메뉴 건너뛰기




Volumn 14, Issue 11, 2012, Pages 1159-1168

Subdiffraction-resolution fluorescence microscopy reveals a domain of the centrosome critical for pericentriolar material organization

Author keywords

[No Author keywords available]

Indexed keywords

PERICENTRIN; PERICENTRIN LIKE PROTEIN; UNCLASSIFIED DRUG;

EID: 84869001801     PISSN: 14657392     EISSN: 14764679     Source Type: Journal    
DOI: 10.1038/ncb2597     Document Type: Article
Times cited : (299)

References (72)
  • 1
    • 34249336078 scopus 로고    scopus 로고
    • Centrosome biogenesis and function: Centrosomics brings new understanding
    • DOI 10.1038/nrm2180, PII NRM2180
    • Bettencourt-Dias, M. & Glover, D.M. Centrosome biogenesis and function: centro- somics brings new understanding. Nat. Rev. Mol. Cell Biol. 8, 451-463 (2007 (Pubitemid 46809152)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.6 , pp. 451-463
    • Bettencourt-Dias, M.1    Glover, D.M.2
  • 2
    • 80053553994 scopus 로고    scopus 로고
    • The centrosome cycle: Centriole biogenesis, duplication and inherent asymmetries
    • Nigg, E.A. & Stearns, T. The centrosome cycle: centriole biogenesis, duplication and inherent asymmetries. Nat. Cell Biol. 13, 1154-1160 (2011
    • (2011) Nat. Cell Biol , vol.13 , pp. 1154-1160
    • Nigg, E.A.1    Stearns, T.2
  • 4
    • 79960629889 scopus 로고    scopus 로고
    • Centrosomes and cilia in human disease
    • Bettencourt-Dias, M. et al. Centrosomes and cilia in human disease. Trends Genet. 27, 307-315 (2011
    • (2011) Trends Genet , vol.27 , pp. 307-315
    • Bettencourt-Dias M1
  • 6
    • 0020468680 scopus 로고
    • 2 cells: Asymmetric distribution and structural changes in the pericentriolar material
    • Rieder, C.L. The centrosome cycle in PtK2 cells: Asymmetric distribution and structural changes in the pericentriolar material. Biol. Cell. 44, 117-132 (1982 (Pubitemid 13238313)
    • (1982) Biology of the Cell , vol.44 , Issue.2 , pp. 117-132
    • Rieder, C.L.1    Borisy, G.G.2
  • 7
    • 0023461179 scopus 로고
    • Structural and chemical characterization of isolated centrosomes
    • Bornens, M. et al. Structural and chemical characterization of isolated centrosomes. Cell Motil. Cytoskeleton. 8, 238-249 (1987
    • (1987) Cell Motil. Cytoskeleton , vol.8 , pp. 238-249
    • Bornens, M.1
  • 8
    • 0033825277 scopus 로고    scopus 로고
    • Microtubule minus-end anchorage at centrosomal and non-centrosomal sites: The role of ninein
    • Mogensen, M.M. et al. Microtubule minus-end anchorage at centrosomal and non-centrosomal sites: The role of ninein. J. Cell Sci. 113, 3013-3023 (2000
    • (2000) J. Cell Sci , vol.113 , pp. 3013-3023
    • Mogensen, M.M.1
  • 9
    • 0036468420 scopus 로고    scopus 로고
    • Centrosome composition and microtubule anchoring mechanisms
    • DOI 10.1016/S0955-0674(01)00290-3
    • Bornens, M. Centrosome composition and microtubule anchoring mechanisms. Curr. Opin. Cell Biol. 14, 25-34 (2002 (Pubitemid 34131653)
    • (2002) Current Opinion in Cell Biology , vol.14 , Issue.1 , pp. 25-34
    • Bornens, M.1
  • 10
    • 0028973450 scopus 로고
    • Microtubule nucleation by gamma-tubulin-containing rings by the centrosome
    • DOI 10.1038/378638a0
    • Moritz, M. et al. Microtubule nucleation by -tubulin-containing rings in the centrosome. Nature 378, 638-640 (1995 (Pubitemid 3005786)
    • (1995) Nature , vol.378 , Issue.6557 , pp. 638-640
