메뉴 건너뛰기




Volumn 74, Issue 5, 2007, Pages 617-628

Role of sialic acid in bovine sperm-zona pellucida binding

Author keywords

Acid sialic; Cow; Gamete interaction; Mannose; Zona pellucida

Indexed keywords

ANTIBODY; ASIALOFETUIN; FETUIN; GALACTOSE; GLYCOPROTEIN; LECTIN; MANNOSE; MEMBRANE PROTEIN; N ACETYLGALACTOSAMINE; N ACETYLGLUCOSAMINE; SIALIC ACID; SIALIDASE; SIALIDASE INHIBITOR; TRISACCHARIDE;

EID: 33947620521     PISSN: 1040452X     EISSN: 10982795     Source Type: Journal    
DOI: 10.1002/mrd.20619     Document Type: Article
Times cited : (57)

References (68)
  • 1
    • 0035040864 scopus 로고    scopus 로고
    • Essential role of the nonreducing terminal α-mannosyl residues of the N-linked carbohydrate chain of bovine zona pellucida glycoproteins in sperm-egg binding
    • Amari S, Yonezawa N, Mitsui S, Katsumata T, Hamano S, Kuwayama M, Hashimoto Y, Suzuki A, Takeda Y, Nakano M. 2001. Essential role of the nonreducing terminal α-mannosyl residues of the N-linked carbohydrate chain of bovine zona pellucida glycoproteins in sperm-egg binding. Mol Reprod Dev 59:221-226.
    • (2001) Mol Reprod Dev , vol.59 , pp. 221-226
    • Amari, S.1    Yonezawa, N.2    Mitsui, S.3    Katsumata, T.4    Hamano, S.5    Kuwayama, M.6    Hashimoto, Y.7    Suzuki, A.8    Takeda, Y.9    Nakano, M.10
  • 2
    • 0036462606 scopus 로고    scopus 로고
    • Chemical diversity in the sialic acids and related keto acids: An evolutionary perspective
    • Angata T, Varki A. 2002. Chemical diversity in the sialic acids and related keto acids: An evolutionary perspective. Chem Rev 102:439-470.
    • (2002) Chem Rev , vol.102 , pp. 439-470
    • Angata, T.1    Varki, A.2
  • 3
    • 0029779241 scopus 로고    scopus 로고
    • Immunocytochemical localization and biochemical characterization of a novel plasma membrane-associated, neutral pH optimum alpha-L-fucosidase from rat testis and epididymal spermatozoa
    • Aviles M, Abascal I, Martinez-Menarguez JA, Castells MT, Skalaban SR, Ballesta J, Alhadeff JA. 1996. Immunocytochemical localization and biochemical characterization of a novel plasma membrane-associated, neutral pH optimum alpha-L-fucosidase from rat testis and epididymal spermatozoa. Biochem J 15:821-831.
    • (1996) Biochem J , vol.15 , pp. 821-831
    • Aviles, M.1    Abascal, I.2    Martinez-Menarguez, J.A.3    Castells, M.T.4    Skalaban, S.R.5    Ballesta, J.6    Alhadeff, J.A.7
  • 4
    • 0030782216 scopus 로고    scopus 로고
    • Modifications of carbohydrate residues and ZP2 and ZP3 glycoproteins in the mouse zona pellucida after fertilization
    • Aviles M, Jaber L, Castells MT, Ballesta J, Kan FW. 1997. Modifications of carbohydrate residues and ZP2 and ZP3 glycoproteins in the mouse zona pellucida after fertilization. Biol Reprod 57:1155-1163.
    • (1997) Biol Reprod , vol.57 , pp. 1155-1163
    • Aviles, M.1    Jaber, L.2    Castells, M.T.3    Ballesta, J.4    Kan, F.W.5
  • 5
    • 0033772543 scopus 로고    scopus 로고
    • Differential expression of glycoside residues in the mammalian zona pellucida
    • Aviles M, Okinaga T, Sur BD, Ballesta J. 2000a. Differential expression of glycoside residues in the mammalian zona pellucida. Mol Reprod Dev 57:296-308.
