메뉴 건너뛰기




Volumn 5, Issue , 2014, Pages

Kinesin-14 and kinesin-5 antagonistically regulate microtubule nucleation by γ-TuRC in yeast and human cells

Author keywords

[No Author keywords available]

Indexed keywords

GAMMA TUBULIN; GAMMA TUBULIN RING COMPLEX; KINESIN; KINESIN 14; KINESIN 5; UNCLASSIFIED DRUG; PEPTIDE; PROTEIN BINDING; SCHIZOSACCHAROMYCES POMBE PROTEIN; TUBULIN;

EID: 84923226696     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms6339     Document Type: Article
Times cited : (44)

References (69)
  • 1
    • 0037418910 scopus 로고    scopus 로고
    • Mitosis through the microscope: Advances in seeing inside live dividing cells
    • Rieder, C. & Khodjakov, A. Mitosis through the microscope: advances in seeing inside live dividing cells. Science 300, 91-96 (2003).
    • (2003) Science , vol.300 , pp. 91-96
    • Rieder, C.1    Khodjakov, A.2
  • 4
    • 0000292359 scopus 로고
    • The evolution of the mitotic apparatus: An attempt at comparative ultrastructural plant cytology in dividing plant cells
    • Pickett-Heaps, J. D. The evolution of the mitotic apparatus: an attempt at comparative ultrastructural plant cytology in dividing plant cells. Cytobios 1, 257-280 (1969).
    • (1969) Cytobios , vol.1 , pp. 257-280
    • Pickett-Heaps, J.D.1
  • 5
    • 0024589503 scopus 로고
    • Identification of gamma-tubulin, a new member of the tubulin superfamily encoded by mipA gene of Aspergillus nidulans
    • Oakley, C. E. & Oakley, B. R. Identification of gamma-tubulin, a new member of the tubulin superfamily encoded by mipA gene of Aspergillus nidulans. Nature 338, 662-664 (1989).
    • (1989) Nature , vol.338 , pp. 662-664
    • Oakley, C.E.1    Oakley, B.R.2
  • 6
    • 0025849047 scopus 로고
    • γ-tubulin is a highly conserved component of the centrosome
    • Stearns, T., Evans, L. & Kirschner, M. γ-tubulin is a highly conserved component of the centrosome. Cell 65, 625-636 (1991).
    • (1991) Cell , vol.65 , pp. 625-636
    • Stearns, T.1    Evans, L.2    Kirschner, M.3
  • 7
    • 0033775854 scopus 로고    scopus 로고
    • Structure of the γ-tubulin ring complex: A template for microtubule nucleation
    • Moritz, M. et al. Structure of the γ-tubulin ring complex: a template for microtubule nucleation. Nat. Cell Biol. 2, 365-370 (2000).
    • (2000) Nat. Cell Biol. , vol.2 , pp. 365-370
    • Moritz, M.1
  • 8
    • 33751160346 scopus 로고    scopus 로고
    • Microtubule nucleation: γ-tubulin and beyond
    • Wiese, C. & Zheng, Y. Microtubule nucleation: γ-tubulin and beyond. J. Cell Sci. 119, 4143-4153 (2006).
    • (2006) J. Cell Sci. , vol.119 , pp. 4143-4153
    • Wiese, C.1    Zheng, Y.2
  • 9
    • 33847776094 scopus 로고    scopus 로고
    • Microtubule-organizing centres: A re-evaluation
    • Lüders, J. & Stearns, T. Microtubule-organizing centres: a re-evaluation. Nat. Rev. Mol. Cell Biol. 8, 161-167 (2007).
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 161-167
    • Lüders, J.1    Stearns, T.2
  • 10
    • 0032495513 scopus 로고    scopus 로고
    • Structure of the α/β-tubulin dimer by electron crystallography
    • Nogales, E., Wolf, S. G. & Downing, K. H. Structure of the α/β-tubulin dimer by electron crystallography. Nature 391, 199-203 (1998).