    • Moritz, M.1    Braunfeld, M.B.2    Sedat, J.W.3    Alberts, B.4    Agard, D.A.5
  • 11
    • 80054901400 scopus 로고    scopus 로고
    • Microtubule nucleation by -tubulin complexes
    • Kollman, J.M. et al. Microtubule nucleation by -tubulin complexes. Nat. Rev. Mol. Cell Biol. 12, 709-721 (2011
    • (2011) Nat. Rev. Mol. Cell Biol , vol.12 , pp. 709-721
    • Kollman, J.M.1
  • 12
    • 0034565442 scopus 로고    scopus 로고
    • Centrosome maturation
    • Palazzo, R.E. et al. Centrosome maturation. Curr. Top Dev. Biol. 49, 449-470 (2000
    • (2000) Curr. Top Dev. Biol , vol.49 , pp. 449-470
    • Palazzo, R.E.1
  • 13
    • 79961243037 scopus 로고    scopus 로고
    • Limiting amounts of centrosome material set centrosome size in C
    • Decker, M. et al. Limiting amounts of centrosome material set centrosome size in C. elegans embryos. Curr. Biol. 21, 1259-1267 (2011
    • (2011) Elegans embryos. Curr. Biol , vol.21 , pp. 1259-1267
    • Decker, M.1
  • 14
    • 0346874342 scopus 로고    scopus 로고
    • Proteomic characterization of the human centrosome by protein correlation profiling
    • DOI 10.1038/nature02166
    • Andersen, J.S. et al. Proteomic characterization of the human centrosome by protein correlation pro-ling. Nature 426, 570-574 (2003 (Pubitemid 37522644)
    • (2003) Nature , vol.426 , Issue.6966 , pp. 570-574
    • Andersen, J.S.1    Wilkinson, C.J.2    Mayor, T.3    Mortensen, P.4    Nigg, E.A.5    Mann, M.6
  • 15
    • 77957810181 scopus 로고    scopus 로고
    • Proteomic and functional analysis of the mitotic Drosophila centrosome
    • Muller, H. et al. Proteomic and functional analysis of the mitotic Drosophila centrosome. EMBO J. 29, 3344-3357 (2010
    • (2010) EMBO J. , vol.29 , pp. 3344-3357
    • Muller, H.1
  • 16
    • 2342501364 scopus 로고    scopus 로고
    • Comparative genomics identi-es a -agellar and basal body proteome that includes the BBS5 human disease gene
    • Li, J.B. et al. Comparative genomics identi-es a -agellar and basal body proteome that includes the BBS5 human disease gene. Cell 117, 541-552 (2004
    • (2004) Cell , vol.117 , pp. 541-552
    • Li, J.B.1
  • 18
    • 20544436245 scopus 로고    scopus 로고
    • Proteomic analysis of isolated Chlamydomonas centrioles reveals orthologs of ciliary-disease genes
    • DOI 10.1016/j.cub.2005.05.024, PII S0960982205005130
    • Keller, L.C. et al. Proteomic analysis of isolated Chlamydomonas centrioles reveals orthologs of ciliary-disease genes. Curr. Biol. 15, 1090-1098 (2005 (Pubitemid 40841351)
    • (2005) Current Biology , vol.15 , Issue.12 , pp. 1090-1098
    • Keller, L.C.1    Romijn, E.P.2    Zamora, I.3    Yates III, J.R.4    Marshall, W.F.5
  • 20
    • 77951979181 scopus 로고    scopus 로고
    • Procentriole assembly revealed by cryo-electron tomography
    • Guichard, P. et al. Procentriole assembly revealed by cryo-electron tomography. EMBO J. 29, 1565-1572 (2010
    • (2010) EMBO J. , vol.29 , pp. 1565-1572
    • Guichard, P.1
  • 21
    • 0026606831 scopus 로고
    • Centrosome organization and centriole architecture: Their sensitivity to divalent cations
    • Paintrand, M. et al. Centrosome organization and centriole architecture: Their sensitivity to divalent cations. J. Struct. Biol. 108, 107-128 (1992
    • (1992) J. Struct. Biol , vol.108 , pp. 107-128
    • Paintrand, M.1
  • 22
    • 84856411124 scopus 로고    scopus 로고
    • Three-dimensional structure of basal body triplet revealed by electron cryo-tomography
