메뉴 건너뛰기




Volumn 236, Issue 8, 2007, Pages 2027-2038

Flipping the switch: How a sperm activates the egg at fertilization

Author keywords

Calcium, egg; Fertilization; Sperm

Indexed keywords

CALCIUM ION; CYCLIC ADENOSINE DIPHOSPHATE RIBOSE; GUANINE NUCLEOTIDE BINDING PROTEIN; NICOTINIC ACID ADENINE DINUCLEOTIDE PHOSPHATE; NITRIC OXIDE; PHOSPHOLIPASE C; PHOSPHOLIPASE C GAMMA;

EID: 34548059203     PISSN: 10588388     EISSN: 10970177     Source Type: Journal    
DOI: 10.1002/dvdy.21255     Document Type: Review
Times cited : (89)

References (155)
  • 1
    • 16744368265 scopus 로고    scopus 로고
    • Calcium and the control of mammalian cortical granule exocytosis
    • Abbott AL, 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
  • 2
    • 0029015942 scopus 로고
    • Regulation of mouse egg activation: Presence of ryanodine receptors and effects of microinjected ryanodine and cyclic ADP ribose on uninseminated and inseminated eggs
    • Ayabe T, Kopf GS, Schultz RM. 1995. Regulation of mouse egg activation: presence of ryanodine receptors and effects of microinjected ryanodine and cyclic ADP ribose on uninseminated and inseminated eggs. Development 121:2233-2244.
    • (1995) Development , vol.121 , pp. 2233-2244
    • Ayabe, T.1    Kopf, G.S.2    Schultz, R.M.3
  • 3
    • 0036795474 scopus 로고    scopus 로고
    • Nicotinic acid adenine dinucleotide phosphate (NAADP) is present at micromolar concentrations in sea urchin spermatozoa
    • Billington RA, Ho A, Genazzani AA. 2002. Nicotinic acid adenine dinucleotide phosphate (NAADP) is present at micromolar concentrations in sea urchin spermatozoa. J Physiol 544:107-112.
    • (2002) J Physiol , vol.544 , pp. 107-112
    • Billington, R.A.1    Ho, A.2    Genazzani, A.A.3
  • 4
    • 17844372569 scopus 로고    scopus 로고
    • G protein betagamma directly regulates SNARE protein fusion machinery for secretory granule exocytosis
    • Blackmer T, Larsen EC, Takahashi M, Martin TF, Alford S, Hamm HE. 2005. G protein betagamma directly regulates SNARE protein fusion machinery for secretory granule exocytosis. Nat Neurosci 8:421-425.
    • (2005) Nat Neurosci , vol.8 , pp. 421-425
    • Blackmer, T.1    Larsen, E.C.2    Takahashi, M.3    Martin, T.F.4    Alford, S.5    Hamm, H.E.6
  • 6
    • 0026676806 scopus 로고
    • Isozyme-selective stimulation of phospholipase C-beta 2 by G protein beta gamma-subunits
    • Camps M, Carozzi A, Schnabel P, Scheer A, Parker PJ, Gierschik P. 1992. Isozyme-selective stimulation of phospholipase C-beta 2 by G protein beta gamma-subunits. Nature 360:684-686.
    • (1992) Nature , vol.360 , pp. 684-686
    • Camps, M.1    Carozzi, A.2    Schnabel, P.3    Scheer, A.4    Parker, P.J.5    Gierschik, P.6
  • 8
    • 0033556702 scopus 로고    scopus 로고
    • Identification of PL-Cgamma-dependent and -independent events during fertilization of sea urchin eggs
    • Carroll DJ, Albay DT, Terasaki M, Jaffe LA, Foltz KR. 1999. Identification of PL-Cgamma-dependent and -independent events during fertilization of sea urchin eggs. Dev Biol 206:232-247.
    • (1999) Dev Biol , vol.206 , pp. 232-247
    • Carroll, D.J.1    Albay, D.T.2    Terasaki, M.3    Jaffe, L.A.4    Foltz, K.R.5
  • 11
    • 0033826182 scopus 로고    scopus 로고
    • Egg activation: Upstream of the fertilization calcium signal
    • Ciapa B, Chiri S. 2000. Egg activation: upstream of the fertilization calcium signal. Biol Cell 92:215-233.
    • (2000) Biol Cell , vol.92 , pp. 215-233
    • Ciapa, B.1    Chiri, S.2
  • 12
    • 0026316821 scopus 로고
    • A rapid change in phosphorylation on tyrosine accompanies fertilization of sea urchin eggs
    • Ciapa B, Epel D. 1991. A rapid change in phosphorylation on tyrosine accompanies fertilization of sea urchin eggs. FEBS Lett 295:167-170.
    • (1991) FEBS Lett , vol.295 , pp. 167-170
    • Ciapa, B.1    Epel, D.2
  • 13
    • 0022490785 scopus 로고
    • Two phases of inositol polyphosphate and diacylglycerol production at fertilisation
    • Ciapa B, Whitaker M. 1986. Two phases of inositol polyphosphate and diacylglycerol production at fertilisation. Febs Lett 195:347-351.
    • (1986) Febs Lett , vol.195 , pp. 347-351
    • Ciapa, B.1    Whitaker, M.2
  • 14
    • 0023219685 scopus 로고
    • Pyridine nucleotide metabolites stimulate calcium release from sea urchin egg microsomes desensitized to inositol trisphosphate
    • Clapper DL, Walseth TF, Dargie PJ, Lee HC. 1987. Pyridine nucleotide metabolites stimulate calcium release from sea urchin egg microsomes desensitized to inositol trisphosphate. J Biol Chem 262:9561-9568.
    • (1987) J Biol Chem , vol.262 , pp. 9561-9568
    • Clapper, D.L.1    Walseth, T.F.2    Dargie, P.J.3    Lee, H.C.4
  • 15
    • 0038706027 scopus 로고    scopus 로고
    • Teleost fish spermatozoa contain a cytosolic protein factor that induces calcium release in sea urchin egg homogenates and triggers calcium oscillations when injected into mouse oocytes
    • Coward K, Campos-Mendoza A, Larman M, Hibbitt O, McAndrew B, Bromage N, Parrington J. 2003. Teleost fish spermatozoa contain a cytosolic protein factor that induces calcium release in sea urchin egg homogenates and triggers calcium oscillations when injected into mouse oocytes. Biochem Biophys Res Commun 305:299-304.
    • (2003) Biochem Biophys Res Commun , vol.305 , pp. 299-304
    • Coward, K.1    Campos-Mendoza, A.2    Larman, M.3    Hibbitt, O.4    McAndrew, B.5    Bromage, N.6    Parrington, J.7
  • 17
    • 0034747998 scopus 로고    scopus 로고
    • Nitric oxide synthase sequences in the marine fish Stenotomus chrysops and the sea urchin Arbacia punctulata, and phylogenetic analysis of nitric oxide synthase calmodulin-binding domains
    • Cox RL, Mariano T, Heck DE, Laskin JD, Stegeman JJ. 2001. Nitric oxide synthase sequences in the marine fish Stenotomus chrysops and the sea urchin Arbacia punctulata, and phylogenetic analysis of nitric oxide synthase calmodulin-binding domains. Comp Biochem Physiol B Biochem Mol Biol 130:479-491.
    • (2001) Comp Biochem Physiol B Biochem Mol Biol , vol.130 , pp. 479-491
    • Cox, R.L.1    Mariano, T.2    Heck, D.E.3    Laskin, J.D.4    Stegeman, J.J.5
  • 18
    • 0023741431 scopus 로고
    • Initiation of the cortical reaction in hamster and sheep oocytes in response to inositol trisphosphate
    • Cran DG, Moor RM, Irvine RF. 1988. Initiation of the cortical reaction in hamster and sheep oocytes in response to inositol trisphosphate. J Cell Sci 91:139-144.
