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Volumn 187, Issue 1, 1997, Pages 79-93

Characterization of the binding of recombinant mouse sperm fertilin β subunit to mouse eggs: Evidence for adhesive activity via an egg β1 integrin-mediated interaction

Author keywords

[No Author keywords available]

Indexed keywords

FERTILIN; INTEGRIN; MEMBRANE PROTEIN; UNCLASSIFIED DRUG;

EID: 0031193325     PISSN: 00121606     EISSN: None     Source Type: Journal    
DOI: 10.1006/dbio.1997.8611     Document Type: Article
Times cited : (138)

References (64)
  • 1
    • 0024337558 scopus 로고
    • Identification and characterization of cell-substratum adhesion receptors on cultured endothelial cells
    • Albelda S. M., Daise M., Levine E. M., Buck C. A. Identification and characterization of cell-substratum adhesion receptors on cultured endothelial cells. J. Clin. Invest. 83:1989;1992-2002.
    • (1989) J. Clin. Invest. , vol.83 , pp. 1992-2002
    • Albelda, S.M.1    Daise, M.2    Levine, E.M.3    Buck, C.A.4
  • 2
    • 0028955151 scopus 로고
    • Monoclonal antibodies which recognize equatorial segment epitopes presentedde novo
    • Allen C. A., Green D. P. L. Monoclonal antibodies which recognize equatorial segment epitopes presentedde novo. J. Cell Sci. 108:1995;767-777.
    • (1995) J. Cell Sci. , vol.108 , pp. 767-777
    • Allen, C.A.1    Green, D.P.L.2
  • 4
    • 0024451936 scopus 로고
    • Trophoblast/leukocyte-common antigen is expressed by human testicular germ cells and appears on the surface of acrosome-reacted-sperm
    • Anderson D. J., Michealson J. S., Johnson P. M. Trophoblast/leukocyte-common antigen is expressed by human testicular germ cells and appears on the surface of acrosome-reacted-sperm. Biol. Reprod. 41:1989;285-293.
    • (1989) Biol. Reprod. , vol.41 , pp. 285-293
    • Anderson, D.J.1    Michealson, J.S.2    Johnson, P.M.3
  • 5
    • 0027444742 scopus 로고
    • The role of complement component C3b and its receptors in sperm-oocyte interaction
    • Anderson D. J., Abbott A. F., Jack R. M. The role of complement component C3b and its receptors in sperm-oocyte interaction. Proc. Natl. Acad. Sci. USA. 90:1993;10051-10055.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10051-10055
    • Anderson, D.J.1    Abbott, A.F.2    Jack, R.M.3
  • 6
    • 0027930754 scopus 로고
    • Sequence and expression of a monkey testicular transcript encoding tMDC I, a novel member of the metalloprotease-like, disintegrin-like, cysteine-rich (MDC) protein family
    • Barker H. L., Perry A. C. F., Jones R., Hall L. Sequence and expression of a monkey testicular transcript encoding tMDC I, a novel member of the metalloprotease-like, disintegrin-like, cysteine-rich (MDC) protein family. Biochim. Biophys. Acta. 1218:1994;429-431.
    • (1994) Biochim. Biophys. Acta. , vol.1218 , pp. 429-431
    • Barker, H.L.1    Perry, A.C.F.2    Jones, R.3    Hall, L.4
  • 7
    • 0023731968 scopus 로고
    • Identification of a secondary sperm receptor in the mouse eggzona pellucida:
    • Bleil J. D., Greve J. M., Wassarman P. M. Identification of a secondary sperm receptor in the mouse eggzona pellucida: Dev. Biol. 128:1988;376-385.
    • (1988) Dev. Biol. , vol.128 , pp. 376-385
    • Bleil, J.D.1    Greve, J.M.2    Wassarman, P.M.3
  • 8
    • 0025371355 scopus 로고
    • Proteolytic processing of a protein involved in sperm-egg fusion correlates with acquisition of fertilization competence
    • Blobel C. P., Myles D. G., Primakoff P., White J. M. Proteolytic processing of a protein involved in sperm-egg fusion correlates with acquisition of fertilization competence. J. Cell Biol. 111:1990;69-67.