    • Li, S. et al. Three-dimensional structure of basal body triplet revealed by electron cryo-tomography. EMBO J. 31, 552-562 (2012
    • (2012) EMBO J. , vol.31 , pp. 552-562
    • Li, S.1
  • 23
    • 0015385636 scopus 로고
    • The three-dimensional structure of the basal body from the rhesus monkey oviduct
    • Anderson, R.G. The three-dimensional structure of the basal body from the rhesus monkey oviduct. J. Cell. Biol. 54, 246-265 (1972
    • (1972) J. Cell. Biol , vol.54 , pp. 246-265
    • Anderson, R.G.1
  • 24
    • 0038159661 scopus 로고    scopus 로고
    • Three-dimensional organization of basal bodies from wild-type and δ-tubulin deletion strains of Chlamydomonas reinhardtii
    • DOI 10.1091/mbc.E02-11-0755
    • O'Toole, E.T. et al. Three-dimensional organization of basal bodies from wild-type and delta-tubulin deletion strains of Chlamydomonas reinhardtii. Mol. Biol. Cell 14, 2999-3012 (2003 (Pubitemid 36871537)
    • (2003) Molecular Biology of the Cell , vol.14 , Issue.7 , pp. 2999-3012
    • O'Toole, E.T.1    Giddings, T.H.2    McIntosh, J.R.3    Dutcher, S.K.4
  • 25
    • 0033771941 scopus 로고    scopus 로고
    • A new function for the -tubulin ring complex as a microtubule minus-end cap
    • Wiese, C. & Zheng, Y. A new function for the -tubulin ring complex as a microtubule minus-end cap. Nat. Cell Biol. 2, 358-364 (2000
    • (2000) Nat. Cell Biol , vol.2 , pp. 358-364
    • Wiese, C.1    Zheng, Y.2
  • 26
    • 0033771535 scopus 로고    scopus 로고
    • Immunostructural evidence for the template mechanism of microtubule nucleation
    • Keating, T.J. & Borisy, G.G. Immunostructural evidence for the template mechanism of microtubule nucleation. Nat. Cell Biol. 2, 352-357 (2000
    • (2000) Nat. Cell Biol , vol.2 , pp. 352-357
    • Keating, T.J.1    Borisy, G.G.2
  • 27
    • 0029124180 scopus 로고
    • Three-dimensional structural characterization of centrosomes from early Drosophila embryos
    • Moritz, M. et al. Three-dimensional structural characterization of centrosomes from early Drosophila embryos. J. Cell. Biol. 130, 1149-1159 (1995
    • (1995) J. Cell. Biol , vol.130 , pp. 1149-1159
    • Moritz M1
  • 28
    • 58149522518 scopus 로고    scopus 로고
    • Electron tomography study of isolated human centrioles
    • Ibrahim, R. et al. Electron tomography study of isolated human centrioles. Microsc. Res. Tech. 72, 42-48 (2009
    • (2009) Microsc. Res. Tech , vol.72 , pp. 42-48
    • Ibrahim, R.1
  • 29
    • 0031854868 scopus 로고    scopus 로고
    • Recruitment of the γ-tubulin ring complex to Drosophila salt-stripped centrosome scaffolds
    • DOI 10.1083/jcb.142.3.775
    • Moritz, M. et al. Recruitment of the -tubulin ring complex to Drosophila salt- stripped centrosome scaffolds. J. Cell. Biol. 142, 775-786 (1998 (Pubitemid 28381494)
    • (1998) Journal of Cell Biology , vol.142 , Issue.3 , pp. 775-786
    • Moritz, M.1    Zheng, Y.2    Alberts, B.M.3    Oegema, K.4
  • 30
    • 0034126839 scopus 로고    scopus 로고
    • Reconstitution of microtubule nucleation potential in centrosomes isolated from Spisula solidissima oocytes
    • Schnackenberg, B.J. et al. Reconstitution of microtubule nucleation potential in centrosomes isolated from Spisula solidissima oocytes. J. Cell Sci. 113, 943-953 (2000 (Pubitemid 30179474)
    • (2000) Journal of Cell Science , vol.113 , Issue.6 , pp. 943-953
