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Volumn 25, Issue 2, 1999, Pages 83-86

Fertilization in animals

Author keywords

Acrosomal proteases; Acrosome reaction; Ca2+ channels; Capacitation; Chemotaxis; Fertilization; Nuclear transformation; Sperm activation; Vilelline envelope; Zona pellucida

Indexed keywords

ACROSIN; CALCIUM CHANNEL; SPERM ACTIVATING PEPTIDE;

EID: 0032858642     PISSN: 0192253X     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1520-6408(1999)25:2<83::AID-DVG1>3.0.CO;2-J     Document Type: Review
Times cited : (30)

References (39)
  • 3
    • 0027948083 scopus 로고
    • Sperm from mice carrying a targeted mutation of the acrosin gene can penetrate the oocyte zona pellucida and effect fertilization
    • Baba T, Azuma S, Kashiwabra S-I, Toyoda, Y. 1994. Sperm from mice carrying a targeted mutation of the acrosin gene can penetrate the oocyte zona pellucida and effect fertilization. J Biol Chem 269:31845-31849.
    • (1994) J Biol Chem , vol.269 , pp. 31845-31849
    • Baba, T.1    Azuma, S.2    Kashiwabra, S.-I.3    Toyoda, Y.4
  • 4
    • 0022446203 scopus 로고
    • Transformation of sperm nuclei to metaphase chromosomes in the cytoplasm of maturing oocytes of the mouse
    • Clarke HJ, Masui Y. 1986. Transformation of sperm nuclei to metaphase chromosomes in the cytoplasm of maturing oocytes of the mouse. J Cell Biol 102:1039-1046.
    • (1986) J Cell Biol , vol.102 , pp. 1039-1046
    • Clarke, H.J.1    Masui, Y.2
  • 5
    • 0029686055 scopus 로고    scopus 로고
    • Ion channels: Key elements in gamete signaling
    • Darszon A, Liévano A, Beltran C. 1996. Ion channels: key elements in gamete signaling. Curr Top Dev Biol 34:117-167.
    • (1996) Curr Top Dev Biol , vol.34 , pp. 117-167
    • Darszon, A.1    Liévano, A.2    Beltran, C.3
  • 6
    • 0016883432 scopus 로고
    • Miotic chromosome condensation in the sperm nucleus during post-fertilization maturation division in Urechis eggs
    • Das NK, Baker C. 1976. Miotic chromosome condensation in the sperm nucleus during post-fertilization maturation division in Urechis eggs. J Cell Biol 68:155-159.
    • (1976) J Cell Biol , vol.68 , pp. 155-159
    • Das, N.K.1    Baker, C.2
  • 7
    • 0002494818 scopus 로고
    • The spermatozoon
    • Knobil E, Neill JD, editors New York: Raven Press
    • Eddy EM, O'Brien DA. 1994. The spermatozoon. In: Knobil E, Neill JD, editors. The physiology of reproduction. New York: Raven Press. p 29-78.
    • (1994) The Physiology of Reproduction , pp. 29-78
    • Eddy, E.M.1    O'Brien, D.A.2
  • 8
    • 0033060654 scopus 로고    scopus 로고
    • Sperm chemotaxis
    • Eisenbach M. 1999a. Sperm chemotaxis. Rev Reprod 4:56-66.
    • (1999) Rev Reprod , vol.4 , pp. 56-66
    • Eisenbach, M.1
  • 9
    • 0032817345 scopus 로고    scopus 로고
    • Mammalian sperm chemotaxis and its association with capacitation
    • Eisenbach M. 1999b. Mammalian sperm chemotaxis and its association with capacitation. Dev Genet 25:87-94.
    • (1999) Dev Genet , vol.25 , pp. 87-94
    • Eisenbach, M.1
  • 11
    • 0001072026 scopus 로고    scopus 로고
    • An intimate biochemistry: Egg-regulated acrosome reactions of mammalian sperm
    • Florman HM, Arnoult C, Kazam IC, Li C, OToole CMB. 1999. An intimate biochemistry: egg-regulated acrosome reactions of mammalian sperm. Adv Dev Biochem 5:199-234.
    • (1999) Adv Dev Biochem , vol.5 , pp. 199-234
    • Florman, H.M.1    Arnoult, C.2    Kazam, I.C.3    Li, C.4    OToole, C.M.B.5
  • 12
    • 0024309828 scopus 로고
    • Molecular basis of fertilization
