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Volumn 8, Issue 4, 2010, Pages 881-915

Impact of marine drugs on cytoskeleton-mediated reproductive events

Author keywords

Marine drugs; Microfilaments; Microtubules; Reproduction; Toxins

Indexed keywords

AZASPIRACID DERIVATIVE; BETA TUBULIN; CALYCULIN; CAULERPENYNE; DINOPHYSISTOXIN 1; DINOPHYSISTOXIN DERIVATIVE; DOLASTATIN; DOLASTATIN 15; F ACTIN; GEODIAMOLIDE DERIVATIVE; JASPAMIDE; LATRUNCULIN; LATRUNCULIN A; LATRUNCULIN B; MARINE TOXIN; METHOXYCONIDIOL; NATURAL PRODUCT; OKADAIC ACID; OXYLIPIN; PALYTOXIN; PECTENOTOXIN; PEPTIDE DERIVATIVE; PHOSPHOPROTEIN PHOSPHATASE INHIBITOR; PSEUDOPTEROLIDE; STRONGYLOPHORINE DERIVATIVE; STYPOLDIONE; SWINHOLIDE; SWINHOLIDE A; THEONELLAPEPTOLIDE IE; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 77952572330     PISSN: None     EISSN: 16603397     Source Type: Journal    
DOI: 10.3390/md8040881     Document Type: Review
Times cited : (16)

References (249)
  • 1
    • 75149120280 scopus 로고    scopus 로고
    • Impact of marine drugs on animal reproductive processes
    • Silvestre, F.; Tosti, E. Impact of marine drugs on animal reproductive processes. Mar. Drugs 2009, 7, 539-564.
    • (2009) Mar. Drugs , vol.7 , pp. 539-564
    • Silvestre, F.1    Tosti, E.2
  • 2
    • 0017176529 scopus 로고
    • Head to tail polymerization of actin
    • Wegner, A. Head to tail polymerization of actin. J. Mol. Biol. 1976, 108, 139-150.
    • (1976) J. Mol. Biol. , vol.108 , pp. 139-150
    • Wegner, A.1
  • 3
    • 69249088090 scopus 로고    scopus 로고
    • Structural plasticity in actin and tubulin polymer dynamics
    • Kueh, H.Y.; Mitchison, T.J. Structural plasticity in actin and tubulin polymer dynamics. Science 2009, 325, 960-963.
    • (2009) Science , vol.325 , pp. 960-963
    • Kueh, H.Y.1    Mitchison, T.J.2
  • 4
    • 0642286487 scopus 로고    scopus 로고
    • The actin cytoskeleton as a therapeutic target: State of the art and future directions
    • Giganti, A.; Friederich, E. The actin cytoskeleton as a therapeutic target: state of the art and future directions. Prog. Cell Cycle Res. 2003, 5, 511-525.
    • (2003) Prog. Cell Cycle Res. , vol.5 , pp. 511-525
    • Giganti, A.1    Friederich, E.2
  • 6
    • 34548446806 scopus 로고    scopus 로고
    • Actin-based dynamics during spermatogenesis and its significance
    • Xiao, X.; Yang, W.X. Actin-based dynamics during spermatogenesis and its significance. J. Zhejiang Univ. Sci. B 2007, 8, 498-506.
    • (2007) J. Zhejiang Univ. Sci. B , vol.8 , pp. 498-506
    • Xiao, X.1    Yang, W.X.2
  • 7
    • 5044242038 scopus 로고    scopus 로고
    • Actions by actin: Reciprocal regulation of cortactin activity by tyrosine kinases and Factin
    • Gunst, S.J. Actions by actin: reciprocal regulation of cortactin activity by tyrosine kinases and Factin. Biochem. J. 2004, 380, e7-e8.
    • (2004) Biochem. J. , vol.380
    • Gunst, S.J.1
  • 9
    • 16644380895 scopus 로고    scopus 로고
    • Beginning and ending an actin filament: Control at the barbed end
    • Zigmond, S.H. Beginning and ending an actin filament: control at the barbed end. Curr. Top. Dev. Biol. 2004, 63, 145-188.
    • (2004) Curr. Top. Dev. Biol. , vol.63 , pp. 145-188
    • Zigmond, S.H.1
  • 10
    • 12344250639 scopus 로고    scopus 로고
    • Chronophin, a novel HAD-type serine protein phosphatase, regulates cofilin-dependent actin dynamics
    • Gohla, A.; Birkenfeld, J.; Bokoch, G.M. Chronophin, a novel HAD-type serine protein phosphatase, regulates cofilin-dependent actin dynamics. Nat. Cell Biol. 2005, 7, 21-29.
    • (2005) Nat. Cell Biol. , vol.7 , pp. 21-29
    • Gohla, A.1    Birkenfeld, J.2    Bokoch, G.M.3
  • 11
    • 33244481055 scopus 로고    scopus 로고
    • Regulation of dynamic events by microfilaments during oocyte maturation and fertilization
    • Sun, Q.Y.; Schatten, H. Regulation of dynamic events by microfilaments during oocyte maturation and fertilization. Reproduction 2006, 131, 193-205.
    • (2006) Reproduction , vol.131 , pp. 193-205
    • Sun, Q.Y.1    Schatten, H.2
  • 12
    • 0032475981 scopus 로고    scopus 로고
    • Synergy between actin depolymerizing factor/cofilin and profilin in increasing actin filament turnover
    • Didry, D.; Carlier, M.F.; Pantaloni, D. Synergy between actin depolymerizing factor/cofilin and profilin in increasing actin filament turnover. J. Biol. Chem. 1998, 273, 25602-25611.
    • (1998) J. Biol. Chem. , vol.273 , pp. 25602-25611
    • Didry, D.1    Carlier, M.F.2    Pantaloni, D.3
  • 13
    • 0033533789 scopus 로고    scopus 로고
    • Reconstitution of actin-based motility of Listeria and Shigella using pure proteins
    • Loisel, T.P.; Boujemaa, R.; Pantaloni, D.; Carlier, M.F. Reconstitution of actin-based motility of Listeria and Shigella using pure proteins. Nature 1999, 401, 613-616.
    • (1999) Nature , vol.401 , pp. 613-616
    • Loisel, T.P.1    Boujemaa, R.2    Pantaloni, D.3    Carlier, M.F.4
  • 14
    • 0028179555 scopus 로고
    • The Schizosaccharomyces pombe cdc3+ gene encodes a profilin essential for cytokinesis
    • Balasubramanian, M.K.; Hirani, B.R.; Burke, J.D.; Gould, K.L. The Schizosaccharomyces pombe cdc3+ gene encodes a profilin essential for cytokinesis. J. Cell Biol. 1994, 125, 1289-1301.
    • (1994) J. Cell Biol. , vol.125 , pp. 1289-1301
    • Balasubramanian, M.K.1    Hirani, B.R.2    Burke, J.D.3    Gould, K.L.4
  • 15
    • 0028799957 scopus 로고
    • Mutations in twinstar, a Drosophila gene encoding a cofilin/ADF homologue, result in defects in centrosome migration and cytokinesis
    • Gunsalus, K.C.; Bonaccorsi, S.; Williams, E.; Verni, F.; Gatti, M.; Goldberg, M.L. Mutations in twinstar, a Drosophila gene encoding a cofilin/ADF homologue, result in defects in centrosome migration and cytokinesis. J. Cell Biol. 1995, 131, 1243-1259.
    • (1995) J. Cell Biol. , vol.131 , pp. 1243-1259
    • Gunsalus, K.C.1    Bonaccorsi, S.2    Williams, E.3    Verni, F.4    Gatti, M.5    Goldberg, M.L.6
  • 16
    • 0036329002 scopus 로고    scopus 로고
    • Molecular dissection of cytokinesis by RNA interference in Drosophila cultured cells
    • Somma, M.P.; Fasulo, B.; Cenci, G.; Cundari, E.; Gatti, M. Molecular dissection of cytokinesis by RNA interference in Drosophila cultured cells. Mol. Biol. Cell 2002, 13, 2448-2460.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 2448-2460
    • Somma, M.P.1    Fasulo, B.2    Cenci, G.3    Cundari, E.4    Gatti, M.5
  • 18
    • 0032829103 scopus 로고    scopus 로고
    • New anti-actin drugs in the study of the organization and function of the actin cytoskeleton
    • Spector, I.; Braet, F.; Shochet, N.R.; Bubb, M.R. New anti-actin drugs in the study of the organization and function of the actin cytoskeleton. Microsc. Res. Tech. 1999, 47, 18-37.
    • (1999) Microsc. Res. Tech. , vol.47 , pp. 18-37
    • Spector, I.1    Braet, F.2    Shochet, N.R.3    Bubb, M.R.4
  • 19
    • 0038348755 scopus 로고    scopus 로고
    • Small-molecule inhibitors of actin dynamics and cell motility
    • Fenteany, G.; Zhu, S. Small-molecule inhibitors of actin dynamics and cell motility. Curr. Top. Med. Chem. 2003, 3, 593-616.
    • (2003) Curr. Top. Med. Chem. , vol.3 , pp. 593-616
    • Fenteany, G.1    Zhu, S.2
  • 20
    • 0032006059 scopus 로고    scopus 로고
    • Microtubules and actin filaments: Dynamic targets for cancer chemotherapy
    • Jordan, M.A.; Wilson, L. Microtubules and actin filaments: dynamic targets for cancer chemotherapy. Curr. Opin. Cell Biol. 1998, 10, 123-130.
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 123-130
    • Jordan, M.A.1    Wilson, L.2
  • 21
    • 33749059234 scopus 로고    scopus 로고
    • Actin-targeting natural products: Structures, properties and mechanisms of action
    • Allingham, J.S.; Klenchin, V.A.; Rayment, I. Actin-targeting natural products: structures, properties and mechanisms of action. Cell. Mol. Life Sci. 2006, 63, 2119-2134.
    • (2006) Cell. Mol. Life Sci. , vol.63 , pp. 2119-2134
    • Allingham, J.S.1    Klenchin, V.A.2    Rayment, I.3
  • 23
    • 56849129945 scopus 로고    scopus 로고
    • Marine toxins and the cytoskeleton: Pectenotoxins, unusual macrolides that disrupt actin
    • Espina, B.; Rubiolo, J.A. Marine toxins and the cytoskeleton: pectenotoxins, unusual macrolides that disrupt actin. Febs J. 2008, 275, 6082-6088.
    • (2008) Febs J. , vol.275 , pp. 6082-6088
    • Espina, B.1    Rubiolo, J.A.2
  • 24
    • 0020698663 scopus 로고
    • Latrunculins: Novel marine toxins that disrupt microfilament organization in cultured cells
    • Spector, I.; Shochet, N.R.; Kashman, Y.; Groweiss, A. Latrunculins: novel marine toxins that disrupt microfilament organization in cultured cells. Science 1983, 219, 493-495.
    • (1983) Science , vol.219 , pp. 493-495
    • Spector, I.1    Shochet, N.R.2    Kashman, Y.3    Groweiss, A.4
  • 25
    • 0034623126 scopus 로고    scopus 로고
    • Actin-latrunculin A structure and function. Differential modulation of actin-binding protein function by latrunculin A
    • Yarmola, E.G.; Somasundaram, T.; Boring, T.A.; Spector, I.; Bubb, M.R. Actin-latrunculin A structure and function. Differential modulation of actin-binding protein function by latrunculin A. J. Biol. Chem. 2000, 275, 28120-28127.
    • (2000) J. Biol. Chem. , vol.275 , pp. 28120-28127
    • Yarmola, E.G.1    Somasundaram, T.2    Boring, T.A.3    Spector, I.4    Bubb, M.R.5
  • 26
    • 0023142377 scopus 로고
    • Inhibition of actin polymerization by latrunculin A
    • Coue, M.; Brenner, S.L.; Spector, I.; Korn, E.D. Inhibition of actin polymerization by latrunculin A. FEBS Lett. 1987, 213, 316-318.
    • (1987) FEBS Lett. , vol.213 , pp. 316-318
    • Coue, M.1    Brenner, S.L.2    Spector, I.3    Korn, E.D.4
  • 27
    • 0037177848 scopus 로고    scopus 로고
    • Control of actin dynamics by proteins made of beta-thymosin repeats: The actobindin family
    • Hertzog, M.; Yarmola, E.G.; Didry, D.; Bubb, M.R.; Carlier, M.F. Control of actin dynamics by proteins made of beta-thymosin repeats: the actobindin family. J. Biol. Chem. 2002, 277, 14786-14792.
    • (2002) J. Biol. Chem. , vol.277 , pp. 14786-14792
    • Hertzog, M.1    Yarmola, E.G.2    Didry, D.3    Bubb, M.R.4    Carlier, M.F.5
  • 28
    • 0030978526 scopus 로고    scopus 로고
    • High rates of actin filament turnover in budding yeast and roles for actin in establishment and maintenance of cell polarity revealed using the actin inhibitor latrunculin-A
    • Ayscough, K.R.; Stryker, J.; Pokala, N.; Sanders, M.; Crews, P.; Drubin, D.G. High rates of actin filament turnover in budding yeast and roles for actin in establishment and maintenance of cell polarity revealed using the actin inhibitor latrunculin-A. J. Cell Biol. 1997, 137, 399-416.
    • (1997) J. Cell Biol. , vol.137 , pp. 399-416
    • Ayscough, K.R.1    Stryker, J.2    Pokala, N.3    Sanders, M.4    Crews, P.5    Drubin, D.G.6
  • 29
    • 0033775855 scopus 로고    scopus 로고
    • Latrunculin alters the actin-monomer subunit interface to prevent polymerization
    • Morton, W.M.; Ayscough, K.R.; McLaughlin, P.J. Latrunculin alters the actin-monomer subunit interface to prevent polymerization. Nat. Cell Biol. 2000, 2, 376-378.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 376-378
    • Morton, W.M.1    Ayscough, K.R.2    McLaughlin, P.J.3
  • 30
    • 65249102232 scopus 로고    scopus 로고
    • Toxins affecting actin filaments and microtubules
    • Saito, S.Y. Toxins affecting actin filaments and microtubules. Prog. Mol. Subcell. Biol. 2009, 46, 187-219.
    • (2009) Prog. Mol. Subcell. Biol. , vol.46 , pp. 187-219
    • Saito, S.Y.1
  • 31
    • 0024360298 scopus 로고
    • Latrunculins - Novel marine macrolides that disrupt microfilament organization and affect cell growth: I. Comparison with cytochalasin D
    • Spector, I.; Shochet, N.R.; Blasberger, D.; Kashman, Y. Latrunculins - novel marine macrolides that disrupt microfilament organization and affect cell growth: I. Comparison with cytochalasin D. Cell Motil. Cytoskeleton 1989, 13, 127-144.
