메뉴 건너뛰기




Volumn 85, Issue 5, 1996, Pages 629-637

The molecules of mammalian fertilization

Author keywords

[No Author keywords available]

Indexed keywords

ACROSOME REACTION; CELL ADHESION; CELL INTERACTION; EXTRACELLULAR MATRIX; FERTILIZATION; GAMETE; GENE EXPRESSION; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL; REVIEW; ZONA PELLUCIDA;

EID: 0029896017     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)81230-1     Document Type: Review
Times cited : (215)

References (70)
  • 1
    • 0028955151 scopus 로고
    • Monoclonal antibodies which recognize equatorial segment epitopes presented de novo following the A23187-induced acrosome reaction of guinea pig sperm
    • Allen, C.A., and Green, D.P.L. (1995). Monoclonal antibodies which recognize equatorial segment epitopes presented de novo following the A23187-induced acrosome reaction of guinea pig sperm. J. Cell Sci. 108, 767-777.
    • (1995) J. Cell Sci. , vol.108 , pp. 767-777
    • Allen, C.A.1    Green, D.P.L.2
  • 3
    • 0030062129 scopus 로고    scopus 로고
    • Characterization of novel complexes on the cell surface between integrins and proteins with 4 transmembrane domains (TM4 proteins)
    • Berditchevski, F., Zutter, M.M., and Hemler, M.E. (1996). Characterization of novel complexes on the cell surface between integrins and proteins with 4 transmembrane domains (TM4 proteins). Mol. Biol. Cell 7, 193-207.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 193-207
    • Berditchevski, F.1    Zutter, M.M.2    Hemler, M.E.3
  • 4
    • 0025075878 scopus 로고
    • Identification of a ZP3-binding protein on acrosome-intact mouse sperm by photoaffinity crosslinking
    • Bleil, J.D., and Wassarman, P.M. (1990). Identification of a ZP3-binding protein on acrosome-intact mouse sperm by photoaffinity crosslinking. Proc. Natl. Acad. Sci. USA 87, 5563-5567.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 5563-5567
    • Bleil, J.D.1    Wassarman, P.M.2
  • 5
    • 0023731968 scopus 로고
    • Identification of a secondary sperm receptor in the mouse egg zona pellucida: Role in maintenance of binding of acrosome-reacted sperm to eggs
    • Bleil, J.D., Greve, J.M., and Wassarman, P.M. (1988). Identification of a secondary sperm receptor in the mouse egg zona pellucida: role in maintenance of binding of acrosome-reacted sperm to eggs. Dev. Biol. 128, 376-385.
    • (1988) Dev. Biol. , vol.128 , pp. 376-385
    • Bleil, J.D.1    Greve, J.M.2    Wassarman, P.M.3
  • 6
    • 0026510747 scopus 로고
    • A potential fusion peptide and an integrin ligand domain in a protein active in sperm-egg fusion
    • Blobel, C.P., Wolfsberg, T.G., Turck, C.W., Myles, D.G., Primakoff, P., and White, J.M. (1992). A potential fusion peptide and an integrin ligand domain in a protein active in sperm-egg fusion. Nature 356, 248-252.
    • (1992) Nature , vol.356 , pp. 248-252
    • Blobel, C.P.1    Wolfsberg, T.G.2    Turck, C.W.3    Myles, D.G.4    Primakoff, P.5    White, J.M.6
  • 7
    • 0029063226 scopus 로고
    • Tissue- and species-specific expression of sp56, a mouse sperm fertilization protein
    • Bookbinder, L.H., Cheng, A., and Bleil, J.D. (1995).Tissue- and species-specific expression of sp56, a mouse sperm fertilization protein. Science 269, 86-89.
    • (1995) Science , vol.269 , pp. 86-89
    • Bookbinder, L.H.1    Cheng, A.2    Bleil, J.D.3
  • 8
    • 0029078864 scopus 로고
    • Echistatin, a disintegrin, inhibits sperm-oolemmal adhesion but not oocyte penetration
    • Bronson, R.A., Gailit, J., Bronson, S., and Oula, L. (1995). Echistatin, a disintegrin, inhibits sperm-oolemmal adhesion but not oocyte penetration. Fert. Ster. 64, 414-420.