    • Garbers DL. 1989. Molecular basis of fertilization. Annu Rev Biochem 58:719-742.
    • (1989) Annu Rev Biochem , vol.58 , pp. 719-742
    • Garbers, D.L.1
  • 13
    • 0030779895 scopus 로고    scopus 로고
    • Three-dimensional structure of the zona pellucida
    • Green DPL. 1997. Three-dimensional structure of the zona pellucida. Rev Reprod 2:147-156.
    • (1997) Rev Reprod , vol.2 , pp. 147-156
    • Green, D.P.L.1
  • 14
    • 0026683132 scopus 로고
    • Oviductin. Purification and properties of the oviductal protease that processes the molecular weight 43,000 glycoprotein of Xenopus laevis egg envelope
    • Hardy DM, Hedrick JL. 1992. Oviductin. Purification and properties of the oviductal protease that processes the molecular weight 43,000 glycoprotein of Xenopus laevis egg envelope. Biochemistry 31:4466-4472.
    • (1992) Biochemistry , vol.31 , pp. 4466-4472
    • Hardy, D.M.1    Hedrick, J.L.2
  • 15
    • 0032872970 scopus 로고    scopus 로고
    • Studies on fertilization in the teleost. III. The relationship between nuclear behavior and the histone H1 kinase activity in anesthitized medaka eggs
    • Iwamatsu T, Shibata Y, Kikuyama M, Yamashita M. 1999. Studies on fertilization in the teleost. III. The relationship between nuclear behavior and the histone H1 kinase activity in anesthitized medaka eggs. Dev Genet 25:137-145.
    • (1999) Dev Genet , vol.25 , pp. 137-145
    • Iwamatsu, T.1    Shibata, Y.2    Kikuyama, M.3    Yamashita, M.4
  • 16
    • 0002479532 scopus 로고
    • Role of oviductal secretions in mediating gamete fusion in anuran amphibians
    • Katagiri C. 1987. Role of oviductal secretions in mediating gamete fusion in anuran amphibians. Zool Sci 4:1-14.
    • (1987) Zool Sci , vol.4 , pp. 1-14
    • Katagiri, C.1
  • 17
    • 0028122642 scopus 로고
    • Expression of a putative precursor mRNA for sperm-activating peptide I in accessory cells of the ovary in sea urchin Hemicentrotus pulcherrimus
    • Kinoh H, Shimizu T, Fujimoto H, Suzuki N. 1994. Expression of a putative precursor mRNA for sperm-activating peptide I in accessory cells of the ovary in sea urchin Hemicentrotus pulcherrimus. Rouxs Arch Dev Biol 203:381-388.
    • (1994) Rouxs Arch Dev Biol , vol.203 , pp. 381-388
    • Kinoh, H.1    Shimizu, T.2    Fujimoto, H.3    Suzuki, N.4
  • 19
    • 0030766728 scopus 로고    scopus 로고
    • A major glycoprotein of Xenopus egg vitelline envelope, gp41, is a frog homolog of mammalian ZP3
    • Kubo H, Kawano T, Tsubuki S, Kawashima S, Katagiri C, Suzuki A. 1997. A major glycoprotein of Xenopus egg vitelline envelope, gp41, is a frog homolog of mammalian ZP3. Dev Growth Diff 39:405-417.
    • (1997) Dev Growth Diff , vol.39 , pp. 405-417
    • Kubo, H.1    Kawano, T.2    Tsubuki, S.3    Kawashima, S.4    Katagiri, C.5    Suzuki, A.6
  • 20
    • 0032818491 scopus 로고    scopus 로고
    • Molecular basis for oviductin-mediated processing from gp43 to gp41, the predominant glycoproteins of Xenopus egg envelopes
    • Kubo H, Matsushita M, Kotani M, Kawasaki H, Saido TC, Kawahima S, Katagiri C, Suzuki A. 1999. Molecular basis for oviductin-mediated processing from gp43 to gp41, the predominant glycoproteins of Xenopus egg envelopes. Dev Genet 25:123-129.
    • (1999) Dev Genet , vol.25 , pp. 123-129
    • Kubo, H.1    Matsushita, M.2    Kotani, M.3    Kawasaki, H.4    Saido, T.C.5    Kawahima, S.6    Katagiri, C.7    Suzuki, A.8
  • 22
  • 23
    • 0032838931 scopus 로고    scopus 로고
    • Sequence analysis of cDNAs encoding precursors of starfish asterosaps