    • (1998) Nature , vol.391 , pp. 199-203
    • Nogales, E.1    Wolf, S.G.2    Downing, K.H.3
  • 11
    • 19544384914 scopus 로고    scopus 로고
    • Insights into microtubule nucleation from the crystal structure of human γ-tubulin
    • Aldaz, H., Rice, L. M., Stearns, T. & Agard, D. A. Insights into microtubule nucleation from the crystal structure of human γ-tubulin. Nature 435, 523-527 (2005).
    • (2005) Nature , vol.435 , pp. 523-527
    • Aldaz, H.1    Rice, L.M.2    Stearns, T.3    Agard, D.A.4
  • 12
    • 79961027813 scopus 로고    scopus 로고
    • Crystal structure of γ-tubulin complex protein GCP4 provides insight into microtubule nucleation
    • Guillet, V. et al. Crystal structure of γ-tubulin complex protein GCP4 provides insight into microtubule nucleation. Nat. Struc. Mol. Biol. 18, 915-921 (2011).
    • (2011) Nat. Struc. Mol. Biol. , vol.18 , pp. 915-921
    • Guillet, V.1
  • 13
    • 38749100508 scopus 로고    scopus 로고
    • The structure of the γ-tubulin small complex: Implications of its architecture and flexibility for microtubule nucleation
    • Kollman, J. M. et al. The structure of the γ-tubulin small complex: implications of its architecture and flexibility for microtubule nucleation. MBoC 19, 207-215 (2008).
    • (2008) MBoC , vol.19 , pp. 207-215
    • Kollman, J.M.1
  • 14
    • 0027935027 scopus 로고
    • Human γ-tubulin functions in fission yeast
    • Horio, T. & Oakley, B. R. Human γ-tubulin functions in fission yeast. J. Cell Biol. 126, 1465-1473 (1994).
    • (1994) J. Cell Biol. , vol.126 , pp. 1465-1473
    • Horio, T.1    Oakley, B.R.2
  • 15
    • 84885455196 scopus 로고    scopus 로고
    • Functional conservation of fission yeast γ-tubulin small complex proteins Alp4 and Alp6 by human GCP2 and GCP3
    • Riehlman, T. R. et al. Functional conservation of fission yeast γ-tubulin small complex proteins Alp4 and Alp6 by human GCP2 and GCP3. J. Cell Sci. 126, 4406-4413 (2013).
    • (2013) J. Cell Sci. , vol.126 , pp. 4406-4413
    • Riehlman, T.R.1
  • 16
    • 84884485078 scopus 로고    scopus 로고
    • Fission yeast MOZART/Mzt1 is an essential γ-tubulin complex component for complex recruitment to the microtubule organizing center, but not its assembly
    • Masuda, H., Mori, R., Yukawa, M. & Toda, T. Fission yeast MOZART/Mzt1 is an essential γ-tubulin complex component for complex recruitment to the microtubule organizing center, but not its assembly. MBoC 24, 2894-2906 (2013).
    • (2013) MBoC , vol.24 , pp. 2894-2906
    • Masuda, H.1    Mori, R.2    Yukawa, M.3    Toda, T.4
  • 17
    • 84874627818 scopus 로고    scopus 로고
    • Kinesin-14 Pkl1 targets γ-tubulin for release from the γ-tubulin ring complex (γ-TuRC)
    • Olmsted, Z. T. et al. Kinesin-14 Pkl1 targets γ-tubulin for release from the γ-tubulin ring complex (γ-TuRC). Cell Cycle 12, 842-848 (2013).
    • (2013) Cell Cycle , vol.12 , pp. 842-848
    • Olmsted, Z.T.1
  • 18
    • 0029794091 scopus 로고    scopus 로고
    • Fission yeast pkl1 is a kinesin-related protein involved in mitotic spindle function
    • Pidoux, A. L., LeDizet, M. & Cande, W. Z. Fission yeast pkl1 is a kinesin-related protein involved in mitotic spindle function. MBoC 7, 1639-1655 (1996).
