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Volumn 2004, Issue 74, 2004, Pages 523-544

Sea urchin spermatozoa

Author keywords

[No Author keywords available]

Indexed keywords

ANIMAL; CELL FRACTIONATION; CELL MEMBRANE; CELL ORGANELLE; CYTOCHEMISTRY; CYTOLOGY; FERTILIZATION; INSTRUMENTATION; MALE; METHODOLOGY; MICRODISSECTION; PHYSIOLOGY; REVIEW; SEA URCHIN; SPERMATOZOON; STAINING; ULTRASTRUCTURE;

EID: 16644387164     PISSN: 0091679X     EISSN: None     Source Type: Book Series    
DOI: 10.1016/s0091-679x(04)74021-2     Document Type: Review
Times cited : (27)

References (76)
  • 1
    • 0030012652 scopus 로고    scopus 로고
    • Membrane potential regulates sea urchin sperm adenylylcyclase
    • Beltrán, C., Zapata, O., and Darszon, A. (1996). Membrane potential regulates sea urchin sperm adenylylcyclase. Biochemistry 35, 7591-7598.
    • (1996) Biochemistry , vol.35 , pp. 7591-7598
    • Beltrán, C.1    Zapata, O.2    Darszon, A.3
  • 2
    • 0031771544 scopus 로고    scopus 로고
    • The molecular evolution of bindin in six species of sea urchins (Echinoidea: Strongylocentrotidae)
    • Biermann, C. H. (1998). The molecular evolution of bindin in six species of sea urchins (Echinoidea: Strongylocentrotidae). Mol. Biol. Evol. 15, 1761-1771.
    • (1998) Mol. Biol. Evol. , vol.15 , pp. 1761-1771
    • Biermann, C.H.1
  • 3
    • 0034730455 scopus 로고    scopus 로고
    • 2+ on the secondary structure of a histidine-rich fusagenic peptide and its interaction with lipid membranes
    • 2+ on the secondary structure of a histidine-rich fusagenic peptide and its interaction with lipid membranes. Biochim. Biophys. Acta 1468, 345-358.
    • (2000) Biochim. Biophys. Acta , vol.1468 , pp. 345-358
    • Binder, H.1    Arnold, K.2    Ulrich, A.S.3    Zschornig, O.4
  • 4
    • 0025086820 scopus 로고
    • Identification of sea urchin sperm adenylate cyclase
    • Bookbinder, L. H., Moy, G. W., and Vacquier, V. D. (1990). Identification of sea urchin sperm adenylate cyclase. J. Cell Biol. 111, 1859-1866.
    • (1990) J. Cell Biol. , vol.111 , pp. 1859-1866
    • Bookbinder, L.H.1    Moy, G.W.2    Vacquier, V.D.3
  • 5
    • 0036785117 scopus 로고    scopus 로고
    • Computer simulation of flagellar movement VIII: Coordination of dynein by local curvature control can generate helical bending waves
    • Brokaw, C. J. (2002). Computer simulation of flagellar movement VIII: Coordination of dynein by local curvature control can generate helical bending waves. Cell Motil. Cytoskel. 53, 103-124.
    • (2002) Cell Motil. Cytoskel. , vol.53 , pp. 103-124
    • Brokaw, C.J.1
  • 7
    • 0034026566 scopus 로고    scopus 로고
    • Formation of the sea urchin male pronucleus in cell-free extracts
    • Collas, P. (2000). Formation of the sea urchin male pronucleus in cell-free extracts. Mol. Reprod. Dev. 56, 265-270.
    • (2000) Mol. Reprod. Dev. , vol.56 , pp. 265-270
    • Collas, P.1
  • 8
    • 0020647691 scopus 로고
    • Isolation and electrophoretic characterization of the plasma membrane of sea urchin sperm
    • Cross, N. L. (1983). Isolation and electrophoretic characterization of the plasma membrane of sea urchin sperm. J. Cell Sci. 59, 13-25.
    • (1983) J. Cell Sci. , vol.59 , pp. 13-25
    • Cross, N.L.1
  • 11
    • 0033693014 scopus 로고    scopus 로고
    • Evaluation of sequence variation and selection in the bindin locus of the red sea urchin, Strongylocentrotus franciscanus
    • Debenham, P., Brzezinski, M. A., and Foltz, K. R. (2000). Evaluation of sequence variation and selection in the bindin locus of the red sea urchin, Strongylocentrotus franciscanus. J. Mol. Evol. 51, 481-490.