    • (1990) J. Cell Biol. , vol.111 , pp. 69-167
    • Blobel, C.P.1    Myles, D.G.2    Primakoff, P.3    White, J.M.4
  • 9
    • 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., White J. M. A potential fusion peptide and an integrin ligand domain in a protein active in sperm-egg fusion. Nature. 356:1992;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
  • 10
    • 84988074679 scopus 로고
    • Improved silver staining of plant proteins, RNA, and DNA in polyacrylamide gels
    • Blum H., Beier H., Gross H. J. Improved silver staining of plant proteins, RNA, and DNA in polyacrylamide gels. Electrophoresis. 8:1987;93-99.
    • (1987) Electrophoresis , vol.8 , pp. 93-99
    • Blum, H.1    Beier, H.2    Gross, H.J.3
  • 11
    • 0022655747 scopus 로고
    • An improved method for isolation of fertilezona
    • Boldt J., Wolf D. P. An improved method for isolation of fertilezona. Gamete Res. 13:1986;213-222.
    • (1986) Gamete Res. , vol.13 , pp. 213-222
    • Boldt, J.1    Wolf, D.P.2
  • 12
    • 0023715973 scopus 로고
    • Enzymatic alteration of the ability of mouse egg plasma membrane to interact with sperm
    • Boldt J., Howe A. M., Preble J. Enzymatic alteration of the ability of mouse egg plasma membrane to interact with sperm. Biol. Reprod. 39:1988;19-27.
    • (1988) Biol. Reprod. , vol.39 , pp. 19-27
    • Boldt, J.1    Howe, A.M.2    Preble, J.3
  • 13
    • 0024672217 scopus 로고
    • Characterization of cell surfaces polypeptides of unfertilized, fertilized, and protease-treatedzona
    • Boldt J., Gunter L. E., Howe A. M. Characterization of cell surfaces polypeptides of unfertilized, fertilized, and protease-treatedzona. Gamete Res. 23:1989;91-101.
    • (1989) Gamete Res. , vol.23 , pp. 91-101
    • Boldt, J.1    Gunter, L.E.2    Howe, A.M.3
  • 14
    • 0025650560 scopus 로고
    • Evidence that an Arg-Gly-Asp adhesion sequence plays a role in mammalian fertilization
    • Bronson R. A., Fusi F. M. Evidence that an Arg-Gly-Asp adhesion sequence plays a role in mammalian fertilization. Biol. Reprod. 43:1990;1019-1025.
    • (1990) Biol. Reprod. , vol.43 , pp. 1019-1025
    • Bronson, R.A.1    Fusi, F.M.2
  • 15
    • 0029078864 scopus 로고
    • Echistatin, a disintegrin, inhibits sperm oolemal adhesion but not oocyte penetration
    • Bronson R. A., Gailit J., Bronson S., Oula L. Echistatin, a disintegrin, inhibits sperm oolemal adhesion but not oocyte penetration. Fert. Steril. 64:1995;414-420.
    • (1995) Fert. Steril. , vol.64 , pp. 414-420
    • Bronson, R.A.1    Gailit, J.2    Bronson, S.3    Oula, L.4
  • 16
    • 0022977603 scopus 로고
    • Integrin (the CSAT antigen): Functionality requires oligomeric integrity
    • Buck C. A., Shea E., Duggan K., Horwirz A. F. Integrin (the CSAT antigen): Functionality requires oligomeric integrity. J. Cell Biol. 103:1986;2421-2428.
    • (1986) J. Cell Biol. , vol.103 , pp. 2421-2428
    • Buck, C.A.1    Shea, E.2    Duggan, K.3    Horwirz, A.F.4
  • 18
    • 0025315789 scopus 로고
    • Cell adhesion, spreading and neurite stimulation by laminin fragment E8 depends on maintenance of secondary and tertiary structure in its rod and globular domain
    • Deutzmann R., Aumailley M., Wiedemann H., Pysny W., Timpl R., Edgar E. Cell adhesion, spreading and neurite stimulation by laminin fragment E8 depends on maintenance of secondary and tertiary structure in its rod and globular domain. Eur. J. Biochem. 191:1990;513-522.
    • (1990) Eur. J. Biochem. , vol.191 , pp. 513-522
    • Deutzmann, R.1    Aumailley, M.2    Wiedemann, H.3    Pysny, W.4    Timpl, R.5    Edgar, E.6
  • 19
    • 0028929353 scopus 로고
    • Identification and localization of integrin subunits in oocytes and eggs of the mouse
    • Evans J. P., Schultz R. M., Kopf G. S. Identification and localization of integrin subunits in oocytes and eggs of the mouse. Mol. Reprod. Dev. 40:1995a;211-220.