    • (1988) J Cell Sci , vol.91 , pp. 139-144
    • Cran, D.G.1    Moor, R.M.2    Irvine, R.F.3
  • 19
    • 0035164184 scopus 로고    scopus 로고
    • Chemiluminescence microscopy as a tool in biomedical research
    • Creton R, Jaffe LF. 2001 Chemiluminescence microscopy as a tool in biomedical research. Biotechniques 31:1098-1100.
    • (2001) Biotechniques , vol.31 , pp. 1098-1100
    • Creton, R.1    Jaffe, L.F.2
  • 20
    • 0026114521 scopus 로고
    • Guanosine 5′- thiotriphosphate may stimulate phosphoinositide messenger production in sea urchin eggs by a different route than the fertilizing sperm
    • Crossley I, Whalley T, Whitaker M. 1991. Guanosine 5′- thiotriphosphate may stimulate phosphoinositide messenger production in sea urchin eggs by a different route than the fertilizing sperm. Cell Regul 2:121-133.
    • (1991) Cell Regul , vol.2 , pp. 121-133
    • Crossley, I.1    Whalley, T.2    Whitaker, M.3
  • 21
    • 0023783839 scopus 로고
    • Primary and secondary messengers in the activation of ascidian eggs
    • Dale B. 1988. Primary and secondary messengers in the activation of ascidian eggs. Exp Cell Res 177:205-211.
    • (1988) Exp Cell Res , vol.177 , pp. 205-211
    • Dale, B.1
  • 22
    • 0022426591 scopus 로고
    • Injection of a soluble sperm fraction into sea-urchin eggs triggers the cortical reaction
    • Dale B, DeFelice LJ, Ehrenstein G. 1985. Injection of a soluble sperm fraction into sea-urchin eggs triggers the cortical reaction. Experientia 41:1068-1070.
    • (1985) Experientia , vol.41 , pp. 1068-1070
    • Dale, B.1    DeFelice, L.J.2    Ehrenstein, G.3
  • 23
    • 34548095177 scopus 로고
    • Observations sur le mechanisme et les phenomènes qui accompagnent la formation de l'embryon chez l'oursin comestible
    • Derbès AA. 1847. Observations sur le mechanisme et les phenomènes qui accompagnent la formation de l'embryon chez l'oursin comestible. Ann Sci Nat Zool 8:80-98.
    • (1847) Ann Sci Nat Zool , vol.8 , pp. 80-98
    • Derbès, A.A.1
  • 24
    • 0027202456 scopus 로고
    • Molecular mechanisms of nitric oxide regulation. Potential relevance to cardiovascular disease
    • Dinerman JL, Lowenstein CJ, Snyder SH. 1993. Molecular mechanisms of nitric oxide regulation. Potential relevance to cardiovascular disease. Circ Res 73:217-222.
    • (1993) Circ Res , vol.73 , pp. 217-222
    • Dinerman, J.L.1    Lowenstein, C.J.2    Snyder, S.H.3
  • 25
    • 0034708184 scopus 로고    scopus 로고
    • Xenopus and chicken sperm contain a cytosolic soluble protein factor which can trigger calcium oscillations in mouse eggs
    • Dong JB, Tang TS, Sun FZ. 2000. Xenopus and chicken sperm contain a cytosolic soluble protein factor which can trigger calcium oscillations in mouse eggs. Biochem Biophys Res Commun. 268:947-951.
    • (2000) Biochem Biophys Res Commun , vol.268 , pp. 947-951
    • Dong, J.B.1    Tang, T.S.2    Sun, F.Z.3
  • 26
    • 0029977431 scopus 로고    scopus 로고
    • Phospholipase C in mouse oocytes: Characterization of beta and gamma isoforms and their possible involvement in sperm-induced Ca2+ spiking
    • Dupont G, McGuinness OM, Johnson MH, Berridge MJ, Borgese F. 1996. Phospholipase C in mouse oocytes: characterization of beta and gamma isoforms and their possible involvement in sperm-induced Ca2+ spiking. Biochem J 316:583-591.
    • (1996) Biochem J , vol.316 , pp. 583-591
    • Dupont, G.1    McGuinness, O.M.2    Johnson, M.H.3    Berridge, M.J.4    Borgese, F.5
  • 27
    • 0031880170 scopus 로고    scopus 로고
    • Molecular mechanisms of sperm-egg interactions and egg activation
    • Evans JP, Kopf GS. 1998. Molecular mechanisms of sperm-egg interactions and egg activation. Andrologia 30:297-307.
    • (1998) Andrologia , vol.30 , pp. 297-307
    • Evans, J.P.1    Kopf, G.S.2
  • 28
    • 0028578120 scopus 로고
    • Mechanism of calcium oscillations in fertilized rabbit eggs
    • Fissore RA, Robl JM. 1994. Mechanism of calcium oscillations in fertilized rabbit eggs. Dev Biol 166:634-642.
    • (1994) Dev Biol , vol.166 , pp. 634-642
    • Fissore, R.A.1    Robl, J.M.2
  • 29
    • 0031835352 scopus 로고    scopus 로고
    • Fertilization failures and abnormal fertilization after intracytoplasmic sperm injection
    • Flaherty SP, Payne D, Matthews CD. 1998. Fertilization failures and abnormal fertilization after intracytoplasmic sperm injection. Hum Reprod Suppl 1:155-164.
    • (1998) Hum Reprod , Issue.SUPPL. 1 , pp. 155-164
    • Flaherty, S.P.1    Payne, D.2    Matthews, C.D.3
  • 31
    • 0018084733 scopus 로고
    • Activation of mammalian oocytes by intracellular injection of calcium
    • Fulton BP, Whittingham DG. 1978. Activation of mammalian oocytes by intracellular injection of calcium. Nature 273:149-151.
    • (1978) Nature , vol.273 , pp. 149-151
    • Fulton, B.P.1    Whittingham, D.G.2
  • 32
    • 0026418298 scopus 로고
    • 2+ release in sea urchin egg homogenates: Modulation by cyclic ADP-ribose
    • 2+ release in sea urchin egg homogenates: modulation by cyclic ADP-ribose. Science 253:1143-1146.
    • (1991) Science , vol.253 , pp. 1143-1146
    • Galione, A.1    Lee, H.C.2    Busa, W.B.3
  • 33
    • 0027282375 scopus 로고
    • Redundant mechanisms of calcium-induced calcium release underlying calcium waves during fertilization of sea urchin eggs
    • Galione A, McDougall A, Busa WB, Willmott N, Gillot I, Whitaker M. 1993. Redundant mechanisms of calcium-induced calcium release underlying calcium waves during fertilization of sea urchin eggs. Science 261:348-352.
    • (1993) Science , vol.261 , pp. 348-352
    • Galione, A.1    McDougall, A.2    Busa, W.B.3    Willmott, N.4    Gillot, I.5    Whitaker, M.6
  • 36
    • 0032828091 scopus 로고    scopus 로고
    • Requirement of a Src family kinase for initiating calcium release at fertilization in starfish eggs
    • Giusti AF, Carroll DJ, Abassi YA, Terasaki M, Foltz KR, Jaffe LA. 1999. Requirement of a Src family kinase for initiating calcium release at fertilization in starfish eggs. J Biol Chem 274:29318-29322.
    • (1999) J Biol Chem , vol.274 , pp. 29318-29322
    • Giusti, A.F.1    Carroll, D.J.2    Abassi, Y.A.3    Terasaki, M.4    Foltz, K.R.5    Jaffe, L.A.6
  • 37
    • 0344643005 scopus 로고    scopus 로고
    • Function of a sea urchin egg Src family kinase in initiating Ca2+ release at fertilization
    • Giusti AF, O'Neill FJ, Yamasu K, Foltz KR, Jaffe LA. 2003. Function of a sea urchin egg Src family kinase in initiating Ca2+ release at fertilization. Dev Biol 256:367-378.
