메뉴 건너뛰기




Volumn 32, Issue 13, 2013, Pages 1886-1902

The nuclear F-actin interactome of Xenopus oocytes reveals an actin-bundling kinesin that is essential for meiotic cytokinesis

Author keywords

Cytokinesis; Kinesins; Meiosis; Nuclear actin; Pxhalloidin

Indexed keywords

ACTIN BINDING PROTEIN; ACTIN BUNDLING KINESIN; F ACTIN; KARYOPHERIN BETA; MYOSIN ADENOSINE TRIPHOSPHATASE; RAN PROTEIN; UNCLASSIFIED DRUG;

EID: 84880193973     PISSN: 02614189     EISSN: 14602075     Source Type: Journal    
DOI: 10.1038/emboj.2013.108     Document Type: Article
Times cited : (58)

References (71)
  • 1
    • 0024094841 scopus 로고
    • Proteins regulating actin assembly in oogenesis and early embryogenesis of Xenopus laevis: Gelsolin is the major cytoplasmic actin-binding protein
    • Ankenbauer T, Kleinschmidt JA, Vandekerckhove J, Franke WW (1988) Proteins regulating actin assembly in oogenesis and early embryogenesis of Xenopus laevis: gelsolin is the major cytoplasmic actin-binding protein. J Cell Biol 107: 1489-1498
    • (1988) J Cell Biol , vol.107 , pp. 1489-1498
    • Ankenbauer, T.1    Kleinschmidt, J.A.2    Vandekerckhove, J.3    Franke, W.W.4
  • 3
    • 33745484364 scopus 로고    scopus 로고
    • Visualization of the cytoskeleton in Xenopus oocytes and eggs by confocal immunofluorescence microscopy
    • Becker BE, Gard DL (2006) Visualization of the cytoskeleton in Xenopus oocytes and eggs by confocal immunofluorescence microscopy. Methods Mol Biol 322: 69-86
    • (2006) Methods Mol Biol , vol.322 , pp. 69-86
    • Becker, B.E.1    Gard, D.L.2
  • 5
    • 0022981734 scopus 로고
    • Initiation of DNA replication in nuclei and purified DNA by a cell-free extract of Xenopus eggs
    • Blow JJ, Laskey RA (1986) Initiation of DNA replication in nuclei and purified DNA by a cell-free extract of Xenopus eggs. Cell 47: 577-587
    • (1986) Cell , vol.47 , pp. 577-587
    • Blow, J.J.1    Laskey, R.A.2
  • 6
    • 33644747345 scopus 로고    scopus 로고
    • A selective block of nuclear actin export stabilizes the giant nuclei of Xenopus oocytes
    • Bohnsack MT, Stuven T, Kuhn C, Cordes VC, Gorlich D (2006) A selective block of nuclear actin export stabilizes the giant nuclei of Xenopus oocytes. Nat Cell Biol 8: 257-263
    • (2006) Nat Cell Biol , vol.8 , pp. 257-263
    • Bohnsack, M.T.1    Stuven, T.2    Kuhn, C.3    Cordes, V.C.4    Gorlich, D.5
  • 7
    • 79952723337 scopus 로고    scopus 로고
    • Active liquid-like behavior of nucleoli determines their size and shape in Xenopus laevis oocytes
    • Brangwynne CP, Mitchison TJ, Hyman AA (2011) Active liquid-like behavior of nucleoli determines their size and shape in Xenopus laevis oocytes. Proc Natl Acad Sci USA 108: 4334-4339
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 4334-4339
    • Brangwynne, C.P.1    Mitchison, T.J.2    Hyman, A.A.3
  • 8
    • 0033536178 scopus 로고    scopus 로고
    • Generation of GTP-bound Ran by RCC1 is required for chromatin-induced mitotic spindle formation
    • Carazo-Salas RE, Guarguaglini G, Gruss OJ, Segref A, Karsenti E, Mattaj IW (1999) Generation of GTP-bound Ran by RCC1 is required for chromatin-induced mitotic spindle formation. Nature 400: 178-181
    • (1999) Nature , vol.400 , pp. 178-181
    • Carazo-Salas, R.E.1    Guarguaglini, G.2    Gruss, O.J.3    Segref, A.4    Karsenti, E.5    Mattaj, I.W.6
