메뉴 건너뛰기




Volumn 8, Issue 2, 2009, Pages 926-941

Hamster zona pellucida is formed by four glycoproteins: ZP1, ZP2, ZP3, and ZP4

Author keywords

Mesocncetus auratus; Oocyte; Sperm binding protein; Zona pellucida

Indexed keywords

AMINO ACID; GLYCOPROTEIN; PROTEIN ZP1; PROTEIN ZP2; PROTEIN ZP3; PROTEIN ZP4; UNCLASSIFIED DRUG;

EID: 61849147409     PISSN: 15353893     EISSN: None     Source Type: Journal    
DOI: 10.1021/pr800568x     Document Type: Article
Times cited : (50)

References (56)
  • 1
    • 0002302562 scopus 로고
    • Mammalian fertilization
    • Knobil, E, Neill, J. D, Eds, Raven Press: New York
    • Yanagimachi, R. Mammalian fertilization. Physiology of reproduction; Knobil, E., Neill, J. D., Eds.; Raven Press: New York, 1994; pp 189-317.
    • (1994) Physiology of reproduction , pp. 189-317
    • Yanagimachi, R.1
  • 2
    • 0018822414 scopus 로고
    • Structure and function of the zona pellucida: Identification and characterization of the proteins of the mouse oocyte's zona pellucida
    • Bleil, J. D.; Wassarman, P. M. Structure and function of the zona pellucida: Identification and characterization of the proteins of the mouse oocyte's zona pellucida. Dev. Biol. 1980, 76, 185-202.
    • (1980) Dev. Biol , vol.76 , pp. 185-202
    • Bleil, J.D.1    Wassarman, P.M.2
  • 3
    • 0023217444 scopus 로고
    • On the macromolecular composition of the zona pellucida from porcine oocytes
    • Hedrick, J. L.; Wardrip, N. J. On the macromolecular composition of the zona pellucida from porcine oocytes. Dev. Biol. 1987, 121, 478-488.
    • (1987) Dev. Biol , vol.121 , pp. 478-488
    • Hedrick, J.L.1    Wardrip, N.J.2
  • 5
    • 16844387092 scopus 로고    scopus 로고
    • Human sperm do not bind to rat zonae pellucidae despite the presence of four homologous glycoproteins
    • Hoodbhoy, T.; Joshi, S.; Boja, E. S.; Williams, S. A.; Stanley, P.; Dean, J. Human sperm do not bind to rat zonae pellucidae despite the presence of four homologous glycoproteins. J. Biol. Chem. 2005, 280, 12721-12731.
    • (2005) J. Biol. Chem , vol.280 , pp. 12721-12731
    • Hoodbhoy, T.1    Joshi, S.2    Boja, E.S.3    Williams, S.A.4    Stanley, P.5    Dean, J.6
  • 6
    • 36849054653 scopus 로고    scopus 로고
    • Bonnet Monkey (Macaca radiata) Ovaries, like human oocytes, express four zona pellucida glycoproteins
    • Ganguly, A.; Sharma, R. K.; Gupta, S. K. Bonnet Monkey (Macaca radiata) Ovaries, like human oocytes, express four zona pellucida glycoproteins. Mol. Reprod. Dev. 2008, 75, 156-166.
    • (2008) Mol. Reprod. Dev , vol.75 , pp. 156-166
    • Ganguly, A.1    Sharma, R.K.2    Gupta, S.K.3
  • 7
    • 43249100861 scopus 로고    scopus 로고
    • Phylogenetic analysis and identification of pseudogenes reveal a progressive loss of zona pellucida genes during evolution of vertebrates
    • Goudet, G.; Mugnier, S.; Callebaut, I.; Monget, P. Phylogenetic analysis and identification of pseudogenes reveal a progressive loss of zona pellucida genes during evolution of vertebrates. Biol. Reprod. 2008, 78, 796-806.
    • (2008) Biol. Reprod , vol.78 , pp. 796-806
    • Goudet, G.1    Mugnier, S.2    Callebaut, I.3    Monget, P.4
  • 8
    • 0032719660 scopus 로고    scopus 로고
    • Identification of the true human orthologue of the mouse Zp1 gene: Evidence for greater complexity in the mammalian zona pellucida
    • Hughes, D. C.; Barratt, C. L. Identification of the true human orthologue of the mouse Zp1 gene: evidence for greater complexity in the mammalian zona pellucida. Biochim. Biophys. Acta 1999, 1447, 303-306.