    • (2003) Dev Biol , vol.256 , pp. 367-378
    • Giusti, A.F.1    O'Neill, F.J.2    Yamasu, K.3    Foltz, K.R.4    Jaffe, L.A.5
  • 38
    • 0033620487 scopus 로고    scopus 로고
    • Heptahelical receptor signaling: Beyond the G protein paradigm
    • Hall RA, Premont RT, Lefkowitz RJ. 1999. Heptahelical receptor signaling: beyond the G protein paradigm. J Cell Biol 145:927-932.
    • (1999) J Cell Biol , vol.145 , pp. 927-932
    • Hall, R.A.1    Premont, R.T.2    Lefkowitz, R.J.3
  • 39
    • 0028021882 scopus 로고
    • Pleckstrin homology domains bind to phosphatidylinositol-4,5-bisphosphate
    • Harlan JE, Hajduk PJ, Yoon HS, Fesik SW. 1994. Pleckstrin homology domains bind to phosphatidylinositol-4,5-bisphosphate. Nature 371:168-170.
    • (1994) Nature , vol.371 , pp. 168-170
    • Harlan, J.E.1    Hajduk, P.J.2    Yoon, H.S.3    Fesik, S.W.4
  • 41
    • 25144496216 scopus 로고    scopus 로고
    • Treatment option for sperm- or oocyte-related fertilization failure: Assisted oocyte activation following diagnostic heterologous ICSI
    • Heindryckx B, Van der Elst J, De Sutter P, Dhont M. 2005. Treatment option for sperm- or oocyte-related fertilization failure: assisted oocyte activation following diagnostic heterologous ICSI. Hum Reprod 20:2237-2241.
    • (2005) Hum Reprod , vol.20 , pp. 2237-2241
    • Heindryckx, B.1    Van der Elst, J.2    De Sutter, P.3    Dhont, M.4
  • 42
    • 0035371449 scopus 로고    scopus 로고
    • Simultaneous measurement of intracellular nitric oxide and free calcium levels in chordate eggs demonstrates that nitric oxide has no role at fertilization
    • Hyslop LA, Carroll M, Nixon VL, McDougall A, Jones KT. 2001. Simultaneous measurement of intracellular nitric oxide and free calcium levels in chordate eggs demonstrates that nitric oxide has no role at fertilization. Dev Biol 234:216-230.
    • (2001) Dev Biol , vol.234 , pp. 216-230
    • Hyslop, L.A.1    Carroll, M.2    Nixon, V.L.3    McDougall, A.4    Jones, K.T.5
  • 43
    • 0036318233 scopus 로고    scopus 로고
    • Group I mGluRs increase excitability of hippocampal CA1 pyramidal neurons by a PLC-independent mechanism
    • Ireland DR. Abraham WC. 2002. Group I mGluRs increase excitability of hippocampal CA1 pyramidal neurons by a PLC-independent mechanism. J Neurophysiol 88:107-116.
    • (2002) J Neurophysiol , vol.88 , pp. 107-116
    • Ireland, D.R.1    Abraham, W.C.2
  • 44
    • 0017127374 scopus 로고
    • Fast block to polyspermy in sea urchin eggs is electrically mediated
    • Jaffe LA. 1976. Fast block to polyspermy in sea urchin eggs is electrically mediated. Nature 261:68-71.
    • (1976) Nature , vol.261 , pp. 68-71
    • Jaffe, L.A.1
  • 45
    • 0020841230 scopus 로고
    • Sources of calcium in egg activation: A review and hypothesis
    • Jaffe LF. 1983. Sources of calcium in egg activation: a review and hypothesis. Dev Biol 99:265-276.
    • (1983) Dev Biol , vol.99 , pp. 265-276
    • Jaffe, L.F.1
  • 46
    • 0025582545 scopus 로고
    • First messengers at fertilization
    • Jaffe LA. 1990. First messengers at fertilization. J Reprod Fertil Suppl 42:107-116.
    • (1990) J Reprod Fertil , Issue.SUPPL. 42 , pp. 107-116
    • Jaffe, L.A.1
  • 47
    • 0026006483 scopus 로고
    • The path of calcium in cytosolic calcium oscillations: A unifying hypothesis
    • Jaffe LF. 1991. The path of calcium in cytosolic calcium oscillations: a unifying hypothesis. Proc Natl Acad Sci USA 88:9883-9887.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 9883-9887
    • Jaffe, L.F.1
  • 49
    • 0032217313 scopus 로고    scopus 로고
    • The passage of Ca2+ and fluorescent markers between the sperm and egg after fusion in the mouse
    • Jones KT, Soeller C, Cannell MB. 1998. The passage of Ca2+ and fluorescent markers between the sperm and egg after fusion in the mouse. Development. 125:4627-4635.
    • (1998) Development , vol.125 , pp. 4627-4635
    • Jones, K.T.1    Soeller, C.2    Cannell, M.B.3
  • 50
    • 0034653539 scopus 로고    scopus 로고
    • Different Ca2+-releasing abilities of sperm extracts compared with tissue extracts and phospholipase C isoforms in sea urchin egg homogenate and mouse eggs
    • Jones KT, Matsuda M, Parrington J, Katan M, Swann K. 2000. Different Ca2+-releasing abilities of sperm extracts compared with tissue extracts and phospholipase C isoforms in sea urchin egg homogenate and mouse eggs. Biochem J 346:743-749.
    • (2000) Biochem J , vol.346 , pp. 743-749
    • Jones, K.T.1    Matsuda, M.2    Parrington, J.3    Katan, M.4    Swann, K.5
  • 52
    • 0023928624 scopus 로고
    • Calcium-dependent events at fertilization of the frog egg: Injection of a calcium buffer blocks ion channel opening, exocytosis, and formation of pronuclei
    • Kline D. 1988. Calcium-dependent events at fertilization of the frog egg: injection of a calcium buffer blocks ion channel opening, exocytosis, and formation of pronuclei. Dev Biol 126:346-361.
    • (1988) Dev Biol , vol.126 , pp. 346-361
    • Kline, D.1
  • 53
    • 0026551829 scopus 로고
    • Repetitive calcium transients and the role of calcium in exocytosis and cell cycle activation in the mouse egg
    • Kline D, Kline JT. 1992. Repetitive calcium transients and the role of calcium in exocytosis and cell cycle activation in the mouse egg. Dev Biol 149:80-89.
    • (1992) Dev Biol , vol.149 , pp. 80-89
    • Kline, D.1    Kline, J.T.2
  • 54
    • 14844318766 scopus 로고    scopus 로고
    • Transgenic RNA interference reveals role for mouse sperm phospholipase Czeta in triggering Ca2+ oscillations during fertilization
    • Knott JG, Kurokawa M, Fissore RA, Schultz RM, Williams CJ. 2005. Transgenic RNA interference reveals role for mouse sperm phospholipase Czeta in triggering Ca2+ oscillations during fertilization. Biol Reprod 72:992-996.
    • (2005) Biol Reprod , vol.72 , pp. 992-996
    • Knott, J.G.1    Kurokawa, M.2    Fissore, R.A.3    Schultz, R.M.4    Williams, C.J.5
  • 55
    • 20444388673 scopus 로고    scopus 로고
    • The role of EF-hand domains and C2 domain in regulation of enzymatic activity of phospholipase Czeta
    • Kouchi Z, Shikano T, Nakamura Y, Shirakawa H, Fukami K, Miyazaki S. 2005. The role of EF-hand domains and C2 domain in regulation of enzymatic activity of phospholipase Czeta. J Biol Chem 280:21015-21021.
    • (2005) J Biol Chem , vol.280 , pp. 21015-21021
    • Kouchi, Z.1    Shikano, T.2    Nakamura, Y.3    Shirakawa, H.4    Fukami, K.5    Miyazaki, S.6
  • 57
    • 25844503701 scopus 로고    scopus 로고
    • Functional, biochemical, and chromatographic characterization of the complete [Ca2+]i oscillation-inducing activity of porcine sperm
    • Kurokawa M, Sato K, Wu H, He C, Malcuit C, Black SJ, Fukami K, Fissore RA. 2005. Functional, biochemical, and chromatographic characterization of the complete [Ca2+]i oscillation-inducing activity of porcine sperm. Dev Biol 285:376-392.