    • (1995) Fert. Ster. , vol.64 , pp. 414-420
    • Bronson, R.A.1    Gailit, J.2    Bronson, S.3    Oula, L.4
  • 9
    • 0029042753 scopus 로고
    • Interaction of a tyrosine kinase from human sperm with the zona pellucida at fertilization
    • Burks, D.J., Carballada, R., Moore, H.D.M., and Saling, P.M. (1995). Interaction of a tyrosine kinase from human sperm with the zona pellucida at fertilization. Science 269, 83-86.
    • (1995) Science , vol.269 , pp. 83-86
    • Burks, D.J.1    Carballada, R.2    Moore, H.D.M.3    Saling, P.M.4
  • 10
    • 0029155323 scopus 로고
    • Distribution and dynamics of mouse sperm surface galactosyltransferase: Implications for mammalian fertilization
    • Cardullo, R.A., and Wolf, D.E. (1995). Distribution and dynamics of mouse sperm surface galactosyltransferase: implications for mammalian fertilization. Biochemistry 34, 10027-10035.
    • (1995) Biochemistry , vol.34 , pp. 10027-10035
    • Cardullo, R.A.1    Wolf, D.E.2
  • 11
    • 0028227343 scopus 로고
    • Sperm-egg recognition in the mouse: Characterization of sp56, a sperm protein having specific affinity for ZP3
    • Cheng, A., Le, T., Palacios, M., Bookbinder, L.H., Wassarman, P.M., Suzuki, F., and Bleil, J.D. (1994). Sperm-egg recognition in the mouse: characterization of sp56, a sperm protein having specific affinity for ZP3. J. Cell Biol. 125, 867-878.
    • (1994) J. Cell Biol. , vol.125 , pp. 867-878
    • Cheng, A.1    Le, T.2    Palacios, M.3    Bookbinder, L.H.4    Wassarman, P.M.5    Suzuki, F.6    Bleil, J.D.7
  • 12
    • 0028987936 scopus 로고
    • Integrins and signal transduction pathways: The road taken
    • Clark, E.A., and Brugge, J.S. (1995). Integrins and signal transduction pathways: the road taken. Science 268, 233-239.
    • (1995) Science , vol.268 , pp. 233-239
    • Clark, E.A.1    Brugge, J.S.2
  • 13
    • 0029143629 scopus 로고
    • Photolabeling identifies a putative fusion domain in the envelope glycoprotein of rabies and vesicular stomatitis viruses
    • Durrer, P., Gaudin, Y., Ruigrok, R.W.H., Graf, R., and Brunner, J. (1995). Photolabeling identifies a putative fusion domain in the envelope glycoprotein of rabies and vesicular stomatitis viruses. J. Biol. Chem. 270, 17575-17581.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17575-17581
    • Durrer, P.1    Gaudin, Y.2    Ruigrok, R.W.H.3    Graf, R.4    Brunner, J.5
  • 14
    • 0029118482 scopus 로고
    • Fus2 localizes near the site of cell fusion and is required for both cell fusion and nuclear alignment during zygote formation
    • Elion, E.A., Trueheart, J., and Fink, G.R. (1995). Fus2 localizes near the site of cell fusion and is required for both cell fusion and nuclear alignment during zygote formation. J. Cell Biol. 130, 1283-1296.
    • (1995) J. Cell Biol. , vol.130 , pp. 1283-1296
    • Elion, E.A.1    Trueheart, J.2    Fink, G.R.3
  • 15
    • 0029162781 scopus 로고
    • Mouse sperm-egg plasma membrane interactions: Analysis of roles of egg integrins and the mouse sperm homologue of PH-30 (fertilin) β
    • Evans, J.P., Schultz, R.M., and Kopf, G.S. (1995). Mouse sperm-egg plasma membrane interactions: analysis of roles of egg integrins and the mouse sperm homologue of PH-30 (fertilin) β. J. Cell Sci. 108, 3267-3278.