    • (1996) MBoC , vol.7 , pp. 1639-1655
    • Pidoux, A.L.1    LeDizet, M.2    Cande, W.Z.3
  • 19
    • 0030933383 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae kinesin-related motor Kar3p acts a preanaphase spindle poles to limit the number and length of cytoplasmic microtubules
    • Saunders, W., Hornack, D., Lengyel, V. & Deng, C. The Saccharomyces cerevisiae kinesin-related motor Kar3p acts a preanaphase spindle poles to limit the number and length of cytoplasmic microtubules. J. Cell Biol. 137, 417-431 (1997).
    • (1997) J. Cell Biol. , vol.137 , pp. 417-431
    • Saunders, W.1    Hornack, D.2    Lengyel, V.3    Deng, C.4
  • 20
    • 34250348345 scopus 로고    scopus 로고
    • Mitotic chromosome biorientation in fission yeast is enhanced by dynein and a minus-end directed, kinesin-like protein
    • Grishchuk, E. L., Spiridonov, I. S. & McIntosh, J. R. Mitotic chromosome biorientation in fission yeast is enhanced by dynein and a minus-end directed, kinesin-like protein. MBoC 18, 2216-2225 (2007).
    • (2007) MBoC , vol.18 , pp. 2216-2225
    • Grishchuk, E.L.1    Spiridonov, I.S.2    McIntosh, J.R.3
  • 21
    • 77953133964 scopus 로고    scopus 로고
    • Proper organization of microtubule minus-ends is needed for midzone stability and cytokinesis
    • Cai, S., Weaver, L. N., Ems-McClung, S. C. & Walczak, C. E. Proper organization of microtubule minus-ends is needed for midzone stability and cytokinesis. Curr. Biol. 20, 880-885 (2010).
    • (2010) Curr. Biol. , vol.20 , pp. 880-885
    • Cai, S.1    Weaver, L.N.2    Ems-McClung, S.C.3    Walczak, C.E.4
  • 22
    • 44349176903 scopus 로고    scopus 로고
    • Protein complexes at the microtubule organizing center regulate bipolar spindle assembly
    • Rodriguez, A. S. et al. Protein complexes at the microtubule organizing center regulate bipolar spindle assembly. Cell Cycle 7, 1246-1253 (2008).
    • (2008) Cell Cycle , vol.7 , pp. 1246-1253
    • Rodriguez, A.S.1
  • 23
    • 70449717040 scopus 로고    scopus 로고
    • Distinct kinesin-14 mitotic mechanisms in spindle bipolarity
    • Simeonov, D. R. et al. Distinct kinesin-14 mitotic mechanisms in spindle bipolarity. Cell Cycle 8, 3563-3575 (2009).
    • (2009) Cell Cycle , vol.8 , pp. 3563-3575
    • Simeonov, D.R.1
  • 24
    • 0034044992 scopus 로고    scopus 로고
    • A mutation in γ-tubulin alters microtubule dynamics and organization and is synthetically lethal with the Klp Pkl1p
    • Paluh, J. L. et al. A mutation in γ-tubulin alters microtubule dynamics and organization and is synthetically lethal with the Klp Pkl1p. MBoC 11, 1225-1239 (2000).
    • (2000) MBoC , vol.11 , pp. 1225-1239
    • Paluh, J.L.1
  • 25
    • 3843148390 scopus 로고    scopus 로고
    • Functional dissection of the γ-tubulin complex by suppressor analysis of gtb1 and alp4 mutations in Schizosaccharomyces pombe
    • Tange, Y., Fujita, A., Toda, T. & Niwa, O. Functional dissection of the γ-tubulin complex by suppressor analysis of gtb1 and alp4 mutations in Schizosaccharomyces pombe. Genetics 167, 1095-1107 (2004).
    • (2004) Genetics , vol.167 , pp. 1095-1107
    • Tange, Y.1    Fujita, A.2    Toda, T.3    Niwa, O.4
  • 26
    • 33746614146 scopus 로고    scopus 로고
    • An extended anaphase signaling pathway for Mad2p includes microtubule organizing center proteins and multiple motor transitions
    • Mayer, C., Filopei, J., Batac, J., Alford, L. & Paluh, J. L. An extended anaphase signaling pathway for Mad2p includes microtubule organizing center proteins and multiple motor transitions. Cell Cycle 5, 1456-1463 (2006).