    • (1995) Mol. Reprod. Dev. , vol.40 , pp. 211-220
    • Evans, J.P.1    Schultz, R.M.2    Kopf, G.S.3
  • 20
    • 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., Kopf G. S. 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. 108:1995b;3267-3278.
    • (1995) J. Cell Sci. , vol.108 , pp. 3267-3278
    • Evans, J.P.1    Schultz, R.M.2    Kopf, G.S.3
  • 21
    • 0031194395 scopus 로고    scopus 로고
    • Characterization of the bindery of recombinant mouse sperm fertilin α subunit to mouse eggs: Evidence for function as a cell adhesion molecule in sperm-egg binding
    • Evans J. P., Schultz R. M., Kopf G. S. Characterization of the bindery of recombinant mouse sperm fertilin α subunit to mouse eggs: Evidence for function as a cell adhesion molecule in sperm-egg binding. Dev. Biol. 187:1997;94-106.
    • (1997) Dev. Biol. , vol.187 , pp. 94-106
    • Evans, J.P.1    Schultz, R.M.2    Kopf, G.S.3
  • 22
    • 0025086346 scopus 로고
    • Localization and characterization of the acrosomal antigen recognized by GB24 on human spermatozoa
    • Fénichel P., Dohr G., Grivaux C., Cervoni F., Donzeau M., Hsi B.-L. Localization and characterization of the acrosomal antigen recognized by GB24 on human spermatozoa. Mol. Reprod. Dev. 27:1990;173-178.
    • (1990) Mol. Reprod. Dev. , vol.27 , pp. 173-178
    • Fénichel, P.1    Dohr, G.2    Grivaux, C.3    Cervoni, F.4    Donzeau, M.5    Hsi, B.-L.6
  • 23
    • 0026544398 scopus 로고
    • Sperm surface fibronectin: Expression following capacitation
    • Fusi F. M., Bronson R. A. Sperm surface fibronectin: Expression following capacitation. J. Androl. 13:1992;28-35.
    • (1992) J. Androl. , vol.13 , pp. 28-35
    • Fusi, F.M.1    Bronson, R.A.2
  • 24
    • 0025780480 scopus 로고
    • Complement component C1q and its receptor are involved in the interaction of human sperm withzona
    • Fusi F. M., Bronson R. A., Hong Y., Ghebrehiwet B. Complement component C1q and its receptor are involved in the interaction of human sperm withzona. Mol. Reprod. Dev. 29:1991;180-188.
    • (1991) Mol. Reprod. Dev. , vol.29 , pp. 180-188
    • Fusi, F.M.1    Bronson, R.A.2    Hong, Y.3    Ghebrehiwet, B.4
  • 25
    • 0026486927 scopus 로고
    • Sperm surface proteins after capacitation: Expression of vitronectin on the spermatozoan head and laminin on the sperm tail
    • Fusi F. M., Lorenzetti I., Vignali M., Bronson R. A. Sperm surface proteins after capacitation: Expression of vitronectin on the spermatozoan head and laminin on the sperm tail. J. Androl. 13:1992;488-497.
    • (1992) J. Androl. , vol.13 , pp. 488-497
    • Fusi, F.M.1    Lorenzetti, I.2    Vignali, M.3    Bronson, R.A.4
  • 29
    • 0028142840 scopus 로고
    • Integrin-ligand interactions: A year in review
    • Haas T. A., Plow E. F. Integrin-ligand interactions: a year in review. Curr. Op. Cell Biol. 6:1994;656-662.
    • (1994) Curr. Op. Cell Biol. , vol.6 , pp. 656-662
    • Haas, T.A.1    Plow, E.F.2
  • 30
    • 0029850171 scopus 로고    scopus 로고
    • Cloning and expression of recombinant rabbit fertilin
    • Hardy C. M., Holland M. K. Cloning and expression of recombinant rabbit fertilin. Mol. Reprod. Biol. 45:1996;107-116.
    • (1996) Mol. Reprod. Biol. , vol.45 , pp. 107-116
    • Hardy, C.M.1    Holland, M.K.2
  • 32
    • 0028347145 scopus 로고
    • Localization of fibronectin on the surface of human spermatozoa and relation to the sperm-egg interaction
    • Hoshi K., Sasaki H., Yanagida K., Sato A., Tsuiki A. Localization of fibronectin on the surface of human spermatozoa and relation to the sperm-egg interaction. Fert. Steril. 61:1994;542-547.