    • (1989) Cell Motil. Cytoskeleton , vol.13 , pp. 127-144
    • Spector, I.1    Shochet, N.R.2    Blasberger, D.3    Kashman, Y.4
  • 32
    • 0025674098 scopus 로고
    • Marine natural products. XXIII. Three new cytotoxic dimeric macrolides, swinholides B and C and isoswinholide A, congeners of swinholide A, from the Okinawan marine sponge Theonella swinhoei
    • Kobayashi, M.; Tanaka, J.; Katori, T.; Kitagawa, I. Marine natural products. XXIII. Three new cytotoxic dimeric macrolides, swinholides B and C and isoswinholide A, congeners of swinholide A, from the Okinawan marine sponge Theonella swinhoei. Chem. Pharm. Bull. (Tokyo) 1990, 38, 2960-2966.
    • (1990) Chem. Pharm. Bull. (Tokyo) , vol.38 , pp. 2960-2966
    • Kobayashi, M.1    Tanaka, J.2    Katori, T.3    Kitagawa, I.4
  • 33
    • 0028967310 scopus 로고
    • Swinholide A is a microfilament disrupting marine toxin that stabilizes actin dimers and severs actin filaments
    • Bubb, M.R.; Spector, I.; Bershadsky, A.D.; Korn, E.D. Swinholide A is a microfilament disrupting marine toxin that stabilizes actin dimers and severs actin filaments. J. Biol. Chem. 1995, 270, 3463-3466.
    • (1995) J. Biol. Chem. , vol.270 , pp. 3463-3466
    • Bubb, M.R.1    Spector, I.2    Bershadsky, A.D.3    Korn, E.D.4
  • 34
    • 0024378138 scopus 로고
    • Mycalolides A-C, hybrid macrolides of ulapualides and halichondramide, from a sponge of the genus Mycale
    • Fusetani, N.; Yasumuro, K.; Matsunaga, S.; Hashimoto, K. Mycalolides A-C, hybrid macrolides of ulapualides and halichondramide, from a sponge of the genus Mycale. Tetrahedron Lett. 1989, 30, 2809-2812.
    • (1989) Tetrahedron Lett. , vol.30 , pp. 2809-2812
    • Fusetani, N.1    Yasumuro, K.2    Matsunaga, S.3    Hashimoto, K.4
  • 37
    • 0027159833 scopus 로고
    • Mycalolide-B, a novel and specific inhibitor of actomyosin ATPase isolated from marine sponge
    • DOI 10.1016/0014-5793(93)81557-G
    • Hori, M.; Saito, S.; Shin, Y.Z.; Ozaki, H.; Fusetani, N.; Karaki, H. Mycalolide-B, a novel and specific inhibitor of actomyosin ATPase isolated from marine sponge. FEBS Lett. 1993, 322, 151-154. (Pubitemid 23140367)
    • (1993) FEBS Letters , vol.322 , Issue.2 , pp. 151-154
    • Hori, M.1    Saito, S.2    Shin, Y.Z.3    Ozaki, H.4    Fusetani, N.5    Karaki, H.6
  • 38
    • 0030954604 scopus 로고    scopus 로고
    • Application of physiologically active substances isolated from natural resources to pharmacological studies
    • Ohizumi, Y. Application of physiologically active substances isolated from natural resources to pharmacological studies. Jpn. J. Pharmacol. 1997, 73, 263-289. (Pubitemid 27226159)
    • (1997) Japanese Journal of Pharmacology , vol.73 , Issue.4 , pp. 263-289
    • Ohizumi, Y.1
  • 39
    • 0028244823 scopus 로고
    • Jasplakinolide, a cytotoxic natural product, induces actin polymerization and competitively inhibits the binding of phalloidin to F-actin
    • Bubb, M.R.; Senderowicz, A.M.; Sausville, E.A.; Duncan, K.L.; Korn, E.D. Jasplakinolide, a cytotoxic natural product, induces actin polymerization and competitively inhibits the binding of phalloidin to F-actin. J. Biol. Chem. 1994, 269, 14869-14871.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14869-14871
    • Bubb, M.R.1    Senderowicz, A.M.2    Sausville, E.A.3    Duncan, K.L.4    Korn, E.D.5
  • 40
    • 0034681423 scopus 로고    scopus 로고
    • Effects of jasplakinolide on the kinetics of actin polymerization. An explanation for certain in vivo observations
    • Bubb, M.R.; Spector, I.; Beyer, B.B.; Fosen, K.M. Effects of jasplakinolide on the kinetics of actin polymerization. An explanation for certain in vivo observations. J. Biol. Chem. 2000, 275, 5163-5170.
    • (2000) J. Biol. Chem. , vol.275 , pp. 5163-5170
    • Bubb, M.R.1    Spector, I.2    Beyer, B.B.3    Fosen, K.M.4
  • 41
    • 56849132857 scopus 로고    scopus 로고
    • Marine toxins and the cytoskeleton
    • Botana, L.M. Marine toxins and the cytoskeleton. Febs J. 2008, 275, 6059.
    • (2008) Febs J. , vol.275 , pp. 6059
    • Botana, L.M.1
  • 42
    • 56849104094 scopus 로고    scopus 로고
    • Marine toxins and the cytoskeleton: Okadaic acid and dinophysistoxins
    • Vale, C.; Botana, L.M. Marine toxins and the cytoskeleton: okadaic acid and dinophysistoxins. Febs J. 2008, 275, 6060-6066.
    • (2008) Febs J. , vol.275 , pp. 6060-6066
    • Vale, C.1    Botana, L.M.2
  • 43
    • 38149030719 scopus 로고    scopus 로고
    • Phosphatases, DNA damage checkpoints and checkpoint deactivation
    • Heideker, J.; Lis, E.T.; Romesberg, F.E. Phosphatases, DNA damage checkpoints and checkpoint deactivation. Cell Cycle 2007, 6, 3058-3064.
    • (2007) Cell Cycle , vol.6 , pp. 3058-3064
    • Heideker, J.1    Lis, E.T.2    Romesberg, F.E.3
  • 46
    • 0031917829 scopus 로고    scopus 로고
    • Transient exposure of rhesus macaque oocytes to calyculin-A and okadaic acid stimulates germinal vesicle breakdown permitting subsequent development and fertilization
    • Smith, G.D.; Sadhu, A.; Wolf, D.P. Transient exposure of rhesus macaque oocytes to calyculin-A and okadaic acid stimulates germinal vesicle breakdown permitting subsequent development and fertilization. Biol. Reprod. 1998, 58, 880-886.
    • (1998) Biol. Reprod. , vol.58 , pp. 880-886
    • Smith, G.D.1    Sadhu, A.2    Wolf, D.P.3
  • 47
    • 33746866335 scopus 로고    scopus 로고
    • Cytoskeleton alterations induced by Geodia corticostylifera depsipeptides in breast cancer cells
    • Rangel, M.; Prado, M.P.; Konno, K.; Naoki, H.; Freitas, J.C.; Machado-Santelli, G.M. Cytoskeleton alterations induced by Geodia corticostylifera depsipeptides in breast cancer cells. Peptides 2006, 27, 2047-2057.
    • (2006) Peptides , vol.27 , pp. 2047-2057
    • Rangel, M.1    Prado, M.P.2    Konno, K.3    Naoki, H.4    Freitas, J.C.5    Machado-Santelli, G.M.6
  • 48
    • 54249139074 scopus 로고    scopus 로고
    • Marine pharmacology in 2005-2006: Antitumour and cytotoxic compounds
    • Mayer, A.M.; Gustafson, K.R. Marine pharmacology in 2005-2006: antitumour and cytotoxic compounds. Eur. J. Cancer. 2008, 44, 2357-2387.
    • (2008) Eur. J. Cancer. , vol.44 , pp. 2357-2387
    • Mayer, A.M.1    Gustafson, K.R.2
  • 50
    • 0025893070 scopus 로고
    • Marine natural products. XXVI. Biologically active tridecapeptide lactones from the Okinawan marine sponge Theonella swinhoei (Theonellidae). (2). Structures of theonellapeptolides Ia, Ib, Ic, and Ie
    • Kobayashi, M.; Lee, N.K.; Shibuya, H.; Momose, T.; Kitagawa, I. Marine natural products. XXVI. Biologically active tridecapeptide lactones from the Okinawan marine sponge Theonella swinhoei (Theonellidae). (2). Structures of theonellapeptolides Ia, Ib, Ic, and Ie. Chem. Pharm. Bull. (Tokyo) 1991, 39, 1177-1184.
    • (1991) Chem. Pharm. Bull. (Tokyo) , vol.39 , pp. 1177-1184
    • Kobayashi, M.1    Lee, N.K.2    Shibuya, H.3    Momose, T.4    Kitagawa, I.5
  • 51
    • 4544369750 scopus 로고    scopus 로고
    • Malformation of immature starfish oocytes by theonellapeptolide Ie, a Tridecapeptide lactone from a marine sponge Petrosia species, through disturbance of cortical F-actin distribution
    • Ohta, E.; Okada, H.; Ohta, S.; Kobayashi, M.; Kitagawa, I.; Horiike, S.; Takahashi, T.; Hosoya, H.; Yamamoto, K.; Ikegami, S. Malformation of immature starfish oocytes by theonellapeptolide Ie, a Tridecapeptide lactone from a marine sponge Petrosia species, through disturbance of cortical F-actin distribution. Biosci. Biotechnol. Biochem. 2003, 67, 1908-1915.
    • (2003) Biosci. Biotechnol. Biochem. , vol.67 , pp. 1908-1915
    • Ohta, E.1    Okada, H.2    Ohta, S.3    Kobayashi, M.4    Kitagawa, I.5    Horiike, S.6    Takahashi, T.7    Hosoya, H.8    Yamamoto, K.9    Ikegami, S.10
  • 52
    • 0032582026 scopus 로고    scopus 로고
    • Azaspiracid, a new marine toxin having unique spiro ring assemblies, isolated from Irish mussels, Mytilus edulis
    • Satake, M.; Ofuji, K.; Naoki, H.; James, K.; Furey, A.; McMahon, T.; Silke, J.; Yasumoto, T. Azaspiracid, a new marine toxin having unique spiro ring assemblies, isolated from Irish mussels, Mytilus edulis. J. Am. Chem. Soc. 1998, 120, 9967-9968.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 9967-9968
    • Satake, M.1    Ofuji, K.2    Naoki, H.3    James, K.4    Furey, A.5    McMahon, T.6    Silke, J.7    Yasumoto, T.8
  • 53
    • 0033390733 scopus 로고    scopus 로고
    • Two analogs of azaspiracid isolated from mussels, Mytilus edulis, involved in human intoxication in Ireland
    • Ofuji, K.; Satake, M.; McMahon, T.; Silke, J.; James, K.J.; Naoki, H.; Oshima, Y.; Yasumoto, T. Two analogs of azaspiracid isolated from mussels, Mytilus edulis, involved in human intoxication in Ireland. Nat. Toxins 1999, 7, 99-102.
    • (1999) Nat. Toxins , vol.7 , pp. 99-102
    • Ofuji, K.1    Satake, M.2    McMahon, T.3    Silke, J.4    James, K.J.5    Naoki, H.6    Oshima, Y.7    Yasumoto, T.8
  • 54
    • 0035289355 scopus 로고    scopus 로고
    • Structures of azaspiracid analogs, azaspiracid-4 and azaspiracid-5, causative toxins of azaspiracid poisoning in Europe
    • Ofuji, K.; Satake, M.; McMahon, T.; James, K.J.; Naoki, H.; Oshima, Y.; Yasumoto, T. Structures of azaspiracid analogs, azaspiracid-4 and azaspiracid-5, causative toxins of azaspiracid poisoning in Europe. Biosci. Biotechnol. Biochem. 2001, 65, 740-742.
    • (2001) Biosci. Biotechnol. Biochem. , vol.65 , pp. 740-742
    • Ofuji, K.1    Satake, M.2    McMahon, T.3    James, K.J.4    Naoki, H.5    Oshima, Y.6    Yasumoto, T.7
  • 55
    • 0036918228 scopus 로고    scopus 로고
    • Studies on azaspiracid biotoxins. I. Ultrafast high-resolution liquid chromatography/mass spectrometry separations using monolithic columns
    • DOI 10.1002/rcm.851
    • Volmer, D.A.; Brombacher, S.; Whitehead, B. Studies on azaspiracid biotoxins. I. Ultrafast high-resolution liquid chromatography/mass spectrometry separations using monolithic columns. Rapid Commun. Mass Spectrom. 2002, 16, 2298-2305. (Pubitemid 36014709)
    • (2002) Rapid Communications in Mass Spectrometry , vol.16 , Issue.24 , pp. 2298-2305
    • Volmer, D.A.1    Brombacher, S.2    Whitehead, B.3
  • 56
    • 0037355392 scopus 로고    scopus 로고
    • Detection of five new hydroxyl analogues of azaspiracids in shellfish using multiple tandem mass spectrometry
    • DOI 10.1016/S0041-0101(02)00288-X, PII S004101010200288X
    • James, K.J.; Sierra, M.D.; Lehane, M.; Brana Magdalena, A.; Furey, A. Detection of five new hydroxyl analogues of azaspiracids in shellfish using multiple tandem mass spectrometry. Toxicon 2003, 41, 277-283. (Pubitemid 36144165)
    • (2003) Toxicon , vol.41 , Issue.3 , pp. 277-283
    • James, K.J.1    Sierra, M.D.2    Lehane, M.3    Brana Magdalena, A.4    Furey, A.5
  • 57
    • 39749120849 scopus 로고    scopus 로고
    • Discovery of new analogs of the marine biotoxin azaspiracid in blue mussels (Mytilus edulis) by ultra-performance liquid chromatography/tandem mass spectrometry
    • Rehmann, N.; Hess, P.; Quilliam, M.A. Discovery of new analogs of the marine biotoxin azaspiracid in blue mussels (Mytilus edulis) by ultra-performance liquid chromatography/tandem mass spectrometry. Rapid Commun. Mass Spectrom. 2008, 22, 549-558.
    • (2008) Rapid Commun. Mass Spectrom , vol.22 , pp. 549-558
    • Rehmann, N.1    Hess, P.2    Quilliam, M.A.3
  • 58
    • 56849120307 scopus 로고    scopus 로고
    • Marine toxins and the cytoskeleton: Azaspiracids
    • Vilarino, N. Marine toxins and the cytoskeleton: azaspiracids. Febs J. 2008, 275, 6075-6081.