    • (1995) J. Cell Sci. , vol.108 , pp. 3267-3278
    • Evans, J.P.1    Schultz, R.M.2    Kopf, G.S.3
  • 16
    • 0028136068 scopus 로고
    • 2+ are initiated by the zona pellucida during acrosomal exocytosis
    • 2+ are initiated by the zona pellucida during acrosomal exocytosis. Dev. Biol. 165, 152-164.
    • (1994) Dev. Biol. , vol.165 , pp. 152-164
    • Florman, H.M.1
  • 17
    • 0027416845 scopus 로고
    • Sea urchin egg receptor for sperm: Sequence similarity of binding domain and hsp70
    • Foltz, K.R., Partin, J.S., and Lennarz, W.J. (1993). Sea urchin egg receptor for sperm: sequence similarity of binding domain and hsp70. Science 259, 1421-1425.
    • (1993) Science , vol.259 , pp. 1421-1425
    • Foltz, K.R.1    Partin, J.S.2    Lennarz, W.J.3
  • 18
    • 85023448302 scopus 로고
    • + requirements for capacitation and acrosomal exocytosis in mammalian sperm
    • + requirements for capacitation and acrosomal exocytosis in mammalian sperm. Int. Rev. Cytol. 149, 1-49.
    • (1994) Int. Rev. Cytol. , vol.149 , pp. 1-49
    • Fraser, L.R.1
  • 19
    • 0029094342 scopus 로고
    • Activation of a G protein complex by aggregation of β-1,4 galactosyltransferase on the surface of sperm
    • Gong, X.H., Dubois, D.H., Miller, D.J., and Shur, B.D. (1995). Activation of a G protein complex by aggregation of β-1,4 galactosyltransferase on the surface of sperm. Science 269, 1718-1721.
    • (1995) Science , vol.269 , pp. 1718-1721
    • Gong, X.H.1    Dubois, D.H.2    Miller, D.J.3    Shur, B.D.4
  • 22
    • 0028846510 scopus 로고
    • A sperm membrane protein that binds in a species-specific manner to the egg extracellular matrix is homologous to van Willebrand factor
    • Hardy, D.M., and Garbers, D.L. (1995). A sperm membrane protein that binds in a species-specific manner to the egg extracellular matrix is homologous to van Willebrand factor. J. Biol. Chem. 270, 26025-26028.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26025-26028
    • Hardy, D.M.1    Garbers, D.L.2
  • 23
    • 0024312610 scopus 로고
    • The hexokinase isoenzyme PII of Saccharomyces cerevisiae is a protein kinase
    • Herrero, P., Fernandez, R., and Moreno, F. (1989). The hexokinase isoenzyme PII of Saccharomyces cerevisiae is a protein kinase. J. Gen. Microbiol. 135, 1209-1216.
    • (1989) J. Gen. Microbiol. , vol.135 , pp. 1209-1216
    • Herrero, P.1    Fernandez, R.2    Moreno, F.3
  • 24
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation, and signaling in cell adhesion
    • Hynes, R.O. (1992). Integrins: versatility, modulation, and signaling in cell adhesion. Cell 69, 11-25.
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 25
    • 0001911523 scopus 로고    scopus 로고
    • Egg membranes during fertilization
    • S.G. Schultz, T. Andreoli, A. Brown, D. Fambrough, J. Hoffman, and M. Welsh, ed. (New York: Plenum Publishing Co.), in press
    • Jaffe, L.A. (1996). Egg membranes during fertilization. In Molecular Biology of Membrane Transport Disorders, S.G. Schultz, T. Andreoli, A. Brown, D. Fambrough, J. Hoffman, and M. Welsh, ed. (New York: Plenum Publishing Co.), in press.
