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Volumn 49, Issue 5, 2011, Pages 323-330

Ca2+ signaling, genes and the cell cycle

Author keywords

Ca signaling; Cell cycle; Fertilization; Gene expression; T cell activation

Indexed keywords

ADENOSINE TRIPHOSPHATASE (CALCIUM); CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE II; CALCIUM ION; CALCIUM RELEASE ACTIVATED CALCIUM CHANNEL 1; CALMODULIN; CYCLIN B; CYCLIN D; CYCLIN DEPENDENT KINASE 2; CYCLIN DEPENDENT KINASE 4; CYCLIN E; STROMAL INTERACTION MOLECULE 1;

EID: 79958210180     PISSN: 01434160     EISSN: 15321991     Source Type: Journal    
DOI: 10.1016/j.ceca.2011.05.004     Document Type: Erratum
Times cited : (48)

References (144)
  • 3
    • 37149029370 scopus 로고    scopus 로고
    • Calcium signaling
    • Clapham D.E. Calcium signaling. Cell 2007, 131:1047-1058.
    • (2007) Cell , vol.131 , pp. 1047-1058
    • Clapham, D.E.1
  • 4
    • 47249152762 scopus 로고    scopus 로고
    • Ca2+ microdomains near plasma membrane Ca2+ channels: impact on cell function
    • Parekh A.B. Ca2+ microdomains near plasma membrane Ca2+ channels: impact on cell function. J. Physiol. 2008, 586:3043-3054.
    • (2008) J. Physiol. , vol.586 , pp. 3043-3054
    • Parekh, A.B.1
  • 6
    • 0038758748 scopus 로고    scopus 로고
    • Measurements of the free luminal ER Ca(2+) concentration with targeted " cameleon" fluorescent proteins
    • Demaurex N., Frieden M. Measurements of the free luminal ER Ca(2+) concentration with targeted " cameleon" fluorescent proteins. Cell Calcium 2003, 34:109-119.
    • (2003) Cell Calcium , vol.34 , pp. 109-119
    • Demaurex, N.1    Frieden, M.2
  • 7
    • 0009032641 scopus 로고
    • The release of calcium in Arbacia eggs on fertilization
    • Mazia D. The release of calcium in Arbacia eggs on fertilization. J. Comp. Cell. Phys. 1937, 10:291-304.
    • (1937) J. Comp. Cell. Phys. , vol.10 , pp. 291-304
    • Mazia, D.1
  • 8
    • 78649445055 scopus 로고
    • Les mouvements du calcium dans l'oeuf d'Arbacia lixula au moment de la fecondation
    • Nigon V., Do F. Les mouvements du calcium dans l'oeuf d'Arbacia lixula au moment de la fecondation. C.R.H. Acad. Sci. 1963, 257:2178-2180.
    • (1963) C.R.H. Acad. Sci. , vol.257 , pp. 2178-2180
    • Nigon, V.1    Do, F.2
  • 9
    • 0015424972 scopus 로고
    • Calcium uptake and release by dividing sea urchin eggs
    • Clothier G., Timourian H. Calcium uptake and release by dividing sea urchin eggs. Exp. Cell Res. 1972, 75:105-110.
    • (1972) Exp. Cell Res. , vol.75 , pp. 105-110
    • Clothier, G.1    Timourian, H.2
  • 10
    • 0016163713 scopus 로고
    • Activation of sea-urchin eggs by a calcium ionophore
    • Steinhardt R.A., Epel D. Activation of sea-urchin eggs by a calcium ionophore. Proc. Natl. Acad. Sci. U.S.A. 1974, 71:1915-1919.
    • (1974) Proc. Natl. Acad. Sci. U.S.A. , vol.71 , pp. 1915-1919
    • Steinhardt, R.A.1    Epel, D.2
  • 11
    • 50349104711 scopus 로고
    • On the acid formation, breakdown of cytoplasmic inclusions, and increased viscosity in papcentrotus egg homogenates after the addition of calcium
    • Hutlin T. On the acid formation, breakdown of cytoplasmic inclusions, and increased viscosity in papcentrotus egg homogenates after the addition of calcium. Exp. Cell Res. 1950, 1:272-283.
    • (1950) Exp. Cell Res. , vol.1 , pp. 272-283
    • Hutlin, T.1
  • 12
    • 0014876819 scopus 로고
    • Ca2+ uptake H+ ejection and respiration in sea urchin eggs on fertilization
    • Nakazawa T., Asami K., Shoger R., Fujiwara A., Yasumasu I. Ca2+ uptake H+ ejection and respiration in sea urchin eggs on fertilization. Exp. Cell Res. 1970, 63:143-146.
    • (1970) Exp. Cell Res. , vol.63 , pp. 143-146
    • Nakazawa, T.1    Asami, K.2    Shoger, R.3    Fujiwara, A.4    Yasumasu, I.5
  • 13
    • 0014807816 scopus 로고
    • Contractile responses at the surface of an amphibian egg
    • Gingell D. Contractile responses at the surface of an amphibian egg. J. Embryol. Exp. Morphol. 1970, 23:583-609.
    • (1970) J. Embryol. Exp. Morphol. , vol.23 , pp. 583-609
    • Gingell, D.1
  • 14
    • 0015338250 scopus 로고
    • Intracellular calcium and cell cleavage in early embryos of Xenopus laevis
    • Baker P.F., Warner A.E. Intracellular calcium and cell cleavage in early embryos of Xenopus laevis. J. Cell Biol. 1972, 53:579-581.
    • (1972) J. Cell Biol. , vol.53 , pp. 579-581
    • Baker, P.F.1    Warner, A.E.2
  • 16
    • 0017647298 scopus 로고
    • Intracellular calcium release at fertilization in the sea urchin egg
    • Steinhardt R.A., Zucker R., Schatten G. Intracellular calcium release at fertilization in the sea urchin egg. Dev. Biol. 1977, 58:185-196.
    • (1977) Dev. Biol. , vol.58 , pp. 185-196
    • Steinhardt, R.A.1    Zucker, R.2    Schatten, G.3
  • 17
    • 0017870894 scopus 로고
    • A free calcium wave traverses the activating egg of the Medaka, Oryzias latipes
    • Gilkey J.C., Jaffe L.F., Ridgway E.B., Reynolds G.T. A free calcium wave traverses the activating egg of the Medaka, Oryzias latipes. J. Cell Biol. 1978, 76:448-466.
    • (1978) J. Cell Biol. , vol.76 , pp. 448-466
    • Gilkey, J.C.1    Jaffe, L.F.2    Ridgway, E.B.3    Reynolds, G.T.4
  • 18
    • 0016267925 scopus 로고
    • The activation of sea urchin eggs by the divalent ionophores A23187 and X-537A
    • Chambers E.L., Pressman B.C., Rose B. The activation of sea urchin eggs by the divalent ionophores A23187 and X-537A. Biochem. Biophys. Res. Commun. 1974, 60:126-132.
    • (1974) Biochem. Biophys. Res. Commun. , vol.60 , pp. 126-132
    • Chambers, E.L.1    Pressman, B.C.2    Rose, B.3
  • 19
    • 0016357186 scopus 로고
    • Is calcium ionophore a universal activator for unfertilised eggs?
    • Steinhardt R.A., Epel D., Carroll E.J., Yanagimachi R. Is calcium ionophore a universal activator for unfertilised eggs?. Nature 1974, 252:41-43.
    • (1974) Nature , vol.252 , pp. 41-43
    • Steinhardt, R.A.1    Epel, D.2    Carroll, E.J.3    Yanagimachi, R.4
  • 20
    • 0033566185 scopus 로고    scopus 로고
    • Comparative biology of calcium signaling during fertilization and egg activation in animals
    • Stricker S.A. Comparative biology of calcium signaling during fertilization and egg activation in animals. Dev. Biol. 1999, 211:157-176.
    • (1999) Dev. Biol. , vol.211 , pp. 157-176
    • Stricker, S.A.1
  • 21
    • 33745899901 scopus 로고    scopus 로고
    • Thirty years of calcium signals at fertilization
    • Miyazaki S. Thirty years of calcium signals at fertilization. Semin. Cell Dev. Biol. 2006, 17:233-243.