    • (2008) Febs J. , vol.275 , pp. 6075-6081
    • Vilarino, N.1
  • 60
    • 0141432163 scopus 로고    scopus 로고
    • Ostreopsis sp., a possible origin of palytoxin (PTX) in parrotfish Scarus ovifrons
    • DOI 10.1016/S0041-0101(03)00097-7
    • Taniyama, S.; Arakawa, O.; Terada, M.; Nishio, S.; Takatani, T.; Mahmud, Y.; Noguchi, T. Ostreopsis sp., a possible origin of palytoxin (PTX) in parrotfish Scarus ovifrons. Toxicon 2003, 42, 29-33. (Pubitemid 37297557)
    • (2003) Toxicon , vol.42 , Issue.1 , pp. 29-33
    • Taniyama, S.1    Arakawa, O.2    Terada, M.3    Nishio, S.4    Takatani, T.5    Mahmud, Y.6    Noguchi, T.7
  • 61
    • 56849119797 scopus 로고    scopus 로고
    • Marine toxins and the cytoskeleton: A new view of palytoxin toxicity
    • Louzao, M.C.; Ares, I.R.; Cagide, E. Marine toxins and the cytoskeleton: a new view of palytoxin toxicity. Febs J. 2008, 275, 6067-6074.
    • (2008) Febs J. , vol.275 , pp. 6067-6074
    • Louzao, M.C.1    Ares, I.R.2    Cagide, E.3
  • 63
    • 70349597628 scopus 로고    scopus 로고
    • The influence of bioactive oxylipins from marine diatoms on invertebrate reproduction and development
    • Caldwell, G.S. The influence of bioactive oxylipins from marine diatoms on invertebrate reproduction and development. Mar. Drugs 2009, 7, 367-400.
    • (2009) Mar. Drugs , vol.7 , pp. 367-400
    • Caldwell, G.S.1
  • 64
    • 3042802305 scopus 로고    scopus 로고
    • First evidence of sperm motility inhibition by the diatom aldehyde 2E,4E-decadienal
    • Caldwell, G.S.; Bentley, M.G.; Olive, P.J.W. First evidence of sperm motility inhibition by the diatom aldehyde 2E,4E-decadienal. Mar. Ecol. Prog. Ser. 2004, 273, 97-108.
    • (2004) Mar. Ecol. Prog. Ser. , vol.273 , pp. 97-108
    • Caldwell, G.S.1    Bentley, M.G.2    Olive, P.J.W.3
  • 65
    • 20044382424 scopus 로고    scopus 로고
    • Strongylophorine-26, a Rho-dependent inhibitor of tumor cell invasion that reduces actin stress fibers and induces nonpolarized lamellipodial extensions
    • DOI 10.1158/1535-7163.MCT-04-0310
    • McHardy, L.M.; Warabi, K.; Andersen, R.J.; Roskelley, C.D.; Roberge, M. Strongylophorine-26, a Rho-dependent inhibitor of tumor cell invasion that reduces actin stress fibers and induces nonpolarized lamellipodial extensions. Mol Cancer Ther. 2005, 4, 772-778. (Pubitemid 40767121)
    • (2005) Molecular Cancer Therapeutics , vol.4 , Issue.5 , pp. 772-778
    • McHardy, L.M.1    Warabi, K.2    Andersen, R.J.3    Roskelley, C.D.4    Roberge, M.5
  • 66
    • 0021686169 scopus 로고
    • Dynamic instability of microtubule growth
    • Mitchison, T.; Kirschner, M. Dynamic instability of microtubule growth. Nature 1984, 312, 237-242.
    • (1984) Nature , vol.312 , pp. 237-242
    • Mitchison, T.1    Kirschner, M.2
  • 67
    • 0017835961 scopus 로고
    • Opposite end assembly and disassembly of mircotubules at steady state in vitro
    • Margolis, R.L.; Wilson, L. Opposite end assembly and disassembly of microtubules at steady state in vitro. Cell 1978, 13, 1-8. (Pubitemid 8296143)
    • (1978) Cell , vol.13 , Issue.1 , pp. 1-8
    • Margolis, R.L.1    Wilson, L.2
  • 68
    • 0019782697 scopus 로고
    • Microtubule treadmills - Possible molecular machinery
    • Margolis, R.L.; Wilson, L. Microtubule treadmills - possible molecular machinery. Nature 1981, 293, 705-711.
    • (1981) Nature , vol.293 , pp. 705-711
    • Margolis, R.L.1    Wilson, L.2
  • 69
    • 0022390903 scopus 로고
    • Exchange of actin subunits at the leading edge of living fibroblasts: Possible role of treadmilling
    • Wang, Y.L. Exchange of actin subunits at the leading edge of living fibroblasts: possible role of treadmilling. J. Cell Biol. 1985, 101, 597-602.
    • (1985) J. Cell Biol. , vol.101 , pp. 597-602
    • Wang, Y.L.1
  • 70
    • 0025740949 scopus 로고
    • Actin microfilament dynamics in locomoting cells
    • Theriot, J.A.; Mitchison, T.J. Actin microfilament dynamics in locomoting cells. Nature 1991, 352, 126-131.
    • (1991) Nature , vol.352 , pp. 126-131
    • Theriot, J.A.1    Mitchison, T.J.2
  • 71
    • 0034654023 scopus 로고    scopus 로고
    • Dissecting the role of molecular motors in the mitotic spindle
    • Mountain, V.; Compton, D.A. Dissecting the role of molecular motors in the mitotic spindle. Anat. Rec. 2000, 261, 14-24.
    • (2000) Anat. Rec. , vol.261 , pp. 14-24
    • Mountain, V.1    Compton, D.A.2
  • 72
    • 63249089461 scopus 로고    scopus 로고
    • Cytoskeleton structure and dynamic behaviour: Quick excursus from basic molecular mechanisms to some implications in cancer chemotherapy
    • Alberti, C. Cytoskeleton structure and dynamic behaviour: quick excursus from basic molecular mechanisms to some implications in cancer chemotherapy. Eur. Rev. Med. Pharmacol. Sci. 2009, 13, 13-21.
    • (2009) Eur. Rev. Med. Pharmacol. Sci. , vol.13 , pp. 13-21
    • Alberti, C.1
  • 73
    • 70350571135 scopus 로고    scopus 로고
    • On and around microtubules: An overview
    • Wade, R.H. On and around microtubules: an overview. Mol. Biotechnol. 2009, 43, 177-191.
    • (2009) Mol. Biotechnol. , vol.43 , pp. 177-191
    • Wade, R.H.1
  • 74
    • 0024425887 scopus 로고
    • Checkpoints: Controls that ensure the order of cell cycle events
    • Hartwell, L.H.; Weinert, T.A. Checkpoints: controls that ensure the order of cell cycle events. Science 1989, 246, 629-634.
    • (1989) Science , vol.246 , pp. 629-634
    • Hartwell, L.H.1    Weinert, T.A.2
  • 75
    • 0026703325 scopus 로고
    • Creative blocks: Cell-cycle checkpoints and feedback controls
    • Murray, A.W. Creative blocks: cell-cycle checkpoints and feedback controls. Nature 1992, 359, 599-604.
    • (1992) Nature , vol.359 , pp. 599-604
    • Murray, A.W.1
  • 76
    • 0037459061 scopus 로고    scopus 로고
    • The molecular motor toolbox for intracellular transport
    • Vale, R.D. The molecular motor toolbox for intracellular transport. Cell 2003, 112, 467-480.
    • (2003) Cell , vol.112 , pp. 467-480
    • Vale, R.D.1
  • 77
    • 0842333851 scopus 로고    scopus 로고
    • Dynein: An ancient motor protein involved in multiple modes of transport
    • Vallee, R.B.; Williams, J.C.; Varma, D.; Barnhart, L.E. Dynein: An ancient motor protein involved in multiple modes of transport. J. Neurobiol. 2004, 58, 189-200.
    • (2004) J. Neurobiol. , vol.58 , pp. 189-200
    • Vallee, R.B.1    Williams, J.C.2    Varma, D.3    Barnhart, L.E.4
  • 78
    • 0024463944 scopus 로고
    • Movement of microtubules by single kinesin molecules
    • Howard, J.; Hudspeth, A.J.; Vale, R.D. Movement of microtubules by single kinesin molecules. Nature 1989, 342, 154-158.
    • (1989) Nature , vol.342 , pp. 154-158
    • Howard, J.1    Hudspeth, A.J.2    Vale, R.D.3
  • 79
    • 0025222347 scopus 로고
    • Bead movement by single kinesin molecules studied with optical tweezers
    • Block, S.M.; Goldstein, L.S.; Schnapp, B.J. Bead movement by single kinesin molecules studied with optical tweezers. Nature 1990, 348, 348-352.
    • (1990) Nature , vol.348 , pp. 348-352
    • Block, S.M.1    Goldstein, L.S.2    Schnapp, B.J.3
  • 80
    • 0028859428 scopus 로고
    • Single cytoplasmic dynein molecule movements: Characterization and comparison with kinesin
    • Wang, Z.; Khan, S.; Sheetz, M.P. Single cytoplasmic dynein molecule movements: characterization and comparison with kinesin. Biophys. J. 1995, 69, 2011-2023.
    • (1995) Biophys. J. , vol.69 , pp. 2011-2023
    • Wang, Z.1    Khan, S.2    Sheetz, M.P.3
  • 81
    • 1342325553 scopus 로고    scopus 로고
    • Cytoplasmic dynein functions as a gear in response to load
    • Mallik, R.; Carter, B.C.; Lex, S.A.; King, S.J.; Gross, S.P. Cytoplasmic dynein functions as a gear in response to load. Nature 2004, 427, 649-652.
    • (2004) Nature , vol.427 , pp. 649-652
    • Mallik, R.1    Carter, B.C.2    Lex, S.A.3    King, S.J.4    Gross, S.P.5
  • 84
    • 36249009069 scopus 로고    scopus 로고
    • Force-induced bidirectional stepping of cytoplasmic dynein
    • Gennerich, A.; Carter, A.P.; Reck-Peterson, S.L.; Vale, R.D. Force-induced bidirectional stepping of cytoplasmic dynein. Cell 2007, 131, 952-965.
    • (2007) Cell , vol.131 , pp. 952-965
    • Gennerich, A.1    Carter, A.P.2    Reck-Peterson, S.L.3    Vale, R.D.4
  • 85
    • 60749121148 scopus 로고    scopus 로고
    • Walking the walk: How kinesin and dynein coordinate their steps
    • Gennerich, A.; Vale, R.D. Walking the walk: how kinesin and dynein coordinate their steps. Curr. Opin. Cell Biol. 2009, 21, 59-67.
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 59-67
    • Gennerich, A.1    Vale, R.D.2
  • 86
    • 6344228431 scopus 로고    scopus 로고
    • Kinesin superfamily proteins and their various functions and dynamics
    • DOI 10.1016/j.yexcr.2004.08.010, PII S0014482704004537
    • Hirokawa, N.; Takemura, R. Kinesin superfamily proteins and their various functions and dynamics. Exp. Cell Res. 2004, 301, 50-59. (Pubitemid 39388896)
    • (2004) Experimental Cell Research , vol.301 , Issue.1 , pp. 50-59
    • Hirokawa, N.1    Takemura, R.2
  • 87
    • 0034677929 scopus 로고    scopus 로고
    • The dynein microtubule motor
    • King, S.M. The dynein microtubule motor. Biochim. Biophys. Acta 2000, 1496, 60-75.
    • (2000) Biochim. Biophys. Acta , vol.1496 , pp. 60-75
    • King, S.M.1
  • 88
    • 0033936009 scopus 로고    scopus 로고
    • Connecting vesicle transport to the cytoskeleton
    • Kamal, A.; Goldstein, L.S. Connecting vesicle transport to the cytoskeleton. Curr. Opin. Cell Biol. 2000, 12, 503-508.
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 503-508
    • Kamal, A.1    Goldstein, L.S.2
  • 91
    • 0001421356 scopus 로고
    • Antimicrobial and antineoplastic activity in some south Florida seaweeds
    • Hodgson, L.M. Antimicrobial and antineoplastic activity in some south Florida seaweeds. Bot. Mar. 1984, 27, 387-390.
    • (1984) Bot. Mar. , vol.27 , pp. 387-390
    • Hodgson, L.M.1
  • 92
    • 0001285112 scopus 로고
    • Chemical defense in tropical green algae, order Caulerpales
    • Paul, V.J.; Fenical, W. Chemical defense in tropical green algae, order Caulerpales. Mar. Ecol. Prog. Ser. 1986, 34, 157-169.
    • (1986) Mar. Ecol. Prog. Ser. , vol.34 , pp. 157-169
    • Paul, V.J.1    Fenical, W.2
  • 94
    • 2442433768 scopus 로고    scopus 로고
    • Antibacterial activity in marine algae from the coast of Yucatan, Mexico
    • Freile-Pelegrin, Y.; Morales, J.L. Antibacterial activity in marine algae from the coast of Yucatan, Mexico. Bot. Mar. 2004, 47, 140-146.
    • (2004) Bot. Mar. , vol.47 , pp. 140-146
    • Freile-Pelegrin, Y.1    Morales, J.L.2
  • 96
    • 33749534479 scopus 로고    scopus 로고
    • Antiproliferative and newly attributed apoptotic activities from an invasive marine alga: Caulerpa racemosa var. cylindracea
    • Cavas, L.; Baskin, Y.; Yurdakoc, K.; Olgun, N. Antiproliferative and newly attributed apoptotic activities from an invasive marine alga: Caulerpa racemosa var. cylindracea. J. Exp. Mar. Biol. Ecol. 2006, 339, 111-119.
    • (2006) J. Exp. Mar. Biol. Ecol. , vol.339 , pp. 111-119
    • Cavas, L.1    Baskin, Y.2    Yurdakoc, K.3    Olgun, N.4
  • 97
    • 0035940774 scopus 로고    scopus 로고
    • Caulerpenyne, a toxin from the seaweed Caulerpa taxifolia, depresses afterhyperpolarization in invertebrate neurons
    • Mozzachiodi, R.; Scuri, R.; Roberto, M.; Brunelli, M. Caulerpenyne, a toxin from the seaweed Caulerpa taxifolia, depresses afterhyperpolarization in invertebrate neurons. NeuroScience 2001, 107, 519-526.
    • (2001) NeuroScience , vol.107 , pp. 519-526
    • Mozzachiodi, R.1    Scuri, R.2    Roberto, M.3    Brunelli, M.4
  • 98
    • 0035861845 scopus 로고    scopus 로고
    • Caulerpenyne from Caulerpa taxifolia has an antiproliferative activity on tumor cell line SK-N-SH and modifies the microtubule network
    • Barbier, P.; Guise, S.; Huitorel, P.; Amade, P.; Pesando, D.; Briand, C.; Peyrot, V. Caulerpenyne from Caulerpa taxifolia has an antiproliferative activity on tumor cell line SK-N-SH and modifies the microtubule network. Life Sci. 2001, 70, 415-429.
    • (2001) Life Sci. , vol.70 , pp. 415-429
    • Barbier, P.1    Guise, S.2    Huitorel, P.3    Amade, P.4    Pesando, D.5    Briand, C.6    Peyrot, V.7
  • 100
    • 0025183762 scopus 로고
    • Binding of dolastatin 10 to tubulin at a distinct site for peptide antimitotic agents near the exchangeable nucleotide and vinca alkaloid sites
    • Bai, R.L.; Pettit, G.R.; Hamel, E. Binding of dolastatin 10 to tubulin at a distinct site for peptide antimitotic agents near the exchangeable nucleotide and vinca alkaloid sites. J. Biol. Chem. 1990, 265, 17141-17149.
