GERTON, G.L. and HEDRICK, J.L. (1986a). The celomic envelope to vitelline envelope conversion in eggs of xenopus-laevis. Journal of Cellular Biochemistry 30: 341-350.
    • (1986) Journal of Cellular Biochemistry , vol.30 , pp. 341-350
    • GERTON, G.L.1    HEDRICK, J.L.2
  • 34
    • 0022871835 scopus 로고
    • The vitelline envelope to fertilization envelope conversion in eggs of xenopus-laevis
    • GERTON, G.L. and HEDRICK, J.L. (1986b). The vitelline envelope to fertilization envelope conversion in eggs of xenopus-laevis. Developmental Biology 116: 1-7.
    • (1986) Developmental Biology , vol.116 , pp. 1-7
    • GERTON, G.L.1    HEDRICK, J.L.2
  • 35
    • 0024465090 scopus 로고
    • Effect of sodium dodecyl-sulfate on the hamster zona pellucida before and after a cortical reaction induced by the ionophore a23187
    • GREEN, D.P.L. (1989). Effect of sodium dodecyl-sulfate on the hamster zona pellucida before and after a cortical reaction induced by the ionophore a23187. Journal of Reproduction and Fertility 87: 447-453.
    • (1989) Journal of Reproduction and Fertility , vol.87 , pp. 447-453
    • GREEN, D.P.L.1
  • 36
    • 54249144330 scopus 로고    scopus 로고
    • Fertilization biophysics
    • HARDY, D.M, Ed, Academic Press, San Diego, pp
    • GREEN, D.P.L. (2002). Fertilization biophysics. In: HARDY, D.M., Ed. Fertilization. Academic Press, San Diego, pp. 387-399.
    • (2002) Fertilization , pp. 387-399
    • GREEN, D.P.L.1
  • 37
    • 0022364583 scopus 로고
    • N-acetyl-β-D-glucosaminidase activity in the cortical granules of xenopus-laevis eggs
    • GREVE, L.C., PRODY, G.A. and HEDRICK, J.L. (1985). N-acetyl-β-D-glucosaminidase activity in the cortical granules of xenopus-laevis eggs. Gamete Research 12: 305-312.
    • (1985) Gamete Research , vol.12 , pp. 305-312
    • GREVE, L.C.1    PRODY, G.A.2    HEDRICK, J.L.3
  • 38
    • 54249156902 scopus 로고
    • Formation of fertilization envelope in eggs of xenopus-laevis
    • GREY, R.D., WOLF, D.P. and HEDRICK, J.L. (1972). Formation of fertilization envelope in eggs of xenopus-laevis. Journal of Cell Biology 55: A96-A96.
    • (1972) Journal of Cell Biology , vol.55
    • GREY, R.D.1    WOLF, D.P.2    HEDRICK, J.L.3
  • 39
    • 0017176734 scopus 로고
    • Evidence that fertilization envelope blocks sperm entry in eggs of xenopus-laevis - interaction of sperm with isolated envelopes
    • GREY, R.D., WORKING, P.K. and HEDRICK,. J.L. (1976). Evidence that fertilization envelope blocks sperm entry in eggs of xenopus-laevis - interaction of sperm with isolated envelopes. Developmental Biology 54: 52-60.
    • (1976) Developmental Biology , vol.54 , pp. 52-60
    • GREY, R.D.1    WORKING, P.K.2    HEDRICK, J.L.3
  • 40
    • 0017508192 scopus 로고    scopus 로고
    • GREY, R.D., WORKING, P.K. and HEDRICK, J.L. (1977). Alteration of structure and penetrability of vitelline envelope after passage of eggs from coelom to oviduct in xenopus-laevis. Journal of Experimental Zoology 201: 73-&.
    • GREY, R.D., WORKING, P.K. and HEDRICK, J.L. (1977). Alteration of structure and penetrability of vitelline envelope after passage of eggs from coelom to oviduct in xenopus-laevis. Journal of Experimental Zoology 201: 73-&.
  • 42
    • 0026683132 scopus 로고
    • Oviductin - purification and properties of the oviductal protease that processes the molecular-weight 43 000 glycoprotein of the xenopus-laevis egg envelope
    • HARDY, D.M. and HEDRICK, J.L. (1992). Oviductin - purification and properties of the oviductal protease that processes the molecular-weight 43 000 glycoprotein of the xenopus-laevis egg envelope. Biochemistry 31: 4466-4472.
    • (1992) Biochemistry , vol.31 , pp. 4466-4472
    • HARDY, D.M.1    HEDRICK, J.L.2
  • 43
    • 0028045713 scopus 로고
    • Cloning and characterization of zona-pellucida genes and cDNAs from a variety of mammalian-species - the ZPA, ZPB and ZPC gene families
    • HARRIS, J.D., HIBLER, D.W., FONTENOT, G.K., HSU, K.T., YUREWICZ, E.C.and SACCO, A.G. (1994). Cloning and characterization of zona-pellucida genes and cDNAs from a variety of mammalian-species - the ZPA, ZPB and ZPC gene families. DNA Sequence 4: 361-393.
    • (1994) DNA Sequence , vol.4 , pp. 361-393
    • HARRIS, J.D.1    HIBLER, D.W.2    FONTENOT, G.K.3    HSU, K.T.4    YUREWICZ, E.C.5    SACCO, A.G.6
  • 44
    • 0028325798 scopus 로고
    • Amino acid sequence of a porcine zona pellucida glycoprotein ZP4 determined by peptide mapping and cDNA cloning
    • HASEGAWA, A., KOYAMA, K., OKAZAKI, Y., SUGIMOTO, M. and ISOJIMA, S. (1994). Amino acid sequence of a porcine zona pellucida glycoprotein ZP4 determined by peptide mapping and cDNA cloning. Journal of Reproduction and Fertility 100: 245-255.
    • (1994) Journal of Reproduction and Fertility , vol.100 , pp. 245-255
    • HASEGAWA, A.1    KOYAMA, K.2    OKAZAKI, Y.3    SUGIMOTO, M.4    ISOJIMA, S.5
  • 45
    • 0022552320 scopus 로고
    • Isolation of the zona-pellucida and purification of its glycoprotein families from pig oocytes
    • HEDRICK, J.L. and WARDRIP, N.J. (1986). Isolation of the zona-pellucida and purification of its glycoprotein families from pig oocytes. Analytical Biochemistry 157: 63-70.
    • (1986) Analytical Biochemistry , vol.157 , pp. 63-70
    • HEDRICK, J.L.1    WARDRIP, N.J.2
  • 46
    • 0023217444 scopus 로고
    • On the macromolecular-composition of the zona-pellucida from porcine oocytes
    • HEDRICK, J.L. and WARDRIP, N.J. (1987). On the macromolecular-composition of the zona-pellucida from porcine oocytes. Developmental Biology 121: 478-488.
    • (1987) Developmental Biology , vol.121 , pp. 478-488
    • HEDRICK, J.L.1    WARDRIP, N.J.2
  • 47
    • 0023152870 scopus 로고
    • Differences in the macromolecular-composition of the zona-pellucida isolated from pig oocytes, eggs, and zygotes
    • HEDRICK, J.L., WARDRIP, N.J. and BERGER, T. (1987). Differences in the macromolecular-composition of the zona-pellucida isolated from pig oocytes, eggs, and zygotes. Journal of Experimental Zoology 241: 257-262.
    • (1987) Journal of Experimental Zoology , vol.241 , pp. 257-262
    • HEDRICK, J.L.1    WARDRIP, N.J.2    BERGER, T.3
  • 48
    • 0026301819 scopus 로고
    • Isolation of extracellular-matrix structures from xenopus-laevis oocytes, eggs, and embryos
    • HEDRICK, J.L. and HARDY, D.M. (1991). Isolation of extracellular-matrix structures from xenopus-laevis oocytes, eggs, and embryos. Methods in Cell Biology 36: 231-247.