    • (2000) Mol Reprod Dev , vol.57 , pp. 296-308
    • Aviles, M.1    Okinaga, T.2    Sur, B.D.3    Ballesta, J.4
  • 6
    • 0034030959 scopus 로고    scopus 로고
    • Cytochemical demonstration of modification of carbohydrates in the mouse zona pellucida during folliculogenesis
    • Aviles M, El-Mestrah M, Jaber L, Castells MT, Ballesta J, Kan FWK. 2000b. Cytochemical demonstration of modification of carbohydrates in the mouse zona pellucida during folliculogenesis. Histochem Cell Biol 113:207-219.
    • (2000) Histochem Cell Biol , vol.113 , pp. 207-219
    • Aviles, M.1    El-Mestrah, M.2    Jaber, L.3    Castells, M.T.4    Ballesta, J.5    Kan, F.W.K.6
  • 7
    • 0031183547 scopus 로고    scopus 로고
    • Carbohydrates and fertilization: An overview
    • Benoff S. 1997. Carbohydrates and fertilization: An overview. Mol Hum Reprod 3:599-637.
    • (1997) Mol Hum Reprod , vol.3 , pp. 599-637
    • Benoff, S.1
  • 8
    • 0036534774 scopus 로고    scopus 로고
    • Effects of sialic acid substitutions on recognition by sambucus nigra agglutinin and Maackia amurensis hemagglutinin
    • Brinkman-Van der Linden ECM, Sonnenburg JL, Varki A. 2002. Effects of sialic acid substitutions on recognition by sambucus nigra agglutinin and Maackia amurensis hemagglutinin. Anal Biochem 303:98-104.
    • (2002) Anal Biochem , vol.303 , pp. 98-104
    • Brinkman-Van der Linden, E.C.M.1    Sonnenburg, J.L.2    Varki, A.3
  • 10
    • 0001481450 scopus 로고
    • The sialic acids. VI. Purification and properties of sialidase from Clostridium Perfringens
    • Cassidy JT, Jourdian GW, Roseman S. 1965. The sialic acids. VI. Purification and properties of sialidase from Clostridium Perfringens. J Biol Chem 240:3501-3506.
    • (1965) J Biol Chem , vol.240 , pp. 3501-3506
    • Cassidy, J.T.1    Jourdian, G.W.2    Roseman, S.3
  • 11
    • 12744279374 scopus 로고    scopus 로고
    • Maintenance of meiotic arrest in bovine oocytes using the S-enantiomer of roscovitine: Effects on maturation, fertilization and subsequent embryo development in vitro
    • Coy P, Romar R, Payton RR, McCann L, Saxton AM, Edwards JL. 2005a. Maintenance of meiotic arrest in bovine oocytes using the S-enantiomer of roscovitine: Effects on maturation, fertilization and subsequent embryo development in vitro. Reproduction 129:19-26.
    • (2005) Reproduction , vol.129 , pp. 19-26
    • Coy, P.1    Romar, R.2    Payton, R.R.3    McCann, L.4    Saxton, A.M.5    Edwards, J.L.6
  • 12
    • 21044444460 scopus 로고    scopus 로고
    • Birth of piglets after transferring of in vitro-produced embryos pre-matured with R-roscovitine
    • Coy P, Romar R, Ruiz S, Canovas S, Gadea J, Garcia-Vazquez F, Matas C. 2005b. Birth of piglets after transferring of in vitro-produced embryos pre-matured with R-roscovitine. Reproduction 129:747-755.
    • (2005) Reproduction , vol.129 , pp. 747-755
    • Coy, P.1    Romar, R.2    Ruiz, S.3    Canovas, S.4    Gadea, J.5    Garcia-Vazquez, F.6    Matas, C.7
  • 13
    • 0347004637 scopus 로고    scopus 로고
    • Reassessing the molecular biology of sperm-egg recognition with mouse genetics
    • Dean J. 2004. Reassessing the molecular biology of sperm-egg recognition with mouse genetics. BioEssays 26:29-38.
