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Volumn 18, Issue 9, 2007, Pages 3667-3680

Chromatin remodeling proteins interact with pericentrin to regulate centrosome integrity

Author keywords

[No Author keywords available]

Indexed keywords

ACYLTRANSFERASE; CELL CYCLE PROTEIN; CHROMODOMAIN HELICASE DNA BINDING PROTEIN 3; CHROMODOMAIN HELICASE DNA BINDING PROTEIN 4; DNA BINDING PROTEIN; GAMMA TUBULIN; NUCLEOSOME REMODELING DEACETYLASE; PERICENTRIN; UNCLASSIFIED DRUG;

EID: 34548474527     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E06-07-0604     Document Type: Article
Times cited : (40)

References (57)
  • 1
    • 0035374836 scopus 로고    scopus 로고
    • Centrosome protein centrin 2/caltractin 1 is part of the xeroderma pigmentosum group C complex that initiates global genome nucleotide excision repair
    • Araki, M., Masutani, C., Takemura, M., Uchida, A., Sugasawa, K., Kondoh, J., Ohkuma, Y., and Hanaoka, F. (2001). Centrosome protein centrin 2/caltractin 1 is part of the xeroderma pigmentosum group C complex that initiates global genome nucleotide excision repair. J. Biol. Chem. 276, 18665-18672.
    • (2001) J. Biol. Chem , vol.276 , pp. 18665-18672
    • Araki, M.1    Masutani, C.2    Takemura, M.3    Uchida, A.4    Sugasawa, K.5    Kondoh, J.6    Ohkuma, Y.7    Hanaoka, F.8
  • 2
    • 0032526270 scopus 로고    scopus 로고
    • Identification of a human 17p-located cDNA encoding a protein of the Snf2-like helicase family
    • Aubry, F., Mattei, M. G., and Galibert, F. (1998). Identification of a human 17p-located cDNA encoding a protein of the Snf2-like helicase family. Eur. J. Biochem. 254, 558-564.
    • (1998) Eur. J. Biochem , vol.254 , pp. 558-564
    • Aubry, F.1    Mattei, M.G.2    Galibert, F.3
  • 5
    • 0037166937 scopus 로고    scopus 로고
    • Cell cycle-dependent localization of macroH2A in chromatin of the inactive X chromosome
    • Chadwick, B. P., and Willard, H. F. (2002). Cell cycle-dependent localization of macroH2A in chromatin of the inactive X chromosome. J. Cell Biol. 157, 1113-1123.
    • (2002) J. Cell Biol , vol.157 , pp. 1113-1123
    • Chadwick, B.P.1    Willard, H.F.2
  • 6
    • 1042266629 scopus 로고    scopus 로고
    • Centrosomal anchoring of protein kinase C betaII by pericentrin controls microtubule organization, spindle function, and cytokinesis
    • Chen, D., Purohit, A., Halilovic, E., Doxsey, S. J., and Newton, A. C. (2004). Centrosomal anchoring of protein kinase C betaII by pericentrin controls microtubule organization, spindle function, and cytokinesis. J. Biol. Chem. 279, 4829-4839.
    • (2004) J. Biol. Chem , vol.279 , pp. 4829-4839
    • Chen, D.1    Purohit, A.2    Halilovic, E.3    Doxsey, S.J.4    Newton, A.C.5
  • 7
    • 31344481209 scopus 로고    scopus 로고
    • SUMO-1 modification of centrosomal protein hNinein promotes hNinein nuclear localization
    • Cheng, T. S., Chang, L. K., Howng, S. L., Lu, P. J., Lee, C. I., and Hong, Y. R. (2006). SUMO-1 modification of centrosomal protein hNinein promotes hNinein nuclear localization. Life Sci. 78, 1114-1120.
    • (2006) Life Sci , vol.78 , pp. 1114-1120
    • Cheng, T.S.1    Chang, L.K.2    Howng, S.L.3    Lu, P.J.4    Lee, C.I.5    Hong, Y.R.6
  • 11
    • 0034611693 scopus 로고    scopus 로고
    • Pericentrin anchors protein kinase A at the centrosome through a newly identified RH-binding domain
    • Diviani, D., Langeberg, L. K., Doxsey, S. J., and Scott, J. D. (2000). Pericentrin anchors protein kinase A at the centrosome through a newly identified RH-binding domain. Curr. Biol. 10, 417-420.