    • (2000) J. Mol. Evol. , vol.51 , pp. 481-490
    • Debenham, P.1    Brzezinski, M.A.2    Foltz, K.R.3
  • 12
    • 0034657308 scopus 로고    scopus 로고
    • Participation of a K+ channel modulated directly by cGMP in the speract induced signaling cascade of Strongylocentrotus purpuratus sea urchin sperm
    • Galindo, B. E., Beltrán, C., Cragoe, E. J., Jr., and Darszon, A. (2000). Participation of a K+ channel modulated directly by cGMP in the speract induced signaling cascade of Strongylocentrotus purpuratus sea urchin sperm. Dev. Biol. 221, 285-294.
    • (2000) Dev. Biol. , vol.221 , pp. 285-294
    • Galindo, B.E.1    Beltrán, C.2    Cragoe Jr., E.J.3    Darszon, A.4
  • 14
    • 0024309828 scopus 로고
    • Molecular basis for fertilization
    • Garbers, D. L. (1989). Molecular basis for fertilization. Ann. Rev. Biochem. 58, 719-742.
    • (1989) Ann. Rev. Biochem. , vol.58 , pp. 719-742
    • Garbers, D.L.1
  • 15
    • 0021796408 scopus 로고
    • Regulation of internal pH of sea urchin sperm
    • Gatti, J.-L., and Christen, R. (1985). Regulation of internal pH of sea urchin sperm. J. Biol. Chem. 260, 7599-7602.
    • (1985) J. Biol. Chem. , vol.260 , pp. 7599-7602
    • Gatti, J.-L.1    Christen, R.2
  • 16
    • 0032508032 scopus 로고    scopus 로고
    • Molecular identification of a hyperpolarization activated channel in sea urchin sperm
    • Gauss, R., Seifert, R., and Kaupp, U. B. (1998). Molecular identification of a hyperpolarization activated channel in sea urchin sperm. Nature 393, 583-587.
    • (1998) Nature , vol.393 , pp. 583-587
    • Gauss, R.1    Seifert, R.2    Kaupp, U.B.3
  • 17
    • 33749821421 scopus 로고    scopus 로고
    • Structural analysis of a fusogenic peptide sequence from the sea urchin fertilization protein bindin
    • Glaser, R. W., Grüne, M., Wandelt, C., and Ulrich, A. S. (1999). Structural analysis of a fusogenic peptide sequence from the sea urchin fertilization protein bindin. Biochemistry 58, 2300-2309.
    • (1999) Biochemistry , vol.58 , pp. 2300-2309
    • Glaser, R.W.1    Grüne, M.2    Wandelt, C.3    Ulrich, A.S.4
  • 19
    • 0017231487 scopus 로고
    • Guanylate cyclase from sea urchin sperm: Subcellular localization
    • Gray, J. P., and Drummond, G. I. (1976). Guanylate cyclase from sea urchin sperm: Subcellular localization. Arch. Biochem. Biophys. 172, 31-38.
    • (1976) Arch. Biochem. Biophys. , vol.172 , pp. 31-38
    • Gray, J.P.1    Drummond, G.I.2
  • 20
    • 0030845347 scopus 로고    scopus 로고
    • The heterotrimeric motor protein kinesin-II localizes to the midpiece and flagellum of sea urchin and sand dollar sperm
    • Henson, J. H., Cole, D. G., Roesener, C. D., Capuano, S., Mendola, R. J., and Scholey, J. M. (1997). The heterotrimeric motor protein kinesin-II localizes to the midpiece and flagellum of sea urchin and sand dollar sperm. Cell Motil. Cytoskel. 38, 29-37.
    • (1997) Cell Motil. Cytoskel. , vol.38 , pp. 29-37
    • Henson, J.H.1    Cole, D.G.2    Roesener, C.D.3    Capuano, S.4    Mendola, R.J.5    Scholey, J.M.6
  • 21
    • 0036385833 scopus 로고    scopus 로고
    • Egg fucose sulfate polymer, sialoglycan, and speract all trigger the sea urchin sperm acrosome reaction
    • Hirohashi, N., and Vacquier, V. D. (2002a). Egg fucose sulfate polymer, sialoglycan, and speract all trigger the sea urchin sperm acrosome reaction. Biochem. Biophys. Res. Comm. 296, 833-839.