    • (2005) Dev Biol , vol.285 , pp. 376-392
    • Kurokawa, M.1    Sato, K.2    Wu, H.3    He, C.4    Malcuit, C.5    Black, S.J.6    Fukami, K.7    Fissore, R.A.8
  • 58
    • 0031793768 scopus 로고    scopus 로고
    • Injection of sperm extract mimics spatiotemporal dynamics of Ca2+ responses and progression of meiosis at fertilization of ascidian oocytes
    • Kyozuka K, Deguchi R, Mohri T, Miyazaki S. 1998. Injection of sperm extract mimics spatiotemporal dynamics of Ca2+ responses and progression of meiosis at fertilization of ascidian oocytes. Development 125:4099-4105.
    • (1998) Development , vol.125 , pp. 4099-4105
    • Kyozuka, K.1    Deguchi, R.2    Mohri, T.3    Miyazaki, S.4
  • 59
    • 3042818381 scopus 로고    scopus 로고
    • Cell cycle-dependent Ca2+ oscillations in mouse embryos are regulated by nuclear targeting of PLCzeta
    • Larman MG, Saunders CM, Carroll J, Lai FA, Swann K. 2004. Cell cycle-dependent Ca2+ oscillations in mouse embryos are regulated by nuclear targeting of PLCzeta. J Cell Sci 117:2513-2521.
    • (2004) J Cell Sci , vol.117 , pp. 2513-2521
    • Larman, M.G.1    Saunders, C.M.2    Carroll, J.3    Lai, F.A.4    Swann, K.5
  • 60
    • 0031029117 scopus 로고    scopus 로고
    • Sperm-egg fusion is the prelude to the initial Ca2+ increase at fertilization in the mouse
    • Lawrence Y, Whitaker M, Swann K. 1997. Sperm-egg fusion is the prelude to the initial Ca2+ increase at fertilization in the mouse. Development 124:233-241.
    • (1997) Development , vol.124 , pp. 233-241
    • Lawrence, Y.1    Whitaker, M.2    Swann, K.3
  • 62
    • 0028172098 scopus 로고
    • Regulation of phospholipase C-beta 4 by ribonucleotides and the alpha subunit of Gq
    • Lee CW, Lee KH, Lee SB, Park D, Rhee SG. 1994. Regulation of phospholipase C-beta 4 by ribonucleotides and the alpha subunit of Gq. J Biol Chem 269:25335-25338.
    • (1994) J Biol Chem , vol.269 , pp. 25335-25338
    • Lee, C.W.1    Lee, K.H.2    Lee, S.B.3    Park, D.4    Rhee, S.G.5
  • 63
    • 0027518440 scopus 로고
    • Potentiation of calcium- and caffeine-induced calcium release by cyclic ADP-ribose
    • Lee HC. 1993. Potentiation of calcium- and caffeine-induced calcium release by cyclic ADP-ribose. J Biol Chem 268:293-299.
    • (1993) J Biol Chem , vol.268 , pp. 293-299
    • Lee, H.C.1
  • 64
    • 0028950282 scopus 로고
    • A derivative of NAADP mobilizes calcium stores insensitive to inositol trisphosphate and cyclic ADP-ribose
    • Lee HC, Aarhus R. 1995. A derivative of NAADP mobilizes calcium stores insensitive to inositol trisphosphate and cyclic ADP-ribose. J Biol Chem 270:2152-2157.
    • (1995) J Biol Chem , vol.270 , pp. 2152-2157
    • Lee, H.C.1    Aarhus, R.2
  • 65
    • 0034496224 scopus 로고    scopus 로고
    • Functional visualization of the separate but interacting calcium stores sensitive to NAADP and cyclic ADP-ribose
    • Lee HC, Aarhus R. 2000. Functional visualization of the separate but interacting calcium stores sensitive to NAADP and cyclic ADP-ribose. J Cell Sci 113:4413-4420.
    • (2000) J Cell Sci , vol.113 , pp. 4413-4420
    • Lee, H.C.1    Aarhus, R.2
  • 66
    • 0027295646 scopus 로고
    • Calcium mobilization by dual receptors during fertilization of sea urchin eggs
    • Lee HC, Aarhus R, Graeff RM. 1993. Calcium mobilization by dual receptors during fertilization of sea urchin eggs. Science 261:352-355.
    • (1993) Science , vol.261 , pp. 352-355
    • Lee, H.C.1    Aarhus, R.2    Graeff, R.M.3
  • 67
    • 0028961777 scopus 로고
    • Sensitization of calcium-induced calcium release by cyclic ADP-ribose and calmodulin
    • Lee HC, Aarhus R, Graeff RM. 1995. Sensitization of calcium-induced calcium release by cyclic ADP-ribose and calmodulin. J Biol Chem 270:9060-9066.
    • (1995) J Biol Chem , vol.270 , pp. 9060-9066
    • Lee, H.C.1    Aarhus, R.2    Graeff, R.M.3
  • 68
    • 0031845050 scopus 로고    scopus 로고
    • U73122 blocked the cGMP-induced calcium release in sea urchin eggs
    • Lee SJ, Madden PJ, Shen SS. 1998. U73122 blocked the cGMP-induced calcium release in sea urchin eggs. Exp Cell Res 242:328-340
    • (1998) Exp Cell Res , vol.242 , pp. 328-340
    • Lee, S.J.1    Madden, P.J.2    Shen, S.S.3
  • 69
    • 33750319963 scopus 로고    scopus 로고
    • The Histamine H1 receptor activates the nitric oxide pathway at fertilization
    • Leguia M, Wessel GM. 2006. The Histamine H1 receptor activates the nitric oxide pathway at fertilization. Mol Reprod Dev 73:1550-1563.
    • (2006) Mol Reprod Dev , vol.73 , pp. 1550-1563
    • Leguia, M.1    Wessel, G.M.2
  • 70
    • 10444280038 scopus 로고    scopus 로고
    • Structure-function studies on nitric oxide synthases
    • Li H. Poulos TL. 2005. Structure-function studies on nitric oxide synthases. J Inorg Biochem 99:293-305.
    • (2005) J Inorg Biochem , vol.99 , pp. 293-305
    • Li, H.1    Poulos, T.L.2
  • 71
    • 4444267588 scopus 로고    scopus 로고
    • Src kinase mediates angiotensin II-dependent increase in pulmonary endothelial nitric oxide synthase
    • Li X, Lerea KM, Li J, Olson SC. 2004. Src kinase mediates angiotensin II-dependent increase in pulmonary endothelial nitric oxide synthase. Am J Respir Cell Mol Biol 31:365-372.
    • (2004) Am J Respir Cell Mol Biol , vol.31 , pp. 365-372
    • Li, X.1    Lerea, K.M.2    Li, J.3    Olson, S.C.4
  • 72
    • 0001384802 scopus 로고
    • The mechanism of fertilization
    • Lillie FR. 1913. The mechanism of fertilization. Science 38:524-528.
    • (1913) Science , vol.38 , pp. 524-528
    • Lillie, F.R.1
  • 74
    • 0031786125 scopus 로고    scopus 로고
    • The sevenfold way of PKC regulation
    • Liu WS, Heckman CA. 1998. The sevenfold way of PKC regulation. Cell Signal 10:529-542.
    • (1998) Cell Signal , vol.10 , pp. 529-542
    • Liu, W.S.1    Heckman, C.A.2
  • 75
    • 0007707159 scopus 로고
    • On the nature of the process of fertilization and the artificial production of normal larvae (Plutei) from the unfertilized eggs of the sea urchin
    • Loeb J. 1899. On the nature of the process of fertilization and the artificial production of normal larvae (Plutei) from the unfertilized eggs of the sea urchin. Am J Physiol 3:135-138.
