메뉴 건너뛰기




Volumn 475, Issue , 2008, Pages 99-113

Mammalian fertilization is dependent on multiple membrane fusion events

Author keywords

Acrosome reaction; Cortical reaction; Eggs; Mammalian fertilization; Sperm; Sperm egg fusion

Indexed keywords

MAMMALIA;

EID: 84934434592     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-59745-250-2_6     Document Type: Review
Times cited : (26)

References (75)
  • 2
    • 0037459076 scopus 로고    scopus 로고
    • Membrane fusion
    • Jahn, R., Lang, T., and Sudhof, T. C. (2003) Membrane fusion. Cell 112, 519-533.
    • (2003) Cell , vol.112 , pp. 519-533
    • Jahn, R.1    Lang, T.2    Sudhof, T.C.3
  • 4
    • 85046913038 scopus 로고    scopus 로고
    • The state of the union: The cell biology of fertilization
    • Evans, J. P. and Florman, H. M. (2002) The state of the union: the cell biology of fertilization. Nat. Cell Biol. 4 (Suppl. 1), S57-S63.
    • (2002) Nat. Cell Biol , vol.4 , Issue.SUPPL. 1
    • Evans, J.P.1    Florman, H.M.2
  • 5
    • 0036629075 scopus 로고    scopus 로고
    • The molecular basis of sperm-oocyte membrane interactions during mammalian fertilization
    • Evans, J. P. (2002) The molecular basis of sperm-oocyte membrane interactions during mammalian fertilization. Hum. Reprod. Update 8, 297-311.
    • (2002) Hum. Reprod. Update , vol.8 , pp. 297-311
    • Evans, J.P.1
  • 6
    • 84884102082 scopus 로고    scopus 로고
    • Fertilization in mammals
    • Neill J.D, ed, Elsevier, San Diego, pp
    • Florman, H. M. and Ducibella, T. (2006) Fertilization in mammals, in The Physiology of Reproduction (Neill J.D., ed.), vol. 1. Elsevier, San Diego, pp. 55-112.
    • (2006) The Physiology of Reproduction , vol.1 , pp. 55-112
    • Florman, H.M.1    Ducibella, T.2
  • 7
    • 0345919870 scopus 로고    scopus 로고
    • Gamete fusion in mammals
    • Hardy, D. M, ed, Academic Press, San Diego, pp
    • Primakoff, P. and Myles, D. G. (2002) Gamete fusion in mammals, in Fertilization (Hardy, D. M., ed.). Academic Press, San Diego, pp. 303-318.
    • (2002) Fertilization , pp. 303-318
    • Primakoff, P.1    Myles, D.G.2
  • 8
    • 85069283405 scopus 로고    scopus 로고
    • Control of membrane fusion during spermiogenesis and the acrosome reaction
    • Ramalho-Santos, J., Schatten, G., and Moreno, R. D. (2002) Control of membrane fusion during spermiogenesis and the acrosome reaction. Biol. Reprod. 69, 254-260.
    • (2002) Biol. Reprod , vol.69 , pp. 254-260
    • Ramalho-Santos, J.1    Schatten, G.2    Moreno, R.D.3
  • 9
    • 13444282238 scopus 로고    scopus 로고
    • Sperm-egg fusion: Events at the plasma membrane
    • Stein, K. K., Primakoff, P., and Myles, D. (2004) Sperm-egg fusion: events at the plasma membrane. J. Cell Sci. 117, 6269-6274.
    • (2004) J. Cell Sci , vol.117 , pp. 6269-6274
    • Stein, K.K.1    Primakoff, P.2    Myles, D.3
  • 10
    • 0033593530 scopus 로고    scopus 로고
    • Mammalian fertilization: Molecular aspects of gamete adhesion, exocytosis, and fusion
    • Wassarman, P. M. (1999) Mammalian fertilization: molecular aspects of gamete adhesion, exocytosis, and fusion. Cell 96, 175-183.