    • (1996) Molecular Biology of Membrane Transport Disorders
    • Jaffe, L.A.1
  • 26
    • 0028111490 scopus 로고
    • p95, the major phosphotyrosine-containing protein in mouse spermatozoa, is a hexokinase with unique properties
    • Kalab, P., Visconti, P., Leclerc, P., and Kopf, G.S. (1994). p95, the major phosphotyrosine-containing protein in mouse spermatozoa, is a hexokinase with unique properties. J. Biol. Chem. 269, 3810-3817.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3810-3817
    • Kalab, P.1    Visconti, P.2    Leclerc, P.3    Kopf, G.S.4
  • 27
    • 0030051131 scopus 로고    scopus 로고
    • Molecular cloning of a protein kinase whose phosphorylation is regulated by gametic adhesion during Chlamydomonas fertilization
    • Kurvari, V., Zhang, Y., Luo, Y., and Snell, W. (1996). Molecular cloning of a protein kinase whose phosphorylation is regulated by gametic adhesion during Chlamydomonas fertilization. Proc. Natl. Acad. Sci. USA 193, 39-43.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.193 , pp. 39-43
    • Kurvari, V.1    Zhang, Y.2    Luo, Y.3    Snell, W.4
  • 28
    • 0029030462 scopus 로고
    • Mouse sperm adenylyl cyclase: General properties and regulation by the zona pellucida
    • Leclerc, P., and Kopf, G.S. (1995). Mouse sperm adenylyl cyclase: general properties and regulation by the zona pellucida. Biol. Reprod. 52, 1227-1233.
    • (1995) Biol. Reprod. , vol.52 , pp. 1227-1233
    • Leclerc, P.1    Kopf, G.S.2
  • 29
    • 0024356430 scopus 로고
    • 95 kd sperm proteins bind ZP3 and serve astyrosine kinasesubstrates in responseto zona binding
    • Leyton, L., and Saling, P. (1989). 95 kd sperm proteins bind ZP3 and serve astyrosine kinasesubstrates in responseto zona binding. Cell 57, 1123-1130.
    • (1989) Cell , vol.57 , pp. 1123-1130
    • Leyton, L.1    Saling, P.2
  • 30
    • 0027080725 scopus 로고
    • Regulation of mousegamete interaction by a sperm tyrosine kinase
    • Leyton, L., Leguen, P., Bunch, D., and Saling, P.M. (1992). Regulation of mousegamete interaction by a sperm tyrosine kinase. Proc. Natl. Acad. Sci. USA 89, 11692-11695.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 11692-11695
    • Leyton, L.1    Leguen, P.2    Bunch, D.3    Saling, P.M.4
  • 31
    • 0028882345 scopus 로고
    • LL95 monoclonal antibody mimics functional effects of ZP3 on mouse sperm: Evidence that the antigen recognized is not hexokinase
    • Leyton, L., Tomes, C., and Saling, P. (1995). LL95 monoclonal antibody mimics functional effects of ZP3 on mouse sperm: evidence that the antigen recognized is not hexokinase. Mol. Reprod. Dev. 42, 347-358.
    • (1995) Mol. Reprod. Dev. , vol.42 , pp. 347-358
    • Leyton, L.1    Tomes, C.2    Saling, P.3
  • 32
    • 0028237149 scopus 로고
    • A hyaluronidase activity of the sperm plasma membrane protein PH-20 enables sperm to penetrate the cumulus cell layer surrounding the egg
    • Lin, Y., Mahan, K., Lathrop, W.F., Myles, D.G., and Primakoff, P. (1994). A hyaluronidase activity of the sperm plasma membrane protein PH-20 enables sperm to penetrate the cumulus cell layer surrounding the egg. J. Cell Biol. 125, 1157-1163.
    • (1994) J. Cell Biol. , vol.125 , pp. 1157-1163
    • Lin, Y.1    Mahan, K.2    Lathrop, W.F.3    Myles, D.G.4    Primakoff, P.5
  • 33
    • 0028841726 scopus 로고
    • Delayed translation and posttranslational processing of cyritestin, an integral transmembrane protein of the mouse acrosome
    • Linder, B., Bammer, S., and Heinlein, U.A.O. (1995). Delayed translation and posttranslational processing of cyritestin, an integral transmembrane protein of the mouse acrosome. Expt. Cell Res. 221, 66-72.