    • (2004) BioEssays , vol.26 , pp. 29-38
    • Dean, J.1
  • 16
    • 0034677921 scopus 로고    scopus 로고
    • Structural analysis of murine zona pellucida glycans. Evidence for the expression of core-2-type O-glycans and the sda antigen
    • Easton RL, Patankar MS, Lattanzio FA, Leaven TH, Morris HR, Clark GF, Dell A. 2000. Structural analysis of murine zona pellucida glycans. Evidence for the expression of core-2-type O-glycans and the sda antigen. J Biol Chem 275:7731-7742.
    • (2000) J Biol Chem , vol.275 , pp. 7731-7742
    • Easton, R.L.1    Patankar, M.S.2    Lattanzio, F.A.3    Leaven, T.H.4    Morris, H.R.5    Clark, G.F.6    Dell, A.7
  • 17
    • 0030205061 scopus 로고    scopus 로고
    • Elevated temperature increases heat shock protein 70 synthesis in bovine two-cell embryos and compromises function of maturing oocytes
    • Edwards JL, Hansen PJ. 1996. Elevated temperature increases heat shock protein 70 synthesis in bovine two-cell embryos and compromises function of maturing oocytes. Biol Reprod 55: 341-346.
    • (1996) Biol Reprod , vol.55 , pp. 341-346
    • Edwards, J.L.1    Hansen, P.J.2
  • 18
    • 0032744357 scopus 로고    scopus 로고
    • Characterization of derivatization of sialic acid with 2-aminoacridone and determination of sialic acid content in glycoproteins by capillary electrophoresis and high performance liquid chromatography-ion trap mass spectrometry
    • Fa-Yun Che, Xiao-Xia Shao, Ke-Yi Wang, Qi-Chang Xia. 1999. Characterization of derivatization of sialic acid with 2-aminoacridone and determination of sialic acid content in glycoproteins by capillary electrophoresis and high performance liquid chromatography-ion trap mass spectrometry. Electrophoresis 20:2930-2937.
    • (1999) Electrophoresis , vol.20 , pp. 2930-2937
    • Che, F.1    Shao, X.2    Wang, K.3    Xia, Q.4
  • 19
    • 0037296759 scopus 로고    scopus 로고
    • Sperm surface hyaluronan binding protein (HABPl) interacts with zona pellucida of water buffalo (Bubalus bubalis) through its clustered mannose residues
    • Ghosh I, Datta K. 2003. Sperm surface hyaluronan binding protein (HABPl) interacts with zona pellucida of water buffalo (Bubalus bubalis) through its clustered mannose residues. Mol Reprod Dev 64:235-244.
    • (2003) Mol Reprod Dev , vol.64 , pp. 235-244
    • Ghosh, I.1    Datta, K.2
  • 20
    • 0024411583 scopus 로고
    • Determination of mono-O-acetylated N-acetylneuraminic acids in human and rat sera by fluorometric high-performance liquid chromatography
    • Hara S, Yamaguchi M, Takemori Y, Furuhata K, Ogura H, Nakamura M. 1989. Determination of mono-O-acetylated N-acetylneuraminic acids in human and rat sera by fluorometric high-performance liquid chromatography. Anal Biochem 179:162-166.
    • (1989) Anal Biochem , vol.179 , pp. 162-166
    • Hara, S.1    Yamaguchi, M.2    Takemori, Y.3    Furuhata, K.4    Ogura, H.5    Nakamura, M.6
  • 21
    • 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 JD, Hibler DW, Fontenot GK, Hsu KT, Yurewicz EC, Sacco AG. 1994. Cloning and characterization of zona pellucida genes and cDNAs from a variety of mammalian species: The ZPA, ZPB and ZPC gene families. DNA Seq 4:361-393.
    • (1994) DNA Seq , 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
  • 22
    • 0026653276 scopus 로고
    • Changes in the properties and composition of zona pellucida of pigs during fertilization in vitro
    • Hatanaka Y, Nagai T, Tobita T, Nakano M. 1992. Changes in the properties and composition of zona pellucida of pigs during fertilization in vitro. J Reprod Fertil 95:431-440.