    • (2002) Biochem. Biophys. Res. Comm. , vol.296 , pp. 833-839
    • Hirohashi, N.1    Vacquier, V.D.2
  • 22
    • 0036431113 scopus 로고    scopus 로고
    • Structural requirements for species-specific induction of the sperm acrosome reaction by sea urchin egg sulfated fucan
    • Hirohashi, N., Vilela-Silva, A.-C. E. S., Mourão, P. A. S., and Vacquier, V. D. (2002). Structural requirements for species-specific induction of the sperm acrosome reaction by sea urchin egg sulfated fucan. Biochem. Biophys. Res. Comm. 298, 403-407.
    • (2002) Biochem. Biophys. Res. Comm. , vol.298 , pp. 403-407
    • Hirohashi, N.1    Vilela-Silva, A.-C.E.S.2    Mourão, P.A.S.3    Vacquier, V.D.4
  • 23
    • 0037059738 scopus 로고    scopus 로고
    • 2+ channels involved in triggering the sea urchin sperm acrosome reaction
    • 2+ channels involved in triggering the sea urchin sperm acrosome reaction. J. Biol. Chem. 277, 1182-1189.
    • (2002) J. Biol. Chem. , vol.277 , pp. 1182-1189
    • Hirohashi, N.1    Vacquier, V.D.2
  • 24
    • 0037040933 scopus 로고    scopus 로고
    • Egg sialoglycans increase intracellular pH and potentiate the acrosome reaction of sea urchin sperm
    • Hirohashi, N., and Vacquier, V. D. (2002c). Egg sialoglycans increase intracellular pH and potentiate the acrosome reaction of sea urchin sperm. J. Biol. Chem. 277, 8041-8047.
    • (2002) J. Biol. Chem. , vol.277 , pp. 8041-8047
    • Hirohashi, N.1    Vacquier, V.D.2
  • 25
    • 0037414438 scopus 로고    scopus 로고
    • Store-operated calcium channels trigger exocytosis of the sea urchin sperm acrosomal vesicle
    • Hirohashi, N., and Vacquier, V. D. (2003). Store-operated calcium channels trigger exocytosis of the sea urchin sperm acrosomal vesicle. Biochem. Biophys. Res. Commun. 304, 285-292.
    • (2003) Biochem. Biophys. Res. Commun. , vol.304 , pp. 285-292
    • Hirohashi, N.1    Vacquier, V.D.2
  • 26
    • 0036203332 scopus 로고    scopus 로고
    • Differential distribution of glutamylated tubulin isoforms along the sea urchin sperm axoneme
    • Huitorel, P., White, D., Fouquet, J. P., Kann, M. L., Cosson, J., and Gagnon, C. (2002). Differential distribution of glutamylated tubulin isoforms along the sea urchin sperm axoneme. Mol. Reprod. Dev. 62, 139-148.
    • (2002) Mol. Reprod. Dev. , vol.62 , pp. 139-148
    • Huitorel, P.1    White, D.2    Fouquet, J.P.3    Kann, M.L.4    Cosson, J.5    Gagnon, C.6
  • 27
    • 0036707893 scopus 로고    scopus 로고
    • Genetics and pathogenesis of polycystic kidney disease
    • Igarashi, P., and Somlo, S. (2002). Genetics and pathogenesis of polycystic kidney disease. J. Am. Soc. Nephrol. 13, 2384-2398.
    • (2002) J. Am. Soc. Nephrol. , vol.13 , pp. 2384-2398
    • Igarashi, P.1    Somlo, S.2
  • 29
    • 0021342999 scopus 로고
    • Sodium and proton transport in flagella isolated from sea urchin spermatozoa
    • Lee, H.-C. (1984). Sodium and proton transport in flagella isolated from sea urchin spermatozoa. J. Biol. Chem. 259, 4957-4963.
    • (1984) J. Biol. Chem. , vol.259 , pp. 4957-4963
    • Lee, H.-C.1
  • 30
    • 0022214250 scopus 로고
    • + exchange in sea urchin spermatozoa flagellar membrane vesicles studied with an entrapped pH probe
    • + exchange in sea urchin spermatozoa flagellar membrane vesicles studied with an entrapped pH probe. J. Biol. Chem. 260, 10794-10799.
    • (1985) J. Biol. Chem. , vol.260 , pp. 10794-10799
    • Lee, H.-C.1
  • 31
    • 0029175153 scopus 로고
    • Isolation of flagella and their membranes from sea urchin spermatozoa
    • Lee, H.-C. (1995). Isolation of flagella and their membranes from sea urchin spermatozoa. Meth. Cell. Biol. 47, 43-46.