    • (1999) Cell , vol.96 , pp. 175-183
    • Wassarman, P.M.1
  • 12
    • 0038290760 scopus 로고    scopus 로고
    • Protein-lipid interplay in fusion and fission of biological membranes
    • Chernomordik, L. V. and Kozlov, M. M. (2003) Protein-lipid interplay in fusion and fission of biological membranes. Annu. Rev. Biochem. 72, 175-207.
    • (2003) Annu. Rev. Biochem , vol.72 , pp. 175-207
    • Chernomordik, L.V.1    Kozlov, M.M.2
  • 14
    • 0036437326 scopus 로고    scopus 로고
    • Membrane fusion in eukaryotic cells
    • Mayer, A. (2002) Membrane fusion in eukaryotic cells. Annu. Rev. Cell Dev. Biol. 18, 289-314.
    • (2002) Annu. Rev. Cell Dev. Biol , vol.18 , pp. 289-314
    • Mayer, A.1
  • 15
    • 84884073858 scopus 로고    scopus 로고
    • The spermatozoon
    • Neill J. D, ed, Elsevier, San Diego, pp
    • Eddy, E. M. (2006) The spermatozoon, in The Physiology of Reproduction (Neill J. D., ed.), vol. 1. Elsevier, San Diego, pp. 3-54.
    • (2006) The Physiology of Reproduction , vol.1 , pp. 3-54
    • Eddy, E.M.1
  • 16
    • 0001953357 scopus 로고    scopus 로고
    • Function of the sperm acrosome
    • Hardy, D. M, ed, Academic Press, San Diego, pp
    • Gerton, G. L. (2002) Function of the sperm acrosome, in Fertilization (Hardy, D. M., ed.). Academic Press, San Diego, pp. 265-302.
    • (2002) Fertilization , pp. 265-302
    • Gerton, G.L.1
  • 17
    • 0002302562 scopus 로고
    • Mammalian fertilization
    • Knobil E. and Neill J. D, eds, Raven Press, New York, pp
    • Yanagimachi, R. (1994) Mammalian fertilization, in The Physiology of Reproduction (Knobil E. and Neill J. D., eds.), vol. 1. Raven Press, New York, pp. 189-317.
    • (1994) The Physiology of Reproduction , vol.1 , pp. 189-317
    • Yanagimachi, R.1
  • 18
    • 0002466714 scopus 로고
    • Cellular and molecular biology of the mammalian ovum
    • Knobil, E. Neill, J. D, eds, Raven Press, NY, pp
    • Wassarman, P. M. and Albertini, D. F. (1994) Cellular and molecular biology of the mammalian ovum, in The Physiology of Reproduction (Knobil, E. Neill, J. D., eds.), vol. 1. Raven Press, NY, pp. 79-122.
    • (1994) The Physiology of Reproduction , vol.1 , pp. 79-122
    • Wassarman, P.M.1    Albertini, D.F.2
  • 19
    • 0002192060 scopus 로고
    • Mechanisms of fertilization in mammals
    • Mastroianni L. and Biggers J. D, eds, Plenum Press, New York, pp
    • Yanagimachi, R. (1981) Mechanisms of fertilization in mammals, in Fertilization and Embryonic Development In Vitro (Mastroianni L. and Biggers J. D., eds.). Plenum Press, New York, pp. 81-187.
    • (1981) Fertilization and Embryonic Development In Vitro , pp. 81-187
    • Yanagimachi, R.1
  • 20
    • 0002402368 scopus 로고    scopus 로고
    • Capacitation
    • Hardy, D. M, ed, Academic Press, San Diego, pp
    • Jaiswal, B. S. and Eisenbach, M. (2002) Capacitation, in Fertilization (Hardy, D. M., ed.). Academic Press, San Diego, pp. 57-117.
    • (2002) Fertilization , pp. 57-117
    • Jaiswal, B.S.1    Eisenbach, M.2
  • 21
    • 0242624744 scopus 로고    scopus 로고
    • Differential release of soluble and matrix components: Evidence for intermediate states of secretion during spontaneous acrosomal exocytosis in mouse sperm
    • Kim, K.-S. and Gerton, G. L. (2003) Differential release of soluble and matrix components: evidence for intermediate states of secretion during spontaneous acrosomal exocytosis in mouse sperm. Dev. Biol. 264, 141-152.
