메뉴 건너뛰기




Volumn 70, Issue 2, 2005, Pages 198-210

Actin polymerization in the equatorial and postacrosomal regions of guinea pig spermatozoa during the acrosome reaction is regulated by G proteins

Author keywords

Arp2 3; GDP S; GTP S; Lysophosphatidic acid; Profilin; Rho GTPases; WASp

Indexed keywords

ACTIN RELATED PROTEIN 2; ACTIN RELATED PROTEIN 3; F ACTIN; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANOSINE 5' O (2 THIODIPHOSPHATE); GUANOSINE 5' O (3 THIOTRIPHOSPHATE); GUANOSINE TRIPHOSPHATASE; LYSOPHOSPHATIDIC ACID; PROFILIN; PROTEIN CDC42; PROTEIN WASP; RHOA GUANINE NUCLEOTIDE BINDING PROTEIN; RHOB GUANINE NUCLEOTIDE BINDING PROTEIN; UNCLASSIFIED DRUG;

EID: 11244275411     PISSN: 1040452X     EISSN: None     Source Type: Journal    
DOI: 10.1002/mrd.20192     Document Type: Article
Times cited : (34)

References (77)
  • 1
    • 0029680639 scopus 로고    scopus 로고
    • Two GTPases, Cdc42, and Rac, bind directly to a protein implicated in the immunodeficiency disorder Wiskott-Aldrich syndrome
    • Aspenstrom P, Lindberg U, Hall A. 1996. Two GTPases, Cdc42, and Rac, bind directly to a protein implicated in the immunodeficiency disorder Wiskott-Aldrich syndrome. Curr Biol 6:70-75.
    • (1996) Curr Biol , vol.6 , pp. 70-75
    • Aspenstrom, P.1    Lindberg, U.2    Hall, A.3
  • 2
    • 0033545605 scopus 로고    scopus 로고
    • Actin polymerization: Where the WASP stings
    • Bi E, Zigmond SH. 1999. Actin polymerization: Where the WASP stings. Curr Biol 9:R160-R163.
    • (1999) Curr Biol , vol.9
    • Bi, E.1    Zigmond, S.H.2
  • 3
    • 0028828371 scopus 로고
    • The basic isoform of profilin in pathogenic Entamoeba histolytica, cDNA cloning, heterologous expression, and actin-binding properties
    • Binder M, Ortner S, Erben H, Scheiner O, Wiedermann G, Valenta R, Buchene M. 1995. The basic isoform of profilin in pathogenic Entamoeba histolytica, cDNA cloning, heterologous expression, and actin-binding properties. Eur J Biochem 233:976-981.
    • (1995) Eur J Biochem , vol.233 , pp. 976-981
    • Binder, M.1    Ortner, S.2    Erben, H.3    Scheiner, O.4    Wiedermann, G.5    Valenta, R.6    Buchene, M.7
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0030920630 scopus 로고    scopus 로고
    • Modulation of sperm acrosomal exocytosis by guanyl nucleotides and G-protein-modifier agents
    • Brandelli A. 1997. Modulation of sperm acrosomal exocytosis by guanyl nucleotides and G-protein-modifier agents. Biochem Mol Biol Int 41:1217-1225.
    • (1997) Biochem Mol Biol Int , vol.41 , pp. 1217-1225
    • Brandelli, A.1
  • 6
    • 0031937368 scopus 로고    scopus 로고
    • Localization of actobindin, profilin I, profilin II, and phosphatidylinositol-4,5-bisphosphate (PIP2) in Acantamoeba castellanii
    • Bubb MR, Baines IC, Korn ED. 1998. Localization of actobindin, profilin I, profilin II, and phosphatidylinositol-4,5-bisphosphate (PIP2) in Acantamoeba castellanii. Cell Motil Cytoskeleton 39:134-146.