    • (1999) Biochim. Biophys. Acta , vol.1447 , pp. 303-306
    • Hughes, D.C.1    Barratt, C.L.2
  • 10
    • 0034665996 scopus 로고    scopus 로고
    • The major chicken egg envelope protein ZP1 is different from ZPB and is synthesized in the liver
    • Bausek, N.; Waclawek, M.; Wolfgang, J. S.; Wohlrab, F. The major chicken egg envelope protein ZP1 is different from ZPB and is synthesized in the liver. J. Biol. Chem. 2000, 275, 28866-28872.
    • (2000) J. Biol. Chem , vol.275 , pp. 28866-28872
    • Bausek, N.1    Waclawek, M.2    Wolfgang, J.S.3    Wohlrab, F.4
  • 11
    • 0025181610 scopus 로고
    • Structural and functional relationships between mouse and hamster zona pellucida glycoproteins
    • Moller, C. C.; Bleil, J. D.; Kinloch, R. A.; Wassarman, P. M. Structural and functional relationships between mouse and hamster zona pellucida glycoproteins. Dev. Biol. 1990, 137, 276-286.
    • (1990) Dev. Biol , vol.137 , pp. 276-286
    • Moller, C.C.1    Bleil, J.D.2    Kinloch, R.A.3    Wassarman, P.M.4
  • 12
    • 0025765162 scopus 로고
    • Genomic organization and polypeptide primary structure of zona pellucida glycoprotein hZP3, the hamster sperm receptor
    • Kinloch, R. A.; Ruiz-Seiler, B.; Wassarman, P. M. Genomic organization and polypeptide primary structure of zona pellucida glycoprotein hZP3, the hamster sperm receptor. Dev. Biol. 1991, 145, 203-204.
    • (1991) Dev. Biol , vol.145 , pp. 203-204
    • Kinloch, R.A.1    Ruiz-Seiler, B.2    Wassarman, P.M.3
  • 13
    • 0024212067 scopus 로고
    • Rapid production of full-length cDNAs from rare transcript: Amplification using a single gene specific oligonucleotide primer
    • Frohman, M. A.; Dusk, M. K.; Martin, G. R. Rapid production of full-length cDNAs from rare transcript: amplification using a single gene specific oligonucleotide primer. Proc. Natl. Acad. Sci. U.SA. 1988, 85, 8998-9002.
    • (1988) Proc. Natl. Acad. Sci. U.SA , vol.85 , pp. 8998-9002
    • Frohman, M.A.1    Dusk, M.K.2    Martin, G.R.3
  • 14
    • 0024512566 scopus 로고
    • PCR-based cDNA library construction: General cDNA libraries at the level of a few cells
    • Belyavsky, A.; Vinogradova, T; Rajewsky, K. PCR-based cDNA library construction: general cDNA libraries at the level of a few cells. Nucleic Acids Res. 1989, 17, 2919-2932.
    • (1989) Nucleic Acids Res , vol.17 , pp. 2919-2932
    • Belyavsky, A.1    Vinogradova, T.2    Rajewsky, K.3
  • 16
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukariotic signal peptides and prediction of their cleavage sites
    • Nielsen, H.; Engelbrecht, J; Brunak, S.; von Heijne, G. Identification of prokaryotic and eukariotic signal peptides and prediction of their cleavage sites. Protein Eng. 1997, 10, 1-6.
    • (1997) Protein Eng , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    von Heijne, G.4
  • 17
    • 0030860232 scopus 로고    scopus 로고
    • O-GLYBASE version 2.0: A revised database of O-glycosylated proteins
    • Hansen, J. E.; Lund, O.; Rapacki, K.; Brunak, S. O-GLYBASE version 2.0: A revised database of O-glycosylated proteins. Nucleic Acids Res. 1997, 25, 278-282.
    • (1997) Nucleic Acids Res , vol.25 , pp. 278-282
    • Hansen, J.E.1    Lund, O.2    Rapacki, K.3    Brunak, S.4
  • 18
    • 0031809552 scopus 로고    scopus 로고
    • NetOglyc: Prediction of mucin type O-glycosylation sites based on sequence context and surface accesibility
    • Hansen, J. E.; Lund, O.; Tolstrup, N.; Gooley, A. A.; Williams, K. L.; Brunak, S. NetOglyc: prediction of mucin type O-glycosylation sites based on sequence context and surface accesibility. Glycoconj. J. 1998, 15, 115-130.