    • (2006) Cell Cycle , vol.5 , pp. 1456-1463
    • Mayer, C.1    Filopei, J.2    Batac, J.3    Alford, L.4    Paluh, J.L.5
  • 27
    • 0025107502 scopus 로고
    • Novel potential mitotic motor protein encoded by the fission yeast cut7 + gene
    • Hagan, I. & Yanagida, M. Novel potential mitotic motor protein encoded by the fission yeast cut7 + gene. Nature 347, 563-566 (1990).
    • (1990) Nature , vol.347 , pp. 563-566
    • Hagan, I.1    Yanagida, M.2
  • 28
    • 68349105806 scopus 로고    scopus 로고
    • Phosphoregulated interaction between Kinesin-6 Klp9 and microtubule bundler Ase1p promotes spindle elongation
    • Fu, C. et al. Phosphoregulated interaction between Kinesin-6 Klp9 and microtubule bundler Ase1p promotes spindle elongation. Dev. Cell 17, 257-267 (2009).
    • (2009) Dev. Cell , vol.17 , pp. 257-267
    • Fu, C.1
  • 29
    • 0031954955 scopus 로고    scopus 로고
    • Mutations in the bimC box of Cut7 indicate divergence of regulation within the bimC family of kinesin related proteins
    • Drummond, D. R. & Hagan, I. M. Mutations in the bimC box of Cut7 indicate divergence of regulation within the bimC family of kinesin related proteins. J. Cell Sci. 111, 853-865 (1998).
    • (1998) J. Cell Sci. , vol.111 , pp. 853-865
    • Drummond, D.R.1    Hagan, I.M.2
  • 30
    • 0027363577 scopus 로고
    • The Kinesin-like protein KLP61F is essential for mitosis in Drosophila
    • Heck, M. M. S. et al. The Kinesin-like protein KLP61F is essential for mitosis in Drosophila. J. Cell Biol. 123, 665-679 (1993).
    • (1993) J. Cell Biol. , vol.123 , pp. 665-679
    • Heck, M.M.S.1
  • 31
    • 4644349081 scopus 로고    scopus 로고
    • A standardized kinesin nomenclature
    • Lawrence, C. J. et al. A standardized kinesin nomenclature. J. Cell Biol. 167, 19-22 (2004).
    • (2004) J. Cell Biol. , vol.167 , pp. 19-22
    • Lawrence, C.J.1
  • 32
    • 0025326231 scopus 로고
    • Mutation of a gene that encodes a kinesin-like protein blocks nuclear division in A. Nidulans
    • Enos, A. P. & Morris, N. R. Mutation of a gene that encodes a kinesin-like protein blocks nuclear division in A. nidulans. Cell 60, 1019-1027 (1990).
    • (1990) Cell , vol.60 , pp. 1019-1027
    • Enos, A.P.1    Morris, N.R.2
  • 33
    • 84889596859 scopus 로고    scopus 로고
    • Antagonistic spindle motors and MAPs regulate metaphase spindle length and chromosome segregation
    • Syrovatkina, V., Fu, C. & Tran, P. T. Antagonistic spindle motors and MAPs regulate metaphase spindle length and chromosome segregation. Curr. Biol. 23, 2423-2429 (2013).
    • (2013) Curr. Biol. , vol.23 , pp. 2423-2429
    • Syrovatkina, V.1    Fu, C.2    Tran, P.T.3
  • 34
    • 0030982137 scopus 로고    scopus 로고
    • The Spg1p GTPase is an essential, dosage-dependent inducer of septum formation in Schizosaccharomyces pombe
    • Schmidt, S., Sohrmann, M., Hofmann, K., Woollard, A. & Simanis, V. The Spg1p GTPase is an essential, dosage-dependent inducer of septum formation in Schizosaccharomyces pombe. Genes Dev. 11, 1519-1534 (1997).