    • (1994) Fert. Steril. , vol.61 , pp. 542-547
    • Hoshi, K.1    Sasaki, H.2    Yanagida, K.3    Sato, A.4    Tsuiki, A.5
  • 33
    • 0030071684 scopus 로고    scopus 로고
    • Monoclonal antibodies against unfertilizedzona
    • Jin M., Larsson A., Nilsson B. O. Monoclonal antibodies against unfertilizedzona. Mol. Reprod. Dev. 43:1996;47-54.
    • (1996) Mol. Reprod. Dev. , vol.43 , pp. 47-54
    • Jin, M.1    Larsson, A.2    Nilsson, B.O.3
  • 34
    • 0026687270 scopus 로고
    • Recovery of penetration ability in protease treatedzona
    • Kellom T., Vick A., Boldt J. Recovery of penetration ability in protease treatedzona. Mol. Reprod. Dev. 33:1992;46-52.
    • (1992) Mol. Reprod. Dev. , vol.33 , pp. 46-52
    • Kellom, T.1    Vick, A.2    Boldt, J.3
  • 35
    • 0029670028 scopus 로고    scopus 로고
    • Metargidin, a membrane-anchored metalloprotease-disintegrin protein with an RGD integrin-binding sequence
    • Krätzschmar J., Lum L., Blobel C. P. Metargidin, a membrane-anchored metalloprotease-disintegrin protein with an RGD integrin-binding sequence. J. Biol. Chem. 271:1996;4593-4596.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4593-4596
    • Krätzschmar, J.1    Lum, L.2    Blobel, C.P.3
  • 36
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of the bacteriophage T4
    • Laemmli U. K. Cleavage of structural proteins during the assembly of the head of the bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 37
    • 0028841726 scopus 로고
    • Delayed translation and posttranslational processing of cyritestin, an integral membrane protein of the mouse acrosome
    • Linder B., Bammer S., Heinlein U. A. O. Delayed translation and posttranslational processing of cyritestin, an integral membrane protein of the mouse acrosome. Exp. Cell Res. 221:1995;66-72.
    • (1995) Exp. Cell Res. , vol.221 , pp. 66-72
    • Linder, B.1    Bammer, S.2    Heinlein, U.A.O.3
  • 38
    • 0027972994 scopus 로고
    • Integrin mediated cell adhesion: The extracellular face
    • Loftus J. C., Smith J. W., Ginsberg M. H. Integrin mediated cell adhesion: The extracellular face. J. Biol. Chem. 269:1994;25235-25238.
    • (1994) J. Biol. Chem. , vol.269 , pp. 25235-25238
    • Loftus, J.C.1    Smith, J.W.2    Ginsberg, M.H.3
  • 39
    • 0023430459 scopus 로고
    • Redistribution of mouse sperm surface galactosyltransferase after the acrosome reaction
    • Lopez L. C., Shur B. D. Redistribution of mouse sperm surface galactosyltransferase after the acrosome reaction. J. Cell. Biol. 105:1987;1663-1670.
    • (1987) J. Cell. Biol. , vol.105 , pp. 1663-1670
    • Lopez, L.C.1    Shur, B.D.2
  • 40
    • 0025785915 scopus 로고
    • Differential binding of gold-labeled zona pellucida glycoproteins mZP2 and mZP3 to mouse sperm membrane compartments
    • Mortillo S., Wassarman P. M. Differential binding of gold-labeled zona pellucida glycoproteins mZP2 and mZP3 to mouse sperm membrane compartments. Development. 113:1991;141-149.
    • (1991) Development , vol.113 , pp. 141-149
    • Mortillo, S.1    Wassarman, P.M.2
  • 41
    • 0027275871 scopus 로고
    • Molecular mechanisms of sperm-egg membrane binding and fusion in mammals
    • Myles D. G. Molecular mechanisms of sperm-egg membrane binding and fusion in mammals. Dev. Biol. 158:1993;35-45.
    • (1993) Dev. Biol. , vol.158 , pp. 35-45
    • Myles, D.G.1
  • 42
    • 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., Primakoff P. Identification of a binding site in the disintegrin domain of fertilin required for sperm-egg fusion. Proc. Natl. Acad. Sci. USA. 91:1994;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
  • 43
    • 0023801763 scopus 로고
    • Effect of a monclonal anti-mouse sperm antibody (OBF13) on the interaction of mouse sperm with zona-free mouse and hamster eggs
    • Okabe M., Yagasaki M., Oda H., Matzno S., Kohama Y., Mimura T. Effect of a monclonal anti-mouse sperm antibody (OBF13) on the interaction of mouse sperm with zona-free mouse and hamster eggs. J. Reprod. Immunol. 13:1988;211-219.