  • 10
    • 84886632310 scopus 로고
    • Actin polymerizability is influenced by profilin, a low molecular weight protein in non-muscle cells
    • Carlsson L, Nystrom LE, Sundkvist I, Markey F, Lindberg U (1977) Actin polymerizability is influenced by profilin, a low molecular weight protein in non-muscle cells. J Mol Biol 115: 465-483
    • (1977) J Mol Biol , vol.115 , pp. 465-483
    • Carlsson, L.1    Nystrom, L.E.2    Sundkvist, I.3    Markey, F.4    Lindberg, U.5
  • 11
    • 0037462726 scopus 로고    scopus 로고
    • Involvement of Aurora A kinase during meiosis I-II transition in Xenopus oocytes
    • Castro A, Mandart E, Lorca T, Galas S (2003) Involvement of Aurora A kinase during meiosis I-II transition in Xenopus oocytes. J Biol Chem 278: 2236-2241
    • (2003) J Biol Chem , vol.278 , pp. 2236-2241
    • Castro, A.1    Mandart, E.2    Lorca, T.3    Galas, S.4
  • 13
    • 33748745132 scopus 로고    scopus 로고
    • INF2 Is a WASP homology 2 motif-containing formin that severs actin filaments and accelerates both polymerization and depolymerization
    • Chhabra ES, Higgs HN (2006) INF2 Is a WASP homology 2 motif-containing formin that severs actin filaments and accelerates both polymerization and depolymerization. J Biol Chem 281: 26754-26767
    • (2006) J Biol Chem , vol.281 , pp. 26754-26767
    • Chhabra, E.S.1    Higgs, H.N.2
  • 14
    • 79954529507 scopus 로고    scopus 로고
    • ProtTest 3: Fast selection of best-fit models of protein evolution
    • Darriba D, Taboada GL, Doallo R, Posada D (2011) ProtTest 3: fast selection of best-fit models of protein evolution. Bioinformatics 27: 1164-1165
    • (2011) Bioinformatics , vol.27 , pp. 1164-1165
    • Darriba, D.1    Taboada, G.L.2    Doallo, R.3    Posada, D.4
  • 16
    • 74949132733 scopus 로고    scopus 로고
    • Epithelial cell transforming protein 2 (ECT2) depletion blocks polar body extrusion and generates mouse oocytes containing two metaphase II spindles
    • Elbaz J, Reizel Y, Nevo N, Galiani D, Dekel N (2010) Epithelial cell transforming protein 2 (ECT2) depletion blocks polar body extrusion and generates mouse oocytes containing two metaphase II spindles. Endocrinology 151: 755-765
    • (2010) Endocrinology , vol.151 , pp. 755-765
    • Elbaz, J.1    Reizel, Y.2    Nevo, N.3    Galiani, D.4    Dekel, N.5
  • 17
    • 0026579853 scopus 로고
    • Simultaneous assay for amatoxins and phallotoxins in Amanita phalloides Fr. by high-performance liquid chromatography
    • Enjalbert F, Gallion C, Jehl F, Monteil H, Faulstich H (1992) Simultaneous assay for amatoxins and phallotoxins in Amanita phalloides Fr. by high-performance liquid chromatography. J Chromatogr 598: 227-236
    • (1992) J Chromatogr , vol.598 , pp. 227-236
    • Enjalbert, F.1    Gallion, C.2    Jehl, F.3    Monteil, H.4    Faulstich, H.5
  • 18
    • 84860514120 scopus 로고    scopus 로고
    • Molecular control of animal cell cytokinesis
    • Fededa JP, Gerlich DW (2012) Molecular control of animal cell cytokinesis. Nat Cell Biol 14: 440-447
    • (2012) Nat Cell Biol , vol.14 , pp. 440-447
    • Fededa, J.P.1    Gerlich, D.W.2
  • 20
    • 33646073458 scopus 로고    scopus 로고
    • Exporting actin
    • Gall JG (2006) Exporting actin. Nat Cell Biol 8: 205-207
    • (2006) Nat Cell Biol , vol.8 , pp. 205-207
    • Gall, J.G.1
  • 21