    • (1992) J Reprod Fertil , vol.95 , pp. 431-440
    • Hatanaka, Y.1    Nagai, T.2    Tobita, T.3    Nakano, M.4
  • 23
    • 0027183480 scopus 로고
    • Structure of three acidic O-linked carbohydrate chains of porcine zona pellucida glycoproteins
    • Hokke CH, Damm JBL, Kamerling JP, Vliegenthart JFG. 1993. Structure of three acidic O-linked carbohydrate chains of porcine zona pellucida glycoproteins. FEBS Lett 329:29-34.
    • (1993) FEBS Lett , vol.329 , pp. 29-34
    • Hokke, C.H.1    Damm, J.B.L.2    Kamerling, J.P.3    Vliegenthart, J.F.G.4
  • 25
    • 1842843784 scopus 로고    scopus 로고
    • Insights into the molecular basis of sperm-egg recognition in mammals
    • Hoodbhoy T, Dean J. 2004. Insights into the molecular basis of sperm-egg recognition in mammals. Reproduction 127:417-422.
    • (2004) Reproduction , vol.127 , pp. 417-422
    • Hoodbhoy, T.1    Dean, J.2
  • 26
    • 0027941888 scopus 로고
    • Mammalian cortical granules: Contents, fate, and function
    • Hoodbhoy T, Talbot P. 1994. Mammalian cortical granules: Contents, fate, and function. Mol Reprod Dev 39:439-448.
    • (1994) Mol Reprod Dev , vol.39 , pp. 439-448
    • Hoodbhoy, T.1    Talbot, P.2
  • 27
    • 0025851040 scopus 로고
    • Purification and properties of cloned Salmonella typhimurium LT2 sialidase with virus-typical kinetic preference for sialyl alpha 2-3 linkages
    • Hoyer LL, Roggentin P, Schauer R, Vimr ER. 1991. Purification and properties of cloned Salmonella typhimurium LT2 sialidase with virus-typical kinetic preference for sialyl alpha 2-3 linkages. J Biochem (Tokyo) 110:462-467.
    • (1991) J Biochem (Tokyo) , vol.110 , pp. 462-467
    • Hoyer, L.L.1    Roggentin, P.2    Schauer, R.3    Vimr, E.R.4
  • 28
    • 0037081129 scopus 로고    scopus 로고
    • An improved fluorometric high-performance liquid chromatography method for sialic acid determination: An internal standard method, and its application to sialic acid analysis of human apolipoprotein E
    • Ito M, Ikeda K, Suzuki Y, Tanaka K, Saito M. 2002. An improved fluorometric high-performance liquid chromatography method for sialic acid determination: An internal standard method, and its application to sialic acid analysis of human apolipoprotein E. Anal Biochem 300:260-266.
    • (2002) Anal Biochem , vol.300 , pp. 260-266
    • Ito, M.1    Ikeda, K.2    Suzuki, Y.3    Tanaka, K.4    Saito, M.5
  • 29
    • 0032703522 scopus 로고    scopus 로고
    • Disulfide formation in bovine zona pellucida glycoproteins during fertilization: Evidence for the involvement of cystine cross-linkages in hardening of the zona pellucida
    • Iwamoto K, Ikeda K, Yonezawa N, Noguchi S, Kudo K, Hamano S, Kuwayama M, Nakano M. 1999. Disulfide formation in bovine zona pellucida glycoproteins during fertilization: Evidence for the involvement of cystine cross-linkages in hardening of the zona pellucida. J Reprod Fertil 117:395-402.
    • (1999) J Reprod Fertil , vol.117 , pp. 395-402
    • Iwamoto, K.1    Ikeda, K.2    Yonezawa, N.3    Noguchi, S.4    Kudo, K.5    Hamano, S.6    Kuwayama, M.7    Nakano, M.8
  • 31
    • 0031915969 scopus 로고    scopus 로고
    • Murine sperm-zona binding, a fucosyl residue is required for a high affinity sperm-binding ligand. A second site on sperm binds a nonfucosylated, beta-galactosyl-capped oligosaccharide
    • Johnston DS, Wright WW, Shaper JH, Hokke CH, Van den Eijnden DH, Joziasse DH. 1998. Murine sperm-zona binding, a fucosyl residue is required for a high affinity sperm-binding ligand. A second site on sperm binds a nonfucosylated, beta-galactosyl-capped oligosaccharide. J Bio Chem 273:1888-1895.