    • (2000) Curr. Biol , vol.10 , pp. 417-420
    • Diviani, D.1    Langeberg, L.K.2    Doxsey, S.J.3    Scott, J.D.4
  • 12
    • 0028218025 scopus 로고
    • Pericentrin, a highly conserved centrosome protein involved in microtubule organization
    • Doxsey, S. J., Stein, P., Evans, L., Calarco, P. D., and Kirschner, M. (1994). Pericentrin, a highly conserved centrosome protein involved in microtubule organization. Cell 76, 639-650.
    • (1994) Cell , vol.76 , pp. 639-650
    • Doxsey, S.J.1    Stein, P.2    Evans, L.3    Calarco, P.D.4    Kirschner, M.5
  • 13
    • 20444407162 scopus 로고    scopus 로고
    • Centrosome control of the cell cycle
    • Doxsey, S., Zimmerman, W., and Mikule, K. (2005). Centrosome control of the cell cycle. Trends Cell Biol. 15, 303-311.
    • (2005) Trends Cell Biol , vol.15 , pp. 303-311
    • Doxsey, S.1    Zimmerman, W.2    Mikule, K.3
  • 14
    • 33745122231 scopus 로고    scopus 로고
    • Identification of multiple distinct Snf2 subfamilies with conserved structural motifs
    • Flaus, A., Martin, D. M., Barton, G. J., and Owen-Hughes, T. (2006). Identification of multiple distinct Snf2 subfamilies with conserved structural motifs. Nucleic Acids Res. 34, 2887-2905.
    • (2006) Nucleic Acids Res , vol.34 , pp. 2887-2905
    • Flaus, A.1    Martin, D.M.2    Barton, G.J.3    Owen-Hughes, T.4
  • 15
    • 0036193204 scopus 로고    scopus 로고
    • Pcp1p, an Spc110p-related calmodulin target at the centrosome of the fission yeast Schizosaccharomyces pombe
    • Flory, M. R., Morphew, M., Joseph, J. D., Means, A. R., and Davis, T. N. (2002). Pcp1p, an Spc110p-related calmodulin target at the centrosome of the fission yeast Schizosaccharomyces pombe. Cell Growth Differ. 13, 47-58.
    • (2002) Cell Growth Differ , vol.13 , pp. 47-58
    • Flory, M.R.1    Morphew, M.2    Joseph, J.D.3    Means, A.R.4    Davis, T.N.5
  • 16
    • 5344280456 scopus 로고    scopus 로고
    • MTA3 and the Mi-2/NuRD complex regulate cell fate during B lymphocyte differentiation
    • Fujita, N., Jaye, D. L., Geigerman, C., Akyildiz, A., Mooney, M. R., Boss, J. M., and Wade, P. A. (2004). MTA3 and the Mi-2/NuRD complex regulate cell fate during B lymphocyte differentiation. Cell 119, 75-86.
    • (2004) Cell , vol.119 , pp. 75-86
    • Fujita, N.1    Jaye, D.L.2    Geigerman, C.3    Akyildiz, A.4    Mooney, M.R.5    Boss, J.M.6    Wade, P.A.7
  • 17
    • 1942468753 scopus 로고    scopus 로고
    • The transforming acidic coiled coil proteins interact with nuclear histone acetyltransferases
    • Gangisetty, O., Lauffart, B., Sondarva, G. V., Chelsea, D. M., and Still, I. H. (2004). The transforming acidic coiled coil proteins interact with nuclear histone acetyltransferases. Oncogene 23, 2559-2563.