    • (1990) J. Biol. Chem. , vol.265 , pp. 17141-17149
    • Bai, R.L.1    Pettit, G.R.2    Hamel, E.3
  • 101
    • 0026748367 scopus 로고
    • Dolastatin 15, a potent antimitotic depsipeptide derived from Dolabella auricularia. Interaction with tubulin and effects of cellular microtubules
    • Bai, R.; Friedman, S.J.; Pettit, G.R.; Hamel, E. Dolastatin 15, a potent antimitotic depsipeptide derived from Dolabella auricularia. Interaction with tubulin and effects of cellular microtubules. Biochem. Pharmacol. 1992, 43, 2637-2645.
    • (1992) Biochem. Pharmacol. , vol.43 , pp. 2637-2645
    • Bai, R.1    Friedman, S.J.2    Pettit, G.R.3    Hamel, E.4
  • 102
    • 0141447346 scopus 로고    scopus 로고
    • Dolastatin 15 binds in the vinca domain of tubulin as demonstrated by Hummel-Dreyer chromatography
    • Cruz-Monserrate, Z.; Mullaney, J.T.; Harran, P.G.; Pettit, G.R.; Hamel, E. Dolastatin 15 binds in the vinca domain of tubulin as demonstrated by Hummel-Dreyer chromatography. Eur. J. Biochem. 2003, 270, 3822-3828.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 3822-3828
    • Cruz-Monserrate, Z.1    Mullaney, J.T.2    Harran, P.G.3    Pettit, G.R.4    Hamel, E.5
  • 105
    • 0021054028 scopus 로고
    • Inhibition of bovine brain microtubule assembly in vitro by stypoldione
    • O'Brien, E.T.; Jacobs, R.S.; Wilson, L. Inhibition of bovine brain microtubule assembly in vitro by stypoldione. Mol. Pharmacol. 1983, 24, 493-499.
    • (1983) Mol. Pharmacol. , vol.24 , pp. 493-499
    • O'Brien, E.T.1    Jacobs, R.S.2    Wilson, L.3
  • 106
    • 0021054029 scopus 로고
    • Effect of stypoldione on cell cycle progression, DNA and protein synthesis, and cell division in cultured sea urchin embryos
    • White, S.J.; Jacobs, R.S. Effect of stypoldione on cell cycle progression, DNA and protein synthesis, and cell division in cultured sea urchin embryos. Mol. Pharmacol. 1983, 24, 500-508.
    • (1983) Mol. Pharmacol. , vol.24 , pp. 500-508
    • White, S.J.1    Jacobs, R.S.2
  • 107
    • 0024411430 scopus 로고
    • Selective inhibition of cytokinesis in sea urchin embryos by low concentrations of stypoldione, a marine natural product that reacts with sulfhydryl groups
    • O'Brien, E.T.; Asai, D.J.; Jacobs, R.S.; Wilson, L. Selective inhibition of cytokinesis in sea urchin embryos by low concentrations of stypoldione, a marine natural product that reacts with sulfhydryl groups. Mol. Pharmacol. 1989, 35, 635-642.
    • (1989) Mol. Pharmacol. , vol.35 , pp. 635-642
    • O'Brien, E.T.1    Asai, D.J.2    Jacobs, R.S.3    Wilson, L.4
  • 108
    • 0002302562 scopus 로고
    • Mammalian fertilization
    • Knobil, E., Neil, J.; Eds.; Raven press: New York, NY, USA
    • Yanagimachi, R. Mammalian fertilization. In The Physiology of Reproduction; Knobil, E., Neil, J.; Eds.; Raven press: New York, NY, USA, 1994; pp. 189-317.
    • (1994) The Physiology of Reproduction , pp. 189-317
    • Yanagimachi, R.1
  • 110
    • 0025590570 scopus 로고
    • Why life histories evolve differently in the sea
    • Stratmhann, R.R. Why life histories evolve differently in the sea. Soc. Integ. Comp. Biol. 1990, 30, 197-207.
    • (1990) Soc. Integ. Comp. Biol. , vol.30 , pp. 197-207
    • Stratmhann, R.R.1
  • 111
    • 0028535882 scopus 로고
    • Sperm activation in species with external fertilisation
    • Tosti, E. Sperm activation in species with external fertilisation. Zygote 1994, 2, 359-361.
    • (1994) Zygote , vol.2 , pp. 359-361
    • Tosti, E.1
  • 113
    • 33846586935 scopus 로고    scopus 로고
    • Ectoplasmic specialization: A friend or a foe of spermatogenesis?
    • Yan, H.H.; Mruk, D.D.; Lee, W.M.; Cheng, C.Y. Ectoplasmic specialization: a friend or a foe of spermatogenesis? Bioessays 2007, 29, 36-48.
    • (2007) Bioessays , vol.29 , pp. 36-48
    • Yan, H.H.1    Mruk, D.D.2    Lee, W.M.3    Cheng, C.Y.4
  • 114
    • 0036788073 scopus 로고    scopus 로고
    • Cell junction dynamics in the testis: Sertoli-germ cell interactions and male contraceptive development
    • Cheng, C.Y.; Mruk, D.D. Cell junction dynamics in the testis: Sertoli-germ cell interactions and male contraceptive development. Physiol. Rev. 2002, 82, 825-874.
    • (2002) Physiol. Rev. , vol.82 , pp. 825-874
    • Cheng, C.Y.1    Mruk, D.D.2
  • 115
    • 3242811705 scopus 로고    scopus 로고
    • Ectoplasmic specialization, a testis-specific cell-cell actin-based adherens junction type: Is this a potential target for male contraceptive development?
    • Lee, N.P.; Cheng, C.Y. Ectoplasmic specialization, a testis-specific cell-cell actin-based adherens junction type: is this a potential target for male contraceptive development? Hum. Reprod. Update 2004, 10, 349-369.
    • (2004) Hum. Reprod. Update , vol.10 , pp. 349-369
    • Lee, N.P.1    Cheng, C.Y.2
  • 116
    • 23844478817 scopus 로고    scopus 로고
    • AF-2364 [1-(2,4-dichlorobenzyl)-1H-indazole-3-carbohydrazide] is a potential male contraceptive: A review of recent data
    • Cheng, C.Y.; Mruk, D.; Silvestrini, B.; Bonanomi, M.; Wong, C.H.; Siu, M.K.; Lee, N.P.; Lui, W.Y.; Mo, M.Y. AF-2364 [1-(2,4-dichlorobenzyl)-1H- indazole-3-carbohydrazide] is a potential male contraceptive: a review of recent data. Contraception 2005, 72, 251-261.
    • (2005) Contraception , vol.72 , pp. 251-261
    • Cheng, C.Y.1    Mruk, D.2    Silvestrini, B.3    Bonanomi, M.4    Wong, C.H.5    Siu, M.K.6    Lee, N.P.7    Lui, W.Y.8    Mo, M.Y.9
  • 117
    • 0025753031 scopus 로고
    • Microtubule polarity in Sertoli cells: A model for microtubule-based spermatid transport
    • Redenbach, D.M.; Vogl, A.W. Microtubule polarity in Sertoli cells: a model for microtubule-based spermatid transport. Eur. J. Cell Biol. 1991, 54, 277-290.
    • (1991) Eur. J. Cell Biol. , vol.54 , pp. 277-290
    • Redenbach, D.M.1    Vogl, A.W.2
  • 118
    • 0027082608 scopus 로고
    • Binding between mammalian spermatidectoplasmic specialization complexes and microtubules
    • Redenbach, D.M.; Boekelheide, K.; Vogl, A.W. Binding between mammalian spermatidectoplasmic specialization complexes and microtubules. Eur. J. Cell Biol. 1992, 59, 433-448.
    • (1992) Eur. J. Cell Biol. , vol.59 , pp. 433-448
    • Redenbach, D.M.1    Boekelheide, K.2    Vogl, A.W.3
  • 119
    • 0033021426 scopus 로고    scopus 로고
    • Spermatid translocation in the rat seminiferous epithelium: Coupling membrane trafficking machinery to a junction plaque
    • Beach, S.F.; Vogl, A.W. Spermatid translocation in the rat seminiferous epithelium: coupling membrane trafficking machinery to a junction plaque. Biol. Reprod. 1999, 60, 1036-1046.
    • (1999) Biol. Reprod. , vol.60 , pp. 1036-1046
    • Beach, S.F.1    Vogl, A.W.2
  • 120
    • 0033945047 scopus 로고    scopus 로고
    • Dynein and plus-end microtubule-dependent motors are associated with specialized Sertoli cell junction plaques (ectoplasmic specializations)
    • Guttman, J.A.; Kimel, G.H.; Vogl, A.W. Dynein and plus-end microtubule-dependent motors are associated with specialized Sertoli cell junction plaques (ectoplasmic specializations). J. Cell. Sci. 2000, 113 (Pt 12), 2167-2176.
    • (2000) J. Cell. Sci. , vol.113 , Issue.PART 12 , pp. 2167-2176
    • Guttman, J.A.1    Kimel, G.H.2    Vogl, A.W.3
  • 121
  • 122
    • 0024844354 scopus 로고
    • Preparation of microtubules from rat liver and testis: Cytoplasmic dynein is a major microtubule associated protein
    • Collins, C.A.; Vallee, R.B. Preparation of microtubules from rat liver and testis: cytoplasmic dynein is a major microtubule associated protein. Cell Motil. Cytoskeleton 1989, 14, 491-500.
    • (1989) Cell Motil. Cytoskeleton , vol.14 , pp. 491-500
    • Collins, C.A.1    Vallee, R.B.2
  • 123
    • 0026538425 scopus 로고
    • Distribution of the microtubule-dependent motors cytoplasmic dynein and kinesin in rat testis
    • Hall, E.S.; Eveleth, J.; Jiang, C.; Redenbach, D.M.; Boekelheide, K. Distribution of the microtubule-dependent motors cytoplasmic dynein and kinesin in rat testis. Biol. Reprod. 1992, 46, 817-828.
    • (1992) Biol. Reprod. , vol.46 , pp. 817-828
    • Hall, E.S.1    Eveleth, J.2    Jiang, C.3    Redenbach, D.M.4    Boekelheide, K.5
  • 124
    • 0032981916 scopus 로고    scopus 로고
    • Rat testis motor proteins associated with spermatid translocation (dynein) and spermatid flagella (kinesin-II)
    • Miller, M.G.; Mulholland, D.J.; Vogl, A.W. Rat testis motor proteins associated with spermatid translocation (dynein) and spermatid flagella (kinesin-II). Biol. Reprod. 1999, 60, 1047-1056.
    • (1999) Biol. Reprod. , vol.60 , pp. 1047-1056
    • Miller, M.G.1    Mulholland, D.J.2    Vogl, A.W.3
  • 125
    • 0034090944 scopus 로고    scopus 로고
    • Evidence that actin and myosin are involved in the poleward flux of tubulin in metaphase kinetochore microtubules of crane-fly spermatocytes
    • Silverman-Gavrila, R.V.; Forer, A. Evidence that actin and myosin are involved in the poleward flux of tubulin in metaphase kinetochore microtubules of crane-fly spermatocytes. J. Cell. Sci. 2000, 113 (Pt 4), 597-609.
    • (2000) J. Cell. Sci. , vol.113 , Issue.PART 4 , pp. 597-609
    • Silverman-Gavrila, R.V.1    Forer, A.2
  • 126
    • 0033035201 scopus 로고    scopus 로고
    • First evidence of some dinoflagellates reducing male copepod fertilization capacity
    • Ianora, A.; Miralto, A.; Buttino, I.; Romano, G.; Poulet, S.A. First evidence of some dinoflagellates reducing male copepod fertilization capacity. Limnol. Oceanogr. 1999, 44, 147-153.
    • (1999) Limnol. Oceanogr. , vol.44 , pp. 147-153
    • Ianora, A.1    Miralto, A.2    Buttino, I.3    Romano, G.4    Poulet, S.A.5
  • 127
    • 0021907825 scopus 로고
    • A quantitative description of flagellar movement in golden hamster spermatozoa
    • Ishijima, S.; Mohri, H. A quantitative description of flagellar movement in golden hamster spermatozoa. J. Exp. Biol. 1985, 114, 463-475.
    • (1985) J. Exp. Biol. , vol.114 , pp. 463-475
    • Ishijima, S.1    Mohri, H.2
  • 128
    • 0024597141 scopus 로고
    • Maturation and capacitation of mammalian spermatozoa
    • Mohri, H.; Awano, M.; Ishijima, S. Maturation and capacitation of mammalian spermatozoa. Prog. Clin. Biol. Res. 1989, 294, 53-62.
    • (1989) Prog. Clin. Biol. Res. , vol.294 , pp. 53-62
    • Mohri, H.1    Awano, M.2    Ishijima, S.3
  • 129
    • 0027361855 scopus 로고
    • Role of tubulin and dynein in spermatozoan motility
    • Mohri, H. Role of tubulin and dynein in spermatozoan motility. Mol. Reprod. Dev. 1993, 36, 221-223.
    • (1993) Mol. Reprod. Dev. , vol.36 , pp. 221-223
    • Mohri, H.1
  • 130
    • 0015188644 scopus 로고    scopus 로고
    • Adenosine triphosphate-induced sliding of tubules in trypsin-treated flagella of sea-urchin sperm
    • Summers, K.E.; Gibbons, I.R. Adenosine triphosphate-induced sliding of tubules in trypsin-treated flagella of sea-urchin sperm. Proc. Natl. Acad. Sci. USA 1971, 68, 3092-3096.
    • Proc. Natl. Acad. Sci. USA 1971 , vol.68 , pp. 3092-3096
    • Summers, K.E.1    Gibbons, I.R.2
  • 131
    • 33846439765 scopus 로고    scopus 로고
    • F-actin involvement in guinea pig sperm motility
    • Azamar, Y.; Uribe, S.; Mujica, A. F-actin involvement in guinea pig sperm motility. Mol. Reprod. Dev. 2007, 74, 312-320.
    • (2007) Mol. Reprod. Dev. , vol.74 , pp. 312-320
    • Azamar, Y.1    Uribe, S.2    Mujica, A.3
  • 132
    • 0043269914 scopus 로고    scopus 로고
    • Bioactive aldehydes from diatoms block the fertilization current in ascidian oocytes
    • Tosti, E.; Romano, G.; Buttino, I.; Cuomo, A.; Ianora, A.; Miralto, A. Bioactive aldehydes from diatoms block the fertilization current in ascidian oocytes. Mol. Reprod. Dev. 2003, 66, 72-80.