    • (2006) Semin. Cell Dev. Biol. , vol.17 , pp. 233-243
    • Miyazaki, S.1
  • 22
    • 34848895752 scopus 로고    scopus 로고
    • Ca2+ signaling differentiation during oocyte maturation
    • Machaca K. Ca2+ signaling differentiation during oocyte maturation. J. Cell. Physiol. 2007, 213:331-340.
    • (2007) J. Cell. Physiol. , vol.213 , pp. 331-340
    • Machaca, K.1
  • 23
    • 78649446639 scopus 로고    scopus 로고
    • Mechanisms controlling the remodeling of Ca2+ signaling pathways during Xenopus oocyte maturation in preparation for fertilization
    • Research Signpost, Kerala, India, J. Kubiak, M.A. Ciemerych, L. Richard-Parpaillon (Eds.)
    • Machaca K. Mechanisms controlling the remodeling of Ca2+ signaling pathways during Xenopus oocyte maturation in preparation for fertilization. Cell Cycle and Development in Vertebrates 2000, Research Signpost, Kerala, India. J. Kubiak, M.A. Ciemerych, L. Richard-Parpaillon (Eds.).
    • (2000) Cell Cycle and Development in Vertebrates
    • Machaca, K.1
  • 24
    • 84982335304 scopus 로고
    • Cytological and experimental studies of polyspermy in the newt, Triturus viridescens. I. Normal fertilization
    • Fankhauser G., Moore C. Cytological and experimental studies of polyspermy in the newt, Triturus viridescens. I. Normal fertilization. J. Morphol. 1941, 68:347-385.
    • (1941) J. Morphol. , vol.68 , pp. 347-385
    • Fankhauser, G.1    Moore, C.2
  • 25
    • 65949090031 scopus 로고
    • Recherches sur les oeufs di-et-trispermiques de grenouille
    • Herlant M. Recherches sur les oeufs di-et-trispermiques de grenouille. Arch. Biol. 1911, 26:103-336.
    • (1911) Arch. Biol. , vol.26 , pp. 103-336
    • Herlant, M.1
  • 26
    • 2442533056 scopus 로고    scopus 로고
    • The endogenous calcium-activated Cl channel in Xenopus oocytes: a physiologically and biophysically rich model system
    • Academic Press, San Diego, C.M. Fuller (Ed.)
    • Machaca K., Qu Z., Kuruma A., Hartzell H.C., McCarty N. The endogenous calcium-activated Cl channel in Xenopus oocytes: a physiologically and biophysically rich model system. Calcium Activates Chloride Channels 2001, 3-39. Academic Press, San Diego. C.M. Fuller (Ed.).
    • (2001) Calcium Activates Chloride Channels , pp. 3-39
    • Machaca, K.1    Qu, Z.2    Kuruma, A.3    Hartzell, H.C.4    McCarty, N.5
  • 27
    • 0020807717 scopus 로고
    • Studies of the voltage-dependent polyspermy block using cross-species fertilization of amphibians
    • Jaffe L.A., Cross N.L., Picheral B. Studies of the voltage-dependent polyspermy block using cross-species fertilization of amphibians. Dev. Biol. 1983, 98:319-326.
    • (1983) Dev. Biol. , vol.98 , pp. 319-326
    • Jaffe, L.A.1    Cross, N.L.2    Picheral, B.3
  • 28
    • 0017127374 scopus 로고
    • Fast block to polyspermy in sea urchin eggs is electrically mediated
    • Jaffe L.A. Fast block to polyspermy in sea urchin eggs is electrically mediated. Nature 1976, 261:68-71.
    • (1976) Nature , vol.261 , pp. 68-71
    • Jaffe, L.A.1
  • 29
    • 34547842767 scopus 로고    scopus 로고
    • A comparative analysis of molecular mechanisms for blocking polyspermy: identification of a lectin-ligand binding reaction in mammalian eggs
    • Hedrick J.L. A comparative analysis of molecular mechanisms for blocking polyspermy: identification of a lectin-ligand binding reaction in mammalian eggs. Soc. Reprod. Fertil. Suppl. 2007, 63:409-419.
    • (2007) Soc. Reprod. Fertil. Suppl. , vol.63 , pp. 409-419
    • Hedrick, J.L.1
  • 30
    • 0029868296 scopus 로고    scopus 로고
    • The cortical reaction and development of activation competence in mammalian oocytes
    • Ducibella T. The cortical reaction and development of activation competence in mammalian oocytes. Hum. Reprod. Update 1996, 2:29-42.
    • (1996) Hum. Reprod. Update , vol.2 , pp. 29-42
    • Ducibella, T.1
  • 31
    • 0015076873 scopus 로고
    • Cytoplasmic control of nuclear behavior during meiotic maturation of frog oocytes
    • Masui Y., Markert C.L. Cytoplasmic control of nuclear behavior during meiotic maturation of frog oocytes. J. Exp. Zool. 1971, 177:129-145.
    • (1971) J. Exp. Zool. , vol.177 , pp. 129-145
    • Masui, Y.1    Markert, C.L.2
  • 32
    • 0023753715 scopus 로고
    • The Xenopus cdc2 protein is a component of MPF, a cytoplasmic regulator of mitosis
    • Dunphy W.G., Brizuela L., Beach D., Newport J. The Xenopus cdc2 protein is a component of MPF, a cytoplasmic regulator of mitosis. Cell 1988, 54:423-431.
    • (1988) Cell , vol.54 , pp. 423-431
    • Dunphy, W.G.1    Brizuela, L.2    Beach, D.3    Newport, J.4
  • 33
    • 0025012866 scopus 로고
    • Cyclin is a component of maturation-promoting factor from Xenopus
    • Gautier J., Minshull J., Lohka M., Glotzer M., Hunt T., Maller J.L. Cyclin is a component of maturation-promoting factor from Xenopus. Cell 1990, 60:487-494.
    • (1990) Cell , vol.60 , pp. 487-494
    • Gautier, J.1    Minshull, J.2    Lohka, M.3    Glotzer, M.4    Hunt, T.5    Maller, J.L.6
  • 34
    • 0345054420 scopus 로고
    • Purification of maturation-promoting factor, an intracellular regulator of early mitotic events
    • Lohka M.J., Hayes M.K., Maller J.L. Purification of maturation-promoting factor, an intracellular regulator of early mitotic events. Proc. Natl. Acad. Sci. U.S.A. 1988, 85:3009-3013.
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 3009-3013
    • Lohka, M.J.1    Hayes, M.K.2    Maller, J.L.3
  • 35
    • 0025246110 scopus 로고
    • Universal control mechanism regulating onset of M-phase
    • Nurse P. Universal control mechanism regulating onset of M-phase. Nature 1990, 344:503-508.
    • (1990) Nature , vol.344 , pp. 503-508
    • Nurse, P.1
  • 36
    • 0036284778 scopus 로고    scopus 로고
    • The anaphase-promoting complex: proteolysis in mitosis and beyond
    • Peters J.M. The anaphase-promoting complex: proteolysis in mitosis and beyond. Mol. Cell 2002, 9:931-943.
    • (2002) Mol. Cell , vol.9 , pp. 931-943
    • Peters, J.M.1
  • 37
    • 0037444220 scopus 로고    scopus 로고
    • Under arrest: cytostatic factor (CSF)-mediated metaphase arrest in vertebrate eggs
    • Tunquist B.J., Maller J.L. Under arrest: cytostatic factor (CSF)-mediated metaphase arrest in vertebrate eggs. Genes Dev. 2003, 17:683-710.
    • (2003) Genes Dev. , vol.17 , pp. 683-710
    • Tunquist, B.J.1    Maller, J.L.2
  • 38
    • 13844253522 scopus 로고    scopus 로고
    • Xenopus polo-like kinase Plx1 regulates XErp1, a novel inhibitor of APC/C activity
    • Schmidt A., Duncan P.I., Rauh N.R., et al. Xenopus polo-like kinase Plx1 regulates XErp1, a novel inhibitor of APC/C activity. Genes Dev. 2005, 19:502-513.