    • (2004) Oncogene , vol.23 , pp. 2559-2563
    • Gangisetty, O.1    Lauffart, B.2    Sondarva, G.V.3    Chelsea, D.M.4    Still, I.H.5
  • 18
    • 0034687657 scopus 로고    scopus 로고
    • The TACC domain identifies a family of centrosomal proteins that can interact with microtubules
    • Gergely, F., Karlsson, C., Still, I., Cowell, J., Kilmartin, J., and Raff, J. W. (2000). The TACC domain identifies a family of centrosomal proteins that can interact with microtubules. Proc. Natl. Acad. Sci. USA 97, 14352-14357.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 14352-14357
    • Gergely, F.1    Karlsson, C.2    Still, I.3    Cowell, J.4    Kilmartin, J.5    Raff, J.W.6
  • 19
    • 14244249406 scopus 로고    scopus 로고
    • Systematic identification and analysis of mammalian small ubiquitin-like modifier substrates
    • Gocke, C. B., Yu, H., and Kang, J. (2005). Systematic identification and analysis of mammalian small ubiquitin-like modifier substrates. J. Biol. Chem. 280, 5004-5012.
    • (2005) J. Biol. Chem , vol.280 , pp. 5004-5012
    • Gocke, C.B.1    Yu, H.2    Kang, J.3
  • 20
    • 21644469164 scopus 로고    scopus 로고
    • Membrane type-1 matrix metalloproteinase (MT1-MMP) exhibits an important intracellular cleavage function and causes chromosome instability
    • Golubkov, V. S., Boyd, S., Savinov, A. Y., Chekanov, A. V., Osterman, A. L., Remade, A., Rozanov, D. V., Doxsey, S. J., and Strongin, A. Y. (2005a). Membrane type-1 matrix metalloproteinase (MT1-MMP) exhibits an important intracellular cleavage function and causes chromosome instability. J. Biol. Chem. 280, 25079-25086.
    • (2005) J. Biol. Chem , vol.280 , pp. 25079-25086
    • Golubkov, V.S.1    Boyd, S.2    Savinov, A.Y.3    Chekanov, A.V.4    Osterman, A.L.5    Remade, A.6    Rozanov, D.V.7    Doxsey, S.J.8    Strongin, A.Y.9
  • 21
    • 29644437767 scopus 로고    scopus 로고
    • Centrosomal pericentrin is a direct cleavage target of membrane type-1 matrix metalloproteinase in humans but not in mice: Potential implications for tumorigenesis
    • Golubkov, V. S., Chekanov, A. V., Doxsey, S. J., and Strongin, A. Y. (2005b). Centrosomal pericentrin is a direct cleavage target of membrane type-1 matrix metalloproteinase in humans but not in mice: potential implications for tumorigenesis. J. Biol. Chem. 280, 42237-42241.
    • (2005) J. Biol. Chem , vol.280 , pp. 42237-42241
    • Golubkov, V.S.1    Chekanov, A.V.2    Doxsey, S.J.3    Strongin, A.Y.4
  • 22
    • 0037936560 scopus 로고    scopus 로고
    • A novel human protein of the maternal centriole is required for the final stages of cytokinesis and entry into S phase
    • Gromley, A., Jurczyk, A., Sillibourne, J., Halilovic, E., Mogensen, M., Groisman, I., Blomberg, M., and Doxsey, S. (2003). A novel human protein of the maternal centriole is required for the final stages of cytokinesis and entry into S phase. J. Cell Biol. 161, 535-545.
    • (2003) J. Cell Biol , vol.161 , pp. 535-545
    • Gromley, A.1    Jurczyk, A.2    Sillibourne, J.3    Halilovic, E.4    Mogensen, M.5    Groisman, I.6    Blomberg, M.7    Doxsey, S.8
  • 25
    • 0031932083 scopus 로고    scopus 로고
    • Isolation and characterization of hrp1+, a new member of the SNF2/SWI2 gene family from the fission yeast Schizosaccharomyces pombe
    • Jin, Y. H. et al. (1998). Isolation and characterization of hrp1+, a new member of the SNF2/SWI2 gene family from the fission yeast Schizosaccharomyces pombe. Mol. Gen. Genet. 257, 319-329.