    • (1995) Meth. Cell. Biol. , vol.47 , pp. 43-46
    • Lee, H.-C.1
  • 32
    • 0037167878 scopus 로고    scopus 로고
    • Voltage-sensing mechanism is conserved among ion channels gated by opposite voltages
    • Männikkö, R., Elinder, F., and Larsson, H. P. (2002). Voltage-sensing mechanism is conserved among ion channels gated by opposite voltages. Nature 419, 837-841.
    • (2002) Nature , vol.419 , pp. 837-841
    • Männikkö, R.1    Elinder, F.2    Larsson, H.P.3
  • 33
    • 0027167712 scopus 로고
    • A GPI-anchored sea urchin sperm membrane protein containing EGF domains is related to human uromodulin
    • Mendoza, L. M., Nishioka, D., and Vacquier, V. D. (1993). A GPI-anchored sea urchin sperm membrane protein containing EGF domains is related to human uromodulin. J. Cell Biol. 121, 1291-1297.
    • (1993) J. Cell Biol. , vol.121 , pp. 1291-1297
    • Mendoza, L.M.1    Nishioka, D.2    Vacquier, V.D.3
  • 34
    • 0037059813 scopus 로고    scopus 로고
    • suREJ3, a polycystin-1 protein, is cleaved at the GPS domain and localizes to the acrosomal region of sea urchin sperm
    • Mengerink, K. J., Moy, G. W., and Vacquier, V. D. (2002). suREJ3, a polycystin-1 protein, is cleaved at the GPS domain and localizes to the acrosomal region of sea urchin sperm. J. Biol. Chem. 277, 943-948.
    • (2002) J. Biol. Chem. , vol.277 , pp. 943-948
    • Mengerink, K.J.1    Moy, G.W.2    Vacquier, V.D.3
  • 35
    • 0037174847 scopus 로고    scopus 로고
    • An ATP-binding cassette transporter is a major glycoprotein of sea urchin sperm membranes
    • Mengerink, K. J., and Vacquier, V. D. (2002). An ATP-binding cassette transporter is a major glycoprotein of sea urchin sperm membranes. J. Biol. Chem. 277, 40729-40734.
    • (2002) J. Biol. Chem. , vol.277 , pp. 40729-40734
    • Mengerink, K.J.1    Vacquier, V.D.2
  • 36
    • 0030033286 scopus 로고    scopus 로고
    • Positive selection and sequence rearrangements generate extensive polymorphism in the gamete recognition protein bindin
    • Metz, E. C., and Palumbi, S. R. (1996). Positive selection and sequence rearrangements generate extensive polymorphism in the gamete recognition protein bindin. Mol. Biol. Evol. 13, 397-406.
    • (1996) Mol. Biol. Evol. , vol.13 , pp. 397-406
    • Metz, E.C.1    Palumbi, S.R.2
  • 37
    • 0028110612 scopus 로고
    • Fertilization between closely related sea urchins is blocked by incompatibilities during sperm-egg attachment and early stages of fusion
    • Metz, E. C., Kane, R. E., Yanagimachi, H., and Palumbi, S. R. (1994). Fertilization between closely related sea urchins is blocked by incompatibilities during sperm-egg attachment and early stages of fusion. Biol. Bull. 187, 23-34.
    • (1994) Biol. Bull. , vol.187 , pp. 23-34
    • Metz, E.C.1    Kane, R.E.2    Yanagimachi, H.3    Palumbi, S.R.4
  • 38
    • 0025938299 scopus 로고
    • Comparison of the bindin proteins of Strongylocentrotus franciscanus, S. purpuratus, Lytechinus variegatus: Sequences involved in the species specificity of fertilization
    • Minor, J. E., Fromson, D. R., Britten, R. J., and Davidson, E. H. (1991). Comparison of the bindin proteins of Strongylocentrotus franciscanus, S. purpuratus, Lytechinus variegatus: Sequences involved in the species specificity of fertilization. Mol. Biol. Evol. 8, 781-795.
    • (1991) Mol. Biol. Evol. , vol.8 , pp. 781-795
    • Minor, J.E.1    Fromson, D.R.2    Britten, R.J.3    Davidson, E.H.4
  • 39
    • 0023911498 scopus 로고
    • Energy metabolism of sea urchin spermatozoa, with phosphatidylcholine as the preferred substrate
    • Mita, M., and Ueta, N. (1988). Energy metabolism of sea urchin spermatozoa, with phosphatidylcholine as the preferred substrate. Biochim. Biophys. Acta 959, 361-369.