    • (1998) Cell Motil Cytoskeleton , vol.39 , pp. 134-146
    • Bubb, M.R.1    Baines, I.C.2    Korn, E.D.3
  • 7
    • 0036196268 scopus 로고    scopus 로고
    • Lysophosphatidic acid and its role in reproduction
    • Budnik LT, Mukhopadhyay AK. 2002. Lysophosphatidic acid and its role in reproduction. Biol Reprod 66:859-865.
    • (2002) Biol Reprod , vol.66 , pp. 859-865
    • Budnik, L.T.1    Mukhopadhyay, A.K.2
  • 9
    • 0027420594 scopus 로고
    • Actin polymerization in boar spermatozoa: Fertilization is reduced with use of cytochalasin D
    • Castellani-Ceresa L, Mattioli M, Radaelli G, Barboni B, Brivio MF. 1993. Actin polymerization in boar spermatozoa: Fertilization is reduced with use of cytochalasin D. Mol Reprod Dev 36:203-211.
    • (1993) Mol Reprod Dev , vol.36 , pp. 203-211
    • Castellani-Ceresa, L.1    Mattioli, M.2    Radaelli, G.3    Barboni, B.4    Brivio, M.F.5
  • 11
    • 0025982039 scopus 로고
    • The role of actin polymerization in cell motility
    • Cooper JA. 1991. The role of actin polymerization in cell motility. Annu Rev Physiol 53:585-605.
    • (1991) Annu Rev Physiol , vol.53 , pp. 585-605
    • Cooper, J.A.1
  • 12
    • 0027937223 scopus 로고
    • Isolation of a novel gene mutated in Wiskott-Aldrich syndrome
    • Deny JM, Ochs HD, Francke U. 1994. Isolation of a novel gene mutated in Wiskott-Aldrich syndrome. Cell 78:635-644.
    • (1994) Cell , vol.78 , pp. 635-644
    • Deny, J.M.1    Ochs, H.D.2    Francke, U.3
  • 13
    • 0031568332 scopus 로고    scopus 로고
    • Transient expression of Dp140, a product of the Duchenne muscular dystrophy locus, during kidney tubulogenesis
    • Durbeej M, Jung D, Hjalt T, Campbell KP, Ekblom P. 1997. Transient expression of Dp140, a product of the Duchenne muscular dystrophy locus, during kidney tubulogenesis. Dev Biol 181:156-167.
    • (1997) Dev Biol , vol.181 , pp. 156-167
    • Durbeej, M.1    Jung, D.2    Hjalt, T.3    Campbell, K.P.4    Ekblom, P.5
  • 14
    • 0027275643 scopus 로고
    • Arole for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin
    • Ervasti JM, Campbell KP. 1993. Arole for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin. J Cell Biol 122:809-823.
    • (1993) J Cell Biol , vol.122 , pp. 809-823
    • Ervasti, J.M.1    Campbell, K.P.2
  • 15
    • 0033760991 scopus 로고    scopus 로고
    • Activation of protein kinase Cα in the lysophosphatidic acid-induced bovine sperm acrosome reaction and phospholipase D1 regulation
    • Garbi M, Rubinstein S, Lax Y, Breitbart H. 2000. Activation of protein kinase Cα in the lysophosphatidic acid-induced bovine sperm acrosome reaction and phospholipase D1 regulation. Biol Reprod 63:1271-1277.
    • (2000) Biol Reprod , vol.63 , pp. 1271-1277
    • Garbi, M.1    Rubinstein, S.2    Lax, Y.3    Breitbart, H.4
  • 16
    • 0024541333 scopus 로고
    • Identification of distinct cytoplasmic targets for ras/R-ras and rho regulatory proteins
    • Garrett MD, Self AJ, Van Oers C, Hall A. 1989. Identification of distinct cytoplasmic targets for ras/R-ras and rho regulatory proteins. J Biol Chem 264:10-13.