    • (1998) Glycoconj. J , vol.15 , pp. 115-130
    • Hansen, J.E.1    Lund, O.2    Tolstrup, N.3    Gooley, A.A.4    Williams, K.L.5    Brunak, S.6
  • 19
    • 0036370537 scopus 로고    scopus 로고
    • Prediction of glycosilation across the human proteome and the correlation to protein function
    • Gupta, R.; Brunak, S. Prediction of glycosilation across the human proteome and the correlation to protein function. Pac. Symp. Biocomput. 2002, 310-322.
    • (2002) Pac. Symp. Biocomput , pp. 310-322
    • Gupta, R.1    Brunak, S.2
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 21
    • 0030627982 scopus 로고    scopus 로고
    • Neural network prediction of translation initiation sites in eukaryotes: Perspectives for EST and genome analysis
    • Pedersen, A. G.; Nielsen, H. Neural network prediction of translation initiation sites in eukaryotes: perspectives for EST and genome analysis. Proc. Int. Conf. Intell. Syst. Mol. Biol. 1997, 5, 226-233.
    • (1997) Proc. Int. Conf. Intell. Syst. Mol. Biol , vol.5 , pp. 226-233
    • Pedersen, A.G.1    Nielsen, H.2
  • 22
    • 0025792297 scopus 로고
    • Structural features in eukaryotic mRNAs that modulate the initiation of translation
    • Kozak, M. Structural features in eukaryotic mRNAs that modulate the initiation of translation. J. Biol. Chem. 1991, 266, 19867-19870.
    • (1991) J. Biol. Chem , vol.266 , pp. 19867-19870
    • Kozak, M.1
  • 23
    • 3042521098 scopus 로고    scopus 로고
    • Improved prediction of signal peptides: SignalP 3.0
    • Bendtsen, J. D.; Nielsen, H.; von, H. G.; Brunak, S. Improved prediction of signal peptides: SignalP 3.0. J. Mol. Biol. 2004, 340, 783-795.
    • (2004) J. Mol. Biol , vol.340 , pp. 783-795
    • Bendtsen, J.D.1    Nielsen, H.2    von, H.G.3    Brunak, S.4
  • 24
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes
    • Krogh, A.; Larsson, B.; von, H. G.; Sonnhammer, E. L. Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. J. Mol. Biol. 2001, 305, 567-580.
    • (2001) J. Mol. Biol , vol.305 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    von, H.G.3    Sonnhammer, E.L.4
  • 25
    • 0842313260 scopus 로고    scopus 로고
    • Prediction of proprotein conver-tase cleavage sites
    • Ducker, P.; Brunak, S.; Blom, N. Prediction of proprotein conver-tase cleavage sites. Protein Eng. Des. Sel 2004, 17, 107-112.
    • (2004) Protein Eng. Des. Sel , vol.17 , pp. 107-112
    • Ducker, P.1    Brunak, S.2    Blom, N.3
  • 26
    • 29244453640 scopus 로고    scopus 로고
    • Structural conservation of mouse and rat zona pellucida glycoproteins. Probing the native rat zona pellucida proteome by mass spectrometry
    • Boja, E. S.; Hoodbhoy, T.; Garfield, M.; Fales, H. M. Structural conservation of mouse and rat zona pellucida glycoproteins. Probing the native rat zona pellucida proteome by mass spectrometry. Biochemistry 2005, 44, 16445-16460.
    • (2005) Biochemistry , vol.44 , pp. 16445-16460
    • Boja, E.S.1    Hoodbhoy, T.2    Garfield, M.3    Fales, H.M.4
  • 27
    • 0022429080 scopus 로고
    • Mouse egg extracellular coat is a matrix of interconnected filaments possessing a structural repeat
    • Greve, J. M.; Wassarman, P. M. Mouse egg extracellular coat is a matrix of interconnected filaments possessing a structural repeat. J. Mol. Biol. 1985, 181, 253-264.
    • (1985) J. Mol. Biol , vol.181 , pp. 253-264
    • Greve, J.M.1    Wassarman, P.M.2
  • 29
    • 0347004637 scopus 로고    scopus 로고
    • Reassessing the molecular biology of sperm-egg recognition with mouse genetics
    • Dean, J. Reassessing the molecular biology of sperm-egg recognition with mouse genetics. Bioessays 2004, 26, 29-38.