    • (1991) Methods in Cell Biology , vol.36 , pp. 231-247
    • HEDRICK, J.L.1    HARDY, D.M.2
  • 49
    • 0026085725 scopus 로고
    • Structure and function of the extracellular-matrix of anuran eggs
    • HEDRICK, J.L. and NISHIHARA, T. (1991). Structure and function of the extracellular-matrix of anuran eggs. Journal of Electron Microscopy Technique 17: 319-335.
    • (1991) Journal of Electron Microscopy Technique , vol.17 , pp. 319-335
    • HEDRICK, J.L.1    NISHIHARA, T.2
  • 50
    • 0030333348 scopus 로고    scopus 로고
    • Comparative structural and antigenic properties of zona pellucida glycoproteins
    • HEDRICK, J.L. (1996). Comparative structural and antigenic properties of zona pellucida glycoproteins. Journal of Reproduction and Fertility 9-17.
    • (1996) Journal of Reproduction and Fertility , pp. 9-17
    • HEDRICK, J.L.1
  • 51
    • 34547842767 scopus 로고    scopus 로고
    • A comparative analysis of molecular mechanisms for blocking polyspermy: Identification of a lectin-ligand binding reaction in mammalian eggs
    • GUPTA, S.K, KOYAMA, K. and MURRAY, J.F, Eds, Nottingham Press, Nottingham, pp
    • HEDRICK, J.L. (2007). A comparative analysis of molecular mechanisms for blocking polyspermy: Identification of a lectin-ligand binding reaction in mammalian eggs. In: GUPTA, S.K., KOYAMA, K. and MURRAY, J.F., Eds., Gamete Biology: Emerging Frontiers in Fertility and Contraceptive Development. Nottingham Press, Nottingham, pp. 409-420.
    • (2007) Gamete Biology: Emerging Frontiers in Fertility and Contraceptive Development , pp. 409-420
    • HEDRICK, J.L.1
  • 53
    • 0036499914 scopus 로고    scopus 로고
    • Oviductin, the oviductal protease that mediates gamete interaction by affecting the vitelline coat in Bufo japonicus: Its molecular cloning and analyses of expression and posttranslational activation
    • HIYOSHI, M., TAKAMUNE, K., MITA, K., KUBO, H., SUGIMOTO, Y. and KATAGIRI, C. (2002). Oviductin, the oviductal protease that mediates gamete interaction by affecting the vitelline coat in Bufo japonicus: Its molecular cloning and analyses of expression and posttranslational activation. Developmental Biology 243: 176-184.
    • (2002) Developmental Biology , vol.243 , pp. 176-184
    • HIYOSHI, M.1    TAKAMUNE, K.2    MITA, K.3    KUBO, H.4    SUGIMOTO, Y.5    KATAGIRI, C.6
  • 55
    • 34547640132 scopus 로고    scopus 로고
    • ZP genes in avian species illustrate the dynamic evolution of the vertebrate egg envelope
    • HUGHES, D.C. (2007). ZP genes in avian species illustrate the dynamic evolution of the vertebrate egg envelope. Cytogenetic and Genome Research 117: 86-91.
    • (2007) Cytogenetic and Genome Research , vol.117 , pp. 86-91
    • HUGHES, D.C.1
  • 56
    • 0020478511 scopus 로고
    • Properties of the vitelline coat lysin from toad sperm
    • IWAO, Y. and KATAGIRI, C. (1982). Properties of the vitelline coat lysin from toad sperm. Journal of Experimental Zoology 219: 87-95.
    • (1982) Journal of Experimental Zoology , vol.219 , pp. 87-95
    • IWAO, Y.1    KATAGIRI, C.2
  • 57
    • 0034238369 scopus 로고    scopus 로고
    • Mechanisms of egg activation and polyspermy block in amphibians and comparative aspects with fertilization in other vertebrates
    • IWAO, Y. (2000a). Mechanisms of egg activation and polyspermy block in amphibians and comparative aspects with fertilization in other vertebrates. Zoological Science 17: 699-709.
    • (2000) Zoological Science , vol.17 , pp. 699-709
    • IWAO, Y.1
  • 58
    • 0002719638 scopus 로고    scopus 로고
    • Fertilization in amphibians
    • TARIN, J.J. and CANO, A, Eds, Springer-Verlag, Heidelberg, pp
    • IWAO, Y. (2000b). Fertilization in amphibians. In: TARIN, J.J. and CANO, A., Eds., Fertilization in Protozoa and Metazoan Animals. Springer-Verlag, Heidelberg, pp. 147-191.
    • (2000) Fertilization in Protozoa and Metazoan Animals , pp. 147-191
    • IWAO, Y.1
  • 59
    • 0036307181 scopus 로고    scopus 로고
    • The ZP domain is a conserved module for polymerization of extracellular proteins
    • JOVINE, L., QI, H.Y., WILLIAMS, Z., LITSCHER, E. and WASSARMAN, P.M. (2002). The ZP domain is a conserved module for polymerization of extracellular proteins. Nature Cell Biology 4: 457-461.
    • (2002) Nature Cell Biology , vol.4 , pp. 457-461
    • JOVINE, L.1    QI, H.Y.2    WILLIAMS, Z.3    LITSCHER, E.4    WASSARMAN, P.M.5
  • 62
    • 0033991985 scopus 로고    scopus 로고
    • Systematic identification of genes expressed during early oogenesis in medaka
    • KANAMORI, A. (2000). Systematic identification of genes expressed during early oogenesis in medaka. Molecular Reproduction and Development 55: 31-36.
    • (2000) Molecular Reproduction and Development , vol.55 , pp. 31-36
    • KANAMORI, A.1
  • 63
    • 0016769521 scopus 로고
    • Properties of hatching enzyme from frog embryos
    • KATAGIRI, C. (1975). Properties of hatching enzyme from frog embryos. Journal of Experimental Zoology193: 109-118.
    • (1975) Journal of Experimental Zoology , vol.193 , pp. 109-118
    • KATAGIRI, C.1
  • 64
    • 0020215230 scopus 로고
    • Participation of oviducal pars recta secretions in inducing the acrosome reaction and release of vitelline coat lysin in fertilizing toad sperm
    • KATAGIRI, C., IWAO, Y. and YOSHIZAKI, N. (1982). Participation of oviducal pars recta secretions in inducing the acrosome reaction and release of vitelline coat lysin in fertilizing toad sperm. Developmental Biology 94: 1-10.
    • (1982) Developmental Biology , vol.94 , pp. 1-10
    • KATAGIRI, C.1    IWAO, Y.2    YOSHIZAKI, N.3
  • 65
    • 0002479532 scopus 로고
    • Role of oviducal secretions in mediating gamete fusion in anuran amphibians
    • KATAGIRI, C. (1987). Role of oviducal secretions in mediating gamete fusion in anuran amphibians. Zoological Science 4: 1-14.
    • (1987) Zoological Science , vol.4 , pp. 1-14
    • KATAGIRI, C.1
  • 67
    • 0028956002 scopus 로고
    • Molecular-cloning of chick beta-tectorin, an extracellular-matrix molecule of the inner-ear
    • KILLICK, R., LEGAN, P.K, MALENCZAK, C. and RICHARDSON, G.P. (1995). Molecular-cloning of chick beta-tectorin, an extracellular-matrix molecule of the inner-ear. Journal of Cell Biology 129: 535-547.
    • (1995) Journal of Cell Biology , vol.129 , pp. 535-547
    • KILLICK, R.1    LEGAN, P.K.2    MALENCZAK, C.3    RICHARDSON, G.P.4
  • 69
    • 0032818491 scopus 로고    scopus 로고
    • Molecular basis for oviductin-mediated processing from gp43 to gp41, the predominant glycoproteins of Xenopus egg envelopes
    • KUBO, H., MATSUSHITA, R., KOTANI, M., KAWASAKI, H., SAIDO, T.C., KAWASHIMA, S., KATGIRI, C. and SUZUKI, A. (1999). Molecular basis for oviductin-mediated processing from gp43 to gp41, the predominant glycoproteins of Xenopus egg envelopes. Developmental Genetics 25: 123-129.