    • (1989) J Biol Chem , vol.264 , pp. 10-13
    • Garrett, M.D.1    Self, A.J.2    Van Oers, C.3    Hall, A.4
  • 17
    • 0028904661 scopus 로고
    • Distinct biochemical characteristics of the two human profilin isoforms
    • Gieselmann R, Kwiatkowski DJ, Janmey PA, Witke W. 1995. Distinct biochemical characteristics of the two human profilin isoforms. Eur J Biochem 229:621-628.
    • (1995) Eur J Biochem , vol.229 , pp. 621-628
    • Gieselmann, R.1    Kwiatkowski, D.J.2    Janmey, P.A.3    Witke, W.4
  • 18
    • 0025078512 scopus 로고
    • The cellular functions of small GTP-binding proteins
    • Hall A. 1990. The cellular functions of small GTP-binding proteins. Science 249:635-640.
    • (1990) Science , vol.249 , pp. 635-640
    • Hall, A.1
  • 19
    • 0032559362 scopus 로고    scopus 로고
    • Rho GTPases and the actin cytoskeleton
    • Hall A. 1998. Rho GTPases and the actin cytoskeleton. Science 279:509-514.
    • (1998) Science , vol.279 , pp. 509-514
    • Hall, A.1
  • 20
    • 0028004565 scopus 로고
    • Dictyostelium amoebae that lack G-actin-sequestering profilins show defects in F-actin content, cytokinesis, and development
    • Haugwitz M, Noegel AA, Karakesisoglou J, Schleicher M. 1994. Dictyostelium amoebae that lack G-actin-sequestering profilins show defects in F-actin content, cytokinesis, and development. Cell 79:303-314.
    • (1994) Cell , vol.79 , pp. 303-314
    • Haugwitz, M.1    Noegel, A.A.2    Karakesisoglou, J.3    Schleicher, M.4
  • 21
    • 0036403819 scopus 로고    scopus 로고
    • Novel actin-related proteins Arp-T1 and Arp-T2 as components of the cytoskeletal calyx of the mammalian sperm head
    • Heid H, Figge U, Winter S, Kuhn C, Zimbelmann R, Franke W. 2002. Novel actin-related proteins Arp-T1 and Arp-T2 as components of the cytoskeletal calyx of the mammalian sperm head. Exp Cell Res 279:177-187.
    • (2002) Exp Cell Res , vol.279 , pp. 177-187
    • Heid, H.1    Figge, U.2    Winter, S.3    Kuhn, C.4    Zimbelmann, R.5    Franke, W.6
  • 23
    • 0035694258 scopus 로고    scopus 로고
    • Comparative distribution of short dystrophin superfamily products in various guinea pig spermatozoa domains
    • Hernández-González EO, Martínez-Rojas D, Mornet D, Rendon A, Mújica A. 2001. Comparative distribution of short dystrophin superfamily products in various guinea pig spermatozoa domains. Eur J Cell Biol 80:792-798.
    • (2001) Eur J Cell Biol , vol.80 , pp. 792-798
    • Hernández-González, E.O.1    Martínez-Rojas, D.2    Mornet, D.3    Rendon, A.4    Mújica, A.5
  • 24
    • 0032702259 scopus 로고    scopus 로고
    • Regulation of actin polymerization by Arp2/3 complex and WASp/Scar proteins
    • Higgs HN, Pollard TD. 1999. Regulation of actin polymerization by Arp2/3 complex and WASp/Scar proteins. J Biol Chem 274:32531-32534.
    • (1999) J Biol Chem , vol.274 , pp. 32531-32534
    • Higgs, H.N.1    Pollard, T.D.2
  • 25
    • 0034683671 scopus 로고    scopus 로고
    • 2 of Wiskott-Aldrich syndrome protein (WASp) stimulates actin nucleation by Arp2/3 complex
    • 2 of Wiskott-Aldrich syndrome protein (WASp) stimulates actin nucleation by Arp2/3 complex. J Cell Biol 150:1311-1320.