    • (2004) Bioessays , vol.26 , pp. 29-38
    • Dean, J.1
  • 30
    • 0141557578 scopus 로고    scopus 로고
    • Structural characterization of native mouse zona pellucida 'proteins using mass spectrometry
    • Boja, E. S.; Hoodbhoy, T.; Fales, H. M.; Dean, J. Structural characterization of native mouse zona pellucida 'proteins using mass spectrometry. J. Biol. Chem. 2003, 278, 34189-34202.
    • (2003) J. Biol. Chem , vol.278 , pp. 34189-34202
    • Boja, E.S.1    Hoodbhoy, T.2    Fales, H.M.3    Dean, J.4
  • 31
    • 0020823176 scopus 로고
    • Probable asymmetry in the organization of components of the hamster zona
    • Ahuja, K. K.; Bolwell, G. P. Probable asymmetry in the organization of components of the hamster zona. J. Reprod. Fertil. 1983, 69, 49-55.
    • (1983) J. Reprod. Fertil , vol.69 , pp. 49-55
    • Ahuja, K.K.1    Bolwell, G.P.2
  • 32
    • 0023889087 scopus 로고
    • A glycoprotein of oviductal origin alters biochemical properties of the zona pellucida of hamster egg
    • Oikawa, T.; Sendai, Y.; Kurata, S.; Yanagimachi, R. A glycoprotein of oviductal origin alters biochemical properties of the zona pellucida of hamster egg. Gamete Res. 1988, 19, 113-122.
    • (1988) Gamete Res , vol.19 , pp. 113-122
    • Oikawa, T.1    Sendai, Y.2    Kurata, S.3    Yanagimachi, R.4
  • 33
    • 0026545275 scopus 로고
    • A large domain common to sperm receptors (ZP2 and ZP3) and TGF-β type III receptor
    • Bork, P.; Sander, C. A large domain common to sperm receptors (ZP2 and ZP3) and TGF-β type III receptor. Fed. Eur. Biochem. Soc. 1992, 300, 237-240.
    • (1992) Fed. Eur. Biochem. Soc , vol.300 , pp. 237-240
    • Bork, P.1    Sander, C.2
  • 34
    • 0036241725 scopus 로고    scopus 로고
    • Secretion of egg envelope protein ZPc after C-terminal proteolytic processing in quail granulosa cells
    • Sasanami, T.; Pan, J.; Doi, Y.; Hisada, M.; Koshaka, T.; Toriyama, M. Secretion of egg envelope protein ZPc after C-terminal proteolytic processing in quail granulosa cells. Eur. J. Biochem. 2002, 269, 2223-2231.
    • (2002) Eur. J. Biochem , vol.269 , pp. 2223-2231
    • Sasanami, T.1    Pan, J.2    Doi, Y.3    Hisada, M.4    Koshaka, T.5    Toriyama, M.6
  • 36
    • 0036042540 scopus 로고    scopus 로고
    • Localization of N-linked carbohydrate cahins in glycoprotein ZPA of the bovine egg zona pellucida
    • Ikeda, K.; Yonezawa, N.; Naoi, K.; Katsumata, T.; Hamano, S.; Nakano, M. Localization of N-linked carbohydrate cahins in glycoprotein ZPA of the bovine egg zona pellucida. Eur. J. Biochem. 2002, 269, 4257-4266.
    • (2002) Eur. J. Biochem , vol.269 , pp. 4257-4266
    • Ikeda, K.1    Yonezawa, N.2    Naoi, K.3    Katsumata, T.4    Hamano, S.5    Nakano, M.6
  • 37
    • 0016374598 scopus 로고
    • Development of the zona pellucida in the rat oocyte
    • Kang, Y. Development of the zona pellucida in the rat oocyte. Am. J. Anat. 1974, 139, 535-566.
    • (1974) Am. J. Anat , vol.139 , pp. 535-566
    • Kang, Y.1
  • 38
    • 0016538915 scopus 로고
    • Ultrastructural localization of lectin binding sites on the zona pellucida and plasma membranes of mammalian eggs
    • Nicolson, G. L.; Yanagimachi, R.; Yanagimachi, H. Ultrastructural localization of lectin binding sites on the zona pellucida and plasma membranes of mammalian eggs. J. Cell Biol. 1975, 66, 263-274.