    • (1998) Mol. Gen. Genet , vol.257 , pp. 319-329
    • Jin, Y.H.1
  • 26
    • 4444320182 scopus 로고    scopus 로고
    • Pericentrin forms a complex with intraflagellar transport proteins and polycystin-2 and is required for primary cilia assembly
    • Jurczyk, A., Gromley, A., Redick, S., San Agustin, J., Witman, G., Pazour, G. J., Peters, D. J., and Doxsey, S. (2004). Pericentrin forms a complex with intraflagellar transport proteins and polycystin-2 and is required for primary cilia assembly. J. Cell Biol. 166, 637-643.
    • (2004) J. Cell Biol , vol.166 , pp. 637-643
    • Jurczyk, A.1    Gromley, A.2    Redick, S.3    San Agustin, J.4    Witman, G.5    Pazour, G.J.6    Peters, D.J.7    Doxsey, S.8
  • 27
    • 0347360338 scopus 로고    scopus 로고
    • Characterization of a Drosophila centrosome protein CP309 that shares homology with Kendrin and CG-NAP
    • Kawaguchi, S., and Zheng, Y. (2004). Characterization of a Drosophila centrosome protein CP309 that shares homology with Kendrin and CG-NAP. Mol. Biol. Cell 15, 37-45.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 37-45
    • Kawaguchi, S.1    Zheng, Y.2
  • 29
    • 0033538844 scopus 로고    scopus 로고
    • The sudden recruitment of gamma-tubulin to the centrosome at the onset of mitosis and its dynamic exchange throughout the cell cycle, do not require microtubules
    • Khodjakov, A., and Rieder, C. L. (1999). The sudden recruitment of gamma-tubulin to the centrosome at the onset of mitosis and its dynamic exchange throughout the cell cycle, do not require microtubules. J. Cell Biol. 146, 585-596.
    • (1999) J. Cell Biol , vol.146 , pp. 585-596
    • Khodjakov, A.1    Rieder, C.L.2
  • 30
    • 0029791665 scopus 로고    scopus 로고
    • Spc110p: Assembly properties and role in the connection of nuclear microtubules to the yeast spindle pole body
    • Kilmartin, J. V., and Goh, P. Y. (1996). Spc110p: assembly properties and role in the connection of nuclear microtubules to the yeast spindle pole body. EMBO J. 15, 4592-4602.
    • (1996) EMBO J , vol.15 , pp. 4592-4602
    • Kilmartin, J.V.1    Goh, P.Y.2
  • 31
    • 0035086902 scopus 로고    scopus 로고
    • Kendrin/pericentrin-B, a centrosome protein with homology to pericentrin that complexes with PCM-1
    • Li, Q., Hansen, D., Killilea, A., Joshi, H. C., Palazzo, R. E., and Balczon, R. (2001). Kendrin/pericentrin-B, a centrosome protein with homology to pericentrin that complexes with PCM-1. J. Cell Sci. 114, 797-809.
    • (2001) J. Cell Sci , vol.114 , pp. 797-809
    • Li, Q.1    Hansen, D.2    Killilea, A.3    Joshi, H.C.4    Palazzo, R.E.5    Balczon, R.6
  • 32
    • 0034676439 scopus 로고    scopus 로고
    • Deacetylation of p53 modulates its effect on cell growth and apoptosis
    • Luo, J., Su, F., Chen, D., Shiloh, A., and Gu, W. (2000). Deacetylation of p53 modulates its effect on cell growth and apoptosis. Nature 408, 377-381.
    • (2000) Nature , vol.408 , pp. 377-381
    • Luo, J.1    Su, F.2    Chen, D.3    Shiloh, A.4    Gu, W.5
  • 33
    • 2942692444 scopus 로고    scopus 로고
    • The Drosophila pericentrin-like protein is essential for cilia/flagella function, but appears to be dispensable for mitosis
    • Martinez-Campos, M., Basto, R., Baker, J., Kernan, M., and Raff, J. W. (2004). The Drosophila pericentrin-like protein is essential for cilia/flagella function, but appears to be dispensable for mitosis. J. Cell Biol. 165, 673-683.