    • (2003) Mol. Reprod. Dev. , vol.66 , pp. 72-80
    • Tosti, E.1    Romano, G.2    Buttino, I.3    Cuomo, A.4    Ianora, A.5    Miralto, A.6
  • 133
    • 0037076391 scopus 로고    scopus 로고
    • A flagellar K(+)-dependent Na(+)/Ca(2+) exchanger keeps Ca(2+) low in sea urchin spermatozoa
    • Su, Y.H.; Vacquier, V.D. A flagellar K(+)-dependent Na(+)/Ca(2+) exchanger keeps Ca(2+) low in sea urchin spermatozoa. Proc. Natl. Acad. Sci. USA 2002, 99, 6743-6748.
    • Proc. Natl. Acad. Sci. USA 2002 , vol.99 , pp. 6743-6748
    • Su, Y.H.1    Vacquier, V.D.2
  • 134
    • 0016247865 scopus 로고
    • Calcium ion regulation of flagellar beat symmetry in reactivated sea urchin spermatozoa
    • Brokaw, C.J.; Josslin, R.; Bobrow, L. Calcium ion regulation of flagellar beat symmetry in reactivated sea urchin spermatozoa. Biochem. Biophys. Res. Commun. 1974, 58, 795-800.
    • (1974) Biochem. Biophys. Res. Commun. , vol.58 , pp. 795-800
    • Brokaw, C.J.1    Josslin, R.2    Bobrow, L.3
  • 135
    • 0018584031 scopus 로고
    • Calcium-induced asymmetrical beating of triton-demembranated sea urchin sperm flagella
    • Brokaw, C.J. Calcium-induced asymmetrical beating of triton-demembranated sea urchin sperm flagella. J. Cell Biol. 1979, 82, 401-411.
    • (1979) J. Cell Biol. , vol.82 , pp. 401-411
    • Brokaw, C.J.1
  • 136
    • 0018843689 scopus 로고
    • Calcium-induced quiescence in reactivated sea urchin sperm
    • Gibbons, B.H.; Gibbons, I.R. Calcium-induced quiescence in reactivated sea urchin sperm. J. Cell Biol. 1980, 84, 13-27.
    • (1980) J. Cell Biol. , vol.84 , pp. 13-27
    • Gibbons, B.H.1    Gibbons, I.R.2
  • 137
    • 34447639411 scopus 로고    scopus 로고
    • Calcium and other ion dynamics during gamete maturation and fertilization
    • Boni, R.; Gualtieri, R.; Talevi, R.; Tosti, E. Calcium and other ion dynamics during gamete maturation and fertilization. Theriogenology 2007, 68 (Suppl 1), S156-S164.
    • (2007) Theriogenology , vol.68 , Issue.SUPPL. 1
    • Boni, R.1    Gualtieri, R.2    Talevi, R.3    Tosti, E.4
  • 139
    • 0022180825 scopus 로고
    • Processes controlling sperm-egg fusion
    • Monroy, A. Processes controlling sperm-egg fusion. Eur. J. Biochem. 1985, 152, 51-56.
    • (1985) Eur. J. Biochem. , vol.152 , pp. 51-56
    • Monroy, A.1
  • 140
  • 142
    • 0031990354 scopus 로고    scopus 로고
    • Developmental roles of nuclear complex factors released during oocyte maturation in the ascidians Halocynthia roretzi and Boltenia villosa
    • Bates, W.R.; Nishida, H. Developmental roles of nuclear complex factors released during oocyte maturation in the ascidians Halocynthia roretzi and Boltenia villosa. Zoolog. Sci. 1998, 15, 69-76.
    • (1998) Zoolog. Sci. , vol.15 , pp. 69-76
    • Bates, W.R.1    Nishida, H.2
  • 143
    • 0004284825 scopus 로고    scopus 로고
    • 2nd ed.; Cambridge University Press: Cambridge, UK
    • Elder, K.; Dale, B. In Vitro Fertilization, 2nd ed.; Cambridge University Press: Cambridge, UK, 2000.
    • (2000) In Vitro Fertilization
    • Elder, K.1    Dale, B.2
  • 144
    • 27544472085 scopus 로고    scopus 로고
    • Stops and starts in mammalian oocytes: Recent advances in understanding the regulation of meiotic arrest and oocyte maturation
    • Mehlmann, L.M. Stops and starts in mammalian oocytes: recent advances in understanding the regulation of meiotic arrest and oocyte maturation. Reproduction 2005, 130, 791-799.
    • (2005) Reproduction , vol.130 , pp. 791-799
    • Mehlmann, L.M.1
  • 145
    • 0033630892 scopus 로고    scopus 로고
    • Molecular mechanisms of the initiation of oocyte maturation: General and species-specific aspects
    • Yamashita, M.; Mita, K.; Yoshida, N.; Kondo, T. Molecular mechanisms of the initiation of oocyte maturation: general and species-specific aspects. Prog. Cell Cycle Res. 2000, 4, 115-129.
    • (2000) Prog. Cell Cycle Res. , vol.4 , pp. 115-129
    • Yamashita, M.1    Mita, K.2    Yoshida, N.3    Kondo, T.4
  • 146
    • 17644381627 scopus 로고    scopus 로고
    • Calcium currents correlate with oocyte maturation during the reproductive cycle in Octopus vulgaris
    • Cuomo, A.; Di Cristo, C.; Paolucci, M.; Di Cosmo, A.; Tosti, E. Calcium currents correlate with oocyte maturation during the reproductive cycle in Octopus vulgaris. J. Exp. Zoolog. A Comp. Exp. Biol. 2005, 303, 193-202.
    • (2005) J. Exp. Zoolog. A Comp. Exp. Biol. , vol.303 , pp. 193-202
    • Cuomo, A.1    Di Cristo, C.2    Paolucci, M.3    Di Cosmo, A.4    Tosti, E.5
  • 147
    • 33644866860 scopus 로고    scopus 로고
    • Ca2+ and Na+ current patterns during oocyte maturation, fertilization, and early developmental stages of Ciona intestinalis
    • Cuomo, A.; Silvestre, F.; De Santis, R.; Tosti, E. Ca2+ and Na+ current patterns during oocyte maturation, fertilization, and early developmental stages of Ciona intestinalis. Mol. Reprod. Dev. 2006, 73, 501-511.
    • (2006) Mol. Reprod. Dev. , vol.73 , pp. 501-511
    • Cuomo, A.1    Silvestre, F.2    De Santis, R.3    Tosti, E.4
  • 148
    • 33745102744 scopus 로고    scopus 로고
    • Calcium ion currents mediating oocyte maturation events
    • Tosti, E. Calcium ion currents mediating oocyte maturation events. Reprod. Biol. Endocrinol. 2006, 4, 26.
    • (2006) Reprod. Biol. Endocrinol. , vol.4 , pp. 26
    • Tosti, E.1
  • 149
    • 33846007706 scopus 로고    scopus 로고
    • Maternally derived transcripts: Identification and characterisation during oocyte maturation and early cleavage
    • Cui, X.S.; Kim, N.H. Maternally derived transcripts: identification and characterisation during oocyte maturation and early cleavage. Reprod. Fertil. Dev. 2007, 19, 25-34.
    • (2007) Reprod. Fertil. Dev. , vol.19 , pp. 25-34
    • Cui, X.S.1    Kim, N.H.2
  • 150
    • 70349269882 scopus 로고    scopus 로고
    • Ion current activity and molecules modulating maturation and growth stages of ascidian (Ciona intestinalis) oocytes
    • Silvestre, F.; Cuomo, A.; Tosti, E. Ion current activity and molecules modulating maturation and growth stages of ascidian (Ciona intestinalis) oocytes. Mol. Reprod. Dev. 2009, 76, 1084-1093.
    • (2009) Mol. Reprod. Dev. , vol.76 , pp. 1084-1093
    • Silvestre, F.1    Cuomo, A.2    Tosti, E.3
  • 151
    • 31544453323 scopus 로고    scopus 로고
    • Establishment of animal-vegetal polarity during maturation in ascidian oocytes
    • Prodon, F.; Chenevert, J.; Sardet, C. Establishment of animal-vegetal polarity during maturation in ascidian oocytes. Dev. Biol. 2006, 290, 297-311.
    • (2006) Dev. Biol. , vol.290 , pp. 297-311
    • Prodon, F.1    Chenevert, J.2    Sardet, C.3
  • 152
    • 0027378136 scopus 로고
    • Ectopic spindle assembly during maturation of Xenopus oocytes: Evidence for functional polarization of the oocyte cortex
    • Gard, D.L. Ectopic spindle assembly during maturation of Xenopus oocytes: evidence for functional polarization of the oocyte cortex. Dev. Biol. 1993, 159, 298-310.
    • (1993) Dev. Biol. , vol.159 , pp. 298-310
    • Gard, D.L.1
  • 153
    • 14044261737 scopus 로고    scopus 로고
    • RNA localization mechanisms in oocytes
    • Kloc, M.; Etkin, L.D. RNA localization mechanisms in oocytes. J. Cell. Sci. 2005, 118, 269-282.
    • (2005) J. Cell. Sci. , vol.118 , pp. 269-282
    • Kloc, M.1    Etkin, L.D.2
  • 154
    • 0028229608 scopus 로고
    • Redistribution of cytoplasmic components during germinal vesicle breakdown in starfish oocytes
    • Terasaki, M. Redistribution of cytoplasmic components during germinal vesicle breakdown in starfish oocytes. J. Cell. Sci. 1994, 107 (Pt 7), 1797-1805.
    • (1994) J. Cell. Sci. , vol.107 , Issue.PART 7 , pp. 1797-1805
    • Terasaki, M.1
  • 155
    • 0037371466 scopus 로고    scopus 로고
    • Dynamics of the endoplasmic reticulum during early development of Drosophila melanogaster
    • Bobinnec, Y.; Marcaillou, C.; Morin, X.; Debec, A. Dynamics of the endoplasmic reticulum during early development of Drosophila melanogaster. Cell Motil. Cytoskeleton 2003, 54, 217-225.
    • (2003) Cell Motil. Cytoskeleton , vol.54 , pp. 217-225
    • Bobinnec, Y.1    Marcaillou, C.2    Morin, X.3    Debec, A.4
  • 156
    • 0034912353 scopus 로고    scopus 로고
    • Translocation of active mitochondria during pig oocyte maturation, fertilization and early embryo development in vitro
    • Sun, Q.Y.; Wu, G.M.; Lai, L.; Park, K.W.; Cabot, R.; Cheong, H.T.; Day, B.N.; Prather, R.S.; Schatten, H. Translocation of active mitochondria during pig oocyte maturation, fertilization and early embryo development in vitro. Reproduction 2001, 122, 155-163.
    • (2001) Reproduction , vol.122 , pp. 155-163
    • Sun, Q.Y.1    Wu, G.M.2    Lai, L.3    Park, K.W.4    Cabot, R.5    Cheong, H.T.6    Day, B.N.7    Prather, R.S.8    Schatten, H.9
  • 157
    • 0024207258 scopus 로고
    • Microtubules are required for centrosome expansion and positioning while microfilaments are required for centrosome separation in sea urchin eggs during fertilization and mitosis
    • DOI 10.1002/cm.970110404
    • Schatten, H.; Walter, M.; Biessmann, H.; Schatten, G. Microtubules are required for centrosome expansion and positioning while microfilaments are required for centrosome separation in sea urchin eggs during fertilization and mitosis. Cell Motil. Cytoskeleton 1988, 11, 248-259. (Pubitemid 19020073)
    • (1988) Cell Motility and the Cytoskeleton , vol.11 , Issue.4 , pp. 248-259
    • Schatten, H.1    Walter, M.2    Biessmann, H.3    Schatten, G.4
  • 158
    • 17444421190 scopus 로고    scopus 로고
    • The role of microfilaments in early meiotic maturation of mouse oocytes
    • DOI 10.1017/S1431927605050154
    • Calarco, P.G. The role of microfilaments in early meiotic maturation of mouse oocytes. Microsc. Microanal. 2005, 11, 146-153. (Pubitemid 40534808)
    • (2005) Microscopy and Microanalysis , vol.11 , Issue.2 , pp. 146-153
    • Calarco, P.G.1
  • 159
    • 0036746622 scopus 로고    scopus 로고
    • Cortical granule translocation is microfilament mediated and linked to meiotic maturation in the sea urchin oocyte
    • Wessel, G.M.; Conner, S.D.; Berg, L. Cortical granule translocation is microfilament mediated and linked to meiotic maturation in the sea urchin oocyte. Development 2002, 129, 4315-4325.
    • (2002) Development , vol.129 , pp. 4315-4325
    • Wessel, G.M.1    Conner, S.D.2    Berg, L.3
  • 160
    • 0032145734 scopus 로고    scopus 로고
    • Involvement of the cytoskeleton in the movement of cortical granules during oocyte maturation, and cortical granule anchoring in mouse eggs
    • Connors, S.A.; Kanatsu-Shinohara, M.; Schultz, R.M.; Kopf, G.S. Involvement of the cytoskeleton in the movement of cortical granules during oocyte maturation, and cortical granule anchoring in mouse eggs. Dev. Biol. 1998, 200, 103-115.
    • (1998) Dev. Biol. , vol.200 , pp. 103-115
    • Connors, S.A.1    Kanatsu-Shinohara, M.2    Schultz, R.M.3    Kopf, G.S.4
  • 161
    • 39149121143 scopus 로고    scopus 로고
    • Interactions between chromosomes, microfilaments and microtubules revealed by the study of small GTPases in a big cell, the vertebrate oocyte
    • Verlhac, M.H.; Dumont, J. Interactions between chromosomes, microfilaments and microtubules revealed by the study of small GTPases in a big cell, the vertebrate oocyte. Mol. Cell. Endocrinol. 2008, 282, 12-17.
    • (2008) Mol. Cell. Endocrinol. , vol.282 , pp. 12-17
    • Verlhac, M.H.1    Dumont, J.2
  • 162
    • 1942521613 scopus 로고    scopus 로고
    • Formation and function of the polar body contractile ring in Spisula
    • Pielak, R.M.; Gaysinskaya, V.A.; Cohen, W.D. Formation and function of the polar body contractile ring in Spisula. Dev. Biol. 2004, 269, 421-432.
    • (2004) Dev. Biol. , vol.269 , pp. 421-432
    • Pielak, R.M.1    Gaysinskaya, V.A.2    Cohen, W.D.3
  • 163
    • 0034651945 scopus 로고    scopus 로고
    • Premeiotic aster as a device to anchor the germinal vesicle to the cell surface of the presumptive animal pole in starfish oocytes
    • Miyazaki, A.; Kamitsubo, E.; Nemoto, S.I. Premeiotic aster as a device to anchor the germinal vesicle to the cell surface of the presumptive animal pole in starfish oocytes. Dev. Biol. 2000, 218, 161-171.