    • (2003) Dev. Biol , vol.264 , pp. 141-152
    • Kim, K.-S.1    Gerton, G.L.2
  • 22
    • 0002824572 scopus 로고    scopus 로고
    • Signaling mechanisms controlling mammalian sperm fertilization competence and activation
    • Gagnon C, ed, Cache River Press, Vienna, IL
    • Kopf, G. S., Ning, X. P., Visconti, P. E., Purdon, M., Galantino-Homer, H., and Fornes, M. (1999) Signaling mechanisms controlling mammalian sperm fertilization competence and activation. In The Male Gamete (Gagnon C., ed.) 105-118. Cache River Press, Vienna, IL.
    • (1999) The Male Gamete , pp. 105-118
    • Kopf, G.S.1    Ning, X.P.2    Visconti, P.E.3    Purdon, M.4    Galantino-Homer, H.5    Fornes, M.6
  • 24
    • 0002820741 scopus 로고    scopus 로고
    • Signal transduction mechanisms regulating sperm acrosomal exocytosis
    • Hardy, D. M, ed, Academic Press, San Diego, pp
    • Kopf, G. S. (2002) Signal transduction mechanisms regulating sperm acrosomal exocytosis, in Fertilization (Hardy, D. M., ed.). Academic Press, San Diego, pp. 181-223.
    • (2002) Fertilization , pp. 181-223
    • Kopf, G.S.1
  • 26
    • 0029775791 scopus 로고    scopus 로고
    • ZP3-dependent activation of sperm cation channels regulates acrosomal secretion during mammalian fertilization
    • Arnoult, C., Zeng, Y., and Florman, H. M. (1996) ZP3-dependent activation of sperm cation channels regulates acrosomal secretion during mammalian fertilization. J. Cell Biol. 134, 637-645.
    • (1996) J. Cell Biol , vol.134 , pp. 637-645
    • Arnoult, C.1    Zeng, Y.2    Florman, H.M.3
  • 29
    • 26444433186 scopus 로고    scopus 로고
    • Dynamics of SNARE assembly and disassembly during sperm acrosomal exocytosis
    • De Blas, G. A., Roggero, C. M., Tomes, C. N., and Mayorga, L. S. (2005) Dynamics of SNARE assembly and disassembly during sperm acrosomal exocytosis. PloS Biol. 3, e323.
    • (2005) PloS Biol , vol.3
    • De Blas, G.A.1    Roggero, C.M.2    Tomes, C.N.3    Mayorga, L.S.4
  • 30
    • 0033168842 scopus 로고    scopus 로고
    • Identification of Rab3A GTPase as an acrosome-associated small GTP-binding protein in rat sperm
    • Iida, H., Yoshinaga, Y., Tanaka, S., Toshimori, K., and Mori, T. (1999) Identification of Rab3A GTPase as an acrosome-associated small GTP-binding protein in rat sperm. Dev. Biol. 211, 144-155.
    • (1999) Dev. Biol , vol.211 , pp. 144-155
    • Iida, H.1    Yoshinaga, Y.2    Tanaka, S.3    Toshimori, K.4    Mori, T.5
  • 34
    • 0034106739 scopus 로고    scopus 로고
    • Rab3A triggers the acrosome reaction in permeabilized human spermatozoa
    • Yunes, R., Michaut, M., Tomes, C., and Mayorga, L. S. (2000) Rab3A triggers the acrosome reaction in permeabilized human spermatozoa. Biol. Reprod. 62, 1084-1089.
    • (2000) Biol. Reprod , vol.62 , pp. 1084-1089
    • Yunes, R.1    Michaut, M.2    Tomes, C.3    Mayorga, L.S.4
  • 35
    • 0037367647 scopus 로고    scopus 로고
    • Secondary binding of mammalian sperm to the zona pellucida
    • Howes, E. A. and Jones, R. (2003) Secondary binding of mammalian sperm to the zona pellucida. ChemTracts Biochem. Mol. Biol. 16, 134-141.