    • (1997) Genes Dev. , vol.11 , pp. 1519-1534
    • Schmidt, S.1    Sohrmann, M.2    Hofmann, K.3    Woollard, A.4    Simanis, V.5
  • 35
    • 2442462328 scopus 로고    scopus 로고
    • Recruitment of NIMA kinase shows that maturation of the S. Pombe spindle-pole body occurs over consecutive cell cycles and reveals a role for NIMA in modulating SIN activity
    • Grallert, A., Krapp, A., Bagley, S., Simanis, V. & Hagan, I. M. Recruitment of NIMA kinase shows that maturation of the S. pombe spindle-pole body occurs over consecutive cell cycles and reveals a role for NIMA in modulating SIN activity. Genes Dev. 18, 1007-1021 (2004).
    • (2004) Genes Dev. , vol.18 , pp. 1007-1021
    • Grallert, A.1    Krapp, A.2    Bagley, S.3    Simanis, V.4    Hagan, I.M.5
  • 36
    • 44949179893 scopus 로고    scopus 로고
    • Sister kinetochore recapture in fission yeast occurs by two distinct mechanisms, both requiring Dam1 and Klp2
    • Gachet, Y. et al. Sister kinetochore recapture in fission yeast occurs by two distinct mechanisms, both requiring Dam1 and Klp2. MBoC 19, 1646-1662 (2008).
    • (2008) MBoC , vol.19 , pp. 1646-1662
    • Gachet, Y.1
  • 37
    • 0026577748 scopus 로고
    • Kinesin-related cut7 protein associates with mitotic and meiotic spindles in fission yeast
    • Hagan, I. & Yanagida, M. Kinesin-related cut7 protein associates with mitotic and meiotic spindles in fission yeast. Nature 356, 74-76 (1992).
    • (1992) Nature , vol.356 , pp. 74-76
    • Hagan, I.1    Yanagida, M.2
  • 38
    • 78649957196 scopus 로고    scopus 로고
    • Mechanisms of centrosome separation and bipolar spindle assembly
    • Tanenbaum, M. E. & Medema, R. H. Mechanisms of centrosome separation and bipolar spindle assembly. Dev. Cell 19, 797-806 (2010).
    • (2010) Dev. Cell , vol.19 , pp. 797-806
    • Tanenbaum, M.E.1    Medema, R.H.2
  • 39
    • 69949118412 scopus 로고    scopus 로고
    • Polo kinase and separase regulate the mitotic licensing of centriole duplication in human cells
    • Tsou, M-F. B. et al. Polo kinase and separase regulate the mitotic licensing of centriole duplication in human cells. Dev. Cell 17, 344-354 (2009).
    • (2009) Dev. Cell , vol.17 , pp. 344-354
    • Tsou, M.-F.B.1
  • 40
    • 0029898255 scopus 로고    scopus 로고
    • Analysis of Tub4p, a yeast γ-tubulin-like protein: Implications for microtubule-organizing center function
    • Marschall, L. G., Jeng, R. L., Mulholland, J. & Stearns, T. Analysis of Tub4p, a yeast γ-tubulin-like protein: implications for microtubule-organizing center function. J. Cell Biol. 134, 443-454 (1996).
    • (1996) J. Cell Biol. , vol.134 , pp. 443-454
    • Marschall, L.G.1    Jeng, R.L.2    Mulholland, J.3    Stearns, T.4
  • 41
    • 79958250238 scopus 로고    scopus 로고
    • Centriolar kinesin Kif24 interacts with CP110 to remodel microtubules and regulate ciliogenesis
    • Kobayashi, T., Tsang, W. Y., Li, J., Lane, W. & Dynlacht, B. D. Centriolar kinesin Kif24 interacts with CP110 to remodel microtubules and regulate ciliogenesis. Cell 145, 914-925 (2011).
    • (2011) Cell , vol.145 , pp. 914-925
    • Kobayashi, T.1    Tsang, W.Y.2    Li, J.3    Lane, W.4    Dynlacht, B.D.5
  • 42
    • 49649109248 scopus 로고    scopus 로고
    • Regulation of mitotic spindle asymmetry by SUMO and the spindle-assembly checkpoint in yeast
    • Leisner, C. et al. Regulation of mitotic spindle asymmetry by SUMO and the spindle-assembly checkpoint in yeast. Curr. Biol. 18, 1249-1255 (2008).