    • Schnackenberg, B.J.1    Hull, D.R.2    Balczon, R.D.3    Palazzo, R.E.4
  • 32
    • 0033799252 scopus 로고    scopus 로고
    • A subset of centrosomal proteins are arranged in a tubular conformation that is reproduced during centrosome duplication
    • Ou, Y. & Rattner, J.B. A subset of centrosomal proteins are arranged in a tubular conformation that is reproduced during centrosome duplication. Cell Motil. Cytoskeleton. 47, 13-24 (2000
    • (2000) Cell Motil. Cytoskeleton , vol.47 , pp. 13-24
    • Ou, Y.1    Rattner, J.B.2
  • 33
    • 42149143016 scopus 로고    scopus 로고
    • Three-dimensional resolution doubling in wide-eld -uorescence microscopy by structured illumination
    • Gustafsson, M.G. et al. Three-dimensional resolution doubling in wide-eld -uorescence microscopy by structured illumination. Biophys. J. 94, 4957-4970 (2008
    • (2008) Biophys. J. , vol.94 , pp. 4957-4970
    • Gustafsson, M.G.1
  • 34
    • 38949216802 scopus 로고    scopus 로고
    • Three-dimensional super-resolution imaging by stochastic optical reconstruction microscopy
    • DOI 10.1126/science.1153529
    • Huang, B. et al. Three-dimensional super-resolution imaging by stochastic optical reconstruction microscopy. Science 319, 810-813 (2008 (Pubitemid 351225870)
    • (2008) Science , vol.319 , Issue.5864 , pp. 810-813
    • Huang, B.1    Wang, W.2    Bates, M.3    Zhuang, X.4
  • 35
    • 67650762824 scopus 로고    scopus 로고
    • Super-resolution -uorescence microscopy
    • Huang, B., Bates, M. & Zhuang, X. Super-resolution -uorescence microscopy. Annu. Rev. Biochem. 78, 993-1016 (2009
    • (2009) Annu. Rev. Biochem , vol.78 , pp. 993-1016
    • Huang, B.1    Bates, M.2    Zhuang, X.3
  • 36
    • 77049098517 scopus 로고    scopus 로고
    • Centrioles in -ies: The exception to the rule? Semin
    • Gogendeau, D. & Basto, R. Centrioles in -ies: The exception to the rule? Semin. Cell Dev. Biol. 21, 163-173 (2010
    • (2010) Cell Dev. Biol , vol.21 , pp. 163-173
    • Gogendeau, D.1    Basto, R.2
  • 38
    • 48449085139 scopus 로고    scopus 로고
    • SAS-6 is a Cartwheel Protein that Establishes the 9-Fold Symmetry of the Centriole
    • DOI 10.1016/j.cub.2007.11.046, PII S0960982207022853
    • Nakazawa, Y. et al. SAS-6 is a cartwheel protein that establishes the 9-fold symmetry of the centriole. Curr. Biol. 17, 2169-2174 (2007 (Pubitemid 50014863)
    • (2007) Current Biology , vol.17 , Issue.24 , pp. 2169-2174
    • Nakazawa, Y.1    Hiraki, M.2    Kamiya, R.3    Hirono, M.4
  • 40
    • 79959547445 scopus 로고    scopus 로고
    • SAS-4 provides a scaffold for cytoplasmic complexes and tethers them in a centrosome
    • Gopalakrishnan, J. et al. SAS-4 provides a scaffold for cytoplasmic complexes and tethers them in a centrosome. Nat. Commun. 2, 359 (2011
    • (2011) Nat. Commun , vol.2 , Issue.359
    • Gopalakrishnan, J.1
  • 41
    • 0037459108 scopus 로고    scopus 로고
    • SAS-4 is a C. elegans centriolar protein that controls centrosome size
    • DOI 10.1016/S0092-8674(03)00117-X
    • Kirkham, M. et al. SAS-4 is a C. elegans centriolar protein that controls centrosome size. Cell 112, 575-587 (2003 (Pubitemid 36263088)
    • (2003) Cell , vol.112 , Issue.4 , pp. 575-587
    • Kirkham, M.1    Muller-Reichert, T.2    Oegema, K.3    Grill, S.4    Hyman, A.A.5
  • 42
    • 79952280152 scopus 로고    scopus 로고
    • Structures of SAS-6 suggest its organization in centrioles