    • (2000) J Cell Biol , vol.150 , pp. 1311-1320
    • Higgs, H.N.1    Pollard, T.D.2
  • 26
    • 0034911925 scopus 로고    scopus 로고
    • Regulation of actin filament network formation through ARP2/3 complex: Activation by a diverse array of proteins
    • Higgs HN, Pollard TD. 2001. Regulation of actin filament network formation through ARP2/3 complex: Activation by a diverse array of proteins. Annu Rev Biochem 70:649-676.
    • (2001) Annu Rev Biochem , vol.70 , pp. 649-676
    • Higgs, H.N.1    Pollard, T.D.2
  • 28
    • 0028036369 scopus 로고
    • Membrane interactions with the actin cytoskeleton
    • Hitt AL, Luna EJ. 1994. Membrane interactions with the actin cytoskeleton. Curr Opin Cell Biol 6:120-130.
    • (1994) Curr Opin Cell Biol , vol.6 , pp. 120-130
    • Hitt, A.L.1    Luna, E.J.2
  • 29
    • 0035185978 scopus 로고    scopus 로고
    • Cell motility: Proline-rich proteins promote protrusions
    • Holt MR, Koffer A. 2001. Cell motility: Proline-rich proteins promote protrusions. Trends Cell Biol 11:38-46.
    • (2001) Trends Cell Biol , vol.11 , pp. 38-46
    • Holt, M.R.1    Koffer, A.2
  • 30
    • 0035183921 scopus 로고    scopus 로고
    • Actin and actin-binding proteins in bovine spermatozoa: Potential role in membrane remodeling and intracellular signaling during epididymal maturation and the acrosome reaction
    • Howes EA, Hurst SM, Jones R. 2001. Actin and actin-binding proteins in bovine spermatozoa: Potential role in membrane remodeling and intracellular signaling during epididymal maturation and the acrosome reaction. J Androl 22:62-72.
    • (2001) J Androl , vol.22 , pp. 62-72
    • Howes, E.A.1    Hurst, S.M.2    Jones, R.3
  • 31
    • 0342905060 scopus 로고    scopus 로고
    • A perinuclear theca substructure is formed during epididymal guinea pig sperm maturation and disappears in acrosome reacted cells
    • Juárez-Mosqueda M, Mújica A. 1999. A perinuclear theca substructure is formed during epididymal guinea pig sperm maturation and disappears in acrosome reacted cells. J Struct Biol 128:225-236.
    • (1999) J Struct Biol , vol.128 , pp. 225-236
    • Juárez-Mosqueda, M.1    Mújica, A.2
  • 32
    • 0034624753 scopus 로고    scopus 로고
    • Autoinhibition and activation mechanisms of the Wiskott-Aldrich syndrome protein
    • Kim AS, Kakalis LT, Abdul-Manan N, Liu GA, Rosen MK. 2000. Autoinhibition and activation mechanisms of the Wiskott-Aldrich syndrome protein. Nature 404:151-158.
    • (2000) Nature , vol.404 , pp. 151-158
    • Kim, A.S.1    Kakalis, L.T.2    Abdul-Manan, N.3    Liu, G.A.4    Rosen, M.K.5
  • 33
    • 0033604638 scopus 로고    scopus 로고
    • Signaling to Rho GTPases
    • Kjøller L, Hall A. 1999. Signaling to Rho GTPases. Exp Cell Res 253:166-179.
    • (1999) Exp Cell Res , vol.253 , pp. 166-179
    • Kjøller, L.1    Hall, A.2
  • 34
    • 0019973176 scopus 로고
    • A simple and rapid method for purification of profilin from bovine thyroid
    • Kobayashi R, Bradley WA, Field JB. 1982. A simple and rapid method for purification of profilin from bovine thyroid. Anal Biochem 120:106-110.