    • Matsumoto M, Briones AV, Nishigaki T, Hoshi M. 1999. Sequence analysis of cDNAs encoding precursors of starfish asterosaps. Dev Genet 25:130-136.
    • (1999) Dev Genet , vol.25 , pp. 130-136
    • Matsumoto, M.1    Briones, A.V.2    Nishigaki, T.3    Hoshi, M.4
  • 25
    • 0030202724 scopus 로고    scopus 로고
    • Structure and function of asterosaps, sperm-activating peptides from the jelly coat of starfish eggs
    • Nishigachi T, Chiba K, Miki W, Hoshi M. 1996. Structure and function of asterosaps, sperm-activating peptides from the jelly coat of starfish eggs. Zygote 4:237-245.
    • (1996) Zygote , vol.4 , pp. 237-245
    • Nishigachi, T.1    Chiba, K.2    Miki, W.3    Hoshi, M.4
  • 28
    • 0025355836 scopus 로고
    • A single mRNA encodes multiple copies of the egg peptide speract
    • Romarao CS, Burks DJ, Garbers DL. 1990. A single mRNA encodes multiple copies of the egg peptide speract. Biochemistry 29:3383-3388.
    • (1990) Biochemistry , vol.29 , pp. 3383-3388
    • Romarao, C.S.1    Burks, D.J.2    Garbers, D.L.3
  • 31
    • 0030933883 scopus 로고    scopus 로고
    • Gamete interaction in Xenopus laevis: Identification of sperm binding glycoproteins in the egg vitelline envelope
    • Tian J, Gong H, Thomsen GH, Lennarz WJ. 1997. Gamete interaction in Xenopus laevis: identification of sperm binding glycoproteins in the egg vitelline envelope. J Cell Biol 136:1099-1108.
    • (1997) J Cell Biol , vol.136 , pp. 1099-1108
    • Tian, J.1    Gong, H.2    Thomsen, G.H.3    Lennarz, W.J.4
  • 32
    • 0033514313 scopus 로고    scopus 로고
    • Xenopus laevis sperm receptor gp69/64 glycoprotein is a homolog of mammalian sperm receptor ZP2
    • Tian J, Gong H, Lennarz WJ. 1999. Xenopus laevis sperm receptor gp69/64 glycoprotein is a homolog of mammalian sperm receptor ZP2. Proc Natl Acad Sci USA 96:829-834.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 829-834
    • Tian, J.1    Gong, H.2    Lennarz, W.J.3
  • 33
    • 0027297159 scopus 로고
    • Molecular events mediating sperm activation
    • Ward CR, Kopf GS. 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
  • 35
    • 0033593530 scopus 로고    scopus 로고
    • Mammalian fertilization: Molecular aspects of gamete adhesion, exocytosis, and fusion
    • Wassarman PM. 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
  • 37
    • 0032875968 scopus 로고    scopus 로고
    • Discrimination of acrosomal serine protease systems in mouse and other rodent sperm
    • Yamagata K, Honda A, Kashiwabara S-I, Baba T. 1999. Discrimination of acrosomal serine protease systems in mouse and other rodent sperm. Dev Genet 25:115-122.
    • (1999) Dev Genet , vol.25 , pp. 115-122
    • Yamagata, K.1    Honda, A.2    Kashiwabara, S.-I.3    Baba, T.4
  • 38
    • 0002302562 scopus 로고
    • Mammalian fertilization
    • Knobil E, Neill J, editors: New York: Raven Press
    • Yanagimachi R. 1994. Mammalian fertilization. In: Knobil E, Neill J, editors: The physiology of reproduction. New York: Raven Press. p 189-317.
    • (1994) The Physiology of Reproduction , pp. 189-317
    • Yanagimachi, R.1
  • 39
    • 0030814963 scopus 로고    scopus 로고
    • cDNA cloning a sequence analysis of the Xenopus laevis egg envelope glycoprotein gp43
    • Yang JC, Hedrick JL. 1997. cDNA cloning a sequence analysis of the Xenopus laevis egg envelope glycoprotein gp43. Dev Growth Diff 39:457-467.
    • (1997) Dev Growth Diff , vol.39 , pp. 457-467
    • Yang, J.C.1    Hedrick, J.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.