    • (1999) Developmental Genetics , vol.25 , pp. 123-129
    • KUBO, H.1    MATSUSHITA, R.2    KOTANI, M.3    KAWASAKI, H.4    SAIDO, T.C.5    KAWASHIMA, S.6    KATGIRI, C.7    SUZUKI, A.8
  • 71
    • 0032521660 scopus 로고    scopus 로고
    • Localization of carbohydrate chains of pig sperm ligand in the glycoprotein ZPB of egg zona pellucida
    • KUDO, K., YONEZAWA, N., KATSUMATA, T., AOKI, H. and NAKANO, M. (1998). Localization of carbohydrate chains of pig sperm ligand in the glycoprotein ZPB of egg zona pellucida. European Journal of Biochemistry 252: 492-499.
    • (1998) European Journal of Biochemistry , vol.252 , pp. 492-499
    • KUDO, K.1    YONEZAWA, N.2    KATSUMATA, T.3    AOKI, H.4    NAKANO, M.5
  • 72
    • 54249111778 scopus 로고
    • Ueber aktive betheiligung des dotters am befruchtungsakte bei Bufo variabilis and vulgaris
    • KUPFFER, C. (1882). Ueber aktive betheiligung des dotters am befruchtungsakte bei Bufo variabilis and vulgaris. Sitzungsb. d. math. -physik Classe d. k. b. Akad. di Wiss. zu Munchen 12: 608-618.
    • (1882) Sitzungsb. d. math. -physik Classe d. k. b. Akad. di Wiss. zu Munchen , vol.12 , pp. 608-618
    • KUPFFER, C.1
  • 73
    • 0023678527 scopus 로고
    • The extracellular-matrix of xenopuslaevis eggs - a quick-freeze, deep-etch analysis of its modification at fertilization
    • LARABELL, C.A. and CHANDLER, D.E. (1988). The extracellular-matrix of xenopuslaevis eggs - a quick-freeze, deep-etch analysis of its modification at fertilization. Journal of Cell Biology 107: 731-741.
    • (1988) Journal of Cell Biology , vol.107 , pp. 731-741
    • LARABELL, C.A.1    CHANDLER, D.E.2
  • 74
    • 0024460003 scopus 로고
    • Quick-freeze, deep-etch, rotary-shadow views of the extracellular-matrix and cortical cytoskeleton of xenopus-laevis eggs
    • LARABELL, C.A. and CHANDLER, D.E. (1989). Quick-freeze, deep-etch, rotary-shadow views of the extracellular-matrix and cortical cytoskeleton of xenopus-laevis eggs. Journal of Electron Microscopy Technique 13: 228-243.
    • (1989) Journal of Electron Microscopy Technique , vol.13 , pp. 228-243
    • LARABELL, C.A.1    CHANDLER, D.E.2
  • 75
    • 0025331468 scopus 로고
    • Stepwise transformation of the vitelline envelope of xenopus eggs at activation - a quick-freeze, deep-etch analysis
    • LARABELL, C.A. and CHANDLER, D.E. (1990). Stepwise transformation of the vitelline envelope of xenopus eggs at activation - a quick-freeze, deep-etch analysis. Developmental Biology 139: 263-268.
    • (1990) Developmental Biology , vol.139 , pp. 263-268
    • LARABELL, C.A.1    CHANDLER, D.E.2
  • 76
    • 0030889074 scopus 로고    scopus 로고
    • The mouse tectorins - modular matrix proteins of the inner ear homologous to components of the sperm-egg adhesion system
    • LEGAN, P.K., RAU, A., KEEN, J.N. and RICHARDSON, G.P. (1997). The mouse tectorins - modular matrix proteins of the inner ear homologous to components of the sperm-egg adhesion system. Journal of Biological Chemistry 272: 8791-8801.
    • (1997) Journal of Biological Chemistry , vol.272 , pp. 8791-8801
    • LEGAN, P.K.1    RAU, A.2    KEEN, J.N.3    RICHARDSON, G.P.4
  • 77
    • 0024313690 scopus 로고
    • Proteases released from xenopus-laevis eggs at activation and their role in envelope conversion
    • LINDSAY, L.L. and HEDRICK, J.L. (1989). Proteases released from xenopus-laevis eggs at activation and their role in envelope conversion. Developmental Biology 135: 202-211.
    • (1989) Developmental Biology , vol.135 , pp. 202-211
    • LINDSAY, L.L.1    HEDRICK, J.L.2
  • 78
    • 0026484831 scopus 로고
    • Localization of a chymotrypsin-like protease to the perivitelline space of xenopus-laevis eggs
    • LINDSAY, L.L., LARABELL, C.A. and HEDRICK, J.L. (1992). Localization of a chymotrypsin-like protease to the perivitelline space of xenopus-laevis eggs. Developmental Biology 154: 433-436.
    • (1992) Developmental Biology , vol.154 , pp. 433-436
    • LINDSAY, L.L.1    LARABELL, C.A.2    HEDRICK, J.L.3
  • 79
    • 0028927831 scopus 로고
    • Isolation and characterization of ovochymase, a chymotrypsin-like protease released during xenopus-laevis egg activation
    • LINDSAY, L.L. and HEDRICK, J.L. (1995). Isolation and characterization of ovochymase, a chymotrypsin-like protease released during xenopus-laevis egg activation. Developmental Biology 167: 513-516.
    • (1995) Developmental Biology , vol.167 , pp. 513-516
    • LINDSAY, L.L.1    HEDRICK, J.L.2
  • 80
    • 0032981826 scopus 로고    scopus 로고
    • Oviductin, the Xenopus laevis oviductal protease that processes egg envelope glycoprotein gp43, increases sperm binding to envelopes, and is translated as part of an unusual mosaic protein composed of two protease and several cub domains
    • LINDSAY, L.L., WIEDUWILT, M.J. and HEDRICK, J.L. (1999a). Oviductin, the Xenopus laevis oviductal protease that processes egg envelope glycoprotein gp43, increases sperm binding to envelopes, and is translated as part of an unusual mosaic protein composed of two protease and several cub domains. Biology of Reproduction 60: 989-995.
    • (1999) Biology of Reproduction , vol.60 , pp. 989-995
    • LINDSAY, L.L.1    WIEDUWILT, M.J.2    HEDRICK, J.L.3
  • 82
    • 0035726506 scopus 로고    scopus 로고
    • A hatching enzyme substrate in the Xenopus laevis egg envelope is a high molecular weight ZPA homolog
    • LINDSAY, L.L., WALLACE, M.A. and HEDRICK, J.L. (2001). A hatching enzyme substrate in the Xenopus laevis egg envelope is a high molecular weight ZPA homolog. Development Growth & Differentiation 43: 305-313.
    • (2001) Development Growth & Differentiation , vol.43 , pp. 305-313
    • LINDSAY, L.L.1    WALLACE, M.A.2    HEDRICK, J.L.3
  • 85
    • 84993875637 scopus 로고
    • Modification of the vitelline envelope of coelomic Bufo arenarum oocytes by products of the cortical granules
    • MARIANO, M.I. and CABADA, M.O. (1978). Modification of the vitelline envelope of coelomic Bufo arenarum oocytes by products of the cortical granules. Rev. Microsc. Electr. 5: 50-51.
    • (1978) Rev. Microsc. Electr , vol.5 , pp. 50-51
    • MARIANO, M.I.1    CABADA, M.O.2
  • 86
    • 0021321475 scopus 로고
    • Morphological modifications of oocyte vitelline envelope from Bufo arenarum during different functional states
    • MARIANO, M.I., DE MARTIN, M.G. and PISANO, E. (1984). Morphological modifications of oocyte vitelline envelope from Bufo arenarum during different functional states. Development, Growth & Differentiation 26: 33-42.