    • (1982) Anal Biochem , vol.120 , pp. 106-110
    • Kobayashi, R.1    Bradley, W.A.2    Field, J.B.3
  • 37
    • 0028986034 scopus 로고
    • The Ras-related protein Cdc42Hs and bradykinin promote formation of peripheral actin microspikes and filopodia in Swiss 3T3 fibroblasts
    • Kozma R, Ahmed S, Best A, Lim L. 1995. The Ras-related protein Cdc42Hs and bradykinin promote formation of peripheral actin microspikes and filopodia in Swiss 3T3 fibroblasts. Mol Cell Biol 15:1942-1952.
    • (1995) Mol Cell Biol , vol.15 , pp. 1942-1952
    • Kozma, R.1    Ahmed, S.2    Best, A.3    Lim, L.4
  • 38
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 39
    • 0029011187 scopus 로고
    • Purification and characterization of bovine profilin II. Actin, poly(L-proline) and inositolphospholipid binding
    • Lambrechts A, Van Damme J, Goethals M, Vandekerckhove J, Ampe C. 1995. Purification and characterization of bovine profilin II. Actin, poly(L-proline) and inositolphospholipid binding. Eur J Biochem 230:281-286.
    • (1995) Eur J Biochem , vol.230 , pp. 281-286
    • Lambrechts, A.1    Van Damme, J.2    Goethals, M.3    Vandekerckhove, J.4    Ampe, C.5
  • 40
    • 0031024690 scopus 로고    scopus 로고
    • The mammalian profilin isoforms display complementary affinities for PIP2 and proline-rich sequences
    • Lambrechts A, Verschelde J, Jonckheere V, Goethals M, Vandekerckhove J, Ampe C. 1997. The mammalian profilin isoforms display complementary affinities for PIP2 and proline-rich sequences. EMBO J 16:484-494.
    • (1997) EMBO J , vol.16 , pp. 484-494
    • Lambrechts, A.1    Verschelde, J.2    Jonckheere, V.3    Goethals, M.4    Vandekerckhove, J.5    Ampe, C.6
  • 42
    • 0025793237 scopus 로고
    • Formation of the perinuclear theca in spermatozoa of diverse mammalian species: Relationship of the manchette and multiple band polypeptides
    • Longo FJ, Cook S. 1991. Formation of the perinuclear theca in spermatozoa of diverse mammalian species: Relationship of the manchette and multiple band polypeptides. Mol Reprod Dev 28:380-393.
    • (1991) Mol Reprod Dev , vol.28 , pp. 380-393
    • Longo, F.J.1    Cook, S.2
  • 43
    • 0026497661 scopus 로고
    • Cytoskeleton-plasma membrane interactions
    • Luna EJ, Hitt AL. 1992. Cytoskeleton-plasma membrane interactions. Science 258:955-964.
    • (1992) Science , vol.258 , pp. 955-964
    • Luna, E.J.1    Hitt, A.L.2
  • 44
    • 0021830154 scopus 로고
    • A novel ras-related gene family
    • Madaule P, Axel R. 1985. A novel ras-related gene family. Cell 41:31-40.
    • (1985) Cell , vol.41 , pp. 31-40
    • Madaule, P.1    Axel, R.2
  • 45
    • 0029815611 scopus 로고    scopus 로고
    • 2-dependent manner downstream of tyrosine kinases
    • 2-dependent manner downstream of tyrosine kinases. EMBO J 15:5326-5335.
    • (1996) EMBO J , vol.15 , pp. 5326-5335
    • Miki, H.1    Miura, K.2    Takenawa, T.3
  • 46
    • 0033604620 scopus 로고    scopus 로고
    • Bioactive lysophospholipids and their G protein-coupled receptors
    • Moolenaar WH. 1999. Bioactive lysophospholipids and their G protein-coupled receptors. Exp Cell Res 253:230-238.
    • (1999) Exp Cell Res , vol.253 , pp. 230-238
    • Moolenaar, W.H.1
  • 47
    • 0026662066 scopus 로고
    • F-actin in guinea pig spermatozoa: Its role in calmodulin translocation during acrosome reaction
    • Moreno-Fierros L, Hernández EO, Salgado ZO, Mújica A. 1992. F-actin in guinea pig spermatozoa: Its role in calmodulin translocation during acrosome reaction. Mol Reprod Dev 33:172-181.