    • (1975) J. Cell Biol , vol.66 , pp. 263-274
    • Nicolson, G.L.1    Yanagimachi, R.2    Yanagimachi, H.3
  • 39
    • 0033772543 scopus 로고    scopus 로고
    • Differential expression of glycoside residues in the mammalian zona pellucida
    • Avilés, M.; Okinaga, T.; Shur, B. D.; Ballesta, J. Differential expression of glycoside residues in the mammalian zona pellucida. Mol. Reprod. Dev. 2000, 57, 296-308.
    • (2000) Mol. Reprod. Dev , vol.57 , pp. 296-308
    • Avilés, M.1    Okinaga, T.2    Shur, B.D.3    Ballesta, J.4
  • 40
    • 0016739307 scopus 로고
    • Labeling of the zona pellucida of mouse oocytes
    • Oakberg, E. F.; Tyrell, P. D. Labeling of the zona pellucida of mouse oocytes. Biol. Reprod. 1975, 12, 477-482.
    • (1975) Biol. Reprod , vol.12 , pp. 477-482
    • Oakberg, E.F.1    Tyrell, P.D.2
  • 41
    • 0017327567 scopus 로고
    • Radioautographic study of glycoprotein biosynthesis and renewal in the ovarian follicles of mice and the origin of the zona pellucida
    • Haddad, A.; Nagai, E. T. Radioautographic study of glycoprotein biosynthesis and renewal in the ovarian follicles of mice and the origin of the zona pellucida. Cell Tissue Res. 1977, 177, 347-369.
    • (1977) Cell Tissue Res , vol.177 , pp. 347-369
    • Haddad, A.1    Nagai, E.T.2
  • 42
    • 0031183547 scopus 로고    scopus 로고
    • Carbohydrates and fertilization: An overview
    • Benoff, S. Carbohydrates and fertilization: an overview. Mol. Hum. Reprod. 1997, 3, 599-637.
    • (1997) Mol. Hum. Reprod , vol.3 , pp. 599-637
    • Benoff, S.1
  • 43
    • 0030872253 scopus 로고    scopus 로고
    • Mammalian fertilization: A carbohydrate-mediate event
    • Tulsiani, D. R.; Yoshida-Komiya, H.; Araki, Y. Mammalian fertilization: a carbohydrate-mediate event. Biol. Reprod. 1997, 57, 487-494.
    • (1997) Biol. Reprod , vol.57 , pp. 487-494
    • Tulsiani, D.R.1    Yoshida-Komiya, H.2    Araki, Y.3
  • 44
    • 38449086464 scopus 로고    scopus 로고
    • Sperm-egg binding requires a multiplicity of receptor-ligand interactions: New insights into the nature of gamete receptors derived from reproductive tract secretions
    • Ling, R.; Shur, B. D. Sperm-egg binding requires a multiplicity of receptor-ligand interactions: new insights into the nature of gamete receptors derived from reproductive tract secretions. Soc. Reprod. Fertil. Suppl. 2007, 65, 335-351.
    • (2007) Soc. Reprod. Fertil. Suppl , vol.65 , pp. 335-351
    • Ling, R.1    Shur, B.D.2
  • 45
    • 0038105489 scopus 로고    scopus 로고
    • Identification of the carboxyl termini of porcine zona pellucida glycoproteins ZPB and ZPC
    • Yonezawa, N.; Nakano, M. Identification of the carboxyl termini of porcine zona pellucida glycoproteins ZPB and ZPC. Biochem. Biophys. Res. Commun. 2003, 307, 877-882.
    • (2003) Biochem. Biophys. Res. Commun , vol.307 , pp. 877-882
    • Yonezawa, N.1    Nakano, M.2
  • 48
    • 9144252658 scopus 로고    scopus 로고
    • Dell, A.; Chalabi, S.; Easton, R. L.; Haslam, S. M.; Sutton-Smith, M.; Patankar, M. S.; Lattanzio, F.; Panico, M.; Morris, H. R.; Clark, G. F. Murine and human zona pellucida 3 derived from mouse eggs express identical O-glycans. PNAS Dev. Biol. 2003,100, 15631-15636.
    • Dell, A.; Chalabi, S.; Easton, R. L.; Haslam, S. M.; Sutton-Smith, M.; Patankar, M. S.; Lattanzio, F.; Panico, M.; Morris, H. R.; Clark, G. F. Murine and human zona pellucida 3 derived from mouse eggs express identical O-glycans. PNAS Dev. Biol. 2003,100, 15631-15636.