    • (1998) J Bio Chem , vol.273 , pp. 1888-1895
    • Johnston, D.S.1    Wright, W.W.2    Shaper, J.H.3    Hokke, C.H.4    Van den Eijnden, D.H.5    Joziasse, D.H.6
  • 32
    • 0029830057 scopus 로고    scopus 로고
    • Structural characterization of the N-linked carbohydrate chains of the zona pellucida glycoproteins from bovine ovarian and fertilized eggs
    • Katsumata T, Noguchi S, Yonezawa N, Tanokura M, Nakano M. 1996. Structural characterization of the N-linked carbohydrate chains of the zona pellucida glycoproteins from bovine ovarian and fertilized eggs. Eur J Biochem 240:448-453.
    • (1996) Eur J Biochem , vol.240 , pp. 448-453
    • Katsumata, T.1    Noguchi, S.2    Yonezawa, N.3    Tanokura, M.4    Nakano, M.5
  • 33
    • 0016154247 scopus 로고
    • Studies on Hemagglutinins from Maackia amurensis Seeds
    • Kawaguchi T, Matsumoto I, Osawa T. 1974. Studies on Hemagglutinins from Maackia amurensis Seeds. J Biol Chem 249:2786-2792.
    • (1974) J Biol Chem , vol.249 , pp. 2786-2792
    • Kawaguchi, T.1    Matsumoto, I.2    Osawa, T.3
  • 34
    • 0030902350 scopus 로고    scopus 로고
    • New sialic acids from biological sources identified by a comprehensive and sensitive approach: Liquid chromatography-electrospray ionization-mass spectrometry (LC-ESI-MS) of SIA quinoxalinones
    • Klein A, Diaz S, Ferreira I, Lamblin G, Roussel P, Manzi AE. 1997. New sialic acids from biological sources identified by a comprehensive and sensitive approach: Liquid chromatography-electrospray ionization-mass spectrometry (LC-ESI-MS) of SIA quinoxalinones. Glycobiology 7:421-432.
    • (1997) Glycobiology , vol.7 , pp. 421-432
    • Klein, A.1    Diaz, S.2    Ferreira, I.3    Lamblin, G.4    Roussel, P.5    Manzi, A.E.6
  • 36
    • 33751155433 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, Renkonen O, Wassarman PM. 1995. Oligosaccharide constructs with defined structures that inhibit binding of mouse sperm to unfertilized eggs in vitro. Biochemistry 34:4662-4669.
    • (1995) Biochemistry , vol.34 , pp. 4662-4669
    • Litscher, E.S.1    Juntunen, K.2    Seppo, A.3    Penttila, L.4    Niemela, R.5    Renkonen, O.6    Wassarman, P.M.7
  • 37
    • 0026611050 scopus 로고
    • Complementarity between sperm surface beta-1,4 transferase and egg-coat ZP3 mediates sperm-egg binding
    • Miller DJ, Macek MB, Shur BD. 1992. Complementarity between sperm surface beta-1,4 transferase and egg-coat ZP3 mediates sperm-egg binding. Nature 357:589-593.
    • (1992) Nature , vol.357 , pp. 589-593
    • Miller, D.J.1    Macek, M.B.2    Shur, B.D.3
  • 38
    • 0027752372 scopus 로고
    • Egg cortical granule N-acetylglucosaminidase is required for the mouse zona block to polyspermy
    • Miller DJ, Gong X, Decker G, Shur BD. 1993. Egg cortical granule N-acetylglucosaminidase is required for the mouse zona block to polyspermy. J Cell Biol 123:1431-1440.
    • (1993) J Cell Biol , vol.123 , pp. 1431-1440
    • Miller, D.J.1    Gong, X.2    Decker, G.3    Shur, B.D.4
  • 39
    • 0024515399 scopus 로고
    • Characterization of a proteinase that cleaves zona pellucida glycoprotein ZP2 following activation of mouse eggs
    • Moller CC, Wassarman PM. 1989. Characterization of a proteinase that cleaves zona pellucida glycoprotein ZP2 following activation of mouse eggs. Dev Biol 132:103-112.