    • (1988) Biochim. Biophys. Acta , vol.959 , pp. 361-369
    • Mita, M.1    Ueta, N.2
  • 40
    • 0029977293 scopus 로고    scopus 로고
    • The sea urchin sperm receptor for egg jelly is a modular protein with extensive homology to the human polycystic kidney disease protein, PKD1
    • Moy, G. W., Mendoza, L. M., Schulz, J. R., Swanson, W. J., Glabe, C. G., and Vacquier, V. D. (1996). The sea urchin sperm receptor for egg jelly is a modular protein with extensive homology to the human polycystic kidney disease protein, PKD1. J. Cell Biol. 133, 809-817.
    • (1996) J. Cell Biol. , vol.133 , pp. 809-817
    • Moy, G.W.1    Mendoza, L.M.2    Schulz, J.R.3    Swanson, W.J.4    Glabe, C.G.5    Vacquier, V.D.6
  • 41
    • 0029757769 scopus 로고    scopus 로고
    • The a and B tubules of the outer doublets of sea urchin sperm axonemes are composed of different tubulin variants
    • Multigner, L., Pignot-Paintrand, I., Saoudi, Y., Job, D., Plessmann, U., Rudiger, M., and Weber, K. (1996). The A and B tubules of the outer doublets of sea urchin sperm axonemes are composed of different tubulin variants. Biochemistry 35, 10862-10871.
    • (1996) Biochemistry , vol.35 , pp. 10862-10871
    • Multigner, L.1    Pignot-Paintrand, I.2    Saoudi, Y.3    Job, D.4    Plessmann, U.5    Rudiger, M.6    Weber, K.7
  • 42
    • 0033583779 scopus 로고    scopus 로고
    • Isolation and characterization of low density detergent-insoluble membrane (LD-DIM) fraction from sea urchin sperm
    • Ohta, K., Sato, C., Matsuda, T., Toriyama, M., Lennarz, W. J., and Kitajima, K. (1999). Isolation and characterization of low density detergent-insoluble membrane (LD-DIM) fraction from sea urchin sperm. Biochem. Biophys. Res. Commun. 258, 616-623.
    • (1999) Biochem. Biophys. Res. Commun. , vol.258 , pp. 616-623
    • Ohta, K.1    Sato, C.2    Matsuda, T.3    Toriyama, M.4    Lennarz, W.J.5    Kitajima, K.6
  • 43
    • 0034530296 scopus 로고    scopus 로고
    • Co-localization of receptor and transducer proteins in the glycosphingolipid-enriched, low density, detergent-insoluble membrane fraction of sea urchin sperm
    • Ohta, K., Sato, C., Matsuda, T., Toriyama, M., Vacquier, V. D., Lennarz, W. J., and Kitajima, K. (2000). Co-localization of receptor and transducer proteins in the glycosphingolipid-enriched, low density, detergent-insoluble membrane fraction of sea urchin sperm. Glycoconjugate J. 17, 205-214.
    • (2000) Glycoconjugate J. , vol.17 , pp. 205-214
    • Ohta, K.1    Sato, C.2    Matsuda, T.3    Toriyama, M.4    Vacquier, V.D.5    Lennarz, W.J.6    Kitajima, K.7
  • 44
    • 0033607142 scopus 로고    scopus 로고
    • All males are not created equal: Fertility differences depend on gamete recognition polymorphisms in sea urchins
    • Palumbi, S. R. (1999). All males are not created equal: Fertility differences depend on gamete recognition polymorphisms in sea urchins. Proc. Natl. Acad. Sci. USA 96, 12632-12637.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 12632-12637
    • Palumbi, S.R.1
  • 45
    • 0002281819 scopus 로고
    • Reactivation and remodeling of the sperm nucleus after fertilization
    • (H. Schatten and G. Schatten, eds.). Academic Press, San Diego
    • Poccia, D. L. (1989). Reactivation and remodeling of the sperm nucleus after fertilization. In "The Molecular Biology of Fertilization" (H. Schatten and G. Schatten, eds.), pp. 115-131. Academic Press, San Diego.
    • (1989) The Molecular Biology of Fertilization , pp. 115-131
    • Poccia, D.L.1
  • 46
    • 0022585279 scopus 로고
    • Nuclei and chromosomal proteins
    • Poccia, D. L., and Green, G. R. (1986). Nuclei and chromosomal proteins. Meth. Cell Biol. 27, 153-174.