    • (2004) J. Cell Biol , vol.165 , pp. 673-683
    • Martinez-Campos, M.1    Basto, R.2    Baker, J.3    Kernan, M.4    Raff, J.W.5
  • 35
    • 0034680441 scopus 로고    scopus 로고
    • Covalent modification of p73alpha by SUMO-1. Two-hybrid screening with p73 identifies novel SUMO-1-interacting proteins and a SUMO-1 interaction motif
    • Minty, A., Dumont, X., Kaghad, M., and Caput, D. (2000). Covalent modification of p73alpha by SUMO-1. Two-hybrid screening with p73 identifies novel SUMO-1-interacting proteins and a SUMO-1 interaction motif. J. Biol. Chem. 275, 36316-36323.
    • (2000) J. Biol. Chem , vol.275 , pp. 36316-36323
    • Minty, A.1    Dumont, X.2    Kaghad, M.3    Caput, D.4
  • 38
    • 9744257012 scopus 로고    scopus 로고
    • The centrosomal protein CP190 is a component of the gypsy chromatin insulator
    • Pai, C. Y., Lei, E. P., Ghosh, D., and Corces, V. G. (2004). The centrosomal protein CP190 is a component of the gypsy chromatin insulator. Mol. Cell 16, 737-748.
    • (2004) Mol. Cell , vol.16 , pp. 737-748
    • Pai, C.Y.1    Lei, E.P.2    Ghosh, D.3    Corces, V.G.4
  • 39
    • 1242342234 scopus 로고    scopus 로고
    • Centrosome maturation: Measurement of microtubule nucleation throughout the cell cycle by using GFP-tagged EB1
    • Piehl, M., Tulu, U. S., Wadsworth, P., and Cassimeris, L. (2004). Centrosome maturation: measurement of microtubule nucleation throughout the cell cycle by using GFP-tagged EB1. Proc. Natl. Acad. Sci. USA 101, 1584-1588.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 1584-1588
    • Piehl, M.1    Tulu, U.S.2    Wadsworth, P.3    Cassimeris, L.4
  • 40
    • 0033229726 scopus 로고    scopus 로고
    • Direct interaction of pericentrin with cytoplasmic dynein light intermediate chain contributes to mitotic spindle organization
    • Purohit, A., Tynan, S. H., Vallee, R., and Doxsey, S. J. (1999). Direct interaction of pericentrin with cytoplasmic dynein light intermediate chain contributes to mitotic spindle organization. J. Cell Biol. 147, 481-492.
    • (1999) J. Cell Biol , vol.147 , pp. 481-492
    • Purohit, A.1    Tynan, S.H.2    Vallee, R.3    Doxsey, S.J.4
  • 41
    • 2242476587 scopus 로고    scopus 로고
    • MBD3 and HDAC1, two components of the NuRD complex, are localized at Aurora-A-positive centrosomes in M phase
    • Sakai, H., Urano, T., Ookata, K., Kim, M. H., Hirai, Y., Saito, M., Nojima, Y., and Ishikawa, F. (2002). MBD3 and HDAC1, two components of the NuRD complex, are localized at Aurora-A-positive centrosomes in M phase. J. Biol. Chem. 277, 48714-48723.
    • (2002) J. Biol. Chem , vol.277 , pp. 48714-48723
    • Sakai, H.1    Urano, T.2    Ookata, K.3    Kim, M.H.4    Hirai, Y.5    Saito, M.6    Nojima, Y.7    Ishikawa, F.8
  • 42
    • 0033517797 scopus 로고    scopus 로고
    • Molecular association between ATR and two components of the nucleosome remodeling and deacetylating complex, HDAC2 and CHD4
    • Schmidt, D. R., and Schreiber, S. L. (1999). Molecular association between ATR and two components of the nucleosome remodeling and deacetylating complex, HDAC2 and CHD4. Biochemistry 38, 14711-14717.
    • (1999) Biochemistry , vol.38 , pp. 14711-14717
    • Schmidt, D.R.1    Schreiber, S.L.2
  • 43
    • 0036150409 scopus 로고    scopus 로고
    • CHD5 defines a new subfamily of chromodomain-SWI2/SNF2-like helicases
    • Schuster, E. F., and Stoger, R. (2002). CHD5 defines a new subfamily of chromodomain-SWI2/SNF2-like helicases. Mamm. Genome 13, 117-119.