    • (2005) Genes Dev. , vol.19 , pp. 502-513
    • Schmidt, A.1    Duncan, P.I.2    Rauh, N.R.3
  • 39
    • 15444373311 scopus 로고    scopus 로고
    • A role for the anaphase-promoting complex inhibitor Emi2/XErp1, a homolog of early mitotic inhibitor 1, in cytostatic factor arrest of Xenopus eggs
    • Tung J.J., Hansen D.V., Ban K.H., et al. A role for the anaphase-promoting complex inhibitor Emi2/XErp1, a homolog of early mitotic inhibitor 1, in cytostatic factor arrest of Xenopus eggs. Proc. Natl. Acad. Sci. U.S.A. 2005, 102:4318-4323.
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 4318-4323
    • Tung, J.J.1    Hansen, D.V.2    Ban, K.H.3
  • 40
    • 23944518069 scopus 로고    scopus 로고
    • Calcium elevation at fertilization coordinates phosphorylation of XErp1/Emi2 by Plx1 and CaMK II to release metaphase arrest by cytostatic factor
    • Liu j, Maller J.L. Calcium elevation at fertilization coordinates phosphorylation of XErp1/Emi2 by Plx1 and CaMK II to release metaphase arrest by cytostatic factor. Curr. Biol. 2005, 15:1458-1468.
    • (2005) Curr. Biol. , vol.15 , pp. 1458-1468
    • Liu j1    Maller, J.L.2
  • 41
    • 31444440363 scopus 로고    scopus 로고
    • CaMKII and polo-like kinase 1 sequentially phosphorylate the cytostatic factor Emi2/XErp1 to trigger its destruction and meiotic exit
    • Hansen D.V., Tung J.J., Jackson P.K. CaMKII and polo-like kinase 1 sequentially phosphorylate the cytostatic factor Emi2/XErp1 to trigger its destruction and meiotic exit. Proc. Natl. Acad. Sci. U.S.A. 2006, 103:608-613.
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 608-613
    • Hansen, D.V.1    Tung, J.J.2    Jackson, P.K.3
  • 42
    • 27144516795 scopus 로고    scopus 로고
    • Calcium triggers exit from meiosis II by targeting the APC/C inhibitor XErp1 for degradation
    • Rauh N.R., Schmidt A., Bormann J., Nigg E.A., Mayer T.U. Calcium triggers exit from meiosis II by targeting the APC/C inhibitor XErp1 for degradation. Nature 2005, 437:1048-1052.
    • (2005) Nature , vol.437 , pp. 1048-1052
    • Rauh, N.R.1    Schmidt, A.2    Bormann, J.3    Nigg, E.A.4    Mayer, T.U.5
  • 43
    • 34548864699 scopus 로고    scopus 로고
    • Calcineurin is required to release Xenopus egg extracts from meiotic M phase
    • Mochida S., Hunt T. Calcineurin is required to release Xenopus egg extracts from meiotic M phase. Nature 2007, 449:336-340.
    • (2007) Nature , vol.449 , pp. 336-340
    • Mochida, S.1    Hunt, T.2
  • 44
    • 34548841712 scopus 로고    scopus 로고
    • Transient activation of calcineurin is essential to initiate embryonic development in Xenopus laevis
    • Nishiyama T., Yoshizaki N., Kishimoto T., Ohsumi K. Transient activation of calcineurin is essential to initiate embryonic development in Xenopus laevis. Nature 2007, 449:341-345.
    • (2007) Nature , vol.449 , pp. 341-345
    • Nishiyama, T.1    Yoshizaki, N.2    Kishimoto, T.3    Ohsumi, K.4
  • 45
    • 0020522663 scopus 로고
    • Ionic changes in the mitotic apparatus at the metaphase/anaphase transition
    • Wolniak S.M., Hepler P.K., Jackson W.T. Ionic changes in the mitotic apparatus at the metaphase/anaphase transition. J. Cell Biol. 1983, 96:598-605.
    • (1983) J. Cell Biol. , vol.96 , pp. 598-605
    • Wolniak, S.M.1    Hepler, P.K.2    Jackson, W.T.3
  • 47
    • 0021840109 scopus 로고
    • Changes of free calcium levels with stages of the cell division cycle
    • Poenie M., Alderton J.M., Tsien R.Y., Steinhardt R.A. Changes of free calcium levels with stages of the cell division cycle. Nature 1985, 315:147-149.
    • (1985) Nature , vol.315 , pp. 147-149
    • Poenie, M.1    Alderton, J.M.2    Tsien, R.Y.3    Steinhardt, R.A.4
  • 48
    • 0022468347 scopus 로고
    • Calcium rises abruptly and briefly throughout the cell at the onset of anaphase
    • Poenie M., Alderton J., Steinhardt R.A., Tsien R.Y. Calcium rises abruptly and briefly throughout the cell at the onset of anaphase. Science 1986, 233:886-889.
    • (1986) Science , vol.233 , pp. 886-889
    • Poenie, M.1    Alderton, J.2    Steinhardt, R.A.3    Tsien, R.Y.4
  • 49
    • 0024076970 scopus 로고
    • Long-lasting and rapid calcium changes during mitosis
    • Ratan R.R., Maxfield F.R., Shelanski M.L. Long-lasting and rapid calcium changes during mitosis. J. Cell Biol. 1988, 107:993-999.
    • (1988) J. Cell Biol. , vol.107 , pp. 993-999
    • Ratan, R.R.1    Maxfield, F.R.2    Shelanski, M.L.3
  • 50
    • 0023882072 scopus 로고
    • Intracellular free calcium rise triggers nuclear envelope breakdown in the sea urchin embryo
    • Steinhardt R.A., Alderton J.M. Intracellular free calcium rise triggers nuclear envelope breakdown in the sea urchin embryo. Nature 1988, 332:364-366.
    • (1988) Nature , vol.332 , pp. 364-366
    • Steinhardt, R.A.1    Alderton, J.M.2
  • 51
    • 0024295662 scopus 로고
    • Translational control of InsP3-induced chromatin condensation during the early cell cycles of sea urchin embryos
    • Twigg J., Patel R., Whitaker M. Translational control of InsP3-induced chromatin condensation during the early cell cycles of sea urchin embryos. Nature 1988, 332:366-369.
    • (1988) Nature , vol.332 , pp. 366-369
    • Twigg, J.1    Patel, R.2    Whitaker, M.3
  • 52
    • 0025194832 scopus 로고
    • Active involvement of Ca2+ in mitotic progression of Swiss 3T3 fibroblasts
    • Kao J.P., Alderton J.M., Tsien R.Y., Steinhardt R.A. Active involvement of Ca2+ in mitotic progression of Swiss 3T3 fibroblasts. J. Cell Biol. 1990, 111:183-196.
    • (1990) J. Cell Biol. , vol.111 , pp. 183-196
    • Kao, J.P.1    Alderton, J.M.2    Tsien, R.Y.3    Steinhardt, R.A.4
  • 53
    • 0025514416 scopus 로고
    • Multifunctional Ca2+/calmodulin-dependent protein kinase is necessary for nuclear envelope breakdown
    • Baitinger C., Alderton J., Poenie M., Schulman H., Steinhardt R.A. Multifunctional Ca2+/calmodulin-dependent protein kinase is necessary for nuclear envelope breakdown. J. Cell Biol. 1990, 111:1763-1773.
    • (1990) J. Cell Biol. , vol.111 , pp. 1763-1773
    • Baitinger, C.1    Alderton, J.2    Poenie, M.3    Schulman, H.4    Steinhardt, R.A.5
  • 54
    • 0026636047 scopus 로고
    • Meiosis, egg activation, and nuclear envelope breakdown are differentially reliant on Ca2+, whereas germinal vesicle breakdown is Ca2+ independent in the mouse oocyte
    • Tombes R.M., Simerly C., Borisy G.G., Schatten G. Meiosis, egg activation, and nuclear envelope breakdown are differentially reliant on Ca2+, whereas germinal vesicle breakdown is Ca2+ independent in the mouse oocyte. J. Cell Biol. 1992, 117:799-811.