    • (1995) Expt. Cell Res. , vol.221 , pp. 66-72
    • Linder, B.1    Bammer, S.2    Heinlein, U.A.O.3
  • 35
    • 0026611050 scopus 로고
    • Complementarity between sperm surface 3-1,4-galactosyl-transferase and egg-coat ZP3 mediates sperm egg binding
    • Miller, D.J., Macek, M.B., and Shur, B.D. (1992). Complementarity between sperm surface (3-1,4-galactosyl-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
  • 36
    • 0027752372 scopus 로고
    • Egg cortical granule N-acetylglucosaminidase is required for the mouse zona block to polyspermy
    • Miller, D.J., Gong, X., Decker, G., and Shur, B.D. (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
  • 37
    • 0028293970 scopus 로고
    • Membrane interactive and conformational properties of the putative fusion peptide of PH-30, a protein active in sperm-egg fusion
    • Muga, A., Neugebauer, W., Hirama, T., and Surewicz, W.K. (1994). Membrane interactive and conformational properties of the putative fusion peptide of PH-30, a protein active in sperm-egg fusion. Biochem. 33, 4444-4448.
    • (1994) Biochem. , vol.33 , pp. 4444-4448
    • Muga, A.1    Neugebauer, W.2    Hirama, T.3    Surewicz, W.K.4
  • 38
    • 0027275871 scopus 로고
    • Molecular mechanisms of sperm-egg membrane binding and fusion in mammals
    • Myles, D.G. (1993). Molecular mechanisms of sperm-egg membrane binding and fusion in mammals. Dev. Biol. 158, 35-45.
    • (1993) Dev. Biol. , vol.158 , pp. 35-45
    • Myles, D.G.1
  • 39
    • 0028325475 scopus 로고
    • Identification of a binding site in the disintegrin domain of fertilin required for sperm-egg fusion
    • Myles, D.G., Kimmel, L.H., Blobel, C.P., White, J.M., and Primakoff, P. (1994). Identification of a binding site in the disintegrin domain of fertilin required for sperm-egg fusion. Proc. Natl. Acad. Sci. USA 91, 4195-4198.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 4195-4198
    • Myles, D.G.1    Kimmel, L.H.2    Blobel, C.P.3    White, J.M.4    Primakoff, P.5
  • 40
    • 0028218423 scopus 로고
    • Interaction of the HIV-1 fusion peptide with phospholipid vesicles: Different structural requirements for fusion and leakage
    • Nieva, J.L., Nir, S., Muga, A., Goni, F.M., and Wilschut, J. (1994). Interaction of the HIV-1 fusion peptide with phospholipid vesicles: different structural requirements for fusion and leakage. Biochemistry 33, 3201-3209.
    • (1994) Biochemistry , vol.33 , pp. 3201-3209
    • Nieva, J.L.1    Nir, S.2    Muga, A.3    Goni, F.M.4    Wilschut, J.5
  • 41
    • 0030031745 scopus 로고    scopus 로고
    • Sperm from mice carrying two t haplotypes do not possess a tyrosine phosphorylated form of hexokinase
    • Olds-Clarke, P., Pilder, S.H., Visconti, P.E., Moss, S.B., Orth, J.M., and Kopf, G.S. (1996). Sperm from mice carrying two t haplotypes do not possess a tyrosine phosphorylated form of hexokinase. Mol. Reprod. Dev. 43, 94-104.
    • (1996) Mol. Reprod. Dev. , vol.43 , pp. 94-104
    • Olds-Clarke, P.1    Pilder, S.H.2    Visconti, P.E.3    Moss, S.B.4    Orth, J.M.5    Kopf, G.S.6
  • 42
    • 0030035074 scopus 로고    scopus 로고
    • Calcium oscillations in mammalian eggs triggered by a soluble sperm factor
    • Parrington, J., Swann, K., Shevchenko, V.I., Sesay, A.K., and Lai, F.A. (1996). Calcium oscillations in mammalian eggs triggered by a soluble sperm factor. Nature 379, 364-368.