    • (1986) Meth. Cell Biol. , vol.27 , pp. 153-174
    • Poccia, D.L.1    Green, G.R.2
  • 47
    • 0021721318 scopus 로고
    • Wheat germ agglutinin blocks the acrosome reaction in Strongylocentrotus purpuratus sperm by binding a 210,000-mol-wt membrane protein
    • Podell, S. B., and Vacquier, V. D. (1984). Wheat germ agglutinin blocks the acrosome reaction in Strongylocentrotus purpuratus sperm by binding a 210,000-mol-wt membrane protein. J. Cell Biol. 99, 1598-1604.
    • (1984) J. Cell Biol. , vol.99 , pp. 1598-1604
    • Podell, S.B.1    Vacquier, V.D.2
  • 48
    • 0021690605 scopus 로고
    • Isolation and characterization of a plasma membrane fraction from sea urchin sperm exhibiting species specific recognition of the egg surface
    • Podell, S. B., Moy, G. W., and Vacquier, V. D. (1984). Isolation and characterization of a plasma membrane fraction from sea urchin sperm exhibiting species specific recognition of the egg surface. Biochim. Biophys. Acta 778, 25-37.
    • (1984) Biochim. Biophys. Acta , vol.778 , pp. 25-37
    • Podell, S.B.1    Moy, G.W.2    Vacquier, V.D.3
  • 49
    • 0031007608 scopus 로고    scopus 로고
    • Myristoylated and nonmyristoylated pools of sea urchin sperm flagellar creatine kinase exist side-by-side: Myristoylation is necessary for efficient lipid association
    • Quest, A. F., Harvey, D. J., and McIlhinney, R. A. (1997). Myristoylated and nonmyristoylated pools of sea urchin sperm flagellar creatine kinase exist side-by-side: Myristoylation is necessary for efficient lipid association. Biochemistry 36, 6993-7002.
    • (1997) Biochemistry , vol.36 , pp. 6993-7002
    • Quest, A.F.1    Harvey, D.J.2    McIlhinney, R.A.3
  • 51
    • 0037235162 scopus 로고    scopus 로고
    • Intracellular sodium changes during the speract response and the acrosome reaction in sea urchin sperm
    • Rodríguez, E., and Darszon, A. (2003). Intracellular sodium changes during the speract response and the acrosome reaction in sea urchin sperm. J. Physiol. 546, 80-100.
    • (2003) J. Physiol. , vol.546 , pp. 80-100
    • Rodríguez, E.1    Darszon, A.2
  • 52
    • 0036788528 scopus 로고    scopus 로고
    • Pore topology of the hyperpolarization-activated cyclic nucleotide-gated channel from sea urchin sperm
    • Roncaglia, P., Mistrik, P., and Torre, V. (2002). Pore topology of the hyperpolarization-activated cyclic nucleotide-gated channel from sea urchin sperm. Biophys. J. 83, 1953-1964.
    • (2002) Biophys. J. , vol.83 , pp. 1953-1964
    • Roncaglia, P.1    Mistrik, P.2    Torre, V.3
  • 53
    • 0036143456 scopus 로고    scopus 로고
    • Voltage-controlled gating at the intracellular entrance to a hyperpolarization-activated cation channel
    • Rothberg, B. S., Shin, K. S., Phale, P. S., and Yellen, G. (2002). Voltage-controlled gating at the intracellular entrance to a hyperpolarization-activated cation channel. J. Gen. Physiol. 119, 83-91.
    • (2002) J. Gen. Physiol. , vol.119 , pp. 83-91
    • Rothberg, B.S.1    Shin, K.S.2    Phale, P.S.3    Yellen, G.4
  • 55
    • 0031281655 scopus 로고    scopus 로고
    • The exocytotic regulatory proteins syntaxin and VAMP are shed from sea urchin sperm during the acrosome reaction
    • Schulz, J. R., Wessel, G. M., and Vacquier, V. D. (1997). The exocytotic regulatory proteins syntaxin and VAMP are shed from sea urchin sperm during the acrosome reaction. Dev. Biol. 191, 80-87.
    • (1997) Dev. Biol. , vol.191 , pp. 80-87
    • Schulz, J.R.1    Wessel, G.M.2    Vacquier, V.D.3
  • 56
    • 0032544692 scopus 로고    scopus 로고
    • Increased association of synaptosome-associated protein of 25kDa with syntaxin and vesicle-associated membrane protein following acrosomal exocytosis of sea urchin sperm
    • Schulz, J. R., Sasaki, J. D., and Vacquier, V. D. (1998). Increased association of synaptosome-associated protein of 25kDa with syntaxin and vesicle-associated membrane protein following acrosomal exocytosis of sea urchin sperm. J. Biol. Chem. 273, 24355-24359.