    • (1992) J. Cell Biol. , vol.117 , pp. 799-811
    • Tombes, R.M.1    Simerly, C.2    Borisy, G.G.3    Schatten, G.4
  • 55
    • 2442580771 scopus 로고    scopus 로고
    • Ca2+cyt negatively regulates the initiation of oocyte maturation
    • Sun L., Machaca K. Ca2+cyt negatively regulates the initiation of oocyte maturation. J. Cell Biol. 2004, 165:63-75.
    • (2004) J. Cell Biol. , vol.165 , pp. 63-75
    • Sun, L.1    Machaca, K.2
  • 56
    • 0037229320 scopus 로고    scopus 로고
    • Nuclear envelope dynamics in oocytes: from germinal vesicle breakdown to mitosis
    • Lenart P., Ellenberg J. Nuclear envelope dynamics in oocytes: from germinal vesicle breakdown to mitosis. Curr. Opin. Cell Biol. 2003, 15:88-95.
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 88-95
    • Lenart, P.1    Ellenberg, J.2
  • 57
    • 0027172088 scopus 로고
    • The role of calcium in mammalian oocyte maturation and egg activation
    • Homa S.T., Carroll J., Swann K. The role of calcium in mammalian oocyte maturation and egg activation. Hum. Reprod. 1993, 8:1274-1281.
    • (1993) Hum. Reprod. , vol.8 , pp. 1274-1281
    • Homa, S.T.1    Carroll, J.2    Swann, K.3
  • 58
    • 0028299969 scopus 로고
    • Cell-cycle calcium transients driven by cyclic changes in inositol trisphosphate levels
    • Ciapa B., Pesando D., Wilding M., Whitaker M. Cell-cycle calcium transients driven by cyclic changes in inositol trisphosphate levels. Nature 1994, 368:875-878.
    • (1994) Nature , vol.368 , pp. 875-878
    • Ciapa, B.1    Pesando, D.2    Wilding, M.3    Whitaker, M.4
  • 59
    • 0025018367 scopus 로고
    • 1-Methyladenine can consistently induce a fura-detectable transient calcium increase which is neither necessary nor sufficient for maturation in oocytes of the starfish Asterina miniata
    • Witchel H.J., Steinhardt R.A. 1-Methyladenine can consistently induce a fura-detectable transient calcium increase which is neither necessary nor sufficient for maturation in oocytes of the starfish Asterina miniata. Dev. Biol. 1990, 141:393-398.
    • (1990) Dev. Biol. , vol.141 , pp. 393-398
    • Witchel, H.J.1    Steinhardt, R.A.2
  • 60
    • 0020062918 scopus 로고
    • Calmodulin and the cell cycle: involvement in regulation of cell-cycle progression
    • Chafouleas J.G., Bolton W.E., Hidaka H., Boyd A.E., Means A.R. Calmodulin and the cell cycle: involvement in regulation of cell-cycle progression. Cell 1982, 28:41-50.
    • (1982) Cell , vol.28 , pp. 41-50
    • Chafouleas, J.G.1    Bolton, W.E.2    Hidaka, H.3    Boyd, A.E.4    Means, A.R.5
  • 61
    • 0021328588 scopus 로고
    • Changes in calmodulin and its mRNA accompany reentry of quiescent (G0) cells into the cell cycle
    • Chafouleas J.G., Lagace L., Bolton W.E., Boyd A.E., Means A.R. Changes in calmodulin and its mRNA accompany reentry of quiescent (G0) cells into the cell cycle. Cell 1984, 36:73-81.
    • (1984) Cell , vol.36 , pp. 73-81
    • Chafouleas, J.G.1    Lagace, L.2    Bolton, W.E.3    Boyd, A.E.4    Means, A.R.5
  • 62
    • 0024440855 scopus 로고
    • Calmodulin is required for cell-cycle progression during G1 and mitosis
    • Rasmussen C.D., Means A.R. Calmodulin is required for cell-cycle progression during G1 and mitosis. EMBO J. 1989, 8:73-82.
    • (1989) EMBO J. , vol.8 , pp. 73-82
    • Rasmussen, C.D.1    Means, A.R.2
  • 63
    • 0026551634 scopus 로고
    • Cooperative regulation of cell proliferation by calcium and calmodulin in Aspergillus nidulans
    • Lu K.P., Rasmussen C.D., May G.S., Means A.R. Cooperative regulation of cell proliferation by calcium and calmodulin in Aspergillus nidulans. Mol. Endocrinol. 1992, 6:365-374.
    • (1992) Mol. Endocrinol. , vol.6 , pp. 365-374
    • Lu, K.P.1    Rasmussen, C.D.2    May, G.S.3    Means, A.R.4
  • 64
    • 0027289307 scopus 로고
    • Essential roles for calcium and calmodulin in G2/M progression in Aspergillus nidulans
    • Lu K.P., Osmani S.A., Osmani A.H., Means A.R. Essential roles for calcium and calmodulin in G2/M progression in Aspergillus nidulans. J. Cell Biol. 1993, 121:621-630.
    • (1993) J. Cell Biol. , vol.121 , pp. 621-630
    • Lu, K.P.1    Osmani, S.A.2    Osmani, A.H.3    Means, A.R.4
  • 65
    • 0026629519 scopus 로고
    • A temperature-sensitive calmodulin mutant loses viability during mitosis
    • Davis T.N. A temperature-sensitive calmodulin mutant loses viability during mitosis. J. Cell Biol. 1992, 118:607-617.
    • (1992) J. Cell Biol. , vol.118 , pp. 607-617
    • Davis, T.N.1
  • 66
    • 0030809387 scopus 로고    scopus 로고
    • Calmodulin localizes to the spindle pole body of Schizosaccharomyces pombe and performs an essential function in chromosome segregation
    • Moser M.J., Flory M.R., Davis T.N. Calmodulin localizes to the spindle pole body of Schizosaccharomyces pombe and performs an essential function in chromosome segregation. J. Cell Sci. 1997, 110(Pt 15):1805-1812.
    • (1997) J. Cell Sci. , vol.110 , Issue.PART 15 , pp. 1805-1812
    • Moser, M.J.1    Flory, M.R.2    Davis, T.N.3
  • 67
    • 0024503203 scopus 로고
    • A galactose-dependent cmd1 mutant of Saccharomyces cerevisiae: involvement of calmodulin in nuclear division
    • Ohya Y., Anraku Y. A galactose-dependent cmd1 mutant of Saccharomyces cerevisiae: involvement of calmodulin in nuclear division. Curr. Genet. 1989, 15:113-120.
    • (1989) Curr. Genet. , vol.15 , pp. 113-120
    • Ohya, Y.1    Anraku, Y.2
  • 68
    • 0028266837 scopus 로고
    • Diverse essential functions revealed by complementing yeast calmodulin mutants
    • Ohya Y., Botstein D. Diverse essential functions revealed by complementing yeast calmodulin mutants. Science 1994, 263:963-966.
    • (1994) Science , vol.263 , pp. 963-966
    • Ohya, Y.1    Botstein, D.2
  • 69
    • 0029823512 scopus 로고    scopus 로고
    • Ca(2+)/calmodulin-dependent kinase is essential for both growth and nuclear division in Aspergillus nidulans
    • Dayton J.S., Means A.R. Ca(2+)/calmodulin-dependent kinase is essential for both growth and nuclear division in Aspergillus nidulans. Mol. Biol. Cell 1996, 7:1511-1519.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 1511-1519
    • Dayton, J.S.1    Means, A.R.2
  • 70
    • 0347949547 scopus 로고    scopus 로고
    • Regulation of cell cycle progression by calcium/calmodulin-dependent pathways
    • Kahl C.R., Means A. Regulation of cell cycle progression by calcium/calmodulin-dependent pathways. Endocr. Rev. 2003, 24:719-736.
    • (2003) Endocr. Rev. , vol.24 , pp. 719-736
    • Kahl, C.R.1    Means, A.2
  • 71
    • 0026569334 scopus 로고
    • Expression of a constitutive form of calcium/calmodulin dependent protein kinase II leads to arrest of the cell cycle in G2
    • Planas-Silva M.D., Means A.R. Expression of a constitutive form of calcium/calmodulin dependent protein kinase II leads to arrest of the cell cycle in G2. EMBO J. 1992, 11:507-517.