    • (1992) Mol Reprod Dev , vol.33 , pp. 172-181
    • Moreno-Fierros, L.1    Hernández, E.O.2    Salgado, Z.O.3    Mújica, A.4
  • 48
    • 0033960791 scopus 로고    scopus 로고
    • How WASP-family proteins and the Arp2/3 complex convert intracellular signals into cytoskeletal structures
    • Mullins RD. 2000. How WASP-family proteins and the Arp2/3 complex convert intracellular signals into cytoskeletal structures. Curr Opin Cell Biol 12:91-96.
    • (2000) Curr Opin Cell Biol , vol.12 , pp. 91-96
    • Mullins, R.D.1
  • 49
    • 0033117823 scopus 로고    scopus 로고
    • Structure and function of the Arp2/3 complex
    • Mullins RD, Pollard TD. 1999a. Structure and function of the Arp2/3 complex. Curr Opin Struct Biol 9:244-249.
    • (1999) Curr Opin Struct Biol , vol.9 , pp. 244-249
    • Mullins, R.D.1    Pollard, T.D.2
  • 50
    • 0033594548 scopus 로고    scopus 로고
    • Rho-family GTPases require the ARP2/3 complex to stimulate actin polymerization in Acanthamoeba extracts
    • Mullins RD, Pollard TD. 1999b. Rho-family GTPases require the ARP2/3 complex to stimulate actin polymerization in Acanthamoeba extracts. Curr Biol 9:405-415.
    • (1999) Curr Biol , vol.9 , pp. 405-415
    • Mullins, R.D.1    Pollard, T.D.2
  • 51
    • 0000544299 scopus 로고
    • A simplified ultrasensitive silver stain for detecting proteins in polyacrylamide gels
    • Oakley BR, Kirsch DR, Morris NR. 1980. A simplified ultrasensitive silver stain for detecting proteins in polyacrylamide gels. Anal Biochem 105:361-363.
    • (1980) Anal Biochem , vol.105 , pp. 361-363
    • Oakley, B.R.1    Kirsch, D.R.2    Morris, N.R.3
  • 52
    • 0027772556 scopus 로고
    • How profilin promotes actin filament assembly in the presence of thymosin beta 4
    • Pantaloni D, Carlier MF. 1993. How profilin promotes actin filament assembly in the presence of thymosin beta 4. Cell. 75:1007-1014.
    • (1993) Cell. , vol.75 , pp. 1007-1014
    • Pantaloni, D.1    Carlier, M.F.2
  • 54
    • 0034721696 scopus 로고    scopus 로고
    • Integration of multiple signals through cooperative regulation of the N-WASP-Arp2/3 complex
    • Prehoda KE, Scott JA, Mullins RD, Lim WA. 2000. Integration of multiple signals through cooperative regulation of the N-WASP-Arp2/3 complex. Science 290:801-806.
    • (2000) Science , vol.290 , pp. 801-806
    • Prehoda, K.E.1    Scott, J.A.2    Mullins, R.D.3    Lim, W.A.4
  • 55
    • 0031465588 scopus 로고    scopus 로고
    • The GTP-binding protein Rho
    • Ridley AJ. 1997. The GTP-binding protein Rho. Int J Biochem Cell Biol 29:1225-1229.
    • (1997) Int J Biochem Cell Biol , vol.29 , pp. 1225-1229
    • Ridley, A.J.1
  • 56
    • 0026778133 scopus 로고
    • The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors
    • Ridley AJ, Hall A. 1992. The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell 70:389-399.
    • (1992) Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Hall, A.2
  • 57
    • 0016701307 scopus 로고
    • Retardation of guinea pig sperm acrosome reaction by glucose: The possible importance of pyruvate and lactate metabolism in capacitation and the acrosome reaction
    • Rogers BJ, Yanagimachi R. 1975. Retardation of guinea pig sperm acrosome reaction by glucose: The possible importance of pyruvate and lactate metabolism in capacitation and the acrosome reaction. Biol Reprod 13:568-575.