    • (2002) Mamm. Genome , vol.13 , pp. 117-119
    • Schuster, E.F.1    Stoger, R.2
  • 44
    • 0036736094 scopus 로고    scopus 로고
    • Centrosomal proteins CG-NAP and kendrin provide microtubule nucleation sites by anchoring gamma-tubulin ring complex
    • Takahashi, M., Yamagiwa, A., Nishimura, T., Mukai, H., and Ono, Y. (2002). Centrosomal proteins CG-NAP and kendrin provide microtubule nucleation sites by anchoring gamma-tubulin ring complex. Mol. Biol. Cell 13, 3235-3245.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 3235-3245
    • Takahashi, M.1    Yamagiwa, A.2    Nishimura, T.3    Mukai, H.4    Ono, Y.5
  • 45
    • 0037455722 scopus 로고    scopus 로고
    • CHD5, a new member of the chromodomain gene family, is preferentially expressed in the nervous system
    • Thompson, P. M., Gotoh, T., Kok, M., White, P. S., and Brodeur, G. M. (2003). CHD5, a new member of the chromodomain gene family, is preferentially expressed in the nervous system. Oncogene 22, 1002-1011.
    • (2003) Oncogene , vol.22 , pp. 1002-1011
    • Thompson, P.M.1    Gotoh, T.2    Kok, M.3    White, P.S.4    Brodeur, G.M.5
  • 46
    • 0032578762 scopus 로고    scopus 로고
    • Chromatin deacetylation by an ATP-dependent nucleosome remodelling complex
    • Tong, J. K., Hassig, C. A., Schnitzler, G. R., Kingston, R. E., and Schreiber, S. L. (1998). Chromatin deacetylation by an ATP-dependent nucleosome remodelling complex. Nature 395, 917-921.
    • (1998) Nature , vol.395 , pp. 917-921
    • Tong, J.K.1    Hassig, C.A.2    Schnitzler, G.R.3    Kingston, R.E.4    Schreiber, S.L.5
  • 47
    • 0034657071 scopus 로고    scopus 로고
    • The chromo domain protein chd1p from budding yeast is an ATP-dependent chromatin-modifying factor
    • Tran, H. G., Steger, D. J., Iyer, V. R., and Johnson, A. D. (2000). The chromo domain protein chd1p from budding yeast is an ATP-dependent chromatin-modifying factor. EMBO J. 19, 2323-2331.
    • (2000) EMBO J , vol.19 , pp. 2323-2331
    • Tran, H.G.1    Steger, D.J.2    Iyer, V.R.3    Johnson, A.D.4
  • 48
    • 0034520843 scopus 로고    scopus 로고
    • The C. elegans Mi-2 chromatin-remodelling proteins function in vulval cell fate determination
    • von Zelewsky, T., Palladino, F., Brunschwig, K., Tobler, H., Hajnal, A., and Muller, F. (2000). The C. elegans Mi-2 chromatin-remodelling proteins function in vulval cell fate determination. Development 127, 5277-5284.
    • (2000) Development , vol.127 , pp. 5277-5284
    • von Zelewsky, T.1    Palladino, F.2    Brunschwig, K.3    Tobler, H.4    Hajnal, A.5    Muller, F.6
  • 49
    • 0032474826 scopus 로고    scopus 로고
    • A multiple subunit Mi-2 histone deacetylase from Xenopus laevis cofractionates with an associated Snf2 superfamily ATPase
    • Wade, P. A., Jones, P. L., Vermaak, D., and Wolffe, A. P. (1998). A multiple subunit Mi-2 histone deacetylase from Xenopus laevis cofractionates with an associated Snf2 superfamily ATPase. Curr. Biol. 8, 843-846.
    • (1998) Curr. Biol , vol.8 , pp. 843-846
    • Wade, P.A.1    Jones, P.L.2    Vermaak, D.3    Wolffe, A.P.4
  • 50
    • 0035875298 scopus 로고    scopus 로고
    • Mi2, an auto-antigen for dermatomyositis, is an ATP-dependent nucleosome remodeling factor
    • Wang, H. B., and Zhang, Y. (2001). Mi2, an auto-antigen for dermatomyositis, is an ATP-dependent nucleosome remodeling factor. Nucleic Acids Res. 29, 2517-2521.