    • (1992) EMBO J. , vol.11 , pp. 507-517
    • Planas-Silva, M.D.1    Means, A.R.2
  • 72
    • 0034937572 scopus 로고    scopus 로고
    • Calmodulin protects cells from death under normal growth conditions and mitogenic starvation but plays a mediating role in cell death upon B-cell receptor stimulation
    • Schmalzigaug R., Ye Q., Berchtold M.W. Calmodulin protects cells from death under normal growth conditions and mitogenic starvation but plays a mediating role in cell death upon B-cell receptor stimulation. Immunology 2001, 103:332-342.
    • (2001) Immunology , vol.103 , pp. 332-342
    • Schmalzigaug, R.1    Ye, Q.2    Berchtold, M.W.3
  • 73
    • 0026450868 scopus 로고
    • Calmodulin-specific monoclonal antibodies inhibit DNA replication in mammalian cells
    • Reddy G.P., Reed W.C., Sheehan E., Sacks D.B. Calmodulin-specific monoclonal antibodies inhibit DNA replication in mammalian cells. Biochemistry 1992, 31:10426-10430.
    • (1992) Biochemistry , vol.31 , pp. 10426-10430
    • Reddy, G.P.1    Reed, W.C.2    Sheehan, E.3    Sacks, D.B.4
  • 74
    • 0343374101 scopus 로고
    • N-(6-aminohexyl)-5-chloro-1-naphthalenesulfonamide, a calmodulin antagonist, inhibits cell proliferation
    • Hidaka H., Sasaki Y., Tanaka T., et al. N-(6-aminohexyl)-5-chloro-1-naphthalenesulfonamide, a calmodulin antagonist, inhibits cell proliferation. Proc. Natl. Acad. Sci. U.S.A. 1981, 78:4354-4357.
    • (1981) Proc. Natl. Acad. Sci. U.S.A. , vol.78 , pp. 4354-4357
    • Hidaka, H.1    Sasaki, Y.2    Tanaka, T.3
  • 75
    • 0027398566 scopus 로고
    • Ca(2+)-dependent stimulation of retinoblastoma gene product phosphorylation and p34cdc2 kinase activation in serum-stimulated human fibroblasts
    • Takuwa N., Zhou W., Kumada M., Takuwa Y. Ca(2+)-dependent stimulation of retinoblastoma gene product phosphorylation and p34cdc2 kinase activation in serum-stimulated human fibroblasts. J. Biol. Chem. 1993, 268:138-145.
    • (1993) J. Biol. Chem. , vol.268 , pp. 138-145
    • Takuwa, N.1    Zhou, W.2    Kumada, M.3    Takuwa, Y.4
  • 76
    • 0028091346 scopus 로고
    • The ins and outs of Rb: coupling gene expression to the cell cycle clock
    • Sherr C.J. The ins and outs of Rb: coupling gene expression to the cell cycle clock. Trends Cell Biol. 1994, 4:15-18.
    • (1994) Trends Cell Biol. , vol.4 , pp. 15-18
    • Sherr, C.J.1
  • 77
    • 0037113877 scopus 로고    scopus 로고
    • Cyclosporine inhibits growth through the activating transcription factor/cAMP-responsive element-binding protein binding site in the cyclin D1 promoter
    • Schneider G., Oswald F., Wahl C., Greten F.R., Adler G., Schmid R.M. Cyclosporine inhibits growth through the activating transcription factor/cAMP-responsive element-binding protein binding site in the cyclin D1 promoter. J. Biol. Chem. 2002, 277:43599-43607.
    • (2002) J. Biol. Chem. , vol.277 , pp. 43599-43607
    • Schneider, G.1    Oswald, F.2    Wahl, C.3    Greten, F.R.4    Adler, G.5    Schmid, R.M.6
  • 78
    • 0033545299 scopus 로고    scopus 로고
    • Cyclosporine induces cancer progression by a cell-autonomous mechanism
    • Hojo M., Morimoto T., Maluccio M., et al. Cyclosporine induces cancer progression by a cell-autonomous mechanism. Nature 1999, 397:530-534.
    • (1999) Nature , vol.397 , pp. 530-534
    • Hojo, M.1    Morimoto, T.2    Maluccio, M.3
  • 79
    • 0037154992 scopus 로고    scopus 로고
    • Role of cyclic nucleotide signaling in oocyte maturation
    • Conti M., Andersen C.B., Richard F., et al. Role of cyclic nucleotide signaling in oocyte maturation. Mol. Cell. Endocrinol. 2002, 187:153-159.
    • (2002) Mol. Cell. Endocrinol. , vol.187 , pp. 153-159
    • Conti, M.1    Andersen, C.B.2    Richard, F.3
  • 80
    • 0029189631 scopus 로고
    • Calcium signalling during mammalian fertilization
    • Miyazaki S. Calcium signalling during mammalian fertilization. Ciba Found. Symp. 1995, 188:235-251.
    • (1995) Ciba Found. Symp. , vol.188 , pp. 235-251
    • Miyazaki, S.1
  • 81
    • 0024840220 scopus 로고
    • The induction of oocyte maturation: transmembrane signaling events and regulation of the cell cycle
    • Smith L.D. The induction of oocyte maturation: transmembrane signaling events and regulation of the cell cycle. Development 1989, 107:685-699.
    • (1989) Development , vol.107 , pp. 685-699
    • Smith, L.D.1
  • 82
    • 0035319804 scopus 로고    scopus 로고
    • To err (meiotically) is human: the genesis of human aneuploidy
    • Hassold T., Hunt P. To err (meiotically) is human: the genesis of human aneuploidy. Nat. Rev. Genet. 2001, 2:280-291.
    • (2001) Nat. Rev. Genet. , vol.2 , pp. 280-291
    • Hassold, T.1    Hunt, P.2
  • 85
    • 84942761580 scopus 로고    scopus 로고
    • Regulation of mammalian oocyte maturation
    • Elsevier Press, San Diego, E.Y. Adashi, P.C.K. Leung (Eds.)
    • Eppig J.J., Viveiros M.M., Marin-Bivens C., De La Fuente R. Regulation of mammalian oocyte maturation. The Ovary 2004, 113-129. Elsevier Press, San Diego. E.Y. Adashi, P.C.K. Leung (Eds.).
    • (2004) The Ovary , pp. 113-129
    • Eppig, J.J.1    Viveiros, M.M.2    Marin-Bivens, C.3    De La Fuente, R.4
  • 86
    • 0018418804 scopus 로고
    • Early effect of progesterone on levels of cyclic adenosine 3':5'-monophosphate in Xenopus oocytes
    • Maller J.L., Butcher F.R., Krebs E.G. Early effect of progesterone on levels of cyclic adenosine 3':5'-monophosphate in Xenopus oocytes. J. Biol. Chem. 1979, 254:579-582.
    • (1979) J. Biol. Chem. , vol.254 , pp. 579-582
    • Maller, J.L.1    Butcher, F.R.2    Krebs, E.G.3
  • 87
    • 33847235683 scopus 로고    scopus 로고
    • The role of Xenopus membrane progesterone receptor beta in mediating the effect of progesterone on oocyte maturation
    • Josefsberg Ben-Yehoshua L., Lewellyn A.L., Thomas P., Maller J.L. The role of Xenopus membrane progesterone receptor beta in mediating the effect of progesterone on oocyte maturation. Mol. Endocrinol. 2007, 21:664-673.
    • (2007) Mol. Endocrinol. , vol.21 , pp. 664-673
    • Josefsberg Ben-Yehoshua, L.1    Lewellyn, A.L.2    Thomas, P.3    Maller, J.L.4
  • 88
    • 0033724683 scopus 로고    scopus 로고
    • Regulation of the meiotic cell cycle in oocytes
    • Nebreda A.R., Ferby I. Regulation of the meiotic cell cycle in oocytes. Curr. Opin. Cell Biol. 2000, 12:666-675.