    • (1975) Biol Reprod , vol.13 , pp. 568-575
    • Rogers, B.J.1    Yanagimachi, R.2
  • 59
    • 0344653597 scopus 로고    scopus 로고
    • Effects of single amino acid substitutions in the actin-binding site on the biological activity of bovine profilin I
    • Schlüter K, Schleicher M, Jockusch BM. 1998. Effects of single amino acid substitutions in the actin-binding site on the biological activity of bovine profilin I. J Cell Sci 111:3261-3273.
    • (1998) J Cell Sci , vol.111 , pp. 3261-3273
    • Schlüter, K.1    Schleicher, M.2    Jockusch, B.M.3
  • 60
    • 0024832265 scopus 로고
    • Evidence of GTP-binding protein regulation of phospholipase A2 activity in isolated human platelet membranes
    • Silk ST, Clejan S, Witkom K. 1989. Evidence of GTP-binding protein regulation of phospholipase A2 activity in isolated human platelet membranes. J Biol Chem 264:21466-21469.
    • (1989) J Biol Chem , vol.264 , pp. 21466-21469
    • Silk, S.T.1    Clejan, S.2    Witkom, K.3
  • 62
    • 0030006284 scopus 로고    scopus 로고
    • Wiskott-Aldrich syndrome protein, a novel effector for the GTPase Cdc42Hs, is implicated in actin polymerization
    • Symons M, Derry JM, Karlak B, Jiang S, Lemahieu V, Mccormick F, Francke U, Abo A. 1996. Wiskott-Aldrich syndrome protein, a novel effector for the GTPase Cdc42Hs, is implicated in actin polymerization. Cell 84:723-734.
    • (1996) Cell , vol.84 , pp. 723-734
    • Symons, M.1    Derry, J.M.2    Karlak, B.3    Jiang, S.4    Lemahieu, V.5    Mccormick, F.6    Francke, U.7    Abo, A.8
  • 63
    • 0036888011 scopus 로고    scopus 로고
    • Cytochalasin-D retards sperm incorporation deep into the egg cytoplasm but not membrane fusion with the egg plasma membrane
    • Sánchez-Gutiérrez M, Contreras RG, Mújica A. 2002. Cytochalasin-D retards sperm incorporation deep into the egg cytoplasm but not membrane fusion with the egg plasma membrane. Mol Reprod Dev 63:518-528.
    • (2002) Mol Reprod Dev , vol.63 , pp. 518-528
    • Sánchez-Gutiérrez, M.1    Contreras, R.G.2    Mújica, A.3
  • 64
    • 0031042493 scopus 로고    scopus 로고
    • Rho, Rac, and Cdc42 GTPases regulate the organization of the actin cytoskeleton
    • Tapon N, Hall A. 1997. Rho, Rac, and Cdc42 GTPases regulate the organization of the actin cytoskeleton. Curr Opin Cell Biol 9:86-92.
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 86-92
    • Tapon, N.1    Hall, A.2
  • 65
    • 0034506070 scopus 로고    scopus 로고
    • The Wiskott-Aldrich syndrome: Disordered actin dynamics in haematopoietic cells
    • Thrasher AJ, Burns S, Lorenzi R, Jones GE. 2000. The Wiskott-Aldrich syndrome: Disordered actin dynamics in haematopoietic cells. Inmunol Rev 178:118-128.
    • (2000) Inmunol Rev , vol.178 , pp. 118-128
    • Thrasher, A.J.1    Burns, S.2    Lorenzi, R.3    Jones, G.E.4
  • 66
    • 0025830491 scopus 로고
    • A monoclonal antibody, MN13, that recognizes specifically a novel substance between the postacrosomal sheath and the overlying plasma membrane in the mammalian sperm head
    • Toshimori K, Tanii I, Oura C, Eddy EM. 1991. A monoclonal antibody, MN13, that recognizes specifically a novel substance between the postacrosomal sheath and the overlying plasma membrane in the mammalian sperm head. Mol Reprod Dev 29:289-293.