    • (1984) Development, Growth & Differentiation , vol.26 , pp. 33-42
    • MARIANO, M.I.1    DE MARTIN, M.G.2    PISANO, E.3
  • 87
    • 0030203206 scopus 로고    scopus 로고
    • Assessment of the acrosome reaction in Bufo arenarum spermatozoa by immunostaining: Comparison with other methods
    • MARTINEZ, M.L. and CABADA, M.O. (1996). Assessment of the acrosome reaction in Bufo arenarum spermatozoa by immunostaining: Comparison with other methods, Zygote 4: 181-190.
    • (1996) Zygote , vol.4 , pp. 181-190
    • MARTINEZ, M.L.1    CABADA, M.O.2
  • 88
    • 0042863046 scopus 로고    scopus 로고
    • Oviduct-specific glycoprotein modulates spermzona binding and improves efficiency of porcine fertilization in vitro
    • MCCAULEY, T.C., BUHI, W.C., WU, G.M., MAO, J., CAAMANO, J.N., DIDION, B.A. and DAY, B.N. (2003). Oviduct-specific glycoprotein modulates spermzona binding and improves efficiency of porcine fertilization in vitro. Biology of Reproduction 69: 828-834.
    • (2003) Biology of Reproduction , vol.69 , pp. 828-834
    • MCCAULEY, T.C.1    BUHI, W.C.2    WU, G.M.3    MAO, J.4    CAAMANO, J.N.5    DIDION, B.A.6    DAY, B.N.7
  • 92
    • 35748952171 scopus 로고    scopus 로고
    • Structural and functional events on the porcine zona pellucida during maturation, fertilization and embryonic development: A scanning electron microscopy analysis
    • MICHELMANN, H.W., RATH, D., TOPFER-PETERSEN, E. and SCHWARTZ, P. (2007). Structural and functional events on the porcine zona pellucida during maturation, fertilization and embryonic development: A scanning electron microscopy analysis. Reproduction in Domestic Animals 42: 594-602.
    • (2007) Reproduction in Domestic Animals , vol.42 , pp. 594-602
    • MICHELMANN, H.W.1    RATH, D.2    TOPFER-PETERSEN, E.3    SCHWARTZ, P.4
  • 93
    • 0027752372 scopus 로고
    • Egg cortical granule N-acetylglucosaminidase is required for the mouse zona block to polyspermy
    • MILLER, D.J., GONG, X.H., DECKER, G. and SHUR, S.D. (1993). Egg cortical granule N-acetylglucosaminidase is required for the mouse zona block to polyspermy. Journal of Cell Biology 123: 1431-1440.
    • (1993) Journal of Cell Biology , vol.123 , pp. 1431-1440
    • MILLER, D.J.1    GONG, X.H.2    DECKER, G.3    SHUR, S.D.4
  • 94
    • 0024515399 scopus 로고
    • Characterization of a proteinase that cleaves zona pellucida glycoprotein-ZP2 following activation of mouse eggs
    • MOLLER, C.C. and WASSARMAN, P.M. (1989). Characterization of a proteinase that cleaves zona pellucida glycoprotein-ZP2 following activation of mouse eggs. Developmental Biology 132: 103-112.
    • (1989) Developmental Biology , vol.132 , pp. 103-112
    • MOLLER, C.C.1    WASSARMAN, P.M.2
  • 95
    • 33748648790 scopus 로고    scopus 로고
    • Tracking down the ZP domain: From the mammalian zona pellucida to the molluscan vitelline envelope
    • MONNE, M., HAN, L. and JOVINE, L. (2006). Tracking down the ZP domain: From the mammalian zona pellucida to the molluscan vitelline envelope. Seminars in Reproductive Medicine 24: 204-216.
    • (2006) Seminars in Reproductive Medicine , vol.24 , pp. 204-216
    • MONNE, M.1    HAN, L.2    JOVINE, L.3
  • 97
    • 0025975588 scopus 로고
    • Neutral oligosaccharide structures linked to asparagines of porcine zona-pellucida glycoproteins
    • MORI, E., TAKASAKI, S., HEDRICK, J.L., WARDRIP, N.J., MORI, T. and KOBATA, A. (1991). Neutral oligosaccharide structures linked to asparagines of porcine zona-pellucida glycoproteins. Biochemistry 30: 2078-2087.
    • (1991) Biochemistry , vol.30 , pp. 2078-2087
    • MORI, E.1    TAKASAKI, S.2    HEDRICK, J.L.3    WARDRIP, N.J.4    MORI, T.5    KOBATA, A.6
  • 98
    • 0031860314 scopus 로고    scopus 로고
    • Occurrence of reducing terminal N-acetylglucosamine 3-sulfate and fucosylated outer chains in acidic N-glycans of porcine zona pellucida glycoproteins
    • MORI, E., HEDRICK, J.L., WARDRIP, N.J., MORI, T. and TAKASAKI, S. (1998). Occurrence of reducing terminal N-acetylglucosamine 3-sulfate and fucosylated outer chains in acidic N-glycans of porcine zona pellucida glycoproteins. Glycoconjugate Journal 15: 447-456.
    • (1998) Glycoconjugate Journal , vol.15 , pp. 447-456
    • MORI, E.1    HEDRICK, J.L.2    WARDRIP, N.J.3    MORI, T.4    TAKASAKI, S.5
  • 99
    • 54249161794 scopus 로고
    • Hatching and birth
    • New York, pp
    • NEEDHAM, J. (1963). Hatching and birth. In: Chemical embryology. New York, pp. 1595-1605.
    • (1963) Chemical embryology , pp. 1595-1605
    • NEEDHAM, J.1
  • 101
    • 33745833820 scopus 로고
    • On the impregnation of the ovum in amphibia. And on the direct agency of the spermatozoon
    • NEWPORT, G. (1853). On the impregnation of the ovum in amphibia. And on the direct agency of the spermatozoon. Philosophical Transactions of the Royal Society of London 143: 233-290.
    • (1853) Philosophical Transactions of the Royal Society of London , vol.143 , pp. 233-290
    • NEWPORT, G.1
  • 102
    • 15844404405 scopus 로고
    • Researches on the impregnation of the ovum in amphibia; and on the early stages of development of the embryo
    • NEWPORT, G. and ELLIS, G.V. (1854). Researches on the impregnation of the ovum in amphibia; and on the early stages of development of the embryo. Philosophical Transactions of the Royal Society of London 144: 229-244.
    • (1854) Philosophical Transactions of the Royal Society of London , vol.144 , pp. 229-244
    • NEWPORT, G.1    ELLIS, G.V.2
  • 104
  • 105
    • 0346354383 scopus 로고
    • Molecular mechanism for envelop elevation at fertilization
    • NISHIHARA, T. and HEDRICK, J.L. (1977). Molecular mechanism for envelop elevation at fertilization. Federation Proceedings 36: 811.
    • (1977) Federation Proceedings , vol.36 , pp. 811
    • NISHIHARA, T.1    HEDRICK, J.L.2
  • 107
    • 0023044272 scopus 로고
    • Isolation and characterization of a lectin from the cortical granules of xenopus-laevis eggs
    • NISHIHARA, T., WYRICK, R.E., WORKING, P.K., CHEN, Y.H. and HEDRICK, J.L. (1986). Isolation and characterization of a lectin from the cortical granules of xenopus-laevis eggs. Biochemistry 25: 6013-6020.
    • (1986) Biochemistry , vol.25 , pp. 6013-6020
    • NISHIHARA, T.1    WYRICK, R.E.2    WORKING, P.K.3    CHEN, Y.H.4    HEDRICK, J.L.5
  • 108
    • 0026607821 scopus 로고
    • Structural-analysis of the N-linked carbohydrate chains of the 55-kda glycoprotein family (pZP3) from porcine zona-pellucida
    • NOGUCHI, S., HATANAKA, Y., TOBITA, T. and NAKANO, M. (1992). Structural-analysis of the N-linked carbohydrate chains of the 55-kda glycoprotein family (pZP3) from porcine zona-pellucida. European Journal of Biochemistry 204: 1089-1100.