    • (2000) Dev. Biol. , vol.218 , pp. 161-171
    • Miyazaki, A.1    Kamitsubo, E.2    Nemoto, S.I.3
  • 164
    • 0026087534 scopus 로고
    • Organization, nucleation, and acetylation of microtubules in Xenopus laevis oocytes: A study by confocal immunofluorescence microscopy
    • Gard, D.L. Organization, nucleation, and acetylation of microtubules in Xenopus laevis oocytes: a study by confocal immunofluorescence microscopy. Dev. Biol. 1991, 143, 346-362.
    • (1991) Dev. Biol. , vol.143 , pp. 346-362
    • Gard, D.L.1
  • 165
    • 14844299802 scopus 로고    scopus 로고
    • Role of microtubules and centrosomes in the eccentric relocation of the germinal vesicle upon meiosis reinitiation in sea-cucumber oocytes
    • DOI 10.1016/j.ydbio.2005.01.026
    • Miyazaki, A.; Kato, K.H.; Nemoto, S. Role of microtubules and centrosomes in the eccentric relocation of the germinal vesicle upon meiosis reinitiation in sea-cucumber oocytes. Dev. Biol. 2005, 280, 237-247. (Pubitemid 40342756)
    • (2005) Developmental Biology , vol.280 , Issue.1 , pp. 237-247
    • Miyazaki, A.1    Kato, K.H.2    Nemoto, S.-I.3
  • 166
    • 34447575736 scopus 로고    scopus 로고
    • From oocyte to 16-cell stage: Cytoplasmic and cortical reorganizations that pattern the ascidian embryo
    • DOI 10.1002/dvdy.21136
    • Sardet, C.; Paix, A.; Prodon, F.; Dru, P.; Chenevert, J. From oocyte to 16-cell stage: cytoplasmic and cortical reorganizations that pattern the ascidian embryo. Dev Dyn. 2007, 236, 1716-1731. (Pubitemid 47076006)
    • (2007) Developmental Dynamics , vol.236 , Issue.7 , pp. 1716-1731
    • Sardet, C.1    Paix, A.2    Prodon, F.3    Dru, P.4    Chenevert, J.5
  • 167
    • 18844367189 scopus 로고    scopus 로고
    • Kinesin-1 mediates translocation of the meiotic spindle to the oocyte cortex through KCA-1, a novel cargo adapter
    • Yang, H.Y.; Mains, P.E.; McNally, F.J. Kinesin-1 mediates translocation of the meiotic spindle to the oocyte cortex through KCA-1, a novel cargo adapter. J. Cell Biol. 2005, 169, 447-457.
    • (2005) J. Cell Biol. , vol.169 , pp. 447-457
    • Yang, H.Y.1    Mains, P.E.2    McNally, F.J.3
  • 168
    • 0023775713 scopus 로고
    • Micromanipulation studies of the asymmetric positioning of the maturation spindle in Chaetopterus sp. oocytes: I. Anchorage of the spindle to the cortex and migration of a displaced spindle
    • Lutz, D.A.; Hamaguchi, Y.; Inoue, S. Micromanipulation studies of the asymmetric positioning of the maturation spindle in Chaetopterus sp. oocytes: I. Anchorage of the spindle to the cortex and migration of a displaced spindle. Cell Motil. Cytoskeleton 1988, 11, 83-96.
    • (1988) Cell Motil. Cytoskeleton , vol.11 , pp. 83-96
    • Lutz, D.A.1    Hamaguchi, Y.2    Inoue, S.3
  • 169
    • 4644326930 scopus 로고    scopus 로고
    • A microtubule-binding myosin required for nuclear anchoring and spindle assembly
    • Weber, K.L.; Sokac, A.M.; Berg, J.S.; Cheney, R.E.; Bement, W.M. A microtubule-binding myosin required for nuclear anchoring and spindle assembly. Nature 2004, 431, 325-329.
    • (2004) Nature , vol.431 , pp. 325-329
    • Weber, K.L.1    Sokac, A.M.2    Berg, J.S.3    Cheney, R.E.4    Bement, W.M.5
  • 170
    • 0036902809 scopus 로고    scopus 로고
    • Polar body formation: New rules for asymmetric divisions
    • Maro, B.; Verlhac, M.H. Polar body formation: new rules for asymmetric divisions. Nat. Cell Biol. 2002, 4, E281-E283.
    • (2002) Nat. Cell Biol. , vol.4
    • Maro, B.1    Verlhac, M.H.2
  • 171
    • 0034088666 scopus 로고    scopus 로고
    • Microfilament stabilization by Jasplakinolide arrests oocyte maturation, cortical granule exocytosis, sperm incorporation cone resorption, and cell- Cycle progression, but not DNA replication, during fertilization in mice
    • DOI 10.1002/(SICI)1098-2795(200005)56:1<89::AID-MRD11>3.0.CO;2-I
    • Terada, Y.; Simerly, C.; Schatten, G. Microfilament stabilization by jasplakinolide arrests oocyte maturation, cortical granule exocytosis, sperm incorporation cone resorption, and cell-cycle progression, but not DNA replication, during fertilization in mice. Mol. Reprod. Dev. 2000, 56, 89-98. (Pubitemid 30193866)
    • (2000) Molecular Reproduction and Development , vol.56 , Issue.1 , pp. 89-98
    • Terada, Y.1    Simerly, C.2    Schatten, G.3
  • 172
    • 0029145506 scopus 로고
    • Localization of microfilaments during oocyte maturation of golden hamster
    • Terada, Y.; Fukaya, T.; Yajima, A. Localization of microfilaments during oocyte maturation of golden hamster. Mol. Reprod. Dev. 1995, 41, 486-492.
    • (1995) Mol. Reprod. Dev. , vol.41 , pp. 486-492
    • Terada, Y.1    Fukaya, T.2    Yajima, A.3
  • 173
    • 0034136459 scopus 로고    scopus 로고
    • The distribution and requirements of microtubules and microfilaments in bovine oocytes during in vitro maturation
    • Kim, N.H.; Cho, S.K.; Choi, S.H.; Kim, E.Y.; Park, S.P.; Lim, J.H. The distribution and requirements of microtubules and microfilaments in bovine oocytes during in vitro maturation. Zygote 2000, 8, 25-32.
    • (2000) Zygote , vol.8 , pp. 25-32
    • Kim, N.H.1    Cho, S.K.2    Choi, S.H.3    Kim, E.Y.4    Park, S.P.5    Lim, J.H.6
  • 174
    • 0031666956 scopus 로고    scopus 로고
    • Microtubule and microfilament organization in maturing human oocytes
    • Kim, N.H.; Chung, H.M.; Cha, K.Y.; Chung, K.S. Microtubule and microfilament organization in maturing human oocytes. Hum Reprod. 1998, 13, 2217-2222.
    • (1998) Hum Reprod. , vol.13 , pp. 2217-2222
    • Kim, N.H.1    Chung, H.M.2    Cha, K.Y.3    Chung, K.S.4
  • 175
    • 0022457826 scopus 로고
    • Influence of cytochalasin B on oocyte maturation in Xenopus laevis
    • DOI 10.1016/0045-6039(86)90065-5
    • Ryabova, L.V.; Betina, M.I.; Vassetzky, S.G. Influence of cytochalasin B on oocyte maturation in Xenopus laevis. Cell Differ. 1986, 19, 89-96. (Pubitemid 16041648)
    • (1986) Cell Differentiation , vol.19 , Issue.2 , pp. 89-96
    • Ryabova, L.V.1    Betina, M.I.2    Vassetzky, S.G.3
  • 176
    • 0029240344 scopus 로고
    • F-actin is required for spindle anchoring and rotation in Xenopus oocytes: A re-examination of the effects of cytochalasin B on oocyte maturation
    • Gard, D.L.; Cha, B.J.; Roeder, A.D. F-actin is required for spindle anchoring and rotation in Xenopus oocytes: a re-examination of the effects of cytochalasin B on oocyte maturation. Zygote 1995, 3, 17-26.
    • (1995) Zygote , vol.3 , pp. 17-26
    • Gard, D.L.1    Cha, B.J.2    Roeder, A.D.3
  • 178
    • 67651089485 scopus 로고    scopus 로고
    • Guanine nucleotides in the meiotic maturation of starfish oocytes: Regulation of the actin cytoskeleton and of Ca(2+) signaling
    • Kyozuka, K.; Chun, J.T.; Puppo, A.; Gragnaniello, G.; Garante, E.; Santella, L. Guanine nucleotides in the meiotic maturation of starfish oocytes: regulation of the actin cytoskeleton and of Ca(2+) signaling. PLoS One 2009, 4, e6296.
    • (2009) PLoS One , vol.4
    • Kyozuka, K.1    Chun, J.T.2    Puppo, A.3    Gragnaniello, G.4    Garante, E.5    Santella, L.6
  • 179
    • 21344467001 scopus 로고    scopus 로고
    • Seven new meroditerpenoids, from the marine sponge Strongylophora strongylata, that inhibited the maturation of starfish oocytes
    • Liu, H.; Namikoshi, M.; Akano, K.; Kobayashi, H.; Nagai, H.; Yao, X. Seven new meroditerpenoids, from the marine sponge Strongylophora strongylata, that inhibited the maturation of starfish oocytes. J. Asian Nat. Prod. Res. 2005, 7, 661-670.
    • (2005) J. Asian Nat. Prod. Res. , vol.7 , pp. 661-670
    • Liu, H.1    Namikoshi, M.2    Akano, K.3    Kobayashi, H.4    Nagai, H.5    Yao, X.6
  • 180
    • 0024956595 scopus 로고
    • La microinjection d'acide okadaique, un inhibiteur de phosphoproteine phosphatase, induit la maturation de l'ovocyte de l'etoile de mer
    • Pondaven, P.; Meijer, L.; Bialojan, C. La microinjection d'acide okadaique, un inhibiteur de phosphoproteine phosphatase, induit la maturation de l'ovocyte de l'etoile de mer. C. r. hebd. Seances Acad. Sci. (Paris). 1989, 309, 563-569.
    • (1989) C. R. Hebd. Seances Acad. Sci. (Paris) , vol.309 , pp. 563-569
    • Pondaven, P.1    Meijer, L.2    Bialojan, C.3
  • 181
    • 0024851781 scopus 로고
    • Involvement of protein phosphatases 1 and 2A in the control of M phase-promoting factor activity in starfish
    • Picard, A.; Capony, J.P.; Brautigan, D.L.; Doree, M. Involvement of protein phosphatases 1 and 2A in the control of M phase-promoting factor activity in starfish. J. Cell Biol. 1989, 109, 3347-3354.
    • (1989) J. Cell Biol. , vol.109 , pp. 3347-3354
    • Picard, A.1    Capony, J.P.2    Brautigan, D.L.3    Doree, M.4
  • 183
    • 0025024183 scopus 로고
    • Protein phosphatases are involved in the in vivo activation of histone H1 kinase in mouse oocyte
    • DOI 10.1016/0012-1606(90)90106-S
    • Rime, H.; Ozon, R. Protein phosphatases are involved in the in vivo activation of histone H1 kinase in mouse oocyte. Dev. Biol. 1990, 141, 115-122. (Pubitemid 20265715)
    • (1990) Developmental Biology , vol.141 , Issue.1 , pp. 115-122
    • Rime, H.1    Ozon, R.2
  • 184
    • 0025976084 scopus 로고
    • Induction of M-phase entry of prophase-blocked mouse oocytes through microinjection of okadaic acid, a specific phosphatase inhibitor
    • Gavin, A.C.; Tsukitani, Y.; Schorderet-Slatkine, S. Induction of M-phase entry of prophase-blocked mouse oocytes through microinjection of okadaic acid, a specific phosphatase inhibitor. Exp. Cell. Res. 1991, 192, 75-81.
    • (1991) Exp. Cell. Res. , vol.192 , pp. 75-81
    • Gavin, A.C.1    Tsukitani, Y.2    Schorderet-Slatkine, S.3
  • 185
    • 33750202125 scopus 로고    scopus 로고
    • New insight into the role of phosphodiesterase 3A in porcine oocyte maturation
    • Sasseville, M.; Cote, N.; Guillemette, C.; Richard, F.J. New insight into the role of phosphodiesterase 3A in porcine oocyte maturation. BMC Dev. Biol. 2006, 6, 47.
    • (2006) BMC Dev. Biol. , vol.6 , pp. 47
    • Sasseville, M.1    Cote, N.2    Guillemette, C.3    Richard, F.J.4
  • 186
    • 33947513747 scopus 로고    scopus 로고
    • Proper chromatin condensation and maintenance of histone H3 phosphorylation during mouse oocyte meiosis requires protein phosphatase activity
    • Swain, J.E.; Ding, J.; Brautigan, D.L.; Villa-Moruzzi, E.; Smith, G.D. Proper chromatin condensation and maintenance of histone H3 phosphorylation during mouse oocyte meiosis requires protein phosphatase activity. Biol. Reprod. 2007, 76, 628-638.
    • (2007) Biol. Reprod. , vol.76 , pp. 628-638
    • Swain, J.E.1    Ding, J.2    Brautigan, D.L.3    Villa-Moruzzi, E.4    Smith, G.D.5
  • 187
    • 15844363885 scopus 로고    scopus 로고
    • Role of actin cytoskeleton in mammalian sperm capacitation and the acrosome reaction
    • Breitbart, H.; Cohen, G.; Rubinstein, S. Role of actin cytoskeleton in mammalian sperm capacitation and the acrosome reaction. Reproduction 2005, 129, 263-268.
    • (2005) Reproduction , vol.129 , pp. 263-268
    • Breitbart, H.1    Cohen, G.2    Rubinstein, S.3
  • 188
    • 0036069351 scopus 로고    scopus 로고
    • Induction of sperm maturation in vitro in epididymal cell cultures of the tammar wallaby (Macropus eugenii): Disruption of motility initiation and sperm morphogenesis by inhibition of actin polymerization
    • Lin, M.; Hess, R.; Aitken, R.J. Induction of sperm maturation in vitro in epididymal cell cultures of the tammar wallaby (Macropus eugenii): disruption of motility initiation and sperm morphogenesis by inhibition of actin polymerization. Reproduction 2002, 124, 107-117.
    • (2002) Reproduction , vol.124 , pp. 107-117
    • Lin, M.1    Hess, R.2    Aitken, R.J.3
  • 189
    • 0017959167 scopus 로고
    • Hamster sperm cross react with antiactin
    • Talbot, P.; Kleve, M.G. Hamster sperm cross react with antiactin. J. Exp. Zool. 1978, 204, 131-136.
    • (1978) J. Exp. Zool. , vol.204 , pp. 131-136
    • Talbot, P.1    Kleve, M.G.2
  • 190
    • 0022859744 scopus 로고
    • Identification of actin in boar spermatids and spermatozoa by immunoelectron microscopy
    • Camatini, M.; Anelli, G.; Casale, A. Identification of actin in boar spermatids and spermatozoa by immunoelectron microscopy. Eur. J. Cell Biol. 1986, 42, 311-318.