    • (1991) Mol Reprod Dev , vol.29 , pp. 289-293
    • Toshimori, K.1    Tanii, I.2    Oura, C.3    Eddy, E.M.4
  • 67
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H, Staehelin T, Gordon J. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications. Proc Natl Acad Sci USA 76:4350-4354.
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 68
    • 0025179017 scopus 로고
    • Changes in calmodulin compartmentalization throughout capacitation and acrosome reaction in guinea pig spermatozoa
    • Trejo R, Mújica A. 1990. Changes in calmodulin compartmentalization throughout capacitation and acrosome reaction in guinea pig spermatozoa. Mol Reprod Dev 26:366-376.
    • (1990) Mol Reprod Dev , vol.26 , pp. 366-376
    • Trejo, R.1    Mújica, A.2
  • 69
    • 0030968580 scopus 로고    scopus 로고
    • Rho GTPases and signaling networks
    • Van Aelst L, D'Souza-Schorey C. 1997. Rho GTPases and signaling networks. Genes Dev 11:2295-2322.
    • (1997) Genes Dev , vol.11 , pp. 2295-2322
    • Van Aelst, L.1    D'Souza-Schorey, C.2
  • 70
    • 0000121803 scopus 로고
    • Enzime linked inmunosorbent assay (ELISA)
    • Thompson RA, editor. London: Black Well Scientific Publications
    • Voller A, Savigny D. 1981. Enzime linked inmunosorbent assay (ELISA). In: Thompson RA, editor. Techiques in clinical inmunology. 2nd ed. London: Black Well Scientific Publications. pp 157-169.
    • (1981) Techiques in Clinical Inmunology. 2nd Ed. , pp. 157-169
    • Voller, A.1    Savigny, D.2
  • 72
    • 0000399649 scopus 로고
    • The extracellular matrix and cell shape
    • Watt FM. 1986. The extracellular matrix and cell shape. TIBS 11:482-485.
    • (1986) TIBS , vol.11 , pp. 482-485
    • Watt, F.M.1
  • 73
    • 0034649632 scopus 로고    scopus 로고
    • Actin dynamics: Assembly and disassembly of actin networks
    • Wear MA, Schafer DA, Cooper JA. 2000. Actin dynamics: Assembly and disassembly of actin networks. Curr Biol 10:R891-R895.
    • (2000) Curr Biol , vol.10
    • Wear, M.A.1    Schafer, D.A.2    Cooper, J.A.3
  • 75
    • 0002302562 scopus 로고
    • Mammalian fertilization
    • Knobil E, Neill JD, Ewing LL, Greenwold GS, Markert CL, Pfaff DW, editors. New York: Raven Press
    • Yanagimachi R. 1994. Mammalian fertilization. In: Knobil E, Neill JD, Ewing LL, Greenwold GS, Markert CL, Pfaff DW, editors. The physiology of reproduction, Vol. 1. New York: Raven Press. pp 190-302.
    • (1994) The Physiology of Reproduction , vol.1 , pp. 190-302
    • Yanagimachi, R.1
  • 77
    • 0030849454 scopus 로고    scopus 로고
    • Regulation of actin polymerization in cell-free systems by GTP-γ-S and Cdc42
    • Zigmond SH, Joyce M, Borleis J, Bokoch GM, Devreotes PN. 1997. Regulation of actin polymerization in cell-free systems by GTP-γ-S and Cdc42. J Cell Biol 138:363-374.
    • (1997) J Cell Biol , vol.138 , pp. 363-374
    • Zigmond, S.H.1    Joyce, M.2    Borleis, J.3    Bokoch, G.M.4    Devreotes, P.N.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.