    • 0033558963 scopus 로고    scopus 로고
    • Confocal microscopy and 3-D reconstruction of the cytoskeleton of Xenopus oocytes
    • Gard D (1999) Confocal microscopy and 3-D reconstruction of the cytoskeleton of Xenopus oocytes. Microsc Res Tech 44: 388-414
    • (1999) Microsc Res Tech , vol.44 , pp. 388-414
    • Gard, D.1
  • 22
    • 0026717165 scopus 로고
    • Microtubule organization during maturation of Xenopus oocytes: Assembly and rotation of the meiotic spindles
    • Gard DL (1992) Microtubule organization during maturation of Xenopus oocytes: assembly and rotation of the meiotic spindles. Dev Biol 151: 516-530
    • (1992) Dev Biol , vol.151 , pp. 516-530
    • Gard, D.L.1
  • 23
    • 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 DL, Cha BJ, Roeder AD (1995) 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 3: 17-26
    • (1995) Zygote , vol.3 , pp. 17-26
    • Gard, D.L.1    Cha, B.J.2    Roeder, A.D.3
  • 24
    • 0029853631 scopus 로고    scopus 로고
    • Identification of different roles for RanGDP and RanGTP in nuclear protein import
    • Gorlich D, Pante N, Kutay U, Aebi U, Bischoff FR (1996) Identification of different roles for RanGDP and RanGTP in nuclear protein import. EMBO J 15: 5584-5594
    • (1996) EMBO J , vol.15 , pp. 5584-5594
    • Gorlich, D.1    Pante, N.2    Kutay, U.3    Aebi, U.4    Bischoff, F.R.5
  • 25
    • 0037416225 scopus 로고    scopus 로고
    • Characterization of Randriven cargo transport and the RanGTPase system by kinetic measurements and computer simulation
    • Gorlich D, Seewald MJ, Ribbeck K (2003) Characterization of Randriven cargo transport and the RanGTPase system by kinetic measurements and computer simulation. EMBO J 22: 1088-1100
    • (2003) EMBO J , vol.22 , pp. 1088-1100
    • Gorlich, D.1    Seewald, M.J.2    Ribbeck, K.3
  • 29
    • 0032605679 scopus 로고    scopus 로고
    • Microinjection into Xenopus oocytes and embryos
    • Guille M (1999) Microinjection into Xenopus oocytes and embryos. Methods Mol Biol 127: 111-123
    • (1999) Methods Mol Biol , vol.127 , pp. 111-123
    • Guille, M.1
  • 30
    • 80052591179 scopus 로고    scopus 로고
    • DiArk 2.0 provides detailed analyses of the ever increasing eukaryotic genome sequencing data
    • Hammesfahr B, Odronitz F, Hellkamp M, Kollmar M (2011) diArk 2.0 provides detailed analyses of the ever increasing eukaryotic genome sequencing data. BMC Res Notes 4: 338
    • (2011) BMC Res Notes , vol.4 , pp. 338
    • Hammesfahr, B.1    Odronitz, F.2    Hellkamp, M.3    Kollmar, M.4
  • 31
    • 0019519262 scopus 로고
    • Germinal vesicle breakdown in the Xenopus laevis oocyte: Description of a transient microtubular structure
    • Huchon D, Crozet N, Cantenot N, Ozon R (1981) Germinal vesicle breakdown in the Xenopus laevis oocyte: description of a transient microtubular structure. Reprod Nutr Dev 21: 135-148
    • (1981) Reprod Nutr Dev , vol.21 , pp. 135-148
    • Huchon, D.1    Crozet, N.2    Cantenot, N.3    Ozon, R.4
  • 32
    • 0026585534 scopus 로고
    • Changes of drebrin expression in the visual cortex of the cat during development
    • Imamura K, Shirao T, Mori K, Obata K (1992) Changes of drebrin expression in the visual cortex of the cat during development. Neurosci Res 13: 33-41
    • (1992) Neurosci Res , vol.13 , pp. 33-41
    • Imamura, K.1    Shirao, T.2    Mori, K.3    Obata, K.4