    • (2003) ChemTracts Biochem. Mol. Biol , vol.16 , pp. 134-141
    • Howes, E.A.1    Jones, R.2
  • 36
    • 0037368591 scopus 로고    scopus 로고
    • Getting sperm and egg together: The molecules of gamete membrane interactions
    • Oh, E., Wortzman, G. B., Zhu, X., and Evans, J. P. (2003) Getting sperm and egg together: the molecules of gamete membrane interactions. ChemTracts Biochem. Mol. Biol. 16, 142-157.
    • (2003) ChemTracts Biochem. Mol. Biol , vol.16 , pp. 142-157
    • Oh, E.1    Wortzman, G.B.2    Zhu, X.3    Evans, J.P.4
  • 37
    • 0141533033 scopus 로고    scopus 로고
    • ADAMs: Modulators of cell-cell and cell-matrix interactions
    • White, J. M. (2003) ADAMs: modulators of cell-cell and cell-matrix interactions. Curr. Opin. Cell Biol. 15, 598-606.
    • (2003) Curr. Opin. Cell Biol , vol.15 , pp. 598-606
    • White, J.M.1
  • 39
    • 0034660644 scopus 로고    scopus 로고
    • -/- sperm: Evidence for C-terminal modification, α/β dimerization, and lack of essential role of fertilin b in sperm-egg fusion
    • -/- sperm: evidence for C-terminal modification, α/β dimerization, and lack of essential role of fertilin b in sperm-egg fusion. Dev. Biol. 222, 289-295.
    • (2000) Dev. Biol , vol.222 , pp. 289-295
    • Cho, C.1    Ge, H.2    Branciforte, D.3    Primakoff, P.4    Myles, D.G.5
  • 40
    • 0037442567 scopus 로고    scopus 로고
    • None of the integrins known to be present on the mouse egg or to be ADAM receptors are essential for sperm-egg binding and fusion
    • He, Z. Y., Brakefusch, C., Fassler, R., Kreidberg, J. A., Primakoff, P., and Myles, D. G. (2003) None of the integrins known to be present on the mouse egg or to be ADAM receptors are essential for sperm-egg binding and fusion. Dev. Biol. 254, 226-237.
    • (2003) Dev. Biol , vol.254 , pp. 226-237
    • He, Z.Y.1    Brakefusch, C.2    Fassler, R.3    Kreidberg, J.A.4    Primakoff, P.5    Myles, D.G.6
  • 41
    • 33646838999 scopus 로고    scopus 로고
    • Mouse sperm lacking ADAM1β/ADAM2 fertilin can fuse with the egg plasma membrane and effect fertilization
    • Kim, E., Yamashita, M., Nakanishi, T., Park, K.-E., Kimura, M., Kashiwabara, S.-I., and Baba, T. (2006) Mouse sperm lacking ADAM1β/ADAM2 fertilin can fuse with the egg plasma membrane and effect fertilization. J. Biol. Chem. 281, 5634-5639.
    • (2006) J. Biol. Chem , vol.281 , pp. 5634-5639
    • Kim, E.1    Yamashita, M.2    Nakanishi, T.3    Park, K.-E.4    Kimura, M.5    Kashiwabara, S.-I.6    Baba, T.7
  • 42
    • 0034640885 scopus 로고    scopus 로고
    • Normal fertilization occurs with eggs lacking the integrin α6β1 and is CD9-dependent
    • Miller, B. J., Georges-Labouesse, E., Primakoff, P., and Myles, D. G. (2000) Normal fertilization occurs with eggs lacking the integrin α6β1 and is CD9-dependent. J. Cell Biol. 149, 1289-1295.
    • (2000) J. Cell Biol , vol.149 , pp. 1289-1295
    • Miller, B.J.1    Georges-Labouesse, E.2    Primakoff, P.3    Myles, D.G.4
  • 43
    • 0035337709 scopus 로고    scopus 로고
    • Analysis of loss of adhesive function in sperm lacking cyritestin or fertilin β
    • Nishimura, H., Cho, C., Branciforte, D. R., Myles, D. G., and Primakoff, P. (2001) Analysis of loss of adhesive function in sperm lacking cyritestin or fertilin β. Dev. Biol. 233, 204-213.