    • (1986) Eur. J. Cell Biol. , vol.42 , pp. 311-318
    • Camatini, M.1    Anelli, G.2    Casale, A.3
  • 191
    • 0023938811 scopus 로고
    • Localization of actin in human, bull, rabbit, and hamster sperm by immunoelectron microscopy
    • Flaherty, S.P.; Winfrey, V.P.; Olson, G.E. Localization of actin in human, bull, rabbit, and hamster sperm by immunoelectron microscopy. Anat. Rec. 1988, 221, 599-610.
    • (1988) Anat. Rec. , vol.221 , pp. 599-610
    • Flaherty, S.P.1    Winfrey, V.P.2    Olson, G.E.3
  • 192
    • 0025771988 scopus 로고
    • Changes in actin distribution during sperm development in the opossum, Monodelphis domestica
    • Olson, G.E.; Winfrey, V.P. Changes in actin distribution during sperm development in the opossum, Monodelphis domestica. Anat. Rec. 1991, 230, 209-217.
    • (1991) Anat. Rec. , vol.230 , pp. 209-217
    • Olson, G.E.1    Winfrey, V.P.2
  • 193
    • 0026662066 scopus 로고
    • F-actin in guinea pig spermatozoa: Its role in calmodulin translocation during acrosome reaction
    • Moreno-Fierros, L.; Hernandez, E.O.; Salgado, Z.O.; Mujica, A. F-actin in guinea pig spermatozoa: its role in calmodulin translocation during acrosome reaction. Mol. Reprod. Dev. 1992, 33, 172-181.
    • (1992) Mol. Reprod. Dev. , vol.33 , pp. 172-181
    • Moreno-Fierros, L.1    Hernandez, E.O.2    Salgado, Z.O.3    Mujica, A.4
  • 194
    • 0028890205 scopus 로고
    • Actin, alpha-actinin, and spectrin with specific associations with the postacrosomal and acrosomal domains of bovine spermatozoa
    • Yagi, A.; Paranko, J. Actin, alpha-actinin, and spectrin with specific associations with the postacrosomal and acrosomal domains of bovine spermatozoa. Anat. Rec. 1995, 241, 77-87.
    • (1995) Anat. Rec. , vol.241 , pp. 77-87
    • Yagi, A.1    Paranko, J.2
  • 195
    • 0036888011 scopus 로고    scopus 로고
    • Cytochalasin-D retards sperm incorporation deep into the egg cytoplasm but not membrane fusion with the egg plasma membrane
    • Sanchez-Gutierrez, M.; Contreras, R.G.; Mujica, A. Cytochalasin-D retards sperm incorporation deep into the egg cytoplasm but not membrane fusion with the egg plasma membrane. Mol. Reprod. Dev. 2002, 63, 518-528.
    • (2002) Mol. Reprod. Dev. , vol.63 , pp. 518-528
    • Sanchez-Gutierrez, M.1    Contreras, R.G.2    Mujica, A.3
  • 196
    • 0042061388 scopus 로고    scopus 로고
    • Involvement of Rho family G protein in the cell signaling for sperm incorporation during fertilization of mouse eggs: Inhibition by Clostridium difficile toxin B
    • Kumakiri, J.; Oda, S.; Kinoshita, K.; Miyazaki, S. Involvement of Rho family G protein in the cell signaling for sperm incorporation during fertilization of mouse eggs: inhibition by Clostridium difficile toxin B. Dev. Biol. 2003, 260, 522-535.
    • (2003) Dev. Biol. , vol.260 , pp. 522-535
    • Kumakiri, J.1    Oda, S.2    Kinoshita, K.3    Miyazaki, S.4
  • 197
    • 0022557462 scopus 로고
    • Latrunculin inhibits the microfilament-mediated processes during fertilization, cleavage and early development in sea urchins and mice
    • Schatten, G.; Schatten, H.; Spector, I.; Cline, C.; Paweletz, N.; Simerly, C.; Petzelt, C. Latrunculin inhibits the microfilament-mediated processes during fertilization, cleavage and early development in sea urchins and mice. Exp. Cell. Res. 1986, 166, 191-208.
    • (1986) Exp. Cell. Res. , vol.166 , pp. 191-208
    • Schatten, G.1    Schatten, H.2    Spector, I.3    Cline, C.4    Paweletz, N.5    Simerly, C.6    Petzelt, C.7
  • 198
    • 0024309828 scopus 로고
    • Molecular basis of fertilization
    • Garbers, D.L. Molecular basis of fertilization. Annu. Rev. Biochem. 1989, 58, 719-742.
    • (1989) Annu. Rev. Biochem. , vol.58 , pp. 719-742
    • Garbers, D.L.1
  • 199
    • 0016700614 scopus 로고
    • Mosaicism in organisation concanavalin A receptors on surface membrane of mouse egg
    • Johnson, M.H.; Eager, D.; Muggleton-Harris, A.; Grave, H.M. Mosaicism in organisation concanavalin A receptors on surface membrane of mouse egg. Nature 1975, 257, 321-322.
    • (1975) Nature , vol.257 , pp. 321-322
    • Johnson, M.H.1    Eager, D.2    Muggleton-Harris, A.3    Grave, H.M.4
  • 200
    • 40449114833 scopus 로고    scopus 로고
    • Mapping mouse gamete interaction forces reveal several oocyte membrane regions with different mechanical and adhesive properties
    • Jegou, A.; Pincet, F.; Perez, E.; Wolf, J.P.; Ziyyat, A.; Gourier, C. Mapping mouse gamete interaction forces reveal several oocyte membrane regions with different mechanical and adhesive properties. Langmuir 2008, 24, 1451-1458.
    • (2008) Langmuir , vol.24 , pp. 1451-1458
    • Jegou, A.1    Pincet, F.2    Perez, E.3    Wolf, J.P.4    Ziyyat, A.5    Gourier, C.6
  • 201
    • 0021634235 scopus 로고
    • Changes at the hamster oocyte surface from the germinal vesicle stage to ovulation
    • Ebensperger, C.; Barros, D.C. Changes at the hamster oocyte surface from the germinal vesicle stage to ovulation. Gamete Res. 1984, 9, 387-397.
    • (1984) Gamete Res. , vol.9 , pp. 387-397
    • Ebensperger, C.1    Barros, D.C.2
  • 202
    • 0015811961 scopus 로고
    • The polymerization of actin: Its role in the generation of the acrosomal process of certain echinoderm sperm
    • Tilney, L.G.; Hatano, S.; Ishikawa, H.; Mooseker, M.S. The polymerization of actin: its role in the generation of the acrosomal process of certain echinoderm sperm. J. Cell Biol. 1973, 59, 109-126.
    • (1973) J. Cell Biol. , vol.59 , pp. 109-126
    • Tilney, L.G.1    Hatano, S.2    Ishikawa, H.3    Mooseker, M.S.4
  • 203
    • 0017181048 scopus 로고
    • Actin filament-membrane attachment: Are membrane particles involved?
    • Tilney, L.G.; Mooseker, M.S. Actin filament-membrane attachment: are membrane particles involved? J. Cell Biol. 1976, 71, 402-416.
    • (1976) J. Cell Biol. , vol.71 , pp. 402-416
    • Tilney, L.G.1    Mooseker, M.S.2
  • 204
    • 13444282238 scopus 로고    scopus 로고
    • Sperm-egg fusion: Events at the plasma membrane
    • Stein, K.K.; Primakoff, P.; Myles, D. Sperm-egg fusion: events at the plasma membrane. J. Cell. Sci. 2004, 117, 6269-6274.
    • (2004) J. Cell. Sci. , vol.117 , pp. 6269-6274
    • Stein, K.K.1    Primakoff, P.2    Myles, D.3
  • 205
    • 0019780436 scopus 로고
    • Effects of motility inhibitors during sea urchin fertilization: Microfilament inhibitors prevent sperm incorporation and restructuring of fertilized egg cortex, whereas microtubule inhibitors prevent pronuclear migrations
    • Schatten, G.; Schatten, H. Effects of motility inhibitors during sea urchin fertilization: microfilament inhibitors prevent sperm incorporation and restructuring of fertilized egg cortex, whereas microtubule inhibitors prevent pronuclear migrations. Exp. Cell. Res. 1981, 135, 311-330.
    • (1981) Exp. Cell. Res. , vol.135 , pp. 311-330
    • Schatten, G.1    Schatten, H.2
  • 206
    • 0026692942 scopus 로고
    • The sperm entry site during fertilization of the zebrafish egg: Localization of actin
    • Hart, N.H.; Becker, K.A.; Wolenski, J.S. The sperm entry site during fertilization of the zebrafish egg: localization of actin. Mol. Reprod. Dev. 1992, 32, 217-228.
    • (1992) Mol. Reprod. Dev. , vol.32 , pp. 217-228
    • Hart, N.H.1    Becker, K.A.2    Wolenski, J.S.3
  • 207
    • 0036866203 scopus 로고    scopus 로고
    • Fertilization and the cytoskeleton in the red alga Bostrychia moritziana (Rhodomelaceae, Rhodophyta)
    • Wilson, S.M.; Pickett-Heaps, J.D.; West, J.A. Fertilization and the cytoskeleton in the red alga Bostrychia moritziana (Rhodomelaceae, Rhodophyta). Eur. J. Phycol. 2002, 37, 509-522.
    • (2002) Eur. J. Phycol. , vol.37 , pp. 509-522
    • Wilson, S.M.1    Pickett-Heaps, J.D.2    West, J.A.3
  • 208
    • 55849145143 scopus 로고    scopus 로고
    • Alteration of the cortical actin cytoskeleton deregulates Ca2+ signaling, monospermic fertilization, and sperm entry
    • Puppo, A.; Chun, J.T.; Gragnaniello, G.; Garante, E.; Santella, L. Alteration of the cortical actin cytoskeleton deregulates Ca2+ signaling, monospermic fertilization, and sperm entry. PLoS One 2008, 3, e3588.
    • (2008) PLoS One , vol.3
    • Puppo, A.1    Chun, J.T.2    Gragnaniello, G.3    Garante, E.4    Santella, L.5
  • 209
    • 0036786150 scopus 로고    scopus 로고
    • Involvement of calcium signaling and the actin cytoskeleton in the membrane block to polyspermy in mouse eggs
    • McAvey, B.A.; Wortzman, G.B.; Williams, C.J.; Evans, J.P. Involvement of calcium signaling and the actin cytoskeleton in the membrane block to polyspermy in mouse eggs. Biol. Reprod. 2002, 67, 1342-1352.
    • (2002) Biol. Reprod. , vol.67 , pp. 1342-1352
    • McAvey, B.A.1    Wortzman, G.B.2    Williams, C.J.3    Evans, J.P.4
  • 210
    • 0033734830 scopus 로고    scopus 로고
    • Role of the cytoskeleton in sperm entry during fertilization in the freshwater bivalve Dreissena polymorpha
    • Misamore, M.J.; Lynn, J.W. Role of the cytoskeleton in sperm entry during fertilization in the freshwater bivalve Dreissena polymorpha. Biol. Bull. 2000, 199, 144-156.
    • (2000) Biol. Bull. , vol.199 , pp. 144-156
    • Misamore, M.J.1    Lynn, J.W.2
  • 211
    • 0028244534 scopus 로고
    • Involvement of inositol 1,4,5-trisphosphate-mediated Ca2+ release in early and late events of mouse egg activation
    • Xu, Z.; Kopf, G.S.; Schultz, R.M. Involvement of inositol 1,4,5-trisphosphate-mediated Ca2+ release in early and late events of mouse egg activation. Development 1994, 120, 1851-1859.
    • (1994) Development , vol.120 , pp. 1851-1859
    • Xu, Z.1    Kopf, G.S.2    Schultz, R.M.3
  • 212
    • 1342263615 scopus 로고    scopus 로고
    • Electrical events during gamete maturation and fertilization in animals and humans
    • Tosti, E.; Boni, R. Electrical events during gamete maturation and fertilization in animals and humans. Hum. Reprod. Update 2004, 10, 53-65.
    • (2004) Hum. Reprod. Update , vol.10 , pp. 53-65
    • Tosti, E.1    Boni, R.2
  • 213
    • 0036315011 scopus 로고    scopus 로고
    • Activation of oocytes by latrunculin A
    • Lim, D.; Lange, K.; Santella, L. Activation of oocytes by latrunculin A. Faseb J. 2002, 16, 1050-1056.
    • (2002) Faseb J. , vol.16 , pp. 1050-1056
    • Lim, D.1    Lange, K.2    Santella, L.3
  • 215
    • 0024341960 scopus 로고
    • Free calcium pulses following fertilization in the ascidian egg
    • Speksnijder, J.E.; Corson, D.W.; Sardet, C.; Jaffe, L.F. Free calcium pulses following fertilization in the ascidian egg. Dev. Biol. 1989, 135, 182-190.
    • (1989) Dev. Biol. , vol.135 , pp. 182-190
    • Speksnijder, J.E.1    Corson, D.W.2    Sardet, C.3    Jaffe, L.F.4
  • 216
    • 0025359192 scopus 로고
    • The activation wave of calcium in the ascidian egg and its role in ooplasmic segregation
    • Speksnijder, J.E.; Sardet, C.; Jaffe, L.F. The activation wave of calcium in the ascidian egg and its role in ooplasmic segregation. J. Cell Biol. 1990, 110, 1589-1598.
    • (1990) J. Cell Biol. , vol.110 , pp. 1589-1598
    • Speksnijder, J.E.1    Sardet, C.2    Jaffe, L.F.3
  • 217
    • 0029257223 scopus 로고
    • Function and characteristics of repetitive calcium waves associated with meiosis
    • McDougall, A.; Sardet, C. Function and characteristics of repetitive calcium waves associated with meiosis. Curr Biol. 1995, 5, 318-328.
    • (1995) Curr Biol. , vol.5 , pp. 318-328
    • McDougall, A.1    Sardet, C.2
  • 218
    • 0028810747 scopus 로고
    • The sperm entry point defines the orientation of the calcium-induced contraction wave that directs the first phase of cytoplasmic reorganization in the ascidian egg
    • Roegiers, F.; McDougall, A.; Sardet, C. The sperm entry point defines the orientation of the calcium-induced contraction wave that directs the first phase of cytoplasmic reorganization in the ascidian egg. Development 1995, 121, 3457-3466.
    • (1995) Development , vol.121 , pp. 3457-3466
    • Roegiers, F.1    McDougall, A.2    Sardet, C.3
  • 219
    • 0024600165 scopus 로고
    • Fertilization and ooplasmic movements in the ascidian egg
    • Sardet, C.; Speksnijder, J.; Inoue, S.; Jaffe, L. Fertilization and ooplasmic movements in the ascidian egg. Development 1989, 105, 237-249.
    • (1989) Development , vol.105 , pp. 237-249
    • Sardet, C.1    Speksnijder, J.2    Inoue, S.3    Jaffe, L.4
  • 221
    • 15244356577 scopus 로고    scopus 로고
    • The molecular requirements for cytokinesis
    • Glotzer, M. The molecular requirements for cytokinesis. Science 2005, 307, 1735-1739.