    • (2008) Curr. Biol. , vol.18 , pp. 1249-1255
    • Leisner, C.1
  • 43
    • 38749152406 scopus 로고    scopus 로고
    • Asymmetric centrosome behavior and the mechanisms of stem cell division
    • Yamashita, Y. M. & Fuller, M. T. Asymmetric centrosome behavior and the mechanisms of stem cell division. J. Cell Biol. 180, 261-266 (2008).
    • (2008) J. Cell Biol. , vol.180 , pp. 261-266
    • Yamashita, Y.M.1    Fuller, M.T.2
  • 44
    • 65949118255 scopus 로고    scopus 로고
    • A cell cycle timer for asymmetric spindle positioning
    • Campbell, E. K. M., Werts, A. D. & Goldstein, B. A cell cycle timer for asymmetric spindle positioning. PLoS Biol. 7, e1000088 (2009).
    • (2009) PLoS Biol. , vol.7 , pp. e1000088
    • Campbell, E.K.M.1    Werts, A.D.2    Goldstein, B.3
  • 45
    • 78649945231 scopus 로고    scopus 로고
    • Monitoring spindle orientation: Spindle position checkpoint in charge
    • Caydasi, A. K., Ibrahim, B. & Pereira, G. Monitoring spindle orientation: spindle position checkpoint in charge. Cell Div. 5, 1-15 (2010).
    • (2010) Cell Div. , vol.5 , pp. 1-15
    • Caydasi, A.K.1    Ibrahim, B.2    Pereira, G.3
  • 46
    • 84865340670 scopus 로고    scopus 로고
    • The MEN mediates the effects of the spindle assembly checkpoint on Kar9-dependent spindle pole body inheritance in budding yeast
    • Hotz, M., Lengefeld, J. & Barral, Y. The MEN mediates the effects of the spindle assembly checkpoint on Kar9-dependent spindle pole body inheritance in budding yeast. Cell Cycle 11, 3109-3116 (2012).
    • (2012) Cell Cycle , vol.11 , pp. 3109-3116
    • Hotz, M.1    Lengefeld, J.2    Barral, Y.3
  • 47
    • 84867998377 scopus 로고    scopus 로고
    • Polar opposites: Fine-tuning cytokinesis through SIN asymmetry
    • Johnson, A. E., McCollum, D. & Gould, K. L. Polar opposites: fine-tuning cytokinesis through SIN asymmetry. Cytoskeleton 69, 686-699 (2012).
    • (2012) Cytoskeleton , vol.69 , pp. 686-699
    • Johnson, A.E.1    McCollum, D.2    Gould, K.L.3
  • 48
    • 61349122738 scopus 로고    scopus 로고
    • Diffusion and directed movement: In vitro motile properties of fission yeast kinesin-14 Pkl1
    • Furuta, K., Edamatsu, M., Maeda, T. & Toyoshima, Y. Y. Diffusion and directed movement: in vitro motile properties of fission yeast kinesin-14 Pkl1. J. Biol. Chem. 283, 36465-36473 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 36465-36473
    • Furuta, K.1    Edamatsu, M.2    Maeda, T.3    Toyoshima, Y.Y.4
  • 50
    • 0033615357 scopus 로고    scopus 로고
    • Small molecule inhibitor of mitotic spindle bipolarity identified in a phenotype-based screen
    • Mayer, T. U. et al. Small molecule inhibitor of mitotic spindle bipolarity identified in a phenotype-based screen. Science 286, 971-974 (1999).
    • (1999) Science , vol.286 , pp. 971-974
    • Mayer, T.U.1
  • 51
    • 84870527677 scopus 로고    scopus 로고
    • Mitosis-targeted anti-cancer therapies: Where they stand
    • Chan, K.-S. et al. Mitosis-targeted anti-cancer therapies: where they stand. Cell Death Dis. 3, e411 (2012).