    • (1988) J. Reprod. Immunol. , vol.13 , pp. 211-219
    • Okabe, M.1    Yagasaki, M.2    Oda, H.3    Matzno, S.4    Kohama, Y.5    Mimura, T.6
  • 44
    • 0025646684 scopus 로고
    • A human sperm antigen possibly involved in binding and/or fusion with zona-free hamster eggs
    • Okabe M., Nagira M., Kawai Y., Matzno S., Mimura T., Tanaka K. A human sperm antigen possibly involved in binding and/or fusion with zona-free hamster eggs. Fertil. Steril. 54:1990;1121-1126.
    • (1990) Fertil. Steril. , vol.54 , pp. 1121-1126
    • Okabe, M.1    Nagira, M.2    Kawai, Y.3    Matzno, S.4    Mimura, T.5    Tanaka, K.6
  • 45
    • 0029021536 scopus 로고
    • Cloning and analysis of monkey fertilin reveals novel α subunit isoforms
    • Perry A. C. F., Gichuhi P. M., Jones R., Hall L. Cloning and analysis of monkey fertilin reveals novel α subunit isoforms. Biochem. J. 307:1995;843-850.
    • (1995) Biochem. J. , vol.307 , pp. 843-850
    • Perry, A.C.F.1    Gichuhi, P.M.2    Jones, R.3    Hall, L.4
  • 46
    • 0023100910 scopus 로고
    • Identification and purification of a sperm surface protein with a potential role in sperm-egg membrane fusion
    • Primakoff P., Hyatt H., Tredick-Kline J. Identification and purification of a sperm surface protein with a potential role in sperm-egg membrane fusion. J. Cell Biol. 104:1987;141-149.
    • (1987) J. Cell Biol. , vol.104 , pp. 141-149
    • Primakoff, P.1    Hyatt, H.2    Tredick-Kline, J.3
  • 47
    • 0030069394 scopus 로고    scopus 로고
    • Initial evaluation of fertilin as an immunocontraceptive antigen and molecular cloning of the cynomolgus monkey fertilin β subunit
    • Ramarao C. S., Myles D. G., White J. M., Primakoff P. Initial evaluation of fertilin as an immunocontraceptive antigen and molecular cloning of the cynomolgus monkey fertilin β subunit. Mol. Reprod. Dev. 43:1996;70-75.
    • (1996) Mol. Reprod. Dev. , vol.43 , pp. 70-75
    • Ramarao, C.S.1    Myles, D.G.2    White, J.M.3    Primakoff, P.4
  • 48
    • 0029788321 scopus 로고    scopus 로고
    • KUZ, a conserved metalloprotease-disintegrin protein with two roles inDrosophila
    • Rooke J., Pan D., Xu T., Rubin G. M. KUZ, a conserved metalloprotease-disintegrin protein with two roles inDrosophila. Science. 273:1996;1227-1231.
    • (1996) Science , vol.273 , pp. 1227-1231
    • Rooke, J.1    Pan, D.2    Xu, T.3    Rubin, G.M.4
  • 49
    • 0022258280 scopus 로고
    • Mouse sperm antigens that participates in fertilization: I. Inhibitions of sperm fusion with the egg plasma membrane using monoclonal antibodies
    • Saling P. M., Irons G., Waibel R. Mouse sperm antigens that participates in fertilization: I. Inhibitions of sperm fusion with the egg plasma membrane using monoclonal antibodies. Biol. Reprod. 33:1985;515-526.
    • (1985) Biol. Reprod. , vol.33 , pp. 515-526
    • Saling, P.M.1    Irons, G.2    Waibel, R.3
  • 52
    • 0023771015 scopus 로고
    • Identification and characterization of a novel antigen complex on mouse mammary tumor cells using a monoclonal antibody against platelet glycoprotein Ic
    • Sonnenberg A., Hogervorst F., Osterop A., Veltman F. E. M. Identification and characterization of a novel antigen complex on mouse mammary tumor cells using a monoclonal antibody against platelet glycoprotein Ic. J. Biol. Chem. 263:1988a;14030-14038.
    • (1988) J. Biol. Chem. , vol.263 , pp. 14030-14038
    • Sonnenberg, A.1    Hogervorst, F.2    Osterop, A.3    Veltman, F.E.M.4
  • 53
    • 0023812375 scopus 로고
    • Laminin receptor on platelets is the integrin VLA-6
    • Sonnenberg A., Modderman P. W., Hogervorst F. Laminin receptor on platelets is the integrin VLA-6. Nature. 336:1988b;487-489.