    • (1992) European Journal of Biochemistry , vol.204 , pp. 1089-1100
    • NOGUCHI, S.1    HATANAKA, Y.2    TOBITA, T.3    NAKANO, M.4
  • 109
    • 9444249289 scopus 로고    scopus 로고
    • A newly identified zona pellucida glycoprotein, ZPD, and dimeric ZP1 of chicken egg envelope are involved in sperm activation on sperm-egg interaction
    • OKUMURA, H., KOHNO, Y., IWATA, Y., MORI, H., AOKI, N., SATO, C., KITAJIMA K., NADANO, D. and MATSUDA, T. (2004). A newly identified zona pellucida glycoprotein, ZPD, and dimeric ZP1 of chicken egg envelope are involved in sperm activation on sperm-egg interaction. Biochemical Journal 384: 191-199.
    • (2004) Biochemical Journal , vol.384 , pp. 191-199
    • OKUMURA, H.1    KOHNO, Y.2    IWATA, Y.3    MORI, H.4    AOKI, N.5    SATO, C.6    KITAJIMA, K.7    NADANO, D.8    MATSUDA, T.9
  • 110
    • 35648985556 scopus 로고    scopus 로고
    • Association of chicken zona pellucdia glycoprotein (ZP) b1 with ZPC induces formation of ZPB1-ZPC fibrous aggregates containing disulfide-bridged ZPB1 dimer
    • OKUMURA, H., OKAJIMA, T., NADANO, D. and MATSUDA, T. (2007). Association of chicken zona pellucdia glycoprotein (ZP) b1 with ZPC induces formation of ZPB1-ZPC fibrous aggregates containing disulfide-bridged ZPB1 dimer. Biochemical and Biophysical Research Communications 364: 682-688.
    • (2007) Biochemical and Biophysical Research Communications , vol.364 , pp. 682-688
    • OKUMURA, H.1    OKAJIMA, T.2    NADANO, D.3    MATSUDA, T.4
  • 111
    • 0030474666 scopus 로고    scopus 로고
    • Involvement of carbohydrate moieties of the toad egg vitelline coat in binding with fertilizing sperm
    • OMATA, S. and KATAGIRI, C. (1996). Involvement of carbohydrate moieties of the toad egg vitelline coat in binding with fertilizing sperm. Development Growth & Differentiation 38: 663-672.
    • (1996) Development Growth & Differentiation , vol.38 , pp. 663-672
    • OMATA, S.1    KATAGIRI, C.2
  • 112
    • 33744743816 scopus 로고    scopus 로고
    • Behavior of the vitelline envelope of Bufo arenarum oocytes matured in vitro in blockade of polyspermy
    • OTERINO, J., TORANZO, G.S., ZELARAYAN, L., AJMAT, M.T., BONILLA, F. and BpHLER, M.I. (2006). Behavior of the vitelline envelope of Bufo arenarum oocytes matured in vitro in blockade of polyspermy. Zygote 14: 97-106.
    • (2006) Zygote , vol.14 , pp. 97-106
    • OTERINO, J.1    TORANZO, G.S.2    ZELARAYAN, L.3    AJMAT, M.T.4    BONILLA, F.5    BpHLER, M.I.6
  • 113
    • 0004329427 scopus 로고
    • The history of histochemistry
    • Little, Brown, & Company, Boston, pp
    • PEARSE, A.G.E. (1968). The history of histochemistry. In: Histochemistry: Theoretical and Applied. Little, Brown, & Company, Boston, pp. 1-12.
    • (1968) Histochemistry: Theoretical and Applied , pp. 1-12
    • PEARSE, A.G.E.1
  • 114
    • 0027525053 scopus 로고
    • The primary egg envelope of the anuran Lepidobatrachus-laevis - physicochemical and macromolecular alterations during development
    • PEAVY, T.R. and CARROLL, E.J. (1993). The primary egg envelope of the anuran Lepidobatrachus-laevis - physicochemical and macromolecular alterations during development. Development Growth & Differentiation 35: 447-460.
    • (1993) Development Growth & Differentiation , vol.35 , pp. 447-460
    • PEAVY, T.R.1    CARROLL, E.J.2
  • 115
    • 84993917838 scopus 로고
    • N-acetyl-beta-D-glucosaminidase activity in cortical granules - characterization and function
    • PRODY, G.A., GREVE, L.C. and HEDRICK, J.L. (1983). N-acetyl-beta-D-glucosaminidase activity in cortical granules - characterization and function. Journal of Cell Biology 97: A29-A29.
    • (1983) Journal of Cell Biology , vol.97
    • PRODY, G.A.1    GREVE, L.C.2    HEDRICK, J.L.3
  • 116
    • 0017692843 scopus 로고
    • Effect of trypsin-inhibitors and Concanavalin a on Bufo-arenarum fertilization
    • RAISMAN, J.S., MARIANO, M.I. and CABADA, M.O. (1977). Effect of trypsin-inhibitors and Concanavalin a on Bufo-arenarum fertilization. Development Growth & Differentiation 19: 119-123.
    • (1977) Development Growth & Differentiation , vol.19 , pp. 119-123
    • RAISMAN, J.S.1    MARIANO, M.I.2    CABADA, M.O.3
  • 118
    • 11144316603 scopus 로고    scopus 로고
    • Zona pellucida characteristics and sperm-binding patterns of in vivo and in vitro produced porcine oocytes inseminated with differently prepared spermatozoa
    • RATH, D., TOPFER-PETERSEN, E., MICHELMANN, H.W., SCHWARTZ, P. and EBELING, S. (2005). Zona pellucida characteristics and sperm-binding patterns of in vivo and in vitro produced porcine oocytes inseminated with differently prepared spermatozoa. Theriogenology 63: 352-362.
    • (2005) Theriogenology , vol.63 , pp. 352-362
    • RATH, D.1    TOPFER-PETERSEN, E.2    MICHELMANN, H.W.3    SCHWARTZ, P.4    EBELING, S.5
  • 120
    • 0024442504 scopus 로고
    • Porcine zona pellucida - association of sperm receptor activity with the alpha-glycoprotein component of the mr = 55,000 family
    • SACCO, A.G., YUREWICZ, E.C., SUBRAMANIAN, M.G. and MATZAT, P.D. (1989). Porcine zona pellucida - association of sperm receptor activity with the alpha-glycoprotein component of the mr = 55,000 family. Biology of Reproduction 41: 523-532.
    • (1989) Biology of Reproduction , vol.41 , pp. 523-532
    • SACCO, A.G.1    YUREWICZ, E.C.2    SUBRAMANIAN, M.G.3    MATZAT, P.D.4
  • 122
    • 54249111317 scopus 로고    scopus 로고
    • SMART. (2007). Simple modular architecture research tool. Http://smart.Emblheidelberg.De/ accession number sm00042.
    • SMART. (2007). Simple modular architecture research tool. Http://smart.Emblheidelberg.De/ accession number sm00042.
  • 123
    • 0037305191 scopus 로고    scopus 로고
    • Evolution and nomenclature of the zona pellucida gene family
    • SPARGO, S.C. and HOPE, R.M. (2003). Evolution and nomenclature of the zona pellucida gene family. Biology of Reproduction 68: 358-362.
    • (2003) Biology of Reproduction , vol.68 , pp. 358-362
    • SPARGO, S.C.1    HOPE, R.M.2
  • 125
    • 0028129514 scopus 로고
    • Surface alterations of the bovine oocyte and its investments during and after maturation and fertilization in vitro
    • SUZUKI, H., YANG, X. and FOOTE, R.H. (1994). Surface alterations of the bovine oocyte and its investments during and after maturation and fertilization in vitro. Molecular Reproduction and Development 38: 421-430.