    • (2012) Cell Death Dis. , vol.3 , pp. e411
    • Chan, K.-S.1
  • 52
    • 33746294151 scopus 로고    scopus 로고
    • Altered cellular distribution and subcellular sorting of γ-tubulin in diffuse astrocytic gliomas and human glioblastoma cell lines
    • Katsetos, C. D. et al. Altered cellular distribution and subcellular sorting of γ-tubulin in diffuse astrocytic gliomas and human glioblastoma cell lines. J. Neuropathol. Exp. Neurol. 65, 465-477 (2006).
    • (2006) J. Neuropathol. Exp. Neurol. , vol.65 , pp. 465-477
    • Katsetos, C.D.1
  • 53
    • 34250856286 scopus 로고    scopus 로고
    • Class III β-tubulin and γ-tubulin are co-expressed and form complexes in human glioblastoma cells
    • Katsetos, C. D. et al. Class III β-tubulin and γ-tubulin are co-expressed and form complexes in human glioblastoma cells. Neurochem. Res. 32, 1387-1398 (2007).
    • (2007) Neurochem. Res. , vol.32 , pp. 1387-1398
    • Katsetos, C.D.1
  • 54
    • 61649106531 scopus 로고    scopus 로고
    • INK4A promoter methylation occur together in preinvasive lesions and carcinomas of the breast
    • INK4A promoter methylation occur together in preinvasive lesions and carcinomas of the breast. Ann. Oncol. 20, 441-448 (2009).
    • (2009) Ann. Oncol. , vol.20 , pp. 441-448
    • Liu, T.1    Niu, Y.2    Yu, Y.3    Liu, Y.4    Zhang, F.5
  • 55
    • 67449089091 scopus 로고    scopus 로고
    • Increased expression of centrosomal α, γ-tubulin in atypical ductal hyperplasia and carcinoma of the breast
    • Niu, Y. et al. Increased expression of centrosomal α, γ-tubulin in atypical ductal hyperplasia and carcinoma of the breast. Cancer Sci. 100, 580-587 (2009).
    • (2009) Cancer Sci. , vol.100 , pp. 580-587
    • Niu, Y.1
  • 56
    • 62849105653 scopus 로고    scopus 로고
    • Gamma tubulin: A promising indicator of recurrence in squamous cell carcinoma of the larynx
    • Syed, M. I. et al. Gamma tubulin: A promising indicator of recurrence in squamous cell carcinoma of the larynx. Otolaryngol. Head Neck Surg. 140, 498-504 (2009).
    • (2009) Otolaryngol. Head Neck Surg. , vol.140 , pp. 498-504
    • Syed, M.I.1
  • 57
    • 77950842886 scopus 로고    scopus 로고
    • Differential expression and cellular distribution of γ-tubulin and βIII-tubulin in medulloblastomas and human medulloblastoma cell lines
    • Caracciolo, V. et al. Differential expression and cellular distribution of γ-tubulin and βIII-tubulin in medulloblastomas and human medulloblastoma cell lines. J. Cell Physiol. 223, 519-529 (2010).
    • (2010) J. Cell Physiol. , vol.223 , pp. 519-529
    • Caracciolo, V.1
  • 58
    • 85046915393 scopus 로고    scopus 로고
    • Delocalization of γ-tubulin due to increased solubility in human breast cancer cell lines
    • Cho, E. H., Whipple, R. A., Matrone, M. A., Balzer, E. M. & Martin, S. S. Delocalization of γ-tubulin due to increased solubility in human breast cancer cell lines. Cancer Biol. Ther. 9, 66-76 (2010).
    • (2010) Cancer Biol. Ther. , vol.9 , pp. 66-76
    • Cho, E.H.1    Whipple, R.A.2    Matrone, M.A.3    Balzer, E.M.4    Martin, S.S.5
  • 59
    • 77953200264 scopus 로고    scopus 로고
    • Differential expression of centrosomal proteins at different stages of human glioma
    • Loh, J.-K. et al. Differential expression of centrosomal proteins at different stages of human glioma. BMC Cancer 10, 268 (2010).