  • 33
    • 0019256032 scopus 로고
    • An actin-binding protein from Acanthamoeba regulates actin filament polymerization and interactions
    • Isenberg G, Aebi U, Pollard TD (1980) An actin-binding protein from Acanthamoeba regulates actin filament polymerization and interactions. Nature 288: 455-459
    • (1980) Nature , vol.288 , pp. 455-459
    • Isenberg, G.1    Aebi, U.2    Pollard, T.D.3
  • 34
    • 0040251482 scopus 로고    scopus 로고
    • Importin beta, transportin, RanBP5 and RanBP7 mediate nuclear import of ribosomal proteins in mammalian cells
    • Jakel S, Gorlich D (1998) Importin beta, transportin, RanBP5 and RanBP7 mediate nuclear import of ribosomal proteins in mammalian cells. EMBO J 17: 4491-4502
    • (1998) EMBO J , vol.17 , pp. 4491-4502
    • Jakel, S.1    Gorlich, D.2
  • 36
    • 0033528994 scopus 로고    scopus 로고
    • The Ran GTPase regulates mitotic spindle assembly
    • Kalab P, Pu RT, Dasso M (1999) The Ran GTPase regulates mitotic spindle assembly. Curr Biol 9: 481-484
    • (1999) Curr Biol , vol.9 , pp. 481-484
    • Kalab, P.1    Pu, R.T.2    Dasso, M.3
  • 37
    • 79959760930 scopus 로고    scopus 로고
    • The role of RanGTP gradient in vertebrate oocyte maturation
    • Kalab P, Solc P, Motl?k J (2011) The role of RanGTP gradient in vertebrate oocyte maturation. Results Probl Cell Differ 53: 235-267
    • (2011) Results Probl Cell Differ , vol.53 , pp. 235-267
    • Kalab, P.1    Solc, P.2    Motlk, J.3
  • 38
    • 0023613813 scopus 로고
    • The events of the midblastula transition in Xenopus are regulated by changes in the cell cycle
    • Kimelman D, Kirschner M, Scherson T (1987) The events of the midblastula transition in Xenopus are regulated by changes in the cell cycle. Cell 48: 399-407
    • (1987) Cell , vol.48 , pp. 399-407
    • Kimelman, D.1    Kirschner, M.2    Scherson, T.3
  • 39
    • 0037018147 scopus 로고    scopus 로고
    • CHO1, a mammalian kinesin-like protein, interacts with F-actin and is involved in the terminal phase of cytokinesis
    • Kuriyama R, Gustus C, Terada Y, Uetake Y, Matuliene J (2002) CHO1, a mammalian kinesin-like protein, interacts with F-actin and is involved in the terminal phase of cytokinesis. J Cell Biol 156: 783-790
    • (2002) J Cell Biol , vol.156 , pp. 783-790
    • Kuriyama, R.1    Gustus, C.2    Terada, Y.3    Uetake, Y.4    Matuliene, J.5
  • 40
    • 1642333310 scopus 로고    scopus 로고
    • Relating biochemistry and function in the myosin superfamily
    • La Cruz DeEM, Ostap EM (2004) Relating biochemistry and function in the myosin superfamily. Curr Opin Cell Biol 16: 61-67
    • (2004) Curr Opin Cell Biol , vol.16 , pp. 61-67
    • Cruz Deem, L.1    Ostap, E.M.2
  • 41
    • 79955774272 scopus 로고    scopus 로고
    • The small GTPase Cdc42 promotes membrane protrusion during polar body emission via ARP2-nucleated actin polymerization
    • Leblanc J, Zhang X, McKee D, Wang Z-B, Li R, Ma C, Sun Q-Y, Liu XJ (2011) The small GTPase Cdc42 promotes membrane protrusion during polar body emission via ARP2-nucleated actin polymerization. Mol Hum Reprod 17: 305-316
    • (2011) Mol Hum Reprod , vol.17 , pp. 305-316
    • Leblanc, J.1    Zhang, X.2    McKee, D.3    Wang, Z.-B.4    Li, R.5    Ma, C.6    Sun, Q.-Y.7    Liu, X.J.8
  • 42
    • 84862221167 scopus 로고    scopus 로고