    • (2001) Dev. Biol , vol.233 , pp. 204-213
    • Nishimura, H.1    Cho, C.2    Branciforte, D.R.3    Myles, D.G.4    Primakoff, P.5
  • 45
    • 33646863600 scopus 로고    scopus 로고
    • Proteomic analysis of sperm regions that mediate sperm-egg interactions
    • Stein, K. K., Go, J. C., Lane, W. S., Primakoff, P., and Myles, D. G. (2006) Proteomic analysis of sperm regions that mediate sperm-egg interactions. Proteomics 6, 3533-3543.
    • (2006) Proteomics , vol.6 , pp. 3533-3543
    • Stein, K.K.1    Go, J.C.2    Lane, W.S.3    Primakoff, P.4    Myles, D.G.5
  • 46
    • 0031720629 scopus 로고    scopus 로고
    • Integrin associated proteins
    • Hemler, M. E. (1998) Integrin associated proteins. Curr. Opin. Cell Biol. 10, 578-585.
    • (1998) Curr. Opin. Cell Biol , vol.10 , pp. 578-585
    • Hemler, M.E.1
  • 47
    • 0032189153 scopus 로고    scopus 로고
    • Integrins take partners: Cross-talk between integrins and other membrane receptors
    • Porter, J. C. and Hogg, N. (1998) Integrins take partners: cross-talk between integrins and other membrane receptors. Trends Cell Biol. 8, 390-396.
    • (1998) Trends Cell Biol , vol.8 , pp. 390-396
    • Porter, J.C.1    Hogg, N.2
  • 48
    • 0033598128 scopus 로고    scopus 로고
    • Role of transmembrane 4 superfamily (TM4SF) proteins CD9 and CD81 in muscle cell fusion and myotube maintenance
    • Tachibana, I. and Hemler, M. E. (1999) Role of transmembrane 4 superfamily (TM4SF) proteins CD9 and CD81 in muscle cell fusion and myotube maintenance. J. Cell Biol. 146, 893-904.
    • (1999) J. Cell Biol , vol.146 , pp. 893-904
    • Tachibana, I.1    Hemler, M.E.2
  • 54
    • 0344875471 scopus 로고    scopus 로고
    • Direct binding of the ligand PSG17 to CD9 requires a CD9 site essential for sperm-egg fusion
    • Ellerman, D. A., Ha, C., Primakoff, P., Myles, D. G., and Dveksler, G. S. (2003) Direct binding of the ligand PSG17 to CD9 requires a CD9 site essential for sperm-egg fusion. Mol. Biol. Cell 14, 5098-5103.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 5098-5103
    • Ellerman, D.A.1    Ha, C.2    Primakoff, P.3    Myles, D.G.4    Dveksler, G.S.5
  • 55
    • 0035163797 scopus 로고    scopus 로고
    • Sequence specific interaction between the disintegrin domain of mouse ADAM 3 and murine eggs: Role of beta1 integrin-associated proteins CD9, CD81, and CD98
    • Takahashi, Y., Bigler, D., Ito, Y., and White, J. M. (2001) Sequence specific interaction between the disintegrin domain of mouse ADAM 3 and murine eggs: role of beta1 integrin-associated proteins CD9, CD81, and CD98. Mol. Biol. Cell 12, 809-820.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 809-820
    • Takahashi, Y.1    Bigler, D.2    Ito, Y.3    White, J.M.4
  • 56
    • 15044362481 scopus 로고    scopus 로고
    • The immunoglobin superfamily protein Izumo is required for sperm to fuse with eggs
    • Inoue, N., Ikawa, M., Isotani, A., and Okabe, M. (2005) The immunoglobin superfamily protein Izumo is required for sperm to fuse with eggs. Nature 434, 234-238.