    • (1996) Nature , vol.379 , pp. 364-368
    • Parrington, J.1    Swann, K.2    Shevchenko, V.I.3    Sesay, A.K.4    Lai, F.A.5
  • 43
    • 0022373098 scopus 로고
    • A role for the migrating sperm surface antigen PH-20 in guinea pig sperm binding to the egg zona pellucida
    • Primakoff, P., Hyatt, H., and Myles, D.G. (1985). A role for the migrating sperm surface antigen PH-20 in guinea pig sperm binding to the egg zona pellucida. J. Cell Biol. 101, 2239-2244.
    • (1985) J. Cell Biol. , vol.101 , pp. 2239-2244
    • Primakoff, P.1    Hyatt, H.2    Myles, D.G.3
  • 44
    • 0023100910 scopus 로고
    • Identification and purification of a sperm surface protein with a potential role in sperm-egg membrane fusion
    • Primakoff, P., Hyatt, H., and Tredick-Kline, J. (1987). Identification and purification of a sperm surface protein with a potential role in sperm-egg membrane fusion. J. Cell Biol. 104, 141-149.
    • (1987) J. Cell Biol. , vol.104 , pp. 141-149
    • Primakoff, P.1    Hyatt, H.2    Tredick-Kline, J.3
  • 46
    • 0028650360 scopus 로고
    • Exocytosis in spermatozoa in response to progesterone and zona pellucida
    • Roldan, E.R.S., Murase, T., and Shi, Q.X. (1994). Exocytosis in spermatozoa in response to progesterone and zona pellucida. Science 266, 1578-1581.
    • (1994) Science , vol.266 , pp. 1578-1581
    • Roldan, E.R.S.1    Murase, T.2    Shi, Q.X.3
  • 47
    • 0028143698 scopus 로고
    • Mechanisms of intracellular protein transport
    • Rothman, J.E. (1994). Mechanisms of intracellular protein transport. Nature 372, 55-63.
    • (1994) Nature , vol.372 , pp. 55-63
    • Rothman, J.E.1
  • 48
    • 0028825543 scopus 로고
    • Regulation of growth factor activation by proteoglycans: What is the role of low affinity receptors?
    • Schlessinger, J., Lax, I., and Lemmon, M. (1995). Regulation of growth factor activation by proteoglycans: What is the role of low affinity receptors? Cell 83, 357-360.
    • (1995) Cell , vol.83 , pp. 357-360
    • Schlessinger, J.1    Lax, I.2    Lemmon, M.3
  • 49
    • 0018366421 scopus 로고
    • A specific defect in galactosyltransferase regulation on sperm bearing mutant alleles of the T/t locus
    • Shur, B.D., and Bennett, D. (1979). A specific defect in galactosyltransferase regulation on sperm bearing mutant alleles of the T/t locus. Dev. Biol. 71, 243-259.
    • (1979) Dev. Biol. , vol.71 , pp. 243-259
    • Shur, B.D.1    Bennett, D.2
  • 50
    • 0024297290 scopus 로고
    • Plasma membrane association, purification, and partial characterization of mouse sperm beta 1,4-galactosyltransferase
    • Shur, B.D., and Neely, C.A. (1988). Plasma membrane association, purification, and partial characterization of mouse sperm beta 1,4-galactosyltransferase. J. Biol. Chem. 263, 17706-17714.
    • (1988) J. Biol. Chem. , vol.263 , pp. 17706-17714
    • Shur, B.D.1    Neely, C.A.2
  • 51
    • 0027982876 scopus 로고
    • Traffic signals for lymphocyte recirculation and leukocyte emigration: The multistep paradigm
    • Springer, T.A. (1994). Traffic signals for lymphocyte recirculation and leukocyte emigration: the multistep paradigm. Cell 76, 301-314.