    • (2010) BMC Cancer , vol.10 , pp. 268
    • Loh, J.-K.1
  • 60
    • 84866102332 scopus 로고    scopus 로고
    • Overexpression of γ-tubulin in non-small cell lung cancer
    • Maounis, N. F. et al. Overexpression of γ-tubulin in non-small cell lung cancer. Histol. Histopathol. 27, 1183-1194 (2012).
    • (2012) Histol. Histopathol. , vol.27 , pp. 1183-1194
    • Maounis, N.F.1
  • 62
    • 0026025891 scopus 로고
    • Molecular genetic analysis of fission yeast Schizosaccharomyces pombe
    • Moreno, S., Klar, A. & Nurse, P. Molecular genetic analysis of fission yeast Schizosaccharomyces pombe. Methods Enzymol. 194, 795-823 (1991).
    • (1991) Methods Enzymol. , vol.194 , pp. 795-823
    • Moreno, S.1    Klar, A.2    Nurse, P.3
  • 63
    • 0027390036 scopus 로고
    • Thiamine-repressible expression vectors pRep and pRIP for fission yeast
    • Maundrell, K. Thiamine-repressible expression vectors pRep and pRIP for fission yeast. Gene 123, 127-130 (1993).
    • (1993) Gene , vol.123 , pp. 127-130
    • Maundrell, K.1
  • 64
    • 0035970586 scopus 로고    scopus 로고
    • Construction of FLAG and histidine tagging vectors for Schizosaccharomyces pombe
    • Huang, Y., Hamada, M., Patel, J. & Maraia, R. J. Construction of FLAG and histidine tagging vectors for Schizosaccharomyces pombe. Yeast 18, 463-468 (2001).
    • (2001) Yeast , vol.18 , pp. 463-468
    • Huang, Y.1    Hamada, M.2    Patel, J.3    Maraia, R.J.4
  • 65
    • 84872002194 scopus 로고    scopus 로고
    • Csi1 links centromeres to the nuclear envelope for centromere clustering
    • Hou, H. et al. Csi1 links centromeres to the nuclear envelope for centromere clustering. J. Cell Biol. 199, 735-744 (2012).
    • (2012) J. Cell Biol. , vol.199 , pp. 735-744
    • Hou, H.1
  • 66
    • 0033619113 scopus 로고    scopus 로고
    • High-efficiency gene targeting in Schizosaccharomyces pombe using a modular, PCR-based approach with long tracts of flanking homology
    • Krawchuk, M. D. & Wahls, W. P. High-efficiency gene targeting in Schizosaccharomyces pombe using a modular, PCR-based approach with long tracts of flanking homology. Yeast 15, 1419-1427 (1999).
    • (1999) Yeast , vol.15 , pp. 1419-1427
    • Krawchuk, M.D.1    Wahls, W.P.2
  • 67
    • 0024369960 scopus 로고
    • Definition of individual components within the cytoskeleton of Trypanosoma brucei by a library of monoclonal antibodies
    • Woods, A. et al. Definition of individual components within the cytoskeleton of Trypanosoma brucei by a library of monoclonal antibodies. J. Cell Sci. 93, 491-500 (1989).
    • (1989) J. Cell Sci. , vol.93 , pp. 491-500
    • Woods, A.1
  • 68
    • 18544371166 scopus 로고    scopus 로고
    • Fission yeast mto2p regulates microtubule nucleation by the centrosomin-related protein mto1p
    • Samejima, I., Lourenco, P. C. C., Snaith, H. A. & Sawin, K. E. Fission yeast mto2p regulates microtubule nucleation by the centrosomin-related protein mto1p. MBoC 16, 3040-3051 (2005).
    • (2005) MBoC , vol.16 , pp. 3040-3051
    • Samejima, I.1    Lourenco, P.C.C.2    Snaith, H.A.3    Sawin, K.E.4
  • 69
    • 0028978166 scopus 로고
    • Analysis of the γ-tubulin sequences: Implications for the functional properties of γ-tubulin
    • Burns, R. G. Analysis of the γ-tubulin sequences: implications for the functional properties of γ-tubulin. J Cell Sci. 108, 2123-2130 (1995).
    • (1995) J Cell Sci. , vol.108 , pp. 2123-2130
    • Burns, R.G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.