    • (1988) Nature , vol.336 , pp. 487-489
    • Sonnenberg, A.1    Modderman, P.W.2    Hogervorst, F.3
  • 55
    • 0025325167 scopus 로고
    • Cadherins: A molecular family important in selective cell-cell adhesion
    • Takeichi M. Cadherins: A molecular family important in selective cell-cell adhesion. Annu. Rev. Biochem. 59:1990;237-252.
    • (1990) Annu. Rev. Biochem. , vol.59 , pp. 237-252
    • Takeichi, M.1
  • 57
    • 0031025409 scopus 로고    scopus 로고
    • Human fertilin β: Identification, characterization, and chromosonal mapping of an ADMA gene family member
    • Vidaeus C. M., Von Kapp-Herr C., Golden W., Eddy R. L., Shows T. B., Herr J. C. Human fertilin β: Identification, characterization, and chromosonal mapping of an ADMA gene family member. Mol. Rep. Dev. 46:1997;363-369.
    • (1997) Mol. Rep. Dev. , vol.46 , pp. 363-369
    • Vidaeus, C.M.1    Von Kapp-Herr, C.2    Golden, W.3    Eddy, R.L.4    Shows, T.B.5    Herr, J.C.6
  • 58
    • 0030049705 scopus 로고    scopus 로고
    • MDC9, a widely expressed cellular disintegrin containing SH3 ligand domains
    • Weskamp G., Krätzschmar J., Reid M. S., Blobel C. P. MDC9, a widely expressed cellular disintegrin containing SH3 ligand domains. J. Cell Biol. 132:1996;717-726.
    • (1996) J. Cell Biol. , vol.132 , pp. 717-726
    • Weskamp, G.1    Krätzschmar, J.2    Reid, M.S.3    Blobel, C.P.4
  • 59
    • 0000617203 scopus 로고
    • Nutrient requirements for the culture of preimplantation embryosin vitro
    • Whitten W. K. Nutrient requirements for the culture of preimplantation embryosin vitro. Adv. Bio. Sci. 6:1971;129-139.
    • (1971) Adv. Bio. Sci. , vol.6 , pp. 129-139
    • Whitten, W.K.1
  • 60
    • 0027431501 scopus 로고
    • The precursor region of a protein active in sperm-egg fusion contains metalloprotease domain and a disintegrin domain: Structural, functional, and evolutionary implications
    • Wolfsberg T. G., Bazan J. F., Blobel C. P., Myles D. G., Primakoff P., White J. M. The precursor region of a protein active in sperm-egg fusion contains metalloprotease domain and a disintegrin domain: Structural, functional, and evolutionary implications. Proc. Natl. Acad. Sci. USA. 90:1993;10783-10787.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10783-10787
    • Wolfsberg, T.G.1    Bazan, J.F.2    Blobel, C.P.3    Myles, D.G.4    Primakoff, P.5    White, J.M.6
  • 61
    • 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., White J. M. 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. 131:1995a;275-278.
    • (1995) J. Cell Biol. , vol.131 , pp. 275-278
    • Wolfsberg, T.G.1    Primakoff, P.2    Myles, D.G.3    White, J.M.4
  • 62
    • 0029045064 scopus 로고
    • ADAM, a widely distributed and developmentally regulated gene family encoding membrane proteins with A Disintegrin And Metalloprotease domain
    • Wolfsberg T. G., Straight P. D., Gerena R. L., Huovila A.-P. J., Primakoff P., Myles D. G., White J. M. ADAM, a widely distributed and developmentally regulated gene family encoding membrane proteins with A Disintegrin And Metalloprotease domain. Dev. Biol. 169:1995b;378-383.
    • (1995) Dev. Biol. , vol.169 , pp. 378-383
    • Wolfsberg, T.G.1    Straight, P.D.2    Gerena, R.L.3    Huovila, A.-P.J.4    Primakoff, P.5    Myles, D.G.6    White, J.M.7
  • 64
    • 0002302562 scopus 로고
    • Mammalian fertilization
    • New York: Raven Press. p. 189-317
    • Yanagimachi R. Mammalian fertilization. The Physiology of Reproduction. 1994;Raven Press, New York. p. 189-317.
    • (1994) The Physiology of Reproduction
    • Yanagimachi, R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.