    • (1994) Molecular Reproduction and Development , vol.38 , pp. 421-430
    • SUZUKI, H.1    YANG, X.2    FOOTE, R.H.3
  • 126
    • 84985819533 scopus 로고
    • The properties of the oviducal pars recta protease which mediates gamete interaction by affecting the vitelline coat of a toad egg
    • TAKAMUNE, K. and KATAGIRI, C. (1987). The properties of the oviducal pars recta protease which mediates gamete interaction by affecting the vitelline coat of a toad egg. Development Growth & Differentiation 29: 193-203.
    • (1987) Development Growth & Differentiation , vol.29 , pp. 193-203
    • TAKAMUNE, K.1    KATAGIRI, C.2
  • 127
    • 84989636799 scopus 로고
    • Comparative-studies of bufo and xenopus vitelline coat molecular-transformations induced by homologous and heterologous oviducal pars recta proteases
    • TAKAMUNE, K., LINDSAY, L., HEDRICK, J.L. and KATAGIRI, C. (1987). Comparative-studies of bufo and xenopus vitelline coat molecular-transformations induced by homologous and heterologous oviducal pars recta proteases. Journal of Experimental Zooloqy 244: 145-150.
    • (1987) Journal of Experimental Zooloqy , vol.244 , pp. 145-150
    • TAKAMUNE, K.1    LINDSAY, L.2    HEDRICK, J.L.3    KATAGIRI, C.4
  • 128
    • 54249092770 scopus 로고    scopus 로고
    • The 69 and 64 kda glycoproteins in the vitelline envelope of Xenopus eggs mediate sperm-egg binding during fertilization
    • TIAN, J.D., GONG, H., THOMSEN, G.H. and LENNARZ, W.J. (1996). The 69 and 64 kda glycoproteins in the vitelline envelope of Xenopus eggs mediate sperm-egg binding during fertilization. Molecular Biology of the Cell 7: 2807-2807.
    • (1996) Molecular Biology of the Cell , vol.7 , pp. 2807-2807
    • TIAN, J.D.1    GONG, H.2    THOMSEN, G.H.3    LENNARZ, W.J.4
  • 129
    • 0030933883 scopus 로고    scopus 로고
    • Gamete interactions in Xenopus laevis: Identification of sperm binding glycoproteins in the egg vitelline envelope
    • TIAN, J.D., GONG, H., THOMSEN, G.H. and LENNARZ, W.J. (1997). Gamete interactions in Xenopus laevis: Identification of sperm binding glycoproteins in the egg vitelline envelope. Journal of Cell Biology 136: 1099-1108.
    • (1997) Journal of Cell Biology , vol.136 , pp. 1099-1108
    • TIAN, J.D.1    GONG, H.2    THOMSEN, G.H.3    LENNARZ, W.J.4
  • 131
    • 0036499522 scopus 로고    scopus 로고
    • Acrosome reaction in sperm of the frog, Xenopus laevis: Its detection and induction by oviductal pars recta secretion
    • UEDA, Y., YOSHIZAKI, N. and IWAO, Y. (2002). Acrosome reaction in sperm of the frog, Xenopus laevis: Its detection and induction by oviductal pars recta secretion. Developmental Biology 243: 55-64.
    • (2002) Developmental Biology , vol.243 , pp. 55-64
    • UEDA, Y.1    YOSHIZAKI, N.2    IWAO, Y.3
  • 132
    • 0242708844 scopus 로고    scopus 로고
    • Characterization of the acrosome reaction-inducing substance in Xenopus (ARISX) secreted from the oviductal pars recta onto the vitelline envelope
    • UEDA, Y., KUBO, H. and IWAO, Y. (2003). Characterization of the acrosome reaction-inducing substance in Xenopus (ARISX) secreted from the oviductal pars recta onto the vitelline envelope. Developmental Biology 264: 289-298.
    • (2003) Developmental Biology , vol.264 , pp. 289-298
    • UEDA, Y.1    KUBO, H.2    IWAO, Y.3
  • 133
    • 34548013746 scopus 로고    scopus 로고
    • Analysis of terminal sugar moieties and species-specificities of acrosome reaction-inducing substance in Xenopus (ARISX)
    • UEDA, Y., IMAIZUMI, C., KUBO, H., SATO, K.I., FUKAMI, Y. and IWAO, Y. (2007). Analysis of terminal sugar moieties and species-specificities of acrosome reaction-inducing substance in Xenopus (ARISX). Development Growth & Differentiation 49: 591-601.
    • (2007) Development Growth & Differentiation , vol.49 , pp. 591-601
    • UEDA, Y.1    IMAIZUMI, C.2    KUBO, H.3    SATO, K.I.4    FUKAMI, Y.5    IWAO, Y.6
  • 134
  • 135
    • 0019529143 scopus 로고
    • Isolation and characterization of the hatching enzyme from the amphibian, xenopus-laevis
    • URCH, U.A. and HEDRICK, J.L. (1981b). Isolation and characterization of the hatching enzyme from the amphibian, xenopus-laevis. Archives of Biochemistry and Biophysics 206: 424-431.
    • (1981) Archives of Biochemistry and Biophysics , vol.206 , pp. 424-431
    • URCH, U.A.1    HEDRICK, J.L.2
  • 136
    • 0033998948 scopus 로고    scopus 로고
    • Independent and hetero-oligomeric-dependent sperm binding to egg envelope glycoprotein ZPC in Xenopus laevis
    • VO, L.H. and HEDRICK, J.L. (2000). Independent and hetero-oligomeric-dependent sperm binding to egg envelope glycoprotein ZPC in Xenopus laevis. Biology of Reproduction 62: 766-774.
    • (2000) Biology of Reproduction , vol.62 , pp. 766-774
    • VO, L.H.1    HEDRICK, J.L.2
  • 137
    • 0344739563 scopus 로고    scopus 로고
    • Identification of the ZPC oligosaccharide ligand involved in sperm binding and the glycan structures of Xenopus laevis vitelline envelope glycoproteins
    • VO, L.H., YEN, T.Y., MACHER, B.A. and HEDRICK, J.L. (2003). Identification of the ZPC oligosaccharide ligand involved in sperm binding and the glycan structures of Xenopus laevis vitelline envelope glycoproteins. Biology of Reproduction 69: 1822-1830.
    • (2003) Biology of Reproduction , vol.69 , pp. 1822-1830
    • VO, L.H.1    YEN, T.Y.2    MACHER, B.A.3    HEDRICK, J.L.4
  • 138
    • 24044514682 scopus 로고    scopus 로고
    • Analysis of N-linked glycans of porcine zona pellucida glycoprotein ZPA by Maldi-tof MS: A contribution to understanding zone pellucida structure
    • VON WITZENDORFF, D., EKHLASI-HUNDRIESER, M., DOSTALOVA, Z., RESCH, M., RATH, D., MICHELMANN, H.W. and TOPFER-PETERSEN, E. (2005). Analysis of N-linked glycans of porcine zona pellucida glycoprotein ZPA by Maldi-tof MS: A contribution to understanding zone pellucida structure. Glycobiology 15: 475-488.
    • (2005) Glycobiology , vol.15 , pp. 475-488
    • VON WITZENDORFF, D.1    EKHLASI-HUNDRIESER, M.2    DOSTALOVA, Z.3    RESCH, M.4    RATH, D.5    MICHELMANN, H.W.6    TOPFER-PETERSEN, E.7
  • 140
    • 0036996948 scopus 로고    scopus 로고
    • The urodele egg-coat as the apparatus adapted for the internal fertilization
    • WATANABE, A. and ONITAKE, K. (2002). The urodele egg-coat as the apparatus adapted for the internal fertilization. Zoological Science 19: 1341-1347.
    • (2002) Zoological Science , vol.19 , pp. 1341-1347
    • WATANABE, A.1    ONITAKE, K.2
  • 142
    • 0015088967 scopus 로고
    • Molecular approach to fertilization 3. Development of a bioassay for sperm capacitation
    • 25: 360-&
    • WOLF, D.P. and HEDRICK, J.L. (1971). Molecular approach to fertilization 3. Development of a bioassay for sperm capacitation. Developmental Biology 25: 360-&.