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 666-675
    • Nebreda, A.R.1    Ferby, I.2
  • 89
    • 13244256828 scopus 로고    scopus 로고
    • Regulation of Cdc25C activity during the meiotic G2/M transition
    • Perdiguero E., Nebreda A.R. Regulation of Cdc25C activity during the meiotic G2/M transition. Cell Cycle 2004, 3:733-737.
    • (2004) Cell Cycle , vol.3 , pp. 733-737
    • Perdiguero, E.1    Nebreda, A.R.2
  • 90
    • 0028783413 scopus 로고
    • Myt1: a membrane-associated inhibitory kinase that phosphorylates Cdc2 on both threonine-14 and tyrosine-15
    • Mueller P.R., Coleman T.R., Kumagai A., Dunphy W.G. Myt1: a membrane-associated inhibitory kinase that phosphorylates Cdc2 on both threonine-14 and tyrosine-15. Science 1995, 270:86-90.
    • (1995) Science , vol.270 , pp. 86-90
    • Mueller, P.R.1    Coleman, T.R.2    Kumagai, A.3    Dunphy, W.G.4
  • 91
    • 0025980359 scopus 로고
    • The cdc25 protein controls tyrosine dephosphorylation of the cdc2 protein in a cell-free system
    • Kumagai A., Dunphy W.G. The cdc25 protein controls tyrosine dephosphorylation of the cdc2 protein in a cell-free system. Cell 1991, 64:903-914.
    • (1991) Cell , vol.64 , pp. 903-914
    • Kumagai, A.1    Dunphy, W.G.2
  • 92
    • 0031470835 scopus 로고    scopus 로고
    • Checkpoint pathways come of age
    • Nurse P. Checkpoint pathways come of age. Cell 1997, 91:865-867.
    • (1997) Cell , vol.91 , pp. 865-867
    • Nurse, P.1
  • 93
    • 4344718628 scopus 로고    scopus 로고
    • Cdc25 phosphatases and cancer
    • Kristjansdottir K., Rudolph J. Cdc25 phosphatases and cancer. Chem. Biol. 2004, 11:1043-1051.
    • (2004) Chem. Biol. , vol.11 , pp. 1043-1051
    • Kristjansdottir, K.1    Rudolph, J.2
  • 94
    • 0016548052 scopus 로고
    • Initiation of meiotic maturation in Xenopus laevis oocytes by the combination of divalent cations and ionophore A23187
    • Wasserman W.J., Masui Y. Initiation of meiotic maturation in Xenopus laevis oocytes by the combination of divalent cations and ionophore A23187. J. Exp. Zool. 1975, 193:369-375.
    • (1975) J. Exp. Zool. , vol.193 , pp. 369-375
    • Wasserman, W.J.1    Masui, Y.2
  • 95
    • 0017002589 scopus 로고
    • Electrophoretic introduction of calcium into the cortex of Xenopus laevis oocytes triggers meiosis reinitiation
    • Moreau M., Doree M., Guerrier P. Electrophoretic introduction of calcium into the cortex of Xenopus laevis oocytes triggers meiosis reinitiation. J. Exp. Zool. 1976, 197:443-449.
    • (1976) J. Exp. Zool. , vol.197 , pp. 443-449
    • Moreau, M.1    Doree, M.2    Guerrier, P.3
  • 96
    • 0017672773 scopus 로고
    • Calcium, potassium, and sodium exchange by full-grown and maturing Xenopus laevis oocytes
    • O'Connor C.M., Robinson K.R., Smith L.D. Calcium, potassium, and sodium exchange by full-grown and maturing Xenopus laevis oocytes. Dev. Biol. 1977, 61:28-40.
    • (1977) Dev. Biol. , vol.61 , pp. 28-40
    • O'Connor, C.M.1    Robinson, K.R.2    Smith, L.D.3
  • 98
    • 0019307714 scopus 로고
    • Free calcium changes associated with hormone action in amphibian oocytes
    • Moreau M., Vilain J.P., Guerrier P. Free calcium changes associated with hormone action in amphibian oocytes. Dev. Biol. 1980, 78:201-214.
    • (1980) Dev. Biol. , vol.78 , pp. 201-214
    • Moreau, M.1    Vilain, J.P.2    Guerrier, P.3
  • 99
    • 0021871150 scopus 로고
    • Maturation of Xenopus oocytes is not accompanied by electrode-detectable calcium changes
    • Robinson K.R. Maturation of Xenopus oocytes is not accompanied by electrode-detectable calcium changes. Dev. Biol. 1985, 109:504-508.
    • (1985) Dev. Biol. , vol.109 , pp. 504-508
    • Robinson, K.R.1
  • 100
    • 0023191464 scopus 로고
    • A rise in cytosolic calcium is not necessary for maturation of Xenopus laevis oocytes
    • Cork R.J., Cicirelli M.F., Robinson K.R. A rise in cytosolic calcium is not necessary for maturation of Xenopus laevis oocytes. Dev. Biol. 1987, 121:41-47.
    • (1987) Dev. Biol. , vol.121 , pp. 41-47
    • Cork, R.J.1    Cicirelli, M.F.2    Robinson, K.R.3
  • 101
    • 0021878537 scopus 로고
    • Inositol 1,4,5-trisphosphate microinjection triggers activation, but not meiotic maturation in amphibian and starfish oocytes
    • Picard A., Giraud F., Le Bouffant F., Sladeczek F., Le Peuch C., Doree M. Inositol 1,4,5-trisphosphate microinjection triggers activation, but not meiotic maturation in amphibian and starfish oocytes. FEBS Lett. 1985, 182:446-450.
    • (1985) FEBS Lett. , vol.182 , pp. 446-450
    • Picard, A.1    Giraud, F.2    Le Bouffant, F.3    Sladeczek, F.4    Le Peuch, C.5    Doree, M.6
  • 102
    • 0029845146 scopus 로고    scopus 로고
    • The role of Ca2+ in progesterone-induced germinal vesicle breakdown of Xenopus laevis oocytes: the synergic effects of microtubule depolymerization and Ca2+
    • Duesbery N.S., Masui Y. The role of Ca2+ in progesterone-induced germinal vesicle breakdown of Xenopus laevis oocytes: the synergic effects of microtubule depolymerization and Ca2+. Dev. Genes Evol. 1996, 206:110-124.
    • (1996) Dev. Genes Evol. , vol.206 , pp. 110-124
    • Duesbery, N.S.1    Masui, Y.2
  • 104
    • 0019972712 scopus 로고
    • Calcium homeostasis in intact lymphocytes: cytoplasmic free calcium monitored with a new, intracellularly trapped fluorescent indicator
    • Tsien R.Y., Pozzan T., Rink T.J. Calcium homeostasis in intact lymphocytes: cytoplasmic free calcium monitored with a new, intracellularly trapped fluorescent indicator. J. Cell Biol. 1982, 94:325-334.
    • (1982) J. Cell Biol. , vol.94 , pp. 325-334
    • Tsien, R.Y.1    Pozzan, T.2    Rink, T.J.3
  • 105
    • 0019333905 scopus 로고
    • New calcium indicators and buffers with high selectivity against magnesium and protons: design, synthesis, and properties of prototype structures
    • Tsien R.Y. New calcium indicators and buffers with high selectivity against magnesium and protons: design, synthesis, and properties of prototype structures. Biochemistry 1980, 19:2396-2404.
    • (1980) Biochemistry , vol.19 , pp. 2396-2404
    • Tsien, R.Y.1
  • 106
  • 108
    • 0035064074 scopus 로고    scopus 로고
    • Calcium signaling mechanisms in T lymphocytes
    • Lewis R.S. Calcium signaling mechanisms in T lymphocytes. Annu. Rev. Immunol. 2001, 19:497-521.
    • (2001) Annu. Rev. Immunol. , vol.19 , pp. 497-521
    • Lewis, R.S.1
  • 109
    • 0025893168 scopus 로고
    • Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes
    • Liu j, Farmer J.D., Lane W.S., Friedman J., Weissman I., Schreiber S.L. Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes. Cell 1991, 66:807-815.