    • (1989) Dev Biol , vol.132 , pp. 103-112
    • Moller, C.C.1    Wassarman, P.M.2
  • 40
    • 0034142329 scopus 로고    scopus 로고
    • Calcium ion-independent recognition of sialyl and nonsialyl N-acetyllactosamine and Lex structures by boar sperm
    • Mori E, Yoshitani N, Mori T, Takasaki S. 2000. Calcium ion-independent recognition of sialyl and nonsialyl N-acetyllactosamine and Lex structures by boar sperm. Arch Biochem Biophys 374: 86-92.
    • (2000) Arch Biochem Biophys , vol.374 , pp. 86-92
    • Mori, E.1    Yoshitani, N.2    Mori, T.3    Takasaki, S.4
  • 41
    • 0016732212 scopus 로고
    • Purification and characterization of neuraminidase from Clostridium perfringens
    • Nees SVR, Schauer R. 1975. Purification and characterization of neuraminidase from Clostridium perfringens. Hoppe Seylers Z Physiol Chem 6:1027-1042.
    • (1975) Hoppe Seylers Z Physiol Chem , vol.6 , pp. 1027-1042
    • Nees, S.V.R.1    Schauer, R.2
  • 42
    • 0002449645 scopus 로고
    • LR white embedding medium for colloidal gold methods
    • Hyat MA, editor, San Diego: Academic Press
    • Newman G. 1989. LR white embedding medium for colloidal gold methods. In: Hyat MA, editor. Colloidal gold: Principles, methods, and applications. San Diego: Academic Press. Vol. 2. pp 47-75.
    • (1989) Colloidal gold: Principles, methods, and applications , vol.2 , pp. 47-75
    • Newman, G.1
  • 43
    • 0026441404 scopus 로고
    • Structure of the acidic N-linked carbohydrate chains of the 55-kDa glycoprotein family (PZP3) from porcine zona pellucida
    • Noguchi S, Nakano M. 1992. Structure of the acidic N-linked carbohydrate chains of the 55-kDa glycoprotein family (PZP3) from porcine zona pellucida. Eur J Biochem 209:883-894.
    • (1992) Eur J Biochem , vol.209 , pp. 883-894
    • Noguchi, S.1    Nakano, M.2
  • 44
    • 0034020994 scopus 로고    scopus 로고
    • Lectin histochemical detection of sulfoglycans in the zona pellucida of mammalian antral oocytes full article
    • Parillo F, Fagioli O, Dall'Aglio C, Verini-Supplizi A. 2000. Lectin histochemical detection of sulfoglycans in the zona pellucida of mammalian antral oocytes full article. Acta Histochem 102:193-202.
    • (2000) Acta Histochem , vol.102 , pp. 193-202
    • Parillo, F.1    Fagioli, O.2    Dall'Aglio, C.3    Verini-Supplizi, A.4
  • 46
    • 4544360519 scopus 로고    scopus 로고
    • Susceptibility of bovine germinal vesicle-stage oocytes from antral follicles to direct effects of heat stress in vitro
    • Payton RR, Romar R, Coy P, Saxton AM, Lawrence JL, Edwards JL. 2004. Susceptibility of bovine germinal vesicle-stage oocytes from antral follicles to direct effects of heat stress in vitro. Biol Reprod 71:1303-1308.
    • (2004) Biol Reprod , vol.71 , pp. 1303-1308
    • Payton, R.R.1    Romar, R.2    Coy, P.3    Saxton, A.M.4    Lawrence, J.L.5    Edwards, J.L.6
  • 47
    • 0028317007 scopus 로고
    • Evidence for presence of hyaluronan binding protein on spermatozoa and its possible involvement in sperm function
    • Ranganathan S, Ganguly AK, Datta K. 1994. Evidence for presence of hyaluronan binding protein on spermatozoa and its possible involvement in sperm function. Mol Reprod Dev 38:69-76.