    • (1971) Developmental Biology
    • WOLF, D.P.1    HEDRICK, J.L.2
  • 143
    • 0017079646 scopus 로고
    • Isolation, physicochemical properties, and macromolecular-composition of vitelline and fertilization envelopes from xenopus-laevis eggs
    • WOLF, D.P., NISHIHARA, T., WEST, D.M., WYRICK, R.E. and HEDRICK, J.L. (1976). Isolation, physicochemical properties, and macromolecular-composition of vitelline and fertilization envelopes from xenopus-laevis eggs. Biochemistry 15: 3671-3678.
    • (1976) Biochemistry , vol.15 , pp. 3671-3678
    • WOLF, D.P.1    NISHIHARA, T.2    WEST, D.M.3    WYRICK, R.E.4    HEDRICK, J.L.5
  • 144
    • 0000067892 scopus 로고
    • The mammalian egg's block to polyspermy
    • MASTRONIANNI, L. and BIGGERS, J.D, Eds, Plenum Publishing, New York, pp
    • WOLF, D.P. (1981). The mammalian egg's block to polyspermy. In: MASTRONIANNI, L. and BIGGERS, J.D., Eds., Fertilization and embryonic development in vitro. Plenum Publishing, New York, pp. 183-197.
    • (1981) Fertilization and embryonic development in vitro , pp. 183-197
    • WOLF, D.P.1
  • 145
    • 33645885359 scopus 로고    scopus 로고
    • Defending the zygote: Search for the ancestral animal block to polyspermy
    • WONG, J.L. and WESSEL, G.M. (2006). Defending the zygote: Search for the ancestral animal block to polyspermy. Current Topics in Developmental Biology 72: 1-151.
    • (2006) Current Topics in Developmental Biology , vol.72 , pp. 1-151
    • WONG, J.L.1    WESSEL, G.M.2
  • 146
    • 54249162846 scopus 로고
    • Fertilization envelope formation by glycoprotein agglutination and block to polyspermy in xenopus-laevis
    • WYRICK, R.E., NISHIHARA, T. and HEDRICK, J.L. (1974a). Fertilization envelope formation by glycoprotein agglutination and block to polyspermy in xenopus-laevis. Federation Proceedings 33: 1453-1453.
    • (1974) Federation Proceedings , vol.33 , pp. 1453-1453
    • WYRICK, R.E.1    NISHIHARA, T.2    HEDRICK, J.L.3
  • 147
    • 0344726713 scopus 로고
    • Agglutination of jelly coat and cortical granule components and the block to polyspermy in the amphibian Xenopus laevis
    • WYRICK, R.E., NISHIHARA, T. and HEDRICK, J.L. (1974b). Agglutination of jelly coat and cortical granule components and the block to polyspermy in the amphibian Xenopus laevis. Proceedings of the National Academy of Sciences USA 71: 2067-2071.
    • (1974) Proceedings of the National Academy of Sciences USA , vol.71 , pp. 2067-2071
    • WYRICK, R.E.1    NISHIHARA, T.2    HEDRICK, J.L.3
  • 148
    • 84985807758 scopus 로고
    • The synthesis and localization of envelope glycoproteins in oocytes of xenopus-laevis using immunocytochemical methods
    • YAMAGUCHI, S., HEDRICK, J.L. and KATAGIRI, C. (1989). The synthesis and localization of envelope glycoproteins in oocytes of xenopus-laevis using immunocytochemical methods. Development Growth & Differentiation 31: 85-94.
    • (1989) Development Growth & Differentiation , vol.31 , pp. 85-94
    • YAMAGUCHI, S.1    HEDRICK, J.L.2    KATAGIRI, C.3
  • 149
    • 0024052833 scopus 로고
    • Classification, inhibition, and specificity studies of the vitelline coat lysin from toad sperm
    • YAMASAKI, H., TAKAMUNE, K. and KATAGIRI, C. (1988). Classification, inhibition, and specificity studies of the vitelline coat lysin from toad sperm. Gamete Research 20: 287-300.
    • (1988) Gamete Research , vol.20 , pp. 287-300
    • YAMASAKI, H.1    TAKAMUNE, K.2    KATAGIRI, C.3
  • 150
    • 0025288445 scopus 로고
    • Selective degradation of specific components of fertilization coat and differentiation of hatching gland-cells during the 2 phase hatching of buto-japonicus embryos
    • YAMASAKI, H., KATAGIRI, C. and YOSHIZAKI, N. (1990). Selective degradation of specific components of fertilization coat and differentiation of hatching gland-cells during the 2 phase hatching of buto-japonicus embryos. Development Growth & Differentiation 32: 65-72.
    • (1990) Development Growth & Differentiation , vol.32 , pp. 65-72
    • YAMASAKI, H.1    KATAGIRI, C.2    YOSHIZAKI, N.3
  • 151
    • 0030814963 scopus 로고    scopus 로고
    • cDNA cloning and sequence analysis of the Xenopus laevis egg envelope glycoprotein gp43
    • YANG, J.C. and HEDRICK, J.L. (1997). cDNA cloning and sequence analysis of the Xenopus laevis egg envelope glycoprotein gp43. Development Growth & Differentiation 39: 457-467.
    • (1997) Development Growth & Differentiation , vol.39 , pp. 457-467
    • YANG, J.C.1    HEDRICK, J.L.2
  • 152
    • 35548979382 scopus 로고    scopus 로고
    • Ubiquitin c-terminal hydrolase-activity is involved in sperm acrosomal function and anti-polyspermy defense during porcine fertilization
    • YI, Y.J., MANANDHAR, G., SUTOVSKY, M., LI, R., JONAKOVA, V., OKO, R., PARK, C.S., PRATHER, R.S. and SUTOVSKY, P. (2007). Ubiquitin c-terminal hydrolase-activity is involved in sperm acrosomal function and anti-polyspermy defense during porcine fertilization. Biology of Reproduction 77: 780-793.
    • (2007) Biology of Reproduction , vol.77 , pp. 780-793
    • YI, Y.J.1    MANANDHAR, G.2    SUTOVSKY, M.3    LI, R.4    JONAKOVA, V.5    OKO, R.6    PARK, C.S.7    PRATHER, R.S.8    SUTOVSKY, P.9
  • 153
    • 0028877229 scopus 로고
    • Involvement of N-linked carbohydrate chains of pig zona-pellucida in sperm-egg binding
    • YONEZAWA, N., AOKI, H., HATANAKA, Y. and NAKANO, M. (1995a). Involvement of N-linked carbohydrate chains of pig zona-pellucida in sperm-egg binding. European Journal of Biochemistry 233: 35-41.
    • (1995) European Journal of Biochemistry , vol.233 , pp. 35-41
    • YONEZAWA, N.1    AOKI, H.2    HATANAKA, Y.3    NAKANO, M.4
  • 154
    • 0028932425 scopus 로고    scopus 로고
    • YONEZAWA, N., HATANAKA, Y., TAKEYAMA, H. and NAKANO, M. (1995b). Binding of pig sperm receptor in the zona-pellucida to the boar sperm acrosome. Journal of Reproduction and Fertility 103: 1-8. YONEZAWA, N., FUKUI, N., KUDO, K. and NAKANO, M. (1999). Localization of neutral N-linked carbohydrate chains in pig zona pellucida glycoprotein ZPC. European Journal of Biochemistry 260: 57-63.
    • YONEZAWA, N., HATANAKA, Y., TAKEYAMA, H. and NAKANO, M. (1995b). Binding of pig sperm receptor in the zona-pellucida to the boar sperm acrosome. Journal of Reproduction and Fertility 103: 1-8. YONEZAWA, N., FUKUI, N., KUDO, K. and NAKANO, M. (1999). Localization of neutral N-linked carbohydrate chains in pig zona pellucida glycoprotein ZPC. European Journal of Biochemistry 260: 57-63.