    • (1998) J. Biol. Chem. , vol.273 , pp. 24355-24359
    • Schulz, J.R.1    Sasaki, J.D.2    Vacquier, V.D.3
  • 59
    • 0029242430 scopus 로고
    • Structure, function, and biosynthesis of sperm-activating peptides and fucose sulfate glycoconjugate in the extracellular coat of sea urchin eggs
    • Suzuki, N. (1995). Structure, function, and biosynthesis of sperm-activating peptides and fucose sulfate glycoconjugate in the extracellular coat of sea urchin eggs. Zool. Sci. 12, 12-27.
    • (1995) Zool. Sci. , vol.12 , pp. 12-27
    • Suzuki, N.1
  • 60
    • 0035679709 scopus 로고    scopus 로고
    • The regulation and physiological roles of the guanylyl cyclase receptors
    • Tamura, N., Chrisman, T. D., and Garbers, D. L. (2001). The regulation and physiological roles of the guanylyl cyclase receptors. Endocr. J. 48, 611-634.
    • (2001) Endocr. J. , vol.48 , pp. 611-634
    • Tamura, N.1    Chrisman, T.D.2    Garbers, D.L.3
  • 61
    • 0023372480 scopus 로고
    • Creatine kinase-dependent energy transport in sea urchin spermatozoa
    • Tombes, R. M., Brokaw, C. J., and Shapiro, B. M. (1987). Creatine kinase-dependent energy transport in sea urchin spermatozoa. Biophys. J. 52, 75-86.
    • (1987) Biophys. J. , vol.52 , pp. 75-86
    • Tombes, R.M.1    Brokaw, C.J.2    Shapiro, B.M.3
  • 62
    • 0022570941 scopus 로고
    • Handling, labeling, and fractionating sea urchin spermatozoa
    • Vacquier, V. D. (1986a). Handling, labeling, and fractionating sea urchin spermatozoa. Meth. Cell Biol. 27, 15-40.
    • (1986) Meth. Cell Biol. , vol.27 , pp. 15-40
    • Vacquier, V.D.1
  • 63
    • 0001845525 scopus 로고
    • Activation of sea urchin spermatozoa during fertilization
    • Vacquier, V. D. (1986b). Activation of sea urchin spermatozoa during fertilization. Trends Biochem. Sci. 11, 77-81.
    • (1986) Trends Biochem. Sci. , vol.11 , pp. 77-81
    • Vacquier, V.D.1
  • 64
    • 33749817624 scopus 로고
    • Plasma membranes isolated from sea urchin spermatozoa
    • (H. Morhi, ed.). Japan Science Society Press, Tokyo
    • Vacquier, V. D. (1987). Plasma membranes isolated from sea urchin spermatozoa. In "New Horizons in Sperm Cell Research" (H. Morhi, ed.), pp. 217-233. Japan Science Society Press, Tokyo.
    • (1987) New Horizons in Sperm Cell Research , pp. 217-233
    • Vacquier, V.D.1
  • 66
    • 0031456362 scopus 로고    scopus 로고
    • The fucose sulfate polymer of egg jelly binds to sperm REJ and is the inducer of the sea urchin sperm acrosome reaction
    • Vacquier, V. D., and Moy, G. W. (1997). The fucose sulfate polymer of egg jelly binds to sperm REJ and is the inducer of the sea urchin sperm acrosome reaction. Dev. Biol. 192, 125-135.
    • (1997) Dev. Biol. , vol.192 , pp. 125-135
    • Vacquier, V.D.1    Moy, G.W.2
  • 67
    • 0030851631 scopus 로고    scopus 로고
    • Activation of sea urchin sperm motility is accompanied by an increase in the creatine kinase exchange flux
    • van Dorsten, F. A., Wyss, M., Wallimann, T., and Nicolay, K. (1997). Activation of sea urchin sperm motility is accompanied by an increase in the creatine kinase exchange flux. Biochem. J. 325, 411-416.
    • (1997) Biochem. J. , vol.325 , pp. 411-416
    • Van Dorsten, F.A.1    Wyss, M.2    Wallimann, T.3    Nicolay, K.4
  • 68
    • 0037016675 scopus 로고    scopus 로고
    • Sulfated fucans from the egg jellies of the closely related sea urchins Strongylocentrotus droebachiensis and S. pallidus ensure species-specific fertilization
    • Vilela-Silva, A.-C. E. S., Castro, M. O., Valente, A.-P., Biermann, C. H., and Mourão, P. A. S. (2002). Sulfated fucans from the egg jellies of the closely related sea urchins Strongylocentrotus droebachiensis and S. pallidus ensure species-specific fertilization. J. Biol. Chem. 277, 379-387.