    • (2001) Nucleic Acids Res , vol.29 , pp. 2517-2521
    • Wang, H.B.1    Zhang, Y.2
  • 52
    • 0032252209 scopus 로고    scopus 로고
    • NURD, a novel complex with both ATP-dependent chromatin-remodeling and histone deacetylase activities
    • Xue, Y., Wong, J., Moreno, G. T., Young, M. K., Cote, J., and Wang, W. (1998). NURD, a novel complex with both ATP-dependent chromatin-remodeling and histone deacetylase activities. Mol. Cell 2, 851-861.
    • (1998) Mol. Cell , vol.2 , pp. 851-861
    • Xue, Y.1    Wong, J.2    Moreno, G.T.3    Young, M.K.4    Cote, J.5    Wang, W.6
  • 53
    • 0034193119 scopus 로고    scopus 로고
    • Fission yeast hrpl, a chromodomain ATPase, is required for proper chromosome segregation and its overexpression interferes with chromatin condensation
    • Yoo, E. J., Jin, Y. H., Jang, Y. K., Bjerling, P., Tabish, M., Hong, S. H., Ekwall, K., and Park, S. D. (2000). Fission yeast hrpl, a chromodomain ATPase, is required for proper chromosome segregation and its overexpression interferes with chromatin condensation. Nucleic Acids Res. 28, 2004-2011.
    • (2000) Nucleic Acids Res , vol.28 , pp. 2004-2011
    • Yoo, E.J.1    Jin, Y.H.2    Jang, Y.K.3    Bjerling, P.4    Tabish, M.5    Hong, S.H.6    Ekwall, K.7    Park, S.D.8
  • 54
    • 0141638426 scopus 로고    scopus 로고
    • N-CoR mediates DNA methylation-dependent repression through a methyl CpG binding protein Kaiso
    • Yoon, H. G., Chan, D. W., Reynolds, A. B., Qin, J., and Wong, J. (2003). N-CoR mediates DNA methylation-dependent repression through a methyl CpG binding protein Kaiso. Mol. Cell 12, 723-734.
    • (2003) Mol. Cell , vol.12 , pp. 723-734
    • Yoon, H.G.1    Chan, D.W.2    Reynolds, A.B.3    Qin, J.4    Wong, J.5
  • 55
    • 0034047184 scopus 로고    scopus 로고
    • Cytoplasmic dynein-mediated assembly of pericentrin and gamma tubulin onto centrosomes
    • Young, A., Dictenberg, J. B., Purohit, A., Tuft, R., and Doxsey, S. J. (2000). Cytoplasmic dynein-mediated assembly of pericentrin and gamma tubulin onto centrosomes. Mol. Biol. Cell 11, 2047-2056.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 2047-2056
    • Young, A.1    Dictenberg, J.B.2    Purohit, A.3    Tuft, R.4    Doxsey, S.J.5
  • 56
    • 0032538293 scopus 로고    scopus 로고
    • The dermatomyositis-specific autoantigen Mi2 is a component of a complex containing histone deacetylase and nucleosome remodeling activities
    • Zhang, Y., LeRoy, G., Seelig, H. P., Lane, W. S., and Reinberg, D. (1998). The dermatomyositis-specific autoantigen Mi2 is a component of a complex containing histone deacetylase and nucleosome remodeling activities. Cell 95, 279-289.
    • (1998) Cell , vol.95 , pp. 279-289
    • Zhang, Y.1    LeRoy, G.2    Seelig, H.P.3    Lane, W.S.4    Reinberg, D.5
  • 57
    • 3343008017 scopus 로고    scopus 로고
    • Mitosis-specific anchoring of (gamma) tubulin complexes by pericentrin controls spindle organization and mitotic entry
    • Zimmerman, W. C., Sillibourne, J., Rosa, J., and Doxsey, S. J. (2004). Mitosis-specific anchoring of (gamma) tubulin complexes by pericentrin controls spindle organization and mitotic entry. Mol. Biol. Cell 15, 3642-3657.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 3642-3657
    • Zimmerman, W.C.1    Sillibourne, J.2    Rosa, J.3    Doxsey, S.J.4


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