    • (2005) Science , vol.307 , pp. 1735-1739
    • Glotzer, M.1
  • 222
    • 18044376990 scopus 로고    scopus 로고
    • Small GTPase RhoA is required for ooplasmic segregation and spindle rotation, but not for spindle organization and chromosome separation during mouse oocyte maturation, fertilization, and early cleavage
    • Zhong, Z.S.; Huo, L.J.; Liang, C.G.; Chen, D.Y.; Sun, Q.Y. Small GTPase RhoA is required for ooplasmic segregation and spindle rotation, but not for spindle organization and chromosome separation during mouse oocyte maturation, fertilization, and early cleavage. Mol. Reprod. Dev. 2005, 71, 256-261.
    • (2005) Mol. Reprod. Dev. , vol.71 , pp. 256-261
    • Zhong, Z.S.1    Huo, L.J.2    Liang, C.G.3    Chen, D.Y.4    Sun, Q.Y.5
  • 224
    • 0024655779 scopus 로고
    • Distribution and role of microfilaments during early events of sheep fertilization
    • Le Guen, P.; Crozet, N.; Huneau, D.; Gall, L. Distribution and role of microfilaments during early events of sheep fertilization. Gamete Res. 1989, 22, 411-425.
    • (1989) Gamete Res. , vol.22 , pp. 411-425
    • Le Guen, P.1    Crozet, N.2    Huneau, D.3    Gall, L.4
  • 225
    • 0037010211 scopus 로고    scopus 로고
    • Inhibition of embryonic development and fertilization in broadcast spawning marine invertebrates by water soluble diatom extracts and the diatom toxin 2-trans,4-trans decadienal
    • Caldwell, G.S.; Olive, P.J.; Bentley, M.G. Inhibition of embryonic development and fertilization in broadcast spawning marine invertebrates by water soluble diatom extracts and the diatom toxin 2-trans,4-trans decadienal. Aquat. Toxicol. 2002, 60, 123-137.
    • (2002) Aquat. Toxicol. , vol.60 , pp. 123-137
    • Caldwell, G.S.1    Olive, P.J.2    Bentley, M.G.3
  • 226
    • 0033006683 scopus 로고    scopus 로고
    • Water-soluble extracts of the diatom Thalassiosira rotula induce aberrations in embryonic tubulin organisation of the sea urchin Paracentrotus lividus
    • Buttino, I.; Miralto, A.; Ianora, A.; Romano, G.; Poulet, S.A. Water-soluble extracts of the diatom Thalassiosira rotula induce aberrations in embryonic tubulin organisation of the sea urchin Paracentrotus lividus. Mar. Biol. 1999, 134, 147-154.
    • (1999) Mar. Biol. , vol.134 , pp. 147-154
    • Buttino, I.1    Miralto, A.2    Ianora, A.3    Romano, G.4    Poulet, S.A.5
  • 227
    • 0029361930 scopus 로고
    • Nuclear and cytoplasmic dynamics of sperm penetration, pronuclear formation and microtubule organization during fertilization and early preimplantation development in the human
    • Van Blerkom, J.; Davis, P.; Merriam, J.; Sinclair, J. Nuclear and cytoplasmic dynamics of sperm penetration, pronuclear formation and microtubule organization during fertilization and early preimplantation development in the human. Hum. Reprod. Update 1995, 1, 429-461.
    • (1995) Hum. Reprod. Update , vol.1 , pp. 429-461
    • Van Blerkom, J.1    Davis, P.2    Merriam, J.3    Sinclair, J.4
  • 228
    • 0029862532 scopus 로고    scopus 로고
    • Fate of the sperm mitochondria, and the incorporation, conversion, and disassembly of the sperm tail structures during bovine fertilization
    • Sutovsky, P.; Navara, C.S.; Schatten, G. Fate of the sperm mitochondria, and the incorporation, conversion, and disassembly of the sperm tail structures during bovine fertilization. Biol. Reprod. 1996, 55, 1195-1205.
    • (1996) Biol. Reprod. , vol.55 , pp. 1195-1205
    • Sutovsky, P.1    Navara, C.S.2    Schatten, G.3
  • 229
    • 0030712193 scopus 로고    scopus 로고
    • The distribution and requirements of microtubules and microfilaments during fertilization and parthenogenesis in pig oocytes
    • Kim, N.H.; Chung, K.S.; Day, B.N. The distribution and requirements of microtubules and microfilaments during fertilization and parthenogenesis in pig oocytes. J. Reprod. Fertil. 1997, 111, 143-149.
    • (1997) J. Reprod. Fertil. , vol.111 , pp. 143-149
    • Kim, N.H.1    Chung, K.S.2    Day, B.N.3
  • 230
    • 0022597214 scopus 로고
    • Motility and centrosomal organization during sea urchin and mouse fertilization
    • Schatten, H.; Schatten, G. Motility and centrosomal organization during sea urchin and mouse fertilization. Cell Motil. Cytoskeleton 1986, 6, 163-175.
    • (1986) Cell Motil. Cytoskeleton , vol.6 , pp. 163-175
    • Schatten, H.1    Schatten, G.2
  • 231
    • 0028234439 scopus 로고
    • Cleavage furrow: Timing of emergence of contractile ring actin filaments and establishment of the contractile ring by filament bundling in sea urchin eggs
    • Mabuchi, I. Cleavage furrow: timing of emergence of contractile ring actin filaments and establishment of the contractile ring by filament bundling in sea urchin eggs. J. Cell. Sci. 1994, 107 (Pt 7), 1853-1862.
    • (1994) J. Cell. Sci. , vol.107 , Issue.PART 7 , pp. 1853-1862
    • Mabuchi, I.1
  • 232
    • 0035124103 scopus 로고    scopus 로고
    • Reorganization of actin cytoskeleton at the growing end of the cleavage furrow of Xenopus egg during cytokinesis
    • Noguchi, T.; Mabuchi, I. Reorganization of actin cytoskeleton at the growing end of the cleavage furrow of Xenopus egg during cytokinesis. J. Cell. Sci. 2001, 114, 401-412.
    • (2001) J. Cell. Sci. , vol.114 , pp. 401-412
    • Noguchi, T.1    Mabuchi, I.2
  • 234
    • 0036704234 scopus 로고    scopus 로고
    • Microtuble organization in Xenopus eggs during the first cleavage and its role in cytokinesis
    • Takayama, M.; Noguchi, T.; Yamashiro, S.; Mabuchi, I. Microtuble organization in Xenopus eggs during the first cleavage and its role in cytokinesis. Cell Struct. Funct. 2002, 27, 163-171.
    • (2002) Cell Struct. Funct. , vol.27 , pp. 163-171
    • Takayama, M.1    Noguchi, T.2    Yamashiro, S.3    Mabuchi, I.4
  • 235
    • 49649109404 scopus 로고    scopus 로고
    • Dual role for microtubules in regulating cortical contractility during cytokinesis
    • Murthy, K.; Wadsworth, P. Dual role for microtubules in regulating cortical contractility during cytokinesis. J. Cell. Sci. 2008, 121, 2350-2359.
    • (2008) J. Cell. Sci. , vol.121 , pp. 2350-2359
    • Murthy, K.1    Wadsworth, P.2
  • 236
    • 0037179165 scopus 로고    scopus 로고
    • New birth-control aldehydes from the marine diatom Skeletonema costatum: Characterization and biogenesis
    • d'Ippolito, G.; Romano, G.; Iadicicco, O.; Miralto, A.; Ianora, A.; Cimino, G.; Fontana, A. New birth-control aldehydes from the marine diatom Skeletonema costatum: characterization and biogenesis. Tetrahedron Lett. 2002, 43, 6133-6136.
    • (2002) Tetrahedron Lett. , vol.43 , pp. 6133-6136
    • D'Ippolito, G.1    Romano, G.2    Iadicicco, O.3    Miralto, A.4    Ianora, A.5    Cimino, G.6    Fontana, A.7
  • 237
    • 0038696362 scopus 로고    scopus 로고
    • Anti-mitotic activity towards sea urchin embryos in extracts from the marine haptophycean Phaeocystis pouchetii (Hariot) Lagerheim collected along the coast of northern Norway
    • Hansen, E.; Eilertsen, H.C.; Ernstsen, A.; Geneviere, A.M. Anti-mitotic activity towards sea urchin embryos in extracts from the marine haptophycean Phaeocystis pouchetii (Hariot) Lagerheim collected along the coast of northern Norway. Toxicon 2003, 41, 803-812.
    • (2003) Toxicon , vol.41 , pp. 803-812
    • Hansen, E.1    Eilertsen, H.C.2    Ernstsen, A.3    Geneviere, A.M.4
  • 238
    • 4444362073 scopus 로고    scopus 로고
    • The α,β,γ,δ-Unsaturated Aldehyde 2-trans-4-trans-Decadienal Disturbs DNA Replication and Mitotic Events in Early Sea Urchin Embryos
    • Hansen, E.; Even, Y.; Geneviere, A.M. The α,β,γ,δ- Unsaturated Aldehyde 2-trans-4-trans-Decadienal Disturbs DNA Replication and Mitotic Events in Early Sea Urchin Embryos. Toxicol Sci. 2004, 81, 190-197.
    • (2004) Toxicol Sci. , vol.81 , pp. 190-197
    • Hansen, E.1    Even, Y.2    Geneviere, A.M.3
  • 239
    • 0027066986 scopus 로고
    • Selective inhibition of cytokinesis in sea urchin embryos by the marine natural product pseudopterolide
    • Grace, K.J.; Medina, M.; Jacobs, R.S.; Wilson, L. Selective inhibition of cytokinesis in sea urchin embryos by the marine natural product pseudopterolide. Mol. Pharmacol. 1992, 41, 631-638.
    • (1992) Mol. Pharmacol. , vol.41 , pp. 631-638
    • Grace, K.J.1    Medina, M.2    Jacobs, R.S.3    Wilson, L.4
  • 240
    • 19344361922 scopus 로고    scopus 로고
    • Teratogenic effects of azaspiracid-1 identified by microinjection of Japanese medaka (Oryzias latipes) embryos
    • Colman, J.R.; Twiner, M.J.; Hess, P.; McMahon, T.; Satake, M.; Yasumoto, T.; Doucette, G.J.; Ramsdell, J.S. Teratogenic effects of azaspiracid-1 identified by microinjection of Japanese medaka (Oryzias latipes) embryos. Toxicon 2005, 45, 881-890.
    • (2005) Toxicon , vol.45 , pp. 881-890
    • Colman, J.R.1    Twiner, M.J.2    Hess, P.3    McMahon, T.4    Satake, M.5    Yasumoto, T.6    Doucette, G.J.7    Ramsdell, J.S.8
  • 241
    • 23044471179 scopus 로고    scopus 로고
    • Oocyte-based screening of cytokinesis inhibitors and identification of pectenotoxin-2 that induces Bim/Bax-mediated apoptosis in p53-deficient tumors
    • Chae, H.D.; Choi, T.S.; Kim, B.M.; Jung, J.H.; Bang, Y.J.; Shin, D.Y. Oocyte-based screening of cytokinesis inhibitors and identification of pectenotoxin-2 that induces Bim/Bax-mediated apoptosis in p53-deficient tumors. Oncogene 2005, 24, 4813-4819.
    • (2005) Oncogene , vol.24 , pp. 4813-4819
    • Chae, H.D.1    Choi, T.S.2    Kim, B.M.3    Jung, J.H.4    Bang, Y.J.5    Shin, D.Y.6
  • 242
    • 0030272253 scopus 로고    scopus 로고
    • Effects of caulerpenyne, the major toxin from Caulerpa taxifolia on mechanisms related to sea urchin egg cleavage
    • Pesando, D.; Lemee, R.; Ferrua, C.; Amade, P.; Girard, J.P. Effects of caulerpenyne, the major toxin from Caulerpa taxifolia on mechanisms related to sea urchin egg cleavage. Aquat. Toxicol. 1996, 35, 139-155.
    • (1996) Aquat. Toxicol. , vol.35 , pp. 139-155
    • Pesando, D.1    Lemee, R.2    Ferrua, C.3    Amade, P.4    Girard, J.P.5
  • 243
    • 0031662030 scopus 로고    scopus 로고
    • Caulerpenyne interferes with microtubule-dependent events during the first mitotic cycle of sea urchin eggs
    • Pesando, D.; Huitorel, P.; Dolcini, V.; Amade, P.; Girard, J.P. Caulerpenyne interferes with microtubule-dependent events during the first mitotic cycle of sea urchin eggs. Eur. J. Cell Biol. 1998, 77, 19-26.
    • (1998) Eur. J. Cell Biol. , vol.77 , pp. 19-26
    • Pesando, D.1    Huitorel, P.2    Dolcini, V.3    Amade, P.4    Girard, J.P.5
  • 244
    • 33746580789 scopus 로고    scopus 로고
    • Sea urchin embryo as a model organism for the rapid functional screening of tubulin modulators
    • Semenova, M.N.; Kiselyov, A.; Semenov, V.V. Sea urchin embryo as a model organism for the rapid functional screening of tubulin modulators. Biotechniques 2006, 40, 765-774.
    • (2006) Biotechniques , vol.40 , pp. 765-774
    • Semenova, M.N.1    Kiselyov, A.2    Semenov, V.V.3
  • 247
    • 0344082608 scopus 로고    scopus 로고
    • Progress in the development and acquisition of anticancer agents from marine sources
    • Amador, M.L.; Jimeno, J.; Paz-Ares, L.; Cortes-Funes, H.; Hidalgo, M. Progress in the development and acquisition of anticancer agents from marine sources. Ann. Oncol. 2003, 14, 1607-1615.
    • (2003) Ann. Oncol. , vol.14 , pp. 1607-1615
    • Amador, M.L.1    Jimeno, J.2    Paz-Ares, L.3    Cortes-Funes, H.4    Hidalgo, M.5
  • 248
    • 52749092934 scopus 로고    scopus 로고
    • Clinical status of anti-cancer agents derived from marine sources
    • Singh, R.; Sharma, M.; Joshi, P.; Rawat, D.S. Clinical status of anti-cancer agents derived from marine sources. Anticancer Agents Med. Chem. 2008, 8, 603-617.
    • (2008) Anticancer Agents Med. Chem. , vol.8 , pp. 603-617
    • Singh, R.1    Sharma, M.2    Joshi, P.3    Rawat, D.S.4
  • 249
    • 0038461995 scopus 로고    scopus 로고
    • Drugs from the deep: Marine natural products as drug candidates
    • Haefner, B. Drugs from the deep: marine natural products as drug candidates. Drug Discov. Today 2003, 8, 536-544.
    • (2003) Drug Discov. Today , vol.8 , pp. 536-544
    • Haefner, B.1


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