    • (1899) Am J Physiol , vol.3 , pp. 135-138
    • Loeb, J.1
  • 76
    • 7944226933 scopus 로고    scopus 로고
    • Not so strange bedfellows: G-protein-coupled receptors and Src family kinases
    • Luttrell DK, Luttrell LM. 2004. Not so strange bedfellows: G-protein-coupled receptors and Src family kinases. Oncogene 23:7969-7978.
    • (2004) Oncogene , vol.23 , pp. 7969-7978
    • Luttrell, D.K.1    Luttrell, L.M.2
  • 78
    • 0036473397 scopus 로고    scopus 로고
    • The role of beta-arrestins in the termination and transduction of G-protein-coupled receptor signals
    • Luttrell LM, Lefkowitz RJ. 2002. The role of beta-arrestins in the termination and transduction of G-protein-coupled receptor signals. J Cell Sci 115:455-465.
    • (2002) J Cell Sci , vol.115 , pp. 455-465
    • Luttrell, L.M.1    Lefkowitz, R.J.2
  • 79
    • 0034268796 scopus 로고    scopus 로고
    • Src tyrosine kinase is a novel direct effector of G proteins
    • Ma YC, Huang J, Ali S, Lowry W, Huang XY. 2000. Src tyrosine kinase is a novel direct effector of G proteins. Cell 102:635-646.
    • (2000) Cell , vol.102 , pp. 635-646
    • Ma, Y.C.1    Huang, J.2    Ali, S.3    Lowry, W.4    Huang, X.Y.5
  • 80
    • 0038621261 scopus 로고    scopus 로고
    • Failed fertilization: Is it predictable?
    • Mahutte NG, Arid A. 2003. Failed fertilization: is it predictable? Curr Opin Obstet Gynecol 15:211-218.
    • (2003) Curr Opin Obstet Gynecol , vol.15 , pp. 211-218
    • Mahutte, N.G.1    Arid, A.2
  • 82
    • 3042743979 scopus 로고    scopus 로고
    • Fertilization stimulates long-lasting oscillations of CaMKII activity in mouse eggs
    • Markoulaki S, Matson S, Ducibella T. 2004. Fertilization stimulates long-lasting oscillations of CaMKII activity in mouse eggs. Dev Biol 272:15-25.
    • (2004) Dev Biol , vol.272 , pp. 15-25
    • Markoulaki, S.1    Matson, S.2    Ducibella, T.3
  • 83
    • 0041810555 scopus 로고    scopus 로고
    • Regulation of endothelial nitric oxide synthase by protein kinase C
    • Matsubara M, Hayashi N, Jing T, Titani K. 2003. Regulation of endothelial nitric oxide synthase by protein kinase C. J Biochem (Tokyo) 133:773-781.
    • (2003) J Biochem (Tokyo) , vol.133 , pp. 773-781
    • Matsubara, M.1    Hayashi, N.2    Jing, T.3    Titani, K.4
  • 84
    • 0009032641 scopus 로고
    • The release of calcium in Arbacia eggs on fertilization
    • Mazia D. 1937. The release of calcium in Arbacia eggs on fertilization. J Cell Comp Physiol 10:291-304.
    • (1937) J Cell Comp Physiol , vol.10 , pp. 291-304
    • Mazia, D.1
  • 85
    • 0026551217 scopus 로고
    • Fusion of membranes during fertilization. Increases of the sea urchin egg's membrane capacitance and membrane conductance at the site of contact with the sperm
    • McCulloh DH, Chambers EL. 1992. Fusion of membranes during fertilization. Increases of the sea urchin egg's membrane capacitance and membrane conductance at the site of contact with the sperm. J Gen Physiol 99:137-175.
    • (1992) J Gen Physiol , vol.99 , pp. 137-175
    • McCulloh, D.H.1    Chambers, E.L.2
  • 86
    • 0032212731 scopus 로고    scopus 로고
    • SH2 domain-mediated activation of phospholipase Cgamma is not required to initiate Ca2+ release at fertilization of mouse eggs
    • Mehlmann LM, Carpenter G, Rhee SG, Jaffe LA. 1998. SH2 domain-mediated activation of phospholipase Cgamma is not required to initiate Ca2+ release at fertilization of mouse eggs. Dev Biol 203:221-232.
    • (1998) Dev Biol , vol.203 , pp. 221-232
    • Mehlmann, L.M.1    Carpenter, G.2    Rhee, S.G.3    Jaffe, L.A.4
  • 87
    • 0035881623 scopus 로고    scopus 로고
    • Evidence that phospholipase C from the sperm is not responsible for initiating Ca(2 + ) release at fertilization in mouse eggs
    • Mehlmann LM, Chattopadhyay A, Carpenter G, Jaffe LA. 2001. Evidence that phospholipase C from the sperm is not responsible for initiating Ca(2 + ) release at fertilization in mouse eggs. Dev Biol 236:492-501.
    • (2001) Dev Biol , vol.236 , pp. 492-501
    • Mehlmann, L.M.1    Chattopadhyay, A.2    Carpenter, G.3    Jaffe, L.A.4
  • 88
    • 0030711558 scopus 로고    scopus 로고
    • Nitric oxide synthases: Which, where, how, and why?
    • Michel T. Feron O. 1997. Nitric oxide synthases: which, where, how, and why? J Clin Invest 100:2146-2152.
    • (1997) J Clin Invest , vol.100 , pp. 2146-2152
    • Michel, T.1    Feron, O.2
  • 89
    • 0023872015 scopus 로고
    • Inositol 1,4,5-trisphos-phate-induced calcium release and guanine nucleotide-binding protein-mediated periodic calcium rises in golden hamster eggs
    • Miyazaki S. 1988. Inositol 1,4,5-trisphos-phate-induced calcium release and guanine nucleotide-binding protein-mediated periodic calcium rises in golden hamster eggs. J Cell Biol 106:345-353.
    • (1988) J Cell Biol , vol.106 , pp. 345-353
    • Miyazaki, S.1
  • 90
    • 0026611212 scopus 로고
    • Block of Ca2+ wave and Ca2+ oscillation by antibody to the inositol 1,4,5-trisphosphate receptor in fertilized hamster eggs
    • Miyazaki S, Yuzaki M, Nakada K, Shirakawa H, Nakanishi S, Nakade S, Mikoshiba K 1992. Block of Ca2+ wave and Ca2+ oscillation by antibody to the inositol 1,4,5-trisphosphate receptor in fertilized hamster eggs. Science 257:251-255.
    • (1992) Science , vol.257 , pp. 251-255
    • Miyazaki, S.1    Yuzaki, M.2    Nakada, K.3    Shirakawa, H.4    Nakanishi, S.5    Nakade, S.6    Mikoshiba, K.7
  • 92
    • 0025883342 scopus 로고
    • Nitric oxide: Physiology, pathophysiology, and pharmacology
    • Moncada S, Palmer RM, Higgs EA. 1991. Nitric oxide: physiology, pathophysiology, and pharmacology. Pharmacol Rev 43:109-142.
    • (1991) Pharmacol Rev , vol.43 , pp. 109-142
    • Moncada, S.1    Palmer, R.M.2    Higgs, E.A.3
  • 93
    • 0028138752 scopus 로고
    • Roles of heterotrimeric and monomeric G proteins in sperm-induced activation of mouse eggs
    • Moore GD, Ayabe T, Visconti PE, Schultz RM, Kopf GS. 1994. Roles of heterotrimeric and monomeric G proteins in sperm-induced activation of mouse eggs. Development 120:3313-3323.
    • (1994) Development , vol.120 , pp. 3313-3323
    • Moore, G.D.1    Ayabe, T.2    Visconti, P.E.3    Schultz, R.M.4    Kopf, G.S.5
  • 94
    • 84982342161 scopus 로고
    • Studies on a cortical layer response to stimulating agents in the Arbacia egg. I. Response to insemination
    • Moser F. 1939. Studies on a cortical layer response to stimulating agents in the Arbacia egg. I. Response to insemination. J Exp Zool 80:423-445.