    • SMART 7: Recent updates to the protein domain annotation resource
    • Letunic I, Doerks T, Bork P (2011) SMART 7: recent updates to the protein domain annotation resource. Nucleic Acids Res 40: D302-D305
    • (2011) Nucleic Acids Res , vol.40
    • Letunic, I.1    Doerks, T.2    Bork, P.3
  • 44
    • 84867985318 scopus 로고    scopus 로고
    • Polar body emission
    • Liu XJ (2012) Polar body emission. Cytoskeleton 69: 670-685
    • (2012) Cytoskeleton , vol.69 , pp. 670-685
    • Liu, X.J.1
  • 45
    • 33745480218 scopus 로고    scopus 로고
    • Oocyte isolation and enucleation
    • Liu XS, Liu XJ (2006) Oocyte isolation and enucleation. Methods Mol Biol 322: 31-41
    • (2006) Methods Mol Biol , vol.322 , pp. 31-41
    • Liu, X.S.1    Liu, X.J.2
  • 46
    • 0016283134 scopus 로고
    • The interaction of phalloidin Some of its derivatives, and of other cyclic peptides with muscle actin as studied by viscosimetry
    • Low I, Wieland T (1974) The interaction of phalloidin. Some of its derivatives, and of other cyclic peptides with muscle actin as studied by viscosimetry. FEBS Lett 44: 340-343
    • (1974) FEBS Lett , vol.44 , pp. 340-343
    • Low, I.1    Wieland, T.2
  • 47
    • 0026356891 scopus 로고
    • Predicting coiled coils from protein sequences
    • Lupas A, Van Dyke M, Stock J (1991) Predicting coiled coils from protein sequences. Science 252: 1162-1164
    • (1991) Science , vol.252 , pp. 1162-1164
    • Lupas, A.1    Van Dyke, M.2    Stock, J.3
  • 49
    • 3042847011 scopus 로고    scopus 로고
    • Role of the midbody matrix in cytokinesis: RNAi and genetic rescue analysis of the mammalian motor protein CHO1
    • Matuliene J, Kuriyama R (2004) Role of the midbody matrix in cytokinesis: RNAi and genetic rescue analysis of the mammalian motor protein CHO1. Mol Biol Cell 15: 3083-3094
    • (2004) Mol Biol Cell , vol.15 , pp. 3083-3094
    • Matuliene, J.1    Kuriyama, R.2
  • 50
    • 79955683477 scopus 로고    scopus 로고
    • Nuclear actin polymerization is required for transcriptional reprogramming of Oct4 by oocytes
    • Miyamoto K, Pasque V, Jullien J, Gurdon JB (2011) Nuclear actin polymerization is required for transcriptional reprogramming of Oct4 by oocytes. Genes Dev 25: 946-958
    • (2011) Genes Dev , vol.25 , pp. 946-958
    • Miyamoto, K.1    Pasque, V.2    Jullien, J.3    Gurdon, J.B.4
  • 51
    • 79953770641 scopus 로고    scopus 로고
    • Intracellular transport by an anchored homogeneously contracting F-actin meshwork
    • Mori M, Monnier N, Daigle N, Bathe M, Ellenberg J, Lenart P (2011) Intracellular transport by an anchored homogeneously contracting F-actin meshwork. Curr Biol 21: 606-611
    • (2011) Curr Biol , vol.21 , pp. 606-611
    • Mori, M.1    Monnier, N.2    Daigle, N.3    Bathe, M.4    Ellenberg, J.5    Lenart, P.6
  • 52
    • 0032568650 scopus 로고    scopus 로고
    • The interaction of Arp2/3 complex with actin: Nucleation, high affinity pointed end capping, and formation of branching networks of filaments
    • Mullins DD, Heuser JA, Pollard TD (1998) The interaction of Arp2/3 complex with actin: nucleation, high affinity pointed end capping, and formation of branching networks of filaments. Proc Natl Acad Sci USA 95: 6181-6186
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 6181-6186
    • Mullins, D.D.1    Heuser, J.A.2    Pollard, T.D.3
  • 53
