메뉴 건너뛰기




Volumn 24, Issue 3, 2000, Pages 279-282

The gamete fusion process is defective in eggs of Cd9-deficient mice

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; CELL SURFACE PROTEIN;

EID: 0034091646     PISSN: 10614036     EISSN: None     Source Type: Journal    
DOI: 10.1038/73502     Document Type: Article
Times cited : (410)

References (29)
  • 1
    • 43949157634 scopus 로고
    • The ins and outs of the transmembrane 4 superfamily
    • Wright, M.D. & Tomlinson, M.G. The ins and outs of the transmembrane 4 superfamily. Immunol. Today 15, 588-594 (1994).
    • (1994) Immunol. Today , vol.15 , pp. 588-594
    • Wright, M.D.1    Tomlinson, M.G.2
  • 3
    • 0028999004 scopus 로고
    • Membrane-anchored heparin-binding EGF-like growth factor (HB-EGF) and diphtheria toxin receptor-associated protein (DRAP27)/CD9 form a complex with integrin α3β1 at cell-cell contact sites
    • Nakamura, K., Iwamoto, R. & Mekada, E. Membrane-anchored heparin-binding EGF-like growth factor (HB-EGF) and diphtheria toxin receptor-associated protein (DRAP27)/CD9 form a complex with integrin α3β1 at cell-cell contact sites. J. Cell Biol. 129, 1691-1705 (1995).
    • (1995) J. Cell Biol. , vol.129 , pp. 1691-1705
    • Nakamura, K.1    Iwamoto, R.2    Mekada, E.3
  • 4
    • 0031058589 scopus 로고    scopus 로고
    • The platelet antigens CD9, CD42 and integrin α IIb β IIIa can be topographically associated and transduce functionally similar signals
    • Slupsky, J.R. et al. The platelet antigens CD9, CD42 and integrin α IIb β IIIa can be topographically associated and transduce functionally similar signals. Eur. J. Biochem. 244, 168-175 (1997).
    • (1997) Eur. J. Biochem. , vol.244 , pp. 168-175
    • Slupsky, J.R.1
  • 5
    • 0032514919 scopus 로고    scopus 로고
    • CD19 is linked to the integrin-associated tetraspans CD9, CD81, and CD82
    • Horvath, G. et al. CD19 is linked to the integrin-associated tetraspans CD9, CD81, and CD82. J. Biol. Chem. 273, 30537-30543 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 30537-30543
    • Horvath, G.1
  • 6
    • 0027406455 scopus 로고
    • Suppression of cell motility and metastasis by transfection with human motility-related protein (MRP-1/CD9) DNA
    • Ikeyama, S., Koyama, M., Yamaoko, M., Sasada, R. & Miyake, M. Suppression of cell motility and metastasis by transfection with human motility-related protein (MRP-1/CD9) DNA. J. Exp. Med. 177, 1231-1237 (1993).
    • (1993) J. Exp. Med. , vol.177 , pp. 1231-1237
    • Ikeyama, S.1    Koyama, M.2    Yamaoko, M.3    Sasada, R.4    Miyake, M.5
  • 7
  • 8
    • 0028869959 scopus 로고
    • An anti-CD9 monoclonal antibody promotes adhesion and induces proliferation of Schwann cells in vitro
    • Hadjiargyrou, M. & Patterson, P.H. An anti-CD9 monoclonal antibody promotes adhesion and induces proliferation of Schwann cells in vitro. J. Neurosci. 15, 574-583 (1995).
    • (1995) J. Neurosci. , vol.15 , pp. 574-583
    • Hadjiargyrou, M.1    Patterson, P.H.2
  • 9
    • 0033598128 scopus 로고    scopus 로고
    • Role of transmembrane 4 superfamily (TM4SF) proteins CD9 and CD81 in muscle cell fusion and myotube maintenance
    • Tachibana, I. & Hemler, M.E. Role of transmembrane 4 superfamily (TM4SF) proteins CD9 and CD81 in muscle cell fusion and myotube maintenance. J. Cell Biol. 146, 893-904 (1999).
    • (1999) J. Cell Biol. , vol.146 , pp. 893-904
    • Tachibana, I.1    Hemler, M.E.2
  • 10
    • 0031060150 scopus 로고    scopus 로고
    • CD9, a tetraspan transmembrane protein, renders cells susceptible to canine distemper virus
    • Loffler, S. et al. CD9, a tetraspan transmembrane protein, renders cells susceptible to canine distemper virus. J. Virol. 71, 42-49 (1997).
    • (1997) J. Virol. , vol.71 , pp. 42-49
    • Loffler, S.1
  • 11
    • 0031051160 scopus 로고    scopus 로고
    • Inhibition of feline immunodeficiency virus infection by CD9 antibody operates after virus entry and is independent of virus tropism
    • Willett, B., Hosie, M., Shaw, A. & Neil, J. Inhibition of feline immunodeficiency virus infection by CD9 antibody operates after virus entry and is independent of virus tropism. J. Gen. Virol. 78, 611-618 (1997).
    • (1997) J. Gen. Virol. , vol.78 , pp. 611-618
    • Willett, B.1    Hosie, M.2    Shaw, A.3    Neil, J.4
  • 12
    • 0002302562 scopus 로고
    • Mammalian fertilization
    • (eds Knobil, E. & Neill, J.D.) Raven, New York
    • Yanagimachi, R. Mammalian fertilization. in The Physiology of Reproduction (eds Knobil, E. & Neill, J.D.) 189-317 (Raven, New York, 1994).
    • (1994) The Physiology of Reproduction , pp. 189-317
    • Yanagimachi, R.1
  • 13
    • 13044252869 scopus 로고    scopus 로고
    • Role of the integrin-associated protein CD9 in binding between sperm ADAM 2 and the egg integrin α6β1