    • (1991) Cell , vol.66 , pp. 807-815
    • Liu j1    Farmer, J.D.2    Lane, W.S.3    Friedman, J.4    Weissman, I.5    Schreiber, S.L.6
  • 110
    • 0026643141 scopus 로고
    • Identification of calcineurin as a key signalling enzyme in T-lymphocyte activation
    • Clipstone N.A., Crabtree G.R. Identification of calcineurin as a key signalling enzyme in T-lymphocyte activation. Nature 1992, 357:695-697.
    • (1992) Nature , vol.357 , pp. 695-697
    • Clipstone, N.A.1    Crabtree, G.R.2
  • 111
    • 0032577483 scopus 로고    scopus 로고
    • Regulation of the calmodulin-stimulated protein phosphatase, calcineurin
    • Klee C.B., Ren H., Wang X. Regulation of the calmodulin-stimulated protein phosphatase, calcineurin. J. Biol. Chem. 1998, 273:13367-13370.
    • (1998) J. Biol. Chem. , vol.273 , pp. 13367-13370
    • Klee, C.B.1    Ren, H.2    Wang, X.3
  • 112
    • 0028222312 scopus 로고
    • Dual calcium ion regulation of calcineurin by calmodulin and calcineurin B
    • Stemmer P.M., Klee C.B. Dual calcium ion regulation of calcineurin by calmodulin and calcineurin B. Biochemistry 1994, 33:6859-6866.
    • (1994) Biochemistry , vol.33 , pp. 6859-6866
    • Stemmer, P.M.1    Klee, C.B.2
  • 113
    • 0032580202 scopus 로고    scopus 로고
    • Calcium oscillations increase the efficiency and specificity of gene expression
    • Dolmetsch R.E., Xu K., Lewis R.S. Calcium oscillations increase the efficiency and specificity of gene expression. Nature 1998, 392:933-936.
    • (1998) Nature , vol.392 , pp. 933-936
    • Dolmetsch, R.E.1    Xu, K.2    Lewis, R.S.3
  • 114
    • 0030973579 scopus 로고    scopus 로고
    • Transcription factors of the NFAT family: regulation and function
    • Rao A., Luo C., Hogan P.G. Transcription factors of the NFAT family: regulation and function. Annu. Rev. Immunol. 1997, 15:707-747.
    • (1997) Annu. Rev. Immunol. , vol.15 , pp. 707-747
    • Rao, A.1    Luo, C.2    Hogan, P.G.3
  • 115
    • 45449093954 scopus 로고    scopus 로고
    • Calcium signaling in lymphocytes
    • Oh-hora M., Rao A. Calcium signaling in lymphocytes. Curr. Opin. Immunol. 2008, 20:250-258.
    • (2008) Curr. Opin. Immunol. , vol.20 , pp. 250-258
    • Oh-hora, M.1    Rao, A.2
  • 116
    • 33646576875 scopus 로고    scopus 로고
    • A mutation in Orai1 causes immune deficiency by abrogating CRAC channel function
    • Feske S., Gwack Y., Prakriya M., et al. A mutation in Orai1 causes immune deficiency by abrogating CRAC channel function. Nature 2006, 441:179-185.
    • (2006) Nature , vol.441 , pp. 179-185
    • Feske, S.1    Gwack, Y.2    Prakriya, M.3
  • 117
    • 24344476722 scopus 로고    scopus 로고
    • A severe defect in CRAC Ca2+ channel activation and altered K+ channel gating in T cells from immunodeficient patients
    • Feske S., Prakriya M., Rao A., Lewis R.S. A severe defect in CRAC Ca2+ channel activation and altered K+ channel gating in T cells from immunodeficient patients. J. Exp. Med. 2005, 202:651-662.
    • (2005) J. Exp. Med. , vol.202 , pp. 651-662
    • Feske, S.1    Prakriya, M.2    Rao, A.3    Lewis, R.S.4
  • 118
    • 65649088588 scopus 로고    scopus 로고
    • STIM1 mutation associated with a syndrome of immunodeficiency and autoimmunity
    • Picard C., McCarl C.A., Papolos A., et al. STIM1 mutation associated with a syndrome of immunodeficiency and autoimmunity. N. Engl. J. Med. 2009, 360:1971-1980.
    • (2009) N. Engl. J. Med. , vol.360 , pp. 1971-1980
    • Picard, C.1    McCarl, C.A.2    Papolos, A.3
  • 119
    • 0027336649 scopus 로고
    • Mitogen-regulated Ca2+ current of T lymphocytes is activated by depletion of intracellular Ca2+ stores
    • Zweifach A., Lewis R.S. Mitogen-regulated Ca2+ current of T lymphocytes is activated by depletion of intracellular Ca2+ stores. Proc. Natl. Acad. Sci. U.S.A. 1993, 90:6295-6299.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 6295-6299
    • Zweifach, A.1    Lewis, R.S.2
  • 120
    • 0026594980 scopus 로고
    • Depletion of intracellular calcium stores activates a calcium current in mast cells
    • Hoth M., Penner R. Depletion of intracellular calcium stores activates a calcium current in mast cells. Nature 1992, 355:353-356.
    • (1992) Nature , vol.355 , pp. 353-356
    • Hoth, M.1    Penner, R.2
  • 121
    • 0022575011 scopus 로고
    • A model for receptor-regulated calcium entry
    • Putney J.W. A model for receptor-regulated calcium entry. Cell Calcium 1986, 7:1-12.
    • (1986) Cell Calcium , vol.7 , pp. 1-12
    • Putney, J.W.1
  • 122
    • 15544368216 scopus 로고    scopus 로고
    • Store-operated calcium channels
    • Parekh A.B., Putney J.W. Store-operated calcium channels. Physiol. Rev. 2005, 85:757-810.
    • (2005) Physiol. Rev. , vol.85 , pp. 757-810
    • Parekh, A.B.1    Putney, J.W.2
  • 123
    • 67650382292 scopus 로고    scopus 로고
    • Checking your SOCCs and feet: the molecular mechanisms of Ca2+ entry in skeletal muscle
    • Dirksen R.T. Checking your SOCCs and feet: the molecular mechanisms of Ca2+ entry in skeletal muscle. J. Physiol. 2009, 587:3139-3147.
    • (2009) J. Physiol. , vol.587 , pp. 3139-3147
    • Dirksen, R.T.1
  • 124
    • 21844432686 scopus 로고    scopus 로고
    • STIM is a Ca2+ sensor essential for Ca2+-store-depletion-triggered Ca2+ influx
    • Liou J., Kim M.L., Heo W.D., et al. STIM is a Ca2+ sensor essential for Ca2+-store-depletion-triggered Ca2+ influx. Curr. Biol. 2005, 15:1235-1241.
    • (2005) Curr. Biol. , vol.15 , pp. 1235-1241
    • Liou, J.1    Kim, M.L.2    Heo, W.D.3
  • 125
    • 21044439334 scopus 로고    scopus 로고
    • STIM1, an essential and conserved component of store-operated Ca2+ channel function
    • Roos J., DiGregorio P.J., Yeromin A.V., et al. STIM1, an essential and conserved component of store-operated Ca2+ channel function. J. Cell Biol. 2005, 169:435-445.
    • (2005) J. Cell Biol. , vol.169 , pp. 435-445
    • Roos, J.1    DiGregorio, P.J.2    Yeromin, A.V.3
  • 126
    • 33744479684 scopus 로고    scopus 로고
    • CRACM1 is a plasma membrane protein essential for store-operated Ca2+ entry
    • Vig M., Peinelt C., Beck A., et al. CRACM1 is a plasma membrane protein essential for store-operated Ca2+ entry. Science 2006, 312:1220-1223.
    • (2006) Science , vol.312 , pp. 1220-1223
    • Vig, M.1    Peinelt, C.2    Beck, A.3
  • 127
    • 33745139810 scopus 로고    scopus 로고
    • Genome-wide RNAi screen of Ca(2+) influx identifies genes that regulate Ca(2+) release-activated Ca(2+) channel activity
    • Zhang S.L., Yeromin A.V., Zhang X.H., et al. Genome-wide RNAi screen of Ca(2+) influx identifies genes that regulate Ca(2+) release-activated Ca(2+) channel activity. Proc. Natl. Acad. Sci. U.S.A. 2006, 103:9357-9362.