    • (2002) J. Biol. Chem. , vol.277 , pp. 379-387
    • Vilela-Silva, A.-C.E.S.1    Castro, M.O.2    Valente, A.-P.3    Biermann, C.H.4    Mourão, P.A.S.5
  • 69
    • 0021921019 scopus 로고
    • Effects of egg extracts on sperm guanylate cyclase
    • Ward, G. E., Garbers, D. L., and Vacquier, V. D. (1985). Effects of egg extracts on sperm guanylate cyclase. Science 227, 768-770.
    • (1985) Science , vol.227 , pp. 768-770
    • Ward, G.E.1    Garbers, D.L.2    Vacquier, V.D.3
  • 70
    • 0022744296 scopus 로고
    • Phosphorylation of membrane-bound guanylate cyclase of sea urchin spermatozoa
    • Ward, G. E., Moy, G. W., and Vacquier, V. D. (1986). Phosphorylation of membrane-bound guanylate cyclase of sea urchin spermatozoa. J. Cell Biol. 103, 95-101.
    • (1986) J. Cell Biol. , vol.103 , pp. 95-101
    • Ward, G.E.1    Moy, G.W.2    Vacquier, V.D.3
  • 71
    • 0031002436 scopus 로고    scopus 로고
    • The Chlamydomonas mating type plus fertilization tubule, a prototypic cell fusion organelle: Isolation, characterization, and in vitro adhesion to mating type minus gametes
    • Wilson, N. F., Foglesong, M. J., and Snell, W. J. (1997). The Chlamydomonas mating type plus fertilization tubule, a prototypic cell fusion organelle: Isolation, characterization, and in vitro adhesion to mating type minus gametes. J. Cell Biol. 137, 1537-1553.
    • (1997) J. Cell Biol. , vol.137 , pp. 1537-1553
    • Wilson, N.F.1    Foglesong, M.J.2    Snell, W.J.3
  • 72
    • 0037437177 scopus 로고    scopus 로고
    • Speract induces calcium oscillations in the sperm tail
    • Wood, C. D., Darszon, A., and Whitaker, M. (2003). Speract induces calcium oscillations in the sperm tail. J. Cell Biol. 161, 89-101.
    • (2003) J. Cell Biol. , vol.161 , pp. 89-101
    • Wood, C.D.1    Darszon, A.2    Whitaker, M.3
  • 73
    • 0035745123 scopus 로고    scopus 로고
    • A study of helical and planar waves on sea urchin sperm flagella, with a theory of how they are generated
    • Woolley, D. M., and Vernon, G. G. (2001). A study of helical and planar waves on sea urchin sperm flagella, with a theory of how they are generated. J. Exp. Biol. 204, 1333-1345.
    • (2001) J. Exp. Biol. , vol.204 , pp. 1333-1345
    • Woolley, D.M.1    Vernon, G.G.2
  • 74
    • 0025287976 scopus 로고
    • The phosphocreatine shuttle of sea urchin sperm: Flagellar creatine kinase resulted from a gene triplication
    • Wothe, D. D., Charbonneau, H., and Shapiro, B. M. (1990). The phosphocreatine shuttle of sea urchin sperm: Flagellar creatine kinase resulted from a gene triplication. Proc. Natl. Acad. Sci. USA 87, 5203-5207.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 5203-5207
    • Wothe, D.D.1    Charbonneau, H.2    Shapiro, B.M.3
  • 75
    • 0037323873 scopus 로고    scopus 로고
    • Evolution of bindin in the pantropical sea urchin Tripneustes: Comparisons to bindin of other genera
    • Zigler, K. S., and Lessions, H. A. (2003a). Evolution of bindin in the pantropical sea urchin Tripneustes: Comparisons to bindin of other genera. Mol. Biol. Evol. 20, 220-231.
    • (2003) Mol. Biol. Evol. , vol.20 , pp. 220-231
    • Zigler, K.S.1    Lessions, H.A.2
  • 76
    • 0042427480 scopus 로고    scopus 로고
    • 250 Million years of bindin evolution
    • Zigler, K. S., and Lessios, H. A. (2003b). 250 million years of bindin evolution. Biol. Bull. 205, 8-15.
    • (2003) Biol. Bull. , vol.205 , pp. 8-15
    • Zigler, K.S.1    Lessios, H.A.2


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