    • (2005) Nature , vol.434 , pp. 234-238
    • Inoue, N.1    Ikawa, M.2    Isotani, A.3    Okabe, M.4
  • 57
    • 0036785275 scopus 로고    scopus 로고
    • Expression and structure-function analysis of de, a sperm cysteine-rich secretory protein that mediates gamete fusion
    • Ellerman, D. A., Da Ros, V. G., Cohen, D. J., Busso, D., Morgenfeld, M. M., and Cuasnicu, P. S. (2002) Expression and structure-function analysis of de, a sperm cysteine-rich secretory protein that mediates gamete fusion. Biol. Reprod. 67, 1225-1231.
    • (2002) Biol. Reprod , vol.67 , pp. 1225-1231
    • Ellerman, D.A.1    Da Ros, V.G.2    Cohen, D.J.3    Busso, D.4    Morgenfeld, M.M.5    Cuasnicu, P.S.6
  • 58
    • 0038687068 scopus 로고    scopus 로고
    • Infertility in female mice with an oocyte-specific knockout of GPI-anchored proteins
    • Alfieri, J. A., Martin, A. D., Takeda, J., Kondoh, G., Myles, D. G., and Primakoff, P. (2003) Infertility in female mice with an oocyte-specific knockout of GPI-anchored proteins. J. Cell Sci. 116, 2149-2155.
    • (2003) J. Cell Sci , vol.116 , pp. 2149-2155
    • Alfieri, J.A.1    Martin, A.D.2    Takeda, J.3    Kondoh, G.4    Myles, D.G.5    Primakoff, P.6
  • 59
    • 0033559614 scopus 로고    scopus 로고
    • Treatment of mouse oocytes with PI-PLC releases 70-kDa (pI 5) and 35- to 45-kDa (pI 5.5) protein clusters from the egg surface and inhibits sperm-oolemma binding and fusion
    • Coonrod, S. A., Naaby-Hansen, S., Shetty, J., Shibahara, H., Chen, M., White, J. M., and Herr, J. C. (1999) Treatment of mouse oocytes with PI-PLC releases 70-kDa (pI 5) and 35- to 45-kDa (pI 5.5) protein clusters from the egg surface and inhibits sperm-oolemma binding and fusion. Dev. Biol. 207, 334-349.
    • (1999) Dev. Biol , vol.207 , pp. 334-349
    • Coonrod, S.A.1    Naaby-Hansen, S.2    Shetty, J.3    Shibahara, H.4    Chen, M.5    White, J.M.6    Herr, J.C.7
  • 62
    • 85069282891 scopus 로고    scopus 로고
    • Angiotensin-converting enzyme as a GPIase: A critical reevaluation
    • Leisle, L., Parkin, E. T., Turner, A. J., Hooper, N. M. (2005) Angiotensin-converting enzyme as a GPIase: a critical reevaluation. Nat. Med. 11, 1140-1142.
    • (2005) Nat. Med , vol.11 , pp. 1140-1142
    • Leisle, L.1    Parkin, E.T.2    Turner, A.J.3    Hooper, N.M.4
  • 63
    • 0037092883 scopus 로고    scopus 로고
    • Egg activation at fertilization: Where it all begins
    • Runft, L. L., Jaffe, L. A., and Mehlmann, L. M. (2002) Egg activation at fertilization: where it all begins. Dev. Biol. 245, 237-254.
    • (2002) Dev. Biol , vol.245 , pp. 237-254
    • Runft, L.L.1    Jaffe, L.A.2    Mehlmann, L.M.3
  • 64
    • 0347811195 scopus 로고    scopus 로고
    • Membrane events of egg activation
    • Hardy, D. M, ed, Academic Press, San Diego, pp
    • Swann, K. and Jones, K. T. (2002) Membrane events of egg activation, in Fertilization (Hardy, D. M., ed.). Academic Press, San Diego, pp. 319-346.
    • (2002) Fertilization , pp. 319-346
    • Swann, K.1    Jones, K.T.2
  • 65
    • 0029868296 scopus 로고    scopus 로고
    • The cortical reaction and development of activation competence in mammalian oocytes
    • Ducibella, T. (1996) The cortical reaction and development of activation competence in mammalian oocytes. Hum. Reprod. Update 2, 29-42.