    • (1994) Mol Reprod Dev , vol.38 , pp. 69-76
    • Ranganathan, S.1    Ganguly, A.K.2    Datta, K.3
  • 49
    • 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, 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
  • 50
    • 0034065809 scopus 로고    scopus 로고
    • Physiological state of bull sperm affects fucose- and mannose-binding properties
    • Revah I, Gadella BM, Flesch FM, Colenbrander B, Suarez SS. 2000. Physiological state of bull sperm affects fucose- and mannose-binding properties. Biol Reprod 62:1010-1015.
    • (2000) Biol Reprod , vol.62 , pp. 1010-1015
    • Revah, I.1    Gadella, B.M.2    Flesch, F.M.3    Colenbrander, B.4    Suarez, S.S.5
  • 51
    • 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. 2004. Characterization of a novel ZP3-independent sperm-binding ligand that facilitates sperm adhesion to the egg coat. Development 131:503-512.
    • (2004) Development , vol.131 , pp. 503-512
    • Rodeheffer, C.1    Shur, B.D.2
  • 52
    • 0031887174 scopus 로고    scopus 로고
    • Analysis of the N-acetylneuraminic acid and N-glycolylneuraminic acid contents of glycoproteins by high-pH anion-exchange chromatography with pulsed amperometric detection
    • Rohrer JS, Thayer J, Weitzhandler M, Avdalovic N. 1998. Analysis of the N-acetylneuraminic acid and N-glycolylneuraminic acid contents of glycoproteins by high-pH anion-exchange chromatography with pulsed amperometric detection. Glycobiology 8:35-43.
    • (1998) Glycobiology , vol.8 , pp. 35-43
    • Rohrer, J.S.1    Thayer, J.2    Weitzhandler, M.3    Avdalovic, N.4
  • 53
    • 0032578613 scopus 로고    scopus 로고
    • Is sperm galactosyltransferase a signaling subunit of a multimeric gamete receptor?
    • Shur BD. 1998. Is sperm galactosyltransferase a signaling subunit of a multimeric gamete receptor? Biochem Biophys Res Commun 250: 537-543.
    • (1998) Biochem Biophys Res Commun , vol.250 , pp. 537-543
    • Shur, B.D.1
  • 55
    • 0028292786 scopus 로고
    • Differential recognition by conglutinin and mannan-binding protein of N-glycans presented on neoglycolipids and glycoproteins with special reference to complement glycoprotein C3 and ribonuclease B
    • Solis D, Feizi T, Yuen CT, Lawson AM, Harrison RA, Loveless RW. 1994. Differential recognition by conglutinin and mannan-binding protein of N-glycans presented on neoglycolipids and glycoproteins with special reference to complement glycoprotein C3 and ribonuclease B. J Biol Chem 269:11555-11562.
    • (1994) J Biol Chem , vol.269 , pp. 11555-11562
    • Solis, D.1    Feizi, T.2    Yuen, C.T.3    Lawson, A.M.4    Harrison, R.A.5    Loveless, R.W.6
  • 56
    • 0016245734 scopus 로고
    • Structure of the O-glycosidically linked carbohydrate units of fetuin
    • Spiro RG, Bhoyroo VD. 1974. Structure of the O-glycosidically linked carbohydrate units of fetuin. J Biol Chem 249:5704-5717.
    • (1974) J Biol Chem , vol.249 , pp. 5704-5717
    • Spiro, R.G.1    Bhoyroo, V.D.2
  • 57
    • 0028949228 scopus 로고
    • Application of a sensitive HPLC-based fluorometric assay to determine the sialic acid content of human gonadotropin isoforms
    • Stanton PG, Shen Z, Kecorius EA, Burgon PG, Robertson DM, Hearn MTW. 1995. Application of a sensitive HPLC-based fluorometric assay to determine the sialic acid content of human gonadotropin isoforms. J Biochem Biophys Methods 30:37-48.
    • (1995) J Biochem Biophys Methods , vol.30 , pp. 37-48
    • Stanton, P.G.1    Shen, Z.2    Kecorius, E.A.3    Burgon, P.G.4    Robertson, D.M.5    Hearn, M.T.W.6
  • 58
    • 0029451793 scopus 로고
    • Interactions between gametes leading to fertilization: The sperm's eye view
    • Storey B. 1995. Interactions between gametes leading to fertilization: The sperm's eye view. Reprod Fertil Dev 7:927-942.