    • (1939) J Exp Zool , vol.80 , pp. 423-445
    • Moser, F.1
  • 96
    • 0028971813 scopus 로고
    • Phosphoinositide-specific phospholipase C and mitogenic signaling
    • Noh DY, Shin SH, Rhee SG. 1995. Phosphoinositide-specific phospholipase C and mitogenic signaling. Biochim Biophys Acta 1242:99-113.
    • (1995) Biochim Biophys Acta , vol.1242 , pp. 99-113
    • Noh, D.Y.1    Shin, S.H.2    Rhee, S.G.3
  • 98
    • 0035179382 scopus 로고    scopus 로고
    • Does a soluble sperm factor trigger calcium release in the egg at fertilization?
    • Parrington J. 2001. Does a soluble sperm factor trigger calcium release in the egg at fertilization? J Androl 22:1-11.
    • (2001) J Androl , vol.22 , pp. 1-11
    • Parrington, J.1
  • 99
    • 0033165916 scopus 로고    scopus 로고
    • The soluble sperm factor that causes Ca2+ release from sea-urchin (Lytechinus pictus) egg homogenates also triggers Ca2+ oscillations after injection into mouse eggs
    • Parrington J, Jones KT, Lai A, Swann K. 1999. The soluble sperm factor that causes Ca2+ release from sea-urchin (Lytechinus pictus) egg homogenates also triggers Ca2+ oscillations after injection into mouse eggs. Biochem J 341:1-4.
    • (1999) Biochem J , vol.341 , pp. 1-4
    • Parrington, J.1    Jones, K.T.2    Lai, A.3    Swann, K.4
  • 100
    • 0036153870 scopus 로고    scopus 로고
    • Phospholipase C isoforms in mammalian spermatozoa: Potential components of the sperm factor that causes Ca2+ release in eggs
    • Parrington J, Jones KT, Lai A, Swann K. 2002. Phospholipase C isoforms in mammalian spermatozoa: potential components of the sperm factor that causes Ca2+ release in eggs. Reproduction 123:31-39.
    • (2002) Reproduction , vol.123 , pp. 31-39
    • Parrington, J.1    Jones, K.T.2    Lai, A.3    Swann, K.4
  • 101
    • 1242321159 scopus 로고    scopus 로고
    • 2+ release: A new signalling pathway
    • 2+ release: a new signalling pathway. Biol Cell 96:19-28.
    • (2004) Biol Cell , vol.96 , pp. 19-28
    • Patel, S.1
  • 103
    • 0029416975 scopus 로고
    • Ca-2+ release triggered by nicotinate adenine dinucleotide phosphate in intact sea urchin eggs
    • Perez-Terzic CM, Chini EN, Shen SS, Dousa TP, Clapham DE. 1995. Ca-2+ release triggered by nicotinate adenine dinucleotide phosphate in intact sea urchin eggs. Biochem J 312:955-959.
    • (1995) Biochem J , vol.312 , pp. 955-959
    • Perez-Terzic, C.M.1    Chini, E.N.2    Shen, S.S.3    Dousa, T.P.4    Clapham, D.E.5
  • 104
    • 0035805565 scopus 로고    scopus 로고
    • S-nitrosation controls gating and conductance of the alpha 1 subunit of class C L-type Ca(2+) channels
    • Poteser M, Romanin C, Schreibmayer W, Mayer B, Groschner K. 2001. S-nitrosation controls gating and conductance of the alpha 1 subunit of class C L-type Ca(2+) channels. J Biol Chem 276:14797-14803.
    • (2001) J Biol Chem , vol.276 , pp. 14797-14803
    • Poteser, M.1    Romanin, C.2    Schreibmayer, W.3    Mayer, B.4    Groschner, K.5
  • 105
    • 0025663498 scopus 로고
    • Multiple stores of calcium are released in the sea urchin egg during fertilization
    • Rakow TL, Shen SS. 1990. Multiple stores of calcium are released in the sea urchin egg during fertilization. Proc Natl Acad Sci USA 87:9285-9289.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 9285-9289
    • Rakow, T.L.1    Shen, S.S.2
  • 106
    • 0033605718 scopus 로고    scopus 로고
    • The role of phosphoinositide 3-kinase lipid products in cell function
    • Rameh L E, Cantley LC. 1999. The role of phosphoinositide 3-kinase lipid products in cell function. J Biol Chem 274:8347-8350.
    • (1999) J Biol Chem , vol.274 , pp. 8347-8350
    • Rameh, L.E.1    Cantley, L.C.2
  • 107
    • 0034927336 scopus 로고    scopus 로고
    • Regulation of phosphoinositide-specific phospholipase C
    • Rhee SG. 2001. Regulation of phosphoinositide-specific phospholipase C. Annu Rev Biochem 70:281-312.
    • (2001) Annu Rev Biochem , vol.70 , pp. 281-312
    • Rhee, S.G.1
  • 108
    • 0010466626 scopus 로고
    • Free calcium increases explosively in activating medaka eggs
    • Ridgway EB, Gilkey JC, Jaffe LF. 1977. Free calcium increases explosively in activating medaka eggs. Proc Natl Acad Sci USA 74:623-627.
    • (1977) Proc Natl Acad Sci USA , vol.74 , pp. 623-627
    • Ridgway, E.B.1    Gilkey, J.C.2    Jaffe, L.F.3
  • 109
    • 0033571306 scopus 로고    scopus 로고
    • Fertilization-induced activation of phospholipase C in the sea urchin egg
    • Rongish BJ, Wu W, Kinsey WH 1999. Fertilization-induced activation of phospholipase C in the sea urchin egg. Dev Biol 215:147-154.
    • (1999) Dev Biol , vol.215 , pp. 147-154
    • Rongish, B.J.1    Wu, W.2    Kinsey, W.H.3
  • 111
    • 0033845362 scopus 로고    scopus 로고
    • Sperm extract injection into ascidian eggs signals Ca(2 + ) release by the same pathway as fertilization
    • Runft LL, Jaffe LA. 2000. Sperm extract injection into ascidian eggs signals Ca(2 + ) release by the same pathway as fertilization. Development 127:3227-3236.
    • (2000) Development , vol.127 , pp. 3227-3236
    • Runft, L.L.1    Jaffe, L.A.2
  • 112
    • 0033570085 scopus 로고    scopus 로고
    • Calcium release at fertilization of Xenopus eggs requires type I IP(3) receptors, but not SH2 domain-mediated activation of PLCgamma or G(q)-mediated activation of PLCbeta
    • Runft LL, Watras J, Jaffe LA. 1999. Calcium release at fertilization of Xenopus eggs requires type I IP(3) receptors, but not SH2 domain-mediated activation of PLCgamma or G(q)-mediated activation of PLCbeta. Dev Biol 214:399-411.
    • (1999) Dev Biol , vol.214 , pp. 399-411
    • Runft, L.L.1    Watras, J.2    Jaffe, L.A.3
  • 113
    • 0037092883 scopus 로고    scopus 로고
    • Egg activation at fertilization: Where it all begins
    • Runft LL, Jaffe LA, Mehlmann LM. 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
  • 114
    • 1842665585 scopus 로고    scopus 로고
    • Identification of a starfish egg PLC-gamma that regulates Ca2+ release at fertilization
    • Runft LL, Carroll DJ, Gillett J, Giusti AF, O'Neill FJ, Foltz KR. 2004. Identification of a starfish egg PLC-gamma that regulates Ca2+ release at fertilization. Dev Biol 269:220-236.
    • (2004) Dev Biol , vol.269 , pp. 220-236
    • Runft, L.L.1    Carroll, D.J.2    Gillett, J.3    Giusti, A.F.4    O'Neill, F.J.5    Foltz, K.R.6
  • 116
    • 0034663334 scopus 로고    scopus 로고
    • Tyrosine kinase-dependent activation of phospholipase Cgamma is required for calcium transient in Xenopus egg fertilization
    • Sato K, Tokmakov AA, Iwasaki T, Fukami Y. 2000. Tyrosine kinase-dependent activation of phospholipase Cgamma is required for calcium transient in Xenopus egg fertilization. Dev Biol 224:453-469.