  • 49
    • 0039107603 scopus 로고    scopus 로고
    • Localization of neutral N-linked carbohydrate chains in pig zona pellucida glycoprotein ZPC
    • Yonezawa, N.; Fukui, K.; Kudo, K.; Nakano, M. Localization of neutral N-linked carbohydrate chains in pig zona pellucida glycoprotein ZPC. Eur. J. Biochem. 1999, 260, 57-63.
    • (1999) Eur. J. Biochem , vol.260 , pp. 57-63
    • Yonezawa, N.1    Fukui, K.2    Kudo, K.3    Nakano, M.4
  • 51
    • 0025837567 scopus 로고
    • Distribution of lectin receptors sites in the zona pellucida of follicular and ovulated rat oocytes
    • Shalgi, R.; Maymon, R.; Bar-Shira, B.; Amihai, D.; Skutelsky, E. Distribution of lectin receptors sites in the zona pellucida of follicular and ovulated rat oocytes. Mol. Reprod. Dev. 1991, 29, 365-372.
    • (1991) Mol. Reprod. Dev , vol.29 , pp. 365-372
    • Shalgi, R.1    Maymon, R.2    Bar-Shira, B.3    Amihai, D.4    Skutelsky, E.5
  • 52
    • 0028360154 scopus 로고
    • Cytochemical characterization of oligosaccharide side chains of the glycoproteins of rat zona pellucida: An ultrastructural study
    • Avilés, M.; Martínez-Menárguez, J. A.; Castells, M. T.; Madrid, J. F.; Ballesta, J. Cytochemical characterization of oligosaccharide side chains of the glycoproteins of rat zona pellucida: an ultrastructural study. Anat. Rec. 1994, 239, 137-149.
    • (1994) Anat. Rec , vol.239 , pp. 137-149
    • Avilés, M.1    Martínez-Menárguez, J.A.2    Castells, M.T.3    Madrid, J.F.4    Ballesta, J.5
  • 53
    • 0029743117 scopus 로고    scopus 로고
    • Modifications of the lectin binding pattern in the zona pellucida of rat after fertilization
    • Avilés, M.; Jaber, L.; Castells, M. T.; Kan, F. W. K.; Ballesta, J. Modifications of the lectin binding pattern in the zona pellucida of rat after fertilization. Mol. Reprod. Dev. 1996, 44, 370-381.
    • (1996) Mol. Reprod. Dev , vol.44 , pp. 370-381
    • Avilés, M.1    Jaber, L.2    Castells, M.T.3    Kan, F.W.K.4    Ballesta, J.5
  • 54
    • 0030782216 scopus 로고    scopus 로고
    • Modifications of carbohydrate residues in ZP2 and ZP3 in the mouse zona pellucida glycoproteins after fertilization
    • Avilés, M.; Jaber, L.; Castells, M. T.; Ballesta, J.; Kan, F. W. K. Modifications of carbohydrate residues in ZP2 and ZP3 in the mouse zona pellucida glycoproteins after fertilization. Biol. Reprod. 1997, 57, 1155-1163.
    • (1997) Biol. Reprod , vol.57 , pp. 1155-1163
    • Avilés, M.1    Jaber, L.2    Castells, M.T.3    Ballesta, J.4    Kan, F.W.K.5
  • 55
    • 0030750481 scopus 로고    scopus 로고
    • Localization of penultimate carbohydrate residues in zona pellucida and acrosomes by means of lectin cytochemistry and enzymatic treatments
    • Avilés, M.; Castells, M. T.; Martínez-Menárguez, I. A.; Abascal, I.; Ballesta, J. Localization of penultimate carbohydrate residues in zona pellucida and acrosomes by means of lectin cytochemistry and enzymatic treatments. Histochem. J. 1997, 29, 583-592.
    • (1997) Histochem. J , vol.29 , pp. 583-592
    • Avilés, M.1    Castells, M.T.2    Martínez-Menárguez, I.A.3    Abascal, I.4    Ballesta, J.5
  • 56
    • 0028314002 scopus 로고
    • Variations in the distribution of sugar residues in the zona pellucida as possible species-specific determinants of mammalian oocytes
    • Skutelsky, E.; Ranen, E.; Shalgi, R. Variations in the distribution of sugar residues in the zona pellucida as possible species-specific determinants of mammalian oocytes. J. Reprod. Fert. 1994, 100, 35-41.
    • (1994) J. Reprod. Fert , vol.100 , pp. 35-41
    • Skutelsky, E.1    Ranen, E.2    Shalgi, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.