    • Van Breugel, M. et al. Structures of SAS-6 suggest its organization in centrioles. Science 331, 1196-1199 (2011
    • (2011) Science , vol.331 , pp. 1196-1199
    • Van Breugel, M.1
  • 43
    • 79651473154 scopus 로고    scopus 로고
    • Structural basis of the 9-fold symmetry of centrioles
    • Kitagawa, D. et al. Structural basis of the 9-fold symmetry of centrioles. Cell 144, 364-375 (2011
    • (2011) Cell , vol.144 , pp. 364-375
    • Kitagawa, D.1
  • 44
    • 0034574615 scopus 로고    scopus 로고
    • The PACT domain, a conserved centrosomal targeting motif in the coiled-coil proteins AKAP450 and pericentrin
    • Gillingham, A.K. & Munro, S. The PACT domain, a conserved centrosomal targeting motif in the coiled-coil proteins AKAP450 and pericentrin. EMBO Rep. 1, 524-529 (2000
    • (2000) EMBO Rep , vol.1 , pp. 524-529
    • Gillingham, A.K.1    Munro, S.2
  • 45
    • 0347360338 scopus 로고    scopus 로고
    • Characterization of a Drosophila Centrosome Protein CP309 That Shares Homology with Kendrin and CG-NAP
    • DOI 10.1091/mbc.E03-03-0191
    • Kawaguchi, S. & Zheng, Y. Characterization of a Drosophila centrosome protein CP309 that shares homology with Kendrin and CG-NAP. Mol. Biol. Cell 15, 37-45 (2004 (Pubitemid 38044941)
    • (2004) Molecular Biology of the Cell , vol.15 , Issue.1 , pp. 37-45
    • Kawaguchi, S.-I.1    Zheng, Y.2
  • 46
    • 2942692444 scopus 로고    scopus 로고
    • The Drosophila pericentrin-like protein is essential for cilia/-agella function, but appears to be dispensable for mitosis
    • Martinez-Campos, M. et al. The Drosophila pericentrin-like protein is essential for cilia/-agella function, but appears to be dispensable for mitosis. J. Cell. Biol. 165, 673-683 (2004
    • (2004) J. Cell. Biol , vol.165 , pp. 673-683
    • Martinez-Campos, M.1
  • 47
    • 78650437294 scopus 로고    scopus 로고
    • Centrioles regulate centrosome size by controlling the rate of CNN incorporation into the PCM
    • Conduit, P.T. et al. Centrioles regulate centrosome size by controlling the rate of CNN incorporation into the PCM. Curr. Biol. 20, 2178-2186 (2010
    • (2010) Curr. Biol , vol.20 , pp. 2178-2186
    • Conduit, P.T.1
  • 48
    • 77649270954 scopus 로고    scopus 로고
    • Size and shape of protein molecules at the nanometer level determined by sedimentation gel -ltration and electron microscopy
    • Erickson, H.P. Size and shape of protein molecules at the nanometer level determined by sedimentation, gel -ltration, and electron microscopy. Biol. Proced. Online 11, 32-51 (2009
    • (2009) Biol. Proced. Online 11 32-51
    • Erickson, H.P.1
  • 49
    • 84856479181 scopus 로고    scopus 로고
    • Dual-objective STORM reveals three- dimensional -lament organization in the actin cytoskeleton
    • Xu, K., Babcock, H.P. & Zhuang, X. Dual-objective STORM reveals three- dimensional -lament organization in the actin cytoskeleton. Nat. Methods 9, 185-188 (2012
    • (2012) Nat. Methods , vol.9 , pp. 185-188
    • Xu, K.1    Babcock, H.P.2    Zhuang, X.3
  • 50
    • 84862665108 scopus 로고    scopus 로고
    • STED microscopy with optimized labeling density reveals 9-fold arrangement of a centriole protein
    • Lau, L. et al. STED microscopy with optimized labeling density reveals 9-fold arrangement of a centriole protein. Biophys. J. 102, 2926-2935 (2012
    • (2012) Biophys. J. , vol.102 , pp. 2926-2935
    • Lau, L.1
  • 51
    • 77957982182 scopus 로고    scopus 로고