    • (2000) Dev Biol , vol.224 , pp. 453-469
    • Sato, K.1    Tokmakov, A.A.2    Iwasaki, T.3    Fukami, Y.4
  • 119
    • 0034999150 scopus 로고    scopus 로고
    • Kiss and run mechanism in exocytosis
    • Schneider SW. 2001. Kiss and run mechanism in exocytosis. J Membr Biol 181:67-76.
    • (2001) J Membr Biol , vol.181 , pp. 67-76
    • Schneider, S.W.1
  • 120
    • 0028795988 scopus 로고
    • Molecular basis of mammalian egg activation
    • Schultz RM, Kopf GS. 1995. Molecular basis of mammalian egg activation. Curr Top Dev Biol 30:21-62.
    • (1995) Curr Top Dev Biol , vol.30 , pp. 21-62
    • Schultz, R.M.1    Kopf, G.S.2
  • 121
    • 0029828803 scopus 로고    scopus 로고
    • Nicotinamide inhibits cyclic ADP-ribose-mediated calcium signalling in sea urchin eggs
    • Sethi JK, Empson RM, Galione A. 1996. Nicotinamide inhibits cyclic ADP-ribose-mediated calcium signalling in sea urchin eggs. Biochem J 319:613-617.
    • (1996) Biochem J , vol.319 , pp. 613-617
    • Sethi, J.K.1    Empson, R.M.2    Galione, A.3
  • 122
    • 0027167797 scopus 로고
    • Sources of calcium in sea urchin eggs during the fertilization response
    • Shen SS, Buck WR. 1993. Sources of calcium in sea urchin eggs during the fertilization response. Dev Biol 157:157-169.
    • (1993) Dev Biol , vol.157 , pp. 157-169
    • Shen, S.S.1    Buck, W.R.2
  • 123
    • 0027214868 scopus 로고
    • Regulation of purified subtypes of phosphatidylinositol-specific phospholipase C beta by G protein alpha and beta gamma subunits
    • Smrcka AV, Sternweis PC. 1993. Regulation of purified subtypes of phosphatidylinositol-specific phospholipase C beta by G protein alpha and beta gamma subunits. J Biol Chem 268:9667-9674.
    • (1993) J Biol Chem , vol.268 , pp. 9667-9674
    • Smrcka, A.V.1    Sternweis, P.C.2
  • 124
    • 33750995860 scopus 로고    scopus 로고
    • The Sea Urchin Genome Sequencing Consortium. The genome of the sea urchin Strongylocentrotus purpuratus
    • Sodergren E. 2006. The Sea Urchin Genome Sequencing Consortium. The genome of the sea urchin Strongylocentrotus purpuratus. Science 314:941-952.
    • (2006) Science , vol.314 , pp. 941-952
    • Sodergren, E.1
  • 125
    • 0030920782 scopus 로고    scopus 로고
    • G protein mechanisms: Insights from structural analysis
    • Sprang SR. 1997. G protein mechanisms: insights from structural analysis. Annu Rev Biochem 66:639-678.
    • (1997) Annu Rev Biochem , vol.66 , pp. 639-678
    • Sprang, S.R.1
  • 126
    • 0016163713 scopus 로고
    • Activation of sea-urchin eggs by a calcium ionophore
    • Steinhardt RA, Epel D 1974. Activation of sea-urchin eggs by a calcium ionophore. Proc Natl Acad Sci USA. 71:1915-1919.
    • (1974) Proc Natl Acad Sci USA , vol.71 , pp. 1915-1919
    • Steinhardt, R.A.1    Epel, D.2
  • 127
    • 0016357186 scopus 로고
    • Is calcium ionophore a universal activator for unfertilised eggs?
    • Steinhardt RA, Epel D, Carroll EJ Jr, Yanagimachi R. 1974. Is calcium ionophore a universal activator for unfertilised eggs? Nature 252:41-43.
    • (1974) Nature , vol.252 , pp. 41-43
    • Steinhardt, R.A.1    Epel, D.2    Carroll Jr, E.J.3    Yanagimachi, R.4
  • 128
    • 0027968449 scopus 로고
    • Sperm increase inositol 1,4,5-trisphosphate mass in Xenopus laevis eggs preinjected with calcium buffers or heparin
    • Stith BJ, Espinoza R, Roberts D, Smart T. 1994. Sperm increase inositol 1,4,5-trisphosphate mass in Xenopus laevis eggs preinjected with calcium buffers or heparin. Dev Biol 165:206-215.
    • (1994) Dev Biol , vol.165 , pp. 206-215
    • Stith, B.J.1    Espinoza, R.2    Roberts, D.3    Smart, T.4
  • 129
    • 0033566185 scopus 로고    scopus 로고
    • Comparative biology of calcium signaling during fertilization and egg activation in animals
    • Stricker SA. 1999. Comparative biology of calcium signaling during fertilization and egg activation in animals. Dev Biol 211:157-176.
    • (1999) Dev Biol , vol.211 , pp. 157-176
    • Stricker, S.A.1
  • 130
    • 0025637730 scopus 로고
    • Cytosolic sperm factor stimulates repetitive calcium increases and mimics fertilization in hamster eggs
    • Swann KA. 1990. Cytosolic sperm factor stimulates repetitive calcium increases and mimics fertilization in hamster eggs. Development 110:1295-1302.
    • (1990) Development , vol.110 , pp. 1295-1302
    • Swann, K.A.1
  • 131
    • 0028363794 scopus 로고
    • Dynamics of the calcium signal that triggers mammalian egg activation
    • Swann K, Ozil JP. 1994. Dynamics of the calcium signal that triggers mammalian egg activation. Int Rev Cytol 152:183-222.
    • (1994) Int Rev Cytol , vol.152 , pp. 183-222
    • Swann, K.1    Ozil, J.P.2
  • 132
    • 33745909900 scopus 로고    scopus 로고
    • PLCzeta(zeta): A sperm protein that triggers Ca2+ oscillations and egg activation in mammals
    • Swann K, Saunders CM, Rogers NT, Lai FA. 2006. PLCzeta(zeta): a sperm protein that triggers Ca2+ oscillations and egg activation in mammals. Semin Cell Dev Biol 17:264-273.
    • (2006) Semin Cell Dev Biol , vol.17 , pp. 264-273
    • Swann, K.1    Saunders, C.M.2    Rogers, N.T.3    Lai, F.A.4
  • 134
    • 0037465761 scopus 로고    scopus 로고
    • Mechanism of S-nitrosation of recombinant human brain calbindin D28K
    • Tao L, English AM. 2003. Mechanism of S-nitrosation of recombinant human brain calbindin D28K. Biochemistry 42:3326-3334.
    • (2003) Biochemistry , vol.42 , pp. 3326-3334
    • Tao, L.1    English, A.M.2
  • 135
    • 0036055185 scopus 로고    scopus 로고
    • Possible role for Ca(2+) calmodulin-dependent protein kinase II as an effector of the fertilization Ca(2+) signal in mouse oocyte activation
    • Tatone C, Delle Monache S, Iorio R, Caserta D, Di Cola M, Colonna R. 2002. Possible role for Ca(2+) calmodulin-dependent protein kinase II as an effector of the fertilization Ca(2+) signal in mouse oocyte activation. Mol Hum Reprod 8:750-757.
    • (2002) Mol Hum Reprod , vol.8 , pp. 750-757
    • Tatone, C.1    Delle Monache, S.2    Iorio, R.3    Caserta, D.4    Di Cola, M.5    Colonna, R.6
  • 136
    • 9144225522 scopus 로고    scopus 로고
    • Phosphoinositide metabolism at fertilization of sea urchin eggs measured with a GFP-probe
    • Thaler CD, Kuo RC, Patton C, Preston CM, Yagisawa H, Epel D. 2004. Phosphoinositide metabolism at fertilization of sea urchin eggs measured with a GFP-probe. Dev Growth Differ 46:413-423.