    • (1995) Reprod Fertil Dev , vol.7 , pp. 927-942
    • Storey, B.1
  • 59
    • 0031775881 scopus 로고    scopus 로고
    • 2+-dependent lectin on sperm that recognizes lewis-a trisaccharide
    • 2+-dependent lectin on sperm that recognizes lewis-a trisaccharide. Biol Reprod 59:39-44.
    • (1998) Biol Reprod , vol.59 , pp. 39-44
    • Suarez, S.S.1    Revah, I.2    Lo, M.3    Kolle, S.4
  • 60
    • 0038808617 scopus 로고    scopus 로고
    • Cellular and molecular mechanisms leading to cortical reaction and polyspermy block in mammalian eggs
    • Sun Q-Y. 2003. Cellular and molecular mechanisms leading to cortical reaction and polyspermy block in mammalian eggs. Microsc Res Tech 61:342-348.
    • (2003) Microsc Res Tech , vol.61 , pp. 342-348
    • Sun, Q.-Y.1
  • 61
    • 0029836135 scopus 로고    scopus 로고
    • The initial molecular interaction between mouse sperm and the zona pellucida is a complex binding event
    • Thaler CD, Cardullo RA. 1996. The initial molecular interaction between mouse sperm and the zona pellucida is a complex binding event. J Biol Chem 271:23289-23297.
    • (1996) J Biol Chem , vol.271 , pp. 23289-23297
    • Thaler, C.D.1    Cardullo, R.A.2
  • 62
    • 0036136318 scopus 로고    scopus 로고
    • Distinct membrane fractions from mouse sperm bind different zona pellucida glycoproteins
    • Thaler CD, Cardullo RA. 2002. Distinct membrane fractions from mouse sperm bind different zona pellucida glycoproteins. Biol Reprod 66:65-69.
    • (2002) Biol Reprod , vol.66 , pp. 65-69
    • Thaler, C.D.1    Cardullo, R.A.2
  • 63
    • 0034630731 scopus 로고    scopus 로고
    • An O-acetylated sialyl-Tn is involved in ovarian cancer-associated antigenicity
    • Toba S, Tenno M, Kurosaka A. 2000. An O-acetylated sialyl-Tn is involved in ovarian cancer-associated antigenicity. Biochem Biophys Res Commun 271:281-286.
    • (2000) Biochem Biophys Res Commun , vol.271 , pp. 281-286
    • Toba, S.1    Tenno, M.2    Kurosaka, A.3
  • 65
    • 21644466386 scopus 로고    scopus 로고
    • Contribution of mouse egg zona pellucida glycoproteins to gamete recognition during fertilization
    • Wassarman PM. 2005. Contribution of mouse egg zona pellucida glycoproteins to gamete recognition during fertilization. J Cell Physiol 204:388-391.
    • (2005) J Cell Physiol , vol.204 , pp. 388-391
    • Wassarman, P.M.1
  • 66
    • 0002302562 scopus 로고
    • Mammalian fertilization
    • Knobil E, Neil JD, editors, New York, USA: Raven Press. pp
    • Yanagimachi R. 1994. Mammalian fertilization. In: Knobil E, Neil JD, editors. Physiology of reproduction. New York, USA: Raven Press. pp 189-317.
    • (1994) Physiology of reproduction , pp. 189-317
    • Yanagimachi, R.1
  • 67
    • 0034819583 scopus 로고    scopus 로고
    • Molecular cloning of bovine zona pellucida glycoproteins ZPA and ZPB and analysis for sperm-binding component of the zona
    • Yonezawa N, Fukui N, Kuno M, Shinoda M, Goko S, Mitsui S, Nakano M. 2001. Molecular cloning of bovine zona pellucida glycoproteins ZPA and ZPB and analysis for sperm-binding component of the zona. Eur J Biochem 268:3587-3594.
    • (2001) Eur J Biochem , vol.268 , pp. 3587-3594
    • Yonezawa, N.1    Fukui, N.2    Kuno, M.3    Shinoda, M.4    Goko, S.5    Mitsui, S.6    Nakano, M.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.