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 9357-9362
    • Zhang, S.L.1    Yeromin, A.V.2    Zhang, X.H.3
  • 128
    • 33745759762 scopus 로고    scopus 로고
    • Amplification of CRAC current by STIM1 and CRACM1 (Orai1)
    • Peinelt C., Vig M., Koomoa D.L., et al. Amplification of CRAC current by STIM1 and CRACM1 (Orai1). Nat. Cell Biol. 2006, 8:771-773.
    • (2006) Nat. Cell Biol. , vol.8 , pp. 771-773
    • Peinelt, C.1    Vig, M.2    Koomoa, D.L.3
  • 130
    • 77950377028 scopus 로고    scopus 로고
    • Molecular basis of calcium signaling in lymphocytes: STIM and ORAI
    • Hogan P.G., Lewis R.S., Rao A. Molecular basis of calcium signaling in lymphocytes: STIM and ORAI. Annu. Rev. Immunol. 2010, 28:491-533.
    • (2010) Annu. Rev. Immunol. , vol.28 , pp. 491-533
    • Hogan, P.G.1    Lewis, R.S.2    Rao, A.3
  • 131
    • 70349116421 scopus 로고    scopus 로고
    • ORAI1 and STIM1 deficiency in human and mice: roles of store-operated Ca2+ entry in the immune system and beyond
    • Feske S. ORAI1 and STIM1 deficiency in human and mice: roles of store-operated Ca2+ entry in the immune system and beyond. Immunol. Rev. 2009, 231:189-209.
    • (2009) Immunol. Rev. , vol.231 , pp. 189-209
    • Feske, S.1
  • 132
    • 44649097618 scopus 로고    scopus 로고
    • STIM1 signalling controls store-operated calcium entry required for development and contractile function in skeletal muscle
    • Stiber J., Hawkins A., Zhang Z.S., et al. STIM1 signalling controls store-operated calcium entry required for development and contractile function in skeletal muscle. Nat. Cell Biol. 2008, 10:688-697.
    • (2008) Nat. Cell Biol. , vol.10 , pp. 688-697
    • Stiber, J.1    Hawkins, A.2    Zhang, Z.S.3
  • 133
    • 33846840440 scopus 로고    scopus 로고
    • Cell cycle-dependent regulation of store-operated I(CRAC) and Mg2+-nucleotide-regulated MagNuM (TRPM7) currents
    • Tani D., Monteilh-Zoller M.K., Fleig A., Penner R. Cell cycle-dependent regulation of store-operated I(CRAC) and Mg2+-nucleotide-regulated MagNuM (TRPM7) currents. Cell Calcium 2007, 41:249-260.
    • (2007) Cell Calcium , vol.41 , pp. 249-260
    • Tani, D.1    Monteilh-Zoller, M.K.2    Fleig, A.3    Penner, R.4
  • 134
    • 0034623986 scopus 로고    scopus 로고
    • Store-operated calcium entry inactivates at the germinal vesicle breakdown stage of Xenopus meiosis
    • Machaca K., Haun S. Store-operated calcium entry inactivates at the germinal vesicle breakdown stage of Xenopus meiosis. J. Biol. Chem. 2000, 275:38710-38715.
    • (2000) J. Biol. Chem. , vol.275 , pp. 38710-38715
    • Machaca, K.1    Haun, S.2
  • 135
    • 0037033789 scopus 로고    scopus 로고
    • Induction of maturation-promoting factor during Xenopus oocyte maturation uncouples Ca2+ store depletion from store-operated Ca2+ entry
    • Machaca K., Haun S. Induction of maturation-promoting factor during Xenopus oocyte maturation uncouples Ca2+ store depletion from store-operated Ca2+ entry. J. Cell Biol. 2002, 156:75-85.
    • (2002) J. Cell Biol. , vol.156 , pp. 75-85
    • Machaca, K.1    Haun, S.2
  • 136
    • 77954381322 scopus 로고    scopus 로고
    • Regulation of store-operated Ca2+ entry during the cell cycle
    • Arredouani A., Yu F., Sun L., Machaca K. Regulation of store-operated Ca2+ entry during the cell cycle. J. Cell Sci. 2010, 123:2155-2162.
    • (2010) J. Cell Sci. , vol.123 , pp. 2155-2162
    • Arredouani, A.1    Yu, F.2    Sun, L.3    Machaca, K.4
  • 137
    • 70350452754 scopus 로고    scopus 로고
    • Orai1 internalization and STIM1 clustering inhibition modulate SOCE inactivation during meiosis
    • Yu F., Sun L., Machaca K. Orai1 internalization and STIM1 clustering inhibition modulate SOCE inactivation during meiosis. Proc. Natl. Acad. Sci. U.S.A. 2009, 106:17401-17406.
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 17401-17406
    • Yu, F.1    Sun, L.2    Machaca, K.3
  • 138
    • 85013723972 scopus 로고    scopus 로고
    • Constitutive recycling of the store-operated Ca2+ channel Orai1 and its internalization during meiosis, J. Cell Biol., in press.
    • F. Yu, L. Sun, K. Machaca, Constitutive recycling of the store-operated Ca2+ channel Orai1 and its internalization during meiosis, J. Cell Biol., in press.
    • Yu, F.1    Sun, L.2    Machaca, K.3
  • 139
    • 4644275515 scopus 로고    scopus 로고
    • Increased sensitivity and clustering of elementary Ca2+ release events during oocyte maturation
    • Machaca K. Increased sensitivity and clustering of elementary Ca2+ release events during oocyte maturation. Dev. Biol. 2004, 275:170-182.
    • (2004) Dev. Biol. , vol.275 , pp. 170-182
    • Machaca, K.1
  • 140
    • 0035159857 scopus 로고    scopus 로고
    • Changes in organization of the endoplasmic reticulum during Xenopus oocyte maturation and activation
    • Terasaki M., Runft L.L., Hand A.R. Changes in organization of the endoplasmic reticulum during Xenopus oocyte maturation and activation. Mol. Biol. Cell 2001, 12:1103-1116.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 1103-1116
    • Terasaki, M.1    Runft, L.L.2    Hand, A.R.3
  • 141
    • 18044379030 scopus 로고    scopus 로고
    • IP3 receptor activity is differentially regulated in endoplasmic reticulum subdomains during oocyte maturation
    • Boulware M.J., Marchant J.S. IP3 receptor activity is differentially regulated in endoplasmic reticulum subdomains during oocyte maturation. Curr. Biol. 2005, 15:765-770.
    • (2005) Curr. Biol. , vol.15 , pp. 765-770
    • Boulware, M.J.1    Marchant, J.S.2
  • 142
    • 67749131111 scopus 로고    scopus 로고
    • Kinase-dependent regulation of IP3-dependent Ca2+ release during oocyte maturation
    • Sun L., Haun S., Jones R.C., Edmondson R.D., Machaca K. Kinase-dependent regulation of IP3-dependent Ca2+ release during oocyte maturation. J. Biol. Chem. 2009, 284:20184-20196.
    • (2009) J. Biol. Chem. , vol.284 , pp. 20184-20196
    • Sun, L.1    Haun, S.2    Jones, R.C.3    Edmondson, R.D.4    Machaca, K.5
  • 143
    • 29044441873 scopus 로고    scopus 로고
    • Calcium signaling differentiation during Xenopus oocyte maturation
    • El Jouni W., Jang B., Haun S., Machaca K. Calcium signaling differentiation during Xenopus oocyte maturation. Dev. Biol. 2005, 288:514-525.
    • (2005) Dev. Biol. , vol.288 , pp. 514-525
    • El Jouni, W.1    Jang, B.2    Haun, S.3    Machaca, K.4
  • 144
    • 56049087932 scopus 로고    scopus 로고
    • Internalization of plasma membrane Ca2+-ATPase during Xenopus oocyte maturation
    • El Jouni W., Haun S., Machaca K. Internalization of plasma membrane Ca2+-ATPase during Xenopus oocyte maturation. Dev. Biol. 2008, 324:99-107.
    • (2008) Dev. Biol. , vol.324 , pp. 99-107
    • El Jouni, W.1    Haun, S.2    Machaca, K.3


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