    • 33845605457 scopus 로고    scopus 로고
    • Pfarao: A web application for protein family analysis customized for cytoskeletal and motor proteins (CyMoBase)
    • Odronitz F, Kollmar M (2006) Pfarao: a web application for protein family analysis customized for cytoskeletal and motor proteins (CyMoBase). BMC Genomics 7: 300
    • (2006) BMC Genomics , vol.7 , pp. 300
    • Odronitz, F.1    Kollmar, M.2
  • 55
    • 0030831613 scopus 로고    scopus 로고
    • Supervillin (p205): A novel membrane-associated, F-actin-binding protein in the villin/gelsolin superfamily
    • Pestonjamasp KN, Pope RK, Wulfkuhle JD, Luna EJ (1997) Supervillin (p205): A novel membrane-associated, F-actin-binding protein in the villin/gelsolin superfamily. J Cell Biol 139: 1255-1269
    • (1997) J Cell Biol , vol.139 , pp. 1255-1269
    • Pestonjamasp, K.N.1    Pope, R.K.2    Wulfkuhle, J.D.3    Luna, E.J.4
  • 56
    • 70849098888 scopus 로고    scopus 로고
    • Actin, a central player in cell shape and movement
    • Pollard TD, Cooper JA (2009) Actin, a central player in cell shape and movement. Science 326: 1208-1212
    • (2009) Science , vol.326 , pp. 1208-1212
    • Pollard, T.D.1    Cooper, J.A.2
  • 58
    • 0041386108 scopus 로고    scopus 로고
    • MrBayes 3: Bayesian phylogenetic inference under mixed models
    • Ronquist F, Huelsenbeck JP (2003) MrBayes 3: Bayesian phylogenetic inference under mixed models. Bioinformatics 19: 1572-1574
    • (2003) Bioinformatics , vol.19 , pp. 1572-1574
    • Ronquist, F.1    Huelsenbeck, J.P.2
  • 59
    • 70349759984 scopus 로고    scopus 로고
    • ITRAQ-labeling of in-gel digested proteins for relative quantification
    • Schmidt C, Urlaub H (2009) iTRAQ-labeling of in-gel digested proteins for relative quantification. Methods Mol Biol 564: 207-226
    • (2009) Methods Mol Biol , vol.564 , pp. 207-226
    • Schmidt, C.1    Urlaub, H.2
  • 60
    • 34547488455 scopus 로고    scopus 로고
    • Role of actin cytoskeleton in dendritic spine morphogenesis
    • Sekino Y, Kojima N, Shirao T (2007) Role of actin cytoskeleton in dendritic spine morphogenesis. Neurochem Int 51: 92-104
    • (2007) Neurochem Int , vol.51 , pp. 92-104
    • Sekino, Y.1    Kojima, N.2    Shirao, T.3
  • 62
    • 50249100595 scopus 로고    scopus 로고
    • A rapid bootstrap algorithm for the RAxML web servers
    • Stamatakis A, Hoover P, Rougemont J (2008) A rapid bootstrap algorithm for the RAxML web servers. Syst Biol 57: 758-771
    • (2008) Syst Biol , vol.57 , pp. 758-771
    • Stamatakis, A.1    Hoover, P.2    Rougemont, J.3
  • 63
    • 0242641546 scopus 로고    scopus 로고
    • Exportin 6: A novel nuclear export receptor that is specific for profilin.actin complexes
    • Stuven T, Hartmann E, Gorlich D (2003) Exportin 6: a novel nuclear export receptor that is specific for profilin.actin complexes. EMBO J 22: 5928-5940
    • (2003) EMBO J , vol.22 , pp. 5928-5940
    • Stuven, T.1    Hartmann, E.2    Gorlich, D.3
  • 64
    • 34250849566 scopus 로고    scopus 로고
    • Nuclear actin regulates dynamic subcellular localization and activity of the SRF cofactor MAL
    • Vartiainen MK, Guettler S, Larijani B, Treisman R (2007) Nuclear actin regulates dynamic subcellular localization and activity of the SRF cofactor MAL. Science 316: 1749-1752
    • (2007) Science , vol.316 , pp. 1749-1752