    • (1994) Cell , vol.76 , pp. 301-314
    • Springer, T.A.1
  • 52
    • 0029061703 scopus 로고
    • Extraordinary divergence and positive Darwinian selection in a fusagenic protein coating the acrosomal process of abalone spermatozoa
    • Swanson, W.J., and Vacquier, V.D. (1995). Extraordinary divergence and positive Darwinian selection in a fusagenic protein coating the acrosomal process of abalone spermatozoa. Proc. Natl. Acad. Sci. USA 92, 4957-4961.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 4957-4961
    • Swanson, W.J.1    Vacquier, V.D.2
  • 53
    • 0029016878 scopus 로고
    • Biochemical characterization of a glycosylphosphatidylinositol-linked hyaluronidase on mouse sperm
    • Thaler, C.D., and Cardullo, R.A. (1995). Biochemical characterization of a glycosylphosphatidylinositol-linked hyaluronidase on mouse sperm. Biochemistry 34, 7788-7795.
    • (1995) Biochemistry , vol.34 , pp. 7788-7795
    • Thaler, C.D.1    Cardullo, R.A.2
  • 54
    • 0028982258 scopus 로고
    • Oocyte Gal alpha 1,3 Gal epitopes implicated in sperm adhesion to the zona pellucida glycoprotein ZP3 are not required for fertilization in the mouse
    • Thall, A.D., Maly, P., and Lowe, J.B. (1995). Oocyte Gal alpha 1,3 Gal epitopes implicated in sperm adhesion to the zona pellucida glycoprotein ZP3 are not required for fertilization in the mouse. J. Biol. Chem. 270, 21437-21440.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21437-21440
    • Thall, A.D.1    Maly, P.2    Lowe, J.B.3
  • 55
    • 0028910318 scopus 로고
    • Inhibition of zona pellucida gene expression by antisense oligonucleotides injected into mouse oocytes
    • Tong, Z.B., Nelson, L.M., and Dean, J. (1995). Inhibition of zona pellucida gene expression by antisense oligonucleotides injected into mouse oocytes. J. Biol. Chem. 270, 849-853.
    • (1995) J. Biol. Chem. , vol.270 , pp. 849-853
    • Tong, Z.B.1    Nelson, L.M.2    Dean, J.3
  • 56
    • 0027633311 scopus 로고
    • Identification of porcine oocyte 55 kDa alpha and beta proteins within the zona pellucida glycoprotein families indicates that oocyte sperm receptor activity is associated with different zona pellucida proteins in different mammalian species
    • Topfer-Petersen, E., Mann, K., and Calvete, J.J. (1993). Identification of porcine oocyte 55 kDa alpha and beta proteins within the zona pellucida glycoprotein families indicates that oocyte sperm receptor activity is associated with different zona pellucida proteins in different mammalian species. Biol. Chem. Hoppe Seyler 374, 411-417.
    • (1993) Biol. Chem. Hoppe Seyler , vol.374 , pp. 411-417
    • Topfer-Petersen, E.1    Mann, K.2    Calvete, J.J.3
  • 57
  • 59
    • 0029125139 scopus 로고
    • Inositol 1,4,5-trisphosphate receptors selectively localized to the acrosomes of mammalian sperm
    • Walensky, LD., and Snyder, S.H. (1995). Inositol 1,4,5-trisphosphate receptors selectively localized to the acrosomes of mammalian sperm. J. Cell Biol. 730, 857-869.
    • (1995) J. Cell Biol. , vol.730 , pp. 857-869
    • Walensky, L.D.1    Snyder, S.H.2
  • 60
    • 0027297159 scopus 로고
    • Molecular events mediating sperm activation
    • Ward, C.R., and Kopf, G.S. (1993). Molecular events mediating sperm activation. Dev. Biol. 158, 9-34.