  • 155
    • 11244311568 scopus 로고    scopus 로고
    • Participation of the nonreducing terminal beta-galactosyl residues of the neutral N-linked carbohydrate chains of porcine zona pellucida glycoproteins in sperm-egg binding
    • YONEZAWA, N., AMARI, S., TAKAHASHI, K., IKEDA, K., IMAI, F.L., KANAI, S., KIKUCHI, K. and NAKANO, M. (2005). Participation of the nonreducing terminal beta-galactosyl residues of the neutral N-linked carbohydrate chains of porcine zona pellucida glycoproteins in sperm-egg binding. Molecular Reproduction and Development 70: 222-227.
    • (2005) Molecular Reproduction and Development , vol.70 , pp. 222-227
    • YONEZAWA, N.1    AMARI, S.2    TAKAHASHI, K.3    IKEDA, K.4    IMAI, F.L.5    KANAI, S.6    KIKUCHI, K.7    NAKANO, M.8
  • 156
    • 0016732020 scopus 로고
    • Cellular basis for production and secretion of hatching enzyme by frog embryos
    • YOSHIZAKI, N. and KATAGIRI, C. (1975). Cellular basis for production and secretion of hatching enzyme by frog embryos. Journal of Experimental Zoology 192: 203-212.
    • (1975) Journal of Experimental Zoology , vol.192 , pp. 203-212
    • YOSHIZAKI, N.1    KATAGIRI, C.2
  • 157
    • 84986527704 scopus 로고
    • Disintegration of vitelline coat during hatching process in frog
    • YOSHIZAKI, N. (1978). Disintegration of vitelline coat during hatching process in frog. Journal of Experimental Zoology 203: 127-133.
    • (1978) Journal of Experimental Zoology , vol.203 , pp. 127-133
    • YOSHIZAKI, N.1
  • 158
    • 84985848351 scopus 로고
    • Oviducal contribution to alteration of the vitelline coat in the frog, Rana-japonica - an electron-microscopic study
    • YOSHIZAKI, N. and KATAGIRI, C. (1981). Oviducal contribution to alteration of the vitelline coat in the frog, Rana-japonica - an electron-microscopic study. Development Growth & Differentiation 23: 495-506.
    • (1981) Development Growth & Differentiation , vol.23 , pp. 495-506
    • YOSHIZAKI, N.1    KATAGIRI, C.2
  • 159
    • 0020433368 scopus 로고
    • Acrosome reaction in sperm of the toad, Bufo bufo japonicus
    • YOSHIZAKI, N. and KATAGIRI, C. (1982). Acrosome reaction in sperm of the toad, Bufo bufo japonicus. Gamete Research 6: 343-352.
    • (1982) Gamete Research , vol.6 , pp. 343-352
    • YOSHIZAKI, N.1    KATAGIRI, C.2
  • 160
    • 0001747716 scopus 로고
    • Changes in surface ultrastructure and proteolytic activity of hatching gland-cells during development of Xenopus embryo
    • YOSHIZAKI, N. (1991). Changes in surface ultrastructure and proteolytic activity of hatching gland-cells during development of Xenopus embryo. Zoological Science 8: 295-302.
    • (1991) Zoological Science , vol.8 , pp. 295-302
    • YOSHIZAKI, N.1
  • 161
    • 0000838383 scopus 로고
    • Morphological and biochemical-changes in the fertilization coat of Xenopus-laevis during the hatching process
    • YOSHIZAKI, N. and YAMASAKI, H. (1991). Morphological and biochemical-changes in the fertilization coat of Xenopus-laevis during the hatching process. Zoological Science 8: 303-308.
    • (1991) Zoological Science , vol.8 , pp. 303-308
    • YOSHIZAKI, N.1    YAMASAKI, H.2
  • 162
    • 0016690426 scopus 로고
    • Macromolecular-composition of Xenopus-laevis egg jelly coat
    • YUREWICZ, E.C., OLIPHANT, G. and HEDRICK, J.L. (1975). Macromolecular-composition of Xenopus-laevis egg jelly coat. Biochemistry 14: 3101-3107.
    • (1975) Biochemistry , vol.14 , pp. 3101-3107
    • YUREWICZ, E.C.1    OLIPHANT, G.2    HEDRICK, J.L.3
  • 163
    • 0023164968 scopus 로고
    • Structural characterization of the mr = 55,000 antigen (ZP3) of porcine oocyte zona-pellucida - purification and characterization of alpha-glycoprotein and beta-glycoprotein following digestion of lactosaminoglycan with endo-beta-galactosidase
    • YUREWICZ, E.C., SACCO, A.G. and SUBRAMANIAN, M.G. (1987). Structural characterization of the mr = 55,000 antigen (ZP3) of porcine oocyte zona-pellucida - purification and characterization of alpha-glycoprotein and beta-glycoprotein following digestion of lactosaminoglycan with endo-beta-galactosidase. Journal of Biological Chemistry 262: 564-571.
    • (1987) Journal of Biological Chemistry , vol.262 , pp. 564-571
    • YUREWICZ, E.C.1    SACCO, A.G.2    SUBRAMANIAN, M.G.3
  • 164
    • 0025984497 scopus 로고
    • Isolation, composition, and biological-activity of sugar chains of porcine oocyte zona-pellucida 55k-glycoproteins
    • YUREWICZ, E.C., PACK, B.A. and SACCO, A.G. (1991). Isolation, composition, and biological-activity of sugar chains of porcine oocyte zona-pellucida 55k-glycoproteins. Molecular Reproduction and
    • (1991) Molecular Reproduction and Development , vol.30 , pp. 126-134
    • YUREWICZ, E.C.1    PACK, B.A.2    SACCO, A.G.3
  • 165
    • 0027171178 scopus 로고
    • Nucleotide-sequence of cDNA-encoding ZP3-alpha, a sperm-binding glycoprotein from zona-pellucida of pig oocyte
    • YUREWICZ, E.C., HIBLER, D., FONTENOT, G.K., SACCO, A.G. and HARRIS, J. (1993a). Nucleotide-sequence of cDNA-encoding ZP3-alpha, a sperm-binding glycoprotein from zona-pellucida of pig oocyte. Biochimica Et Biophysica Acta 1174: 211-214.
    • (1993) Biochimica Et Biophysica Acta , vol.1174 , pp. 211-214
    • YUREWICZ, E.C.1    HIBLER, D.2    FONTENOT, G.K.3    SACCO, A.G.4    HARRIS, J.5
  • 166
    • 0027508206 scopus 로고
    • Porcine zona-pellucida ZP3-alpha glycoprotein mediates binding of the biotin-labeled m(r)-55,000 family (ZP3) to boar sperm membrane-vesicles
    • YUREWICZ, E.C., PACK, B.A., ARMANT, D.R. and SACCO, A.G. (1993b). Porcine zona-pellucida ZP3-alpha glycoprotein mediates binding of the biotin-labeled m(r)-55,000 family (ZP3) to boar sperm membrane-vesicles. Molecular Reproduction and Development 36: 382-389.
    • (1993) Molecular Reproduction and Development , vol.36 , pp. 382-389
    • YUREWICZ, E.C.1    PACK, B.A.2    ARMANT, D.R.3    SACCO, A.G.4
  • 167
    • 0032571326 scopus 로고    scopus 로고
    • Hetero-oligomerization-dependent binding of pig oocyte zona pellucida glycoproteins ZPB and ZPC to boar sperm membrane vesicles
    • YUREWICZ, E.C., SACCO, A.G., GUPTA, S.K., XU, N.X. and GAGE, D.A. (1998). Hetero-oligomerization-dependent binding of pig oocyte zona pellucida glycoproteins ZPB and ZPC to boar sperm membrane vesicles. Journal of Biological Chemistry 273: 7488-7494.
    • (1998) Journal of Biological Chemistry , vol.273 , pp. 7488-7494
    • YUREWICZ, E.C.1    SACCO, A.G.2    GUPTA, S.K.3    XU, N.X.4    GAGE, D.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.