    • (2004) Dev Growth Differ , vol.46 , pp. 413-423
    • Thaler, C.D.1    Kuo, R.C.2    Patton, C.3    Preston, C.M.4    Yagisawa, H.5    Epel, D.6
  • 137
    • 2342595924 scopus 로고    scopus 로고
    • Zymogen granule exocytosis is characterized by long fusion pore openings and preservation of vesicle lipid identity
    • Thorn P, Fogarty KE, Parker I. 2004. Zymogen granule exocytosis is characterized by long fusion pore openings and preservation of vesicle lipid identity. Proc Natl Acad Sci USA 101:6774-6779.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 6774-6779
    • Thorn, P.1    Fogarty, K.E.2    Parker, I.3
  • 138
    • 33745883247 scopus 로고    scopus 로고
    • Signal transduction at fertilization: The Ca2+ release pathway in echinoderms and other invertebrate deuterostomes
    • Townley IK, Roux MM, Foltz KR. 2006. Signal transduction at fertilization: the Ca2+ release pathway in echinoderms and other invertebrate deuterostomes. Semin Cell Dev Biol. 17:293-302.
    • (2006) Semin Cell Dev Biol , vol.17 , pp. 293-302
    • Townley, I.K.1    Roux, M.M.2    Foltz, K.R.3
  • 139
    • 0022637421 scopus 로고
    • Regulation of cortical vesicle exocytosis in sea urchin eggs by inositol 1,4,5-trisphosphate and GTP-binding protein
    • Turner PR, Jaffe LA, Fein A. 1986. Regulation of cortical vesicle exocytosis in sea urchin eggs by inositol 1,4,5-trisphosphate and GTP-binding protein. J Cell Biol 102:70-76.
    • (1986) J Cell Biol , vol.102 , pp. 70-76
    • Turner, P.R.1    Jaffe, L.A.2    Fein, A.3
  • 140
    • 12344279431 scopus 로고    scopus 로고
    • betagamma subunits of heterotrimeric G-proteins contribute to Ca2+ release at fertilization in the sea urchin
    • Voronina E, Wessel GM. 2004. betagamma subunits of heterotrimeric G-proteins contribute to Ca2+ release at fertilization in the sea urchin. J Cell Sci 117:5995-6005.
    • (2004) J Cell Sci , vol.117 , pp. 5995-6005
    • Voronina, E.1    Wessel, G.M.2
  • 142
    • 0027315182 scopus 로고
    • T cell antigen receptor signal transduction: A tale of tails and cytoplasmic protein-tyrosine kinases
    • Weiss A. 1993. T cell antigen receptor signal transduction: a tale of tails and cytoplasmic protein-tyrosine kinases. Cell 73:209-212.
    • (1993) Cell , vol.73 , pp. 209-212
    • Weiss, A.1
  • 143
    • 0027082726 scopus 로고
    • Internal calcium release and activation of sea urchin eggs by cGMP are independent of the phosphoinositide signaling pathwayy
    • Whalley T, McDougall A, Crossley I, Swann K, Whitaker M. 1992. Internal calcium release and activation of sea urchin eggs by cGMP are independent of the phosphoinositide signaling pathwayy. Mol Biol Cell 3:373-383.
    • (1992) Mol Biol Cell , vol.3 , pp. 373-383
    • Whalley, T.1    McDougall, A.2    Crossley, I.3    Swann, K.4    Whitaker, M.5
  • 144
    • 33750523840 scopus 로고    scopus 로고
    • Calcium microdomains and cell cycle control
    • Whitaker M. 2006. Calcium microdomains and cell cycle control. Cell Calcium 40:585-592.
    • (2006) Cell Calcium , vol.40 , pp. 585-592
    • Whitaker, M.1
  • 145
  • 146
    • 0027403085 scopus 로고
    • Lighting the fuse at fertilization
    • Whitaker MJ, Swann K. 1993. Lighting the fuse at fertilization. Development 117:1-12.
    • (1993) Development , vol.117 , pp. 1-12
    • Whitaker, M.J.1    Swann, K.2
  • 147
    • 0026562632 scopus 로고
    • Role of G proteins in mouse egg activation: Stimulatory effects of acetylcholine on the ZP2 to ZP2f conversion and pronuclear formation in eggs expressing a functional m1 muscarinic receptor
    • Williams CJ, Schultz RM, Kopf GS. 1992. Role of G proteins in mouse egg activation: stimulatory effects of acetylcholine on the ZP2 to ZP2f conversion and pronuclear formation in eggs expressing a functional m1 muscarinic receptor. Dev Biol 151:288-296.
    • (1992) Dev Biol , vol.151 , pp. 288-296
    • Williams, C.J.1    Schultz, R.M.2    Kopf, G.S.3
  • 148
    • 0030044293 scopus 로고    scopus 로고
    • Nitric oxide induced mobilization of intracellular calcium via the cyclic ADP-ribose signalling pathway
    • Willmott N, Sethi JK, Walseth TF, Lee HC, White AM, Galione A. 1996. Nitric oxide induced mobilization of intracellular calcium via the cyclic ADP-ribose signalling pathway. J Biol Chem 271:3699-3705.
    • (1996) J Biol Chem , vol.271 , pp. 3699-3705
    • Willmott, N.1    Sethi, J.K.2    Walseth, T.F.3    Lee, H.C.4    White, A.M.5    Galione, A.6
  • 150
    • 33645885359 scopus 로고    scopus 로고
    • Defending the zygote: Search for the ancestral animal block to polyspermy
    • Schatten G, editor, New York: Academic Press, p
    • Wong J, Wessel GM. 2006. Defending the zygote: Search for the ancestral animal block to polyspermy. In: Schatten G, editor. Current topics in developmental biology, vol. 72. New York: Academic Press, p 1-151.
    • (2006) Current topics in developmental biology , vol.72 , pp. 1-151
    • Wong, J.1    Wessel, G.M.2
  • 152
    • 0032498185 scopus 로고    scopus 로고
    • Activation of the cardiac calcium release channel (ryanodine receptor) by poly-S-nitrosylation
    • Xu L, Eu JP, Meissner G, Stamler JS. 1998. Activation of the cardiac calcium release channel (ryanodine receptor) by poly-S-nitrosylation. Science 279:234-237.
    • (1998) Science , vol.279 , pp. 234-237
    • Xu, L.1    Eu, J.P.2    Meissner, G.3    Stamler, J.S.4
  • 153
    • 24344463972 scopus 로고    scopus 로고
    • Complete fertilization failure in ICSI
    • Yanagida K. 2004. Complete fertilization failure in ICSI. Hum Cell 17:187-193.
    • (2004) Hum Cell , vol.17 , pp. 187-193
    • Yanagida, K.1
  • 154
    • 0028535827 scopus 로고
    • Fertility of mammalian spermatozoa: Its development and relativity
    • Yanagimachi R. 1994. Fertility of mammalian spermatozoa: its development and relativity. Zygote 2:371-372.
    • (1994) Zygote , vol.2 , pp. 371-372
    • Yanagimachi, R.1
  • 155
    • 1942422232 scopus 로고    scopus 로고
    • Ca2+ oscillation-inducing phospholipase C zeta expressed in mouse eggs is accumulated to the pronucleus during egg activation
    • Yoda A, Oda S, Shikano T, Kouchi Z, Awaji T, Shirakawa H, Kinoshita K, Miyazaki S. 2004. Ca2+ oscillation-inducing phospholipase C zeta expressed in mouse eggs is accumulated to the pronucleus during egg activation. Dev Biol 268:245-257.
    • (2004) Dev Biol , vol.268 , pp. 245-257
    • Yoda, A.1    Oda, S.2    Shikano, T.3    Kouchi, Z.4    Awaji, T.5    Shirakawa, H.6    Kinoshita, K.7    Miyazaki, S.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.