    • (1996) Hum. Reprod. Update , vol.2 , pp. 29-42
    • Ducibella, T.1
  • 66
    • 16744368265 scopus 로고    scopus 로고
    • Calcium and the control of mammalian cortical granule exocytosis
    • Abbott, A. L. and Ducibella, T. (2001) Calcium and the control of mammalian cortical granule exocytosis. Front. Biosci. 6, d792-806.
    • (2001) Front. Biosci , vol.6
    • Abbott, A.L.1    Ducibella, T.2
  • 68
    • 14744303173 scopus 로고    scopus 로고
    • The involvement of protein kinase C and actin filaments in cortical granule exocytosis in the rat
    • Eliyahu, E., Tsaadon, A., Shtraizent, N., and Shalgi, R. (2005) The involvement of protein kinase C and actin filaments in cortical granule exocytosis in the rat. Reproduction 129, 161-170.
    • (2005) Reproduction , vol.129 , pp. 161-170
    • Eliyahu, E.1    Tsaadon, A.2    Shtraizent, N.3    Shalgi, R.4
  • 69
    • 0033578731 scopus 로고    scopus 로고
    • Characterization of the targeting, binding, and phosphorylation site domains of an A kinase anchor protein and a myristoylated alanine-rich C kinase substrate-like analog that are encoded by a single gene
    • Rossi, E. A., Li, Z., Feng, H., and Rubin, C. S. (1999) Characterization of the targeting, binding, and phosphorylation site domains of an A kinase anchor protein and a myristoylated alanine-rich C kinase substrate-like analog that are encoded by a single gene. J. Biol. Chem. 274, 27201-27210.
    • (1999) J. Biol. Chem , vol.274 , pp. 27201-27210
    • Rossi, E.A.1    Li, Z.2    Feng, H.3    Rubin, C.S.4
  • 70
    • 0033555056 scopus 로고    scopus 로고
    • Sperm disintegrins, egg integrins, and other cell adhesion molecules of mammalian gamete plasma membrane interactions
    • Evans, J. P. (1999) Sperm disintegrins, egg integrins, and other cell adhesion molecules of mammalian gamete plasma membrane interactions. Front. Biosci. 4, D114-D131.
    • (1999) Front. Biosci , vol.4
    • Evans, J.P.1
  • 71
    • 0030922886 scopus 로고    scopus 로고
    • Spontaneous activation of ovulated mouse eggs: Time-dependent effects on M-phase exit, cortical granule exocytosis, maternal messenger ribonucleic acid recruitment, and inositol 1,4,5-triphosphate sensitivity
    • Xu, Z., Abbott, A., Kopf, G. S., Schultz, R. M., and Ducibella, T. (1997) Spontaneous activation of ovulated mouse eggs: time-dependent effects on M-phase exit, cortical granule exocytosis, maternal messenger ribonucleic acid recruitment, and inositol 1,4,5-triphosphate sensitivity. Biol. Reprod. 57, 743-750.
    • (1997) Biol. Reprod , vol.57 , pp. 743-750
    • Xu, Z.1    Abbott, A.2    Kopf, G.S.3    Schultz, R.M.4    Ducibella, T.5
  • 72
    • 85069278770 scopus 로고    scopus 로고
    • Austin C. R. and Short R. V. (eds.) (1983) Reproduction in Mammals, Book 1, Germ Cells and Fertilization. Cambridge University Press, Cambridge, England.
    • Austin C. R. and Short R. V. (eds.) (1983) Reproduction in Mammals, Book 1, Germ Cells and Fertilization. Cambridge University Press, Cambridge, England.
  • 75
    • 0006086121 scopus 로고
    • Wassarman P. M, ed, vols, and 2. CRC Press, Boca Raton, FL
    • Wassarman P. M. (ed.) (1991) Elements of Mammalian Fertilization, vols. 1 and 2. CRC Press, Boca Raton, FL.
    • (1991) Elements of Mammalian Fertilization , vol.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.