    • (1993) Dev. Biol. , vol.158 , pp. 9-34
    • Ward, C.R.1    Kopf, G.S.2
  • 61
    • 0028181719 scopus 로고
    • Selective activation of G-i1 and G-i2 in mouse sperm by the zona pellucida, the egg's extracellular matrix
    • Ward, C., Storey, B., and Kopf, G. (1994). Selective activation of G-i1 and G-i2 in mouse sperm by the zona pellucida, the egg's extracellular matrix. J. Biol. Chem. 269, 13254-13258.
    • (1994) J. Biol. Chem. , vol.269 , pp. 13254-13258
    • Ward, C.1    Storey, B.2    Kopf, G.3
  • 62
    • 0029122317 scopus 로고
    • Towards a molecular mechanism for gamete adhesion and fusion during mammalian fertilization
    • Wassarman, P.M. (1995). Towards a molecular mechanism for gamete adhesion and fusion during mammalian fertilization.Curr. Opin. Cell Biol. 7, 658-664.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 658-664
    • Wassarman, P.M.1
  • 63
  • 64
    • 0028230414 scopus 로고
    • Cloning and functional expression of a cyclic-nucleotide-gated channel from mammalian sperm
    • Weyand, I., Godde, M., Frings, S., Weiner, J., Muller, F., Altenhofen, W., Hatt, H., and Kaupp, U.B. (1994). Cloning and functional expression of a cyclic-nucleotide-gated channel from mammalian sperm. Nature 368, 859-863.
    • (1994) Nature , vol.368 , pp. 859-863
    • Weyand, I.1    Godde, M.2    Frings, S.3    Weiner, J.4    Muller, F.5    Altenhofen, W.6    Hatt, H.7    Kaupp, U.B.8
  • 66
    • 0028820623 scopus 로고
    • ADAM, a novel family of membrane proteins containing A Disintegrin And Metalloprotease domain: Multipotential functions in cell-cell and cell-matrix interactions
    • Wolfsberg, T.G., Primakoff, P., Myles, D.G., and White, J.M. (1995). ADAM, a novel family of membrane proteins containing A Disintegrin And Metalloprotease domain: multipotential functions in cell-cell and cell-matrix interactions. J. Cell Biol. 737, 275-278.
    • (1995) J. Cell Biol. , vol.737 , pp. 275-278
    • Wolfsberg, T.G.1    Primakoff, P.2    Myles, D.G.3    White, J.M.4
  • 68
    • 0002302562 scopus 로고
    • Mammalian fertilization
    • E. Knobil and J.D. Neill, eds. (New York: Raven Press)
    • Yanagimachi, R. (1994). Mammalian fertilization. In The Physiology of Reproduction, E. Knobil and J.D. Neill, eds. (New York: Raven Press), pp. 189-317.
    • (1994) The Physiology of Reproduction , pp. 189-317
    • Yanagimachi, R.1
  • 69
    • 0028016498 scopus 로고
    • Overexpressing sperm surface β1,4-galactosyltransferase in transgenic mice affects multiple aspects of sperm-egg interactions
    • Youakim, A., Hathaway, H.J., Miller, D.J., Gong, X., and Shur, B.D. (1994). Overexpressing sperm surface β1,4-galactosyltransferase in transgenic mice affects multiple aspects of sperm-egg interactions. J. Cell Biol. 126, 1573-1583.
    • (1994) J. Cell Biol. , vol.126 , pp. 1573-1583
    • Youakim, A.1    Hathaway, H.J.2    Miller, D.J.3    Gong, X.4    Shur, B.D.5
  • 70
    • 0026327353 scopus 로고
    • ATP-dependent regulation of flagellar adenylylcyclase in gametes of Chlamydomonas reinhardtii
    • Zhang, Y., Ross, E.M., and Snell, W.J. (1991). ATP-dependent regulation of flagellar adenylylcyclase in gametes of Chlamydomonas reinhardtii. J. Biol. Chem. 266, 22954-22959.
    • (1991) J. Biol. Chem. , vol.266 , pp. 22954-22959
    • Zhang, Y.1    Ross, E.M.2    Snell, W.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.