    • Vartiainen, M.K.1    Guettler, S.2    Larijani, B.3    Treisman, R.4
  • 65
    • 0039154943 scopus 로고
    • Filamin, a new high-molecularweight protein found in smooth muscle and non-muscle cells
    • Wang K, Ash JF, Singer SJ (1975) Filamin, a new high-molecularweight protein found in smooth muscle and non-muscle cells. Proc Natl Acad Sci USA 72: 4483-4486
    • (1975) Proc Natl Acad Sci USA , vol.72 , pp. 4483-4486
    • Wang, K.1    Ash, J.F.2    Singer, S.J.3
  • 66
    • 4644326930 scopus 로고    scopus 로고
    • A microtubule-binding myosin required for nuclear anchoring and spindle assembly
    • Weber KL, Sokac AM, Berg JS, Cheney RE, Bement WM (2004) A microtubule-binding myosin required for nuclear anchoring and spindle assembly. Nature 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
  • 67
    • 0035031966 scopus 로고    scopus 로고
    • A general empirical model of protein evolution derived from multiple protein families using a maximum-likelihood approach
    • Whelan S, Goldman N (2001) A general empirical model of protein evolution derived from multiple protein families using a maximum-likelihood approach. Mol Biol Evol 18: 691-699
    • (2001) Mol Biol Evol , vol.18 , pp. 691-699
    • Whelan, S.1    Goldman, N.2
  • 68
    • 0021041671 scopus 로고
    • Components of the green deathcap mushroom (amanita-phalloides).LXI Delta-aminophalloin, a 7-analogue of phalloidin, and some biochemically useful, including fluorescent derivatives
    • Wieland T, Hollosi M, Nassal M (1983) Components of the green deathcap mushroom (amanita-phalloides).LXI. Delta-aminophalloin, a 7-analogue of phalloidin, and some biochemically useful, including fluorescent derivatives. Liebigs Ann Chem 9: 1533-1540
    • (1983) Liebigs Ann Chem , vol.9 , pp. 1533-1540
    • Wieland, T.1    Hollosi, M.2    Nassal, M.3
  • 69
    • 47549089279 scopus 로고    scopus 로고
    • Myosin-10 and actin filaments are essential for mitotic spindle function
    • Woolner S, O'Brien LL, Wiese C, Bement WM (2008) Myosin-10 and actin filaments are essential for mitotic spindle function. J Cell Biol 182: 77-88
    • (2008) J Cell Biol , vol.182 , pp. 77-88
    • Woolner, S.1    O'brien, L.L.2    Wiese, C.3    Bement, W.M.4
  • 70
    • 0032820201 scopus 로고    scopus 로고
    • Domain analysis of supervillin, an F-actin bundling plasma membrane protein with functional nuclear localization signals
    • Wulfkuhle JD, Donina IE, Stark NH, Pope RK, Pestonjamasp KN, Niswonger ML, Luna EJ (1999) Domain analysis of supervillin, an F-actin bundling plasma membrane protein with functional nuclear localization signals. J Cell Sci 112(Pt 13): 2125-2136
    • (1999) J Cell Sci , vol.112 , Issue.PART 13 , pp. 2125-2136
    • Wulfkuhle, J.D.1    Donina, I.E.2    Stark, N.H.3    Pope, R.K.4    Pestonjamasp, K.N.5    Niswonger, M.L.6    Luna, E.J.7
  • 71
    • 51449114844 scopus 로고    scopus 로고
    • Polar body emission requires a RhoA contractile ring and Cdc42-mediated membrane protrusion
    • Zhang X, Ma C, Miller AL, Katbi HA, Bement WM, Liu XJ (2008) Polar body emission requires a RhoA contractile ring and Cdc42-mediated membrane protrusion. Dev Cell 15: 386-400
    • (2008) Dev Cell , vol.15 , pp. 386-400
    • Zhang, X.1    Ma, C.2    Miller, A.L.3    Katbi, H.A.4    Bement, W.M.5    Liu, X.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.