    • Asterless is a scaffold for the onset of centriole assembly
    • Dzhindzhev, N.S. et al. Asterless is a scaffold for the onset of centriole assembly. Nature 467, 714-718 (2010
    • (2010) Nature , vol.467 , pp. 714-718
    • Dzhindzhev, N.S.1
  • 52
    • 60849113138 scopus 로고    scopus 로고
    • The SCF Slimb ubiquitin ligase regulates Plk4/Sak levels to block centriole reduplication
    • Rogers, G.C. et al. The SCF Slimb ubiquitin ligase regulates Plk4/Sak levels to block centriole reduplication. J. Cell. Biol. 184, 225-239 (2009
    • (2009) J. Cell. Biol , vol.184 , pp. 225-239
    • Rogers, G.C.1
  • 53
    • 40249107653 scopus 로고    scopus 로고
    • Control of daughter centriole formation by the pericentriolar material
    • DOI 10.1038/ncb1694, PII NCB1694
    • Loncarek, J. et al. Control of daughter centriole formation by the pericentriolar material. Nat. Cell Biol. 10, 322-328 (2008 (Pubitemid 351331019)
    • (2008) Nature Cell Biology , vol.10 , Issue.3 , pp. 322-328
    • Loncarek, J.1    Hergert, P.2    Magidson, V.3    Khodjakov, A.4
  • 54
    • 79958218993 scopus 로고    scopus 로고
    • The conversion of centrioles to centrosomes: Essential coupling of duplication with segregation
    • Wang, W.J. et al. The conversion of centrioles to centrosomes: Essential coupling of duplication with segregation. J. Cell. Biol. 193, 727-739 (2011
    • (2011) J. Cell. Biol , vol.193 , pp. 727-739
    • Wang, W.J.1
  • 55
    • 54749133489 scopus 로고    scopus 로고
    • A genome-wide RNAi screen to dissect centriole duplication and centrosome maturation in Drosophila
    • Dobbelaere, J. et al. A genome-wide RNAi screen to dissect centriole duplication and centrosome maturation in Drosophila. PLoS Biol. 16, e224 (2008
    • (2008) PLoS Biol , vol.16
    • Dobbelaere, J.1
  • 56
    • 51349104215 scopus 로고    scopus 로고
    • A multicomponent assembly pathway contributes to the formation of acentrosomal microtubule arrays in interphase Drosophila cells
    • Rogers, G.C. et al. A multicomponent assembly pathway contributes to the formation of acentrosomal microtubule arrays in interphase Drosophila cells. Mol. Biol. Cell 19, 3163-3178 (2008
    • (2008) Mol. Biol. Cell , vol.19 , pp. 3163-3178
    • Rogers, G.C.1
  • 57
    • 78650115459 scopus 로고    scopus 로고
    • CDK5RAP2 stimulates microtubule nucleation by the -tubulin ring complex
    • Choi, Y.K. et al. CDK5RAP2 stimulates microtubule nucleation by the -tubulin ring complex. J. Cell. Biol. 191, 1089-1095 (2010
    • (2010) J. Cell. Biol , vol.191 , pp. 1089-1095
    • Choi, Y.K.1
  • 58
    • 70349663509 scopus 로고    scopus 로고
    • Pericentrin, a centrosomal protein related to microcephalic primordial dwar-sm, is required for olfactory cilia assembly in mice
    • Miyoshi, K. et al. Pericentrin, a centrosomal protein related to microcephalic primordial dwar-sm, is required for olfactory cilia assembly in mice. FASEB J. 23, 3289-3297 (2009
    • (2009) FASEB J. , vol.23 , pp. 3289-3297
    • Miyoshi, K.1
  • 59
    • 0036736094 scopus 로고    scopus 로고
    • Centrosomal proteins CG-NAP and kendrin provide microtubule nucleation sites by anchoring γ-tubulin ring complex
    • DOI 10.1091/mbc.E02-02-0112
    • Takahashi, M. et al. Centrosomal proteins CG-NAP and kendrin provide microtubule nucleation sites by anchoring -tubulin ring complex. Mol. Biol. Cell 13, 3235-3245 (2002 (Pubitemid 35034258)