    • Chen, M.S. et al. Role of the integrin-associated protein CD9 in binding between sperm ADAM 2 and the egg integrin α6β1. Proc. Natl Acad. Sci. USA 96, 11830-11835 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 11830-11835
    • Chen, M.S.1
  • 15
    • 0026551829 scopus 로고
    • Repetitive calcium transients and the role of calcium in exocytosis and cell cycle activation in the mouse egg
    • Kline, D. & Kline, J.T. Repetitive calcium transients and the role of calcium in exocytosis and cell cycle activation in the mouse egg. Dev. Biol. 149, 80-89 (1992).
    • (1992) Dev. Biol. , vol.149 , pp. 80-89
    • Kline, D.1    Kline, J.T.2
  • 17
    • 0031150016 scopus 로고    scopus 로고
    • 2+ oscillations at fertilization in mammals
    • 2+ oscillations at fertilization in mammals. Bioessay 19, 371-378 (1997).
    • (1997) Bioessay , vol.19 , pp. 371-378
    • Swann, K.1    Lai, F.A.2
  • 18
    • 0022381039 scopus 로고
    • Fine structure of the mammalian egg cortex
    • Long, F.J. Fine structure of the mammalian egg cortex. Am. J. Anat. 174, 303-315 (1985).
    • (1985) Am. J. Anat. , vol.174 , pp. 303-315
    • Long, F.J.1
  • 19
    • 0022352429 scopus 로고
    • Mammalian fertilization as seen with the scanning electron microscope
    • Phillips, D.M., Shalgi, R. & Dekel, N. Mammalian fertilization as seen with the scanning electron microscope. Am. J. Anat. 174, 357-372 (1985).
    • (1985) Am. J. Anat. , vol.174 , pp. 357-372
    • Phillips, D.M.1    Shalgi, R.2    Dekel, N.3
  • 20
    • 0018252047 scopus 로고
    • The visualization of actin filament polarity in thin sections
    • Begg, D.A., Rodewald, R. & Rebhun, L.I. The visualization of actin filament polarity in thin sections. J. Cell Biol. 79, 846-852 (1978).
    • (1978) J. Cell Biol. , vol.79 , pp. 846-852
    • Begg, D.A.1    Rodewald, R.2    Rebhun, L.I.3
  • 21
    • 0032544623 scopus 로고    scopus 로고
    • Fertilization defects in sperm from mice lacking fertilin β
    • Cho, C. et al. Fertilization defects in sperm from mice lacking fertilin β. Science 281, 1857-1859 (1998).
    • (1998) Science , vol.281 , pp. 1857-1859
    • Cho, C.1
  • 22
    • 0029047919 scopus 로고
    • Mouse egg integrin α6β1 functions as a sperm receptor
    • Almeida, E.A.C. et al. Mouse egg integrin α6β1 functions as a sperm receptor. Cell 81, 1095-1104 (1995).
    • (1995) Cell , vol.81 , pp. 1095-1104
    • Almeida, E.A.C.1
  • 23
    • 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. & Helmer, M.E. 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).
    • (1996) Mol. Biol. Cell , vol.7 , pp. 193-207
    • Berditchevski, F.1    Zutter, M.M.2    Helmer, M.E.3
  • 24
    • 0020029183 scopus 로고
    • Ultrastructural observations on binding and membrane fusion between human sperm and zona pellucida-free hamster oocytes
    • Talbot, P. & Chacon, R.S. Ultrastructural observations on binding and membrane fusion between human sperm and zona pellucida-free hamster oocytes. Fertil. Steril. 37, 240-248 (1982).
    • (1982) Fertil. Steril. , vol.37 , pp. 240-248
    • Talbot, P.1    Chacon, R.S.2
  • 25
    • 0023646810 scopus 로고
    • Site-directed mutagenesis by gene targeting in mouse embryo-derived stem cells
    • Thomas, K.R. & Capecchi, M.R. Site-directed mutagenesis by gene targeting in mouse embryo-derived stem cells. Cell 51, 503-512 (1987).
    • (1987) Cell , vol.51 , pp. 503-512
    • Thomas, K.R.1    Capecchi, M.R.2
  • 26
    • 0025672645 scopus 로고
    • Homologous recombination at c-fyn locus of mouse embryonic stem cells with use of diphtheria toxin A-fragment gene in negative selection
    • Yagi, T. et al. Homologous recombination at c-fyn locus of mouse embryonic stem cells with use of diphtheria toxin A-fragment gene in negative selection. Proc. Natl Acad. Sci. USA 87, 9918-9922 (1990).
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 9918-9922
    • Yagi, T.1
  • 27
    • 0031309795 scopus 로고    scopus 로고
    • Spatiotemporal dynamics of intracellular calcium in the mouse egg injected with a spermatozoon
    • Nakano, Y., Shirakawa, H., Mitsuhashi, N., Kuwabara, Y. & Miyazaki, S. Spatiotemporal dynamics of intracellular calcium in the mouse egg injected with a spermatozoon. Mol. Hum. Reprod. 3, 1087-1093 (1997).
    • (1997) Mol. Hum. Reprod. , vol.3 , pp. 1087-1093
    • Nakano, Y.1    Shirakawa, H.2    Mitsuhashi, N.3    Kuwabara, Y.4    Miyazaki, S.5
  • 28
    • 0018084733 scopus 로고
    • Activation of mammalian oocytes by intracellular injection of calcium
    • Fulton, B.P. & Whittingham, D.G. Activation of mammalian oocytes by intracellular injection of calcium. Nature 273, 149-151 (1978).
    • (1978) Nature , vol.273 , pp. 149-151
    • Fulton, B.P.1    Whittingham, D.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.