    • (2002) Molecular Biology of the Cell , vol.13 , Issue.9 , pp. 3235-3245
    • Takahashi, M.1    Yamagiwa, A.2    Nishimura, T.3    Mukai, H.4    Ono, Y.5
  • 60
    • 76149140090 scopus 로고    scopus 로고
    • Pericentrin in cellular function and disease
    • Delaval, B. & Doxsey, S.J. Pericentrin in cellular function and disease. J. Cell. Biol. 188, 181-190 (2010
    • (2010) J. Cell. Biol , vol.188 , pp. 181-190
    • Delaval, B.1    Doxsey, S.J.2
  • 64
  • 65
    • 0042622508 scopus 로고    scopus 로고
    • The centrosomal proteins pericentrin and kendrin are encoded by alternatively spliced products of one gene
    • DOI 10.1016/S0888-7543(03)00119-8
    • Flory, M.R. & Davis, T.N. The centrosomal proteins pericentrin and kendrin are encoded by alternatively spliced products of one gene. Genomics 82, 401-405 (2003 (Pubitemid 36952311)
    • (2003) Genomics , vol.82 , Issue.3 , pp. 401-405
    • Flory, M.R.1    Davis, T.N.2
  • 66
    • 84869050846 scopus 로고    scopus 로고
    • Subdiffraction imaging of centrosomes reveals higher-order organizational features of pericentriolar material
    • Lawo, S., Hasegan, M., Gupta, G.D. & Pelletier, L. Subdiffraction imaging of centrosomes reveals higher-order organizational features of pericentriolar material. Nat. Cell Biol. 14, 1148-1158 (2012
    • (2012) Nat. Cell Biol , vol.14 , pp. 1148-1158
    • Lawo, S.1    Hasegan, M.2    Gupta, G.D.3    Pelletier, L.4
  • 67
    • 84964866213 scopus 로고    scopus 로고
    • 3D-structured illumination microscopy provides novel insight into architecture of human centrosomes
    • Sonnen, K.F., Schermelleh, L., Leonhardt, H. & Nigg, E.A. 3D-structured illumination microscopy provides novel insight into architecture of human centrosomes. Biol. Open 000, 1-12 (2012
    • (2012) Biol. Open , pp. 1-12
    • Sonnen, K.F.1    Schermelleh, L.2    Leonhardt, H.3    Nigg, E.A.4
  • 68
    • 69449089441 scopus 로고    scopus 로고
    • Motor domain phosphorylation and regulation of the Drosophila kinesin 13
    • Mennella, V. et al. Motor domain phosphorylation and regulation of the Drosophila kinesin 13, KLP10A. J. Cell. Biol. 186, 481-490 (2009
    • (2009) KLP10A. J. Cell. Biol , vol.186 , pp. 481-490
    • Mennella, V.1
  • 69
    • 0141433278 scopus 로고    scopus 로고
    • Molecular requirements for actin-based lamella formation in Drosophila S2 cells
    • DOI 10.1083/jcb.200303023
    • Rogers, S.L. et al. Molecular requirements for actin-based lamella formation in Drosophila S2 cells. J. Cell. Biol. 162, 1079-1088 (2003 (Pubitemid 37174190)
    • (2003) Journal of Cell Biology , vol.162 , Issue.6 , pp. 1079-1088
    • Rogers, S.L.1    Wiedemann, U.2    Stuurman, N.3    Vale, R.D.4
  • 71
    • 0028695433 scopus 로고
    • Electron microscopy and EM immunocytochemistry
    • McDonald, K.L. Electron microscopy and EM immunocytochemistry. Method. Cell Biol. 44, 411-444 (1994
    • (1994) Method. Cell Biol , vol.44 , pp. 411-444
    • McDonald, K.L.1
  • 72
    • 84856006967 scopus 로고    scopus 로고
    • Afadin, a ras/rap effector that controls cadherin function, promotes spine and excitatory synapse density in the hippocampus
    • Beaudoin, G.M. 3rd et al. Afadin, a ras/rap effector that controls cadherin function, promotes spine and excitatory synapse density in the hippocampus. J. Neurosci. 32, 99-110 (2012
    • (2012) J. Neurosci , vol.32 , pp. 99-110
    • Beaudoin III, G.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.